|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1007-1572 |
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: 733.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1007 LFMLLNAKGTTVCTASCLQLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPH-AQNLT 1085
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1086 ATLPTVRMivDVSKAACILTSQTLMRLLRSREAAAAVDVKTWPTIIDTDDLPRKRLP-----QLYKPPTPEMLAYLDFSV 1160
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1161 STTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMELENNLFLWLSTV 1240
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1241 NQYKIRDTFCSYSVMELCTKGLGNQVEVLKTRGINLSCVRTCVVVAEERPRVALQQSFSKLFKDIGLSPRAVSTTFGSRV 1320
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1321 NVAICLQGTSGPDPTTVYVDLKSLRHDRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHT 1400
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1401 ASGYYTIYDSETLQADHFN-TRLSFGDaAQTLWARTGYLGFVRRTELTAATGERHDALYVVGALDETLELRGLRYHPIDI 1479
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFPsTRLSTGI-TNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1480 ETSVSRIHRSIAECAVFTWTNLLVVVVEL-CGSEQEALDLVPLVTNVVLEEHYLIVGVVVVVDPGVIPINSRGEKQRMHL 1558
Cdd:cd05905 478 EATVMRVHPYRGRCAVFSITGLVVVVAEQpPGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEI 557
|
570
....*....|....
gi 55749758 1559 RDSFLADQLDPIYV 1572
Cdd:cd05905 558 RQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
355-931 |
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: 689.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 355 CLTALDMTGKPVYTLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPnnDPVMFMVAFYGCLLAEVIPVPIEV 434
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 435 PLtrkdaGGQQIGFLLGSCGIALALTSEVCLKGLPKT-----QNGEIVQFKGWPRLKWVVTDSKYLSKPPKDWQPHISPA 509
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 510 GTEPAYIEYKTSKEGSVMGVTVSRLAMLSHCQALSQACNYSEGETIVNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVM 589
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 590 KTCPLSWVQRVHAHKAKVALVKCRDLHWAMM------AHRDQRDVSLSSLRMLIVTDGaNPWSVSSCDAFLSLFQSHGLK 663
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKdlsstlASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 664 PEAIcpcatSAEAMTVAIRRPGVPGA--PLPGRAILSMNGLSYGVIRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGPP 741
Cdd:cd05905 307 PRAV-----STEFGTRVNPFICWQGTsgPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 742 qLCKTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVNSAGSPVGDVPFIRSGLLGFVGPGS----------LVFVVGK 811
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTKctdlnveehdLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 812 MDGLLMVSGRRHNADDIVATGLAVESiktvYRGRIAVFSVSvfydERIVVVAEQRPdASEEDSFQWMSRVLQAIDSIHQV 891
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 55749758 892 GVYCLALVPANTLPKTPLGGIHISQTKQLFLEGSLHPCNI 931
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
997-1530 |
8.88e-66 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 233.67 E-value: 8.88e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 997 WRAQATPDHVLFMLLNAKGTTVCTASCLQLHKRAERIASVLgdKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTV 1076
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1077 RPPHAqnlTATLPTVRMIVDVSKAACILTSQTLMRLLRSREAAAAVDVKTWPTIIDTDDLPRKRLPQLyKPPTPEMLAYL 1156
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPP-PSPDPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1157 DFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPY--CGLGFALwcLCSVYSGHQSVLIPPMELENNLF 1234
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLIGGL--LTPLYSGGPSVLMSPAAFLRRPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1235 LWLSTVNQYkiRDTFcsySVM-----ELCTKglgnQVEVLKTRGINLSCVRTCVVVAeERPRVALQQSFSKLFKDIGLSP 1309
Cdd:cd05931 233 RWLRLISRY--RATI---SAApnfayDLCVR----RVRDEDLEGLDLSSWRVALNGA-EPVRPATLRRFAEAFAPFGFRP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1310 RAVSTTFG---SRVNVAIclqGTSGPDPTTVYVDLKSLRHDRVRLVERGAPQSLLLSeSGKILPGVKVVIVNPETKGPVG 1386
Cdd:cd05931 303 EAFRPSYGlaeATLFVSG---GPPGTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDQEVRIVDPETGRELP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1387 DSHLGEIWVNSPHTASGYYTiydSETLQADHFNTRLSFGDAAqtlWARTGYLGFVRRteltaatGErhdaLYVVGALDET 1466
Cdd:cd05931 379 DGEVGEIWVRGPSVASGYWG---RPEATAETFGALAATDEGG---WLRTGDLGFLHD-------GE----LYITGRLKDL 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55749758 1467 LELRGLRYHPIDIETSVSRIHRSIAE--CAVFTW----TNLLVVVVELcGSEQEALDLVPLVTNV---VLEEH 1530
Cdd:cd05931 442 IIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEV-ERGADPADLAAIAAAIraaVAREH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
345-922 |
1.44e-62 |
|
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: 224.42 E-value: 1.44e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 345 RWGTTQAKCSCLTALDMTGKPVYTLTYGKLWSRSLKLAYTLLnklgtknePVLKPGDRVALVYPNNdpVMFMVAFYGCLL 424
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAPPG--LDFVAAFLGCLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 425 AEVIPVPIEVPLTRKDAggQQIGFLLGSCGIALALTSEVCLKGLPKTqngeIVQFKGWPRLKWVVTDSKyLSKPPKDWQP 504
Cdd:cd05931 71 AGAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLL-PDTSAADWPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 505 hISPAGTEPAYIEYkTSkeGSV---MGVTVSRLAMLSHCQALSQACNYSEGETIVNVLDFKKDAGLWHGMFANVMN---- 577
Cdd:cd05931 144 -PSPDPDDIAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSggps 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 578 -KMHTISVpysVMKtcPLSWVQRVHAHKAKV------ALVKCrdlhwAMMAHRDQRD-VSLSSLRMLIVtdGANPWSVSS 649
Cdd:cd05931 220 vLMSPAAF---LRR--PLRWLRLISRYRATIsaapnfAYDLC-----VRRVRDEDLEgLDLSSWRVALN--GAEPVRPAT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 650 CDAFLSLFQSHGLKPEAICPCATSAEAmTVAI---RRPGVPGAPLPGRAILSmnglsyGVIRVNTEDKNSALTVQDVGHV 726
Cdd:cd05931 288 LRRFAEAFAPFGFRPEAFRPSYGLAEA-TLFVsggPPGTGPVVLRVDRDALA------GRAVAVAADDPAARELVSCGRP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 727 MPGGMMCIVKPDGPpQLCKTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVNSAGspvgdvPFIRSGLLGFVGPGSLv 806
Cdd:cd05931 361 LPDQEVRIVDPETG-RELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 807 FVVGKMDGLLMVSGRRHNADDIVATglAVESIKTVYRGRIAVFSVSVFYDERIVVVAEQRPDASEEDSFQWMSRVLQAID 886
Cdd:cd05931 433 YITGRLKDLIIVRGRNHYPQDIEAT--AEEAHPALRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVA 510
|
570 580 590
....*....|....*....|....*....|....*.
gi 55749758 887 SIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLFL 922
Cdd:cd05931 511 REHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
995-1470 |
1.55e-51 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 188.29 E-value: 1.55e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 995 LQWRAQATPDHVLFMllNAKGTTVctaSCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPV 1074
Cdd:pfam00501 1 LERQAARTPDKTALE--VGEGRRL---TYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1075 TVRPphaqnlTATLPTVRMIVDVSKAACILTSQTLmRLLRSREAAAAVDVKTWPTIIDTDDLPRKRL-----------PQ 1143
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDDAL-KLEELLEALGKLEVVKLVLVLDRDPVLKEEPlpeeakpadvpPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1144 LYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCE----LYSSRQIAICLDPYCGLGFALWCLCSVYSGH 1219
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1220 QSVLIPPMELeNNLFLWLSTVNQYKIRDTFCSYSVMELCtkglgnqVEVLKTRGINLSCVRTCVVVAeERPRVALQQSFS 1299
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1300 KLFkdiglsPRAVSTTFGSRVNVAICLQGTSGPDPTTvyvdlkslrhdrvrlvergapqslLLSESGKILPGVKVVIVNP 1379
Cdd:pfam00501 299 ELF------GGALVNGYGLTETTGVVTTPLPLDEDLR------------------------SLGSVGRPLPGTEVKIVDD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1380 ETKGPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHFNTrlsfGDaaqtlWARTGYLGfvRRTEltaaTGErhdaLYV 1459
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAFDE----DG-----WYRTGDLG--RRDE----DGY----LEI 406
|
490
....*....|.
gi 55749758 1460 VGALDETLELR 1470
Cdd:pfam00501 407 VGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1153-1517 |
1.89e-35 |
|
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: 138.57 E-value: 1.89e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1153 LAYLDFSVSTTGMLTGVKMSHSAVNALCRAIkLQCELYSSRQIAICLDPYC---GLGFALWCLcsvYSGHQSVLIPPMEL 1229
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFhigGLFGLLGAL---LAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1230 EnnlfLWLSTVNQYKIRDTFCSYSVMELCtkglgnqVEVLKTRGINLSCVRTCVVVAEERPRvALQQSFSKLFKDI---- 1305
Cdd:cd04433 78 E----AALELIEREKVTILLGVPTLLARL-------LKAPESAGYDLSSLRALVSGGAPLPP-ELLERFEEAPGIKlvng 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1306 -GLSPRAVSTTFGSRVNVAIclqgtsgpDPTTVyvdlkslrhdrvrlvergapqslllsesGKILPGVKVVIVNPETkGP 1384
Cdd:cd04433 146 yGLTETGGTVATGPPDDDAR--------KPGSV----------------------------GRPVPGVEVRIVDPDG-GE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1385 VGDSHLGEIWVNSPHTASGYYTIYDsetlqadhfNTRLSFGDAaqtlWARTGYLGFVRrteltaatgeRHDALYVVGALD 1464
Cdd:cd04433 189 LPPGEIGELVVRGPSVMKGYWNNPE---------ATAAVDEDG----WYRTGDLGRLD----------EDGYLYIVGRLK 245
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 55749758 1465 ETLELRGLRYHPIDIETSVSRiHRSIAECAVF-----TWTNLLVVVVELCGSEQEALD 1517
Cdd:cd04433 246 DMIKSGGENVYPAEVEAVLLG-HPGVAEAAVVgvpdpEWGERVVAVVVLRPGADLDAE 302
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
368-912 |
9.08e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 132.76 E-value: 9.08e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 368 TLTYGKLWSRSLKLAYTLlNKLGTknepvlkPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLTRkdAGGQQIG 447
Cdd:PRK05850 35 TLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQG--LEYIVAFLGALQAGLIAVPLSVPQGG--AHDERVS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 448 FLLGSCGIALALT-SEVClkglpktqnGEIVQF----KGWPRLKWVVTDSKYLSKPPKdwqPHISPAG-TEPAYIEYkTS 521
Cdd:PRK05850 103 AVLRDTSPSVVLTtSAVV---------DDVTEYvapqPGQSAPPVIEVDLLDLDSPRG---SDARPRDlPSTAYLQY-TS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 522 keGSV---MGVTVSRLAMLSHC-QALSQACNYSEGE-----TIVNVLDFKKDAGLWHGMFANVMNKMHTI-SVPYSVMKT 591
Cdd:PRK05850 170 --GSTrtpAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSWLPFYHDMGLVLGVCAPILGGCPAVlTSPVAFLQR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 592 cPLSWVQRV----HAHKA------KVALVKCRDlhwAMMAHRDQRDVslsslrmLIVTDGANPWSVSSCDAFLSLFQSHG 661
Cdd:PRK05850 248 -PARWMQLLasnpHAFSAapnfafELAVRKTSD---DDMAGLDLGGV-------LGIISGSERVHPATLKRFADRFAPFN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 662 LKPEAICPCATSAEAMT-VAIRRPGVPgaplPGRAILSMNGLSYGVIRVNTEDKNSALtvqdVGHVMP-GGMMCIVKPDG 739
Cdd:PRK05850 317 LRETAIRPSYGLAEATVyVATREPGQP----PESVRFDYEKLSAGHAKRCETGGGTPL----VSYGSPrSPTVRIVDPDT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 740 PPQlCKTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVN-SAGSPVGdvPFIRSGLLGFVGPGSLvFVVGKMDGLLMV 818
Cdd:PRK05850 389 CIE-CPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATLVDpSPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 819 SGRRHNADDIVATglavesIKTVYRGRIAVFSVSVFYDERIVVVAE-QRPDASEEDSFQWM----SRVLQAIDSIHQVGV 893
Cdd:PRK05850 465 DGRNHYPDDIEAT------IQEITGGRVAAISVPDDGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSV 538
|
570
....*....|....*....
gi 55749758 894 YCLALVPANTLPKTPLGGI 912
Cdd:PRK05850 539 ADLVLVAPGSIPITTSGKI 557
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
991-1485 |
1.01e-31 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 136.45 E-value: 1.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 991 LAEILQWRAQATPDHVLFMLLNAKGTTVCTASCLQLHKRAERIASVLGDKGHLnaGDNVVLLYPPGIELIAAFYGCLYAG 1070
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1071 CIPVTVRPP------HAQNLTAtlptvrmIVDVSKAACILTSQTLMRLLRSREAAAAVDVktwPTIIDTDDLP-----RK 1139
Cdd:PRK05691 89 VIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLDpalaeAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1140 RLPQLykppTPEMLAYLDFSVSTTGMLTGVKMSHSAVNAlcraiklqCELYSSRQIAICLDP----------YCGLGFAL 1209
Cdd:PRK05691 159 QEPAL----QPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1210 WCLCSVYSGHQSVLIPPmelenNLFL-----WLSTVNQYkiRDT----------FCSYSVMELCTKGLgnqvevlktrgi 1274
Cdd:PRK05691 227 GLLQPIFSGVPCVLMSP-----AYFLerplrWLEAISEY--GGTisggpdfayrLCSERVSESALERL------------ 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1275 NLSCVRtcVVVAEERP-RVALQQSFSKLFKDIGLSPRAVSTTFGSRVNVAICLQGTSGPDPTTVYVDLKSLRHDRvrlVE 1353
Cdd:PRK05691 288 DLSRWR--VAYSGSEPiRQDSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNR---AE 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1354 RGAPQSLLlsESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTiyDSETlqadhfnTRLSFGDAAQTLWA 1433
Cdd:PRK05691 363 PGTGSVLM--SCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR--NPEA-------SAKTFVEHDGRTWL 431
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 55749758 1434 RTGYLGFVRRTEltaatgerhdaLYVVGALDETLELRGLRYHPIDIETSVSR 1485
Cdd:PRK05691 432 RTGDLGFLRDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVER 472
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
14-131 |
6.15e-31 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 117.91 E-value: 6.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 14 AALPPEVRAQLAELELELSEGDITQKGYEKKRSKLLSPYSPQTQETdsavqkelrnqtpapsaAQTSAPSKYHRT-RSGG 92
Cdd:pfam06464 3 PSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLHPETP-----------------TKLSAEAQNQLAsLETK 65
|
90 100 110
....*....|....*....|....*....|....*....
