|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1050-1615 |
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: 737.62 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1050 LFMLLNAKGTTVCTASCLQLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPH-AQNLT 1128
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1129 ATLPTVRMvvDVSKAACVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPRKRLP-----QLYKPPTPEMLAYLDFSV 1203
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1204 STTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMELENNLFLWLATV 1283
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1284 NQYKIRDTFCSYSVMELCTKGLGNQVEVLKTRGINLSCIRTCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGSRV 1363
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1364 NVAICLQGTSGPDPTTVYVDLKSLRHDRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHT 1443
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1444 ASGYYTIYDSETLQADHFN-TRLSFGDaAQTLWARTGYLGFVRRTELTAATGERHDALYVVGALDETLELRGLRYHPIDI 1522
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFPsTRLSTGI-TNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1523 ETSVSRVHRSIAECAVFTWTNLLVVVVEL-CGSEQEALDLVPLVTNVVLEEHYLIVGVVVVVDPGVVPINSRGEKQRMHL 1601
Cdd:cd05905 478 EATVMRVHPYRGRCAVFSITGLVVVVAEQpPGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEI 557
|
570
....*....|....
gi 755551660 1602 RDSFLADQLDPIYV 1615
Cdd:cd05905 558 RQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
353-974 |
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: 664.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 353 CLTGLDVTGKPVYTLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPnnDPVMFMVAFYGCLLAEVIPVPIEV 432
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 433 PLtrkdaGGQQIGFLLGSCGIALALTSEICLKGLPKT-----QNGEIVQFKGWPRLKWVVTDSKYLSKPPKDWQPHISPA 507
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 508 GTEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVM 587
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 588 KTCPLSWVQRVHAHKAKVALVKCRDLHWAMM------AHRDQRDVSLSSLRMLIVTDGaNPWSVSSCDAFLSLFQSHGLK 661
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKdlsstlASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 662 PEAIcpcatSAEAMTVAIRRPGVPGA--PLPGRAILSMNGLSYGVIRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGLP 739
Cdd:cd05905 307 PRAV-----STEFGTRVNPFICWQGTsgPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 740 qLCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVTSSGSPVGDVPFIRSGLLGFVGPGS----------LVFVVGK 809
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTKctdlnveehdLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 810 MDGLLMVSGRRHNADDIVATGLAVESiktvYRGrhtgllavpqtcqarpylrtfplsvpsvrnplppdlrvarvltsfRI 889
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRG---------------------------------------------RC 491
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 890 AVFSVSvfydERIVVVAEQRPdASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLFLEGSL 969
Cdd:cd05905 492 AVFSIT----GLVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKL 566
|
....*
gi 755551660 970 HPCNI 974
Cdd:cd05905 567 HPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1040-1573 |
8.44e-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: 8.44e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1040 WRAQATPDHVLFMLLNAKGTTVCTASCLQLHKRAERIASVLgdKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTV 1119
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1120 RPPHAqnlTATLPTVRMVVDVSKAACVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPRKRLPQLyKPPTPEMLAYL 1199
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPP-PSPDPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1200 DFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPY--CGLGFALwcLCSVYSGHQSVLIPPMELENNLF 1277
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLIGGL--LTPLYSGGPSVLMSPAAFLRRPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1278 LWLATVNQYkiRDTFcsySVM-----ELCTKglgnQVEVLKTRGINLSCIRTCVVVAeERPRVSLQQSFSKLFKDIGLSP 1352
Cdd:cd05931 233 RWLRLISRY--RATI---SAApnfayDLCVR----RVRDEDLEGLDLSSWRVALNGA-EPVRPATLRRFAEAFAPFGFRP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1353 RAVSTTFG---SRVNVAIclqGTSGPDPTTVYVDLKSLRHDRVRLVERGAPQSLLLSeSGKILPGVKVVIVNPETKGPVG 1429
Cdd:cd05931 303 EAFRPSYGlaeATLFVSG---GPPGTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDQEVRIVDPETGRELP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1430 DSHLGEIWVNSPHTASGYYTiydSETLQADHFNTRLSFGDAAqtlWARTGYLGFVRRteltaatGErhdaLYVVGALDET 1509
Cdd:cd05931 379 DGEVGEIWVRGPSVASGYWG---RPEATAETFGALAATDEGG---WLRTGDLGFLHD-------GE----LYITGRLKDL 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755551660 1510 LELRGLRYHPIDIETSVSRVHRSIAE--CAVFTW----TNLLVVVVELcGSEQEALDLVPLVTNV---VLEEH 1573
Cdd:cd05931 442 IIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEV-ERGADPADLAAIAAAIraaVAREH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
343-965 |
5.44e-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: 5.44e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 343 RWGSTQAKCPCLTGLDVTGKPVYTLTYGKLWSRSLKLAYTLLnklgtknePVLKPGDRVALVYPNNdpVMFMVAFYGCLL 422
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAPPG--LDFVAAFLGCLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 423 AEVIPVPIEVPLTRKDAggQQIGFLLGSCGIALALTSEICLKGLPKTqngeIVQFKGWPRLKWVVTDSKyLSKPPKDWQP 502
Cdd:cd05931 71 AGAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLL-PDTSAADWPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 503 hISPAGTEPAYIEYkTSkeGSV---MGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMFANVMN---- 575
Cdd:cd05931 144 -PSPDPDDIAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSggps 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 576 -KMHTISVpysVMKtcPLSWVQRVHAHKAKV------ALVKCrdlhwAMMAHRDQRD-VSLSSLRMLIVtdGANPWSVSS 647
Cdd:cd05931 220 vLMSPAAF---LRR--PLRWLRLISRYRATIsaapnfAYDLC-----VRRVRDEDLEgLDLSSWRVALN--GAEPVRPAT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 648 CDAFLSLFQSHGLKPEAICPCATSAEAmTVAI---RRPGVPGAPLPGRAILSmnglsyGVIRVNTEDKNSALTVQDVGHV 724
Cdd:cd05931 288 LRRFAEAFAPFGFRPEAFRPSYGLAEA-TLFVsggPPGTGPVVLRVDRDALA------GRAVAVAADDPAARELVSCGRP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 725 MPGGMMCIVKPDGLpQLCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVTSSGspvgdvPFIRSGLLGFVGPGSLv 804
Cdd:cd05931 361 LPDQEVRIVDPETG-RELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 805 FVVGKMDGLLMVSGRRHNADDIVATglaVESIktvyrgrhtgllavpqtcqarpylrtfplsvpsvrnplPPDLRVARVl 884
Cdd:cd05931 433 YITGRLKDLIIVRGRNHYPQDIEAT---AEEA--------------------------------------HPALRPGCV- 470
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 885 tsfriAVFSVSVFYDERIVVVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLF 964
Cdd:cd05931 471 -----AAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAY 545
|
.
gi 755551660 965 L 965
Cdd:cd05931 546 L 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1038-1513 |
9.58e-51 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 185.98 E-value: 9.58e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1038 LQWRAQATPDHVLFMllNAKGTTVctaSCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPV 1117
Cdd:pfam00501 1 LERQAARTPDKTALE--VGEGRRL---TYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1118 TVRPphaqnlTATLPTVRMVVDVSKAACVLTTQTLmRLLKSREAAAAVDVKTWPAIIDTDDLPRKRL-----------PQ 1186
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDDAL-KLEELLEALGKLEVVKLVLVLDRDPVLKEEPlpeeakpadvpPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1187 LYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCE----LYSSRQIAICLDPYCGLGFALWCLCSVYSGH 1262
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1263 QSVLIPPMELeNNLFLWLATVNQYKIRDTFCSYSVMELCtkglgnqVEVLKTRGINLSCIRTCVVVAeERPRVSLQQSFS 1342
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1343 KLFkdiglsPRAVSTTFGSRVNVAICLQGTSGPDPTTvyvdlkslrhdrvrlvergapqslLLSESGKILPGVKVVIVNP 1422
Cdd:pfam00501 299 ELF------GGALVNGYGLTETTGVVTTPLPLDEDLR------------------------SLGSVGRPLPGTEVKIVDD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1423 ETKGPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHFNTrlsfGDaaqtlWARTGYLGfvRRTEltaaTGErhdaLYV 1502
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAFDE----DG-----WYRTGDLG--RRDE----DGY----LEI 406
|
490
....*....|.
gi 755551660 1503 VGALDETLELR 1513
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 ... |
1196-1560 |
4.32e-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: 137.80 E-value: 4.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1196 LAYLDFSVSTTGMLTGVKMSHSAVNALCRAIkLQCELYSSRQIAICLDPYC---GLGFALWCLcsvYSGHQSVLIPPMEL 1272
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFhigGLFGLLGAL---LAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1273 EnnlfLWLATVNQYKIRDTFCSYSVMELCtkglgnqVEVLKTRGINLSCIRTCVVVAEERPRvSLQQSFSKLFKDI---- 1348
Cdd:cd04433 78 E----AALELIEREKVTILLGVPTLLARL-------LKAPESAGYDLSSLRALVSGGAPLPP-ELLERFEEAPGIKlvng 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1349 -GLSPRAVSTTFGSRVNVAIclqgtsgpDPTTVyvdlkslrhdrvrlvergapqslllsesGKILPGVKVVIVNPETkGP 1427
Cdd:cd04433 146 yGLTETGGTVATGPPDDDAR--------KPGSV----------------------------GRPVPGVEVRIVDPDG-GE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1428 VGDSHLGEIWVNSPHTASGYYTIYDsetlqadhfNTRLSFGDAaqtlWARTGYLGFVRrteltaatgeRHDALYVVGALD 1507
Cdd:cd04433 189 LPPGEIGELVVRGPSVMKGYWNNPE---------ATAAVDEDG----WYRTGDLGRLD----------EDGYLYIVGRLK 245
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 755551660 1508 ETLELRGLRYHPIDIETSVSRvHRSIAECAVF-----TWTNLLVVVVELCGSEQEALD 1560
Cdd:cd04433 246 DMIKSGGENVYPAEVEAVLLG-HPGVAEAAVVgvpdpEWGERVVAVVVLRPGADLDAE 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1034-1528 |
1.04e-31 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 136.45 E-value: 1.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1034 LAEILQWRAQATPDHVLFMLLNAKGTTVCTASCLQLHKRAERIASVLGDKGHLnaGDNVVLLYPPGIELIAAFYGCLYAG 1113
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1114 CIPVTVRPP------HAQNLTAtlptvrmVVDVSKAACVLTTQTLMRLLKSREAAAAVDVKTWPAI--IDTDDLPRKRLP 1185
Cdd:PRK05691 89 VIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVdtLDPALAEAWQEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1186 QLykppTPEMLAYLDFSVSTTGMLTGVKMSHSAVNAlcraiklqCELYSSRQIAICLDP----------YCGLGFALWCL 1255
Cdd:PRK05691 162 AL----QPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1256 CSVYSGHQSVLIPPmelenNLFL-----WLATVNQYkiRDT----------FCSYSVMELCTKGLgnqvevlktrgiNLS 1320
Cdd:PRK05691 230 QPIFSGVPCVLMSP-----AYFLerplrWLEAISEY--GGTisggpdfayrLCSERVSESALERL------------DLS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1321 CIRTCVVVAEERPRVSLqQSFSKLFKDIGLSPRAVSTTFGSRVNVAICLQGTSGPDPTTVYVDLKSLRHDRvrlVERGAP 1400
Cdd:PRK05691 291 RWRVAYSGSEPIRQDSL-ERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNR---AEPGTG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1401 QSLLlsESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTiyDSETlqadhfnTRLSFGDAAQTLWARTGY 1480
Cdd:PRK05691 367 SVLM--SCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR--NPEA-------SAKTFVEHDGRTWLRTGD 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 755551660 1481 LGFVRRTEltaatgerhdaLYVVGALDETLELRGLRYHPIDIETSVSR 1528
Cdd:PRK05691 436 LGFLRDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVER 472
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
14-130 |
1.97e-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: 1.97e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 14 AALPPEVRAQLAELELELSEGDITQKGYEKKRSKLLSPYSPQTQetdsigqkernqtpapTAAQTSAPSKYHR-SRSGGA 92
Cdd:pfam06464 3 PSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLHPE----------------TPTKLSAEAQNQLaSLETKL 66
|
90 100 110
....*....|....*....|....*....|....*...
gi 755551660 93 RDERYRSDIHTEAVQAALAKHKEQKMALPMPTKRRSTF 130
Cdd:pfam06464 67 RDEELSEEVYLEKVKALLAKELERENGLNAPTKEQSGL 104
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1038-1569 |
7.39e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 117.74 E-value: 7.39e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1038 LQWRAQATPDHVLFMLLNAKGTTVCTASCL---QLHKRAERIASVLgdKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGC 1114
Cdd:PRK05850 7 LRERASLQPDDAAFTFIDYEQDPAGVAETLtwsQLYRRTLNVAEEL--RRHGSTGDRAVILAPQGLEYIVAFLGALQAGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1115 IPVTVRPPHAqnlTATLPTVRMVVDVSKAACVLTTqtlmrllksreAAAAVDVKTW---------PAII--DTDDLPRKR 1183
Cdd:PRK05850 85 IAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTT-----------SAVVDDVTEYvapqpgqsaPPVIevDLLDLDSPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1184 LPQLYKPPTPEMlAYLDFSVSTTGMLTGVKMSHSAVNALCRaiKLQCELYSSRQIAICLD-------P-YCGLGFALWCL 1255
Cdd:PRK05850 151 GSDARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMGLVLGVC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1256 CSVYSGHQSVLIPPMElennlFL-----W---LATVNQykirdtfcSYSV-----MELCTKglgnqvevlKTR-----GI 1317
Cdd:PRK05850 228 APILGGCPAVLTSPVA-----FLqrparWmqlLASNPH--------AFSAapnfaFELAVR---------KTSdddmaGL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1318 NLSCIRTcVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFG---SRVNVAIclqGTSGPDPTTVYVDLKSLRHDRVR- 1393
Cdd:PRK05850 286 DLGGVLG-IISGSERVHPATLKRFADRFAPFNLRETAIRPSYGlaeATVYVAT---REPGQPPESVRFDYEKLSAGHAKr 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1394 --------LVERGAPQSLLlsesgkilpgvkVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTiYDSETLQAdhFNTRL 1465
Cdd:PRK05850 362 cetgggtpLVSYGSPRSPT------------VRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQ-KPEETERT--FGATL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1466 ---SFGDAAQTlWARTGYLGFVrrteltaATGErhdaLYVVGALDETLELRGLRYHPIDIETSVSRVHRsiAECAVFT-- 1540
Cdd:PRK05850 427 vdpSPGTPEGP-WLRTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATIQEITG--GRVAAISvp 492
|
570 580 590
....*....|....*....|....*....|....
