|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
978-1543 |
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: 736.08 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 978 LFMLLNAKGTTVCTASCLQLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPH-AQNLT 1056
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1057 ATLPTVRMvvDVSKAACVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPRKRLP-----QLYKPPTPEMLAYLDFSV 1131
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1132 STTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMELENNLFLWLATV 1211
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1212 NQYKIRDTFCSYSVMELCTKGLGNQVEVLKTRGINLSCIRTCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGSRV 1291
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1292 NVAICLQGTSGPDPTTVYVDLKSLRHDRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHT 1371
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1372 ASGYYTIYDSETLQADHFN-TRLSFGDaAQTLWARTGYLGFVRRTELTAATGERHDALYVVGALDETLELRGLRYHPIDI 1450
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFPsTRLSTGI-TNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1451 ETSVSRVHRSIAECAVFTWTNLLVVVVEL-CGSEQEALDLVPLVTNVVLEEHYLIVGVVVVVDPGVVPINSRGEKQRMHL 1529
Cdd:cd05905 478 EATVMRVHPYRGRCAVFSITGLVVVVAEQpPGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEI 557
|
570
....*....|....
gi 755551667 1530 RDSFLADQLDPIYV 1543
Cdd:cd05905 558 RQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
281-902 |
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: 662.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 281 CLTGLDVTGKPVYTLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPnnDPVMFMVAFYGCLLAEVIPVPIEV 360
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 361 PLtrkdaGGQQIGFLLGSCGIALALTSEICLKGLPKT-----QNGEIVQFKGWPRLKWVVTDSKYLSKPPKDWQPHISPA 435
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 436 GTEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVM 515
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 516 KTCPLSWVQRVHAHKAKVALVKCRDLHWAMM------AHRDQRDVSLSSLRMLIVTDGaNPWSVSSCDAFLSLFQSHGLK 589
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKdlsstlASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 590 PEAIcpcatSAEAMTVAIRRPGVPGA--PLPGRAILSMNGLSYGVIRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGLP 667
Cdd:cd05905 307 PRAV-----STEFGTRVNPFICWQGTsgPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 668 qLCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVTSSGSPVGDVPFIRSGLLGFVGPGS----------LVFVVGK 737
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTKctdlnveehdLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 738 MDGLLMVSGRRHNADDIVATGLAVESiktvYRGrhtgllavpqtcqarpylrtfplsvpsvrnplppdlrvarvltsfRI 817
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRG---------------------------------------------RC 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 818 AVFSVSvfydERIVVVAEQRPdASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLFLEGSL 897
Cdd:cd05905 492 AVFSIT----GLVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKL 566
|
....*
gi 755551667 898 HPCNI 902
Cdd:cd05905 567 HPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
968-1501 |
7.40e-65 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 230.97 E-value: 7.40e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 968 WRAQATPDHVLFMLLNAKGTTVCTASCLQLHKRAERIASVLgdKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTV 1047
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1048 RPPHAqnlTATLPTVRMVVDVSKAACVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPRKRLPQLyKPPTPEMLAYL 1127
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPP-PSPDPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1128 DFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPY--CGLGFALwcLCSVYSGHQSVLIPPMELENNLF 1205
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLIGGL--LTPLYSGGPSVLMSPAAFLRRPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1206 LWLATVNQYkiRDTFcsySVM-----ELCTKglgnQVEVLKTRGINLSCIRTCVVVAeERPRVSLQQSFSKLFKDIGLSP 1280
Cdd:cd05931 233 RWLRLISRY--RATI---SAApnfayDLCVR----RVRDEDLEGLDLSSWRVALNGA-EPVRPATLRRFAEAFAPFGFRP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1281 RAVSTTFG---SRVNVAIclqGTSGPDPTTVYVDLKSLRHDRVRLVERGAPQSLLLSeSGKILPGVKVVIVNPETKGPVG 1357
Cdd:cd05931 303 EAFRPSYGlaeATLFVSG---GPPGTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDQEVRIVDPETGRELP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1358 DSHLGEIWVNSPHTASGYYTiydSETLQADHFNTRLSFGDAAqtlWARTGYLGFVRRteltaatGErhdaLYVVGALDET 1437
Cdd:cd05931 379 DGEVGEIWVRGPSVASGYWG---RPEATAETFGALAATDEGG---WLRTGDLGFLHD-------GE----LYITGRLKDL 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755551667 1438 LELRGLRYHPIDIETSVSRVHRSIAE--CAVFTW----TNLLVVVVELcGSEQEALDLVPLVTNV---VLEEH 1501
Cdd:cd05931 442 IIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEV-ERGADPADLAAIAAAIraaVAREH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
271-893 |
4.69e-58 |
|
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: 210.94 E-value: 4.69e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 271 RWGSTQAKCPCLTGLDVTGKPVYTLTYGKLWSRSLKLAYTLLnklgtknePVLKPGDRVALVYPNNdpVMFMVAFYGCLL 350
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAPPG--LDFVAAFLGCLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 351 AEVIPVPIEVPLTRKDAggQQIGFLLGSCGIALALTSEICLKGLPKTqngeIVQFKGWPRLKWVVTDSKyLSKPPKDWQP 430
Cdd:cd05931 71 AGAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLL-PDTSAADWPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 431 hISPAGTEPAYIEYkTSkeGSV---MGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMFANVMN---- 503
Cdd:cd05931 144 -PSPDPDDIAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSggps 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 504 -KMHTISVpysVMKtcPLSWVQRVHAHKAKV------ALVKCrdlhwAMMAHRDQRD-VSLSSLRMLIVtdGANPWSVSS 575
Cdd:cd05931 220 vLMSPAAF---LRR--PLRWLRLISRYRATIsaapnfAYDLC-----VRRVRDEDLEgLDLSSWRVALN--GAEPVRPAT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 576 CDAFLSLFQSHGLKPEAICPCATSAEAmTVAI---RRPGVPGAPLPGRAILSmnglsyGVIRVNTEDKNSALTVQDVGHV 652
Cdd:cd05931 288 LRRFAEAFAPFGFRPEAFRPSYGLAEA-TLFVsggPPGTGPVVLRVDRDALA------GRAVAVAADDPAARELVSCGRP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 653 MPGGMMCIVKPDGLpQLCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVTSSGspvgdvPFIRSGLLGFVGPGSLv 732
Cdd:cd05931 361 LPDQEVRIVDPETG-RELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 733 FVVGKMDGLLMVSGRRHNADDIVATglaVESIktvyrgrhtgllavpqtcqarpylrtfplsvpsvrnplPPDLRVARVl 812
Cdd:cd05931 433 YITGRLKDLIIVRGRNHYPQDIEAT---AEEA--------------------------------------HPALRPGCV- 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 813 tsfriAVFSVSVFYDERIVVVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLF 892
Cdd:cd05931 471 -----AAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAY 545
|
.
gi 755551667 893 L 893
Cdd:cd05931 546 L 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
966-1441 |
1.48e-50 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 185.21 E-value: 1.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 966 LQWRAQATPDHVLFMllNAKGTTVctaSCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPV 1045
Cdd:pfam00501 1 LERQAARTPDKTALE--VGEGRRL---TYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1046 TVRPphaqnlTATLPTVRMVVDVSKAACVLTTQTLmRLLKSREAAAAVDVKTWPAIIDTDDLPRKRL-----------PQ 1114
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDDAL-KLEELLEALGKLEVVKLVLVLDRDPVLKEEPlpeeakpadvpPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1115 LYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCE----LYSSRQIAICLDPYCGLGFALWCLCSVYSGH 1190
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1191 QSVLIPPMELeNNLFLWLATVNQYKIRDTFCSYSVMELCtkglgnqVEVLKTRGINLSCIRTCVVVAeERPRVSLQQSFS 1270
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1271 KLFkdiglsPRAVSTTFGSRVNVAICLQGTSGPDPTTvyvdlkslrhdrvrlvergapqslLLSESGKILPGVKVVIVNP 1350
Cdd:pfam00501 299 ELF------GGALVNGYGLTETTGVVTTPLPLDEDLR------------------------SLGSVGRPLPGTEVKIVDD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1351 ETKGPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHFNTrlsfGDaaqtlWARTGYLGfvRRTEltaaTGErhdaLYV 1430
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAFDE----DG-----WYRTGDLG--RRDE----DGY----LEI 406
|
490
....*....|.
gi 755551667 1431 VGALDETLELR 1441
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 ... |
1124-1488 |
5.55e-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: 137.42 E-value: 5.55e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1124 LAYLDFSVSTTGMLTGVKMSHSAVNALCRAIkLQCELYSSRQIAICLDPYC---GLGFALWCLcsvYSGHQSVLIPPMEL 1200
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFhigGLFGLLGAL---LAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1201 EnnlfLWLATVNQYKIRDTFCSYSVMELCtkglgnqVEVLKTRGINLSCIRTCVVVAEERPRvSLQQSFSKLFKDI---- 1276
Cdd:cd04433 78 E----AALELIEREKVTILLGVPTLLARL-------LKAPESAGYDLSSLRALVSGGAPLPP-ELLERFEEAPGIKlvng 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1277 -GLSPRAVSTTFGSRVNVAIclqgtsgpDPTTVyvdlkslrhdrvrlvergapqslllsesGKILPGVKVVIVNPETkGP 1355
Cdd:cd04433 146 yGLTETGGTVATGPPDDDAR--------KPGSV----------------------------GRPVPGVEVRIVDPDG-GE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1356 VGDSHLGEIWVNSPHTASGYYTIYDsetlqadhfNTRLSFGDAaqtlWARTGYLGFVRrteltaatgeRHDALYVVGALD 1435
Cdd:cd04433 189 LPPGEIGELVVRGPSVMKGYWNNPE---------ATAAVDEDG----WYRTGDLGRLD----------EDGYLYIVGRLK 245
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 755551667 1436 ETLELRGLRYHPIDIETSVSRvHRSIAECAVF-----TWTNLLVVVVELCGSEQEALD 1488
Cdd:cd04433 246 DMIKSGGENVYPAEVEAVLLG-HPGVAEAAVVgvpdpEWGERVVAVVVLRPGADLDAE 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
962-1456 |
7.39e-32 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 136.84 E-value: 7.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 962 LAEILQWRAQATPDHVLFMLLNAKGTTVCTASCLQLHKRAERIASVLGDKGHLnaGDNVVLLYPPGIELIAAFYGCLYAG 1041
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1042 CIPVTVRPP------HAQNLTAtlptvrmVVDVSKAACVLTTQTLMRLLKSREAAAAVDVKTWPAI--IDTDDLPRKRLP 1113
Cdd:PRK05691 89 VIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVdtLDPALAEAWQEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1114 QLykppTPEMLAYLDFSVSTTGMLTGVKMSHSAVNAlcraiklqCELYSSRQIAICLDP----------YCGLGFALWCL 1183
Cdd:PRK05691 162 AL----QPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1184 CSVYSGHQSVLIPPmelenNLFL-----WLATVNQYkiRDT----------FCSYSVMELCTKGLgnqvevlktrgiNLS 1248
Cdd:PRK05691 230 QPIFSGVPCVLMSP-----AYFLerplrWLEAISEY--GGTisggpdfayrLCSERVSESALERL------------DLS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1249 CIRTCVVVAEERPRVSLqQSFSKLFKDIGLSPRAVSTTFGSRVNVAICLQGTSGPDPTTVYVDLKSLRHDRvrlVERGAP 1328
Cdd:PRK05691 291 RWRVAYSGSEPIRQDSL-ERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNR---AEPGTG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1329 QSLLlsESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTiyDSETlqadhfnTRLSFGDAAQTLWARTGY 1408
Cdd:PRK05691 367 SVLM--SCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR--NPEA-------SAKTFVEHDGRTWLRTGD 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 755551667 1409 LGFVRRTEltaatgerhdaLYVVGALDETLELRGLRYHPIDIETSVSR 1456
Cdd:PRK05691 436 LGFLRDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVER 472
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
14-130 |
1.92e-31 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 119.06 E-value: 1.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 14 AALPPEVRAQLAELELELSEGDITQKGYEKKRSKLLSPYSPQTQetdsigqkernqtpapTAAQTSAPSKYHR-SRSGGA 92
Cdd:pfam06464 3 PSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLHPE----------------TPTKLSAEAQNQLaSLETKL 66
|
90 100 110
....*....|....*....|....*....|....*...
gi 755551667 93 RDERYRSDIHTEAVQAALAKHKEQKMALPMPTKRRSTF 130
Cdd:pfam06464 67 RDEELSEEVYLEKVKALLAKELERENGLNAPTKEQSGL 104
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
966-1497 |
6.42e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 117.74 E-value: 6.42e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 966 LQWRAQATPDHVLFMLLNAKGTTVCTASCL---QLHKRAERIASVLgdKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGC 1042
Cdd:PRK05850 7 LRERASLQPDDAAFTFIDYEQDPAGVAETLtwsQLYRRTLNVAEEL--RRHGSTGDRAVILAPQGLEYIVAFLGALQAGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1043 IPVTVRPPHAqnlTATLPTVRMVVDVSKAACVLTTqtlmrllksreAAAAVDVKTW---------PAII--DTDDLPRKR 1111
Cdd:PRK05850 85 IAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTT-----------SAVVDDVTEYvapqpgqsaPPVIevDLLDLDSPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1112 LPQLYKPPTPEMlAYLDFSVSTTGMLTGVKMSHSAVNALCRaiKLQCELYSSRQIAICLD-------P-YCGLGFALWCL 1183
Cdd:PRK05850 151 GSDARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMGLVLGVC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1184 CSVYSGHQSVLIPPMElennlFL-----W---LATVNQykirdtfcSYSV-----MELCTKglgnqvevlKTR-----GI 1245
Cdd:PRK05850 228 APILGGCPAVLTSPVA-----FLqrparWmqlLASNPH--------AFSAapnfaFELAVR---------KTSdddmaGL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1246 NLSCIRTcVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFG---SRVNVAIclqGTSGPDPTTVYVDLKSLRHDRVR- 1321
Cdd:PRK05850 286 DLGGVLG-IISGSERVHPATLKRFADRFAPFNLRETAIRPSYGlaeATVYVAT---REPGQPPESVRFDYEKLSAGHAKr 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1322 --------LVERGAPQSLLlsesgkilpgvkVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTiYDSETLQAdhFNTRL 1393
Cdd:PRK05850 362 cetgggtpLVSYGSPRSPT------------VRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQ-KPEETERT--FGATL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1394 ---SFGDAAQTlWARTGYLGFVrrteltaATGErhdaLYVVGALDETLELRGLRYHPIDIETSVSRVHRsiAECAVFT-- 1468
Cdd:PRK05850 427 vdpSPGTPEGP-WLRTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATIQEITG--GRVAAISvp 492
|
570 580 590
....*....|....*....|....*....|....