gi 55749758 93 ARDERYRSDIHTEAVQAALAKHKEQKMALPMPTKRRSTF 131
Cdd:pfam06464 66 LRDEELSEEVYLEKVKALLAKELERENGLNAPTKEQSGL 104
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
396-926 |
2.91e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 128.69 E-value: 2.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 396 VLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPltrkDAGGQ--QIGFLLGSCGIALALTSEVC-------LK 466
Cdd:PRK07769 75 VTKPGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDP----AEPGHvgRLHAVLDDCTPSAILTTTDSaegvrkfFR 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 467 GLPKTQNgeivqfkgwPRLKWV--VTDSKYLSkppkdWQPhISPAGTEPAYIEYkTSkeGSV---MGVTVSRLAMLSHCQ 541
Cdd:PRK07769 149 ARPAKER---------PRVIAVdaVPDEVGAT-----WVP-PEANEDTIAYLQY-TS--GSTripAGVQITHLNLPTNVL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 542 ALSQACNYSEGETIVNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVMKTcPLSWVQRVHA------------------H 603
Cdd:PRK07769 211 QVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRR-PGRWIRELARkpggtggtfsaapnfafeH 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 604 KAKVALVKcrdlhwammahRDQRDVSLSSLRMLIvtDGANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAmTVAIRR 683
Cdd:PRK07769 290 AAARGLPK-----------DGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEA-TLFVST 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 684 PGVPGAPlpgRAI-LSMNGLSYG-VIRVNTEDKNsALTVQDVGHVMPGGMMCIVKPDGPPQLcKTDEIGEICVSSRTGGM 761
Cdd:PRK07769 356 TPMDEEP---TVIyVDRDELNAGrFVEVPADAPN-AVAQVSAGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGT 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 762 MYFGLAGVTKNTFEVI------PVNSAGSPvGDVPFIRSGLLGFVGPGSLvFVVGKMDGLLMVSGRRHNADDIVATglAV 835
Cdd:PRK07769 431 GYWGKPEETAATFQNIlksrlsESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYT--AQ 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 836 ESIKTVYRGRIAVFSV-------SVFYD-------------ERIVVVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYC 895
Cdd:PRK07769 507 EATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRD 586
|
570 580 590
....*....|....*....|....*....|.
gi 55749758 896 LALVPANTLPKTPLGGIHISQTKQLFLEGSL 926
Cdd:PRK07769 587 VLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
360-928 |
1.53e-29 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 125.89 E-value: 1.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 360 DMTGKPVYTLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVyPNNDPvMFMVAFYGCLLAEVIPVPIEVP--LT 437
Cdd:PRK09192 41 DRRGQLEEALPYQTLRARAEAGARRLLA-LG------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 438 RKDAGGQQIGFLLGSCGIALALTSEVCLKGLPKTQNGEivqfkgwpRLKWVVTDSKYLSKPPKDWQ-PHISPagTEPAYI 516
Cdd:PRK09192 112 GRESYIAQLRGMLASAQPAAIITPDELLPWVNEATHGN--------PLLHVLSHAWFKALPEADVAlPRPTP--DDIAYL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 517 EYkTSkeGSV---MGVTVSRLAMLSHCQALSQ-ACNYSEGETIVNVLDFKKDAGLWHGMFANVMNKMhtiSVPYsvMKTC 592
Cdd:PRK09192 182 QY-SS--GSTrfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQL---SVDY--LPTR 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 593 -----PLSWVQRVHAHKAKVALVKC--RDLHWAMMAHRDQRDVSLSSLRmlIVTDGANPWSVSSCDAFLSLFQSHGLKPE 665
Cdd:PRK09192 254 dfarrPLQWLDLISRNRGTISYSPPfgYELCARRVNSKDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDK 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 666 AICPCATSAEAmTVAIrrpgvpgaplpgrailSMNGLSYGvIRVNT------EDKNSALTVQD----------VGHVMPG 729
Cdd:PRK09192 332 AFMPSYGLAEA-TLAV----------------SFSPLGSG-IVVEEvdrdrlEYQGKAVAPGAetrrvrtfvnCGKALPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 730 GMMCIVKPDGP--PQLcktdEIGEICVssRTGGMM--YFGlagvTKNTFEVIPVNSagspvgdvpFIRSGLLGFVGPGSL 805
Cdd:PRK09192 394 HEIEIRNEAGMplPER----VVGHICV--RGPSLMsgYFR----DEESQDVLAADG---------WLDTGDLGYLLDGYL 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 806 VfVVGKMDGLLMVSGRRHNADDIvatGLAVESIKTVYRGRIAVFSVSVFYDERIVVVAEQRPdASEEDSFQWMSRVLQAI 885
Cdd:PRK09192 455 Y-ITGRAKDLIIINGRNIWPQDI---EWIAEQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALV 529
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 55749758 886 DSIHqvGVYCL-ALVPANTLPKTPLGGIHISQTKQLFLEGSLHP 928
Cdd:PRK09192 530 RSEF--GVEAAvELVPPHSLPRTSSGKLSRAKAKKRYLSGAFAS 571
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
336-924 |
7.97e-29 |
|
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: 123.16 E-value: 7.97e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 336 PPALESALQRWgTTQAKCSCLTALDMTGkPVYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNDPvmF 415
Cdd:cd05906 9 PRTLLELLLRA-AERGPTKGITYIDADG-SEEFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDDNED--F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 416 MVAFYGCLLAEVIPVPIEVPLTRKDAGGQ-----QIGFLLGSCGIalaLTSEVCLKGLPKtqngeivQFKGWPRLKWVVT 490
Cdd:cd05906 78 IPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELVAEFAG-------LETLSGLPGIRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 491 DSKYLSKPPKDWQPHISPAGTePAYIEYKTSKEGSVMGVTVSRLAMLSHCQALSQACNYSEGETIVNVLDFKKDAGLWHG 570
Cdd:cd05906 148 SIEELLDTAADHDLPQSRPDD-LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 571 MFANVMNKMHTISVPYSVMKTCPLSWVQRVHAHKAKV------ALVKCRDLhwamMAHRDQRDVSLSSLRMLIVtdGANP 644
Cdd:cd05906 227 HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLNDL----LEEIEDGTWDLSSLRYLVN--AGEA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 645 WSVSSCDAFLSLFQSHGLKPEAICPCATSAEamTVAirrpgvpgaplpgrailsmnglsyGVI---RVNTEDKNSALTVQ 721
Cdd:cd05906 301 VVAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysrSFPTYDHSQALEFV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 722 DVGHVMPGGMMCIVKPDGppQLCKTDEIGEICVS--SRTGGmmYFGLAGVTKNTFevipvnsagspVGDVPFiRSGLLGF 799
Cdd:cd05906 355 SLGRPIPGVSMRIVDDEG--QLLPEGEVGRLQVRgpVVTKG--YYNNPEANAEAF-----------TEDGWF-RTGDLGF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 800 VGPGSLVFvVGKMDGLLMVSGRRHNADDIVAtglAVESIKTVYRGRIAVFSVsvfYD-----ERIVVVAeqrpdASEEDS 874
Cdd:cd05906 419 LDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAV---RDpgaetEELAIFF-----VPEYDL 486
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 55749758 875 FQWMSRVLQAIDSI--HQVGVYCLALVP--ANTLPKTPLGGIHISQTKQLFLEG 924
Cdd:cd05906 487 QDALSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
995-1526 |
6.29e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 117.74 E-value: 6.29e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 995 LQWRAQATPDHVLFMLLNAKGTTVCTASCL---QLHKRAERIASVLgdKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGC 1071
Cdd:PRK05850 7 LRERASLQPDDAAFTFIDYEQDPAGVAETLtwsQLYRRTLNVAEEL--RRHGSTGDRAVILAPQGLEYIVAFLGALQAGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1072 IPVTVRPPHA----QNLTATLptvrmiVDVSKAACILTSQTLMRLlrsREAAAAVDVKTWPTII--DTDDLPRKRLPQLY 1145
Cdd:PRK05850 85 IAVPLSVPQGgahdERVSAVL------RDTSPSVVLTTSAVVDDV---TEYVAPQPGQSAPPVIevDLLDLDSPRGSDAR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1146 KPPTPEMlAYLDFSVSTTGMLTGVKMSHSAVNALCRaiKLQCELYSSRQIAICLD-------P-YCGLGFALWCLCSVYS 1217
Cdd:PRK05850 156 PRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMGLVLGVCAPILG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1218 GHQSVLIPPMElennlFL-----WLSTVNQYkiRDTFCSYS--VMELCTKglgnqvevlKTR-----GINLSCVRTcVVV 1285
Cdd:PRK05850 233 GCPAVLTSPVA-----FLqrparWMQLLASN--PHAFSAAPnfAFELAVR---------KTSdddmaGLDLGGVLG-IIS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1286 AEERPRVALQQSFSKLFKDIGLSPRAVSTTFG---SRVNVAIclqGTSGPDPTTVYVDLKSLRHDRVR---------LVE 1353
Cdd:PRK05850 296 GSERVHPATLKRFADRFAPFNLRETAIRPSYGlaeATVYVAT---REPGQPPESVRFDYEKLSAGHAKrcetgggtpLVS 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1354 RGAPQSLLlsesgkilpgvkVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTiYDSETLQAdhFNTRL---SFGDAAQT 1430
Cdd:PRK05850 373 YGSPRSPT------------VRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQ-KPEETERT--FGATLvdpSPGTPEGP 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1431 lWARTGYLGFVrrteltaATGErhdaLYVVGALDETLELRGLRYHPIDIETSVSRIHRsiAECAVFT----WTNLLVVVV 1506
Cdd:PRK05850 438 -WLRTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATIQEITG--GRVAAISvpddGTEKLVAII 503
|
570 580
....*....|....*....|...
gi 55749758 1507 EL---CGSEQEALDLVPLVTNVV 1526
Cdd:PRK05850 504 ELkkrGDSDEEAMDRLRTVKREV 526
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
357-926 |
1.43e-26 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 114.91 E-value: 1.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 357 TALDMTGKpvyTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNDPvmFMVAFYGCLLAEVIPVPIEVPL 436
Cdd:COG0318 16 PALVFGGR---RLTYAELDARARRLA-AALRALG------VGPGDRVALLLPNSPE--FVVAFLAALRAGAVVVPLNPRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 437 TRKdaggqQIGFLLGSCGIALALTsevclkglpktqngeivqfkgwprlkwvvtdskylskppkdwqphispagtepAYI 516
Cdd:COG0318 84 TAE-----ELAYILEDSGARALVT-----------------------------------------------------ALI 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 517 EYkTSkeGSV---MGVTVSRLAMLSHCQALSQACNYSEGETIVNVLDFKKDAGLWHGMFANVMNKMHTISVPysvmKTCP 593
Cdd:COG0318 106 LY-TS--GTTgrpKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP----RFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 594 LSWVQRVHAHKA-KVALVKcrDLHWAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLSLFQShglkpeAICPCAT 672
Cdd:COG0318 179 ERVLELIERERVtVLFGVP--TMLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFEERFGV------RIVEGYG 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 673 SAEAMTVAIRRPGVPGAPLPGRailsmnglsygvirvntedknsaltvqdVGHVMPGGMMCIVKPDGppQLCKTDEIGEI 752
Cdd:COG0318 249 LTETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEVRIVDEDG--RELPPGEVGEI 298
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 753 CVssRTGGMM--YFGLAGVTKNTFEvipvnsagspvgDvPFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVA 830
Cdd:COG0318 299 VV--RGPNVMkgYWNDPEATAEAFR------------D-GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEE 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 831 TGLAVESIKTVyrgriAVFSV-SVFYDERIV--VVAEQRPDASEEDSFQWMSRVL---QAIDSIHQVGvyclalvpanTL 904
Cdd:COG0318 364 VLAAHPGVAEA-----AVVGVpDEKWGERVVafVVLRPGAELDAEELRAFLRERLaryKVPRRVEFVD----------EL 428
|
570 580
....*....|....*....|..