gi 755551660 1541 --WTNLLVVVVEL---CGSEQEALDLVPLVTNVV 1569
Cdd:PRK05850 493 ddGTEKLVAIIELkkrGDSDEEAMDRLRTVKREV 526
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
357-969 |
1.10e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 117.52 E-value: 1.10e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 357 LDVTGK----PVYTLT-YGKLWSRSL--KLAYTLLN---------------KLGTKN-------EPVLKPGDRVALVYPN 407
Cdd:PRK07769 9 FDVNGKirfpPNTNLVrHVERWAKVRgdKLAYRFLDfsterdgvardltwsQFGARNravgarlQQVTKPGDRVAILAPQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 408 NdpVMFMVAFYGCLLAEVIPVPIEVPltrkDAGGQ--QIGFLLGSCGIALALTSEIC-------LKGLPKTQNgeivqfk 478
Cdd:PRK07769 89 N--LDYLIAFFGALYAGRIAVPLFDP----AEPGHvgRLHAVLDDCTPSAILTTTDSaegvrkfFRARPAKER------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 479 gwPRLKWV--VTDSKYLSkppkdWQPhISPAGTEPAYIEYkTSkeGSV---MGVTVSRLAMLSQCQALSQACNYSEGETV 553
Cdd:PRK07769 156 --PRVIAVdaVPDEVGAT-----WVP-PEANEDTIAYLQY-TS--GSTripAGVQITHLNLPTNVLQVIDALEGQEGDRG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 554 VNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVMKTcPLSWVQRVHA------------------HKAKVALVKcrdlhw 615
Cdd:PRK07769 225 VSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRR-PGRWIRELARkpggtggtfsaapnfafeHAAARGLPK------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 616 ammahRDQRDVSLSSLRMLIvtDGANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAmTVAIRRPGVPGAPlpgRAI- 694
Cdd:PRK07769 298 -----DGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEA-TLFVSTTPMDEEP---TVIy 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 695 LSMNGLSYG-VIRVNTEDKNsALTVQDVGHVMPGGMMCIVKPDGLPQLcRTDEIGEICVSSRTGGMMYFGLAGVTKNTFE 773
Cdd:PRK07769 367 VDRDELNAGrFVEVPADAPN-AVAQVSAGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFQ 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 774 VI------PVTSSGSPvGDVPFIRSGLLGFVGPGSLvFVVGKMDGLLMVSGRRHNADDIVATglAVESIKTVYRGrhtgl 847
Cdd:PRK07769 445 NIlksrlsESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYT--AQEATKALRTG----- 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 848 lavpqtcqarpYLRTFplSVPSvrNPLPPdlrvarvltsfriAVFSVS---VFYD-----ERIVVVAEQRPDASEEDSFQ 919
Cdd:PRK07769 516 -----------YVAAF--SVPA--NQLPQ-------------VVFDDShagLKFDpedtsEQLVIVAERAPGAHKLDPQP 567
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|
gi 755551660 920 WMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLFLEGSL 969
Cdd:PRK07769 568 IADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1034-1551 |
7.70e-26 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 112.98 E-value: 7.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1034 LAEILQWRAQATPDHVLfmlLNAKGTTVctaSCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 1113
Cdd:COG0318 1 LADLLRRAAARHPDRPA---LVFGGRRL---TYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1114 CIPVTVrpphaqNLTATLPTVRMVVDVSKAACVLTtqtlmrllksreaaaavdvktwpaiidtddlprkrlpqlykpptp 1193
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1194 emlAYLDFSvS-TTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMEL 1272
Cdd:COG0318 103 ---ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1273 ENnlflWLATVNQYKIrdTFCSYS---VMELCtkglgnqvEVLKTRGINLSCIRTCVVVAeERPRVSLQQSFSKLFKdig 1349
Cdd:COG0318 179 ER----VLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLRLVVSGG-APLPPELLERFEERFG--- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1350 lspRAVSTTFGSrvnvaiclqgT-SGPdptTVYVDLKSLRHDRVRLVergapqslllsesGKILPGVKVVIVNPETKgPV 1428
Cdd:COG0318 241 ---VRIVEGYGL----------TeTSP---VVTVNPEDPGERRPGSV-------------GRPLPGVEVRIVDEDGR-EL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1429 GDSHLGEIWVNSPHTASGYYTiyDSETlqadhfnTRLSFGDAaqtlWARTGYLGFVRrteltaATGErhdaLYVVGALDE 1508
Cdd:COG0318 291 PPGEVGEIVVRGPNVMKGYWN--DPEA-------TAEAFRDG----WLRTGDLGRLD------EDGY----LYIVGRKKD 347
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 755551660 1509 TLELRGLRYHPIDIETSVSRvHRSIAECAVF-----TWTNLLVVVVEL 1551
Cdd:COG0318 348 MIISGGENVYPAEVEEVLAA-HPGVAEAAVVgvpdeKWGERVVAFVVL 394
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
367-971 |
1.81e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 110.09 E-value: 1.81e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 367 LTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVyPNNDPvMFMVAFYGCLLAEVIPVPIEVP--LTRKDAGGQQI 444
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLA-LG------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFGGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 445 GFLLGSCGIALALTSEICLKGLPKTQNGEivqfkgwpRLKWVVTDSKYLSKPPKDWQ-PHISPagTEPAYIEYkTSkeGS 523
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGN--------PLLHVLSHAWFKALPEADVAlPRPTP--DDIAYLQY-SS--GS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 524 V---MGVTVSRLAMLSQCQALSQ-ACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMhtiSVPYsvMKTC-----PLSW 594
Cdd:PRK09192 188 TrfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQL---SVDY--LPTRdfarrPLQW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 595 VQRVHAHKAKVALVKC--RDLHWAMMAHRDQRDVSLSSLRmlIVTDGANPWSVSSCDAFLSLFQSHGLKPEAICPCATSA 672
Cdd:PRK09192 263 LDLISRNRGTISYSPPfgYELCARRVNSKDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 673 EAmTVAIrrpgvpgaplpgrailSMNGLSYGvIRVNT------EDKNSALTVQD----------VGHVMPGGMMCIVKPD 736
Cdd:PRK09192 341 EA-TLAV----------------SFSPLGSG-IVVEEvdrdrlEYQGKAVAPGAetrrvrtfvnCGKALPGHEIEIRNEA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 737 G--LPQLcrtdEIGEICVssRTGGMM--YFGlagvTKNTFEVIPVTSsgspvgdvpFIRSGLLGFVGPGSLVfVVGKMDG 812
Cdd:PRK09192 403 GmpLPER----VVGHICV--RGPSLMsgYFR----DEESQDVLAADG---------WLDTGDLGYLLDGYLY-ITGRAKD 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 813 LLMVSGRRHNADDIvatGLAVESIktvyrgrhtgllavpqtcqarpylrtfplsvPSVRnplppdlrvarvltSFRIAVF 892
Cdd:PRK09192 463 LIIINGRNIWPQDI---EWIAEQE-------------------------------PELR--------------SGDAAAF 494
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 893 SVSVFYDERIVVVAEQRPdASEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKTPLGGIHISQTKQLFLEGSLHP 971
Cdd:PRK09192 495 SIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRTSSGKLSRAKAKKRYLSGAFAS 571
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
366-826 |
2.07e-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: 108.74 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 366 TLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNDPvmFMVAFYGCLLAEVIPVPIEVPLTRKdaggqQIG 445
Cdd:COG0318 24 RLTYAELDARARRLA-AALRALG------VGPGDRVALLLPNSPE--FVVAFLAALRAGAVVVPLNPRLTAE-----ELA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 446 FLLGSCGIALALTSEICL----KGLPKtqngeivqfkgwprlkwvvtdskylskppkdwqphispagtepayieyktske 521
Cdd:COG0318 90 YILEDSGARALVTALILYtsgtTGRPK----------------------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 522 gsvmGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMHTISVPysvmKTCPLSWVQRVHAH 601
Cdd:COG0318 117 ----GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP----RFDPERVLELIERE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 602 KA-KVALVKcrDLHWAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLSLFQShglkpeAICPCATSAEAMTVAIR 680
Cdd:COG0318 189 RVtVLFGVP--TMLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFEERFGV------RIVEGYGLTETSPVVTV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 681 RPGVPGAPLPGRailsmnglsygvirvntedknsaltvqdVGHVMPGGMMCIVKPDGLPqlCRTDEIGEICVssRTGGMM 760
Cdd:COG0318 259 NPEDPGERRPGS----------------------------VGRPLPGVEVRIVDEDGRE--LPPGEVGEIVV--RGPNVM 306
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755551660 761 --YFGLAGVTKNTFEvipvtssgspvgDvPFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDI 826
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) ... |
334-967 |
3.82e-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: 3.82e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 334 PPALESALQRWgSTQAKCPCLTGLDVTGkPVYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNDPvmF 413
Cdd:cd05906 9 PRTLLELLLRA-AERGPTKGITYIDADG-SEEFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDDNED--F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 414 MVAFYGCLLAEVIPVPIEVPLTRKDAGGQ-----QIGFLLGSCGIalaLTSEICLKGLPKtqngeivQFKGWPRLKWVVT 488
Cdd:cd05906 78 IPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELVAEFAG-------LETLSGLPGIRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 489 DSKYLSKPPKDWQPHISPAGTePAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHG 568
Cdd:cd05906 148 SIEELLDTAADHDLPQSRPDD-LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 569 MFANVMNKMHTISVPYSVMKTCPLSWVQRVHAHKAKV------ALVKCRDLhwamMAHRDQRDVSLSSLRMLIVtdGANP 642
Cdd:cd05906 227 HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLNDL----LEEIEDGTWDLSSLRYLVN--AGEA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 643 WSVSSCDAFLSLFQSHGLKPEAICPCATSAEamTVAirrpgvpgaplpgrailsmnglsyGVI---RVNTEDKNSALTVQ 719
Cdd:cd05906 301 VVAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysrSFPTYDHSQALEFV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 720 DVGHVMPGGMMCIVKPDGlpQLCRTDEIGEICVS--SRTGGmmYFGLAGVTKNTFevipvTSSGspvgdvpFIRSGLLGF 797
Cdd:cd05906 355 SLGRPIPGVSMRIVDDEG--QLLPEGEVGRLQVRgpVVTKG--YYNNPEANAEAF-----TEDG-------WFRTGDLGF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 798 VGPGSLVFvVGKMDGLLMVSGRRHNADDIVAtglAVESIKTVyrgrhtgllAVPQTCQArpylrtfplsvpSVRNPLPPD 877
Cdd:cd05906 419 LDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGV---------EPSFTAAF------------AVRDPGAET 473
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 878 LRVArvltsfriavfsvsVFYderivvvaeqrpdASEEDSFQWMSRVLQAIDSI--HQVGVYCLALVP--ANTLPKTPLG 953
Cdd:cd05906 474 EELA--------------IFF-------------VPEYDLQDALSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLG 526
|
650
....*....|....
gi 755551660 954 GIHISQTKQLFLEG 967
Cdd:cd05906 527 KIQRSKLKAAFEAG 540
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
365-827 |
2.20e-23 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 105.09 E-value: 2.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 365 YTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVpltrkDAGGQQI 444
Cdd:pfam00501 20 RRLTYRELDERANRLAAGLR-ALG------VGKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPLNP-----RLPAEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 445 GFLLGSCGIALALTSEI--------CLKGLPKTQNGEIVQFKGWPRLKWVVTDSKYLSKPPKdwqPHISPAGTEPAYIEY 516
Cdd:pfam00501 86 AYILEDSGAKVLITDDAlkleelleALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPP---PPPPPDPDDLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 517 kTS------KegsvmGVTVSRLAMLSQCQALSQAC----NYSEGETVVNVLDFKKDAGLWHGMFANVMNKMhTISVPYSV 586
Cdd:pfam00501 163 -TSgttgkpK-----GVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA-TVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 587 MKTCPLSWVQRVHAHKAKV-----ALVKcrdlhwAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLSLFqshglk 661
Cdd:pfam00501 236 PALDPAALLELIERYKVTVlygvpTLLN------MLLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 662 peaicpcatsaeamtvairrpgvpgaplpGRAILSMNGLS--YGVIRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGLp 739
Cdd:pfam00501 302 -----------------------------GGALVNGYGLTetTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETG- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 740 QLCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFevipvTSSGspvgdvpFIRSGLLGFVGPgslvfvvgkmDGLLMVSGR 819
Cdd:pfam00501 352 EPVPPGEPGELCVRGPGVMKGYLNDPELTAEAF-----DEDG-------WYRTGDLGRRDE----------DGYLEIVGR 409
|
....*...