gi 755551667 1469 --WTNLLVVVVEL---CGSEQEALDLVPLVTNVV 1497
Cdd:PRK05850 493 ddGTEKLVAIIELkkrGDSDEEAMDRLRTVKREV 526
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
285-897 |
1.03e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 117.52 E-value: 1.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 285 LDVTGK----PVYTLT-YGKLWSRSL--KLAYTLLN---------------KLGTKN-------EPVLKPGDRVALVYPN 335
Cdd:PRK07769 9 FDVNGKirfpPNTNLVrHVERWAKVRgdKLAYRFLDfsterdgvardltwsQFGARNravgarlQQVTKPGDRVAILAPQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 336 NdpVMFMVAFYGCLLAEVIPVPIEVPltrkDAGGQ--QIGFLLGSCGIALALTSEIC-------LKGLPKTQNgeivqfk 406
Cdd:PRK07769 89 N--LDYLIAFFGALYAGRIAVPLFDP----AEPGHvgRLHAVLDDCTPSAILTTTDSaegvrkfFRARPAKER------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 407 gwPRLKWV--VTDSKYLSkppkdWQPhISPAGTEPAYIEYkTSkeGSV---MGVTVSRLAMLSQCQALSQACNYSEGETV 481
Cdd:PRK07769 156 --PRVIAVdaVPDEVGAT-----WVP-PEANEDTIAYLQY-TS--GSTripAGVQITHLNLPTNVLQVIDALEGQEGDRG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 482 VNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVMKTcPLSWVQRVHA------------------HKAKVALVKcrdlhw 543
Cdd:PRK07769 225 VSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRR-PGRWIRELARkpggtggtfsaapnfafeHAAARGLPK------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 544 ammahRDQRDVSLSSLRMLIvtDGANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAmTVAIRRPGVPGAPlpgRAI- 622
Cdd:PRK07769 298 -----DGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEA-TLFVSTTPMDEEP---TVIy 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 623 LSMNGLSYG-VIRVNTEDKNsALTVQDVGHVMPGGMMCIVKPDGLPQLcRTDEIGEICVSSRTGGMMYFGLAGVTKNTFE 701
Cdd:PRK07769 367 VDRDELNAGrFVEVPADAPN-AVAQVSAGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFQ 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 702 VI------PVTSSGSPvGDVPFIRSGLLGFVGPGSLvFVVGKMDGLLMVSGRRHNADDIVATglAVESIKTVYRGrhtgl 775
Cdd:PRK07769 445 NIlksrlsESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYT--AQEATKALRTG----- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 776 lavpqtcqarpYLRTFplSVPSvrNPLPPdlrvarvltsfriAVFSVS---VFYD-----ERIVVVAEQRPDASEEDSFQ 847
Cdd:PRK07769 516 -----------YVAAF--SVPA--NQLPQ-------------VVFDDShagLKFDpedtsEQLVIVAERAPGAHKLDPQP 567
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 755551667 848 WMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLFLEGSL 897
Cdd:PRK07769 568 IADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
962-1479 |
1.04e-25 |
|
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: 112.60 E-value: 1.04e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 962 LAEILQWRAQATPDHVLfmlLNAKGTTVctaSCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 1041
Cdd:COG0318 1 LADLLRRAAARHPDRPA---LVFGGRRL---TYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1042 CIPVTVrpphaqNLTATLPTVRMVVDVSKAACVLTtqtlmrllksreaaaavdvktwpaiidtddlprkrlpqlykpptp 1121
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1122 emlAYLDFSvS-TTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMEL 1200
Cdd:COG0318 103 ---ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1201 ENnlflWLATVNQYKIrdTFCSYS---VMELCtkglgnqvEVLKTRGINLSCIRTCVVVAeERPRVSLQQSFSKLFKdig 1277
Cdd:COG0318 179 ER----VLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLRLVVSGG-APLPPELLERFEERFG--- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1278 lspRAVSTTFGSrvnvaiclqgT-SGPdptTVYVDLKSLRHDRVRLVergapqslllsesGKILPGVKVVIVNPETKgPV 1356
Cdd:COG0318 241 ---VRIVEGYGL----------TeTSP---VVTVNPEDPGERRPGSV-------------GRPLPGVEVRIVDEDGR-EL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1357 GDSHLGEIWVNSPHTASGYYTiyDSETlqadhfnTRLSFGDAaqtlWARTGYLGFVRrteltaATGErhdaLYVVGALDE 1436
Cdd:COG0318 291 PPGEVGEIVVRGPNVMKGYWN--DPEA-------TAEAFRDG----WLRTGDLGRLD------EDGY----LYIVGRKKD 347
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 755551667 1437 TLELRGLRYHPIDIETSVSRvHRSIAECAVF-----TWTNLLVVVVEL 1479
Cdd:COG0318 348 MIISGGENVYPAEVEEVLAA-HPGVAEAAVVgvpdeKWGERVVAFVVL 394
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
295-899 |
1.37e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 110.48 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 295 LTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVyPNNDPvMFMVAFYGCLLAEVIPVPIEVP--LTRKDAGGQQI 372
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLA-LG------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFGGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 373 GFLLGSCGIALALTSEICLKGLPKTQNGEivqfkgwpRLKWVVTDSKYLSKPPKDWQ-PHISPagTEPAYIEYkTSkeGS 451
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGN--------PLLHVLSHAWFKALPEADVAlPRPTP--DDIAYLQY-SS--GS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 452 V---MGVTVSRLAMLSQCQALSQ-ACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMhtiSVPYsvMKTC-----PLSW 522
Cdd:PRK09192 188 TrfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQL---SVDY--LPTRdfarrPLQW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 523 VQRVHAHKAKVALVKC--RDLHWAMMAHRDQRDVSLSSLRmlIVTDGANPWSVSSCDAFLSLFQSHGLKPEAICPCATSA 600
Cdd:PRK09192 263 LDLISRNRGTISYSPPfgYELCARRVNSKDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 601 EAmTVAIrrpgvpgaplpgrailSMNGLSYGvIRVNT------EDKNSALTVQD----------VGHVMPGGMMCIVKPD 664
Cdd:PRK09192 341 EA-TLAV----------------SFSPLGSG-IVVEEvdrdrlEYQGKAVAPGAetrrvrtfvnCGKALPGHEIEIRNEA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 665 G--LPQLcrtdEIGEICVssRTGGMM--YFGlagvTKNTFEVIPVTSsgspvgdvpFIRSGLLGFVGPGSLVfVVGKMDG 740
Cdd:PRK09192 403 GmpLPER----VVGHICV--RGPSLMsgYFR----DEESQDVLAADG---------WLDTGDLGYLLDGYLY-ITGRAKD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 741 LLMVSGRRHNADDIvatGLAVESIktvyrgrhtgllavpqtcqarpylrtfplsvPSVRnplppdlrvarvltSFRIAVF 820
Cdd:PRK09192 463 LIIINGRNIWPQDI---EWIAEQE-------------------------------PELR--------------SGDAAAF 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 821 SVSVFYDERIVVVAEQRPdASEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKTPLGGIHISQTKQLFLEGSLHP 899
Cdd:PRK09192 495 SIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRTSSGKLSRAKAKKRYLSGAFAS 571
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
294-754 |
2.60e-24 |
|
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: 108.36 E-value: 2.60e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 294 TLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNDPvmFMVAFYGCLLAEVIPVPIEVPLTRKdaggqQIG 373
Cdd:COG0318 24 RLTYAELDARARRLA-AALRALG------VGPGDRVALLLPNSPE--FVVAFLAALRAGAVVVPLNPRLTAE-----ELA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 374 FLLGSCGIALALTSEICL----KGLPKtqngeivqfkgwprlkwvvtdskylskppkdwqphispagtepayieyktske 449
Cdd:COG0318 90 YILEDSGARALVTALILYtsgtTGRPK----------------------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 450 gsvmGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMHTISVPysvmKTCPLSWVQRVHAH 529
Cdd:COG0318 117 ----GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP----RFDPERVLELIERE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 530 KA-KVALVKcrDLHWAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLSLFQShglkpeAICPCATSAEAMTVAIR 608
Cdd:COG0318 189 RVtVLFGVP--TMLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFEERFGV------RIVEGYGLTETSPVVTV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 609 RPGVPGAPLPGRailsmnglsygvirvntedknsaltvqdVGHVMPGGMMCIVKPDGLPqlCRTDEIGEICVssRTGGMM 688
Cdd:COG0318 259 NPEDPGERRPGS----------------------------VGRPLPGVEVRIVDEDGRE--LPPGEVGEIVV--RGPNVM 306
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755551667 689 --YFGLAGVTKNTFEvipvtssgspvgDvPFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDI 754
Cdd:COG0318 307 kgYWNDPEATAEAFR------------D-GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEV 361
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
262-895 |
3.09e-24 |
|
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: 108.91 E-value: 3.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 262 PPALESALQRWgSTQAKCPCLTGLDVTGkPVYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNDPvmF 341
Cdd:cd05906 9 PRTLLELLLRA-AERGPTKGITYIDADG-SEEFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDDNED--F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 342 MVAFYGCLLAEVIPVPIEVPLTRKDAGGQ-----QIGFLLGSCGIalaLTSEICLKGLPKtqngeivQFKGWPRLKWVVT 416
Cdd:cd05906 78 IPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELVAEFAG-------LETLSGLPGIRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 417 DSKYLSKPPKDWQPHISPAGTePAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHG 496
Cdd:cd05906 148 SIEELLDTAADHDLPQSRPDD-LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 497 MFANVMNKMHTISVPYSVMKTCPLSWVQRVHAHKAKV------ALVKCRDLhwamMAHRDQRDVSLSSLRMLIVtdGANP 570
Cdd:cd05906 227 HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLNDL----LEEIEDGTWDLSSLRYLVN--AGEA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 571 WSVSSCDAFLSLFQSHGLKPEAICPCATSAEamTVAirrpgvpgaplpgrailsmnglsyGVI---RVNTEDKNSALTVQ 647
Cdd:cd05906 301 VVAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysrSFPTYDHSQALEFV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 648 DVGHVMPGGMMCIVKPDGlpQLCRTDEIGEICVS--SRTGGmmYFGLAGVTKNTFevipvTSSGspvgdvpFIRSGLLGF 725
Cdd:cd05906 355 SLGRPIPGVSMRIVDDEG--QLLPEGEVGRLQVRgpVVTKG--YYNNPEANAEAF-----TEDG-------WFRTGDLGF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 726 VGPGSLVFvVGKMDGLLMVSGRRHNADDIVAtglAVESIKTVyrgrhtgllAVPQTCQArpylrtfplsvpSVRNPLPPD 805
Cdd:cd05906 419 LDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGV---------EPSFTAAF------------AVRDPGAET 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 806 LRVArvltsfriavfsvsVFYderivvvaeqrpdASEEDSFQWMSRVLQAIDSI--HQVGVYCLALVP--ANTLPKTPLG 881
Cdd:cd05906 474 EELA--------------IFF-------------VPEYDLQDALSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLG 526
|
650
....*....|....
gi 755551667 882 GIHISQTKQLFLEG 895
Cdd:cd05906 527 KIQRSKLKAAFEAG 540
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
294-883 |
2.13e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 106.95 E-value: 2.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 294 TLTYGKLWSRSLKLAYTLlNKLGTknepvlkPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLTRkdAGGQQIG 373
Cdd:PRK05850 35 TLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQG--LEYIVAFLGALQAGLIAVPLSVPQGG--AHDERVS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 374 FLLGSCGIALALT-SEIClkglpktqnGEIVQF----KGWPRLKWVVTDSKYLSKPPKdwqPHISPAG-TEPAYIEYkTS 447
Cdd:PRK05850 103 AVLRDTSPSVVLTtSAVV---------DDVTEYvapqPGQSAPPVIEVDLLDLDSPRG---SDARPRDlPSTAYLQY-TS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 448 keGSV---MGVTVSRLAMLSQC-QALSQACNYSEGE-----TVVNVLDFKKDAGLWHGMFANVMNKMHTI-SVPYSVMKT 517
Cdd:PRK05850 170 --GSTrtpAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSWLPFYHDMGLVLGVCAPILGGCPAVlTSPVAFLQR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 518 cPLSWVQRV----HAHKA------KVALVKCRDlhwAMMAHRDQRDVslsslrmLIVTDGANPWSVSSCDAFLSLFQSHG 587
Cdd:PRK05850 248 -PARWMQLLasnpHAFSAapnfafELAVRKTSD---DDMAGLDLGGV-------LGIISGSERVHPATLKRFADRFAPFN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 588 LKPEAICPCATSAEAMT-VAIRRPGVPgaplPGRAILSMNGLSYGVIRVNTEDKNSALtvqdVGHVMP-GGMMCIVKPDG 665
Cdd:PRK05850 317 LRETAIRPSYGLAEATVyVATREPGQP----PESVRFDYEKLSAGHAKRCETGGGTPL----VSYGSPrSPTVRIVDPDT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 666 LPQlCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVT-SSGSPVGdvPFIRSGLLGFVGPGSLvFVVGKMDGLLMV 744
Cdd:PRK05850 389 CIE-CPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATLVDpSPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 745 SGRRHNADDIVATglavesIKTVYRGrhtgllavpqtcqarpylrtfplsvpsvrnplppdlrvarvltsfRIAVFSVSV 824
Cdd:PRK05850 465 DGRNHYPDDIEAT------IQEITGG---------------------------------------------RVAAISVPD 493
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551667 825 FYDERIVVVAE-QRPDASEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGI 883
Cdd:PRK05850 494 DGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
293-755 |
3.03e-23 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 104.32 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 293 YTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVpltrkDAGGQQI 372
Cdd:pfam00501 20 RRLTYRELDERANRLAAGLR-ALG------VGKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPLNP-----RLPAEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 373 GFLLGSCGIALALTSEI--------CLKGLPKTQNGEIVQFKGWPRLKWVVTDSKYLSKPPKdwqPHISPAGTEPAYIEY 444
Cdd:pfam00501 86 AYILEDSGAKVLITDDAlkleelleALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPP---PPPPPDPDDLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 445 kTS------KegsvmGVTVSRLAMLSQCQALSQAC----NYSEGETVVNVLDFKKDAGLWHGMFANVMNKMhTISVPYSV 514
Cdd:pfam00501 163 -TSgttgkpK-----GVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA-TVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 515 MKTCPLSWVQRVHAHKAKV-----ALVKcrdlhwAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLSLFqshglk 589
Cdd:pfam00501 236 PALDPAALLELIERYKVTVlygvpTLLN------MLLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 590 peaicpcatsaeamtvairrpgvpgaplpGRAILSMNGLS--YGVIRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGLp 667
Cdd:pfam00501 302 -----------------------------GGALVNGYGLTetTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETG- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 668 QLCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFevipvTSSGspvgdvpFIRSGLLGFVGPgslvfvvgkmDGLLMVSGR 747
Cdd:pfam00501 352 EPVPPGEPGELCVRGPGVMKGYLNDPELTAEAF-----DEDG-------WYRTGDLGRRDE----------DGYLEIVGR 409
|
....*...