gi 55749758 905 PKTPLGGIHISQTKQLFLEGSL 926
Cdd:COG0318 429 PRTASGKIDRRALRERYAAGAL 450
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
991-1508 |
2.18e-26 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 114.52 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 991 LAEILQWRAQATPDHVLfmlLNAKGTTVctaSCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 1070
Cdd:COG0318 1 LADLLRRAAARHPDRPA---LVFGGRRL---TYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1071 CIPVTVrpphaqNLTATLPTVRMIVDVSKAACILTsqtlmrllrsreaaaavdvktwptiidtddlprkrlpqlykpptp 1150
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1151 emlAYLDFSvS-TTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMEL 1229
Cdd:COG0318 103 ---ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1230 ENnlflWLSTVNQYKIrdTFCSYS---VMELCtkglgnqvEVLKTRGINLSCVRTCVVVAeERPRVALQQSFSKLFKdig 1306
Cdd:COG0318 179 ER----VLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLRLVVSGG-APLPPELLERFEERFG--- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1307 lspRAVSTTFGSrvnvaiclqgT-SGPdptTVYVDLKSLRHDRVRLVergapqslllsesGKILPGVKVVIVNPETKgPV 1385
Cdd:COG0318 241 ---VRIVEGYGL----------TeTSP---VVTVNPEDPGERRPGSV-------------GRPLPGVEVRIVDEDGR-EL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1386 GDSHLGEIWVNSPHTASGYYTiyDSETlqadhfnTRLSFGDAaqtlWARTGYLGFVRrteltaATGErhdaLYVVGALDE 1465
Cdd:COG0318 291 PPGEVGEIVVRGPNVMKGYWN--DPEA-------TAEAFRDG----WLRTGDLGRLD------EDGY----LYIVGRKKD 347
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 55749758 1466 TLELRGLRYHPIDIETSVSRiHRSIAECAVF-----TWTNLLVVVVEL 1508
Cdd:COG0318 348 MIISGGENVYPAEVEEVLAA-HPGVAEAAVVgvpdeKWGERVVAFVVL 394
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
359-928 |
3.37e-23 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 106.36 E-value: 3.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 359 LDMTGKP---VYTLTYGKLWSRslklaytlLNKLGTKNEPVLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPI--- 432
Cdd:PRK12476 56 LDHSHSAagcAVELTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLfap 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 433 EVP--LTRKDAggqqigfLLGSCGIALALTSevclkglpkTQNGEIVQfkgwprlkwvvtdsKYLSKPPKDWQPHI---- 506
Cdd:PRK12476 126 ELPghAERLDT-------ALRDAEPTVVLTT---------TAAAEAVE--------------GFLRNLPRLRRPRViaid 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 507 -----SPAGTEP--------AYIEYKTSKEGSVMGVTVS-RLAMLSHCQALSQACNYSEGETIVNVLDFKKDAGLWHGMF 572
Cdd:PRK12476 176 aipdsAGESFVPveldtddvSHLQYTSGSTRPPVGVEIThRAVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 573 ANVMNKMHTISVPYSVMKTcPLSWVQRVHAHKAKVALVKCR-DLHWAMMAHR----DQRDVSLSSLRMLIvtdGANPWSV 647
Cdd:PRK12476 256 PAVYGGHSTLMSPTAFVRR-PQRWIKALSEGSRTGRVVTAApNFAYEWAAQRglpaEGDDIDLSNVVLII---GSEPVSI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 648 SSCDAFLSLFQSHGLKPEAICPCATSAEA-MTVAIRRPgvpgAPLPGRAILSMNGLSYG-VIRVNTEDKNSALTVQdVGH 725
Cdd:PRK12476 332 DAVTTFNKAFAPYGLPRTAFKPSYGIAEAtLFVATIAP----DAEPSVVYLDREQLGAGrAVRVAADAPNAVAHVS-CGQ 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 726 VMPGGMMCIVKPDGPPQLcKTDEIGEICVSSRTGGMMYFGLAGVTKNTFEV-----IPVNS--AGSPVGDVpFIRSGLLG 798
Cdd:PRK12476 407 VARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGShaDGAADDGT-WLRTGDLG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 799 FVGPGSLvFVVGKMDGLLMVSGRRHNADDIVATglAVESIKTVYRGRIAVFSVSVFYDERIVVVAEQRPDASEEDSFQWM 878
Cdd:PRK12476 485 VYLDGEL-YITGRIADLIVIDGRNHYPQDIEAT--VAEASPMVRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAI 561
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 55749758 879 SRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLFLEGSLHP 928
Cdd:PRK12476 562 DAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1025-1505 |
1.85e-22 |
|
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: 103.52 E-value: 1.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTAtlPTVRMIVDVSK---AA 1101
Cdd:cd05906 44 DLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPN--ARLRKLRHIWQllgSP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1102 CILTSQTLMRLLRSREAAAAVDVKTWPTIIDTDDLPrkRLPQLYkPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCR 1181
Cdd:cd05906 121 VVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTA--ADHDLP-QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1182 AiKLQCELYSSRQIA---ICLDPYCGLGFAlwCLCSVYSGHQSVLIPPMELENNLFLWLSTVNQYKIRDTFCSYSvmeLC 1258
Cdd:cd05906 198 G-KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1259 TKgLGNQVEVLKTRGINLSCVRtCVVVAEERPRVALQQSFSKLFKDIGLSPRAVSTTFGSRVNVAIClqgtsgpdptTVY 1338
Cdd:cd05906 272 AL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCSGV----------IYS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1339 VDLKSLRHD-RVRLVERGAPqslllsesgkiLPGVKVVIVNPETKGpVGDSHLGEIWVNSPHTASGYytiYDSETLQADH 1417
Cdd:cd05906 340 RSFPTYDHSqALEFVSLGRP-----------IPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGY---YNNPEANAEA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1418 FntrLSFGdaaqtlWARTGYLGFVRRTELTaATGERHDALYVvgaldetlelRGLRYHPIDIETSVSRI----HRSIAEC 1493
Cdd:cd05906 405 F---TEDG------WFRTGDLGFLDNGNLT-ITGRTKDTIIV----------NGVNYYSHEIEAAVEEVpgvePSFTAAF 464
|
490
....*....|....*
gi 55749758 1494 AVF---TWTNLLVVV 1505
Cdd:cd05906 465 AVRdpgAETEELAIF 479
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1046-1484 |
2.87e-22 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 103.67 E-value: 2.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1046 GDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPP----HAQNLTATLPTVRMIVDVSKAAcilTSQTLMRLLRSREAAAA 1121
Cdd:PRK12476 92 GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALRDAEPTVVLTTTA---AAEAVEGFLRNLPRLRR 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1122 vdvktwPTIIDTDDLPrKRLPQLYKPPTPEM--LAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSsRQIAIC- 1198
Cdd:PRK12476 169 ------PRVIAIDAIP-DSAGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLD-RNTHGVs 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1199 -LDPYCGLGFALWCLCSVYSGHqSVLIPPMELENNLFLW---LSTVNQYKIRDTFCSYSVMELCT-KGLGNQVEvlktrG 1273
Cdd:PRK12476 241 wLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWikaLSEGSRTGRVVTAAPNFAYEWAAqRGLPAEGD-----D 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1274 INLSCVrtCVVVAEERPRVALQQSFSKLFKDIGLSPRAVSTTFGsrVNVAICLQGTSGPD--PTTVYVDLKSLRHDRVRL 1351
Cdd:PRK12476 315 IDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG--IAEATLFVATIAPDaePSVVYLDREQLGAGRAVR 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1352 VERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTI-YDSETLQADHFNTRLSFGD---- 1426
Cdd:PRK12476 391 VAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRpEETERTFGAKLQSRLAEGShadg 470
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 55749758 1427 -AAQTLWARTGYLGFVRRTEltaatgerhdaLYVVGALDETLELRGLRYHPIDIETSVS 1484
Cdd:PRK12476 471 aADDGTWLRTGDLGVYLDGE-----------LYITGRIADLIVIDGRNHYPQDIEATVA 518
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1046-1484 |
1.76e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 100.96 E-value: 1.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1046 GDNVVLLYPPGIELIAAFYGCLYAGCIPVTV----RPPHAQNLTATLptvrmivDVSKAACILTS----QTLMRLLRSRE 1117
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHAVL-------DDCTPSAILTTtdsaEGVRKFFRARP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1118 AaaavdvKTWPTIIDTDDLPRKrLPQLYKPPTP--EMLAYLDFSVSTTGMLTGVKMSHSAV--NAL--CRAIKLQcelYS 1191
Cdd:PRK07769 152 A------KERPRVIAVDAVPDE-VGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLptNVLqvIDALEGQ---EG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1192 SRQIAiCLDPYCGLGFaLWCLCSVYSGHQSVLIPPMELENNLFLWLSTVNQyKIRDTFCSYSV-----MELCT-KGLGNQ 1265
Cdd:PRK07769 222 DRGVS-WLPFFHDMGL-ITVLLPALLGHYITFMSPAAFVRRPGRWIRELAR-KPGGTGGTFSAapnfaFEHAAaRGLPKD 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1266 VEvlktRGINLSCVRtCVVVAEERPRVALQQSFSKLFKDIGLSPRAVSTTFGsrVNVAICLQGTSGPD--PTTVYVDLKS 1343
Cdd:PRK07769 299 GE----PPLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYG--MAEATLFVSTTPMDeePTVIYVDRDE 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1344 LRHDRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTIYDsETLQADH--FNTR 1421
Cdd:PRK07769 372 LNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPE-ETAATFQniLKSR 450
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55749758 1422 LS----FGDAAQTLWARTGYLGfvrrtelTAATGErhdaLYVVGALDETLELRGLRYHPIDIETSVS 1484
Cdd:PRK07769 451 LSeshaEGAPDDALWVRTGDYG-------VYFDGE----LYITGRVKDLVIIDGRNHYPQDLEYTAQ 506
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
367-829 |
1.81e-21 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 98.92 E-value: 1.81e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 367 YTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVpltrkDAGGQQI 446
Cdd:pfam00501 20 RRLTYRELDERANRLAAGLR-ALG------VGKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPLNP-----RLPAEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 447 GFLLGSCGIALALTSEV--------CLKGLPKTQNGEIVQFKGWPRLKWVVTDSKYLSKPPKdwqPHISPAGTEPAYIEY 518
Cdd:pfam00501 86 AYILEDSGAKVLITDDAlkleelleALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPP---PPPPPDPDDLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 519 kTS------KegsvmGVTVSRLAMLSHCQALSQAC----NYSEGETIVNVLDFKKDAGLWHGMFANVMNKMhTISVPYSV 588
Cdd:pfam00501 163 -TSgttgkpK-----GVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA-TVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 589 MKTCPLSWVQRVHAHKAKV-----ALVKcrdlhwAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLSLFqshglk 663
Cdd:pfam00501 236 PALDPAALLELIERYKVTVlygvpTLLN------MLLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 664 peaicpcatsaeamtvairrpgvpgaplpGRAILSMNGLS--YGVIRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGpP 741
Cdd:pfam00501 302 -----------------------------GGALVNGYGLTetTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDET-G 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 742 QLCKTDEIGEICVSSRTGGMMYFGLAGVTKNTFEvipvnsagspvgDVPFIRSGLLGFVGPgslvfvvgkmDGLLMVSGR 821
Cdd:pfam00501 352 EPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFD------------EDGWYRTGDLGRRDE----------DGYLEIVGR 409
|
....*...
gi 55749758 822 rhnADDIV 829
Cdd:pfam00501 410 ---KKDQI 414
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1025-1496 |
3.39e-20 |
|
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: 96.13 E-value: 3.39e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQN-----LTATLPTVrMIVD--- 1096
Cdd:cd05911 15 QLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADelahqLKISKPKV-IFTDpdg 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1097 ---VSKAACILTSQTLMRLLRSREAAAavdvktwPTIIDTDDLPRKRLPQLYKPP---TPEMLAYLDFSVSTTGMLTGVK 1170
Cdd:cd05911 93 lekVKEAAKELGPKDKIIVLDDKPDGV-------LSIEDLLSPTLGEEDEDLPPPlkdGKDDTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1171 MSHS---AVNALCRAIKLQCELYSSRQIA-ICLDPYCGLgfaLWCLCSVYSGHQSVLIPPMELEnnlfLWLSTVNQYKIR 1246
Cdd:cd05911 166 LSHRnliANLSQVQTFLYGNDGSNDVILGfLPLYHIYGL---FTTLASLLNGATVIIMPKFDSE----LFLDLIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1247 DTFCSYSVMELctkgLGNQVEVLKtrgINLSCVRTCVVVAEerprvALQQSFSKLFKdiglspravsttfgSRVNVAICL 1326
Cdd:cd05911 239 FLYLVPPIAAA----LAKSPLLDK---YDLSSLRVILSGGA-----PLSKELQELLA--------------KRFPNATIK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1327 QG-----TSGPDPTTVYVDLKSlrhdrvrlverGApqslllseSGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTA 1401
Cdd:cd05911 293 QGygmteTGGILTVNPDGDDKP-----------GS--------VGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVM 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1402 SGYYtiydsetlqadhfntrlsfGDAAQTL-------WARTGYLGFVRRTELtaatgerhdaLYVVGALDETLELRGLRY 1474
Cdd:cd05911 354 KGYY-------------------NNPEATKetfdedgWLHTGDIGYFDEDGY----------LYIVDRKKELIKYKGFQV 404
|
490 500
....*....|....*....|..
