|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
771-1336 |
0e+00 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 733.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 771 LFMLLNAKGTTVCTASCLQLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPH-AQNLT 849
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 850 ATLPTVRMvvDVSKAACVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPRKRLP-----QLYKPPTPEMLAYLDFSV 924
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 925 STTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMELENNLFLWLATV 1004
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1005 NQYKIRDTFCSYSVMELCTKGLGNQVEVLKTRGINLSCIRTCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGSRV 1084
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1085 NVAICLQGTSGPDPTTVYVDLKSLRHDRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHT 1164
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1165 ASGYYTIYDSETLQADHFN-TRLSFGDaAQTLWARTGYLGFVRRTELTAATGERHDALYVVGALDETLELRGLRYHPIDI 1243
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFPsTRLSTGI-TNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDI 477
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1244 ETSVSRVHRSIAECAVFTWTNLLVVVVEL-CGSEQEALDLVPLVTNVVLEEHYLIVGVVVVVDPGVVPINSRGEKQRMHL 1322
Cdd:cd05905 478 EATVMRVHPYRGRCAVFSITGLVVVVAEQpPGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEI 557
|
570
....*....|....
gi 226823266 1323 RDSFLADQLDPIYV 1336
Cdd:cd05905 558 RQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
119-695 |
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: 681.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 119 CLTGLDVTGKPVYTLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPnnDPVMFMVAFYGCLLAEVIPVPIEV 198
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 199 PLtrkdaGGQQIGFLLGSCGIALALTSEICLKGLPKT-----QNGEIVQFKGWPRLKWVVTDSKYLSKPPKDWQPHISPA 273
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 274 GTEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVM 353
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 354 KTCPLSWVQRVHAHKAKVALVKCRDLHWAMM------AHRDQRDVSLSSLRMLIVTDGaNPWSVSSCDAFLSLFQSHGLK 427
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKdlsstlASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 428 PEAIcpcatSAEAMTVAIRRPGVPGA--PLPGRAILSMNGLSYGVIRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGLP 505
Cdd:cd05905 307 PRAV-----STEFGTRVNPFICWQGTsgPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 506 qLCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVTSSGSPVGDVPFIRSGLLGFVGPGS----------LVFVVGK 575
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTKctdlnveehdLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 576 MDGLLMVSGRRHNADDIVATGLAVESiktvYRGRIAVFSVSvfydERIVVVAEQRPdASEEDSFQWMSRVLQAIDSIHQV 655
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 226823266 656 GVYCLALVPANTLPKTPLGGIHISQTKQLFLEGSLHPCNI 695
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
761-1294 |
1.10e-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: 232.90 E-value: 1.10e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 761 WRAQATPDHVLFMLLNAKGTTVCTASCLQLHKRAERIASVLgdKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTV 840
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 841 RPPHAqnlTATLPTVRMVVDVSKAACVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPRKRLPQLyKPPTPEMLAYL 920
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPP-PSPDPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 921 DFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPY--CGLGFALwcLCSVYSGHQSVLIPPMELENNLF 998
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLIGGL--LTPLYSGGPSVLMSPAAFLRRPL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 999 LWLATVNQYkiRDTFcsySVM-----ELCTKglgnQVEVLKTRGINLSCIRTCVVVAeERPRVSLQQSFSKLFKDIGLSP 1073
Cdd:cd05931 233 RWLRLISRY--RATI---SAApnfayDLCVR----RVRDEDLEGLDLSSWRVALNGA-EPVRPATLRRFAEAFAPFGFRP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1074 RAVSTTFG---SRVNVAIclqGTSGPDPTTVYVDLKSLRHDRVRLVERGAPQSLLLSeSGKILPGVKVVIVNPETKGPVG 1150
Cdd:cd05931 303 EAFRPSYGlaeATLFVSG---GPPGTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDQEVRIVDPETGRELP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1151 DSHLGEIWVNSPHTASGYYTiydSETLQADHFNTRLSFGDAAqtlWARTGYLGFVRRteltaatGErhdaLYVVGALDET 1230
Cdd:cd05931 379 DGEVGEIWVRGPSVASGYWG---RPEATAETFGALAATDEGG---WLRTGDLGFLHD-------GE----LYITGRLKDL 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226823266 1231 LELRGLRYHPIDIETSVSRVHRSIAE--CAVFTW----TNLLVVVVELcGSEQEALDLVPLVTNV---VLEEH 1294
Cdd:cd05931 442 IIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEV-ERGADPADLAAIAAAIraaVAREH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
109-686 |
1.08e-64 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 230.20 E-value: 1.08e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 109 RWGSTQAKCPCLTGLDVTGKPVYTLTYGKLWSRSLKLAYTLLnklgtknePVLKPGDRVALVYPNNdpVMFMVAFYGCLL 188
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAPPG--LDFVAAFLGCLY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 189 AEVIPVPIEVPLTRKDAggQQIGFLLGSCGIALALTSEICLKGLPKTqngeIVQFKGWPRLKWVVTDSKyLSKPPKDWQP 268
Cdd:cd05931 71 AGAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLL-PDTSAADWPP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 269 hISPAGTEPAYIEYkTSkeGSV---MGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMFANVMN---- 341
Cdd:cd05931 144 -PSPDPDDIAYLQY-TS--GSTgtpKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSggps 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 342 -KMHTISVpysVMKtcPLSWVQRVHAHKAKV------ALVKCrdlhwAMMAHRDQRD-VSLSSLRMLIVtdGANPWSVSS 413
Cdd:cd05931 220 vLMSPAAF---LRR--PLRWLRLISRYRATIsaapnfAYDLC-----VRRVRDEDLEgLDLSSWRVALN--GAEPVRPAT 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 414 CDAFLSLFQSHGLKPEAICPCATSAEAmTVAI---RRPGVPGAPLPGRAILSmnglsyGVIRVNTEDKNSALTVQDVGHV 490
Cdd:cd05931 288 LRRFAEAFAPFGFRPEAFRPSYGLAEA-TLFVsggPPGTGPVVLRVDRDALA------GRAVAVAADDPAARELVSCGRP 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 491 MPGGMMCIVKPDGLpQLCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVTSSGspvgdvPFIRSGLLGFVGPGSLv 570
Cdd:cd05931 361 LPDQEVRIVDPETG-RELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL- 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 571 FVVGKMDGLLMVSGRRHNADDIVATglAVESIKTVYRGRIAVFSVSVFYDERIVVVAEQRPDASEEDSFQWMSRVLQAID 650
Cdd:cd05931 433 YITGRLKDLIIVRGRNHYPQDIEAT--AEEAHPALRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVA 510
|
570 580 590
....*....|....*....|....*....|....*.
gi 226823266 651 SIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLFL 686
Cdd:cd05931 511 REHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
759-1234 |
2.19e-50 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 184.44 E-value: 2.19e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 759 LQWRAQATPDHVLFMllNAKGTTVctaSCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPV 838
Cdd:pfam00501 1 LERQAARTPDKTALE--VGEGRRL---TYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 839 TVRPphaqnlTATLPTVRMVVDVSKAACVLTTQTLmRLLKSREAAAAVDVKTWPAIIDTDDLPRKRL-----------PQ 907
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDDAL-KLEELLEALGKLEVVKLVLVLDRDPVLKEEPlpeeakpadvpPP 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 908 LYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCE----LYSSRQIAICLDPYCGLGFALWCLCSVYSGH 983
Cdd:pfam00501 148 PPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 984 QSVLIPPMELeNNLFLWLATVNQYKIRDTFCSYSVMELCtkglgnqVEVLKTRGINLSCIRTCVVVAeERPRVSLQQSFS 1063
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1064 KLFkdiglsPRAVSTTFGSRVNVAICLQGTSGPDPTTvyvdlkslrhdrvrlvergapqslLLSESGKILPGVKVVIVNP 1143
Cdd:pfam00501 299 ELF------GGALVNGYGLTETTGVVTTPLPLDEDLR------------------------SLGSVGRPLPGTEVKIVDD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1144 ETKGPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHFNTrlsfGDaaqtlWARTGYLGfvRRTEltaaTGErhdaLYV 1223
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAFDE----DG-----WYRTGDLG--RRDE----DGY----LEI 406
|
490
....*....|.