gi 755551667 748 rhnADDIV 755
Cdd:pfam00501 410 ---KKDQI 414
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
996-1476 |
5.42e-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: 101.98 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTAtlPTVRMVVDVSK---AA 1072
Cdd:cd05906 44 DLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPN--ARLRKLRHIWQllgSP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1073 CVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPrkRLPQLYkPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCR 1152
Cdd:cd05906 121 VVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTA--ADHDLP-QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1153 AiKLQCELYSSRQIA---ICLDPYCGLGFAlwCLCSVYSGHQSVLIPPMELENNLFLWLATVNQYKIRDTFCSYSvmeLC 1229
Cdd:cd05906 198 G-KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1230 TKgLGNQVEVLKTRGINLSCIRtCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGSRVNVAIClqgtsgpdptTVY 1309
Cdd:cd05906 272 AL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCSGV----------IYS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1310 VDLKSLRHD-RVRLVERGAPqslllsesgkiLPGVKVVIVNPETKGpVGDSHLGEIWVNSPHTASGYytiYDSETLQADH 1388
Cdd:cd05906 340 RSFPTYDHSqALEFVSLGRP-----------IPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGY---YNNPEANAEA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1389 FntrLSFGdaaqtlWARTGYLGFVRRTELTaATGERHDALYVvgaldetlelRGLRYHPIDIETSVSRV----HRSIAEC 1464
Cdd:cd05906 405 F---TEDG------WFRTGDLGFLDNGNLT-ITGRTKDTIIV----------NGVNYYSHEIEAAVEEVpgvePSFTAAF 464
|
490
....*....|....*
gi 755551667 1465 AVF---TWTNLLVVV 1476
Cdd:cd05906 465 AVRdpgAETEELAIF 479
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1017-1455 |
2.14e-21 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 100.59 E-value: 2.14e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1017 GDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPP----HAQNLTATL----PTVrmvvdvskaacVLTTQTLMRLLksRE 1088
Cdd:PRK12476 92 GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV-----------VLTTTAAAEAV--EG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1089 AAAAVDVKTWPAIIDTDDLPrKRLPQLYKPPTPEM--LAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSsRQI 1166
Cdd:PRK12476 159 FLRNLPRLRRPRVIAIDAIP-DSAGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLD-RNT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1167 AIC--LDPYCGLGFALWCLCSVYSGHqSVLIPPMELENNLFLWL-ATVNQYKIRDTFCSYS--VMELCT-KGLGNQVEvl 1240
Cdd:PRK12476 237 HGVswLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWIkALSEGSRTGRVVTAAPnfAYEWAAqRGLPAEGD-- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1241 ktrGINLSciRTCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGsrVNVAICLQGTSGPD--PTTVYVDLKSLRHD 1318
Cdd:PRK12476 314 ---DIDLS--NVVLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG--IAEATLFVATIAPDaePSVVYLDREQLGAG 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1319 RVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTI-YDSETLQADHFNTRLSFGD 1397
Cdd:PRK12476 387 RAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRpEETERTFGAKLQSRLAEGS 466
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755551667 1398 -----AAQTLWARTGYLGFVRRTEltaatgerhdaLYVVGALDETLELRGLRYHPIDIETSVS 1455
Cdd:PRK12476 467 hadgaADDGTWLRTGDLGVYLDGE-----------LYITGRIADLIVIDGRNHYPQDIEATVA 518
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1017-1455 |
6.39e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 99.42 E-value: 6.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1017 GDNVVLLYPPGIELIAAFYGCLYAGCIPVTV----RPPHAQNLTAtlptvrmVVDVSKAACVLTT----QTLMRLLKSRE 1088
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHA-------VLDDCTPSAILTTtdsaEGVRKFFRARP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1089 AaaavdvKTWPAIIDTDDLPRKrLPQLYKPPTP--EMLAYLDFSVSTTGMLTGVKMSHSAV--NAL--CRAIKLQcelYS 1162
Cdd:PRK07769 152 A------KERPRVIAVDAVPDE-VGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLptNVLqvIDALEGQ---EG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1163 SRQIAiCLDPYCGLGFaLWCLCSVYSGHQSVLIPPMELENNLFLW---LATVNQykirDTFCSYSV-----MELCT-KGL 1233
Cdd:PRK07769 222 DRGVS-WLPFFHDMGL-ITVLLPALLGHYITFMSPAAFVRRPGRWireLARKPG----GTGGTFSAapnfaFEHAAaRGL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1234 GNQVEvlktRGINLSCIRtCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGsrVNVAICLQGTSGPD--PTTVYVD 1311
Cdd:PRK07769 296 PKDGE----PPLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYG--MAEATLFVSTTPMDeePTVIYVD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1312 LKSLRHDRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTIYDsETLQADH--F 1389
Cdd:PRK07769 369 RDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPE-ETAATFQniL 447
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1390 NTRLS----FGDAAQTLWARTGYLGfvrrtelTAATGErhdaLYVVGALDETLELRGLRYHPIDIETSVS 1455
Cdd:PRK07769 448 KSRLSeshaEGAPDDALWVRTGDYG-------VYFDGE----LYITGRVKDLVIIDGRNHYPQDLEYTAQ 506
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
996-1467 |
4.60e-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: 95.36 E-value: 4.60e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnlTATLPTVRMVVDVSKAACVL 1075
Cdd:cd05911 15 QLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANP------IYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1076 TT-QTLMRLLKSREAAAAVD--------VKTWPAIIDTDDLPRKRLPQLYKPP---TPEMLAYLDFSVSTTGMLTGVKMS 1143
Cdd:cd05911 88 TDpDGLEKVKEAAKELGPKDkiivlddkPDGVLSIEDLLSPTLGEEDEDLPPPlkdGKDDTAAILYSSGTTGLPKGVCLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1144 HS---AVNALCRAIKLQCELYSSRQIA-ICLDPYCGLgfaLWCLCSVYSGHQSVLIPPMELEnnlfLWLATVNQYKIRDT 1219
Cdd:cd05911 168 HRnliANLSQVQTFLYGNDGSNDVILGfLPLYHIYGL---FTTLASLLNGATVIIMPKFDSE----LFLDLIEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1220 FCSYSVMELctkgLGNQVEVLKtrgINLSCIRTCVVVAEerprvSLQQSFSKLFKdiglspravsttfgSRVNVAICLQG 1299
Cdd:cd05911 241 YLVPPIAAA----LAKSPLLDK---YDLSSLRVILSGGA-----PLSKELQELLA--------------KRFPNATIKQG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1300 -----TSGPDPTTVYVDLKSlrhdrvrlverGApqslllseSGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASG 1374
Cdd:cd05911 295 ygmteTGGILTVNPDGDDKP-----------GS--------VGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1375 YYtiydsetlqadhfntrlsfGDAAQTL-------WARTGYLGFVRRTELtaatgerhdaLYVVGALDETLELRGLRYHP 1447
Cdd:cd05911 356 YY-------------------NNPEATKetfdedgWLHTGDIGYFDEDGY----------LYIVDRKKELIKYKGFQVAP 406
|
490 500
....*....|....*....|
gi 755551667 1448 IDIEtSVSRVHRSIAECAVF 1467
Cdd:cd05911 407 AELE-AVLLEHPGVADAAVI 425
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
996-1466 |
2.58e-19 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 92.33 E-value: 2.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltaTLPT--VRMVVDVSKAAC 1073
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDP--------AYPAerLAFILEDAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1074 VLTTQTLmRLLKSREAAAAVDVKTWPAIIDTDDLPrkrLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 1153
Cdd:TIGR01733 76 LLTDSAL-ASRLAGLVLPVILLDPLELAALDDAPA---PPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1154 IKlQCELYSSRQIAICLDPYCGLGFA---LWCLcsvYSGHQSVLIPPMELENNLFLWLATVNQYKIRDTFCSYSVMELCt 1230
Cdd:TIGR01733 152 LA-RRYGLDPDDRVLQFASLSFDASVeeiFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1231 kglgnqvevLKTRGINLSCIRTCVVVAEErprvslqqsfsklfkdigLSPRAVSTTFGSRVNVAIClqGTSGPDPTTVYV 1310
Cdd:TIGR01733 227 ---------AAALPPALASLRLVILGGEA------------------LTPALVDRWRARGPGARLI--NLYGPTETTVWS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1311 DlkslrhdrVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHFN 1390
Cdd:TIGR01733 278 T--------ATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---LNRPELTAERFV 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755551667 1391 TRLsFGDAAQTLWARTGYLgfVRRteltaatgeRHD-ALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECAV 1466
Cdd:TIGR01733 346 PDP-FAGGDGARLYRTGDL--VRY---------LPDgNLEFLGRIDDQVKIRGYRIELGEIEAALLR-HPGVREAVV 409
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
996-1469 |
1.82e-16 |
|
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: 84.34 E-value: 1.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVrpphaqNLTATLPTVRMVVDVSKAACVL 1075
Cdd:cd05959 34 ELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV------NTLLTPDDYAYYLEDSRARVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1076 TTQTLMRLLKSREAAAAVDVKT---------WPAIIDTDDLPRKRLPQLYKPPT-PEMLAYLDFSVSTTGMLTGVKMSHS 1145
Cdd:cd05959 107 VSGELAPVLAAALTKSEHTLVVlivsggagpEAGALLLAELVAAEAEQLKPAAThADDPAFWLYSSGSTGRPKGVVHLHA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1146 AvnalcraIKLQCELYSSRQIAICLDPYC----------GLGFALWCLCSVysGHQSVLIPPMELENNLFlwlATVNQYK 1215
Cdd:cd05959 187 D-------IYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMPERPTPAAVF---KRIRRYR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1216 iRDTFcsYSVMELCTKGLGNqvEVLKTRgiNLSCIRTCVVVAEERPRvSLQQSFSKLFK-DIglspravsttfgsrvnva 1294
Cdd:cd05959 255 -PTVF--FGVPTLYAAMLAA--PNLPSR--DLSSLRLCVSAGEALPA-EVGERWKARFGlDI------------------ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1295 icLQGTSGPDPTTVYVdlkSLRHDRVRLverGApqslllseSGKILPGVKVVIVNpETKGPVGDSHLGEIWVNSPHTASG 1374
Cdd:cd05959 309 --LDGIGSTEMLHIFL---SNRPGRVRY---GT--------TGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATM 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1375 YYTIYDSetlqadhfnTRLSFgdaaQTLWARTGYlGFVRRTELTaatgerhdaLYVVGALDETLELRGLRYHPIDIEtSV 1454
Cdd:cd05959 372 YWNNRDK---------TRDTF----QGEWTRTGD-KYVRDDDGF---------YTYAGRADDMLKVSGIWVSPFEVE-SA 427
|
490
....*....|....*
gi 755551667 1455 SRVHRSIAECAVFTW 1469
Cdd:cd05959 428 LVQHPAVLEAAVVGV 442
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
996-1501 |
2.15e-16 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 84.67 E-value: 2.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHA-QNLTATLPTVRMVVDVSKAACV 1074
Cdd:PRK09192 54 TLRARAEAGARRLLALG-LKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfGGRESYIAQLRGMLASAQPAAI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1075 LTTQTLMRLLKS-REAAAAVDVKTWpAIIDTDDLPRKRLPqlykPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 1153
Cdd:PRK09192 133 ITPDELLPWVNEaTHGNPLLHVLSH-AWFKALPEADVALP----RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1154 IKLQ-CELYSSRQIAICLDPYCGLGFaLWCLCSVYSGHQSV-LIPPMELENNLFLWLATVNqyKIRDTFcSYSV---MEL 1228
Cdd:PRK09192 208 ISHDgLKVRPGDRCVSWLPFYHDMGL-VGFLLTPVATQLSVdYLPTRDFARRPLQWLDLIS--RNRGTI-SYSPpfgYEL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1229 CTKGLGNQVEVlktrGINLSCIRTCVVVAEE-RPRVslQQSFSKLFKDIGLSPRAVSTTFG-SRVNVAIclqgtSGPDPT 1306
Cdd:PRK09192 284 CARRVNSKDLA----ELDLSCWRVAGIGADMiRPDV--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAV-----SFSPLG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1307 TvyvDLKSLRHDRVRLVERGA-----PQSLLLSE---SGKILPGVKVVIVNpETKGPVGDSHLGEIWVNSPHTASGYYTi 1378