gi 55749758 1475 HPIDIEtSVSRIHRSIAECAVF 1496
Cdd:cd05911 405 APAELE-AVLLEHPGVADAAVI 425
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1025-1495 |
5.48e-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: 94.25 E-value: 5.48e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltaTLPT--VRMIVDVSKAAC 1102
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDP--------AYPAerLAFILEDAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1103 ILTSQTLmRLLRSREAAAAVDVKTWPTIIDTDDLPrkrLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 1182
Cdd:TIGR01733 76 LLTDSAL-ASRLAGLVLPVILLDPLELAALDDAPA---PPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1183 IKlQCELYSSRQIAICLDPYCGLGFA---LWCLcsvYSGHQSVLIPPMELENNLFLWLSTVNQYKIRDTFCSYSVMELCt 1259
Cdd:TIGR01733 152 LA-RRYGLDPDDRVLQFASLSFDASVeeiFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1260 kglgnqvevLKTRGINLSCVRTCVVVAEErprvalqqsfsklfkdigLSPRAVSTTFGSRVNVAIClqGTSGPDPTTVYV 1339
Cdd:TIGR01733 227 ---------AAALPPALASLRLVILGGEA------------------LTPALVDRWRARGPGARLI--NLYGPTETTVWS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1340 DlkslrhdrVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHFN 1419
Cdd:TIGR01733 278 T--------ATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---LNRPELTAERFV 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55749758 1420 TRLsFGDAAQTLWARTGYLgfVRRteltaatgeRHD-ALYVVGALDETLELRGLRYHPIDIETSVSRiHRSIAECAV 1495
Cdd:TIGR01733 346 PDP-FAGGDGARLYRTGDL--VRY---------LPDgNLEFLGRIDDQVKIRGYRIELGEIEAALLR-HPGVREAVV 409
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
386-910 |
1.26e-18 |
|
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: 91.40 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 386 LNKLGTKNEPVLKPGDRVALVYPNNDPvmFMVAFYGCLLAEVIPVPIEVpltrkdagGQQIGFLLGScgialaltsevcl 465
Cdd:cd05908 26 LGYLGALQELGIKPGQEVVFQITHNNK--FLYLFWACLLGGMIAVPVSI--------GSNEEHKLKL------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 466 kglpktqngeivqFKGWPRLK--WVVTDSKYLSKPPKdwqphispagtEPAYIEYKTSKEGSVMGVTVSRLAMLSHCQAL 543
Cdd:cd05908 83 -------------NKVWNTLKnpYLITEEEVLCELAD-----------ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 544 SQACNYSEGETIVNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVMKTCPLSWVQRVHAHKAKValVKCRDLHWAMMAHR 623
Cdd:cd05908 139 LNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATI--VSSPNFGYKYFLKT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 624 ----DQRDVSLSSLRMLIvtDGANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAmTVAIRRP--GVPGAPLpgraIL 697
Cdd:cd05908 217 lkpeKANDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA-SVGASLPkaQSPFKTI----TL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 698 SMNGLSYGVIRVNTEDKNS-ALTVQDVGHVMPGGMMCIVkpDGPPQLCKTDEIGEICVSSRTGGMMYFGLAGVTKNTFev 776
Cdd:cd05908 290 GRRHVTHGEPEPEVDKKDSeCLTFVEVGKPIDETDIRIC--DEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVF-- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 777 ipvnsagSPVGdvpFIRSGLLGFVGPGSLVfVVGKMDGLLMVSGRRHNADDIVATGLAVESIKTvyrGRIAVFSV--SVF 854
Cdd:cd05908 366 -------TDDG---WLKTGDLGFIRNGRLV-ITGREKDIIFVNGQNVYPHDIERIAEELEGVEL---GRVVACGVnnSNT 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 55749758 855 YDERIVVVAEQRpdASEEDSFQWMSRVLQAID-----SIHQVgvyclalVPANTLPKTPLG 910
Cdd:cd05908 432 RNEEIFCFIEHR--KSEDDFYPLGKKIKKHLNkrggwQINEV-------LPIRRIPKTTSG 483
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
336-956 |
1.74e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.46 E-value: 1.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 336 PPALESALQRWGTTQAKCSCLTALDMTGKPVYTLTYGKLWSRSLKLAYTLLNKLGtknepvlkPGDRVALVYPNNdpVMF 415
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS--------FGDRAVLLFPSG--PDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 416 MVAFYGCLLAEVIPVPIEVPLTRKDAGGQQIGFLLGSCGIALALTSEVCLKGLpktQNGEIVQFKGWPRLKWVVTdskYL 495
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL---LQMEELAAANAPELLCVDT---LD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 496 SKPPKDWQ-PHISPagTEPAYIEYKTSKEGSVMGVTVSRLAMLSHCQALSQ--ACNYSEGETIVNVLDFKKDAGLWHGMF 572
Cdd:PRK05691 152 PALAEAWQePALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHgfGIDLNPDDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 573 ANVMNkmhtiSVPYSVMKTC-----PLSWVQRVHAHKAKVAlvKCRDLHWAMMAHRdqrdVSLSSLRML------IVTDG 641
Cdd:PRK05691 230 QPIFS-----GVPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER----VSESALERLdlsrwrVAYSG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 642 ANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAMTVairrpgVPGAPlPGRAILSMNgLSYGVIRVNTEDKNSALTVQ 721
Cdd:PRK05691 299 SEPIRQDSLERFAEKFAACGFDPDSFFASYGLAEATLF------VSGGR-RGQGIPALE-LDAEALARNRAEPGTGSVLM 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 722 DVGHVMPGGMMCIVKPDGPPQLcKTDEIGEICVSSRTGGMMYFGLAGVTKNTFevipVNSAGSpvgdvPFIRSGLLGFVG 801
Cdd:PRK05691 371 SCGRSQPGHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGDLGFLR 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 802 PGSLvFVVGKMDGLLMVSGRRHNADDIVATglaVES-IKTVYRGRIAVFSVSVFYDERIVVVAE-----QRPDASEEdsf 875
Cdd:PRK05691 441 DGEL-FVTGRLKDMLIVRGHNLYPQDIEKT---VEReVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPPQA--- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 876 qWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLFLEGSLhpcnilmcphTCVTNLPKPRQKQPGVGPA 955
Cdd:PRK05691 514 -LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYALFPALQAVEAAQTAA 582
|
.
gi 55749758 956 S 956
Cdd:PRK05691 583 S 583
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1025-1530 |
1.31e-16 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 85.44 E-value: 1.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNltatlptvrmivdvSKAACIl 1104
Cdd:PRK09192 54 TLRARAEAGARRLLALG-LKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFG--------------GRESYI- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1105 tsQTLMRLLRSREAAAAV---DVKTW---------------PTIIDTDDLPRKRLPqlykPPTPEMLAYLDFSVSTTGML 1166
Cdd:PRK09192 118 --AQLRGMLASAQPAAIItpdELLPWvneathgnpllhvlsHAWFKALPEADVALP----RPTPDDIAYLQYSSGSTRFP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1167 TGVKMSHSAVNALCRAIKLQ-CELYSSRQIAICLDPYCGLGFaLWCLCSVYSGHQSV-LIPPMELENNLFLWLSTVNqyK 1244
Cdd:PRK09192 192 RGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGL-VGFLLTPVATQLSVdYLPTRDFARRPLQWLDLIS--R 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1245 IRDTFcSYSV---MELCTKGLGNQVEVlktrGINLSCVRTCVVVAEE-RPRVAlqQSFSKLFKDIGLSPRAVSTTFG-SR 1319
Cdd:PRK09192 269 NRGTI-SYSPpfgYELCARRVNSKDLA----ELDLSCWRVAGIGADMiRPDVL--HQFAEAFAPAGFDDKAFMPSYGlAE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1320 VNVAIclqgtSGPDPTTvyvDLKSLRHDRVRLVERGA-----PQSLLLSE---SGKILPGVKVVIVNpETKGPVGDSHLG 1391
Cdd:PRK09192 342 ATLAV-----SFSPLGS---GIVVEEVDRDRLEYQGKavapgAETRRVRTfvnCGKALPGHEIEIRN-EAGMPLPERVVG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1392 EIWVNSPHTASGYYTiyDSETLQAdhfntrlsfgdAAQTLWARTGYLGFVrrteltaATGErhdaLYVVGALDETLELRG 1471
Cdd:PRK09192 413 HICVRGPSLMSGYFR--DEESQDV-----------LAADGWLDTGDLGYL-------LDGY----LYITGRAKDLIIING 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55749758 1472 LRYHPIDIETSVSRI----HRSIAECAVFTWTNLLVVVVELC--GSEQEALDLVPLVTNVVLEEH 1530
Cdd:PRK09192 469 RNIWPQDIEWIAEQEpelrSGDAAAFSIAQENGEKIVLLVQCriSDEERRGQLIHALAALVRSEF 533
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1025-1498 |
1.03e-15 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 82.03 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVrpphaqNLTATLPTVRMIVDVSKAACIL 1104
Cdd:cd05959 34 ELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV------NTLLTPDDYAYYLEDSRARVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1105 TSQTLMRLLRsreAAAAVDVKTWPTIIDTD------------DLPRKRLPQLYKPPT-PEMLAYLDFSVSTTGMLTGVKM 1171
Cdd:cd05959 107 VSGELAPVLA---AALTKSEHTLVVLIVSGgagpeagalllaELVAAEAEQLKPAAThADDPAFWLYSSGSTGRPKGVVH 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1172 SHSavnalcrAIKLQCELYSSRQIAICLDPYC----------GLGFALWCLCSVysGHQSVLIPPMELENNLFlwlSTVN 1241
Cdd:cd05959 184 LHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMPERPTPAAVF---KRIR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1242 QYKiRDTFcsYSVMELCTKGLGNqvEVLKTRgiNLSCVRTCVVVAEERPRvalqqsfsklfkDIGLSPRAvsttfgsRVN 1321
Cdd:cd05959 252 RYR-PTVF--FGVPTLYAAMLAA--PNLPSR--DLSSLRLCVSAGEALPA------------EVGERWKA-------RFG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1322 VAIcLQGTSGPDPTTVYVdlkSLRHDRVRLverGApqslllseSGKILPGVKVVIVNpETKGPVGDSHLGEIWVNSPHTA 1401
Cdd:cd05959 306 LDI-LDGIGSTEMLHIFL---SNRPGRVRY---GT--------TGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1402 SGYYTIYDSetlqadhfnTRLSFgdaaQTLWARTGYlGFVRRTELTaatgerhdaLYVVGALDETLELRGLRYHPIDIEt 1481
Cdd:cd05959 370 TMYWNNRDK---------TRDTF----QGEWTRTGD-KYVRDDDGF---------YTYAGRADDMLKVSGIWVSPFEVE- 425
|
490
....*....|....*..
gi 55749758 1482 SVSRIHRSIAECAVFTW 1498
Cdd:cd05959 426 SALVQHPAVLEAAVVGV 442
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
991-1405 |
2.01e-13 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 74.52 E-value: 2.01e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 991 LAEILQWRAQATPDHVLFMLLNAKGTTVctasclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 1070
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYR------ELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1071 CIPVTVRPphaqnltatlptvrmivdvskaacILTSQTLMRLLRSREAAAAVDVKTWPTIIDTDdlprkRLPQLYKPPTP 1150
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAG-----APLGERVALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1151 EMLAYLDFSVSTTGMLTGVKMSHSAV--NAL-CRAIkLQcELYSSRQIAICLDP-YCGLGFALWCLCSVYSGHQSVLIP- 1225
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLvaNALqIKAW-LE-DLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLIPr 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1226 --PMELennlflwLSTVNQYKIrDTFCS----YSvmelctkGLGNQVEVLKtrgINLSCVRTCVvvaeerprvalqqsfs 1299
Cdd:cd05936 203 frPIGV-------LKEIRKHRV-TIFPGvptmYI-------ALLNAPEFKK---RDFSSLRLCI---------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1300 klfkdiglspravsttfgsrvnvaiclqgtSGPDPTTVYVDLKSLRHDRVRLVE-RGapqsllLSES------------- 1365
Cdd:cd05936 249 ------------------------------SGGAPLPVEVAERFEELTGVPIVEgYG------LTETspvvavnpldgpr 292
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 55749758 1366 -----GKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYY 1405
Cdd:cd05936 293 kpgsiGIPLPGTEVKIVDDDGE-ELPPGEVGELWVRGPQVMKGYW 336
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
397-910 |
1.01e-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: 72.47 E-value: 1.01e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 397 LKPGDRVALVYPNNDP---VMFMVAFYGCLLAEVIpvpieVPLTrKDAGGQQIGFLLGSCGIALALTSEvclKGLPKTQN 473
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIVLADA---GAADRLRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 474 GEIVQfkgwpRLKWVVTDSKYLSKPPKDWQPHIsPAGTEPAYIEYKTSKEGSVMGVTVSRLAMLSHCQALSQACNYSEGE 553
Cdd:cd05922 86 ALPAS-----PDPGTVLDADGIRAARASAPAHE-VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 554 TIVNVLDFKKDAGLwhgmfaNVMNK---------MHTISVPysvmktcPLSWVQRVHAHKAK-VALVKCrdlHWAMMAHR 623
Cdd:cd05922 160 RALTVLPLSYDYGL------SVLNThllrgatlvLTNDGVL-------DDAFWEDLREHGATgLAGVPS---TYAMLTRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 624 DQRDVSLSSLRMLIVTDGANPwsvsscDAFLSLFqshglkpeaicpcatsAEAMtvairrpgvpgaplPGRAILSMNGLS 703
Cdd:cd05922 224 GFDPAKLPSLRYLTQAGGRLP------QETIARL----------------RELL--------------PGAQVYVMYGQT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 704 YGVIRVNTEDKNSALTVQD-VGHVMPGGMMCIVKPDGppQLCKTDEIGEICVSSRTGGMMYFglagvtkntfEVIPVNSA 782
Cdd:cd05922 268 EATRRMTYLPPERILEKPGsIGLAIPGGEFEILDDDG--TPTPPGEPGEIVHRGPNVMKGYW----------NDPPYRRK 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 783 GSPVGDVpfIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIKTVyrgriAVFSVSVFYDERIVVV 862
Cdd:cd05922 336 EGRGGGV--LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA-----AAVGLPDPLGEKLALF 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 55749758 863 AEqrpdASEEDSFQWMSRVLQAIDSIHQVGVYClalVPANTLPKTPLG 910
Cdd:cd05922 409 VT----APDKIDPKDVLRSLAERLPPYKVPATV---RVVDELPLTASG 449
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1025-1500 |
3.14e-12 |
|
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: 70.63 E-value: 3.14e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltaTLPTVRM--IVDVSKAAC 1102
Cdd:cd05930 17 ELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDP--------SYPAERLayILEDSGAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1103 ILTsqtlmrllrsreaaaavdvktwptiidtddlprkrlpqlykppTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 1182
Cdd:cd05930 88 VLT-------------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1183 ikLQCELYSSR-----QIAicldpycGLGF--ALWCL-CSVYSGHQSVLIPPmELENNLFLWLSTVNQYKIRDTFCSYSV 1254
Cdd:cd05930 125 --MQEAYPLTPgdrvlQFT-------SFSFdvSVWEIfGALLAGATLVVLPE-EVRKDPEALADLLAEEGITVLHLTPSL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1255 MELCTKGLGNQvevlktrgiNLSCVRTcVVVAEERPRVALQQSFSKLFKDIGLspravsttfgsrVNVaiclqgtSGPDP 1334
Cdd:cd05930 195 LRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELLPGARL------------VNL-------YGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1335 TTVYVDLKSLRHDRVRlvERGAPqslllseSGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYytiYDSETLQ 1414
Cdd:cd05930 246 ATVDATYYRVPPDDEE--DGRVP-------IGRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLARGY---LNRPELT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1415 ADHFnTRLSFGDaaqtlWA---RTGYLgfVRRTEltaatgerHDALYVVGALDETLELRGLRYHPIDIETSVSRiHRSIA 1491
Cdd:cd05930 313 AERF-VPNPFGP-----GErmyRTGDL--VRWLP--------DGNLEFLGRIDDQVKIRGYRIELGEIEAALLA-HPGVR 375
|
....*....