gi 226823266 1224 VGALDETLELR 1234
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 ... |
917-1281 |
5.90e-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: 137.03 E-value: 5.90e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 917 LAYLDFSVSTTGMLTGVKMSHSAVNALCRAIkLQCELYSSRQIAICLDPYC---GLGFALWCLcsvYSGHQSVLIPPMEL 993
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFhigGLFGLLGAL---LAGGTVVLLPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 994 EnnlfLWLATVNQYKIRDTFCSYSVMELCtkglgnqVEVLKTRGINLSCIRTCVVVAEERPRvSLQQSFSKLFKDI---- 1069
Cdd:cd04433 78 E----AALELIEREKVTILLGVPTLLARL-------LKAPESAGYDLSSLRALVSGGAPLPP-ELLERFEEAPGIKlvng 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1070 -GLSPRAVSTTFGSRVNVAIclqgtsgpDPTTVyvdlkslrhdrvrlvergapqslllsesGKILPGVKVVIVNPETkGP 1148
Cdd:cd04433 146 yGLTETGGTVATGPPDDDAR--------KPGSV----------------------------GRPVPGVEVRIVDPDG-GE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1149 VGDSHLGEIWVNSPHTASGYYTIYDsetlqadhfNTRLSFGDAaqtlWARTGYLGFVRrteltaatgeRHDALYVVGALD 1228
Cdd:cd04433 189 LPPGEIGELVVRGPSVMKGYWNNPE---------ATAAVDEDG----WYRTGDLGRLD----------EDGYLYIVGRLK 245
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*...
gi 226823266 1229 ETLELRGLRYHPIDIETSVSRvHRSIAECAVF-----TWTNLLVVVVELCGSEQEALD 1281
Cdd:cd04433 246 DMIKSGGENVYPAEVEAVLLG-HPGVAEAAVVgvpdpEWGERVVAVVVLRPGADLDAE 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
755-1249 |
1.90e-32 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 138.38 E-value: 1.90e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 755 LAEILQWRAQATPDHVLFMLLNAKGTTVCTASCLQLHKRAERIASVLGDKGHLnaGDNVVLLYPPGIELIAAFYGCLYAG 834
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 835 CIPVTVRPP------HAQNLTAtlptvrmVVDVSKAACVLTTQTLMRLLKSREAAAAVDVKTWPAI--IDTDDLPRKRLP 906
Cdd:PRK05691 89 VIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANAPELLCVdtLDPALAEAWQEP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 907 QLykppTPEMLAYLDFSVSTTGMLTGVKMSHSAVNAlcraiklqCELYSSRQIAICLDP----------YCGLGFALWCL 976
Cdd:PRK05691 162 AL----QPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 977 CSVYSGHQSVLIPPmelenNLFL-----WLATVNQYkiRDT----------FCSYSVMELCTKGLgnqvevlktrgiNLS 1041
Cdd:PRK05691 230 QPIFSGVPCVLMSP-----AYFLerplrWLEAISEY--GGTisggpdfayrLCSERVSESALERL------------DLS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1042 CIRTCVVVAEERPRVSLqQSFSKLFKDIGLSPRAVSTTFGSRVNVAICLQGTSGPDPTTVYVDLKSLRHDRvrlVERGAP 1121
Cdd:PRK05691 291 RWRVAYSGSEPIRQDSL-ERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNR---AEPGTG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1122 QSLLlsESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTiyDSETlqadhfnTRLSFGDAAQTLWARTGY 1201
Cdd:PRK05691 367 SVLM--SCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR--NPEA-------SAKTFVEHDGRTWLRTGD 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 226823266 1202 LGFVRRTEltaatgerhdaLYVVGALDETLELRGLRYHPIDIETSVSR 1249
Cdd:PRK05691 436 LGFLRDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVER 472
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
132-676 |
3.71e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 130.83 E-value: 3.71e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 132 TLTYGKLWSRSLKLAYTLlNKLGTknepvlkPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLTRkdAGGQQIG 211
Cdd:PRK05850 35 TLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQG--LEYIVAFLGALQAGLIAVPLSVPQGG--AHDERVS 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 212 FLLGSCGIALALT-SEIClkglpktqnGEIVQF----KGWPRLKWVVTDSKYLSKPPKdwqPHISPAG-TEPAYIEYkTS 285
Cdd:PRK05850 103 AVLRDTSPSVVLTtSAVV---------DDVTEYvapqPGQSAPPVIEVDLLDLDSPRG---SDARPRDlPSTAYLQY-TS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 286 keGSV---MGVTVSRLAMLSQC-QALSQACNYSEGE-----TVVNVLDFKKDAGLWHGMFANVMNKMHTI-SVPYSVMKT 355
Cdd:PRK05850 170 --GSTrtpAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSWLPFYHDMGLVLGVCAPILGGCPAVlTSPVAFLQR 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 356 cPLSWVQRV----HAHKA------KVALVKCRDlhwAMMAHRDQRDVslsslrmLIVTDGANPWSVSSCDAFLSLFQSHG 425
Cdd:PRK05850 248 -PARWMQLLasnpHAFSAapnfafELAVRKTSD---DDMAGLDLGGV-------LGIISGSERVHPATLKRFADRFAPFN 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 426 LKPEAICPCATSAEAMT-VAIRRPGVPgaplPGRAILSMNGLSYGVIRVNTEDKNSALtvqdVGHVMP-GGMMCIVKPDG 503
Cdd:PRK05850 317 LRETAIRPSYGLAEATVyVATREPGQP----PESVRFDYEKLSAGHAKRCETGGGTPL----VSYGSPrSPTVRIVDPDT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 504 LPQlCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEVIPVT-SSGSPVGdvPFIRSGLLGFVGPGSLvFVVGKMDGLLMV 582
Cdd:PRK05850 389 CIE-CPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATLVDpSPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 583 SGRRHNADDIVATglavesIKTVYRGRIAVFSVSVFYDERIVVVAE-QRPDASEEDSFQWM----SRVLQAIDSIHQVGV 657
Cdd:PRK05850 465 DGRNHYPDDIEAT------IQEITGGRVAAISVPDDGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSV 538
|
570
....*....|....*....