Cdd:PRK09192 353 S---GIVVEEVDRDRLEYQGKavapgAETRRVRTfvnCGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFR- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1379 yDSETLQAdhfntrlsfgdAAQTLWARTGYLGFVrrteltaATGErhdaLYVVGALDETLELRGLRYHPIDIETSVSRV- 1457
Cdd:PRK09192 428 -DEESQDV-----------LAADGWLDTGDLGYL-------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIAEQEp 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 755551667 1458 ---HRSIAECAVFTWTNLLVVVVELC--GSEQEALDLVPLVTNVVLEEH 1501
Cdd:PRK09192 485 elrSGDAAAFSIAQENGEKIVLLVQCriSDEERRGQLIHALAALVRSEF 533
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
285-899 |
9.41e-16 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 82.48 E-value: 9.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 285 LDVTGKP---VYTLTYGKLWSRslklaytlLNKLGTKNEPVLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPI--- 358
Cdd:PRK12476 56 LDHSHSAagcAVELTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLfap 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 359 EVP--LTRKDAggqqigfLLGSCGIALALTSeiclkglpkTQNGEIVQfkgwprlkwvvtdsKYLSKPPKDWQPHI---- 432
Cdd:PRK12476 126 ELPghAERLDT-------ALRDAEPTVVLTT---------TAAAEAVE--------------GFLRNLPRLRRPRViaid 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 433 -----SPAGTEP--------AYIEYKTSKEGSVMGVTVS-RLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMF 498
Cdd:PRK12476 176 aipdsAGESFVPveldtddvSHLQYTSGSTRPPVGVEIThRAVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 499 ANVMNKMHTISVPYSVMKTcPLSWVQRVHAHKAKVALVKCR-DLHWAMMAHR----DQRDVSLSSLRMLIvtdGANPWSV 573
Cdd:PRK12476 256 PAVYGGHSTLMSPTAFVRR-PQRWIKALSEGSRTGRVVTAApNFAYEWAAQRglpaEGDDIDLSNVVLII---GSEPVSI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 574 SSCDAFLSLFQSHGLKPEAICPCATSAEA-MTVAIRRPgvpgAPLPGRAILSMNGLSYG-VIRVNTEDKNSALTVQdVGH 651
Cdd:PRK12476 332 DAVTTFNKAFAPYGLPRTAFKPSYGIAEAtLFVATIAP----DAEPSVVYLDREQLGAGrAVRVAADAPNAVAHVS-CGQ 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 652 VMPGGMMCIVKPDGLPQLcRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEV-----IPVTS--SGSPVGDVpFIRSGLLG 724
Cdd:PRK12476 407 VARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGShaDGAADDGT-WLRTGDLG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 725 FVGPGSLvFVVGKMDGLLMVSGRRHNADDIVATglAVESIKTVYRGRhtgllavpqtcqarpylrtfplsvpsvrnplpp 804
Cdd:PRK12476 485 VYLDGEL-YITGRIADLIVIDGRNHYPQDIEAT--VAEASPMVRRGY--------------------------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 805 dlrvarvltsfrIAVFSVSVFYDERIVVVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIH 884
Cdd:PRK12476 529 ------------VTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLA 596
|
650
....*....|....*
gi 755551667 885 ISQTKQLFLEGSLHP 899
Cdd:PRK12476 597 RRACRAQYLDGRLGV 611
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
312-764 |
1.74e-15 |
|
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: 81.38 E-value: 1.74e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 312 LNKLGTKNEPVLKPGDRVALVYPNNDPvmFMVAFYGCLLAEVIPVPIEVpltrkdagGQQIGFLLGScgialaltseicl 391
Cdd:cd05908 26 LGYLGALQELGIKPGQEVVFQITHNNK--FLYLFWACLLGGMIAVPVSI--------GSNEEHKLKL------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 392 kglpktqngeivqFKGWPRLK--WVVTDSKYLSKPPKdwqphispagtEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQAL 469
Cdd:cd05908 83 -------------NKVWNTLKnpYLITEEEVLCELAD-----------ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 470 SQACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVMKTCPLSWVQRVHAHKAKValVKCRDLHWAMMAHR 549
Cdd:cd05908 139 LNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATI--VSSPNFGYKYFLKT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 550 ----DQRDVSLSSLRMLIvtDGANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAmTVAIRRP--GVPGAPLpgraIL 623
Cdd:cd05908 217 lkpeKANDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA-SVGASLPkaQSPFKTI----TL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 624 SMNGLSYGVIRVNTEDKNS-ALTVQDVGHVMPGGMMCIVKPD--GLPQlcrtDEIGEICVSSRTGGMMYFGLAGVTKNTF 700
Cdd:cd05908 290 GRRHVTHGEPEPEVDKKDSeCLTFVEVGKPIDETDIRICDEDnkILPD----GYIGHIQIRGKNVTPGYYNNPEATAKVF 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551667 701 evipvTSSGspvgdvpFIRSGLLGFVGPGSLVfVVGKMDGLLMVSGRRHNADDIVATGLAVESI 764
Cdd:cd05908 366 -----TDDG-------WLKTGDLGFIRNGRLV-ITGREKDIIFVNGQNVYPHDIERIAEELEGV 416
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
962-1376 |
1.43e-12 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 71.83 E-value: 1.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 962 LAEILQWRAQATPDHVLFMLLNAKGTTVctasclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 1041
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYR------ELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1042 CIPVTVRPphaqnltatlptvrmvvdvskaacVLTTQTLMRLLKSREAAAAVDVKTWpaiidTDDLPRKRLPQLYKPPTP 1121
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSF-----TDLLAAGAPLGERVALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1122 EMLAYLDFSVSTTGMLTGVKMSHSAV--NAL-CRAIkLQcELYSSRQIAICLDP-YCGLGFALWCLCSVYSGHQSVLIP- 1196
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLvaNALqIKAW-LE-DLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLIPr 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1197 --PMELennlflwLATVNQYKIrDTFCS----YSvmelctkGLGNQVEVLKtrgINLSCIRTCVvvaeerprvslqqsfs 1270
Cdd:cd05936 203 frPIGV-------LKEIRKHRV-TIFPGvptmYI-------ALLNAPEFKK---RDFSSLRLCI---------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1271 klfkdiglspravsttfgsrvnvaiclqgtSGPDPTTVYVDLKSLRHDRVRLVE-RGapqsllLSES------------- 1336
Cdd:cd05936 249 ------------------------------SGGAPLPVEVAERFEELTGVPIVEgYG------LTETspvvavnpldgpr 292
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 755551667 1337 -----GKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYY 1376
Cdd:cd05936 293 kpgsiGIPLPGTEVKIVDDDGE-ELPPGEVGELWVRGPQVMKGYW 336
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
970-1492 |
5.16e-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: 5.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 970 AQATPDHVLFMllnAKGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGC--IPVTV 1047
Cdd:cd05945 1 AAANPDRPAVV---EGGRTLTYR---ELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1048 RPPHAQnltatlptVRMVVDVSKAACVlttqtlmrllksreaaaavdvktwpaIIDTDDlprkrlpqlykpptpemLAYL 1127
Cdd:cd05945 74 SSPAER--------IREILDAAKPALL--------------------------IADGDD-----------------NAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1128 DFSVSTTGMLTGVKMSHSAVNALCRAIkLQCELYSSRQIAIC----------LDPYCGL--GFALWCLcsvysghqsvli 1195
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNqapfsfdlsvMDLYPALasGATLVPV------------ 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1196 pPMELENNLFLWLATVNQYKIRDTFCSYSVMELCTKGLGNQVEVLKTrginlscIRTCVVVAEERPRVSLQQSFSKLfkd 1275
Cdd:cd05945 170 -PRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPS-------LRHFLFCGEVLPHKTARALQQRF--- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1276 iglsPRA-VSTTFGS-RVNVAIclqgtsgpdpTTVYVDLKSL-RHDRVRLvergapqslllsesGKILPGVKVVIVNPET 1352
Cdd:cd05945 239 ----PDArIYNTYGPtEATVAV----------TYIEVTPEVLdGYDRLPI--------------GYAKPGAKLVILDEDG 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1353 KgPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHFntrlsFGDAAQTlWARTGYLGFVrrteltAATGErhdaLYVVG 1432
Cdd:cd05945 291 R-PVPPGEKGELVISGPSVSKGY---LNNPEKTAAAF-----FPDEGQR-AYRTGDLVRL------EADGL----LFYRG 350
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551667 1433 ALDETLELRGLRYHPIDIETSVSRVHrSIAECAVFTWTNL-----LVVVVELCGSEqEALDLVPL 1492
Cdd:cd05945 351 RLDFQVKLNGYRIELEEIEAALRQVP-GVKEAVVVPKYKGekvteLIAFVVPKPGA-EAGLTKAI 413
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
996-1466 |
8.43e-12 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 69.57 E-value: 8.43e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLgDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnlTATLPTVRMVVDVSKAACVL 1075
Cdd:cd05904 37 ELERRVRRLAAGL-AKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1076 TTQTLmrLLKSREAAAAV----DVKTWPAIIDTDDLPRKRLPqlykPPTPEM----LAYLDFSVSTTGMLTGVKMSH-SA 1146
Cdd:cd05904 110 TTAEL--AEKLASLALPVvlldSAEFDSLSFSDLLFEADEAE----PPVVVIkqddVAALLYSSGTTGRSKGVMLTHrNL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1147 VNALCRAIKLQCELYSSRQIAICLDPYCGL-GFALWCLCSVYSGHQSVLIPPMELENnlflWLATVNQYKIRDTFCSYSV 1225
Cdd:cd05904 184 IAMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERYKVTHLPVVPPI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1226 MelctKGLGNQVEVLKtrginlscirtcvvvaeeRPRVSLQQSFSklfkdiGLSP--RAVSTTFGSRVNVAICLQG---- 1299
Cdd:cd05904 260 V----LALVKSPIVDK------------------YDLSSLRQIMS------GAAPlgKELIEAFRAKFPNVDLGQGygmt 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1300 TSGPDPTTVYVDLKSLRHdrvrlvergapqsllLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYytiy 1379
Cdd:cd05904 312 ESTGVVAMCFAPEKDRAK---------------YGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGY---- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1380 dsetlqadhfntrlsFGDAAQTL-------WARTGYLGFVRrteltaATGErhdaLYVVGALDETLELRGLRYHPIDIEt 1452
Cdd:cd05904 373 ---------------LNNPEATAatidkegWLHTGDLCYID------EDGY----LFIVDRLKELIKYKGFQVAPAELE- 426
|
490
....*....|....
gi 755551667 1453 SVSRVHRSIAECAV 1466
Cdd:cd05904 427 ALLLSHPEILDAAV 440
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
996-1471 |
1.23e-11 |
|
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: 68.71 E-value: 1.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltaTLPTVRM--VVDVSKAAC 1073
Cdd:cd05930 17 ELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDP--------SYPAERLayILEDSGAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1074 VLTtqtlmrllksreaaaavdvktwpaiidtddlprkrlpqlykppTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 1153
Cdd:cd05930 88 VLT-------------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1154 ikLQCELYSSR-----QIAicldpycGLGF--ALWCL-CSVYSGHQSVLIPPmELENNLFLWLATVNQYKIRDTFCSYSV 1225
Cdd:cd05930 125 --MQEAYPLTPgdrvlQFT-------SFSFdvSVWEIfGALLAGATLVVLPE-EVRKDPEALADLLAEEGITVLHLTPSL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1226 MELCTKGLGNQvevlktrgiNLSCIRTcVVVAEERPRVSLQQSFSKLFKDIGLspravsttfgsrVNVaiclqgtSGPDP 1305
Cdd:cd05930 195 LRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELLPGARL------------VNL-------YGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1306 TTVYVDLKSLRHDRVRlvERGAPqslllseSGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYytiYDSETLQ 1385
Cdd:cd05930 246 ATVDATYYRVPPDDEE--DGRVP-------IGRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLARGY---LNRPELT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1386 ADHFnTRLSFGDaaqtlWA---RTGYLgfVRRTEltaatgerHDALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIA 1462
Cdd:cd05930 313 AERF-VPNPFGP-----GErmyRTGDL--VRWLP--------DGNLEFLGRIDDQVKIRGYRIELGEIEAALLA-HPGVR 375
|
....*....