gi 55749758 1492 ECAVFTWTN 1500
Cdd:cd05930 376 EAAVVARED 384
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
999-1521 |
5.91e-12 |
|
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: 69.97 E-value: 5.91e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 999 AQATPDHVLFMllnAKGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGC--IPVTV 1076
Cdd:cd05945 1 AAANPDRPAVV---EGGRTLTYR---ELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1077 RPPHAQnltatlptVRMIVDVSKAACIltsqtlmrllrsreaaaavdvktwptIIDTDDlprkrlpqlykpptpemLAYL 1156
Cdd:cd05945 74 SSPAER--------IREILDAAKPALL--------------------------IADGDD-----------------NAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1157 DFSVSTTGMLTGVKMSHSAVNALCRAIkLQCELYSSRQIAIC----------LDPYCGL--GFALWCLcsvysghqsvli 1224
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNqapfsfdlsvMDLYPALasGATLVPV------------ 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1225 pPMELENNLFLWLSTVNQYKIRDTFCSYSVMELCTKGLGNQVEVLKTrginlscVRTCVVVAEERPRV---ALQQSFskl 1301
Cdd:cd05945 170 -PRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPS-------LRHFLFCGEVLPHKtarALQQRF--- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1302 fkdiglsPRA-VSTTFGS-RVNVAIclqgtsgpdpTTVYVDLKSL-RHDRVRLvergapqslllsesGKILPGVKVVIVN 1378
Cdd:cd05945 239 -------PDArIYNTYGPtEATVAV----------TYIEVTPEVLdGYDRLPI--------------GYAKPGAKLVILD 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1379 PETKgPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHFntrlsFGDAAQTlWARTGYLGFVrrteltAATGErhdaLY 1458
Cdd:cd05945 288 EDGR-PVPPGEKGELVISGPSVSKGY---LNNPEKTAAAF-----FPDEGQR-AYRTGDLVRL------EADGL----LF 347
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55749758 1459 VVGALDETLELRGLRYHPIDIETSVSRiHRSIAECAVFTWTNL-----LVVVVELCGSEqEALDLVPL 1521
Cdd:cd05945 348 YRGRLDFQVKLNGYRIELEEIEAALRQ-VPGVKEAVVVPKYKGekvteLIAFVVPKPGA-EAGLTKAI 413
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1025-1495 |
4.58e-11 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 67.26 E-value: 4.58e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLgDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnlTATLPTVRMIVDVSKAACIL 1104
Cdd:cd05904 37 ELERRVRRLAAGL-AKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1105 TSQTLMRLLRS--------REAAAAVDVKTWPTII-DTDDLPRKRLPQlykpptpEMLAYLDFSVSTTGMLTGVKMSH-S 1174
Cdd:cd05904 110 TTAELAEKLASlalpvvllDSAEFDSLSFSDLLFEaDEAEPPVVVIKQ-------DDVAALLYSSGTTGRSKGVMLTHrN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1175 AVNALCRAIKLQCELYSSRQIAICLDPYCGL-GFALWCLCSVYSGHQSVLIPPMELENnlflWLSTVNQYKIrdTFCSYS 1253
Cdd:cd05904 183 LIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERYKV--THLPVV 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1254 ---VMELCTKGLGNQVEVLKTRGInlSCvrtcvvvaeerprvalqqsfsklfkdiGLSP--RAVSTTFGSRVNVAICLQG 1328
Cdd:cd05904 257 ppiVLALVKSPIVDKYDLSSLRQI--MS---------------------------GAAPlgKELIEAFRAKFPNVDLGQG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1329 ----TSGPDPTTVYVDLKSlrhdrvrlveRGAPQSlllseSGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGY 1404
Cdd:cd05904 308 ygmtESTGVVAMCFAPEKD----------RAKYGS-----VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGY 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1405 ytiydsetlqadhfntrlsFGDAAQTL-------WARTGYLGFVRrteltaATGErhdaLYVVGALDETLELRGLRYHPI 1477
Cdd:cd05904 373 -------------------LNNPEATAatidkegWLHTGDLCYID------EDGY----LFIVDRLKELIKYKGFQVAPA 423
|
490
....*....|....*...
gi 55749758 1478 DIEtSVSRIHRSIAECAV 1495
Cdd:cd05904 424 ELE-ALLLSHPEILDAAV 440
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1025-1421 |
2.30e-10 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 65.44 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTAtLPTVRmivdvSKAACIL 1104
Cdd:PRK06060 35 QIHDGAARLGEVLRNRG-LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHA-LAARN-----TEPALVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1105 TSQTlmrlLRSREAAAavdvktwpTIIDTDDL---PRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSH----SAVN 1177
Cdd:PRK06060 108 TSDA----LRDRFQPS--------RVAEAAELmseAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHadplTFVD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1178 ALCR-AIKLqcelySSRQIAIC---LDPYCGLGFALWCLCSVYSghqSVLIPPMELENNLFLWLSTVNQ----YKIRDTF 1249
Cdd:PRK06060 176 AMCRkALRL-----TPEDTGLCsarMYFAYGLGNSVWFPLATGG---SAVINSAPVTPEAAAILSARFGpsvlYGVPNFF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1250 CsySVMELCTKGlgnqvevlktrgiNLSCVRtCVVVAEERPRVALQQSFSKLFKDI----GLSPRAVSTTFGSRVnvaic 1325
Cdd:PRK06060 248 A--RVIDSCSPD-------------SFRSLR-CVVSAGEALELGLAERLMEFFGGIpildGIGSTEVGQTFVSNR----- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1326 lqgtsgpdpttvyvdlkslrhdrvrlVERGAPQSLllsesGKILPGVKVVIVNPE--TKGPVGDshlGEIWVNSPHTASG 1403
Cdd:PRK06060 307 --------------------------VDEWRLGTL-----GRVLPPYEIRVVAPDgtTAGPGVE---GDLWVRGPAIAKG 352
|
410
....*....|....*...
gi 55749758 1404 YYTIYDSETLQADHFNTR 1421
Cdd:PRK06060 353 YWNRPDSPVANEGWLDTR 370
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1150-1480 |
2.60e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 64.82 E-value: 2.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1150 PEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMEL 1229
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1230 ENNLFLWLSTVNQYKIRDTFCSysvmELCTKGLGNQVEVLKTRGINLSCVRTCVVVAEerP-RVALQQSFSKLFKDIGLS 1308
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSP----NFGYKYFLKTLKPEKANDWDLSSIRMILNGAE--PiDYELCHEFLDHMSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1309 PRAVSTTFG-SRVNVAICLQGTSGPdPTTVYVDLKSLRH-DRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGpVG 1386
Cdd:cd05908 259 RNAILPVYGlAEASVGASLPKAQSP-FKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1387 DSHLGEIWVNSPHTASGYYTiydsetlqadhfNTRLSFGDAAQTLWARTGYLGFVRRTELTaATGERHDALYVvgaldet 1466
Cdd:cd05908 337 DGYIGHIQIRGKNVTPGYYN------------NPEATAKVFTDDGWLKTGDLGFIRNGRLV-ITGREKDIIFV------- 396
|
330
....*....|....
gi 55749758 1467 lelRGLRYHPIDIE 1480
Cdd:cd05908 397 ---NGQNVYPHDIE 407
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1025-1495 |
4.18e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 64.40 E-value: 4.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGHLNAgdnVVLLYPPGIELIAAFYGCLYAG----CIPVTVRPPHAQNLTATLPTVRMIVDVSKa 1100
Cdd:PRK05851 36 EVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1101 acILTSQTLMRLLRSREAAAAV-DVKTWPtiidtddlpRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNAL 1179
Cdd:PRK05851 112 --VLSHGSHLERLRAVDSSVTVhDLATAA---------HTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1180 CRAIKLQCELYSSRQIAICLDP-YCGLGFAlWCLCSVYSGHQSVLIPPMELENNLFLWLSTVNQYkiRDTFC-----SYS 1253
Cdd:PRK05851 181 LRGLNARVGLDAATDVGCSWLPlYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDS--RATLTaapnfAYN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1254 VmelctkgLGNQVEvlKTRGINLSCVRTCVVVAEerP-RVALQQSFSKLFKDIGLSPRAVSTTFGsrVNVAIClqGTSGP 1332
Cdd:PRK05851 258 L-------IGKYAR--RVSDVDLGALRVALNGGE--PvDCDGFERFATAMAPFGFDAGAAAPSYG--LAESTC--AVTVP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1333 DPTTvyvdlkSLRHDRVRLVERGAPQSLLLSesGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYytiYDSET 1412
Cdd:PRK05851 323 VPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY---LGQAP 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1413 LQADHfntrlsfgdaaqtlWARTGYLGFvrrteLTAatgerhDALYVVGALDETLELRGLRYHPIDIETSVSRIhRSIAE 1492
Cdd:PRK05851 392 IDPDD--------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERVAAQV-RGVRE 445
|
...
gi 55749758 1493 CAV 1495
Cdd:PRK05851 446 GAV 448
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1025-1512 |
2.40e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 61.54 E-value: 2.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPH-AQNLtatlptvRMIVDVSKAACI 1103
Cdd:cd12116 17 ELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYpADRL-------RYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1104 LTSQTLMrllrsreAAAAVDVKTWPTIIDTDDLPRKRLPqlyKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAI 1183
Cdd:cd12116 89 LTDDALP-------DRLPAGLPVLLLALAAAAAAPAAPR---TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1184 KLQCELYSSRQIaICLDPYCglgFALwclcsvysghqSVLippmelenNLFLWLSTVNQYKIRDTFCSYSVMELctkglg 1263
Cdd:cd12116 159 RERLGLGPGDRL-LAVTTYA---FDI-----------SLL--------ELLLPLLAGARVVIAPRETQRDPEAL------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1264 nqVEVLKTRGINlscvrtcvvVAEERPrvalqqSFSKLFKDIGLSPR----------AVSTTFGSR-VNVAICLQGTSGP 1332
Cdd:cd12116 210 --ARLIEAHSIT---------VMQATP------ATWRMLLDAGWQGRagltalcggeALPPDLAARlLSRVGSLWNLYGP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1333 DPTTVYvdlkSLRHdRVRLVERGAPqslllseSGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYytiYDSET 1412
Cdd:cd12116 273 TETTIW----STAA-RVTAAAGPIP-------IGRPLANTQVYVLDAALR-PVPPGVPGELYIGGDGVAQGY---LGRPA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1413 LQADHFnTRLSFGDAAQTLWaRTGYLgfVRRteltaatgERHDALYVVGALDETLELRGLRYHPIDIETSVSRiHRSIAE 1492
Cdd:cd12116 337 LTAERF-VPDPFAGPGSRLY-RTGDL--VRR--------RADGRLEYLGRADGQVKIRGHRIELGEIEAALAA-HPGVAQ 403
|
490 500
....*....|....*....|....
gi 55749758 1493 CAVFTWTN----LLVVVVELCGSE 1512
Cdd:cd12116 404 AAVVVREDggdrRLVAYVVLKAGA 427
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
528-912 |
4.77e-09 |
|
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: 59.99 E-value: 4.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 528 GVTVSRLAMLSHCQALSQACNYSEGETIVNVLDFKKDAGLWhGMFANVMNKMHTISVPysvmKTCPLSWVQRVHAHKAKV 607
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP----KFDPEAALELIEREKVTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 608 ALVKcRDLHWAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLSLF-----QSHGLkPEAICPCATSAEAMtvAIR 682
Cdd:cd04433 92 LLGV-PTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAPgiklvNGYGL-TETGGTVATGPPDD--DAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 683 RPGVPGAPLPGRAILsmnglsygvirvntedknsaltvqdvghvmpggmmcIVKPDGPPqlCKTDEIGEICVssrTGGMM 762
Cdd:cd04433 166 KPGSVGRPVPGVEVR------------------------------------IVDPDGGE--LPPGEIGELVV---RGPSV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 763 YFGLAGVTKNTFEVIPvnsAGspvgdvpFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIKTVy 842
Cdd:cd04433 205 MKGYWNNPEATAAVDE---DG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEA- 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55749758 843 rgriAVFSVsvfYDER------IVVVAEQRPDASEEDSFQWMSRVLQAIDSIHQVgvyclalVPANTLPKTPLGGI 912
Cdd:cd04433 274 ----AVVGV---PDPEwgervvAVVVLRPGADLDAEELRAHVRERLAPYKVPRRV-------VFVDALPRTASGKI 335
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
593-921 |
8.89e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 60.01 E-value: 8.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 593 PLSWVQRVHAHKAKVALVKcrDLHWAMMAHR-----DQRDVSLSSLRmlIVTDGANPWSVSSCDAFLSLFQSHGLKPEAI 667
Cdd:PRK07768 235 PLLWAELISKYRGTMTAAP--NFAYALLARRlrrqaKPGAFDLSSLR--FALNGAEPIDPADVEDLLDAGARFGLRPEAI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 668 CPCATSAEAmTVAIRRPGvPGAPL----PGRAILSMNGlsygviRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGppQL 743
Cdd:PRK07768 311 LPAYGMAEA-TLAVSFSP-CGAGLvvdeVDADLLAALR------RAVPATKGNTRRLATLGPPLPGLEVRVVDEDG--QV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 744 CKTDEIGEICVSSRTggmmyfglagVTKNtfeVIPVNSAGSPVGDVPFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRH 823
Cdd:PRK07768 381 LPPRGVGVIELRGES----------VTPG---YLTMDGFIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNI 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 824 NADDIVAtglAVESIKTVYRGRIavfsVSVFYD-----ERIVVVAEQRPDASEEDSFQWMSRVLQAIDSihQVGV--YCL 896
Cdd:PRK07768 448 YPTDIER---AAARVEGVRPGNA----VAVRLDaghsrEGFAVAVESNAFEDPAEVRRIRHQVAHEVVA--EVGVrpRNV 518
|
330 340
....*....|....*....|....*
gi 55749758 897 ALVPANTLPKTPLGGIHISQTKQLF 921
Cdd:PRK07768 519 VVLGPGSIPKTPSGKLRRANAAELV 543
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
369-839 |
9.06e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.74 E-value: 9.06e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 369 LTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNDPVMfmVAFYGCLLA--EVIPVPIEVPltrkdagGQQI 446
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLR-ARG------VGPEVRVAIAAERSFELV--VALLAVLKAggAYVPLDPNYP-------AERL 2092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 447 GFLLGSCGIALALTSEVCLKGLPKTQngeivqfkGWPRLKwvVTDSKYLSKPPkDWQPHISPAGTEPAYIEYKTSKEGSV 526
Cdd:PRK12316 2093 AYMLEDSGAALLLTQRHLLERLPLPA--------GVARLP--LDRDAEWADYP-DTAPAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 527 MGVTVSRLAMLSHCQALSQACNYSEGETIVNVLDFKKDAGLWhGMFANVMNKMHTISVPYSVMKtcPLSWVQRVHAHkaK 606
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDELWD--PEQLYDEMERH--G 2236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 607 VALVKCRDLHWAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLS------LFQSHGLKPEAICPCATSAEAmTVA 680
Cdd:PRK12316 2237 VTILDFPPVYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEalrpvyLFNGYGPTEAVVTPLLWKCRP-QDP 2313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 681 IRRPGVP-GAPLPGRAilsmnglsygvirvntedknsaltvqdvGHVMPGGMmcivkpdgppQLCKTDEIGEICVSSRTG 759
Cdd:PRK12316 2314 CGAAYVPiGRALGNRR----------------------------AYILDADL----------NLLAPGMAGELYLGGEGL 2355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 760 GMMYFGLAGVTKNTFEVIPVNSAGSPVgdvpfIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIK 839
Cdd:PRK12316 2356 ARGYLNRPGLTAERFVPDPFSASGERL-----YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVR 2430
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
999-1194 |
2.65e-08 |
|
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: 58.51 E-value: 2.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 999 AQATPDHVLfmlLNAKGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG--CIPVTV 1076
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGaaYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1077 RPPhAQNLTAtlptvrmIVDVSKAACILTSQTLM-RLLRSREAAAAVDVKTWPTIIDTDDLPrkrlpqlykPPTPEMLAY 1155
Cdd:cd17651 78 AYP-AERLAF-------MLADAGPVLVLTHPALAgELAVELVAVTLLDQPGAAAGADAEPDP---------ALDADDLAY 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 55749758 1156 LDFSVSTTGMLTGVKMSHSAVNALCRAiklQCELYSSRQ 1194
Cdd:cd17651 141 VIYTSGSTGRPKGVVMPHRSLANLVAW---QARASSLGP 176
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
339-437 |
2.74e-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: 58.34 E-value: 2.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 339 LESALQRWGTTqakcsclTALDMTGKPvytLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNdpVMFMVA 418
Cdd:cd05936 5 LEEAARRFPDK-------TALIFMGRK---LTYRELDALAEAFAAGLQN-LG------VQPGDRVALMLPNC--PQFPIA 65
|
90
....*....|....*....