gi 755551660 820 rhnADDIV 827
Cdd:pfam00501 410 ---KKDQI 414
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
366-955 |
2.30e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 106.95 E-value: 2.30e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 366 TLTYGKLWSRSLKLAYTLlNKLGTknepvlkPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLTRkdAGGQQIG 445
Cdd:PRK05850 35 TLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQG--LEYIVAFLGALQAGLIAVPLSVPQGG--AHDERVS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 446 FLLGSCGIALALT-SEIClkglpktqnGEIVQF----KGWPRLKWVVTDSKYLSKPPKdwqPHISPAG-TEPAYIEYkTS 519
Cdd:PRK05850 103 AVLRDTSPSVVLTtSAVV---------DDVTEYvapqPGQSAPPVIEVDLLDLDSPRG---SDARPRDlPSTAYLQY-TS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 520 keGSV---MGVTVSRLAMLSQC-QALSQACNYSEGE-----TVVNVLDFKKDAGLWHGMFANVMNKMHTI-SVPYSVMKT 589
Cdd:PRK05850 170 --GSTrtpAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSWLPFYHDMGLVLGVCAPILGGCPAVlTSPVAFLQR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 590 cPLSWVQRV----HAHKA------KVALVKCRDlhwAMMAHRDQRDVslsslrmLIVTDGANPWSVSSCDAFLSLFQSHG 659
Cdd:PRK05850 248 -PARWMQLLasnpHAFSAapnfafELAVRKTSD---DDMAGLDLGGV-------LGIISGSERVHPATLKRFADRFAPFN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 660 LKPEAICPCATSAEAMT-VAIRRPGVPgaplPGRAILSMNGLSYGVIRVNTEDKNSALtvqdVGHVMP-GGMMCIVKPDG 737
Cdd:PRK05850 317 LRETAIRPSYGLAEATVyVATREPGQP----PESVRFDYEKLSAGHAKRCETGGGTPL----VSYGSPrSPTVRIVDPDT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 738 LPQlCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVT-SSGSPVGdvPFIRSGLLGFVGPGSLvFVVGKMDGLLMV 816
Cdd:PRK05850 389 CIE-CPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATLVDpSPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 817 SGRRHNADDIVATglavesIKTVYRGrhtgllavpqtcqarpylrtfplsvpsvrnplppdlrvarvltsfRIAVFSVSV 896
Cdd:PRK05850 465 DGRNHYPDDIEAT------IQEITGG---------------------------------------------RVAAISVPD 493
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551660 897 FYDERIVVVAE-QRPDASEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGI 955
Cdd:PRK05850 494 DGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1068-1548 |
6.87e-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: 6.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTAtlPTVRMVVDVSK---AA 1144
Cdd:cd05906 44 DLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPN--ARLRKLRHIWQllgSP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1145 CVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPrkRLPQLYkPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCR 1224
Cdd:cd05906 121 VVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTA--ADHDLP-QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1225 AiKLQCELYSSRQIA---ICLDPYCGLGFAlwCLCSVYSGHQSVLIPPMELENNLFLWLATVNQYKIRDTFCSYSvmeLC 1301
Cdd:cd05906 198 G-KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1302 TKgLGNQVEVLKTRGINLSCIRtCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGSRVNVAIClqgtsgpdptTVY 1381
Cdd:cd05906 272 AL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCSGV----------IYS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1382 VDLKSLRHD-RVRLVERGAPqslllsesgkiLPGVKVVIVNPETKGpVGDSHLGEIWVNSPHTASGYytiYDSETLQADH 1460
Cdd:cd05906 340 RSFPTYDHSqALEFVSLGRP-----------IPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGY---YNNPEANAEA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1461 FntrLSFGdaaqtlWARTGYLGFVRRTELTaATGERHDALYVvgaldetlelRGLRYHPIDIETSVSRV----HRSIAEC 1536
Cdd:cd05906 405 F---TEDG------WFRTGDLGFLDNGNLT-ITGRTKDTIIV----------NGVNYYSHEIEAAVEEVpgvePSFTAAF 464
|
490
....*....|....*
gi 755551660 1537 AVF---TWTNLLVVV 1548
Cdd:cd05906 465 AVRdpgAETEELAIF 479
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1089-1527 |
2.59e-21 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 100.59 E-value: 2.59e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1089 GDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPP----HAQNLTATL----PTVrmvvdvskaacVLTTQTLMRLLksRE 1160
Cdd:PRK12476 92 GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV-----------VLTTTAAAEAV--EG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1161 AAAAVDVKTWPAIIDTDDLPrKRLPQLYKPPTPEM--LAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSsRQI 1238
Cdd:PRK12476 159 FLRNLPRLRRPRVIAIDAIP-DSAGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLD-RNT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1239 AIC--LDPYCGLGFALWCLCSVYSGHqSVLIPPMELENNLFLWL-ATVNQYKIRDTFCSYS--VMELCT-KGLGNQVEvl 1312
Cdd:PRK12476 237 HGVswLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWIkALSEGSRTGRVVTAAPnfAYEWAAqRGLPAEGD-- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1313 ktrGINLSciRTCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGsrVNVAICLQGTSGPD--PTTVYVDLKSLRHD 1390
Cdd:PRK12476 314 ---DIDLS--NVVLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG--IAEATLFVATIAPDaePSVVYLDREQLGAG 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1391 RVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTI-YDSETLQADHFNTRLSFGD 1469
Cdd:PRK12476 387 RAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRpEETERTFGAKLQSRLAEGS 466
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755551660 1470 -----AAQTLWARTGYLGFVRRTEltaatgerhdaLYVVGALDETLELRGLRYHPIDIETSVS 1527
Cdd:PRK12476 467 hadgaADDGTWLRTGDLGVYLDGE-----------LYITGRIADLIVIDGRNHYPQDIEATVA 518
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1089-1527 |
6.79e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 99.42 E-value: 6.79e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1089 GDNVVLLYPPGIELIAAFYGCLYAGCIPVTV----RPPHAQNLTAtlptvrmVVDVSKAACVLTT----QTLMRLLKSRE 1160
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHA-------VLDDCTPSAILTTtdsaEGVRKFFRARP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1161 AaaavdvKTWPAIIDTDDLPRKrLPQLYKPPTP--EMLAYLDFSVSTTGMLTGVKMSHSAV--NAL--CRAIKLQcelYS 1234
Cdd:PRK07769 152 A------KERPRVIAVDAVPDE-VGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLptNVLqvIDALEGQ---EG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1235 SRQIAiCLDPYCGLGFaLWCLCSVYSGHQSVLIPPMELENNLFLW---LATVNQykirDTFCSYSV-----MELCT-KGL 1305
Cdd:PRK07769 222 DRGVS-WLPFFHDMGL-ITVLLPALLGHYITFMSPAAFVRRPGRWireLARKPG----GTGGTFSAapnfaFEHAAaRGL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1306 GNQVEvlktRGINLSCIRtCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGsrVNVAICLQGTSGPD--PTTVYVD 1383
Cdd:PRK07769 296 PKDGE----PPLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYG--MAEATLFVSTTPMDeePTVIYVD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1384 LKSLRHDRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTIYDsETLQADH--F 1461
Cdd:PRK07769 369 RDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPE-ETAATFQniL 447
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1462 NTRLS----FGDAAQTLWARTGYLGfvrrtelTAATGErhdaLYVVGALDETLELRGLRYHPIDIETSVS 1527
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 ... |
1068-1539 |
3.77e-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: 95.74 E-value: 3.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnlTATLPTVRMVVDVSKAACVL 1147
Cdd:cd05911 15 QLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANP------IYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1148 TT-QTLMRLLKSREAAAAVD--------VKTWPAIIDTDDLPRKRLPQLYKPP---TPEMLAYLDFSVSTTGMLTGVKMS 1215
Cdd:cd05911 88 TDpDGLEKVKEAAKELGPKDkiivlddkPDGVLSIEDLLSPTLGEEDEDLPPPlkdGKDDTAAILYSSGTTGLPKGVCLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1216 HS---AVNALCRAIKLQCELYSSRQIA-ICLDPYCGLgfaLWCLCSVYSGHQSVLIPPMELEnnlfLWLATVNQYKIRDT 1291
Cdd:cd05911 168 HRnliANLSQVQTFLYGNDGSNDVILGfLPLYHIYGL---FTTLASLLNGATVIIMPKFDSE----LFLDLIEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1292 FCSYSVMELctkgLGNQVEVLKtrgINLSCIRTCVVVAEerprvSLQQSFSKLFKdiglspravsttfgSRVNVAICLQG 1371
Cdd:cd05911 241 YLVPPIAAA----LAKSPLLDK---YDLSSLRVILSGGA-----PLSKELQELLA--------------KRFPNATIKQG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1372 -----TSGPDPTTVYVDLKSlrhdrvrlverGApqslllseSGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASG 1446
Cdd:cd05911 295 ygmteTGGILTVNPDGDDKP-----------GS--------VGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1447 YYtiydsetlqadhfntrlsfGDAAQTL-------WARTGYLGFVRRTELtaatgerhdaLYVVGALDETLELRGLRYHP 1519
Cdd:cd05911 356 YY-------------------NNPEATKetfdedgWLHTGDIGYFDEDGY----------LYIVDRKKELIKYKGFQVAP 406
|
490 500
....*....|....*....|
gi 755551660 1520 IDIEtSVSRVHRSIAECAVF 1539
Cdd:cd05911 407 AELE-AVLLEHPGVADAAVI 425
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1068-1538 |
2.38e-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: 2.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVtvrPphaqnLTATLPT--VRMVVDVSKAAC 1145
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYV---P-----LDPAYPAerLAFILEDAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1146 VLTTQTLmRLLKSREAAAAVDVKTWPAIIDTDDLPrkrLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 1225
Cdd:TIGR01733 76 LLTDSAL-ASRLAGLVLPVILLDPLELAALDDAPA---PPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1226 IKlQCELYSSRQIAICLDPYCGLGFA---LWCLcsvYSGHQSVLIPPMELENNLFLWLATVNQYKIRDTFCSYSVMELCt 1302
Cdd:TIGR01733 152 LA-RRYGLDPDDRVLQFASLSFDASVeeiFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1303 kglgnqvevLKTRGINLSCIRTCVVVAEErprvslqqsfsklfkdigLSPRAVSTTFGSRVNVAIClqGTSGPDPTTVYV 1382
Cdd:TIGR01733 227 ---------AAALPPALASLRLVILGGEA------------------LTPALVDRWRARGPGARLI--NLYGPTETTVWS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1383 DlkslrhdrVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHFN 1462
Cdd:TIGR01733 278 T--------ATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---LNRPELTAERFV 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755551660 1463 TRLsFGDAAQTLWARTGYLgfVRRteltaatgeRHD-ALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECAV 1538
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 ... |
1068-1541 |
1.92e-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: 1.92e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVrpphaqNLTATLPTVRMVVDVSKAACVL 1147
Cdd:cd05959 34 ELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV------NTLLTPDDYAYYLEDSRARVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1148 TTQTLMRLLKSREAAAAVDVKT---------WPAIIDTDDLPRKRLPQLYKPPT-PEMLAYLDFSVSTTGMLTGVKMSHS 1217
Cdd:cd05959 107 VSGELAPVLAAALTKSEHTLVVlivsggagpEAGALLLAELVAAEAEQLKPAAThADDPAFWLYSSGSTGRPKGVVHLHA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1218 AvnalcraIKLQCELYSSRQIAICLDPYC----------GLGFALWCLCSVysGHQSVLIPPMELENNLFlwlATVNQYK 1287
Cdd:cd05959 187 D-------IYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMPERPTPAAVF---KRIRRYR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1288 iRDTFcsYSVMELCTKGLGNqvEVLKTRgiNLSCIRTCVVVAEERPRvSLQQSFSKLFK-DIglspravsttfgsrvnva 1366
Cdd:cd05959 255 -PTVF--FGVPTLYAAMLAA--PNLPSR--DLSSLRLCVSAGEALPA-EVGERWKARFGlDI------------------ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1367 icLQGTSGPDPTTVYVdlkSLRHDRVRLverGApqslllseSGKILPGVKVVIVNpETKGPVGDSHLGEIWVNSPHTASG 1446
Cdd:cd05959 309 --LDGIGSTEMLHIFL---SNRPGRVRY---GT--------TGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATM 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1447 YYTIYDSetlqadhfnTRLSFgdaaQTLWARTGYlGFVRRTELTaatgerhdaLYVVGALDETLELRGLRYHPIDIEtSV 1526
Cdd:cd05959 372 YWNNRDK---------TRDTF----QGEWTRTGD-KYVRDDDGF---------YTYAGRADDMLKVSGIWVSPFEVE-SA 427
|
490
....*....|....*
gi 755551660 1527 SRVHRSIAECAVFTW 1541
Cdd:cd05959 428 LVQHPAVLEAAVVGV 442
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1068-1573 |
2.66e-16 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 84.29 E-value: 2.66e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHA-QNLTATLPTVRMVVDVSKAACV 1146