gi 226823266 658 YCLALVPANTLPKTPLGGI 676
Cdd:PRK05850 539 ADLVLVAPGSIPITTSGKI 557
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
133-692 |
3.99e-31 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 130.51 E-value: 3.99e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 133 LTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVyPNNDPvMFMVAFYGCLLAEVIPVPIEVP--LTRKDAGGQQI 210
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLA-LG------LKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPmgFGGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 211 GFLLGSCGIALALTSEICLKGLPKTQNGEivqfkgwpRLKWVVTDSKYLSKPPKDWQ-PHISPagTEPAYIEYkTSkeGS 289
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGN--------PLLHVLSHAWFKALPEADVAlPRPTP--DDIAYLQY-SS--GS 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 290 V---MGVTVSRLAMLSQCQALSQ-ACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMhtiSVPYsvMKTC-----PLSW 360
Cdd:PRK09192 188 TrfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQL---SVDY--LPTRdfarrPLQW 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 361 VQRVHAHKAKVA--------LVKCRdlhwamMAHRDQRDVSLSSLRmlIVTDGANPWSVSSCDAFLSLFQSHGLKPEAIC 432
Cdd:PRK09192 263 LDLISRNRGTISysppfgyeLCARR------VNSKDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 433 PCATSAEAmTVAIrrpgvpgaplpgrailSMNGLSYGvIRVNT------EDKNSALTVQD----------VGHVMPGGMM 496
Cdd:PRK09192 335 PSYGLAEA-TLAV----------------SFSPLGSG-IVVEEvdrdrlEYQGKAVAPGAetrrvrtfvnCGKALPGHEI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 497 CIVKPDG--LPQLcrtdEIGEICVssRTGGMM--YFGlagvTKNTFEVIPVTSsgspvgdvpFIRSGLLGFVGPGSLVfV 572
Cdd:PRK09192 397 EIRNEAGmpLPER----VVGHICV--RGPSLMsgYFR----DEESQDVLAADG---------WLDTGDLGYLLDGYLY-I 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 573 VGKMDGLLMVSGRRHNADDIvatGLAVESIKTVYRGRIAVFSVSVFYDERIVVVAEQRPdASEEDSFQWMSRVLQAIDSI 652
Cdd:PRK09192 457 TGRAKDLIIINGRNIWPQDI---EWIAEQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSE 532
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 226823266 653 HqvGVYCL-ALVPANTLPKTPLGGIHISQTKQLFLEGSLHP 692
Cdd:PRK09192 533 F--GVEAAvELVPPHSLPRTSSGKLSRAKAKKRYLSGAFAS 571
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
123-690 |
3.87e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 127.92 E-value: 3.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 123 LDVTGK----PVYTLT-YGKLWSRSL--KLAYTLLN---------------KLGTKN-------EPVLKPGDRVALVYPN 173
Cdd:PRK07769 9 FDVNGKirfpPNTNLVrHVERWAKVRgdKLAYRFLDfsterdgvardltwsQFGARNravgarlQQVTKPGDRVAILAPQ 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 174 NdpVMFMVAFYGCLLAEVIPVPIEVPltrkDAGGQ--QIGFLLGSCGIALALTSEIC-------LKGLPKTQNgeivqfk 244
Cdd:PRK07769 89 N--LDYLIAFFGALYAGRIAVPLFDP----AEPGHvgRLHAVLDDCTPSAILTTTDSaegvrkfFRARPAKER------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 245 gwPRLKWV--VTDSKYLSkppkdWQPhISPAGTEPAYIEYkTSkeGSV---MGVTVSRLAMLSQCQALSQACNYSEGETV 319
Cdd:PRK07769 156 --PRVIAVdaVPDEVGAT-----WVP-PEANEDTIAYLQY-TS--GSTripAGVQITHLNLPTNVLQVIDALEGQEGDRG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 320 VNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVMKTcPLSWVQRVHA------------------HKAKVALVKcrdlhw 381
Cdd:PRK07769 225 VSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRR-PGRWIRELARkpggtggtfsaapnfafeHAAARGLPK------ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 382 ammahRDQRDVSLSSLRMLIvtDGANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAmTVAIRRPGVPGAPlpgRAI- 460
Cdd:PRK07769 298 -----DGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEA-TLFVSTTPMDEEP---TVIy 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 461 LSMNGLSYG-VIRVNTEDKNsALTVQDVGHVMPGGMMCIVKPDGLPQLcRTDEIGEICVSSRTGGMMYFGLAGVTKNTFE 539
Cdd:PRK07769 367 VDRDELNAGrFVEVPADAPN-AVAQVSAGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFQ 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 540 VI------PVTSSGSPvGDVPFIRSGLLGFVGPGSLvFVVGKMDGLLMVSGRRHNADDIVATglAVESIKTVYRGRIAVF 613
Cdd:PRK07769 445 NIlksrlsESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYT--AQEATKALRTGYVAAF 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 614 SV-------SVFYD-------------ERIVVVAEQRPDASEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPL 673
Cdd:PRK07769 521 SVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSS 600
|
650
....*....|....*..
gi 226823266 674 GGIHISQTKQLFLEGSL 690
Cdd:PRK07769 601 GKIARRACRAAYLDGSL 617
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
100-688 |
5.92e-29 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 123.55 E-value: 5.92e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 100 PPALESALQRWgSTQAKCPCLTGLDVTGkPVYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNDPvmF 179
Cdd:cd05906 9 PRTLLELLLRA-AERGPTKGITYIDADG-SEEFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDDNED--F 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 180 MVAFYGCLLAEVIPVPIEVPLTRKDAGGQ-----QIGFLLGSCGIalaLTSEICLKGLPKtqngeivQFKGWPRLKWVVT 254
Cdd:cd05906 78 IPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSPVV---LTDAELVAEFAG-------LETLSGLPGIRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 255 DSKYLSKPPKDWQPHISPAGTePAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHG 334
Cdd:cd05906 148 SIEELLDTAADHDLPQSRPDD-LALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 335 MFANVMNKMHTISVPYSVMKTCPLSWVQRVHAHKAKV------ALVKCRDLhwamMAHRDQRDVSLSSLRMLIVtdGANP 408
Cdd:cd05906 227 HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLNDL----LEEIEDGTWDLSSLRYLVN--AGEA 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 409 WSVSSCDAFLSLFQSHGLKPEAICPCATSAEamTVAirrpgvpgaplpgrailsmnglsyGVI---RVNTEDKNSALTVQ 485
Cdd:cd05906 301 VVAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS------------------------GVIysrSFPTYDHSQALEFV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 486 DVGHVMPGGMMCIVKPDGlpQLCRTDEIGEICVS--SRTGGmmYFGLAGVTKNTFevipvTSSGspvgdvpFIRSGLLGF 563
Cdd:cd05906 355 SLGRPIPGVSMRIVDDEG--QLLPEGEVGRLQVRgpVVTKG--YYNNPEANAEAF-----TEDG-------WFRTGDLGF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 564 VGPGSLVFvVGKMDGLLMVSGRRHNADDIVAtglAVESIKTVYRGRIAVFSVsvfYD-----ERIVVVAeqrpdASEEDS 638
Cdd:cd05906 419 LDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAV---RDpgaetEELAIFF-----VPEYDL 486
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 226823266 639 FQWMSRVLQAIDSI--HQVGVYCLALVP--ANTLPKTPLGGIHISQTKQLFLEG 688
Cdd:cd05906 487 QDALSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
759-1290 |
1.05e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 120.05 E-value: 1.05e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 759 LQWRAQATPDHVLFMLLNAKGTTVCTASCL---QLHKRAERIASVLgdKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGC 835
Cdd:PRK05850 7 LRERASLQPDDAAFTFIDYEQDPAGVAETLtwsQLYRRTLNVAEEL--RRHGSTGDRAVILAPQGLEYIVAFLGALQAGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 836 IPVTVRPPHAqnlTATLPTVRMVVDVSKAACVLTTqtlmrllksreAAAAVDVKTW---------PAII--DTDDLPRKR 904
Cdd:PRK05850 85 IAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTT-----------SAVVDDVTEYvapqpgqsaPPVIevDLLDLDSPR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 905 LPQLYKPPTPEMlAYLDFSVSTTGMLTGVKMSHSAVNALCRaiKLQCELYSSRQIAICLD-------P-YCGLGFALWCL 976
Cdd:PRK05850 151 GSDARPRDLPST-AYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMGLVLGVC 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 977 CSVYSGHQSVLIPPMElennlFL-----W---LATVNQykirdtfcSYSV-----MELCTKglgnqvevlKTR-----GI 1038
Cdd:PRK05850 228 APILGGCPAVLTSPVA-----FLqrparWmqlLASNPH--------AFSAapnfaFELAVR---------KTSdddmaGL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1039 NLSCIRTcVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFG---SRVNVAIclqGTSGPDPTTVYVDLKSLRHDRVR- 1114
Cdd:PRK05850 286 DLGGVLG-IISGSERVHPATLKRFADRFAPFNLRETAIRPSYGlaeATVYVAT---REPGQPPESVRFDYEKLSAGHAKr 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1115 --------LVERGAPQSLLlsesgkilpgvkVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTiYDSETLQAdhFNTRL 1186
Cdd:PRK05850 362 cetgggtpLVSYGSPRSPT------------VRIVDPDTCIECPAGTVGEIWVHGDNVAAGYWQ-KPEETERT--FGATL 426
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1187 ---SFGDAAQTlWARTGYLGFVrrteltaATGErhdaLYVVGALDETLELRGLRYHPIDIETSVSRVHRsiAECAVFT-- 1261
Cdd:PRK05850 427 vdpSPGTPEGP-WLRTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATIQEITG--GRVAAISvp 492
|
570 580 590
....*....|....*....|....*....|....