gi 55749758 419 FYGCLLAEVIPVPIEVPLT 437
Cdd:cd05936 66 YFGALKAGAVVVPLNPLYT 84
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
991-1440 |
2.88e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 58.37 E-value: 2.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 991 LAEILQWRAQATPDHVLFMLLNAKGTTV----CTASCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGC 1066
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVAVPGGRGADGklayDELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1067 LYAGCIPVTVRP----------------------PHAQNLTATL----PTVRMIVDVSKaACILTSQTLMRLLRSREAAA 1120
Cdd:PRK09274 87 FKAGAVPVLVDPgmgiknlkqclaeaqpdafigiPKAHLARRLFgwgkPSVRRLVTVGG-RLLWGGTTLATLLRDGAAAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1121 avdvktwptiidtddlprkrlPQLYKPPTPEMLAYLdFSVSTTGMLTGVKMSHSAVNALCRAIKlqcELYSSRQIAICL- 1199
Cdd:PRK09274 166 ---------------------FPMADLAPDDMAAIL-FTSGSTGTPKGVVYTHGMFEAQIEALR---EDYGIEPGEIDLp 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1200 --------DPYCGlgfalwcLCSVysghqsvlIPPMELE-----NNLFLWlSTVNQYKIRDTFCSYSVMELctkgLGNQv 1266
Cdd:PRK09274 221 tfplfalfGPALG-------MTSV--------IPDMDPTrpatvDPAKLF-AAIERYGVTNLFGSPALLER----LGRY- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1267 evLKTRGINLSCVRTcVVVAEERPRVALQQSFSKLfkdigLSPRA-VSTTFGSRVNVAICLqgtsgpdpttvyVDLKSLR 1345
Cdd:PRK09274 280 --GEANGIKLPSLRR-VISAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS------------IESREIL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1346 HDRVRLVERGAPQSLllsesGKILPGVKVVIVNPeTKGPVGDSH---------LGEIWVNSPHTASGYYTiYDSETLQAd 1416
Cdd:PRK09274 340 FATRAATDNGAGICV-----GRPVDGVEVRIIAI-SDAPIPEWDdalrlatgeIGEIVVAGPMVTRSYYN-RPEATRLA- 411
|
490 500
....*....|....*....|....
gi 55749758 1417 hfntRLSfgDAAQTLWARTGYLGF 1440
Cdd:PRK09274 412 ----KIP--DGQGDVWHRMGDLGY 429
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
991-1165 |
3.06e-08 |
|
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: 58.23 E-value: 3.06e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 991 LAEILQWRAQATPDHVlfmllnAkgtTVCTASCL---QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCL 1067
Cdd:COG1021 27 LGDLLRRRAERHPDRI------A---VVDGERRLsyaELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALF 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1068 YAGCIPVTVRPPH-AQNLTAtlptvrmIVDVSKAACILTSQTLmRLLRSREAAAAVdVKTWPT----IIDTDDLPRKRLP 1142
Cdd:COG1021 97 RAGAIPVFALPAHrRAEISH-------FAEQSEAVAYIIPDRH-RGFDYRALAREL-QAEVPSlrhvLVVGDAGEFTSLD 167
|
170 180 190
....*....|....*....|....*....|.
gi 55749758 1143 QLYKPPTPEMLAYLD------FSVS--TTGM 1165
Cdd:COG1021 168 ALLAAPADLSEPRPDpddvafFQLSggTTGL 198
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1024-1495 |
3.59e-08 |
|
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: 57.86 E-value: 3.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1024 LQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltatlptvrmivdvskaacI 1103
Cdd:cd05919 14 GQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP------------------------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1104 LTSQTLMRLLRSREAAAavdvktwpTIIDTDDlprkrlpqlykpptpemLAYLDFSVSTTGMLTGVKMSHSA----VNAL 1179
Cdd:cd05919 69 LHPDDYAYIARDCEARL--------VVTSADD-----------------IAYLLYSSGTTGPPKGVMHAHRDpllfADAM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1180 CR---AIKLQCELYSSRQIAICLdpycGLGFALWclCSVYSGHQSVLIPPMELENNLFlwlSTVNQYKIRdTFCSYSVME 1256
Cdd:cd05919 124 ARealGLTPGDRVFSSAKMFFGY----GLGNSLW--FPLAVGASAVLNPGWPTAERVL---ATLARFRPT-VLYGVPTFY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1257 LCTKGLGNQVEVLktrginLSCVRTCVVVAEERPRVALQQsfsklFKDIGLSPraVSTTFGSRVNVAICLqgtsgpdptt 1336
Cdd:cd05919 194 ANLLDSCAGSPDA------LRSLRLCVSAGEALPRGLGER-----WMEHFGGP--ILDGIGATEVGHIFL---------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1337 vyvdlkSLRHDRVRlvergapqsllLSESGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYYTIYDSetlqad 1416
Cdd:cd05919 251 ------SNRPGAWR-----------LGSTGRPVPGYEIRLVDEEGH-TIPPGEEGDLLVRGPSAAVGYWNNPEK------ 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55749758 1417 hfnTRLSFGDAaqtlWARTGYLGFVrrteltAATGerhdALYVVGALDETLELRGLRYHPIDIETSVSRiHRSIAECAV 1495
Cdd:cd05919 307 ---SRATFNGG----WYRTGDKFCR------DADG----WYTHAGRADDMLKVGGQWVSPVEVESLIIQ-HPAVAEAAV 367
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
988-1183 |
3.70e-08 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 58.71 E-value: 3.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 988 HQFLAEilqwRAQATPDHV-LfmllnakgttVCTASCL---QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAF 1063
Cdd:COG1020 479 HELFEA----QAARTPDAVaV----------VFGDQSLtyaELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVAL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1064 YGCLYAGC--IPvtvrpphaqnLTATLPT--VRMIVDVSKAACILTSQTLMRLLRSREAaaavdvktwpTIIDTDDLPRK 1139
Cdd:COG1020 544 LAVLKAGAayVP----------LDPAYPAerLAYMLEDAGARLVLTQSALAARLPELGV----------PVLALDALALA 603
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 55749758 1140 RLPQ--LYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAI 1183
Cdd:COG1020 604 AEPAtnPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWM 649
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1025-1495 |
5.57e-08 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 57.10 E-value: 5.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltatlptvrmivdvskaacil 1104
Cdd:cd05958 15 DLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP-------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1105 tsqtlmrLLRSREAAAAVDvKTWPTIIDTDDlprkrlpqlyKPPTPEMLAYLDFSVSTTGMLTGVKMSHsavnalcRAIK 1184
Cdd:cd05958 69 -------LLRPKELAYILD-KARITVALCAH----------ALTASDDICILAFTSGTTGAPKATMHFH-------RDPL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1185 LQCELYsSRQI--AICLDPYCGL-------GFALWCLCSVYSGHQSVLIP---PMELennlflwLSTVNQYKIRDTF--- 1249
Cdd:cd05958 124 ASADRY-AVNVlrLREDDRFVGSpplaftfGLGGVLLFPFGVGASGVLLEeatPDLL-------LSAIARYKPTVLFtap 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1250 CSYSVMelctkglgnqVEVLKTRGINLSCVRTCVVVAEerprvALQQSFSKLFKDiglspravstTFGSRVnvaicLQGT 1329
Cdd:cd05958 196 TAYRAM----------LAHPDAAGPDLSSLRKCVSAGE-----ALPAALHRAWKE----------ATGIPI-----IDGI 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1330 SGPDPTTVYVdlkSLRHDRVRLverGApqslllseSGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPhtaSGYYtiYD 1409
Cdd:cd05958 246 GSTEMFHIFI---SARPGDARP---GA--------TGKPVPGYEAKVVDDEGN-PVPDGTIGRLAVRGP---TGCR--YL 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1410 SETLQADHF-NTRLSFGDAaqTLWARTGYLGFVRRTeltaatgerhDALYVVGaldetlelrGLRYHPIDIEtSVSRIHR 1488
Cdd:cd05958 306 ADKRQRTYVqGGWNITGDT--YSRDPDGYFRHQGRS----------DDMIVSG---------GYNIAPPEVE-DVLLQHP 363
|
....*..
gi 55749758 1489 SIAECAV 1495
Cdd:cd05958 364 AVAECAV 370
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1026-1440 |
5.99e-08 |
|
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: 57.09 E-value: 5.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1026 LHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltatlptvRMIVdvskaacilt 1105
Cdd:cd05910 8 LDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP-------------GMGR---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1106 sQTLMRLLRSREAAAAVDVktwptiidtddlprkrlpqlykpPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKl 1185
Cdd:cd05910 64 -KNLKQCLQEAEPDAFIGI-----------------------PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALR- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1186 qcELYSSRQIAICLDpycglGFALWCLCSVYSGHQSVlIPPMELE-----NNLFLwLSTVNQYKIRDTFCSYSVMELCTk 1260
Cdd:cd05910 119 --QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDPTrparaDPQKL-VGAIRQYGVSIVFGSPALLERVA- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1261 glgnqvEVLKTRGINLSCVRtCVVVAEERPRVALQQSFSKLfkdigLSPRA-VSTTFGSRVNVAICLQGTSgpdpttvyv 1339
Cdd:cd05910 189 ------RYCAQHGITLPSLR-RVLSAGAPVPIALAARLRKM-----LSDEAeILTPYGATEALPVSSIGSR--------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1340 dlkSLRHDRVRLVERGAPQSLllsesGKILPGVKVVIVnPETKGPV---GDSH------LGEIWVNSPHTASGYYTIYDS 1410
Cdd:cd05910 248 ---ELLATTTAATSGGAGTCV-----GRPIPGVRVRII-EIDDEPIaewDDTLelprgeIGEITVTGPTVTPTYVNRPVA 318
|
410 420 430
....*....|....*....|....*....|
gi 55749758 1411 ETLQADHfntrlsfgDAAQTLWARTGYLGF 1440
Cdd:cd05910 319 TALAKID--------DNSEGFWHRMGDLGY 340
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1025-1495 |
1.09e-07 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 56.16 E-value: 1.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGC--IPVTVRPPHAQNltatlptvRMIVDVSKAAC 1102
Cdd:cd17643 17 ELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGayVPIDPAYPVERI--------AFILADSGPSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1103 ILTsqtlmrllrsreaaaavdvktwptiidtddlprkrlpqlykppTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 1182
Cdd:cd17643 88 LLT-------------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1183 IklQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMEL---ENNLFLWLS----TV-NQykirdTFCSYSV 1254
Cdd:cd17643 125 T--QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVarsPEDFARLLRdegvTVlNQ-----TPSAFYQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1255 MelctkglgnqVEVLKTRGINLSCVRTcVVVAEERPRVALQQSFSKLFKDigLSPRAVSTTfgsrvnvaiclqgtsGPDP 1334
Cdd:cd17643 198 L----------VEAADRDGRDPLALRY-VIFGGEALEAAMLRPWAGRFGL--DRPQLVNMY---------------GITE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1335 TTVYVDLKSLRHDRVRLVERgapqslllSESGKILPGVKVVIVNpETKGPVGDSHLGEIWVNSPHTASGYYtiyDSETLQ 1414
Cdd:cd17643 250 TTVHVTFRPLDAADLPAAAA--------SPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYL---GRPELT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1415 ADHFNTrLSFGDAAQTLWaRTGYLgfVRRTeltaATGErhdaLYVVGALDETLELRGLRYHPIDIETSVSRiHRSIAECA 1494
Cdd:cd17643 318 AERFVA-NPFGGPGSRMY-RTGDL--ARRL----PDGE----LEYLGRADEQVKIRGFRIELGEIEAALAT-HPSVRDAA 384
|
.
gi 55749758 1495 V 1495
Cdd:cd17643 385 V 385
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
998-1181 |
1.38e-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: 1.38e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 998 RAQATPDHVLfmlLNAKGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVR 1077
Cdd:cd12117 6 QAARTPDAVA---VVYGDRSLTYA---ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1078 PphaqnltaTLPTVRM--IVDVSKAACILTSQTLMRLLRSREaaaavdvktwPTIIDTDDLPRKRLPQLYKPPTPEMLAY 1155
Cdd:cd12117 79 P--------ELPAERLafMLADAGAKVLLTDRSLAGRAGGLE----------VAVVIDEALDAGPAGNPAVPVSPDDLAY 140
|
170 180
....*....|....*....|....*.