Cdd:PRK09192 54 TLRARAEAGARRLLALG-LKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGfGGRESYIAQLRGMLASAQPAAI 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1147 LTTQTLMRLLKS-REAAAAVDVKTWpAIIDTDDLPRKRLPqlykPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 1225
Cdd:PRK09192 133 ITPDELLPWVNEaTHGNPLLHVLSH-AWFKALPEADVALP----RPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1226 IKLQ-CELYSSRQIAICLDPYCGLGFaLWCLCSVYSGHQSV-LIPPMELENNLFLWLATVNqyKIRDTFcSYSV---MEL 1300
Cdd:PRK09192 208 ISHDgLKVRPGDRCVSWLPFYHDMGL-VGFLLTPVATQLSVdYLPTRDFARRPLQWLDLIS--RNRGTI-SYSPpfgYEL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1301 CTKGLGNQVEVlktrGINLSCIRTCVVVAEE-RPRVslQQSFSKLFKDIGLSPRAVSTTFG-SRVNVAIclqgtSGPDPT 1378
Cdd:PRK09192 284 CARRVNSKDLA----ELDLSCWRVAGIGADMiRPDV--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAV-----SFSPLG 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1379 TvyvDLKSLRHDRVRLVERGA-----PQSLLLSE---SGKILPGVKVVIVNpETKGPVGDSHLGEIWVNSPHTASGYYTi 1450
Cdd:PRK09192 353 S---GIVVEEVDRDRLEYQGKavapgAETRRVRTfvnCGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFR- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1451 yDSETLQAdhfntrlsfgdAAQTLWARTGYLGFVrrteltaATGErhdaLYVVGALDETLELRGLRYHPIDIETSVSRV- 1529
Cdd:PRK09192 428 -DEESQDV-----------LAADGWLDTGDLGYL-------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIAEQEp 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 755551660 1530 ---HRSIAECAVFTWTNLLVVVVELC--GSEQEALDLVPLVTNVVLEEH 1573
Cdd:PRK09192 485 elrSGDAAAFSIAQENGEKIVLLVQCriSDEERRGQLIHALAALVRSEF 533
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
357-971 |
1.12e-15 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 82.48 E-value: 1.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 357 LDVTGKP---VYTLTYGKLWSRslklaytlLNKLGTKNEPVLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPI--- 430
Cdd:PRK12476 56 LDHSHSAagcAVELTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLfap 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 431 EVP--LTRKDAggqqigfLLGSCGIALALTSeiclkglpkTQNGEIVQfkgwprlkwvvtdsKYLSKPPKDWQPHI---- 504
Cdd:PRK12476 126 ELPghAERLDT-------ALRDAEPTVVLTT---------TAAAEAVE--------------GFLRNLPRLRRPRViaid 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 505 -----SPAGTEP--------AYIEYKTSKEGSVMGVTVS-RLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMF 570
Cdd:PRK12476 176 aipdsAGESFVPveldtddvSHLQYTSGSTRPPVGVEIThRAVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 571 ANVMNKMHTISVPYSVMKTcPLSWVQRVHAHKAKVALVKCR-DLHWAMMAHR----DQRDVSLSSLRMLIvtdGANPWSV 645
Cdd:PRK12476 256 PAVYGGHSTLMSPTAFVRR-PQRWIKALSEGSRTGRVVTAApNFAYEWAAQRglpaEGDDIDLSNVVLII---GSEPVSI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 646 SSCDAFLSLFQSHGLKPEAICPCATSAEA-MTVAIRRPgvpgAPLPGRAILSMNGLSYG-VIRVNTEDKNSALTVQdVGH 723
Cdd:PRK12476 332 DAVTTFNKAFAPYGLPRTAFKPSYGIAEAtLFVATIAP----DAEPSVVYLDREQLGAGrAVRVAADAPNAVAHVS-CGQ 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 724 VMPGGMMCIVKPDGLPQLcRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEV-----IPVTS--SGSPVGDVpFIRSGLLG 796
Cdd:PRK12476 407 VARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGShaDGAADDGT-WLRTGDLG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 797 FVGPGSLvFVVGKMDGLLMVSGRRHNADDIVATglAVESIKTVYRGRhtgllavpqtcqarpylrtfplsvpsvrnplpp 876
Cdd:PRK12476 485 VYLDGEL-YITGRIADLIVIDGRNHYPQDIEAT--VAEASPMVRRGY--------------------------------- 528
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 877 dlrvarvltsfrIAVFSVSVFYDERIVVVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIH 956
Cdd:PRK12476 529 ------------VTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLA 596
|
650
....*....|....*
gi 755551660 957 ISQTKQLFLEGSLHP 971
Cdd:PRK12476 597 RRACRAQYLDGRLGV 611
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
384-836 |
1.84e-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: 1.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 384 LNKLGTKNEPVLKPGDRVALVYPNNDPvmFMVAFYGCLLAEVIPVPIEVpltrkdagGQQIGFLLGScgialaltseicl 463
Cdd:cd05908 26 LGYLGALQELGIKPGQEVVFQITHNNK--FLYLFWACLLGGMIAVPVSI--------GSNEEHKLKL------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 464 kglpktqngeivqFKGWPRLK--WVVTDSKYLSKPPKdwqphispagtEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQAL 541
Cdd:cd05908 83 -------------NKVWNTLKnpYLITEEEVLCELAD-----------ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 542 SQACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVMKTCPLSWVQRVHAHKAKValVKCRDLHWAMMAHR 621
Cdd:cd05908 139 LNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATI--VSSPNFGYKYFLKT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 622 ----DQRDVSLSSLRMLIvtDGANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAmTVAIRRP--GVPGAPLpgraIL 695
Cdd:cd05908 217 lkpeKANDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA-SVGASLPkaQSPFKTI----TL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 696 SMNGLSYGVIRVNTEDKNS-ALTVQDVGHVMPGGMMCIVKPD--GLPQlcrtDEIGEICVSSRTGGMMYFGLAGVTKNTF 772
Cdd:cd05908 290 GRRHVTHGEPEPEVDKKDSeCLTFVEVGKPIDETDIRICDEDnkILPD----GYIGHIQIRGKNVTPGYYNNPEATAKVF 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551660 773 evipvTSSGspvgdvpFIRSGLLGFVGPGSLVfVVGKMDGLLMVSGRRHNADDIVATGLAVESI 836
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 ... |
1034-1448 |
1.03e-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: 72.21 E-value: 1.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1034 LAEILQWRAQATPDHVLFMLLNAKGTTVctasclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 1113
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYR------ELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1114 CIPVTVRPphaqnltatlptvrmvvdvskaacVLTTQTLMRLLKSREAAAAVDVKTWpaiidTDDLPRKRLPQLYKPPTP 1193
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSF-----TDLLAAGAPLGERVALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1194 EMLAYLDFSVSTTGMLTGVKMSHSAV--NAL-CRAIkLQcELYSSRQIAICLDP-YCGLGFALWCLCSVYSGHQSVLIP- 1268
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLvaNALqIKAW-LE-DLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLIPr 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1269 --PMELennlflwLATVNQYKIrDTFCS----YSvmelctkGLGNQVEVLKtrgINLSCIRTCVvvaeerprvslqqsfs 1342
Cdd:cd05936 203 frPIGV-------LKEIRKHRV-TIFPGvptmYI-------ALLNAPEFKK---RDFSSLRLCI---------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1343 klfkdiglspravsttfgsrvnvaiclqgtSGPDPTTVYVDLKSLRHDRVRLVE-RGapqsllLSES------------- 1408
Cdd:cd05936 249 ------------------------------SGGAPLPVEVAERFEELTGVPIVEgYG------LTETspvvavnpldgpr 292
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 755551660 1409 -----GKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYY 1448
Cdd:cd05936 293 kpgsiGIPLPGTEVKIVDDDGE-ELPPGEVGELWVRGPQVMKGYW 336
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1042-1564 |
4.30e-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: 70.35 E-value: 4.30e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1042 AQATPDHVLFMllnAKGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGC--IPVTV 1119
Cdd:cd05945 1 AAANPDRPAVV---EGGRTLTYR---ELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1120 RPPHAQnltatlptVRMVVDVSKAACVlttqtlmrllksreaaaavdvktwpaIIDTDDlprkrlpqlykpptpemLAYL 1199
Cdd:cd05945 74 SSPAER--------IREILDAAKPALL--------------------------IADGDD-----------------NAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1200 DFSVSTTGMLTGVKMSHSAVNALCRAIkLQCELYSSRQIAIC----------LDPYCGL--GFALWCLcsvysghqsvli 1267
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNqapfsfdlsvMDLYPALasGATLVPV------------ 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1268 pPMELENNLFLWLATVNQYKIRDTFCSYSVMELCTKGLGNQVEVLKTrginlscIRTCVVVAEERPRVSLQQSFSKLfkd 1347
Cdd:cd05945 170 -PRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPS-------LRHFLFCGEVLPHKTARALQQRF--- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1348 iglsPRA-VSTTFGS-RVNVAIclqgtsgpdpTTVYVDLKSL-RHDRVRLvergapqslllsesGKILPGVKVVIVNPET 1424
Cdd:cd05945 239 ----PDArIYNTYGPtEATVAV----------TYIEVTPEVLdGYDRLPI--------------GYAKPGAKLVILDEDG 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1425 KgPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHFntrlsFGDAAQTlWARTGYLGFVrrteltAATGErhdaLYVVG 1504
Cdd:cd05945 291 R-PVPPGEKGELVISGPSVSKGY---LNNPEKTAAAF-----FPDEGQR-AYRTGDLVRL------EADGL----LFYRG 350
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551660 1505 ALDETLELRGLRYHPIDIETSVSRVHrSIAECAVFTWTNL-----LVVVVELCGSEqEALDLVPL 1564
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 ... |
1068-1538 |
6.58e-12 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 69.96 E-value: 6.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLgDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnlTATLPTVRMVVDVSKAACVL 1147
Cdd:cd05904 37 ELERRVRRLAAGL-AKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1148 TTQTLmrLLKSREAAAAV----DVKTWPAIIDTDDLPRKRLPqlykPPTPEM----LAYLDFSVSTTGMLTGVKMSH-SA 1218
Cdd:cd05904 110 TTAEL--AEKLASLALPVvlldSAEFDSLSFSDLLFEADEAE----PPVVVIkqddVAALLYSSGTTGRSKGVMLTHrNL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1219 VNALCRAIKLQCELYSSRQIAICLDPYCGL-GFALWCLCSVYSGHQSVLIPPMELENnlflWLATVNQYKIRDTFCSYSV 1297
Cdd:cd05904 184 IAMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERYKVTHLPVVPPI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1298 MelctKGLGNQVEVLKtrginlscirtcvvvaeeRPRVSLQQSFSklfkdiGLSP--RAVSTTFGSRVNVAICLQG---- 1371
Cdd:cd05904 260 V----LALVKSPIVDK------------------YDLSSLRQIMS------GAAPlgKELIEAFRAKFPNVDLGQGygmt 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1372 TSGPDPTTVYVDLKSLRHdrvrlvergapqsllLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYytiy 1451
Cdd:cd05904 312 ESTGVVAMCFAPEKDRAK---------------YGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGY---- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1452 dsetlqadhfntrlsFGDAAQTL-------WARTGYLGFVRrteltaATGErhdaLYVVGALDETLELRGLRYHPIDIEt 1524
Cdd:cd05904 373 ---------------LNNPEATAatidkegWLHTGDLCYID------EDGY----LFIVDRLKELIKYKGFQVAPAELE- 426
|
490
....*....|....
gi 755551660 1525 SVSRVHRSIAECAV 1538
Cdd:cd05904 427 ALLLSHPEILDAAV 440
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1068-1543 |
9.05e-12 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 69.09 E-value: 9.05e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltaTLPTVRM--VVDVSKAAC 1145
Cdd:cd05930 17 ELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDP--------SYPAERLayILEDSGAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1146 VLTtqtlmrllksreaaaavdvktwpaiidtddlprkrlpqlykppTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 1225
Cdd:cd05930 88 VLT-------------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1226 ikLQCELYSSR-----QIAicldpycGLGF--ALWCL-CSVYSGHQSVLIPPmELENNLFLWLATVNQYKIRDTFCSYSV 1297
Cdd:cd05930 125 --MQEAYPLTPgdrvlQFT-------SFSFdvSVWEIfGALLAGATLVVLPE-EVRKDPEALADLLAEEGITVLHLTPSL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1298 MELCTKGLGNQvevlktrgiNLSCIRTcVVVAEERPRVSLQQSFSKLFKDIGLspravsttfgsrVNVaiclqgtSGPDP 1377
Cdd:cd05930 195 LRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELLPGARL------------VNL-------YGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1378 TTVYVDLKSLRHDRVRlvERGAPqslllseSGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYytiYDSETLQ 1457
Cdd:cd05930 246 ATVDATYYRVPPDDEE--DGRVP-------IGRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLARGY---LNRPELT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1458 ADHFnTRLSFGDaaqtlWA---RTGYLgfVRRTEltaatgerHDALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIA 1534
Cdd:cd05930 313 AERF-VPNPFGP-----GErmyRTGDL--VRWLP--------DGNLEFLGRIDDQVKIRGYRIELGEIEAALLA-HPGVR 375
|
....*....