gi 226823266 1262 --WTNLLVVVVEL---CGSEQEALDLVPLVTNVV 1290
Cdd:PRK05850 493 ddGTEKLVAIIELkkrGDSDEEAMDRLRTVKREV 526
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
132-690 |
1.29e-26 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 114.91 E-value: 1.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 132 TLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNDPvmFMVAFYGCLLAEVIPVPIEVPLTRKdaggqQIG 211
Cdd:COG0318 24 RLTYAELDARARRLA-AALRALG------VGPGDRVALLLPNSPE--FVVAFLAALRAGAVVVPLNPRLTAE-----ELA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 212 FLLGSCGIALALTSEICL----KGLPKtqngeivqfkgwprlkwvvtdskylskppkdwqphispagtepayieyktske 287
Cdd:COG0318 90 YILEDSGARALVTALILYtsgtTGRPK----------------------------------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 288 gsvmGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMHTISVPysvmKTCPLSWVQRVHAH 367
Cdd:COG0318 117 ----GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP----RFDPERVLELIERE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 368 KA-KVALVKcrDLHWAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLSLFQShglkpeAICPCATSAEAMTVAIR 446
Cdd:COG0318 189 RVtVLFGVP--TMLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFEERFGV------RIVEGYGLTETSPVVTV 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 447 RPGVPGAPLPGRailsmnglsygvirvntedknsaltvqdVGHVMPGGMMCIVKPDGLPqlCRTDEIGEICVssRTGGMM 526
Cdd:COG0318 259 NPEDPGERRPGS----------------------------VGRPLPGVEVRIVDEDGRE--LPPGEVGEIVV--RGPNVM 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 527 --YFGLAGVTKNTFEvipvtssgspvgDvPFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIKT 604
Cdd:COG0318 307 kgYWNDPEATAEAFR------------D-GWLRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAE 373
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 605 VyrgriAVFSV-SVFYDERIV--VVAEQRPDASEEDSFQWMSRVL---QAIDSIHQVGvyclalvpanTLPKTPLGGIHI 678
Cdd:COG0318 374 A-----AVVGVpDEKWGERVVafVVLRPGAELDAEELRAFLRERLaryKVPRRVEFVD----------ELPRTASGKIDR 438
|
570
....*....|..
gi 226823266 679 SQTKQLFLEGSL 690
Cdd:COG0318 439 RALRERYAAGAL 450
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
755-1272 |
8.60e-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: 112.60 E-value: 8.60e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 755 LAEILQWRAQATPDHVLfmlLNAKGTTVctaSCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 834
Cdd:COG0318 1 LADLLRRAAARHPDRPA---LVFGGRRL---TYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 835 CIPVTVrpphaqNLTATLPTVRMVVDVSKAACVLTtqtlmrllksreaaaavdvktwpaiidtddlprkrlpqlykpptp 914
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 915 emlAYLDFSvS-TTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMEL 993
Cdd:COG0318 103 ---ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRFDP 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 994 ENnlflWLATVNQYKIrdTFCSYS---VMELCtkglgnqvEVLKTRGINLSCIRTCVVVAeERPRVSLQQSFSKLFKdig 1070
Cdd:COG0318 179 ER----VLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLRLVVSGG-APLPPELLERFEERFG--- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1071 lspRAVSTTFGSrvnvaiclqgT-SGPdptTVYVDLKSLRHDRVRLVergapqslllsesGKILPGVKVVIVNPETKgPV 1149
Cdd:COG0318 241 ---VRIVEGYGL----------TeTSP---VVTVNPEDPGERRPGSV-------------GRPLPGVEVRIVDEDGR-EL 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1150 GDSHLGEIWVNSPHTASGYYTiyDSETlqadhfnTRLSFGDAaqtlWARTGYLGFVRrteltaATGErhdaLYVVGALDE 1229
Cdd:COG0318 291 PPGEVGEIVVRGPNVMKGYWN--DPEA-------TAEAFRDG----WLRTGDLGRLD------EDGY----LYIVGRKKD 347
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 226823266 1230 TLELRGLRYHPIDIETSVSRvHRSIAECAVF-----TWTNLLVVVVEL 1272
Cdd:COG0318 348 MIISGGENVYPAEVEEVLAA-HPGVAEAAVVgvpdeKWGERVVAFVVL 394
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
123-692 |
3.17e-23 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 106.36 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 123 LDVTGKP---VYTLTYGKLWSRslklaytlLNKLGTKNEPVLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPI--- 196
Cdd:PRK12476 56 LDHSHSAagcAVELTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLfap 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 197 EVP--LTRKDAggqqigfLLGSCGIALALTSeiclkglpkTQNGEIVQfkgwprlkwvvtdsKYLSKPPKDWQPHI---- 270
Cdd:PRK12476 126 ELPghAERLDT-------ALRDAEPTVVLTT---------TAAAEAVE--------------GFLRNLPRLRRPRViaid 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 271 -----SPAGTEP--------AYIEYKTSKEGSVMGVTVS-RLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHGMF 336
Cdd:PRK12476 176 aipdsAGESFVPveldtddvSHLQYTSGSTRPPVGVEIThRAVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 337 ANVMNKMHTISVPYSVMKTcPLSWVQRVHAHKAKVALVKCR-DLHWAMMAHR----DQRDVSLSSLRMLIvtdGANPWSV 411
Cdd:PRK12476 256 PAVYGGHSTLMSPTAFVRR-PQRWIKALSEGSRTGRVVTAApNFAYEWAAQRglpaEGDDIDLSNVVLII---GSEPVSI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 412 SSCDAFLSLFQSHGLKPEAICPCATSAEA-MTVAIRRPgvpgAPLPGRAILSMNGLSYG-VIRVNTEDKNSALTVQdVGH 489
Cdd:PRK12476 332 DAVTTFNKAFAPYGLPRTAFKPSYGIAEAtLFVATIAP----DAEPSVVYLDREQLGAGrAVRVAADAPNAVAHVS-CGQ 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 490 VMPGGMMCIVKPDGLPQLcRTDEIGEICVSSRTGGMMYFGLAGVTKNTFEV-----IPVTS--SGSPVGDVpFIRSGLLG 562
Cdd:PRK12476 407 VARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGShaDGAADDGT-WLRTGDLG 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 563 FVGPGSLvFVVGKMDGLLMVSGRRHNADDIVATglAVESIKTVYRGRIAVFSVSVFYDERIVVVAEQRPDASEEDSFQWM 642
Cdd:PRK12476 485 VYLDGEL-YITGRIADLIVIDGRNHYPQDIEAT--VAEASPMVRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAI 561
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|
gi 226823266 643 SRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLFLEGSLHP 692
Cdd:PRK12476 562 DAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
131-593 |
3.99e-23 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 103.93 E-value: 3.99e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 131 YTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVpltrkDAGGQQI 210
Cdd:pfam00501 20 RRLTYRELDERANRLAAGLR-ALG------VGKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPLNP-----RLPAEEL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 211 GFLLGSCGIALALTSEI--------CLKGLPKTQNGEIVQFKGWPRLKWVVTDSKYLSKPPKdwqPHISPAGTEPAYIEY 282
Cdd:pfam00501 86 AYILEDSGAKVLITDDAlkleelleALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPP---PPPPPDPDDLAYIIY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 283 kTS------KegsvmGVTVSRLAMLSQCQALSQAC----NYSEGETVVNVLDFKKDAGLWHGMFANVMNKMhTISVPYSV 352
Cdd:pfam00501 163 -TSgttgkpK-----GVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA-TVVLPPGF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 353 MKTCPLSWVQRVHAHKAKV-----ALVKcrdlhwAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLSLFqshglk 427
Cdd:pfam00501 236 PALDPAALLELIERYKVTVlygvpTLLN------MLLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF------ 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 428 peaicpcatsaeamtvairrpgvpgaplpGRAILSMNGLS--YGVIRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGLp 505
Cdd:pfam00501 302 -----------------------------GGALVNGYGLTetTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDETG- 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 506 QLCRTDEIGEICVSSRTGGMMYFGLAGVTKNTFevipvTSSGspvgdvpFIRSGLLGFVGPgslvfvvgkmDGLLMVSGR 585
Cdd:pfam00501 352 EPVPPGEPGELCVRGPGVMKGYLNDPELTAEAF-----DEDG-------WYRTGDLGRRDE----------DGYLEIVGR 409
|
....*...