gi 55749758 1156 LDFSVSTTGMLTGVKMSHSAVNALCR 1181
Cdd:cd12117 141 VMYTSGSTGRPKGVAVTHRGVVRLVK 166
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
370-822 |
4.87e-07 |
|
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: 54.19 E-value: 4.87e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 370 TYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEV--PLTRkdaggqqIG 447
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAER-------LA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 448 FLLGSCGIALALTSEvclkglpktQNGEIVQFKGWPRLKWVVTDSKYLSKPPKDWQPHISPAGTEPAYIEYkTSkeGSV- 526
Cdd:TIGR01733 66 FILEDAGARLLLTDS---------ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 527 --MGVTVSRLAMLSHCQALSQACNYSEGETIVNVLDFKKDAGLWHgMFANVMNKMHTISVPYSVMKTCPLSWvQRVHAHK 604
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-AALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 605 aKVALVKCRDLHWAMMAhrDQRDVSLSSLRMLIVtdganpwsvsscdaflslfqshglkpeaicpcatSAEAMTVA-IRR 683
Cdd:TIGR01733 212 -PVTVLNLTPSLLALLA--AALPPALASLRLVIL----------------------------------GGEALTPAlVDR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 684 pgvPGAPLPGRAILSMnglsYG---------VIRVnTEDKNSALTVQDVGHVMPGGMMCIVKPDGppQLCKTDEIGEICV 754
Cdd:TIGR01733 255 ---WRARGPGARLINL----YGptettvwstATLV-DPDDAPRESPVPIGRPLANTRLYVLDDDL--RPVPVGVVGELYI 324
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55749758 755 SSRTGGMMYFGLAGVTKNTFevipVNSAGSPVGDVPFIRSGLLGFVGP-GSLVFvVGKMDGLLMVSGRR 822
Cdd:TIGR01733 325 GGPGVARGYLNRPELTAERF----VPDPFAGGDGARLYRTGDLVRYLPdGNLEF-LGRIDDQVKIRGYR 388
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
368-501 |
9.03e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 53.43 E-value: 9.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 368 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALvYPNNDPvMFMVAFYGCLLAEVIPVPIEvPLTRKDaggqQIG 447
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLL-YMQNSP-QFVIAYYAILRANAVVVPVN-PMNREE----ELA 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 55749758 448 FLLGSCGIALALTSEVCLkglpktqnGEIVQFKGWPRLKWVVTD--SKYLSKPPKD 501
Cdd:PRK08314 102 HYVTDSGARVAIVGSELA--------PKVAPAVGNLRLRHVIVAqySDYLPAEPEI 149
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
967-1183 |
1.22e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 1.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 967 RIAQAAGRDLGQI-----EENDLV---------------RKHQFLAEilqwRAQATPDHVlfmllnakgTTVCTASCL-- 1024
Cdd:PRK12316 1965 QMAEDAQAALGELalldaGERQRIladwdrtpeayprgpGVHQRIAE----QAARAPEAI---------AVVFGDQHLsy 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 -QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHaqnltatlPTVR---MIVDvSKA 1100
Cdd:PRK12316 2032 aELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY--------PAERlayMLED-SGA 2101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1101 ACILTSQTLMRLLRSREAAAAVDVKT---WPtiidtdDLPRKR-LPQLykppTPEMLAYLDFSVSTTGMLTGVKMSHSAV 1176
Cdd:PRK12316 2102 ALLLTQRHLLERLPLPAGVARLPLDRdaeWA------DYPDTApAVQL----AGENLAYVIYTSGSTGLPKGVAVSHGAL 2171
|
....*..
gi 55749758 1177 NALCRAI 1183
Cdd:PRK12316 2172 VAHCQAA 2178
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
368-642 |
1.53e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 52.60 E-value: 1.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 368 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLTrkdagGQQIG 447
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAA-LG------IGKGDRVAIWAPNS--PHWVIAALGALKAGAVVVPLNTRYT-----ADEAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 448 FLLGSCGIALAL-------TSEVCLKGLPKTQNGEIVQF-KGWPRLKWVVTDSKYLSKPPKDWQpHISPAGTEPAYIEYk 519
Cdd:PRK07656 96 YILARGDAKALFvlglflgVDYSATTRLPALEHVVICETeEDDPHTEKMKTFTDFLAAGDPAER-APEVDPDDVADILF- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 520 TSkegsvmGVT-VSRLAMLSHCQALSQA---CNY---SEGETIVNVLDFKKDAGLWHGMFANVMNKMHTISVPysvmKTC 592
Cdd:PRK07656 174 TS------GTTgRPKGAMLTHRQLLSNAadwAEYlglTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP----VFD 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 55749758 593 PLSWVQRVHAHKAKVaLVKCRDLHWAMMAHRDQRDVSLSSLRmLIVTDGA 642
Cdd:PRK07656 244 PDEVFRLIETERITV-LPGPPTMYNSLLQHPDRSAEDLSSLR-LAVTGAA 291
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
991-1186 |
3.51e-06 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 51.64 E-value: 3.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 991 LAEILQWRAQATPDHVLFMLLNAKGTTVCTASclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 1070
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSLTWA--EFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1071 CIPVTVRPphaqnlTATLPTVRMIVDVSKAACILTS--QTLMRLLRSREAAAAV---------------DVKTWPTIID- 1132
Cdd:COG1022 90 AVTVPIYP------TSSAEEVAYILNDSGAKVLFVEdqEQLDKLLEVRDELPSLrhivvldprglrddpRLLSLDELLAl 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 55749758 1133 -TDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSH----SAVNALCRAIKLQ 1186
Cdd:COG1022 164 gREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHrnllSNARALLERLPLG 222
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
368-559 |
4.41e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 51.09 E-value: 4.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 368 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNDpvMFMVAFYGCLLAEVIPVPIEVPLTrkdagGQQIG 447
Cdd:PRK08316 36 SWTYAELDAAVNRVAAALLD-LG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLT-----GEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 448 FLLGSCGIALALTSEVCLKGLPKTQNGEIVQFKGWPRL--------KWVVTDSKYLSKPpkDWQPHISPAGTEPAYIEYk 519
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVlggreapgGWLDFADWAEAGS--VAEPDVELADDDLAQILY- 178
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 55749758 520 TSKegsvmgvTVSRL--AMLSHCQALSQ------ACNYSEGETIVNVL 559
Cdd:PRK08316 179 TSG-------TESLPkgAMLTHRALIAEyvscivAGDMSADDIPLHAL 219
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1025-1183 |
6.11e-06 |
|
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: 50.73 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltaTLPTVRMIVDVSKAACil 1104
Cdd:cd12114 17 ELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDI--------DQPAARREAILADAGA-- 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 55749758 1105 tsqtlmRLLRSREAAAAVDVKTWPTIIDTDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAI 1183
Cdd:cd12114 86 ------RLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
368-638 |
8.77e-06 |
|
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: 50.63 E-value: 8.77e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 368 TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPI--EVPLTRkdaggqq 445
Cdd:COG1020 501 SLTYAELNARANRLAHHLR-ALG------VGPGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLdpAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 446 IGFLLGSCGIALALTSEVCLKGLPKTQngeivqfkgwprLKWVVTDSKYLSKPPKDWqPHISPAGTEPAYIEYkTS---- 521
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPELG------------VPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TSgstg 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 522 --KegsvmGVTVSRLAMLSHCQALSQACNYSEGETIVNV--LDFkkDAGLWhGMFANVMNKMHTISVPYSVMKTcPLSWV 597
Cdd:COG1020 631 rpK-----GVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW-EIFGALLSGATLVLAPPEARRD-PAALA 701
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 55749758 598 QRVHAHkaKVALVKCRDLHWAMMAHRDQRDvsLSSLRMLIV 638
Cdd:COG1020 702 ELLARH--RVTVLNLTPSLLRALLDAAPEA--LPSLRLVLV 738
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
995-1496 |
1.43e-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: 49.53 E-value: 1.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 995 LQWRAQATPDHVLFMLLnakGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPV 1074
Cdd:cd17631 1 LRRRARRHPDRTALVFG---GRSLTYA---ELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1075 tvrpPHAQNLTAtlPTVRMIVDVSKAACILtsqtlmrllrsreaaaavdvktwptiidtDDLprkrlpqlykpptpemlA 1154
Cdd:cd17631 74 ----PLNFRLTP--PEVAYILADSGAKVLF-----------------------------DDL-----------------A 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1155 YLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELySSRQIAICLDPYCGLGFA-LWCLCSVYSGHQSVLIPPMELENnl 1233
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPET-- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1234 flWLSTVNQYKIRDTFCSYSVME-LCTKGlgnqvevlKTRGINLSCVRtCVVVAEERPRVALQQSFsklfKDIGLsprAV 1312
Cdd:cd17631 179 --VLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV---KF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1313 STTFGsrvnvaiclQGTSGPdPTTVyvdlksLRHDRVRlvergapqSLLLSeSGKILPGVKVVIVNPETKgPVGDSHLGE 1392
Cdd:cd17631 241 VQGYG---------MTETSP-GVTF------LSPEDHR--------RKLGS-AGRPVFFVEVRIVDPDGR-EVPPGEVGE 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1393 IWVNSPHTASGYYTiyDSETlqadhfnTRLSFGDAaqtlWARTGYLGFVrrteltaatgeRHDA-LYVVGALDETLELRG 1471
Cdd:cd17631 295 IVVRGPHVMAGYWN--RPEA-------TAAAFRDG----WFHTGDLGRL-----------DEDGyLYIVDRKKDMIISGG 350
|
490 500
....*....|....*....|....*
gi 55749758 1472 LRYHPIDIETSVSRiHRSIAECAVF 1496
Cdd:cd17631 351 ENVYPAEVEDVLYE-HPAVAEVAVI 374
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
997-1176 |
1.54e-05 |
|
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: 49.58 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 997 WRAQA--TPDHVlfmllnAKGTTVCTASCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPV 1074
Cdd:cd17646 4 VAEQAarTPDAP------AVVDEGRTLTYRELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1075 TVRPPHaqnltatlPTVR--MIVDVSKAACILTSQTLMRLLRSREAAAAVDVKTWPTIIDTDDLPrkrlpqlykPPTPEM 1152
Cdd:cd17646 77 PLDPGY--------PADRlaYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV---------PPRPDN 139
|
170 180
....*....|....*....|....
gi 55749758 1153 LAYLDFSVSTTGMLTGVKMSHSAV 1176
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHAGI 163
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
988-1520 |
1.60e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.96 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 988 HQFLAEilqwRAQATPDHVLfMLLNAKgttvcTASCLQLHKRAERIASVLGDKGhlnAGDNVV--LLYPPGIELIAAFYG 1065
Cdd:PRK12316 4554 HQLVAE----RARMTPDAVA-VVFDEE-----KLTYAELNRRANRLAHALIARG---VGPEVLvgIAMERSAEMMVGLLA 4620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1066 CLYAGCIPVTVRPPHAQNLTATlptvrMIVDvSKAACILTSQTLMRLLRSREAAAAVDV---KTWPTIIDTDdlprkrlP 1142
Cdd:PRK12316 4621 VLKAGGAYVPLDPEYPRERLAY-----MMED-SGAALLLTQSHLLQRLPIPDGLASLALdrdEDWEGFPAHD-------P 4687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1143 QLykPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRqiaiCLDPYCGLGF--ALWCLCSVYSGHQ 1220
Cdd:PRK12316 4688 AV--RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDD----RVLQFMSFSFdgSHEGLYHPLINGA 4761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1221 SVLIPPMELENNLFLwLSTVNQYKIRDTFCSYSVMELCTKGLGNQVEVLKTRGINLScvrtcvvvAEERPRVALQQSFSK 1300
Cdd:PRK12316 4762 SVVIRDDSLWDPERL-YAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFG--------GEAVAQASYDLAWRA 4832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1301 LFKDiglspravsttfgsrvnvaiCLQGTSGPDPTTVYVDLKSLRhdrvrlveRGAPQSLLLSESGKILPGVKVVIV--- 1377
Cdd:PRK12316 4833 LKPV--------------------YLFNGYGPTETTVTVLLWKAR--------DGDACGAAYMPIGTPLGNRSGYVLdgq 4884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1378 -NPETKGPVGDSHLGEIWVnsphtASGYytiYDSETLQADHFNTRlSFGDAAQTLWaRTGYLgfvrrteltaATGERHDA 1456
Cdd:PRK12316 4885 lNPLPVGVAGELYLGGEGV-----ARGY---LERPALTAERFVPD-PFGAPGGRLY-RTGDL----------ARYRADGV 4944
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55749758 1457 LYVVGALDETLELRGLRYHPIDIETSVsRIHRSIAECavftwtnlLVVVVELCGSEQEALDLVP 1520
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARL-REHPAVREA--------VVIAQEGAVGKQLVGYVVP 4999
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1034-1508 |
2.09e-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: 2.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1034 ASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTATlpTVRMIVDVSKAACILTSQTLMRLL 1113
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKES--VLRYLVADAGGRIVLADAGAADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1114 RsreaAAAVDVKTWPTIIDTDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSR 1193
Cdd:cd05922 84 R----DALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1194 QIAICLDPYCGLGFALwCLCSVYSGHQSVLIPPMELENnlflwlstvnqykirdtfcsySVMELCTkglgnqvevlKTRG 1273
Cdd:cd05922 160 RALTVLPLSYDYGLSV-LNTHLLRGATLVLTNDGVLDD---------------------AFWEDLR----------EHGA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1274 INLSCVRTcvvVAEERPRVAlqqsfsklFKDIGL-SPRAVSTTFGSRVNVAICLQGTSGPDpTTVYV---------DLKS 1343
Cdd:cd05922 208 TGLAGVPS---TYAMLTRLG--------FDPAKLpSLRYLTQAGGRLPQETIARLRELLPG-AQVYVmygqteatrRMTY 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1344 LRHDRVRlvERgaPQSLllsesGKILPGVKVVIVNPEtKGPVGDSHLGEIWVNSPHTASGYytiydsetlqadhfntrls 1423
Cdd:cd05922 276 LPPERIL--EK--PGSI-----GLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGY------------------- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1424 fgdaaqtlWARTGYLGFVRRTELTAATGE--RHDA---LYVVGALDETLELRGLRYHPIDIETSVSRIhRSIAECAVF-- 1496
Cdd:cd05922 327 --------WNDPPYRRKEGRGGGVLHTGDlaRRDEdgfLFIVGRRDRMIKLFGNRISPTEIEAAARSI-GLIIEAAAVgl 397
|
490
....*....|....