gi 755551660 1535 ECAVFTWTN 1543
Cdd:cd05930 376 EAAVVARED 384
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
334-999 |
9.95e-11 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 67.12 E-value: 9.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 334 PPALESALQRWGSTQAKCPCLTGLDVTGKPVYTLTYGKLWSRSLKLAYTLLNKLGtknepvlkPGDRVALVYPNNdpVMF 413
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS--------FGDRAVLLFPSG--PDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 414 MVAFYGCLLAEVIPVPIEVPLTRKDAGGQQIGFLLGSCGIALALTSEICLKGLpktQNGEIVQFKGWPRLKWVVTdskYL 493
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL---LQMEELAAANAPELLCVDT---LD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 494 SKPPKDWQ-PHISPagTEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQ--ACNYSEGETVVNVLDFKKDAGLWHGMF 570
Cdd:PRK05691 152 PALAEAWQePALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHgfGIDLNPDDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 571 ANVMNkmhtiSVPYSVMKTC-----PLSWVQRVHAHKAKVAlvKCRDLHWAMMAHRdqrdVSLSSLRML------IVTDG 639
Cdd:PRK05691 230 QPIFS-----GVPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER----VSESALERLdlsrwrVAYSG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 640 ANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAMTVairrpgVPGAPlPGRAILSMNgLSYGVIRVNTEDKNSALTVQ 719
Cdd:PRK05691 299 SEPIRQDSLERFAEKFAACGFDPDSFFASYGLAEATLF------VSGGR-RGQGIPALE-LDAEALARNRAEPGTGSVLM 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 720 DVGHVMPGGMMCIVKPDGLPQLcRTDEIGEICVSSRTGGMMYFGLAGVTKNTFevipVTSSGSpvgdvPFIRSGLLGFVG 799
Cdd:PRK05691 371 SCGRSQPGHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGDLGFLR 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 800 PGSLvFVVGKMDGLLMVSGrrHNaddivatglavesiktVYrgrhtgllavPQTCQarpylRTFPLSVPSVRNPlppdlr 879
Cdd:PRK05691 441 DGEL-FVTGRLKDMLIVRG--HN----------------LY----------PQDIE-----KTVEREVEVVRKG------ 480
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 880 varvltsfRIAVFSVSVFYDERIVVVAE-----QRPDASEEdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGG 954
Cdd:PRK05691 481 --------RVAAFAVNHQGEEGIGIAAEisrsvQKILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGK 548
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 755551660 955 IHISQTKQLFLEGSLhpcnilmcphTCVTNLPKPRQKQPGVGPAS 999
Cdd:PRK05691 549 LQRSACRLRLADGSL----------DSYALFPALQAVEAAQTAAS 583
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1193-1523 |
1.78e-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: 1.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1193 PEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMEL 1272
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1273 ENNLFLWLATVNQYKIRDTFCSysvmELCTKGLGNQVEVLKTRGINLSCIRTCVVVAEerP-RVSLQQSFSKLFKDIGLS 1351
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSP----NFGYKYFLKTLKPEKANDWDLSSIRMILNGAE--PiDYELCHEFLDHMSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1352 PRAVSTTFG-SRVNVAICLQGTSGPdPTTVYVDLKSLRH-DRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGpVG 1429
Cdd:cd05908 259 RNAILPVYGlAEASVGASLPKAQSP-FKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1430 DSHLGEIWVNSPHTASGYYTiydsetlqadhfNTRLSFGDAAQTLWARTGYLGFVRRTELTaATGERHDALYVvgaldet 1509
Cdd:cd05908 337 DGYIGHIQIRGKNVTPGYYN------------NPEATAKVFTDDGWLKTGDLGFIRNGRLV-ITGREKDIIFV------- 396
|
330
....*....|....
gi 755551660 1510 lelRGLRYHPIDIE 1523
Cdd:cd05908 397 ---NGQNVYPHDIE 407
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1068-1538 |
6.81e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 63.63 E-value: 6.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGHLNAgdnVVLLYPPGIELIAAFYGCLYAG----CIPVTVRPPHAQNLTATLPTVRMVVDVSKa 1143
Cdd:PRK05851 36 EVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1144 acVLTTQTLMRLLKSREAAAAV-DVKTWPaiidtddlpRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNAL 1222
Cdd:PRK05851 112 --VLSHGSHLERLRAVDSSVTVhDLATAA---------HTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1223 CRAIKLQCELYSSRQIAICLDP-YCGLGFAlWCLCSVYSGHQSVLIPPMELENNLFLWLATVNQYkiRDTFC-----SYS 1296
Cdd:PRK05851 181 LRGLNARVGLDAATDVGCSWLPlYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDS--RATLTaapnfAYN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1297 VmelctkgLGNQVEvlKTRGINLSCIRTCVVVAEERPRVSLQQsFSKLFKDIGLSPRAVSTTFGsrVNVAIClqGTSGPD 1376
Cdd:PRK05851 258 L-------IGKYAR--RVSDVDLGALRVALNGGEPVDCDGFER-FATAMAPFGFDAGAAAPSYG--LAESTC--AVTVPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1377 PTTvyvdlkSLRHDRVRLVERGAPQSLLLSesGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYytiYDSETL 1456
Cdd:PRK05851 324 PGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY---LGQAPI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1457 QADHfntrlsfgdaaqtlWARTGYLGFvrrteLTAatgerhDALYVVGALDETLELRGLRYHPIDIETSVSRVhRSIAEC 1536
Cdd:PRK05851 393 DPDD--------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERVAAQV-RGVREG 446
|
..
gi 755551660 1537 AV 1538
Cdd:PRK05851 447 AV 448
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1068-1555 |
6.99e-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: 6.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPH-AQNLtatlptvRMVVDVSKAACV 1146
Cdd:cd12116 17 ELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYpADRL-------RYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1147 LTTQTLMrllksreAAAAVDVKTWPAIIDTDDLPRKRLPqlyKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAI 1226
Cdd:cd12116 89 LTDDALP-------DRLPAGLPVLLLALAAAAAAPAAPR---TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1227 KLQCELYSSRQIaICLDPYCglgFALwclcsvysghqSVLippmelenNLFLWLATVNQYKIRDTFCSYSVMELctkglg 1306
Cdd:cd12116 159 RERLGLGPGDRL-LAVTTYA---FDI-----------SLL--------ELLLPLLAGARVVIAPRETQRDPEAL------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1307 nqVEVLKTRGINL-----SCIRTcVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTfGSRVNVaiclqgtSGPDPTTVY 1381
Cdd:cd12116 210 --ARLIEAHSITVmqatpATWRM-LLDAGWQGRAGLTALCGGEALPPDLAARLLSRV-GSLWNL-------YGPTETTIW 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1382 vdlkSLRHdRVRLVERGAPqslllseSGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHF 1461
Cdd:cd12116 279 ----STAA-RVTAAAGPIP-------IGRPLANTQVYVLDAALR-PVPPGVPGELYIGGDGVAQGY---LGRPALTAERF 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1462 nTRLSFGDAAQTLWaRTGYLgfVRRteltaatgERHDALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECAVFTW 1541
Cdd:cd12116 343 -VPDPFAGPGSRLY-RTGDL--VRR--------RADGRLEYLGRADGQVKIRGHRIELGEIEAALAA-HPGVAQAAVVVR 409
|
490
....*....|....*...
gi 755551660 1542 TN----LLVVVVELCGSE 1555
Cdd:cd12116 410 EDggdrRLVAYVVLKAGA 427
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1042-1237 |
1.46e-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: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1042 AQATPDHVLfmlLNAKGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG--CIPVTV 1119
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGaaYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1120 RPPhAQNLTATLPTVRMVvdvskaaCVLTTQTLM-RLLKSREAAAAVDVKTWPAIIDTDDLPrkrlpqlykPPTPEMLAY 1198
Cdd:cd17651 78 AYP-AERLAFMLADAGPV-------LVLTHPALAgELAVELVAVTLLDQPGAAAGADAEPDP---------ALDADDLAY 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 755551660 1199 LDFSVSTTGMLTGVKMSHSAVNALCRAiklQCELYSSRQ 1237
Cdd:cd17651 141 VIYTSGSTGRPKGVVMPHRSLANLVAW---QARASSLGP 176
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
367-837 |
3.65e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.82 E-value: 3.65e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 367 LTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNDPVMfmVAFYGCLLA--EVIPVPIEVPltrkdagGQQI 444
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLR-ARG------VGPEVRVAIAAERSFELV--VALLAVLKAggAYVPLDPNYP-------AERL 2092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 445 GFLLGSCGIALALTSEICLKGLPKTQngeivqfkGWPRLKwvVTDSKYLSKPPkDWQPHISPAGTEPAYIEYKTSKEGSV 524
Cdd:PRK12316 2093 AYMLEDSGAALLLTQRHLLERLPLPA--------GVARLP--LDRDAEWADYP-DTAPAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 525 MGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWhGMFANVMNKMHTISVPYSVMKtcPLSWVQRVHAHkaK 604
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDELWD--PEQLYDEMERH--G 2236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 605 VALVKCRDLHWAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLS------LFQSHGLKPEAICPCATSAEAmTVA 678
Cdd:PRK12316 2237 VTILDFPPVYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEalrpvyLFNGYGPTEAVVTPLLWKCRP-QDP 2313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 679 IRRPGVP-GAPLPGRAilsmnglsygvirvntedknsaltvqdvGHVMPGGMmcivkpdglpQLCRTDEIGEICVSSRTG 757
Cdd:PRK12316 2314 CGAAYVPiGRALGNRR----------------------------AYILDADL----------NLLAPGMAGELYLGGEGL 2355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 758 GMMYFGLAGVTKNTFEVIPVTSSGSPVgdvpfIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIK 837
Cdd:PRK12316 2356 ARGYLNRPGLTAERFVPDPFSASGERL-----YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVR 2430
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1034-1537 |
6.48e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 57.22 E-value: 6.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1034 LAEILQWRAQATPDHVLFMLLNAKGTTV----CTASCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGC 1109
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVAVPGGRGADGklayDELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1110 LYAGCIPVTVRPPHA-QNLTATLPTVR--MVVDVSKAacvlttqTLMRLL-----KSREAAAAVDVKTWPAIIDTDDLPR 1181
Cdd:PRK09274 87 FKAGAVPVLVDPGMGiKNLKQCLAEAQpdAFIGIPKA-------HLARRLfgwgkPSVRRLVTVGGRLLWGGTTLATLLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1182 KRLP---QLYKPPTPEMLAYLdFSVSTTGMLTGVKMSHSAVNALCRAIKlqcELYSSRQIAICL---------DPYCGlg 1249
Cdd:PRK09274 160 DGAAapfPMADLAPDDMAAIL-FTSGSTGTPKGVVYTHGMFEAQIEALR---EDYGIEPGEIDLptfplfalfGPALG-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1250 falwcLCSVysghqsvlIPPMELE-----NNLFLWlATVNQYKIRDTFCSYSVMELctkgLGNQvevLKTRGINLSCIRT 1324
Cdd:PRK09274 234 -----MTSV--------IPDMDPTrpatvDPAKLF-AAIERYGVTNLFGSPALLER----LGRY---GEANGIKLPSLRR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1325 cVVVAEERPRVSLQQSFSKLfkdigLSPRA-VSTTFGSRVNVAICLqgtsgpdpttvyVDLKSLRHDRVRLVERGAPQSL 1403
Cdd:PRK09274 293 -VISAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS------------IESREILFATRAATDNGAGICV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1404 llsesGKILPGVKVVIVNPeTKGPVGDSH---------LGEIWVNSPHTASGYYTiYDSETLQAdhfntRLSfgDAAQTL 1474
Cdd:PRK09274 355 -----GRPVDGVEVRIIAI-SDAPIPEWDdalrlatgeIGEIVVAGPMVTRSYYN-RPEATRLA-----KIP--DGQGDV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755551660 1475 WARTGYLGFVrrteltaatgERHDALYVVGALDETLELRGLRYHPIDIEtSVSRVHRSIAECA 1537
Cdd:PRK09274 421 WHRMGDLGYL----------DAQGRLWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGVKRSA 472
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1031-1226 |
8.95e-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: 57.17 E-value: 8.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1031 HQFLAEilqwRAQATPDHV-LfmllnakgttVCTASCL---QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAF 1106
Cdd:COG1020 479 HELFEA----QAARTPDAVaV----------VFGDQSLtyaELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVAL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1107 YGCLYAGC--IPvtvrpphaqnLTATLPT--VRMVVDVSKAACVLTTQTLMRLLksreAAAAVDVktwpaiIDTDDLPRK 1182
Cdd:COG1020 544 LAVLKAGAayVP----------LDPAYPAerLAYMLEDAGARLVLTQSALAARL----PELGVPV------LALDALALA 603
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 755551660 1183 RLPQ--LYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAI 1226
Cdd:COG1020 604 AEPAtnPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWM 649
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
358-818 |
9.74e-08 |
|
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: 56.45 E-value: 9.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 358 DVTGKpvyTLTYGKLWSRSLKLAYTLlNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLTRK 437
Cdd:cd05911 5 ADTGK---ELTYAQLRTLSRRLAAGL-RKLG------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAANPIYTAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 438 DaggqqIGFLLGSCGIALALTSEiclKGLPKTQNgeivQFKGWPRLK--WVVTDSK-YLSKPPKDWQPHISP-------- 506
Cdd:cd05911 73 E-----LAHQLKISKPKVIFTDP---DGLEKVKE----AAKELGPKDkiIVLDDKPdGVLSIEDLLSPTLGEededlppp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 507 ---AGTEPAYIEYKTSKEGSVMGVTVSR---LAMLSQCQALSQAcNYSEGETVVNVLDFKKDAGLWhGMFANVMNKMHTI 580
Cdd:cd05911 141 lkdGKDDTAAILYSSGTTGLPKGVCLSHrnlIANLSQVQTFLYG-NDGSNDVILGFLPLYHIYGLF-TTLASLLNGATVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 581 svpysVM-KTCPLSWVQRVHAHKAKVALVKCRdlHWAMMAHRDQRDV-SLSSLRMLIVtdGANPWSVSSCDAFLSLFQSh 658
Cdd:cd05911 219 -----IMpKFDSELFLDLIEKYKITFLYLVPP--IAAALAKSPLLDKyDLSSLRVILS--GGAPLSKELQELLAKRFPN- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 659 glkpeaicPCATSAEAMTVAirrpGVPGAPLPGrailsmnglsygvirvnTEDKNSAltvqdVGHVMPGGMMCIVKPDGl 738
Cdd:cd05911 289 --------ATIKQGYGMTET----GGILTVNPD-----------------GDDKPGS-----VGRLLPNVEAKIVDDDG- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 739 PQLCRTDEIGEICVssRTGGMM--YFGLAGVTKNTFevipvTSSGspvgdvpFIRSGLLGFVGPGSLVFVVGKMDGLLMV 816
Cdd:cd05911 334 KDSLGPNEPGEICV--RGPQVMkgYYNNPEATKETF-----DEDG-------WLHTGDIGYFDEDGYLYIVDRKKELIKY 399
|
..