gi 755551667 1463 ECAVFTWTN 1471
Cdd:cd05930 376 EAAVVARED 384
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
262-927 |
7.01e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.50 E-value: 7.01e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 262 PPALESALQRWGSTQAKCPCLTGLDVTGKPVYTLTYGKLWSRSLKLAYTLLNKLGtknepvlkPGDRVALVYPNNdpVMF 341
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS--------FGDRAVLLFPSG--PDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 342 MVAFYGCLLAEVIPVPIEVPLTRKDAGGQQIGFLLGSCGIALALTSEICLKGLpktQNGEIVQFKGWPRLKWVVTdskYL 421
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL---LQMEELAAANAPELLCVDT---LD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 422 SKPPKDWQ-PHISPagTEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQ--ACNYSEGETVVNVLDFKKDAGLWHGMF 498
Cdd:PRK05691 152 PALAEAWQePALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHgfGIDLNPDDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 499 ANVMNkmhtiSVPYSVMKTC-----PLSWVQRVHAHKAKVAlvKCRDLHWAMMAHRdqrdVSLSSLRML------IVTDG 567
Cdd:PRK05691 230 QPIFS-----GVPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER----VSESALERLdlsrwrVAYSG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 568 ANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAMTVairrpgVPGAPlPGRAILSMNgLSYGVIRVNTEDKNSALTVQ 647
Cdd:PRK05691 299 SEPIRQDSLERFAEKFAACGFDPDSFFASYGLAEATLF------VSGGR-RGQGIPALE-LDAEALARNRAEPGTGSVLM 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 648 DVGHVMPGGMMCIVKPDGLPQLcRTDEIGEICVSSRTGGMMYFGLAGVTKNTFevipVTSSGSpvgdvPFIRSGLLGFVG 727
Cdd:PRK05691 371 SCGRSQPGHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGDLGFLR 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 728 PGSLvFVVGKMDGLLMVSGrrHNaddivatglavesiktVYrgrhtgllavPQTCQarpylRTFPLSVPSVRNPlppdlr 807
Cdd:PRK05691 441 DGEL-FVTGRLKDMLIVRG--HN----------------LY----------PQDIE-----KTVEREVEVVRKG------ 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 808 varvltsfRIAVFSVSVFYDERIVVVAE-----QRPDASEEdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGG 882
Cdd:PRK05691 481 --------RVAAFAVNHQGEEGIGIAAEisrsvQKILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGK 548
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 755551667 883 IHISQTKQLFLEGSLhpcnilmcphTCVTNLPKPRQKQPGVGPAS 927
Cdd:PRK05691 549 LQRSACRLRLADGSL----------DSYALFPALQAVEAAQTAAS 583
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1121-1451 |
1.68e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 65.59 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1121 PEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMEL 1200
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1201 ENNLFLWLATVNQYKIRDTFCSysvmELCTKGLGNQVEVLKTRGINLSCIRTCVVVAEerP-RVSLQQSFSKLFKDIGLS 1279
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSP----NFGYKYFLKTLKPEKANDWDLSSIRMILNGAE--PiDYELCHEFLDHMSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1280 PRAVSTTFG-SRVNVAICLQGTSGPdPTTVYVDLKSLRH-DRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGpVG 1357
Cdd:cd05908 259 RNAILPVYGlAEASVGASLPKAQSP-FKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1358 DSHLGEIWVNSPHTASGYYTiydsetlqadhfNTRLSFGDAAQTLWARTGYLGFVRRTELTaATGERHDALYVvgaldet 1437
Cdd:cd05908 337 DGYIGHIQIRGKNVTPGYYN------------NPEATAKVFTDDGWLKTGDLGFIRNGRLV-ITGREKDIIFV------- 396
|
330
....*....|....
gi 755551667 1438 lelRGLRYHPIDIE 1451
Cdd:cd05908 397 ---NGQNVYPHDIE 407
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
996-1466 |
4.50e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 64.02 E-value: 4.50e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGHLNAgdnVVLLYPPGIELIAAFYGCLYAG----CIPVTVRPPHAQNLTATLPTVRMVVDVSKa 1071
Cdd:PRK05851 36 EVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1072 acVLTTQTLMRLLKSREAAAAV-DVKTWPaiidtddlpRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNAL 1150
Cdd:PRK05851 112 --VLSHGSHLERLRAVDSSVTVhDLATAA---------HTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1151 CRAIKLQCELYSSRQIAICLDP-YCGLGFAlWCLCSVYSGHQSVLIPPMELENNLFLWLATVNQYkiRDTFC-----SYS 1224
Cdd:PRK05851 181 LRGLNARVGLDAATDVGCSWLPlYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDS--RATLTaapnfAYN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1225 VmelctkgLGNQVEvlKTRGINLSCIRTCVVVAEERPRVSLQQsFSKLFKDIGLSPRAVSTTFGsrVNVAIClqGTSGPD 1304
Cdd:PRK05851 258 L-------IGKYAR--RVSDVDLGALRVALNGGEPVDCDGFER-FATAMAPFGFDAGAAAPSYG--LAESTC--AVTVPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1305 PTTvyvdlkSLRHDRVRLVERGAPQSLLLSesGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYytiYDSETL 1384
Cdd:PRK05851 324 PGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY---LGQAPI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1385 QADHfntrlsfgdaaqtlWARTGYLGFvrrteLTAatgerhDALYVVGALDETLELRGLRYHPIDIETSVSRVhRSIAEC 1464
Cdd:PRK05851 393 DPDD--------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERVAAQV-RGVREG 446
|
..
gi 755551667 1465 AV 1466
Cdd:PRK05851 447 AV 448
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
996-1483 |
7.55e-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: 60.00 E-value: 7.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPH-AQNLtatlptvRMVVDVSKAACV 1074
Cdd:cd12116 17 ELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYpADRL-------RYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1075 LTTQTLMrllksreAAAAVDVKTWPAIIDTDDLPRKRLPqlyKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAI 1154
Cdd:cd12116 89 LTDDALP-------DRLPAGLPVLLLALAAAAAAPAAPR---TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1155 KLQCELYSSRQIaICLDPYCglgFALwclcsvysghqSVLippmelenNLFLWLATVNQYKIRDTFCSYSVMELctkglg 1234
Cdd:cd12116 159 RERLGLGPGDRL-LAVTTYA---FDI-----------SLL--------ELLLPLLAGARVVIAPRETQRDPEAL------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1235 nqVEVLKTRGINL-----SCIRTcVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTfGSRVNVaiclqgtSGPDPTTVY 1309
Cdd:cd12116 210 --ARLIEAHSITVmqatpATWRM-LLDAGWQGRAGLTALCGGEALPPDLAARLLSRV-GSLWNL-------YGPTETTIW 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1310 vdlkSLRHdRVRLVERGAPqslllseSGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHF 1389
Cdd:cd12116 279 ----STAA-RVTAAAGPIP-------IGRPLANTQVYVLDAALR-PVPPGVPGELYIGGDGVAQGY---LGRPALTAERF 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1390 nTRLSFGDAAQTLWaRTGYLgfVRRteltaatgERHDALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECAVFTW 1469
Cdd:cd12116 343 -VPDPFAGPGSRLY-RTGDL--VRR--------RADGRLEYLGRADGQVKIRGHRIELGEIEAALAA-HPGVAQAAVVVR 409
|
490
....*....|....*...
gi 755551667 1470 TN----LLVVVVELCGSE 1483
Cdd:cd12116 410 EDggdrRLVAYVVLKAGA 427
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
970-1165 |
1.51e-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: 59.28 E-value: 1.51e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 970 AQATPDHVLfmlLNAKGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG--CIPVTV 1047
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGaaYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1048 RPPhAQNLTATLPTVRMVvdvskaaCVLTTQTLM-RLLKSREAAAAVDVKTWPAIIDTDDLPrkrlpqlykPPTPEMLAY 1126
Cdd:cd17651 78 AYP-AERLAFMLADAGPV-------LVLTHPALAgELAVELVAVTLLDQPGAAAGADAEPDP---------ALDADDLAY 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 755551667 1127 LDFSVSTTGMLTGVKMSHSAVNALCRAiklQCELYSSRQ 1165
Cdd:cd17651 141 VIYTSGSTGRPKGVVMPHRSLANLVAW---QARASSLGP 176
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
295-765 |
2.69e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.20 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 295 LTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNDPVMfmVAFYGCLLA--EVIPVPIEVPltrkdagGQQI 372
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLR-ARG------VGPEVRVAIAAERSFELV--VALLAVLKAggAYVPLDPNYP-------AERL 2092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 373 GFLLGSCGIALALTSEICLKGLPKTQngeivqfkGWPRLKwvVTDSKYLSKPPkDWQPHISPAGTEPAYIEYKTSKEGSV 452
Cdd:PRK12316 2093 AYMLEDSGAALLLTQRHLLERLPLPA--------GVARLP--LDRDAEWADYP-DTAPAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 453 MGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWhGMFANVMNKMHTISVPYSVMKtcPLSWVQRVHAHkaK 532
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDELWD--PEQLYDEMERH--G 2236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 533 VALVKCRDLHWAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLS------LFQSHGLKPEAICPCATSAEAmTVA 606
Cdd:PRK12316 2237 VTILDFPPVYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEalrpvyLFNGYGPTEAVVTPLLWKCRP-QDP 2313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 607 IRRPGVP-GAPLPGRAilsmnglsygvirvntedknsaltvqdvGHVMPGGMmcivkpdglpQLCRTDEIGEICVSSRTG 685
Cdd:PRK12316 2314 CGAAYVPiGRALGNRR----------------------------AYILDADL----------NLLAPGMAGELYLGGEGL 2355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 686 GMMYFGLAGVTKNTFEVIPVTSSGSPVgdvpfIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIK 765
Cdd:PRK12316 2356 ARGYLNRPGLTAERFVPDPFSASGERL-----YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVR 2430
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
962-1465 |
6.70e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 57.22 E-value: 6.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 962 LAEILQWRAQATPDHVLFMLLNAKGTTV----CTASCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGC 1037
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVAVPGGRGADGklayDELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1038 LYAGCIPVTVRPPHA-QNLTATLPTVR--MVVDVSKAacvlttqTLMRLL-----KSREAAAAVDVKTWPAIIDTDDLPR 1109
Cdd:PRK09274 87 FKAGAVPVLVDPGMGiKNLKQCLAEAQpdAFIGIPKA-------HLARRLfgwgkPSVRRLVTVGGRLLWGGTTLATLLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1110 KRLP---QLYKPPTPEMLAYLdFSVSTTGMLTGVKMSHSAVNALCRAIKlqcELYSSRQIAICL---------DPYCGlg 1177
Cdd:PRK09274 160 DGAAapfPMADLAPDDMAAIL-FTSGSTGTPKGVVYTHGMFEAQIEALR---EDYGIEPGEIDLptfplfalfGPALG-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1178 falwcLCSVysghqsvlIPPMELE-----NNLFLWlATVNQYKIRDTFCSYSVMELctkgLGNQvevLKTRGINLSCIRT 1252
Cdd:PRK09274 234 -----MTSV--------IPDMDPTrpatvDPAKLF-AAIERYGVTNLFGSPALLER----LGRY---GEANGIKLPSLRR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1253 cVVVAEERPRVSLQQSFSKLfkdigLSPRA-VSTTFGSRVNVAICLqgtsgpdpttvyVDLKSLRHDRVRLVERGAPQSL 1331
Cdd:PRK09274 293 -VISAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS------------IESREILFATRAATDNGAGICV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1332 llsesGKILPGVKVVIVNPeTKGPVGDSH---------LGEIWVNSPHTASGYYTiYDSETLQAdhfntRLSfgDAAQTL 1402
Cdd:PRK09274 355 -----GRPVDGVEVRIIAI-SDAPIPEWDdalrlatgeIGEIVVAGPMVTRSYYN-RPEATRLA-----KIP--DGQGDV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755551667 1403 WARTGYLGFVrrteltaatgERHDALYVVGALDETLELRGLRYHPIDIEtSVSRVHRSIAECA 1465
Cdd:PRK09274 421 WHRMGDLGYL----------DAQGRLWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGVKRSA 472
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
959-1154 |
7.67e-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: 57.56 E-value: 7.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 959 HQFLAEilqwRAQATPDHV-LfmllnakgttVCTASCL---QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAF 1034
Cdd:COG1020 479 HELFEA----QAARTPDAVaV----------VFGDQSLtyaELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVAL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1035 YGCLYAGC--IPvtvrpphaqnLTATLPT--VRMVVDVSKAACVLTTQTLMRLLksreAAAAVDVktwpaiIDTDDLPRK 1110
Cdd:COG1020 544 LAVLKAGAayVP----------LDPAYPAerLAYMLEDAGARLVLTQSALAARL----PELGVPV------LALDALALA 603
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 755551667 1111 RLPQ--LYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAI 1154
Cdd:COG1020 604 AEPAtnPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWM 649
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
995-1466 |
1.25e-07 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 55.93 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 995 LQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltatlptvrmvvdvskaacV 1074
Cdd:cd05919 14 GQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP------------------------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1075 LTTQTLMRLLKSREAAAavdvktwpAIIDTDDlprkrlpqlykpptpemLAYLDFSVSTTGMLTGVKMSHSA----VNAL 1150
Cdd:cd05919 69 LHPDDYAYIARDCEARL--------VVTSADD-----------------IAYLLYSSGTTGPPKGVMHAHRDpllfADAM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1151 CR---AIKLQCELYSSRQIAICLdpycGLGFALWclCSVYSGHQSVLIPPMELENNLFlwlATVNQYKIRdTFCSYSVME 1227
Cdd:cd05919 124 ARealGLTPGDRVFSSAKMFFGY----GLGNSLW--FPLAVGASAVLNPGWPTAERVL---ATLARFRPT-VLYGVPTFY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1228 LCTKGLGNQVEVLktrginLSCIRTCVVVAEERPRVSLQQsfsklFKDIGLSPraVSTTFGSRVNVAICLqgtsgpdptt 1307
Cdd:cd05919 194 ANLLDSCAGSPDA------LRSLRLCVSAGEALPRGLGER-----WMEHFGGP--ILDGIGATEVGHIFL---------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1308 vyvdlkSLRHDRVRlvergapqsllLSESGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYYTIYDSetlqad 1387
Cdd:cd05919 251 ------SNRPGAWR-----------LGSTGRPVPGYEIRLVDEEGH-TIPPGEEGDLLVRGPSAAVGYWNNPEK------ 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551667 1388 hfnTRLSFGDAaqtlWARTGYLGFVrrteltAATGerhdALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECAV 1466
Cdd:cd05919 307 ---SRATFNGG----WYRTGDKFCR------DADG----WYTHAGRADDMLKVGGQWVSPVEVESLIIQ-HPAVAEAAV 367
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
286-746 |
1.28e-07 |
|
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: 56.07 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 286 DVTGKpvyTLTYGKLWSRSLKLAYTLlNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLTRK 365
Cdd:cd05911 5 ADTGK---ELTYAQLRTLSRRLAAGL-RKLG------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAANPIYTAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 366 DaggqqIGFLLGSCGIALALTSEiclKGLPKTQNgeivQFKGWPRLK--WVVTDSK-YLSKPPKDWQPHISP-------- 434
Cdd:cd05911 73 E-----LAHQLKISKPKVIFTDP---DGLEKVKE----AAKELGPKDkiIVLDDKPdGVLSIEDLLSPTLGEededlppp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 435 ---AGTEPAYIEYKTSKEGSVMGVTVSR---LAMLSQCQALSQAcNYSEGETVVNVLDFKKDAGLWhGMFANVMNKMHTI 508
Cdd:cd05911 141 lkdGKDDTAAILYSSGTTGLPKGVCLSHrnlIANLSQVQTFLYG-NDGSNDVILGFLPLYHIYGLF-TTLASLLNGATVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 509 svpysVM-KTCPLSWVQRVHAHKAKVALVKCRdlHWAMMAHRDQRDV-SLSSLRMLIVtdGANPWSVSSCDAFLSLFQSh 586
Cdd:cd05911 219 -----IMpKFDSELFLDLIEKYKITFLYLVPP--IAAALAKSPLLDKyDLSSLRVILS--GGAPLSKELQELLAKRFPN- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 587 glkpeaicPCATSAEAMTVAirrpGVPGAPLPGrailsmnglsygvirvnTEDKNSAltvqdVGHVMPGGMMCIVKPDGl 666
Cdd:cd05911 289 --------ATIKQGYGMTET----GGILTVNPD-----------------GDDKPGS-----VGRLLPNVEAKIVDDDG- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 667 PQLCRTDEIGEICVssRTGGMM--YFGLAGVTKNTFevipvTSSGspvgdvpFIRSGLLGFVGPGSLVFVVGKMDGLLMV 744
Cdd:cd05911 334 KDSLGPNEPGEICV--RGPQVMkgYYNNPEATKETF-----DEDG-------WLHTGDIGYFDEDGYLYIVDRKKELIKY 399
|
..