gi 55749758 1497 --TWTNLLVVVVEL 1508
Cdd:cd05922 398 pdPLGEKLALFVTA 411
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1025-1495 |
4.95e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 48.07 E-value: 4.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCiPVTV--RPPHAQNLTA----TLPTVRMI---- 1094
Cdd:PRK07768 34 EVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGA-SLTMlhQPTPRTDLAVwaedTLRVIGMIgaka 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1095 VDVSK---AACILTSQTLMRLLRSREAAAAVDVKtwPTIIDTDDLprkrlpqlykpptpemlAYLDFSVSTTGMLTGVKM 1171
Cdd:PRK07768 112 VVVGEpflAAAPVLEEKGIRVLTVADLLAADPID--PVETGEDDL-----------------ALMQLTSGSTGSPKAVQI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1172 SHSAVNALCRAIKLQCELYSSRQIAICLDPYC---GL-GFalwcLCS-VYSGHQSVLIPPMELENNLFLWLSTVNQYKIR 1246
Cdd:PRK07768 173 THGNLYANAEAMFVAAEFDVETDVMVSWLPLFhdmGMvGF----LTVpMYFGAELVKVTPMDFLRDPLLWAELISKYRGT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1247 DT----FcSYSVmelctkgLGNQVEVLKTRG-INLSCVRtCVVVAEERPRVALQQSFSKLFKDIGLSPRAVSTTFG---S 1318
Cdd:PRK07768 249 MTaapnF-AYAL-------LARRLRRQAKPGaFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGmaeA 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1319 RVNVAICLQGTsGPDPTTVYVDLKSLRHdRVRLVERGAPQSLLLSesGKILPGVKVVIVNpETKGPVGDSHLGEIWVNSP 1398
Cdd:PRK07768 320 TLAVSFSPCGA-GLVVDEVDADLLAALR-RAVPATKGNTRRLATL--GPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGE 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1399 HTASGYYTIYDSETLQADHfntrlsfGdaaqtlWARTGYLGFVrrTELtaatGErhdaLYVVGALDETLELRGLRYHPID 1478
Cdd:PRK07768 395 SVTPGYLTMDGFIPAQDAD-------G------WLDTGDLGYL--TEE----GE----VVVCGRVKDVIIMAGRNIYPTD 451
|
490
....*....|....*..
gi 55749758 1479 IETSVSRIHRSIAECAV 1495
Cdd:PRK07768 452 IERAAARVEGVRPGNAV 468
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
363-462 |
5.31e-05 |
|
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: 47.75 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 363 GKPVY-----TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYpnNDPVMFMVAFYGCLLAEVIPVPIEVPLT 437
Cdd:cd05959 19 DKTAFiddagSLTYAELEAEARRVAGALR-ALG------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100
....*....|....*....|....*
gi 55749758 438 rkdagGQQIGFLLGSCGIALALTSE 462
Cdd:cd05959 90 -----PDDYAYYLEDSRARVVVVSG 109
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
993-1257 |
8.21e-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: 46.94 E-value: 8.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 993 EILQWRAQATPDHVlfmllnakgTTVC---TASCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYA 1069
Cdd:cd17655 1 ELFEEQAEKTPDHT---------AVVFedqTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1070 GCIPVTVRPPHAQNltatlpTVRMIVDVSKAACILTSQTLMRLLRSREAAaavdvktwpTIIDTDDLPRKRLPQLYKPPT 1149
Cdd:cd17655 71 GGAYLPIDPDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLI---------DLLDEDTIYHEESENLEPVSK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1150 PEMLAYLDFSVSTTGMLTGVKMSH--------SAVNALCRAIKLQCELYSSrqiaICLDPYCGLGFAlwclcSVYSGHQS 1221
Cdd:cd17655 136 SDDLAYVIYTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFDASVTEIFA-----SLLSGNTL 206
|
250 260 270
....*....|....*....|....*....|....*.
gi 55749758 1222 VLIPPMELENNLFLwLSTVNQYKIRDTFCSYSVMEL 1257
Cdd:cd17655 207 YIVRKETVLDGQAL-TQYIRQNRITIIDLTPAHLKL 241
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1025-1173 |
9.95e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 46.92 E-value: 9.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRP-------------------------- 1078
Cdd:PRK05605 62 ELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPlytahelehpfedhgarvaivwdkva 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1079 PHAQNLTATLPtVRMIVDVS-KAACILTSQTLMRL-----LRSREA--AAAVDVKTWPTIIDTDDLPRKRLPQLYKPpTP 1150
Cdd:PRK05605 141 PTVERLRRTTP-LETIVSVNmIAAMPLLQRLALRLpipalRKARAAltGPAPGTVPWETLVDAAIGGDGSDVSHPRP-TP 218
|
170 180
....*....|....*....|...
gi 55749758 1151 EMLAYLDFSVSTTGMLTGVKMSH 1173
Cdd:PRK05605 219 DDVALILYTSGTTGKPKGAQLTH 241
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
367-430 |
1.06e-04 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 46.68 E-value: 1.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 55749758 367 YTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPV 430
Cdd:COG1021 49 RRLSYAELDRRADRLAAGLL-ALG------LRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1361-1452 |
1.26e-04 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 46.58 E-value: 1.26e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1361 LLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYY-----TiydSETLQADH-FNTrlsfGDAAQtlWAR 1434
Cdd:cd17640 262 VRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYknpeaT---SKVLDSDGwFNT----GDLGW--LTC 332
|
90 100
....*....|....*....|
gi 55749758 1435 TGYLGFVRRTELTA--ATGE 1452
Cdd:cd17640 333 GGELVLTGRAKDTIvlSNGE 352
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1025-1495 |
1.42e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 47.08 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1025 QLHKRAERIASVLGDKGhlnAGDNVV--LLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTATlptvrMIVDvSKAAC 1102
Cdd:PRK12467 3125 ELNRRANRLAHRLIAIG---VGPDVLvgVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY-----MIED-SGVKL 3195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1103 ILTSQTLMRLLrsreAAAAVDvktwpTIIDTDDLPRKRLPQlyKPPT----PEMLAYLDFSVSTTGMLTGVKMSHSAVNA 1178
Cdd:PRK12467 3196 LLTQAHLLEQL----PAPAGD-----TALTLDRLDLNGYSE--NNPStrvmGENLAYVIYTSGSTGKPKGVGVRHGALAN 3264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1179 LCRAIKLQCELySSRQIAICLDPYCGLGFA---LWCLCsvySGHQSVLIPpmeleNNLFLWLSTVNQYKIRDTfcsySVM 1255
Cdd:PRK12467 3265 HLCWIAEAYEL-DANDRVLLFMSFSFDGAQerfLWTLI---CGGCLVVRD-----NDLWDPEELWQAIHAHRI----SIA 3331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1256 ELCTKGLGNQVEVLKTRgiNLSCVRTCVVVAEERPRVALQQSFSKLfkdiglsPRAvsttfgsrvnvaiCLQGTSGPDPT 1335
Cdd:PRK12467 3332 CFPPAYLQQFAEDAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKL-------KPR-------------GLTNGYGPTEA 3389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1336 TVYVDLKSLRHDRVRLVErGAPqslllseSGKILPGVKVVIVNPETkGPVGDSHLGEIWVNSPHTASGYytiYDSETLQA 1415
Cdd:PRK12467 3390 VVTVTLWKCGGDAVCEAP-YAP-------IGRPVAGRSIYVLDGQL-NPVPVGVAGELYIGGVGLARGY---HQRPSLTA 3457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1416 DHFNTRlSFGDAAQTLWaRTGYLGFVRRTELtaatgerhdaLYVVGALDETLELRGLRYHPIDIETSVsRIHRSIAECAV 1495
Cdd:PRK12467 3458 ERFVAD-PFSGSGGRLY-RTGDLARYRADGV----------IEYLGRIDHQVKIRGFRIELGEIEARL-LQHPSVREAVV 3524
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
991-1173 |
1.65e-04 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 46.29 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 991 LAEILQWRAQATPDHVLFMLlnakGTTVCTASclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 1070
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLVF----GGTRWTYA--EAARAAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1071 CIPVTVrpphaqNLTATLPTVRMIVDVSKAACILTSQTLMRLLRSREAAAAVDVKTWptIIDTDdlPRKRLPQLYK--PP 1148
Cdd:PRK06155 96 AIAVPI------NTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVW--LLDAP--ASVSVPAGWStaPL 165
|
170 180 190
....*....|....*....|....*....|....*...
gi 55749758 1149 TP-------------EMLAYLDFSvSTTGMLTGVKMSH 1173
Cdd:PRK06155 166 PPldapapaaavqpgDTAAILYTS-GTTGPSKGVCCPH 202
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
989-1082 |
3.18e-04 |
|
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: 45.01 E-value: 3.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 989 QFLAEILQWRAQATPDHVlfMLLNAKGTTvctaSCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLY 1068
Cdd:cd05920 15 EPLGDLLARSAARHPDRI--AVVDGDRRL----TYRELDRRADRLAAGLRGLG-IRPGDRVVVQLPNVAEFVVLFFALLR 87
|
90
....*....|....
gi 55749758 1069 AGCIPVTVRPPHAQ 1082
Cdd:cd05920 88 LGAVPVLALPSHRR 101
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1366-1495 |
4.20e-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: 44.56 E-value: 4.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1366 GKILPGVKVVIVNPETKGPVGDSHlGEIWVNSPHTASGYytiYDSETLQADHFNTRlsfgdaaqtlWARTGYLGFVRrte 1445
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGY---WNNPERTAEVLIDG----------WVNTGDLGERR--- 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 55749758 1446 ltaatgeRHDALYVVGALDETLELRGLRYHPIDIETSVSRIhRSIAECAV 1495
Cdd:cd17635 236 -------EDGFLFITGRSSESINCGGVKIAPDEVERIAEGV-SGVQECAC 277
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
357-438 |
1.11e-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: 43.39 E-value: 1.11e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 357 TALDMTGKpvyTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVAlVYPNNDPVMFmVAFYGCLLA--EVIPVPIEV 434
Cdd:cd05945 8 PAVVEGGR---TLTYRELKERADALA-AALASLG------LDAGDPVV-VYGHKSPDAI-AAFLAALKAghAYVPLDASS 75
|
....
gi 55749758 435 PLTR 438
Cdd:cd05945 76 PAER 79
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
369-460 |
1.74e-03 |
|
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: 42.85 E-value: 1.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 369 LTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEvPLTRKDaggqQIGF 448
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKG------VRKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90
....*....|..
gi 55749758 449 LLGSCGIALALT 460
Cdd:cd05935 68 ILNDSGAKVAVV 79
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1366-1496 |
2.24e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 42.34 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1366 GKILPGVKVVIVNpetkgpvgdshlGEIWVNSPHTASGYYTIYDsetlqadhfntrlsFGDAAQTLWARTGYLGFVrrte 1445
Cdd:PRK07824 195 GVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVD--------------PDPFAEPGWFRTDDLGAL---- 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 55749758 1446 ltaatgerHD-ALYVVGALDETLELRGLRYHPIDIETSVSRiHRSIAECAVF 1496
Cdd:PRK07824 245 --------DDgVLTVLGRADDAISTGGLTVLPQVVEAALAT-HPAVADCAVF 287
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
368-446 |
2.39e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 42.35 E-value: 2.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 368 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNndPVMFMVAFYGCLLAEVIPV-------PIEVPLTRKD 440
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPN--LLQYPIALFGILRAGMIVVnvnplytPRELEHQLND 119
|
....*.
gi 55749758 441 AGGQQI 446
Cdd:PRK08974 120 SGAKAI 125
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
368-459 |
2.53e-03 |
|
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: 42.21 E-value: 2.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 368 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNDPvmFMVAFYGCLLAEVIPVPIEVPLTRKDaggqqIG 447
Cdd:cd17631 20 SLTYAELDERVNRLAHALRA-LG------VAKGDRVAVLSKNSPE--FLELLFAAARLGAVFVPLNFRLTPPE-----VA 85
|
90
....*....|..
gi 55749758 448 FLLGSCGIALAL 459
Cdd:cd17631 86 YILADSGAKVLF 97
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1362-1495 |
3.01e-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: 3.01e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 1362 LSESGKILPGVKVVIVNPETKgPVGDshlGEIWVNSPHTASGYY--TIYDSETLQADHFNTrlsfGDaaqtlwarTGYL- 1438
Cdd:cd05912 241 IGSAGKPLFPVELKIEDDGQP-PYEV---GEILLKGPNVTKGYLnrPDATEESFENGWFKT----GD--------IGYLd 304
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55749758 1439 --GFV----RRTELTAATGERhdaLYvvgaldetlelrglryhPIDIETSVSRiHRSIAECAV 1495
Cdd:cd05912 305 eeGFLyvldRRSDLIISGGEN---IY-----------------PAEIEEVLLS-HPAIKEAGV 346
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
368-432 |
3.36e-03 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 42.02 E-value: 3.36e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55749758 368 TLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPI 432
Cdd:COG0365 39 TLTYAELRREVNRFA-NALRALG------VKKGDRVAIYLPNI--PEAVIAMLACARIGAVHSPV 94
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
316-460 |
3.94e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 41.57 E-value: 3.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 316 PEGRQMTPVKgePLGVIcnwppALESALQRWGTTQAKcscLTALDMTGkpvYTLTYGKLWSRSLKLAyTLLNKLGtknep 395
Cdd:PRK06178 19 PAGIPREPEY--PHGER-----PLTEYLRAWARERPQ---RPAIIFYG---HVITYAELDELSDRFA-ALLRQRG----- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55749758 396 vLKPGDRVALVYPNNdPvMFMVAFYGCLLAEVIPVPIEvPLTRkdagGQQIGFLLGSCGIALALT 460
Cdd:PRK06178 80 -VGAGDRVAVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFR----EHELSYELNDAGAEVLLA 136
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
364-438 |
5.64e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 41.03 E-value: 5.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55749758 364 KPVY-----TLTYGKLWSRSLKLAYTLLNKLGTKNEPVlkpgdrvaLVYPNNDPVMfMVAFYGCLLA--EVIPVPIEVPL 436
Cdd:PRK04813 18 FPAYdylgeKLTYGQLKEDSDALAAFIDSLKLPDKSPI--------IVFGHMSPEM-LATFLGAVKAghAYIPVDVSSPA 88
|
..
gi 55749758 437 TR 438
Cdd:PRK04813 89 ER 90
|
|
| |