gi 755551660 817 SG 818
Cdd:cd05911 400 KG 401
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1067-1538 |
1.30e-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: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1067 LQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltatlptvrmvvdvskaacV 1146
Cdd:cd05919 14 GQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP------------------------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1147 LTTQTLMRLLKSREAAAavdvktwpAIIDTDDlprkrlpqlykpptpemLAYLDFSVSTTGMLTGVKMSHSA----VNAL 1222
Cdd:cd05919 69 LHPDDYAYIARDCEARL--------VVTSADD-----------------IAYLLYSSGTTGPPKGVMHAHRDpllfADAM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1223 CR---AIKLQCELYSSRQIAICLdpycGLGFALWclCSVYSGHQSVLIPPMELENNLFlwlATVNQYKIRdTFCSYSVME 1299
Cdd:cd05919 124 ARealGLTPGDRVFSSAKMFFGY----GLGNSLW--FPLAVGASAVLNPGWPTAERVL---ATLARFRPT-VLYGVPTFY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1300 LCTKGLGNQVEVLktrginLSCIRTCVVVAEERPRVSLQQsfsklFKDIGLSPraVSTTFGSRVNVAICLqgtsgpdptt 1379
Cdd:cd05919 194 ANLLDSCAGSPDA------LRSLRLCVSAGEALPRGLGER-----WMEHFGGP--ILDGIGATEVGHIFL---------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1380 vyvdlkSLRHDRVRlvergapqsllLSESGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYYTIYDSetlqad 1459
Cdd:cd05919 251 ------SNRPGAWR-----------LGSTGRPVPGYEIRLVDEEGH-TIPPGEEGDLLVRGPSAAVGYWNNPEK------ 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551660 1460 hfnTRLSFGDAaqtlWARTGYLGFVrrteltAATGerhdALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECAV 1538
Cdd:cd05919 307 ---SRATFNGG----WYRTGDKFCR------DADG----WYTHAGRADDMLKVGGQWVSPVEVESLIIQ-HPAVAEAAV 367
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1068-1538 |
1.30e-07 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 56.16 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGC--IPVTVRPPHAQNltatlptvRMVVDVSKAAC 1145
Cdd:cd17643 17 ELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGayVPIDPAYPVERI--------AFILADSGPSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1146 VLTTqtlmrllksreaaaavdvktwpaiidtddlprkrlpqlykpptPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 1225
Cdd:cd17643 88 LLTD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1226 IklQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMEL---ENNLFLWLA----TV-NQykirdTFCSYSV 1297
Cdd:cd17643 125 T--QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVarsPEDFARLLRdegvTVlNQ-----TPSAFYQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1298 MelctkglgnqVEVLKTRGINLSCIRTcVVVAEERPRVSLQQSFSKLFKDigLSPRAVSTTfgsrvnvaiclqgtsGPDP 1377
Cdd:cd17643 198 L----------VEAADRDGRDPLALRY-VIFGGEALEAAMLRPWAGRFGL--DRPQLVNMY---------------GITE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1378 TTVYVDLKSLRHDRVRLVERgapqslllSESGKILPGVKVVIVNpETKGPVGDSHLGEIWVNSPHTASGYYtiyDSETLQ 1457
Cdd:cd17643 250 TTVHVTFRPLDAADLPAAAA--------SPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYL---GRPELT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1458 ADHFNTrLSFGDAAQTLWaRTGYLgfVRRTeltaATGErhdaLYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECA 1537
Cdd:cd17643 318 AERFVA-NPFGGPGSRMY-RTGDL--ARRL----PDGE----LEYLGRADEQVKIRGFRIELGEIEAALAT-HPSVRDAA 384
|
.
gi 755551660 1538 V 1538
Cdd:cd17643 385 V 385
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1034-1123 |
1.31e-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: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1034 LAEILQWRAQATPDHVlfmllnAkgtTVCTASCL---QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCL 1110
Cdd:COG1021 27 LGDLLRRRAERHPDRI------A---VVDGERRLsyaELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALF 96
|
90
....*....|...
gi 755551660 1111 YAGCIPVTVRPPH 1123
Cdd:COG1021 97 RAGAIPVFALPAH 109
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
366-435 |
1.84e-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: 1.84e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 366 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLT 435
Cdd:cd05936 24 KLTYRELDALAEAFAAGLQN-LG------VQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLNPLYT 84
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1069-1537 |
3.82e-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: 3.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1069 LHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltatlptvRMVVdvskaacvlt 1148
Cdd:cd05910 8 LDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP-------------GMGR---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1149 tQTLMRLLKSREAAAAVDVktwpaiidtddlprkrlpqlykpPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKl 1228
Cdd:cd05910 64 -KNLKQCLQEAEPDAFIGI-----------------------PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALR- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1229 qcELYSSRQIAICLDpycglGFALWCLCSVYSGHQSVlIPPMELE-----NNLFLwLATVNQYKIRDTFCSYSVMELCTk 1303
Cdd:cd05910 119 --QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDPTrparaDPQKL-VGAIRQYGVSIVFGSPALLERVA- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1304 glgnqvEVLKTRGINLSCIRtCVVVAEERPRVSLQQSFSKLfkdigLSPRA-VSTTFGSRVNVAICLQGTSgpdpttvyv 1382
Cdd:cd05910 189 ------RYCAQHGITLPSLR-RVLSAGAPVPIALAARLRKM-----LSDEAeILTPYGATEALPVSSIGSR--------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1383 dlkSLRHDRVRLVERGAPQSLllsesGKILPGVKVVIVnPETKGPV---GDSH------LGEIWVNSPHTASGYYTIYDS 1453
Cdd:cd05910 248 ---ELLATTTAATSGGAGTCV-----GRPIPGVRVRII-EIDDEPIaewDDTLelprgeIGEITVTGPTVTPTYVNRPVA 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1454 ETLQADHfntrlsfgDAAQTLWARTGYLGFVrrteltaatgERHDALYVVGALDETLELRGLRYHPIDIEtSVSRVHRSI 1533
Cdd:cd05910 319 TALAKID--------DNSEGFWHRMGDLGYL----------DDEGRLWFCGRKAHRVITTGGTLYTEPVE-RVFNTHPGV 379
|
....
gi 755551660 1534 AECA 1537
Cdd:cd05910 380 RRSA 383
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
395-839 |
4.26e-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: 4.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 395 LKPGDRVALVYPNNDP---VMFMVAFYGCLLAEVIpvpieVPLTrKDAGGQQIGFLLGSCGIALALTSEiclKGLPKTQN 471
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIVLADA---GAADRLRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 472 GEIVQfkgwpRLKWVVTDSKYLSKPPKDWQPHIsPAGTEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGE 551
Cdd:cd05922 86 ALPAS-----PDPGTVLDADGIRAARASAPAHE-VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 552 TVVNVLDFKKDAGLwhgmfaNVMNK---------MHTISVPysvmktcPLSWVQRVHAHKAK-VALVKCrdlHWAMMAHR 621
Cdd:cd05922 160 RALTVLPLSYDYGL------SVLNThllrgatlvLTNDGVL-------DDAFWEDLREHGATgLAGVPS---TYAMLTRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 622 DQRDVSLSSLRMLIVTDGANPwsvsscDAFLSLFqshglkpeaicpcatsAEAMtvairrpgvpgaplPGRAILSMNGLS 701
Cdd:cd05922 224 GFDPAKLPSLRYLTQAGGRLP------QETIARL----------------RELL--------------PGAQVYVMYGQT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 702 YGVIRVNTEDKNSALTVQD-VGHVMPGGMMCIVKPDGLPqlCRTDEIGEICVSSRTGGMMYFglagvtkNTFEVIPVTSS 780
Cdd:cd05922 268 EATRRMTYLPPERILEKPGsIGLAIPGGEFEILDDDGTP--TPPGEPGEIVHRGPNVMKGYW-------NDPPYRRKEGR 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 755551660 781 GspvGDVpfIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIKTV 839
Cdd:cd05922 339 G---GGV--LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA 392
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1041-1224 |
4.37e-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: 54.51 E-value: 4.37e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1041 RAQATPDHVLfmlLNAKGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVR 1120
Cdd:cd12117 6 QAARTPDAVA---VVYGDRSLTYA---ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1121 PphaqnltaTLPTVRM--VVDVSKAACVLTTqtlmrllksrEAAAAVDVKTWPAIIDTDDLPRKRLPQLYKPPTPEMLAY 1198
Cdd:cd12117 79 P--------ELPAERLafMLADAGAKVLLTD----------RSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAY 140
|
170 180
....*....|....*....|....*.
gi 755551660 1199 LDFSVSTTGMLTGVKMSHSAVNALCR 1224
Cdd:cd12117 141 VMYTSGSTGRPKGVAVTHRGVVRLVK 166
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
368-820 |
8.17e-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: 8.17e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 368 TYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEV--PLTRkdaggqqIG 445
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAER-------LA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 446 FLLGSCGIALALTSEiclkglpktQNGEIVQFKGWPRLKWVVTDSKYLSKPPKDWQPHISPAGTEPAYIEYkTSkeGSV- 524
Cdd:TIGR01733 66 FILEDAGARLLLTDS---------ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 525 --MGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHgMFANVMNKMHTISVPYSVMKTCPLSWvQRVHAHK 602
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-AALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 603 aKVALVKCRDLHWAMMAhrDQRDVSLSSLRMLIVtdganpwsvsscdaflslfqshglkpeaicpcatSAEAMTVA-IRR 681
Cdd:TIGR01733 212 -PVTVLNLTPSLLALLA--AALPPALASLRLVIL----------------------------------GGEALTPAlVDR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 682 pgvPGAPLPGRAILSMnglsYG---------VIRVnTEDKNSALTVQDVGHVMPGGMMCIVKPDGlpQLCRTDEIGEICV 752
Cdd:TIGR01733 255 ---WRARGPGARLINL----YGptettvwstATLV-DPDDAPRESPVPIGRPLANTRLYVLDDDL--RPVPVGVVGELYI 324
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551660 753 SSRTGGMMYFGLAGVTKNTFevipVTSSGSPVGDVPFIRSGLLGFVGP-GSLVFvVGKMDGLLMVSGRR 820
Cdd:TIGR01733 325 GGPGVARGYLNRPELTAERF----VPDPFAGGDGARLYRTGDLVRYLPdGNLEF-LGRIDDQVKIRGYR 388
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1068-1538 |
9.09e-07 |
|
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: 53.25 E-value: 9.09e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltatlptvrmvvdvskaacvl 1147
Cdd:cd05958 15 DLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP-------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1148 ttqtlmrLLKSREAAAAVDvKTWPAIIDTDDlprkrlpqlyKPPTPEMLAYLDFSVSTTGMLTGVKMSHsavnalcRAIK 1227
Cdd:cd05958 69 -------LLRPKELAYILD-KARITVALCAH----------ALTASDDICILAFTSGTTGAPKATMHFH-------RDPL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1228 LQCELYsSRQI--AICLDPYCGL-------GFALWCLCSVYSGHQSVLIP---PMELennlflwLATVNQYKIRDTF--- 1292
Cdd:cd05958 124 ASADRY-AVNVlrLREDDRFVGSpplaftfGLGGVLLFPFGVGASGVLLEeatPDLL-------LSAIARYKPTVLFtap 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1293 CSYSVMelctkglgnqVEVLKTRGINLSCIRTCVVVAEERPrvslQQSFSKLFKDIGLSpraVSTTFGSRVNVAICLQGT 1372
Cdd:cd05958 196 TAYRAM----------LAHPDAAGPDLSSLRKCVSAGEALP----AALHRAWKEATGIP---IIDGIGSTEMFHIFISAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1373 SGpdpttvyvdlkslrHDRVrlverGApqslllseSGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPhtaSGYYtiYD 1452
Cdd:cd05958 259 PG--------------DARP-----GA--------TGKPVPGYEAKVVDDEGN-PVPDGTIGRLAVRGP---TGCR--YL 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1453 SETLQADHF-NTRLSFGDAaqTLWARTGYLGFVRRTeltaatgerhDALYVVGaldetlelrGLRYHPIDIEtSVSRVHR 1531
Cdd:cd05958 306 ADKRQRTYVqGGWNITGDT--YSRDPDGYFRHQGRS----------DDMIVSG---------GYNIAPPEVE-DVLLQHP 363
|
....*..