gi 226823266 586 rhnADDIV 593
Cdd:pfam00501 410 ---KKDQI 414
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
789-1269 |
3.42e-22 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 102.36 E-value: 3.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTAtlPTVRMVVDVSK---AA 865
Cdd:cd05906 44 DLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTYDEPN--ARLRKLRHIWQllgSP 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 866 CVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPrkRLPQLYkPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCR 945
Cdd:cd05906 121 VVLTDAELVAEFAGLETLSGLPGIRVLSIEELLDTA--ADHDLP-QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSA 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 946 AiKLQCELYSSRQIA---ICLDPYCGLGFalwC-LCSVYSGHQSVLIPPMELENNLFLWLATVNQYKIRDTFCSYSvmeL 1021
Cdd:cd05906 198 G-KIQHNGLTPQDVFlnwVPLDHVGGLVE---LhLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---A 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1022 CTKgLGNQVEVLKTRGINLSCIRtCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGSRVNVAIClqgtsgpdptTV 1101
Cdd:cd05906 271 FAL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCSGV----------IY 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1102 YVDLKSLRHD-RVRLVERGAPqslllsesgkiLPGVKVVIVNPETKGpVGDSHLGEIWVNSPHTASGYytiYDSETLQAD 1180
Cdd:cd05906 339 SRSFPTYDHSqALEFVSLGRP-----------IPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGY---YNNPEANAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1181 HFntrLSFGdaaqtlWARTGYLGFVRRTELTaATGERHDALYVvgaldetlelRGLRYHPIDIETSVSRV----HRSIAE 1256
Cdd:cd05906 404 AF---TEDG------WFRTGDLGFLDNGNLT-ITGRTKDTIIV----------NGVNYYSHEIEAAVEEVpgvePSFTAA 463
|
490
....*....|....*.
gi 226823266 1257 CAVF---TWTNLLVVV 1269
Cdd:cd05906 464 FAVRdpgAETEELAIF 479
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
810-1248 |
4.99e-22 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 102.51 E-value: 4.99e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 810 GDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPP----HAQNLTATL----PTVrmvvdvskaacVLTTQTLMRLLksRE 881
Cdd:PRK12476 92 GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV-----------VLTTTAAAEAV--EG 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 882 AAAAVDVKTWPAIIDTDDLPrKRLPQLYKPPTPEM--LAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSsRQI 959
Cdd:PRK12476 159 FLRNLPRLRRPRVIAIDAIP-DSAGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLD-RNT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 960 AIC--LDPYCGLGFALWCLCSVYSGHqSVLIPPMELENNLFLWL-ATVNQYKIRDTFCSYS--VMELCT-KGLGNQVEvl 1033
Cdd:PRK12476 237 HGVswLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWIkALSEGSRTGRVVTAAPnfAYEWAAqRGLPAEGD-- 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1034 ktrGINLSciRTCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGsrVNVAICLQGTSGPD--PTTVYVDLKSLRHD 1111
Cdd:PRK12476 314 ---DIDLS--NVVLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG--IAEATLFVATIAPDaePSVVYLDREQLGAG 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1112 RVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTI-YDSETLQADHFNTRLSFGD 1190
Cdd:PRK12476 387 RAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRpEETERTFGAKLQSRLAEGS 466
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226823266 1191 -----AAQTLWARTGYLGFVRRTEltaatgerhdaLYVVGALDETLELRGLRYHPIDIETSVS 1248
Cdd:PRK12476 467 hadgaADDGTWLRTGDLGVYLDGE-----------LYITGRIADLIVIDGRNHYPQDIEATVA 518
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
810-1248 |
5.24e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 99.42 E-value: 5.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 810 GDNVVLLYPPGIELIAAFYGCLYAGCIPVTV----RPPHAQNLTAtlptvrmVVDVSKAACVLTT----QTLMRLLKSRE 881
Cdd:PRK07769 79 GDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHA-------VLDDCTPSAILTTtdsaEGVRKFFRARP 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 882 AaaavdvKTWPAIIDTDDLPRKrLPQLYKPPTP--EMLAYLDFSVSTTGMLTGVKMSHSAV--NAL--CRAIKLQcelYS 955
Cdd:PRK07769 152 A------KERPRVIAVDAVPDE-VGATWVPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLptNVLqvIDALEGQ---EG 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 956 SRQIAiCLDPYCGLGFaLWCLCSVYSGHQSVLIPPMELENNLFLW---LATVNQykirDTFCSYSV-----MELCT-KGL 1026
Cdd:PRK07769 222 DRGVS-WLPFFHDMGL-ITVLLPALLGHYITFMSPAAFVRRPGRWireLARKPG----GTGGTFSAapnfaFEHAAaRGL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1027 GNQVEvlktRGINLSCIRtCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFGsrVNVAICLQGTSGPD--PTTVYVD 1104
Cdd:PRK07769 296 PKDGE----PPLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYG--MAEATLFVSTTPMDeePTVIYVD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1105 LKSLRHDRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYYTIYDsETLQADH--F 1182
Cdd:PRK07769 369 RDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPE-ETAATFQniL 447
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1183 NTRLS----FGDAAQTLWARTGYLGfvrrtelTAATGErhdaLYVVGALDETLELRGLRYHPIDIETSVS 1248
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 ... |
789-1260 |
4.86e-20 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 95.36 E-value: 4.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnlTATLPTVRMVVDVSKAACVL 868
Cdd:cd05911 15 QLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANP------IYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 869 TT-QTLMRLLKSREAAAAVD--------VKTWPAIIDTDDLPRKRLPQLYKPP---TPEMLAYLDFSVSTTGMLTGVKMS 936
Cdd:cd05911 88 TDpDGLEKVKEAAKELGPKDkiivlddkPDGVLSIEDLLSPTLGEEDEDLPPPlkdGKDDTAAILYSSGTTGLPKGVCLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 937 HS---AVNALCRAIKLQCELYSSRQIA-ICLDPYCGLgfaLWCLCSVYSGHQSVLIPPMELEnnlfLWLATVNQYKIRDT 1012
Cdd:cd05911 168 HRnliANLSQVQTFLYGNDGSNDVILGfLPLYHIYGL---FTTLASLLNGATVIIMPKFDSE----LFLDLIEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1013 FCSYSVMELctkgLGNQVEVLKtrgINLSCIRTCVVVAEerprvSLQQSFSKLFKdiglspravsttfgSRVNVAICLQG 1092