gi 755551667 745 SG 746
Cdd:cd05911 400 KG 401
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
962-1051 |
1.32e-07 |
|
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: 56.31 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 962 LAEILQWRAQATPDHVlfmllnAkgtTVCTASCL---QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCL 1038
Cdd:COG1021 27 LGDLLRRRAERHPDRI------A---VVDGERRLsyaELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALF 96
|
90
....*....|...
gi 755551667 1039 YAGCIPVTVRPPH 1051
Cdd:COG1021 97 RAGAIPVFALPAH 109
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
996-1466 |
1.33e-07 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 55.78 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGC--IPVTVRPPHAQNltatlptvRMVVDVSKAAC 1073
Cdd:cd17643 17 ELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGayVPIDPAYPVERI--------AFILADSGPSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1074 VLTTqtlmrllksreaaaavdvktwpaiidtddlprkrlpqlykpptPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 1153
Cdd:cd17643 88 LLTD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1154 IklQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMEL---ENNLFLWLA----TV-NQykirdTFCSYSV 1225
Cdd:cd17643 125 T--QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVarsPEDFARLLRdegvTVlNQ-----TPSAFYQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1226 MelctkglgnqVEVLKTRGINLSCIRTcVVVAEERPRVSLQQSFSKLFKDigLSPRAVSTTfgsrvnvaiclqgtsGPDP 1305
Cdd:cd17643 198 L----------VEAADRDGRDPLALRY-VIFGGEALEAAMLRPWAGRFGL--DRPQLVNMY---------------GITE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1306 TTVYVDLKSLRHDRVRLVERgapqslllSESGKILPGVKVVIVNpETKGPVGDSHLGEIWVNSPHTASGYYtiyDSETLQ 1385
Cdd:cd17643 250 TTVHVTFRPLDAADLPAAAA--------SPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYL---GRPELT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1386 ADHFNTrLSFGDAAQTLWaRTGYLgfVRRTeltaATGErhdaLYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECA 1465
Cdd:cd17643 318 AERFVA-NPFGGPGSRMY-RTGDL--ARRL----PDGE----LEYLGRADEQVKIRGFRIELGEIEAALAT-HPSVRDAA 384
|
.
gi 755551667 1466 V 1466
Cdd:cd17643 385 V 385
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
294-363 |
1.92e-07 |
|
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: 55.65 E-value: 1.92e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 294 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLT 363
Cdd:cd05936 24 KLTYRELDALAEAFAAGLQN-LG------VQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLNPLYT 84
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
323-767 |
4.19e-07 |
|
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: 54.37 E-value: 4.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 323 LKPGDRVALVYPNNDP---VMFMVAFYGCLLAEVIpvpieVPLTrKDAGGQQIGFLLGSCGIALALTSEiclKGLPKTQN 399
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIVLADA---GAADRLRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 400 GEIVQfkgwpRLKWVVTDSKYLSKPPKDWQPHIsPAGTEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGE 479
Cdd:cd05922 86 ALPAS-----PDPGTVLDADGIRAARASAPAHE-VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 480 TVVNVLDFKKDAGLwhgmfaNVMNK---------MHTISVPysvmktcPLSWVQRVHAHKAK-VALVKCrdlHWAMMAHR 549
Cdd:cd05922 160 RALTVLPLSYDYGL------SVLNThllrgatlvLTNDGVL-------DDAFWEDLREHGATgLAGVPS---TYAMLTRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 550 DQRDVSLSSLRMLIVTDGANPwsvsscDAFLSLFqshglkpeaicpcatsAEAMtvairrpgvpgaplPGRAILSMNGLS 629
Cdd:cd05922 224 GFDPAKLPSLRYLTQAGGRLP------QETIARL----------------RELL--------------PGAQVYVMYGQT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 630 YGVIRVNTEDKNSALTVQD-VGHVMPGGMMCIVKPDGLPqlCRTDEIGEICVSSRTGGMMYFglagvtkNTFEVIPVTSS 708
Cdd:cd05922 268 EATRRMTYLPPERILEKPGsIGLAIPGGEFEILDDDGTP--TPPGEPGEIVHRGPNVMKGYW-------NDPPYRRKEGR 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 755551667 709 GspvGDVpfIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIKTV 767
Cdd:cd05922 339 G---GGV--LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA 392
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
997-1465 |
4.31e-07 |
|
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: 54.39 E-value: 4.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 997 LHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltatlptvRMVVdvskaacvlt 1076
Cdd:cd05910 8 LDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP-------------GMGR---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1077 tQTLMRLLKSREAAAAVDVktwpaiidtddlprkrlpqlykpPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKl 1156
Cdd:cd05910 64 -KNLKQCLQEAEPDAFIGI-----------------------PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALR- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1157 qcELYSSRQIAICLDpycglGFALWCLCSVYSGHQSVlIPPMELE-----NNLFLwLATVNQYKIRDTFCSYSVMELCTk 1231
Cdd:cd05910 119 --QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDPTrparaDPQKL-VGAIRQYGVSIVFGSPALLERVA- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1232 glgnqvEVLKTRGINLSCIRtCVVVAEERPRVSLQQSFSKLfkdigLSPRA-VSTTFGSRVNVAICLQGTSgpdpttvyv 1310
Cdd:cd05910 189 ------RYCAQHGITLPSLR-RVLSAGAPVPIALAARLRKM-----LSDEAeILTPYGATEALPVSSIGSR--------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1311 dlkSLRHDRVRLVERGAPQSLllsesGKILPGVKVVIVnPETKGPV---GDSH------LGEIWVNSPHTASGYYTIYDS 1381
Cdd:cd05910 248 ---ELLATTTAATSGGAGTCV-----GRPIPGVRVRII-EIDDEPIaewDDTLelprgeIGEITVTGPTVTPTYVNRPVA 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1382 ETLQADHfntrlsfgDAAQTLWARTGYLGFVrrteltaatgERHDALYVVGALDETLELRGLRYHPIDIEtSVSRVHRSI 1461
Cdd:cd05910 319 TALAKID--------DNSEGFWHRMGDLGYL----------DDEGRLWFCGRKAHRVITTGGTLYTEPVE-RVFNTHPGV 379
|
....
gi 755551667 1462 AECA 1465
Cdd:cd05910 380 RRSA 383
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
969-1152 |
4.60e-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: 54.13 E-value: 4.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 969 RAQATPDHVLfmlLNAKGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVR 1048
Cdd:cd12117 6 QAARTPDAVA---VVYGDRSLTYA---ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1049 PphaqnltaTLPTVRM--VVDVSKAACVLTTqtlmrllksrEAAAAVDVKTWPAIIDTDDLPRKRLPQLYKPPTPEMLAY 1126
Cdd:cd12117 79 P--------ELPAERLafMLADAGAKVLLTD----------RSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAY 140
|
170 180
....*....|....*....|....*.
gi 755551667 1127 LDFSVSTTGMLTGVKMSHSAVNALCR 1152
Cdd:cd12117 141 VMYTSGSTGRPKGVAVTHRGVVRLVK 166
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
296-748 |
8.31e-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: 53.42 E-value: 8.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 296 TYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEV--PLTRkdaggqqIG 373
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAER-------LA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 374 FLLGSCGIALALTSEiclkglpktQNGEIVQFKGWPRLKWVVTDSKYLSKPPKDWQPHISPAGTEPAYIEYkTSkeGSV- 452
Cdd:TIGR01733 66 FILEDAGARLLLTDS---------ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 453 --MGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHgMFANVMNKMHTISVPYSVMKTCPLSWvQRVHAHK 530
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-AALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 531 aKVALVKCRDLHWAMMAhrDQRDVSLSSLRMLIVtdganpwsvsscdaflslfqshglkpeaicpcatSAEAMTVA-IRR 609
Cdd:TIGR01733 212 -PVTVLNLTPSLLALLA--AALPPALASLRLVIL----------------------------------GGEALTPAlVDR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 610 pgvPGAPLPGRAILSMnglsYG---------VIRVnTEDKNSALTVQDVGHVMPGGMMCIVKPDGlpQLCRTDEIGEICV 680
Cdd:TIGR01733 255 ---WRARGPGARLINL----YGptettvwstATLV-DPDDAPRESPVPIGRPLANTRLYVLDDDL--RPVPVGVVGELYI 324
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551667 681 SSRTGGMMYFGLAGVTKNTFevipVTSSGSPVGDVPFIRSGLLGFVGP-GSLVFvVGKMDGLLMVSGRR 748
Cdd:TIGR01733 325 GGPGVARGYLNRPELTAERF----VPDPFAGGDGARLYRTGDLVRYLPdGNLEF-LGRIDDQVKIRGYR 388
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
294-427 |
9.31e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 53.43 E-value: 9.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 294 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALvYPNNDPvMFMVAFYGCLLAEVIPVPIEvPLTRKDaggqQIG 373
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLL-YMQNSP-QFVIAYYAILRANAVVVPVN-PMNREE----ELA 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 755551667 374 FLLGSCGIALAltseICLKGLPktqnGEIVQFKGWPRLKWVVTD--SKYLSKPPKD 427
Cdd:PRK08314 102 HYVTDSGARVA----IVGSELA----PKVAPAVGNLRLRHVIVAqySDYLPAEPEI 149
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
938-1154 |
1.06e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 938 RIAQAAGRDLGQI-----EENDLV---------------RKHQFLAEilqwRAQATPDHVlfmllnakgTTVCTASCL-- 995
Cdd:PRK12316 1965 QMAEDAQAALGELalldaGERQRIladwdrtpeayprgpGVHQRIAE----QAARAPEAI---------AVVFGDQHLsy 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 -QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHaqnltatlPTVR---MVVDvSKA 1071
Cdd:PRK12316 2032 aELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY--------PAERlayMLED-SGA 2101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1072 ACVLTTQTLMRLLKSREAAAAVDVKT---WPAIIDTDDLPRKrlpqlykppTPEMLAYLDFSVSTTGMLTGVKMSHSAVN 1148
Cdd:PRK12316 2102 ALLLTQRHLLERLPLPAGVARLPLDRdaeWADYPDTAPAVQL---------AGENLAYVIYTSGSTGLPKGVAVSHGALV 2172
|
....*.
gi 755551667 1149 ALCRAI 1154
Cdd:PRK12316 2173 AHCQAA 2178
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
996-1466 |
1.25e-06 |
|
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: 52.87 E-value: 1.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltatlptvrmvvdvskaacvl 1075
Cdd:cd05958 15 DLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP-------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1076 ttqtlmrLLKSREAAAAVDvKTWPAIIDTDDlprkrlpqlyKPPTPEMLAYLDFSVSTTGMLTGVKMSHsavnalcRAIK 1155
Cdd:cd05958 69 -------LLRPKELAYILD-KARITVALCAH----------ALTASDDICILAFTSGTTGAPKATMHFH-------RDPL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1156 LQCELYsSRQI--AICLDPYCGL-------GFALWCLCSVYSGHQSVLIP---PMELennlflwLATVNQYKIRDTF--- 1220
Cdd:cd05958 124 ASADRY-AVNVlrLREDDRFVGSpplaftfGLGGVLLFPFGVGASGVLLEeatPDLL-------LSAIARYKPTVLFtap 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1221 CSYSVMelctkglgnqVEVLKTRGINLSCIRTCVVVAEERPrvslQQSFSKLFKDIGLSpraVSTTFGSRVNVAICLQGT 1300
Cdd:cd05958 196 TAYRAM----------LAHPDAAGPDLSSLRKCVSAGEALP----AALHRAWKEATGIP---IIDGIGSTEMFHIFISAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1301 SGpdpttvyvdlkslrHDRVrlverGApqslllseSGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPhtaSGYYtiYD 1380
Cdd:cd05958 259 PG--------------DARP-----GA--------TGKPVPGYEAKVVDDEGN-PVPDGTIGRLAVRGP---TGCR--YL 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1381 SETLQADHF-NTRLSFGDAaqTLWARTGYLGFVRRTeltaatgerhDALYVVGaldetlelrGLRYHPIDIEtSVSRVHR 1459
Cdd:cd05958 306 ADKRQRTYVqGGWNITGDT--YSRDPDGYFRHQGRS----------DDMIVSG---------GYNIAPPEVE-DVLLQHP 363
|
....*..