gi 755551660 1532 SIAECAV 1538
Cdd:cd05958 364 AVAECAV 370
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
366-499 |
9.32e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 53.43 E-value: 9.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 366 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALvYPNNDPvMFMVAFYGCLLAEVIPVPIEvPLTRKDaggqQIG 445
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLL-YMQNSP-QFVIAYYAILRANAVVVPVN-PMNREE----ELA 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 755551660 446 FLLGSCGIALAltseICLKGLPktqnGEIVQFKGWPRLKWVVTD--SKYLSKPPKD 499
Cdd:PRK08314 102 HYVTDSGARVA----IVGSELA----PKVAPAVGNLRLRHVIVAqySDYLPAEPEI 149
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1010-1226 |
1.34e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1010 RIAQAAGRDLGQI-----EENDLV---------------RKHQFLAEilqwRAQATPDHVlfmllnakgTTVCTASCL-- 1067
Cdd:PRK12316 1965 QMAEDAQAALGELalldaGERQRIladwdrtpeayprgpGVHQRIAE----QAARAPEAI---------AVVFGDQHLsy 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 -QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHaqnltatlPTVR---MVVDvSKA 1143
Cdd:PRK12316 2032 aELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY--------PAERlayMLED-SGA 2101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1144 ACVLTTQTLMRLLKSREAAAAVDVKT---WPAIIDTDDLPRKrlpqlykppTPEMLAYLDFSVSTTGMLTGVKMSHSAVN 1220
Cdd:PRK12316 2102 ALLLTQRHLLERLPLPAGVARLPLDRdaeWADYPDTAPAVQL---------AGENLAYVIYTSGSTGLPKGVAVSHGALV 2172
|
....*.
gi 755551660 1221 ALCRAI 1226
Cdd:PRK12316 2173 AHCQAA 2178
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1034-1229 |
3.71e-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: 3.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1034 LAEILQWRAQATPDHVLFMLLNAKGTTVCTASclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 1113
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSLTWA--EFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1114 CIPVTVRPphaqnlTATLPTVRMVVDVSKAACVL--TTQTLMRLLKSREAAAAV---------------DVKTWPAIID- 1175
Cdd:COG1022 90 AVTVPIYP------TSSAEEVAYILNDSGAKVLFveDQEQLDKLLEVRDELPSLrhivvldprglrddpRLLSLDELLAl 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 755551660 1176 -TDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSH----SAVNALCRAIKLQ 1229
Cdd:COG1022 164 gREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHrnllSNARALLERLPLG 222
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1040-1219 |
4.34e-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: 4.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1040 WRAQA--TPDHVlfmllnAKGTTVCTASCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPV 1117
Cdd:cd17646 4 VAEQAarTPDAP------AVVDEGRTLTYRELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1118 TVRPPHaqnltatlPTVR---MVVDVskAACVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPRkrlpqlykPPTPE 1194
Cdd:cd17646 77 PLDPGY--------PADRlayMLADA--GPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV--------PPRPD 138
|
170 180
....*....|....*....|....*
gi 755551660 1195 MLAYLDFSVSTTGMLTGVKMSHSAV 1219
Cdd:cd17646 139 NLAYVIYTSGSTGRPKGVMVTHAGI 163
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1031-1563 |
4.84e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.88 E-value: 4.84e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1031 HQFLAEilqwRAQATPDHVLfMLLNAKgttvcTASCLQLHKRAERIASVLGDKGhlnAGDNVV--LLYPPGIELIAAFYG 1108
Cdd:PRK12316 4554 HQLVAE----RARMTPDAVA-VVFDEE-----KLTYAELNRRANRLAHALIARG---VGPEVLvgIAMERSAEMMVGLLA 4620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1109 CLYAGCIPVTVRPPHAQNLTATlptvrMVVDvSKAACVLTTQTLMRLLKSREAAAAVDV---KTWPAIIDTDdlprkrlP 1185
Cdd:PRK12316 4621 VLKAGGAYVPLDPEYPRERLAY-----MMED-SGAALLLTQSHLLQRLPIPDGLASLALdrdEDWEGFPAHD-------P 4687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1186 QLykPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRqiaiCLDPYCGLGF--ALWCLCSVYSGHQ 1263
Cdd:PRK12316 4688 AV--RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDD----RVLQFMSFSFdgSHEGLYHPLINGA 4761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1264 SVLIPPMELENNLFLwLATVNQYKIRDTFCSYSVMELCTKGLGNQVEVLKTRGINLScirtcvvvAEERPRVSLQQSFSK 1343
Cdd:PRK12316 4762 SVVIRDDSLWDPERL-YAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFG--------GEAVAQASYDLAWRA 4832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1344 LFKDiglspravsttfgsrvnvaiCLQGTSGPDPTTVYVDLKSLRhdrvrlveRGAPQSLLLSESGKILPGVKVVIV--- 1420
Cdd:PRK12316 4833 LKPV--------------------YLFNGYGPTETTVTVLLWKAR--------DGDACGAAYMPIGTPLGNRSGYVLdgq 4884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1421 -NPETKGPVGDSHLGEIWVnsphtASGYytiYDSETLQADHFNTRlSFGDAAQTLWaRTGYLgfvrrteltaATGERHDA 1499
Cdd:PRK12316 4885 lNPLPVGVAGELYLGGEGV-----ARGY---LERPALTAERFVPD-PFGAPGGRLY-RTGDL----------ARYRADGV 4944
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551660 1500 LYVVGALDETLELRGLRYHPIDIETSVsRVHRSIAECavftwtnlLVVVVELCGSEQEALDLVP 1563
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARL-REHPAVREA--------VVIAQEGAVGKQLVGYVVP 4999
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1068-1226 |
6.04e-06 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 50.73 E-value: 6.04e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltaTLPTVRMVVDVSKAACvl 1147
Cdd:cd12114 17 ELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDI--------DQPAARREAILADAGA-- 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755551660 1148 ttqtlmRLLKSREAAAAVDVKTWPAIIDTDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAI 1226
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 ... |
526-826 |
8.69e-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: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 526 GVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWhGMFANVMNKMHTISVPysvmKTCPLSWVQRVHAHKAKV 605
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP----KFDPEAALELIEREKVTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 606 ALVKcRDLHWAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLSLF-----QSHGLkPEAICPCATSAEAMtvAIR 680
Cdd:cd04433 92 LLGV-PTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAPgiklvNGYGL-TETGGTVATGPPDD--DAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 681 RPGVPGAPLPGRAILsmnglsygvirvntedknsaltvqdvghvmpggmmcIVKPDGLPqlCRTDEIGEICVssrTGGMM 760
Cdd:cd04433 166 KPGSVGRPVPGVEVR------------------------------------IVDPDGGE--LPPGEIGELVV---RGPSV 204
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755551660 761 YFGLAGVTKNTFEVIPvtsSGspvgdvpFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDI 826
Cdd:cd04433 205 MKGYWNNPEATAAVDE---DG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEV 260
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
361-462 |
4.16e-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: 4.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 361 GKPVY-----TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYpnNDPVMFMVAFYGCLLAEVIPVPIEVPLT 435
Cdd:cd05959 19 DKTAFiddagSLTYAELEAEARRVAGALR-ALG------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100
....*....|....*....|....*...
gi 755551660 436 rkdagGQQIGFLLGSCGI-ALALTSEIC 462
Cdd:cd05959 90 -----PDDYAYYLEDSRArVVVVSGELA 112
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1038-1539 |
4.25e-05 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 47.99 E-value: 4.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1038 LQWRAQATPDHVLFMLLnakGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPV 1117
Cdd:cd17631 1 LRRRARRHPDRTALVFG---GRSLTYA---ELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1118 tvrpPHAQNLTAtlPTVRMVVDVSKAACVLttqtlmrllksreaaaavdvktwpaiidtDDLprkrlpqlykpptpemlA 1197
Cdd:cd17631 74 ----PLNFRLTP--PEVAYILADSGAKVLF-----------------------------DDL-----------------A 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1198 YLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELySSRQIAICLDPYCGLGFA-LWCLCSVYSGHQSVLIPPMELENnl 1276
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPET-- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1277 flWLATVNQYKIRDTFCSYSVME-LCTKGlgnqvevlKTRGINLSCIRtCVVVAEERPRVSLQQSFsklfKDIGLsprAV 1355
Cdd:cd17631 179 --VLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV---KF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1356 STTFGsrvnvaiclQGTSGPdPTTVyvdlksLRHDRVRlvergapqSLLLSeSGKILPGVKVVIVNPETKgPVGDSHLGE 1435
Cdd:cd17631 241 VQGYG---------MTETSP-GVTF------LSPEDHR--------RKLGS-AGRPVFFVEVRIVDPDGR-EVPPGEVGE 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1436 IWVNSPHTASGYYTiyDSETlqadhfnTRLSFGDAaqtlWARTGYLGFVrrteltaatgeRHDA-LYVVGALDETLELRG 1514
Cdd:cd17631 295 IVVRGPHVMAGYWN--RPEA-------TAAAFRDG----WFHTGDLGRL-----------DEDGyLYIVDRKKDMIISGG 350
|
490 500
....*....|....*....|....*
gi 755551660 1515 LRYHPIDIETSVSRvHRSIAECAVF 1539
Cdd:cd17631 351 ENVYPAEVEDVLYE-HPAVAEVAVI 374
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
366-557 |
5.68e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 47.62 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 366 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNDpvMFMVAFYGCLLAEVIPVPIEVPLTrkdagGQQIG 445
Cdd:PRK08316 36 SWTYAELDAAVNRVAAALLD-LG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLT-----GEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 446 FLLGSCGIALALTSEICLKGLPKTQNGEIVQFKGWPRL--------KWVVTDSKYLSKPpkDWQPHISPAGTEPAYIEYK 517
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVlggreapgGWLDFADWAEAGS--VAEPDVELADDDLAQILYT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 755551660 518 TSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGETVVNVL 557
Cdd:PRK08316 180 SGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHAL 219
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1068-1216 |
7.94e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 47.30 E-value: 7.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRP-------------------------- 1121
Cdd:PRK05605 62 ELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPlytahelehpfedhgarvaivwdkva 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1122 PHAQNLTATLPtVRMVVDVS-KAACVLTTQTLMRL-----LKSREA--AAAVDVKTWPAIIDTDDLPRKRLPQLYKPpTP 1193
Cdd:PRK05605 141 PTVERLRRTTP-LETIVSVNmIAAMPLLQRLALRLpipalRKARAAltGPAPGTVPWETLVDAAIGGDGSDVSHPRP-TP 218
|
170 180
....*....|....*....|...
gi 755551660 1194 EMLAYLDFSVSTTGMLTGVKMSH 1216
Cdd:PRK05605 219 DDVALILYTSGTTGKPKGAQLTH 241
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
365-428 |
1.24e-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: 1.24e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755551660 365 YTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPV 428
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 ... |
1404-1495 |
1.30e-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: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1404 LLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYY-----TiydSETLQADH-FNTrlsfGDAAQtlWAR 1477
Cdd:cd17640 262 VRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYknpeaT---SKVLDSDGwFNT----GDLGW--LTC 332
|
90 100
....*....|....*....|
gi 755551660 1478 TGYLGFVRRTELTA--ATGE 1495
Cdd:cd17640 333 GGELVLTGRAKDTIvlSNGE 352
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
366-636 |
1.33e-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: 46.77 E-value: 1.33e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 366 TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPI--EVPLTRkdaggqq 443
Cdd:COG1020 501 SLTYAELNARANRLAHHLR-ALG------VGPGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLdpAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 444 IGFLLGSCGIALALTSEICLKGLPKTQngeivqfkgwprLKWVVTDSKYLSKPPKDWqPHISPAGTEPAYIEYkTS---- 519
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPELG------------VPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TSgstg 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 520 --KegsvmGVTVSRLAMLSQCQALSQACNYSEGETVVNV--LDFkkDAGLWhGMFANVMNKMHTISVPYSVMKTcPLSWV 595
Cdd:COG1020 631 rpK-----GVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW-EIFGALLSGATLVLAPPEARRD-PAALA 701
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 755551660 596 QRVHAHkaKVALVKCRDLHWAMMAHRDQRDvsLSSLRMLIV 636
Cdd:COG1020 702 ELLARH--RVTVLNLTPSLLRALLDAAPEA--LPSLRLVLV 738
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1409-1538 |
2.47e-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: 2.47e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1409 GKILPGVKVVIVNPETKGPVGDSHlGEIWVNSPHTASGYytiYDSETLQADHFNTRlsfgdaaqtlWARTGYLGFVRrte 1488
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGY---WNNPERTAEVLIDG----------WVNTGDLGERR--- 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 755551660 1489 ltaatgeRHDALYVVGALDETLELRGLRYHPIDIETSVSRVhRSIAECAV 1538
Cdd:cd17635 236 -------EDGFLFITGRSSESINCGGVKIAPDEVERIAEGV-SGVQECAC 277
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1077-1551 |
3.61e-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: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1077 ASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTATlpTVRMVVDVSKAACVLTTQTLMrll 1156
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKES--VLRYLVADAGGRIVLADAGAA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1157 kSREAAAAVDVKTWPAIIDTDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVnalcraiklqceLYSSR 1236
Cdd:cd05922 81 -DRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNL------------LANAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1237 QIAICLDpYCGLGFALWCLCSVYSGHQSVLippmeleNNLFLWLATV---NQYKIRDTFcsysvMELCTKglgnqvevlk 1313
Cdd:cd05922 148 SIAEYLG-ITADDRALTVLPLSYDYGLSVL-------NTHLLRGATLvltNDGVLDDAF-----WEDLRE---------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1314 TRGINLSCIrtcvvvaeerPrvSLQQSFSKL-FKDIGL-SPRAVSTTFGSRVNVAICLQGTSGPDpTTVYV--------- 1382
Cdd:cd05922 205 HGATGLAGV----------P--STYAMLTRLgFDPAKLpSLRYLTQAGGRLPQETIARLRELLPG-AQVYVmygqteatr 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1383 DLKSLRHDRVRlvERgaPQSLllsesGKILPGVKVVIVNPEtKGPVGDSHLGEIWVNSPHTASGYytiydsetlqadhfn 1462
Cdd:cd05922 272 RMTYLPPERIL--EK--PGSI-----GLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGY--------------- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1463 trlsfgdaaqtlWARTGYLGFVRRTELTAATGE--RHDA---LYVVGALDETLELRGLRYHPIDIETSVsRVHRSIAECA 1537
Cdd:cd05922 327 ------------WNDPPYRRKEGRGGGVLHTGDlaRRDEdgfLFIVGRRDRMIKLFGNRISPTEIEAAA-RSIGLIIEAA 393
|
490
....*....|....*...