Cdd:cd05911 241 YLVPPIAAA----LAKSPLLDK---YDLSSLRVILSGGA-----PLSKELQELLA--------------KRFPNATIKQG 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1093 -----TSGPDPTTVYVDLKSlrhdrvrlverGApqslllseSGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASG 1167
Cdd:cd05911 295 ygmteTGGILTVNPDGDDKP-----------GS--------VGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVMKG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1168 YYtiydsetlqadhfntrlsfGDAAQTL-------WARTGYLGFVRRTELtaatgerhdaLYVVGALDETLELRGLRYHP 1240
Cdd:cd05911 356 YY-------------------NNPEATKetfdedgWLHTGDIGYFDEDGY----------LYIVDRKKELIKYKGFQVAP 406
|
490 500
....*....|....*....|
gi 226823266 1241 IDIEtSVSRVHRSIAECAVF 1260
Cdd:cd05911 407 AELE-AVLLEHPGVADAAVI 425
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
789-1259 |
1.31e-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: 93.10 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltaTLPT--VRMVVDVSKAAC 866
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDP--------AYPAerLAFILEDAGARL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 867 VLTTQTLmRLLKSREAAAAVDVKTWPAIIDTDDLPrkrLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 946
Cdd:TIGR01733 76 LLTDSAL-ASRLAGLVLPVILLDPLELAALDDAPA---PPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAW 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 947 IKlQCELYSSRQIAICLDPYCGLGFA---LWCLcsvYSGHQSVLIPPMELENNLFLWLATVNQYKIRDTFCSYSVMELCt 1023
Cdd:TIGR01733 152 LA-RRYGLDPDDRVLQFASLSFDASVeeiFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1024 kglgnqvevLKTRGINLSCIRTCVVVAEErprvslqqsfsklfkdigLSPRAVSTTFGSRVNVAIClqGTSGPDPTTVYV 1103
Cdd:TIGR01733 227 ---------AAALPPALASLRLVILGGEA------------------LTPALVDRWRARGPGARLI--NLYGPTETTVWS 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1104 DlkslrhdrVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHFN 1183
Cdd:TIGR01733 278 T--------ATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---LNRPELTAERFV 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 226823266 1184 TRLsFGDAAQTLWARTGYLgfVRRteltaatgeRHD-ALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECAV 1259
Cdd:TIGR01733 346 PDP-FAGGDGARLYRTGDL--VRY---------LPDgNLEFLGRIDDQVKIRGYRIELGEIEAALLR-HPGVREAVV 409
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
150-674 |
1.69e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 90.63 E-value: 1.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 150 LNKLGTKNEPVLKPGDRVALVYPNNDPvmFMVAFYGCLLAEVIPVPIEVpltrkdagGQQIGFLLGScgialaltseicl 229
Cdd:cd05908 26 LGYLGALQELGIKPGQEVVFQITHNNK--FLYLFWACLLGGMIAVPVSI--------GSNEEHKLKL------------- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 230 kglpktqngeivqFKGWPRLK--WVVTDSKYLSKPPKdwqphispagtEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQAL 307
Cdd:cd05908 83 -------------NKVWNTLKnpYLITEEEVLCELAD-----------ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 308 SQACNYSEGETVVNVLDFKKDAGLWHGMFANVMNKMHTISVPYSVMKTCPLSWVQRVHAHKAKValVKCRDLHWAMMAHR 387
Cdd:cd05908 139 LNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATI--VSSPNFGYKYFLKT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 388 ----DQRDVSLSSLRMLIvtDGANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAmTVAIRRP--GVPGAPLpgraIL 461
Cdd:cd05908 217 lkpeKANDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA-SVGASLPkaQSPFKTI----TL 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 462 SMNGLSYGVIRVNTEDKNS-ALTVQDVGHVMPGGMMCIVKPD--GLPQlcrtDEIGEICVSSRTGGMMYFGLAGVTKNTF 538
Cdd:cd05908 290 GRRHVTHGEPEPEVDKKDSeCLTFVEVGKPIDETDIRICDEDnkILPD----GYIGHIQIRGKNVTPGYYNNPEATAKVF 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 539 evipvTSSGspvgdvpFIRSGLLGFVGPGSLVfVVGKMDGLLMVSGRRHNADDIVATGLAVESIKTvyrGRIAVFSV--S 616
Cdd:cd05908 366 -----TDDG-------WLKTGDLGFIRNGRLV-ITGREKDIIFVNGQNVYPHDIERIAEELEGVEL---GRVVACGVnnS 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226823266 617 VFYDERIVVVAEQRpdASEEDSFQWMSRVLQAID-----SIHQVgvyclalVPANTLPKTPLG 674
Cdd:cd05908 430 NTRNEEIFCFIEHR--KSEDDFYPLGKKIKKHLNkrggwQINEV-------LPIRRIPKTTSG 483
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
100-720 |
7.38e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 87.15 E-value: 7.38e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 100 PPALESALQRWGSTQAKCPCLTGLDVTGKPVYTLTYGKLWSRSLKLAYTLLNKLGtknepvlkPGDRVALVYPNNdpVMF 179
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS--------FGDRAVLLFPSG--PDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 180 MVAFYGCLLAEVIPVPIEVPLTRKDAGGQQIGFLLGSCGIALALTSEICLKGLpktQNGEIVQFKGWPRLKWVVTdskYL 259
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL---LQMEELAAANAPELLCVDT---LD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 260 SKPPKDWQ-PHISPagTEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQ--ACNYSEGETVVNVLDFKKDAGLWHGMF 336
Cdd:PRK05691 152 PALAEAWQePALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHgfGIDLNPDDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 337 ANVMNkmhtiSVPYSVMKTC-----PLSWVQRVHAHKAKVAlvKCRDLHWAMMAHRdqrdVSLSSLRML------IVTDG 405
Cdd:PRK05691 230 QPIFS-----GVPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER----VSESALERLdlsrwrVAYSG 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 406 ANPWSVSSCDAFLSLFQSHGLKPEAICPCATSAEAMTVairrpgVPGAPlPGRAILSMNgLSYGVIRVNTEDKNSALTVQ 485
Cdd:PRK05691 299 SEPIRQDSLERFAEKFAACGFDPDSFFASYGLAEATLF------VSGGR-RGQGIPALE-LDAEALARNRAEPGTGSVLM 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 486 DVGHVMPGGMMCIVKPDGLPQLcRTDEIGEICVSSRTGGMMYFGLAGVTKNTFevipVTSSGSpvgdvPFIRSGLLGFVG 565
Cdd:PRK05691 371 SCGRSQPGHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGDLGFLR 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 566 PGSLvFVVGKMDGLLMVSGRRHNADDIVATglaVES-IKTVYRGRIAVFSVSVFYDERIVVVAE-----QRPDASEEdsf 639
Cdd:PRK05691 441 DGEL-FVTGRLKDMLIVRGHNLYPQDIEKT---VEReVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPPQA--- 513
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 640 qWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHISQTKQLFLEGSLhpcnilmcphTCVTNLPKPRQKQPGVGPA 719
Cdd:PRK05691 514 -LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYALFPALQAVEAAQTAA 582
|
.