gi 755551667 1460 SIAECAV 1466
Cdd:cd05958 364 AVAECAV 370
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
959-1491 |
3.54e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 52.27 E-value: 3.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 959 HQFLAEilqwRAQATPDHVLfMLLNAKgttvcTASCLQLHKRAERIASVLGDKGhlnAGDNVV--LLYPPGIELIAAFYG 1036
Cdd:PRK12316 4554 HQLVAE----RARMTPDAVA-VVFDEE-----KLTYAELNRRANRLAHALIARG---VGPEVLvgIAMERSAEMMVGLLA 4620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1037 CLYAGCIPVTVRPPHAQNLTATlptvrMVVDvSKAACVLTTQTLMRLLKSREAAAAVDV---KTWPAIIDTDdlprkrlP 1113
Cdd:PRK12316 4621 VLKAGGAYVPLDPEYPRERLAY-----MMED-SGAALLLTQSHLLQRLPIPDGLASLALdrdEDWEGFPAHD-------P 4687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1114 QLykPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRqiaiCLDPYCGLGF--ALWCLCSVYSGHQ 1191
Cdd:PRK12316 4688 AV--RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDD----RVLQFMSFSFdgSHEGLYHPLINGA 4761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1192 SVLIPPMELENNLFLwLATVNQYKIRDTFCSYSVMELCTKGLGNQVEVLKTRGINLScirtcvvvAEERPRVSLQQSFSK 1271
Cdd:PRK12316 4762 SVVIRDDSLWDPERL-YAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFG--------GEAVAQASYDLAWRA 4832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1272 LFKDiglspravsttfgsrvnvaiCLQGTSGPDPTTVYVDLKSLRhdrvrlveRGAPQSLLLSESGKILPGVKVVIV--- 1348
Cdd:PRK12316 4833 LKPV--------------------YLFNGYGPTETTVTVLLWKAR--------DGDACGAAYMPIGTPLGNRSGYVLdgq 4884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1349 -NPETKGPVGDSHLGEIWVnsphtASGYytiYDSETLQADHFNTRlSFGDAAQTLWaRTGYLgfvrrteltaATGERHDA 1427
Cdd:PRK12316 4885 lNPLPVGVAGELYLGGEGV-----ARGY---LERPALTAERFVPD-PFGAPGGRLY-RTGDL----------ARYRADGV 4944
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551667 1428 LYVVGALDETLELRGLRYHPIDIETSVsRVHRSIAECavftwtnlLVVVVELCGSEQEALDLVP 1491
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARL-REHPAVREA--------VVIAQEGAVGKQLVGYVVP 4999
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
962-1157 |
3.55e-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: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 962 LAEILQWRAQATPDHVLFMLLNAKGTTVCTASclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 1041
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSLTWA--EFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1042 CIPVTVRPphaqnlTATLPTVRMVVDVSKAACVL--TTQTLMRLLKSREAAAAV---------------DVKTWPAIID- 1103
Cdd:COG1022 90 AVTVPIYP------TSSAEEVAYILNDSGAKVLFveDQEQLDKLLEVRDELPSLrhivvldprglrddpRLLSLDELLAl 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 755551667 1104 -TDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSH----SAVNALCRAIKLQ 1157
Cdd:COG1022 164 gREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHrnllSNARALLERLPLG 222
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
968-1147 |
4.73e-06 |
|
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: 51.12 E-value: 4.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 968 WRAQA--TPDHVlfmllnAKGTTVCTASCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPV 1045
Cdd:cd17646 4 VAEQAarTPDAP------AVVDEGRTLTYRELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1046 TVRPPHaqnltatlPTVR---MVVDVskAACVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPRkrlpqlykPPTPE 1122
Cdd:cd17646 77 PLDPGY--------PADRlayMLADA--GPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV--------PPRPD 138
|
170 180
....*....|....*....|....*
gi 755551667 1123 MLAYLDFSVSTTGMLTGVKMSHSAV 1147
Cdd:cd17646 139 NLAYVIYTSGSTGRPKGVMVTHAGI 163
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
996-1154 |
5.49e-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: 5.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltaTLPTVRMVVDVSKAACvl 1075
Cdd:cd12114 17 ELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDI--------DQPAARREAILADAGA-- 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551667 1076 ttqtlmRLLKSREAAAAVDVKTWPAIIDTDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAI 1154
Cdd:cd12114 86 ------RLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
454-754 |
9.42e-06 |
|
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: 49.59 E-value: 9.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 454 GVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWhGMFANVMNKMHTISVPysvmKTCPLSWVQRVHAHKAKV 533
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP----KFDPEAALELIEREKVTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 534 ALVKcRDLHWAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLSLF-----QSHGLkPEAICPCATSAEAMtvAIR 608
Cdd:cd04433 92 LLGV-PTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAPgiklvNGYGL-TETGGTVATGPPDD--DAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 609 RPGVPGAPLPGRAILsmnglsygvirvntedknsaltvqdvghvmpggmmcIVKPDGLPqlCRTDEIGEICVssrTGGMM 688
Cdd:cd04433 166 KPGSVGRPVPGVEVR------------------------------------IVDPDGGE--LPPGEIGELVV---RGPSV 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551667 689 YFGLAGVTKNTFEVIPvtsSGspvgdvpFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDI 754
Cdd:cd04433 205 MKGYWNNPEATAAVDE---DG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEV 260
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
294-568 |
2.91e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 48.36 E-value: 2.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 294 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLTrkdagGQQIG 373
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAA-LG------IGKGDRVAIWAPNS--PHWVIAALGALKAGAVVVPLNTRYT-----ADEAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 374 FLLGSCGIALALTSEICL-------KGLPKTQNGEIVQF-KGWPRLKWVVTDSKYLSKPPKDWQpHISPAGTEPAYIEYk 445
Cdd:PRK07656 96 YILARGDAKALFVLGLFLgvdysatTRLPALEHVVICETeEDDPHTEKMKTFTDFLAAGDPAER-APEVDPDDVADILF- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 446 TSkegsvmGVT-VSRLAMLSQCQALSQA---CNY---SEGETVVNVLDFKKDAGLWHGMFANVMNKMHTISVPysvmKTC 518
Cdd:PRK07656 174 TS------GTTgRPKGAMLTHRQLLSNAadwAEYlglTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP----VFD 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 755551667 519 PLSWVQRVHAHKAKVaLVKCRDLHWAMMAHRDQRDVSLSSLRmLIVTDGA 568
Cdd:PRK07656 244 PDEVFRLIETERITV-LPGPPTMYNSLLQHPDRSAEDLSSLR-LAVTGAA 291
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
289-390 |
3.95e-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: 48.13 E-value: 3.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 289 GKPVY-----TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYpnNDPVMFMVAFYGCLLAEVIPVPIEVPLT 363
Cdd:cd05959 19 DKTAFiddagSLTYAELEAEARRVAGALR-ALG------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100
....*....|....*....|....*...
gi 755551667 364 rkdagGQQIGFLLGSCGI-ALALTSEIC 390
Cdd:cd05959 90 -----PDDYAYYLEDSRArVVVVSGELA 112
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
966-1467 |
4.80e-05 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 47.60 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 966 LQWRAQATPDHVLFMLLnakGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPV 1045
Cdd:cd17631 1 LRRRARRHPDRTALVFG---GRSLTYA---ELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1046 tvrpPHAQNLTAtlPTVRMVVDVSKAACVLttqtlmrllksreaaaavdvktwpaiidtDDLprkrlpqlykpptpemlA 1125
Cdd:cd17631 74 ----PLNFRLTP--PEVAYILADSGAKVLF-----------------------------DDL-----------------A 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1126 YLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELySSRQIAICLDPYCGLGFA-LWCLCSVYSGHQSVLIPPMELENnl 1204
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPET-- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1205 flWLATVNQYKIRDTFCSYSVME-LCTKGlgnqvevlKTRGINLSCIRtCVVVAEERPRVSLQQSFsklfKDIGLsprAV 1283
Cdd:cd17631 179 --VLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV---KF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1284 STTFGsrvnvaiclQGTSGPdPTTVyvdlksLRHDRVRlvergapqSLLLSeSGKILPGVKVVIVNPETKgPVGDSHLGE 1363
Cdd:cd17631 241 VQGYG---------MTETSP-GVTF------LSPEDHR--------RKLGS-AGRPVFFVEVRIVDPDGR-EVPPGEVGE 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1364 IWVNSPHTASGYYTiyDSETlqadhfnTRLSFGDAaqtlWARTGYLGFVrrteltaatgeRHDA-LYVVGALDETLELRG 1442
Cdd:cd17631 295 IVVRGPHVMAGYWN--RPEA-------TAAAFRDG----WFHTGDLGRL-----------DEDGyLYIVDRKKDMIISGG 350
|
490 500
....*....|....*....|....*
gi 755551667 1443 LRYHPIDIETSVSRvHRSIAECAVF 1467
Cdd:cd17631 351 ENVYPAEVEDVLYE-HPAVAEVAVI 374
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
294-485 |
5.59e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 47.62 E-value: 5.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 294 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNDpvMFMVAFYGCLLAEVIPVPIEVPLTrkdagGQQIG 373
Cdd:PRK08316 36 SWTYAELDAAVNRVAAALLD-LG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLT-----GEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 374 FLLGSCGIALALTSEICLKGLPKTQNGEIVQFKGWPRL--------KWVVTDSKYLSKPpkDWQPHISPAGTEPAYIEYK 445
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVlggreapgGWLDFADWAEAGS--VAEPDVELADDDLAQILYT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 755551667 446 TSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGETVVNVL 485
Cdd:PRK08316 180 SGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHAL 219
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
996-1144 |
8.35e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 47.30 E-value: 8.35e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRP-------------------------- 1049
Cdd:PRK05605 62 ELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPlytahelehpfedhgarvaivwdkva 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1050 PHAQNLTATLPtVRMVVDVS-KAACVLTTQTLMRL-----LKSREA--AAAVDVKTWPAIIDTDDLPRKRLPQLYKPpTP 1121
Cdd:PRK05605 141 PTVERLRRTTP-LETIVSVNmIAAMPLLQRLALRLpipalRKARAAltGPAPGTVPWETLVDAAIGGDGSDVSHPRP-TP 218
|
170 180
....*....|....*....|...
gi 755551667 1122 EMLAYLDFSVSTTGMLTGVKMSH 1144
Cdd:PRK05605 219 DDVALILYTSGTTGKPKGAQLTH 241
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
294-564 |
1.17e-04 |
|
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: 47.16 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 294 TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPI--EVPLTRkdaggqq 371
Cdd:COG1020 501 SLTYAELNARANRLAHHLR-ALG------VGPGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLdpAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 372 IGFLLGSCGIALALTSEICLKGLPKTQngeivqfkgwprLKWVVTDSKYLSKPPKDWqPHISPAGTEPAYIEYkTS---- 447
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPELG------------VPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TSgstg 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 448 --KegsvmGVTVSRLAMLSQCQALSQACNYSEGETVVNV--LDFkkDAGLWhGMFANVMNKMHTISVPYSVMKTcPLSWV 523
Cdd:COG1020 631 rpK-----GVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW-EIFGALLSGATLVLAPPEARRD-PAALA 701
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 755551667 524 QRVHAHkaKVALVKCRDLHWAMMAHRDQRDvsLSSLRMLIV 564
Cdd:COG1020 702 ELLARH--RVTVLNLTPSLLRALLDAAPEA--LPSLRLVLV 738
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
293-356 |
1.21e-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: 1.21e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551667 293 YTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPV 356
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 ... |
1332-1423 |
1.24e-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: 1.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1332 LLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYY-----TiydSETLQADH-FNTrlsfGDAAQtlWAR 1405
Cdd:cd17640 262 VRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYknpeaT---SKVLDSDGwFNT----GDLGW--LTC 332
|
90 100
....*....|....*....|
gi 755551667 1406 TGYLGFVRRTELTA--ATGE 1423
Cdd:cd17640 333 GGELVLTGRAKDTIvlSNGE 352
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1337-1466 |
2.35e-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: 45.33 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1337 GKILPGVKVVIVNPETKGPVGDSHlGEIWVNSPHTASGYytiYDSETLQADHFNTRlsfgdaaqtlWARTGYLGFVRrte 1416
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGY---WNNPERTAEVLIDG----------WVNTGDLGERR--- 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 755551667 1417 ltaatgeRHDALYVVGALDETLELRGLRYHPIDIETSVSRVhRSIAECAV 1466
Cdd:cd17635 236 -------EDGFLFITGRSSESINCGGVKIAPDEVERIAEGV-SGVQECAC 277
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1005-1479 |
3.52e-04 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 45.12 E-value: 3.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1005 ASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTATlpTVRMVVDVSKAACVLTTQTLMrll 1084
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKES--VLRYLVADAGGRIVLADAGAA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1085 kSREAAAAVDVKTWPAIIDTDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVnalcraiklqceLYSSR 1164
Cdd:cd05922 81 -DRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNL------------LANAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1165 QIAICLDpYCGLGFALWCLCSVYSGHQSVLippmeleNNLFLWLATV---NQYKIRDTFcsysvMELCTKglgnqvevlk 1241
Cdd:cd05922 148 SIAEYLG-ITADDRALTVLPLSYDYGLSVL-------NTHLLRGATLvltNDGVLDDAF-----WEDLRE---------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1242 TRGINLSCIrtcvvvaeerPrvSLQQSFSKL-FKDIGL-SPRAVSTTFGSRVNVAICLQGTSGPDpTTVYV--------- 1310
Cdd:cd05922 205 HGATGLAGV----------P--STYAMLTRLgFDPAKLpSLRYLTQAGGRLPQETIARLRELLPG-AQVYVmygqteatr 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1311 DLKSLRHDRVRlvERgaPQSLllsesGKILPGVKVVIVNPEtKGPVGDSHLGEIWVNSPHTASGYytiydsetlqadhfn 1390
Cdd:cd05922 272 RMTYLPPERIL--EK--PGSI-----GLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGY--------------- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1391 trlsfgdaaqtlWARTGYLGFVRRTELTAATGE--RHDA---LYVVGALDETLELRGLRYHPIDIETSVsRVHRSIAECA 1465
Cdd:cd05922 327 ------------WNDPPYRRKEGRGGGVLHTGDlaRRDEdgfLFIVGRRDRMIKLFGNRISPTEIEAAA-RSIGLIIEAA 393
|
490
....*....|....*...