gi 755551660 1538 VF----TWTNLLVVVVEL 1551
Cdd:cd05922 394 AVglpdPLGEKLALFVTA 411
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1032-1125 |
3.82e-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: 3.82e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1032 QFLAEILQWRAQATPDHVlfMLLNAKGTTvctaSCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLY 1111
Cdd:cd05920 15 EPLGDLLARSAARHPDRI--AVVDGDRRL----TYRELDRRADRLAAGLRGLG-IRPGDRVVVQLPNVAEFVVLFFALLR 87
|
90
....*....|....
gi 755551660 1112 AGCIPVTVRPPHAQ 1125
Cdd:cd05920 88 LGAVPVLALPSHRR 101
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
591-964 |
3.87e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 44.99 E-value: 3.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 591 PLSWVQRVHAHKAKVALVKcrDLHWAMMAHR-----DQRDVSLSSLRmlIVTDGANPWSVSSCDAFLSLFQSHGLKPEAI 665
Cdd:PRK07768 235 PLLWAELISKYRGTMTAAP--NFAYALLARRlrrqaKPGAFDLSSLR--FALNGAEPIDPADVEDLLDAGARFGLRPEAI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 666 CPCATSAEAmTVAIRRPGvPGAPL----PGRAILSMNGlsygviRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGlpQL 741
Cdd:PRK07768 311 LPAYGMAEA-TLAVSFSP-CGAGLvvdeVDADLLAALR------RAVPATKGNTRRLATLGPPLPGLEVRVVDEDG--QV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 742 CRTDEIGEICVSSRTggmmyfglagVTKNTfevipVTSSG--SPVGDVPFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGR 819
Cdd:PRK07768 381 LPPRGVGVIELRGES----------VTPGY-----LTMDGfiPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 820 RHNADDIVATGLAVESIktvyrgRHTGLLAVpqtcqarpylrtfPLSVPSVRnplppdlrvarvltsfriavfsvsvfyd 899
Cdd:PRK07768 446 NIYPTDIERAAARVEGV------RPGNAVAV-------------RLDAGHSR---------------------------- 478
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755551660 900 ERIVVVAEQRPDASEEDSFQWMSRVLQAIDSihQVGV--YCLALVPANTLPKTPLGGIHISQTKQLF 964
Cdd:PRK07768 479 EGFAVAVESNAFEDPAEVRRIRHQVAHEVVA--EVGVrpRNVVVLGPGSIPKTPSGKLRRANAAELV 543
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1034-1216 |
3.96e-04 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 45.13 E-value: 3.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1034 LAEILQWRAQATPDHVLFMLlnakGTTVCTASclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 1113
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLVF----GGTRWTYA--EAARAAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1114 CIPVTV----RPPHaqnLTATLPTVRMVVDVSKAACVLTTQTLMRLLKSREAAAAVD---VKTWPAIIDTDDLPRKRLPQ 1186
Cdd:PRK06155 96 AIAVPIntalRGPQ---LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDapaSVSVPAGWSTAPLPPLDAPA 172
|
170 180 190
....*....|....*....|....*....|.
gi 755551660 1187 LYKPPTP-EMLAYLDFSvSTTGMLTGVKMSH 1216
Cdd:PRK06155 173 PAAAVQPgDTAAILYTS-GTTGPSKGVCCPH 202
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1068-1538 |
4.87e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 44.60 E-value: 4.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCiPVTV--RPPHAQNLTA----TLPTVRMV---- 1137
Cdd:PRK07768 34 EVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGA-SLTMlhQPTPRTDLAVwaedTLRVIGMIgaka 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1138 VDVSK----AACVLTTQ--TLMRLLKSREAAAAVDVKTwpaiiDTDDLprkrlpqlykpptpemlAYLDFSVSTTGMLTG 1211
Cdd:PRK07768 112 VVVGEpflaAAPVLEEKgiRVLTVADLLAADPIDPVET-----GEDDL-----------------ALMQLTSGSTGSPKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1212 VKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYC---GL-GFalwcLCS-VYSGHQSVLIPPMELENNLFLWLATVNQY 1286
Cdd:PRK07768 170 VQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFhdmGMvGF----LTVpMYFGAELVKVTPMDFLRDPLLWAELISKY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1287 KIRDT----FcSYSVmelctkgLGNQVEVLKTRG-INLSCIRtCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFG- 1360
Cdd:PRK07768 246 RGTMTaapnF-AYAL-------LARRLRRQAKPGaFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGm 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1361 --SRVNVAICLQGTsGPDPTTVYVDLKSLRHdRVRLVERGAPQSLLLSesGKILPGVKVVIVNpETKGPVGDSHLGEIWV 1438
Cdd:PRK07768 317 aeATLAVSFSPCGA-GLVVDEVDADLLAALR-RAVPATKGNTRRLATL--GPPLPGLEVRVVD-EDGQVLPPRGVGVIEL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1439 NSPHTASGYYTIYDSETLQADHfntrlsfGdaaqtlWARTGYLGFVrrTELtaatGErhdaLYVVGALDETLELRGLRYH 1518
Cdd:PRK07768 392 RGESVTPGYLTMDGFIPAQDAD-------G------WLDTGDLGYL--TEE----GE----VVVCGRVKDVIIMAGRNIY 448
|
490 500
....*....|....*....|
gi 755551660 1519 PIDIETSVSRVHRSIAECAV 1538
Cdd:PRK07768 449 PTDIERAAARVEGVRPGNAV 468
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
340-430 |
1.06e-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: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 340 ALQRWGSTQAKCPCLTGLDVTGKPVyTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYG 419
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGEDGEER-TLTYAELRREVNRFA-NALRALG------VKKGDRVAIYLPNI--PEAVIAMLA 83
|
90
....*....|.
gi 755551660 420 CLLAEVIPVPI 430
Cdd:COG0365 84 CARIGAVHSPV 94
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1036-1300 |
1.09e-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: 1.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1036 EILQWRAQATPDHVlfmllnakgTTVC---TASCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYA 1112
Cdd:cd17655 1 ELFEEQAEKTPDHT---------AVVFedqTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1113 GCIPVTVRPPHAQNltatlpTVRMVVDVSKAACVLTTQTLMRLLKSREAAAAvdvktwpaiIDTDDLPRKRLPQLYKPPT 1192
Cdd:cd17655 71 GGAYLPIDPDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLIDL---------LDEDTIYHEESENLEPVSK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1193 PEMLAYLDFSVSTTGMLTGVKMSH--------SAVNALCRAIKLQCELYSSrqiaICLDPYCGLGFAlwclcSVYSGHQS 1264
Cdd:cd17655 136 SDDLAYVIYTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFDASVTEIFA-----SLLSGNTL 206
|
250 260 270
....*....|....*....|....*....|....*.
gi 755551660 1265 VLIPPMELENNLFLwLATVNQYKIRDTFCSYSVMEL 1300
Cdd:cd17655 207 YIVRKETVLDGQAL-TQYIRQNRITIIDLTPAHLKL 241
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1068-1538 |
1.53e-03 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 43.61 E-value: 1.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1068 QLHKRAERIASVLGDKGhlnAGDNVV--LLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTATlptvrMVVDvSKAAC 1145
Cdd:PRK12467 3125 ELNRRANRLAHRLIAIG---VGPDVLvgVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY-----MIED-SGVKL 3195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1146 VLTTQtlmRLLKSREAAAAVDVKTwpaiIDTDDLPrkrlPQLYKPPT----PEMLAYLDFSVSTTGMLTGVKMSHSAVNA 1221
Cdd:PRK12467 3196 LLTQA---HLLEQLPAPAGDTALT----LDRLDLN----GYSENNPStrvmGENLAYVIYTSGSTGKPKGVGVRHGALAN 3264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1222 LCRAIKLQCELySSRQIAICLDPYCGLGFA---LWCLCsvySGHQsVLIPPMELENNLFLWlATVNQYKIrdtfcsySVM 1298
Cdd:PRK12467 3265 HLCWIAEAYEL-DANDRVLLFMSFSFDGAQerfLWTLI---CGGC-LVVRDNDLWDPEELW-QAIHAHRI-------SIA 3331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1299 ELCTKGLGNQVEVLKTRgiNLSCIRTCVVVAEERPRVSLQQSFSKLfkdiglsPRAvsttfgsrvnvaiCLQGTSGPDPT 1378
Cdd:PRK12467 3332 CFPPAYLQQFAEDAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKL-------KPR-------------GLTNGYGPTEA 3389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1379 TVYVDLKSLRHDRVRLVErGAPqslllseSGKILPGVKVVIVNPETkGPVGDSHLGEIWVNSPHTASGYytiYDSETLQA 1458
Cdd:PRK12467 3390 VVTVTLWKCGGDAVCEAP-YAP-------IGRPVAGRSIYVLDGQL-NPVPVGVAGELYIGGVGLARGY---HQRPSLTA 3457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1459 DHFNTRlSFGDAAQTLWaRTGYLGFVRRTELtaatgerhdaLYVVGALDETLELRGLRYHPIDIETSVsRVHRSIAECAV 1538
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 ... |
367-458 |
1.79e-03 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 42.85 E-value: 1.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 367 LTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEvPLTRKDaggqQIGF 446
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKG------VRKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90
....*....|..
gi 755551660 447 LLGSCGIALALT 458
Cdd:cd05935 68 ILNDSGAKVAVV 79
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
366-468 |
1.94e-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: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 366 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNDPvmFMVAFYGCLLAEVIPVPIEVPLTRKDaggqqIG 445
Cdd:cd17631 20 SLTYAELDERVNRLAHALRA-LG------VAKGDRVAVLSKNSPE--FLELLFAAARLGAVFVPLNFRLTPPE-----VA 85
|
90 100 110
....*....|....*....|....*....|
gi 755551660 446 FLLGSCGiALALTSEICL-------KGLPK 468
Cdd:cd17631 86 YILADSG-AKVLFDDLALlmytsgtTGRPK 114
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
349-436 |
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 755551660 349 AKCPCLTGLDVTGKpvyTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVAlVYPNNDPVMFmVAFYGCLLA--EVI 426
Cdd:cd05945 2 AANPDRPAVVEGGR---TLTYRELKERADALA-AALASLG------LDAGDPVV-VYGHKSPDAI-AAFLAALKAghAYV 69
|
90
....*....|
gi 755551660 427 PVPIEVPLTR 436
Cdd:cd05945 70 PLDASSPAER 79
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
366-444 |
2.46e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 42.35 E-value: 2.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 366 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNndPVMFMVAFYGCLLAEVIPV-------PIEVPLTRKD 438
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPN--LLQYPIALFGILRAGMIVVnvnplytPRELEHQLND 119
|
....*.
gi 755551660 439 AGGQQI 444
Cdd:PRK08974 120 SGAKAI 125
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1409-1539 |
3.02e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 41.95 E-value: 3.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1409 GKILPGVKVVIVNpetkgpvgdshlGEIWVNSPHTASGYYTIYDsetlqadhfntrlsFGDAAQTLWARTGYLGFVrrte 1488
Cdd:PRK07824 195 GVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVD--------------PDPFAEPGWFRTDDLGAL---- 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 755551660 1489 ltaatgerHD-ALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECAVF 1539
Cdd:PRK07824 245 --------DDgVLTVLGRADDAISTGGLTVLPQVVEAALAT-HPAVADCAVF 287
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1405-1538 |
3.10e-03 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 41.95 E-value: 3.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 1405 LSESGKILPGVKVVIVNPETKgPVGDshlGEIWVNSPHTASGYY--TIYDSETLQADHFNTrlsfGDaaqtlwarTGYL- 1481
Cdd:cd05912 241 IGSAGKPLFPVELKIEDDGQP-PYEV---GEILLKGPNVTKGYLnrPDATEESFENGWFKT----GD--------IGYLd 304
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755551660 1482 --GFV----RRTELTAATGERhdaLYvvgaldetlelrglryhPIDIETSVSRvHRSIAECAV 1538
Cdd:cd05912 305 eeGFLyvldRRSDLIISGGEN---IY-----------------PAEIEEVLLS-HPAIKEAGV 346
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
362-436 |
5.81e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 41.03 E-value: 5.81e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 362 KPVY-----TLTYGKLWSRSLKLAYTLLNKLGTKNEPVlkpgdrvaLVYPNNDPVMfMVAFYGCLLA--EVIPVPIEVPL 434
Cdd:PRK04813 18 FPAYdylgeKLTYGQLKEDSDALAAFIDSLKLPDKSPI--------IVFGHMSPEM-LATFLGAVKAghAYIPVDVSSPA 88
|
..
gi 755551660 435 TR 436
Cdd:PRK04813 89 ER 90
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
314-458 |
6.37e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 41.18 E-value: 6.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755551660 314 PEGRQMTPVKgePLGVIcnwppALESALQRWGSTQAKCPcltGLDVTGkpvYTLTYGKLWSRSLKLAyTLLNKLGtknep 393
Cdd:PRK06178 19 PAGIPREPEY--PHGER-----PLTEYLRAWARERPQRP---AIIFYG---HVITYAELDELSDRFA-ALLRQRG----- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755551660 394 vLKPGDRVALVYPNNdPvMFMVAFYGCLLAEVIPVPIEvPLTRkdagGQQIGFLLGSCGIALALT 458
Cdd:PRK06178 80 -VGAGDRVAVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFR----EHELSYELNDAGAEVLLA 136
|
|
| |