gi 226823266 720 S 720
Cdd:PRK05691 583 S 583
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
789-1294 |
8.98e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 85.44 E-value: 8.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNltatlptvrmvvdvSKAACVl 868
Cdd:PRK09192 54 TLRARAEAGARRLLALG-LKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFG--------------GRESYI- 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 869 ttQTLMRLLKSREAAAAV---DVKTW---------------PAIIDTDDLPRKRLPqlykPPTPEMLAYLDFSVSTTGML 930
Cdd:PRK09192 118 --AQLRGMLASAQPAAIItpdELLPWvneathgnpllhvlsHAWFKALPEADVALP----RPTPDDIAYLQYSSGSTRFP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 931 TGVKMSHSAVNALCRAIKLQ-CELYSSRQIAICLDPYCGLGFaLWCLCSVYSGHQSV-LIPPMELENNLFLWLATVNqyK 1008
Cdd:PRK09192 192 RGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGL-VGFLLTPVATQLSVdYLPTRDFARRPLQWLDLIS--R 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1009 IRDTFcSYSV---MELCTKGLGNQVEVlktrGINLSCIRTCVVVAEE-RPRVslQQSFSKLFKDIGLSPRAVSTTFG-SR 1083
Cdd:PRK09192 269 NRGTI-SYSPpfgYELCARRVNSKDLA----ELDLSCWRVAGIGADMiRPDV--LHQFAEAFAPAGFDDKAFMPSYGlAE 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1084 VNVAIclqgtSGPDPTTvyvDLKSLRHDRVRLVERGA-----PQSLLLSE---SGKILPGVKVVIVNpETKGPVGDSHLG 1155
Cdd:PRK09192 342 ATLAV-----SFSPLGS---GIVVEEVDRDRLEYQGKavapgAETRRVRTfvnCGKALPGHEIEIRN-EAGMPLPERVVG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1156 EIWVNSPHTASGYYTiyDSETLQAdhfntrlsfgdAAQTLWARTGYLGFVrrteltaATGErhdaLYVVGALDETLELRG 1235
Cdd:PRK09192 413 HICVRGPSLMSGYFR--DEESQDV-----------LAADGWLDTGDLGYL-------LDGY----LYITGRAKDLIIING 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226823266 1236 LRYHPIDIETSVSRV----HRSIAECAVFTWTNLLVVVVELC--GSEQEALDLVPLVTNVVLEEH 1294
Cdd:PRK09192 469 RNIWPQDIEWIAEQEpelrSGDAAAFSIAQENGEKIVLLVQCriSDEERRGQLIHALAALVRSEF 533
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
789-1262 |
1.51e-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: 1.51e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVrpphaqNLTATLPTVRMVVDVSKAACVL 868
Cdd:cd05959 34 ELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPV------NTLLTPDDYAYYLEDSRARVVV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 869 TTQTLMRLLKSREAAAAVDVKT---------WPAIIDTDDLPRKRLPQLYKPPT-PEMLAYLDFSVSTTGMLTGVKMSHS 938
Cdd:cd05959 107 VSGELAPVLAAALTKSEHTLVVlivsggagpEAGALLLAELVAAEAEQLKPAAThADDPAFWLYSSGSTGRPKGVVHLHA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 939 AvnalcraIKLQCELYSSRQIAICLDPYC----------GLGFALWCLCSVysGHQSVLIPPMELENNLFlwlATVNQYK 1008
Cdd:cd05959 187 D-------IYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMPERPTPAAVF---KRIRRYR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1009 iRDTFcsYSVMELCTKGLGNqvEVLKTRgiNLSCIRTCVVVAEERPRvSLQQSFSKLFK-DIglspravsttfgsrvnva 1087
Cdd:cd05959 255 -PTVF--FGVPTLYAAMLAA--PNLPSR--DLSSLRLCVSAGEALPA-EVGERWKARFGlDI------------------ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1088 icLQGTSGPDPTTVYVdlkSLRHDRVRLverGApqslllseSGKILPGVKVVIVNpETKGPVGDSHLGEIWVNSPHTASG 1167
Cdd:cd05959 309 --LDGIGSTEMLHIFL---SNRPGRVRY---GT--------TGKPVPGYEVELRD-EDGGDVADGEPGELYVRGPSSATM 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1168 YYTIYDSetlqadhfnTRLSFgdaaQTLWARTGYlGFVRRTELTaatgerhdaLYVVGALDETLELRGLRYHPIDIEtSV 1247
Cdd:cd05959 372 YWNNRDK---------TRDTF----QGEWTRTGD-KYVRDDDGF---------YTYAGRADDMLKVSGIWVSPFEVE-SA 427
|
490
....*....|....*
gi 226823266 1248 SRVHRSIAECAVFTW 1262
Cdd:cd05959 428 LVQHPAVLEAAVVGV 442
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
161-674 |
1.17e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 71.70 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 161 LKPGDRVALVYPNNDP---VMFMVAFYGCLLAEVIpvpieVPLTrKDAGGQQIGFLLGSCGIALALTSEiclKGLPKTQN 237
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIVLADA---GAADRLRD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 238 GEIVQfkgwpRLKWVVTDSKYLSKPPKDWQPHIsPAGTEPAYIEYKTSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGE 317
Cdd:cd05922 86 ALPAS-----PDPGTVLDADGIRAARASAPAHE-VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 318 TVVNVLDFKKDAGLwhgmfaNVMNK---------MHTISVPysvmktcPLSWVQRVHAHKAK-VALVKCrdlHWAMMAHR 387
Cdd:cd05922 160 RALTVLPLSYDYGL------SVLNThllrgatlvLTNDGVL-------DDAFWEDLREHGATgLAGVPS---TYAMLTRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 388 DQRDVSLSSLRMLIVTDGANPwsvsscDAFLSLFqshglkpeaicpcatsAEAMtvairrpgvpgaplPGRAILSMNGLS 467
Cdd:cd05922 224 GFDPAKLPSLRYLTQAGGRLP------QETIARL----------------RELL--------------PGAQVYVMYGQT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 468 YGVIRVNTEDKNSALTVQD-VGHVMPGGMMCIVKPDGLPqlCRTDEIGEICVSSRTGGMMYFglagvtkNTFEVIPVTSS 546
Cdd:cd05922 268 EATRRMTYLPPERILEKPGsIGLAIPGGEFEILDDDGTP--TPPGEPGEIVHRGPNVMKGYW-------NDPPYRRKEGR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 547 GspvGDVpfIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIKTVyrgriAVFSVSVFYDERIVVV 626
Cdd:cd05922 339 G---GGV--LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA-----AAVGLPDPLGEKLALF 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 226823266 627 AEqrpdASEEDSFQWMSRVLQAIDSIHQVGVYClalVPANTLPKTPLG 674
Cdd:cd05922 409 VT----APDKIDPKDVLRSLAERLPPYKVPATV---RVVDELPLTASG 449
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
755-1169 |
1.18e-12 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 71.83 E-value: 1.18e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 755 LAEILQWRAQATPDHVLFMLLNAKGTTVctasclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 834
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYR------ELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 835 CIPVTVRPphaqnltatlptvrmvvdvskaacVLTTQTLMRLLKSREAAAAVDVKTWpaiidTDDLPRKRLPQLYKPPTP 914
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSF-----TDLLAAGAPLGERVALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 915 EMLAYLDFSVSTTGMLTGVKMSHSAV--NAL-CRAIkLQcELYSSRQIAICLDP-YCGLGFALWCLCSVYSGHQSVLIP- 989
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLvaNALqIKAW-LE-DLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLIPr 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 990 --PMELennlflwLATVNQYKIrDTFCS----YSvmelctkGLGNQVEVLKtrgINLSCIRTCVvvaeerprvslqqsfs 1063
Cdd:cd05936 203 frPIGV-------LKEIRKHRV-TIFPGvptmYI-------ALLNAPEFKK---RDFSSLRLCI---------------- 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1064 klfkdiglspravsttfgsrvnvaiclqgtSGPDPTTVYVDLKSLRHDRVRLVE-RGapqsllLSES------------- 1129
Cdd:cd05936 249 ------------------------------SGGAPLPVEVAERFEELTGVPIVEgYG------LTETspvvavnpldgpr 292
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 226823266 1130 -----GKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYY 1169
Cdd:cd05936 293 kpgsiGIPLPGTEVKIVDDDGE-ELPPGEVGELWVRGPQVMKGYW 336
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
763-1285 |
1.87e-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: 71.12 E-value: 1.87e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 763 AQATPDHVLFMllnAKGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGC--IPVTV 840
Cdd:cd05945 1 AAANPDRPAVV---EGGRTLTYR---ELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 841 RPPHAQnltatlptVRMVVDVSKAACVlttqtlmrllksreaaaavdvktwpaIIDTDDlprkrlpqlykpptpemLAYL 920
Cdd:cd05945 74 SSPAER--------IREILDAAKPALL--------------------------IADGDD-----------------NAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 921 DFSVSTTGMLTGVKMSHSAVNALCRAIkLQCELYSSRQIAIC----------LDPYCGL--GFALWCLcsvysghqsvli 988
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNqapfsfdlsvMDLYPALasGATLVPV------------ 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 989 pPMELENNLFLWLATVNQYKIRDTFCSYSVMELCTKGLGNQVEVLKTrginlscIRTCVVVAEERPRVSLQQSFSKLfkd 1068
Cdd:cd05945 170 -PRDATADPKQLFRFLAEHGITVWVSTPSFAAMCLLSPTFTPESLPS-------LRHFLFCGEVLPHKTARALQQRF--- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1069 iglsPRA-VSTTFGS-RVNVAIclqgtsgpdpTTVYVDLKSL-RHDRVRLvergapqslllsesGKILPGVKVVIVNPET 1145
Cdd:cd05945 239 ----PDArIYNTYGPtEATVAV----------TYIEVTPEVLdGYDRLPI--------------GYAKPGAKLVILDEDG 290
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1146 KgPVGDSHLGEIWVNSPHTASGYytiYDSETLQADHFntrlsFGDAAQTlWARTGYLGFVrrteltAATGErhdaLYVVG 1225
Cdd:cd05945 291 R-PVPPGEKGELVISGPSVSKGY---LNNPEKTAAAF-----FPDEGQR-AYRTGDLVRL------EADGL----LFYRG 350
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226823266 1226 ALDETLELRGLRYHPIDIETSVSRVHrSIAECAVFTWTNL-----LVVVVELCGSEqEALDLVPL 1285
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 ... |
789-1259 |
4.24e-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: 70.34 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLgDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnlTATLPTVRMVVDVSKAACVL 868
Cdd:cd05904 37 ELERRVRRLAAGL-AKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 869 TTQTLmrLLKSREAAAAV----DVKTWPAIIDTDDLPRKRLPqlykPPTPEM----LAYLDFSVSTTGMLTGVKMSH-SA 939
Cdd:cd05904 110 TTAEL--AEKLASLALPVvlldSAEFDSLSFSDLLFEADEAE----PPVVVIkqddVAALLYSSGTTGRSKGVMLTHrNL 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 940 VNALCRAIKLQCELYSSRQIAICLDPYCGL-GFALWCLCSVYSGHQSVLIPPMELENnlflWLATVNQYKIRDTFCSYSV 1018
Cdd:cd05904 184 IAMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERYKVTHLPVVPPI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1019 MelctKGLGNQVEVLKtrginlscirtcvvvaeeRPRVSLQQSFSklfkdiGLSP--RAVSTTFGSRVNVAICLQG---- 1092
Cdd:cd05904 260 V----LALVKSPIVDK------------------YDLSSLRQIMS------GAAPlgKELIEAFRAKFPNVDLGQGygmt 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1093 TSGPDPTTVYVDLKSLRHdrvrlvergapqsllLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYytiy 1172
Cdd:cd05904 312 ESTGVVAMCFAPEKDRAK---------------YGSVGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGY---- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1173 dsetlqadhfntrlsFGDAAQTL-------WARTGYLGFVRrteltaATGErhdaLYVVGALDETLELRGLRYHPIDIEt 1245
Cdd:cd05904 373 ---------------LNNPEATAatidkegWLHTGDLCYID------EDGY----LFIVDRLKELIKYKGFQVAPAELE- 426
|
490
....*....|....