gi 755551667 1466 VF----TWTNLLVVVVEL 1479
Cdd:cd05922 394 AVglpdPLGEKLALFVTA 411
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
962-1144 |
3.61e-04 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 45.13 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 962 LAEILQWRAQATPDHVLFMLlnakGTTVCTASclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 1041
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLVF----GGTRWTYA--EAARAAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1042 CIPVTV----RPPHaqnLTATLPTVRMVVDVSKAACVLTTQTLMRLLKSREAAAAVD---VKTWPAIIDTDDLPRKRLPQ 1114
Cdd:PRK06155 96 AIAVPIntalRGPQ---LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDapaSVSVPAGWSTAPLPPLDAPA 172
|
170 180 190
....*....|....*....|....*....|.
gi 755551667 1115 LYKPPTP-EMLAYLDFSvSTTGMLTGVKMSH 1144
Cdd:PRK06155 173 PAAAVQPgDTAAILYTS-GTTGPSKGVCCPH 202
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
960-1053 |
3.67e-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: 3.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 960 QFLAEILQWRAQATPDHVlfMLLNAKGTTvctaSCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLY 1039
Cdd:cd05920 15 EPLGDLLARSAARHPDRI--AVVDGDRRL----TYRELDRRADRLAAGLRGLG-IRPGDRVVVQLPNVAEFVVLFFALLR 87
|
90
....*....|....
gi 755551667 1040 AGCIPVTVRPPHAQ 1053
Cdd:cd05920 88 LGAVPVLALPSHRR 101
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
519-892 |
3.74e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 44.99 E-value: 3.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 519 PLSWVQRVHAHKAKVALVKcrDLHWAMMAHR-----DQRDVSLSSLRmlIVTDGANPWSVSSCDAFLSLFQSHGLKPEAI 593
Cdd:PRK07768 235 PLLWAELISKYRGTMTAAP--NFAYALLARRlrrqaKPGAFDLSSLR--FALNGAEPIDPADVEDLLDAGARFGLRPEAI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 594 CPCATSAEAmTVAIRRPGvPGAPL----PGRAILSMNGlsygviRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGlpQL 669
Cdd:PRK07768 311 LPAYGMAEA-TLAVSFSP-CGAGLvvdeVDADLLAALR------RAVPATKGNTRRLATLGPPLPGLEVRVVDEDG--QV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 670 CRTDEIGEICVSSRTggmmyfglagVTKNTfevipVTSSG--SPVGDVPFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGR 747
Cdd:PRK07768 381 LPPRGVGVIELRGES----------VTPGY-----LTMDGfiPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 748 RHNADDIVATGLAVESIktvyrgRHTGLLAVpqtcqarpylrtfPLSVPSVRnplppdlrvarvltsfriavfsvsvfyd 827
Cdd:PRK07768 446 NIYPTDIERAAARVEGV------RPGNAVAV-------------RLDAGHSR---------------------------- 478
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755551667 828 ERIVVVAEQRPDASEEDSFQWMSRVLQAIDSihQVGV--YCLALVPANTLPKTPLGGIHISQTKQLF 892
Cdd:PRK07768 479 EGFAVAVESNAFEDPAEVRRIRHQVAHEVVA--EVGVrpRNVVVLGPGSIPKTPSGKLRRANAAELV 543
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
996-1466 |
4.63e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 44.60 E-value: 4.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCiPVTV--RPPHAQNLTA----TLPTVRMV---- 1065
Cdd:PRK07768 34 EVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGA-SLTMlhQPTPRTDLAVwaedTLRVIGMIgaka 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1066 VDVSK----AACVLTTQ--TLMRLLKSREAAAAVDVKTwpaiiDTDDLprkrlpqlykpptpemlAYLDFSVSTTGMLTG 1139
Cdd:PRK07768 112 VVVGEpflaAAPVLEEKgiRVLTVADLLAADPIDPVET-----GEDDL-----------------ALMQLTSGSTGSPKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1140 VKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYC---GL-GFalwcLCS-VYSGHQSVLIPPMELENNLFLWLATVNQY 1214
Cdd:PRK07768 170 VQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFhdmGMvGF----LTVpMYFGAELVKVTPMDFLRDPLLWAELISKY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1215 KIRDT----FcSYSVmelctkgLGNQVEVLKTRG-INLSCIRtCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFG- 1288
Cdd:PRK07768 246 RGTMTaapnF-AYAL-------LARRLRRQAKPGaFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGm 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1289 --SRVNVAICLQGTsGPDPTTVYVDLKSLRHdRVRLVERGAPQSLLLSesGKILPGVKVVIVNpETKGPVGDSHLGEIWV 1366
Cdd:PRK07768 317 aeATLAVSFSPCGA-GLVVDEVDADLLAALR-RAVPATKGNTRRLATL--GPPLPGLEVRVVD-EDGQVLPPRGVGVIEL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1367 NSPHTASGYYTIYDSETLQADHfntrlsfGdaaqtlWARTGYLGFVrrTELtaatGErhdaLYVVGALDETLELRGLRYH 1446
Cdd:PRK07768 392 RGESVTPGYLTMDGFIPAQDAD-------G------WLDTGDLGYL--TEE----GE----VVVCGRVKDVIIMAGRNIY 448
|
490 500
....*....|....*....|
gi 755551667 1447 PIDIETSVSRVHRSIAECAV 1466
Cdd:PRK07768 449 PTDIERAAARVEGVRPGNAV 468
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
964-1228 |
1.03e-03 |
|
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: 43.47 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 964 EILQWRAQATPDHVlfmllnakgTTVC---TASCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYA 1040
Cdd:cd17655 1 ELFEEQAEKTPDHT---------AVVFedqTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1041 GCIPVTVRPPHAQNltatlpTVRMVVDVSKAACVLTTQTLMRLLKSREAAAAvdvktwpaiIDTDDLPRKRLPQLYKPPT 1120
Cdd:cd17655 71 GGAYLPIDPDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLIDL---------LDEDTIYHEESENLEPVSK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1121 PEMLAYLDFSVSTTGMLTGVKMSH--------SAVNALCRAIKLQCELYSSrqiaICLDPYCGLGFAlwclcSVYSGHQS 1192
Cdd:cd17655 136 SDDLAYVIYTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFDASVTEIFA-----SLLSGNTL 206
|
250 260 270
....*....|....*....|....*....|....*.
gi 755551667 1193 VLIPPMELENNLFLwLATVNQYKIRDTFCSYSVMEL 1228
Cdd:cd17655 207 YIVRKETVLDGQAL-TQYIRQNRITIIDLTPAHLKL 241
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
268-358 |
1.10e-03 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 43.56 E-value: 1.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 268 ALQRWGSTQAKCPCLTGLDVTGKPVyTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYG 347
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGEDGEER-TLTYAELRREVNRFA-NALRALG------VKKGDRVAIYLPNI--PEAVIAMLA 83
|
90
....*....|.
gi 755551667 348 CLLAEVIPVPI 358
Cdd:COG0365 84 CARIGAVHSPV 94
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
996-1466 |
1.13e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 44.00 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 996 QLHKRAERIASVLGDKGhlnAGDNVV--LLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTATlptvrMVVDvSKAAC 1073
Cdd:PRK12467 3125 ELNRRANRLAHRLIAIG---VGPDVLvgVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY-----MIED-SGVKL 3195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1074 VLTTQtlmRLLKSREAAAAVDVKTwpaiIDTDDLPrkrlPQLYKPPT----PEMLAYLDFSVSTTGMLTGVKMSHSAVNA 1149
Cdd:PRK12467 3196 LLTQA---HLLEQLPAPAGDTALT----LDRLDLN----GYSENNPStrvmGENLAYVIYTSGSTGKPKGVGVRHGALAN 3264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1150 LCRAIKLQCELySSRQIAICLDPYCGLGFA---LWCLCsvySGHQsVLIPPMELENNLFLWlATVNQYKIrdtfcsySVM 1226
Cdd:PRK12467 3265 HLCWIAEAYEL-DANDRVLLFMSFSFDGAQerfLWTLI---CGGC-LVVRDNDLWDPEELW-QAIHAHRI-------SIA 3331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1227 ELCTKGLGNQVEVLKTRgiNLSCIRTCVVVAEERPRVSLQQSFSKLfkdiglsPRAvsttfgsrvnvaiCLQGTSGPDPT 1306
Cdd:PRK12467 3332 CFPPAYLQQFAEDAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKL-------KPR-------------GLTNGYGPTEA 3389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1307 TVYVDLKSLRHDRVRLVErGAPqslllseSGKILPGVKVVIVNPETkGPVGDSHLGEIWVNSPHTASGYytiYDSETLQA 1386
Cdd:PRK12467 3390 VVTVTLWKCGGDAVCEAP-YAP-------IGRPVAGRSIYVLDGQL-NPVPVGVAGELYIGGVGLARGY---HQRPSLTA 3457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1387 DHFNTRlSFGDAAQTLWaRTGYLGFVRRTELtaatgerhdaLYVVGALDETLELRGLRYHPIDIETSVsRVHRSIAECAV 1466
Cdd:PRK12467 3458 ERFVAD-PFSGSGGRLY-RTGDLARYRADGV----------IEYLGRIDHQVKIRGFRIELGEIEARL-LQHPSVREAVV 3524
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
295-386 |
1.78e-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: 42.47 E-value: 1.78e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 295 LTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEvPLTRKDaggqQIGF 374
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKG------VRKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90
....*....|..
gi 755551667 375 LLGSCGIALALT 386
Cdd:cd05935 68 ILNDSGAKVAVV 79
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
294-396 |
1.93e-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: 42.60 E-value: 1.93e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 294 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNDPvmFMVAFYGCLLAEVIPVPIEVPLTRKDaggqqIG 373
Cdd:cd17631 20 SLTYAELDERVNRLAHALRA-LG------VAKGDRVAVLSKNSPE--FLELLFAAARLGAVFVPLNFRLTPPE-----VA 85
|
90 100 110
....*....|....*....|....*....|
gi 755551667 374 FLLGSCGiALALTSEICL-------KGLPK 396
Cdd:cd17631 86 YILADSG-AKVLFDDLALlmytsgtTGRPK 114
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
294-372 |
2.34e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 42.35 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 294 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNndPVMFMVAFYGCLLAEVIPV-------PIEVPLTRKD 366
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPN--LLQYPIALFGILRAGMIVVnvnplytPRELEHQLND 119
|
....*.
gi 755551667 367 AGGQQI 372
Cdd:PRK08974 120 SGAKAI 125
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
277-364 |
2.44e-03 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 42.23 E-value: 2.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 277 AKCPCLTGLDVTGKpvyTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVAlVYPNNDPVMFmVAFYGCLLA--EVI 354
Cdd:cd05945 2 AANPDRPAVVEGGR---TLTYRELKERADALA-AALASLG------LDAGDPVV-VYGHKSPDAI-AAFLAALKAghAYV 69
|
90
....*....|
gi 755551667 355 PVPIEVPLTR 364
Cdd:cd05945 70 PLDASSPAER 79
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1337-1467 |
2.83e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 41.95 E-value: 2.83e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1337 GKILPGVKVVIVNpetkgpvgdshlGEIWVNSPHTASGYYTIYDsetlqadhfntrlsFGDAAQTLWARTGYLGFVrrte 1416
Cdd:PRK07824 195 GVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVD--------------PDPFAEPGWFRTDDLGAL---- 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 755551667 1417 ltaatgerHD-ALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECAVF 1467
Cdd:PRK07824 245 --------DDgVLTVLGRADDAISTGGLTVLPQVVEAALAT-HPAVADCAVF 287
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1333-1466 |
2.95e-03 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 41.95 E-value: 2.95e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 1333 LSESGKILPGVKVVIVNPETKgPVGDshlGEIWVNSPHTASGYY--TIYDSETLQADHFNTrlsfGDaaqtlwarTGYL- 1409
Cdd:cd05912 241 IGSAGKPLFPVELKIEDDGQP-PYEV---GEILLKGPNVTKGYLnrPDATEESFENGWFKT----GD--------IGYLd 304
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755551667 1410 --GFV----RRTELTAATGERhdaLYvvgaldetlelrglryhPIDIETSVSRvHRSIAECAV 1466
Cdd:cd05912 305 eeGFLyvldRRSDLIISGGEN---IY-----------------PAEIEEVLLS-HPAIKEAGV 346
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
290-364 |
5.52e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 41.03 E-value: 5.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 290 KPVY-----TLTYGKLWSRSLKLAYTLLNKLGTKNEPVlkpgdrvaLVYPNNDPVMfMVAFYGCLLA--EVIPVPIEVPL 362
Cdd:PRK04813 18 FPAYdylgeKLTYGQLKEDSDALAAFIDSLKLPDKSPI--------IVFGHMSPEM-LATFLGAVKAghAYIPVDVSSPA 88
|
..
gi 755551667 363 TR 364
Cdd:PRK04813 89 ER 90
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
242-386 |
6.66e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 40.79 E-value: 6.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551667 242 PEGRQMTPVKgePLGVIcnwppALESALQRWGSTQAKCPcltGLDVTGkpvYTLTYGKLWSRSLKLAyTLLNKLGtknep 321
Cdd:PRK06178 19 PAGIPREPEY--PHGER-----PLTEYLRAWARERPQRP---AIIFYG---HVITYAELDELSDRFA-ALLRQRG----- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551667 322 vLKPGDRVALVYPNNdPvMFMVAFYGCLLAEVIPVPIEvPLTRkdagGQQIGFLLGSCGIALALT 386
Cdd:PRK06178 80 -VGAGDRVAVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFR----EHELSYELNDAGAEVLLA 136
|
|
| |