gi 226823266 1246 SVSRVHRSIAECAV 1259
Cdd:cd05904 427 ALLLSHPEILDAAV 440
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
789-1264 |
7.20e-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: 7.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltaTLPTVRM--VVDVSKAAC 866
Cdd:cd05930 17 ELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDP--------SYPAERLayILEDSGAKL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 867 VLTtqtlmrllksreaaaavdvktwpaiidtddlprkrlpqlykppTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 946
Cdd:cd05930 88 VLT-------------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLW 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 947 ikLQCELYSSR-----QIAicldpycGLGF--ALWCL-CSVYSGHQSVLIPPmELENNLFLWLATVNQYKIRDTFCSYSV 1018
Cdd:cd05930 125 --MQEAYPLTPgdrvlQFT-------SFSFdvSVWEIfGALLAGATLVVLPE-EVRKDPEALADLLAEEGITVLHLTPSL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1019 MELCTKGLGNQvevlktrgiNLSCIRTcVVVAEERPRVSLQQSFSKLFKDIGLspravsttfgsrVNVaiclqgtSGPDP 1098
Cdd:cd05930 195 LRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELLPGARL------------VNL-------YGPTE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1099 TTVYVDLKSLRHDRVRlvERGAPqslllseSGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYytiYDSETLQ 1178
Cdd:cd05930 246 ATVDATYYRVPPDDEE--DGRVP-------IGRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLARGY---LNRPELT 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1179 ADHFnTRLSFGDaaqtlWA---RTGYLgfVRRTEltaatgerHDALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIA 1255
Cdd:cd05930 313 AERF-VPNPFGP-----GErmyRTGDL--VRWLP--------DGNLEFLGRIDDQVKIRGYRIELGEIEAALLA-HPGVR 375
|
....*....
gi 226823266 1256 ECAVFTWTN 1264
Cdd:cd05930 376 EAAVVARED 384
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
914-1244 |
1.41e-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: 1.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 914 PEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMEL 993
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 994 ENNLFLWLATVNQYKIRDTFCSysvmELCTKGLGNQVEVLKTRGINLSCIRTCVVVAEerP-RVSLQQSFSKLFKDIGLS 1072
Cdd:cd05908 185 IRRPILWLKKASEHKATIVSSP----NFGYKYFLKTLKPEKANDWDLSSIRMILNGAE--PiDYELCHEFLDHMSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1073 PRAVSTTFG-SRVNVAICLQGTSGPdPTTVYVDLKSLRH-DRVRLVERGAPQSLLLSESGKILPGVKVVIVNPETKGpVG 1150
Cdd:cd05908 259 RNAILPVYGlAEASVGASLPKAQSP-FKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LP 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1151 DSHLGEIWVNSPHTASGYYTiydsetlqadhfNTRLSFGDAAQTLWARTGYLGFVRRTELTaATGERHDALYVvgaldet 1230
Cdd:cd05908 337 DGYIGHIQIRGKNVTPGYYN------------NPEATAKVFTDDGWLKTGDLGFIRNGRLV-ITGREKDIIFV------- 396
|
330
....*....|....
gi 226823266 1231 lelRGLRYHPIDIE 1244
Cdd:cd05908 397 ---NGQNVYPHDIE 407
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
789-1259 |
1.60e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 65.17 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGHLNAgdnVVLLYPPGIELIAAFYGCLYAG----CIPVTVRPPHAQNLTATLPTVRMVVDVSKa 864
Cdd:PRK05851 36 EVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT- 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 865 acVLTTQTLMRLLKSREAAAAV-DVKTWPaiidtddlpRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNAL 943
Cdd:PRK05851 112 --VLSHGSHLERLRAVDSSVTVhDLATAA---------HTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 944 CRAIKLQCELYSSRQIAICLDP-YCGLGFAlWCLCSVYSGHQSVLIPPMELENNLFLWLATVNQYkiRDTFC-----SYS 1017
Cdd:PRK05851 181 LRGLNARVGLDAATDVGCSWLPlYHDMGLA-FLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDS--RATLTaapnfAYN 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1018 VmelctkgLGNQVEvlKTRGINLSCIRTCVVVAEERPRVSLQQsFSKLFKDIGLSPRAVSTTFGsrVNVAIClqGTSGPD 1097
Cdd:PRK05851 258 L-------IGKYAR--RVSDVDLGALRVALNGGEPVDCDGFER-FATAMAPFGFDAGAAAPSYG--LAESTC--AVTVPV 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1098 PTTvyvdlkSLRHDRVRLVERGAPQSLLLSesGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYytiYDSETL 1177
Cdd:PRK05851 324 PGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY---LGQAPI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1178 QADHfntrlsfgdaaqtlWARTGYLGFvrrteLTAatgerhDALYVVGALDETLELRGLRYHPIDIETSVSRVhRSIAEC 1257
Cdd:PRK05851 393 DPDD--------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERVAAQV-RGVREG 446
|
..
gi 226823266 1258 AV 1259
Cdd:PRK05851 447 AV 448
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
789-1276 |
1.44e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 61.92 E-value: 1.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPH-AQNLtatlptvRMVVDVSKAACV 867
Cdd:cd12116 17 ELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYpADRL-------RYILEDAEPALV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 868 LTTQTLMrllksreAAAAVDVKTWPAIIDTDDLPRKRLPqlyKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAI 947
Cdd:cd12116 89 LTDDALP-------DRLPAGLPVLLLALAAAAAAPAAPR---TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 948 KLQCELYSSRQIaICLDPYCglgFALwclcsvysghqSVLippmelenNLFLWLATVNQYKIRDTFCSYSVMELctkglg 1027
Cdd:cd12116 159 RERLGLGPGDRL-LAVTTYA---FDI-----------SLL--------ELLLPLLAGARVVIAPRETQRDPEAL------ 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1028 nqVEVLKTRGINlscirtcvvVAEERPrvslqqSFSKLFKDIGLSPR----------AVSTTFGSR-VNVAICLQGTSGP 1096
Cdd:cd12116 210 --ARLIEAHSIT---------VMQATP------ATWRMLLDAGWQGRagltalcggeALPPDLAARlLSRVGSLWNLYGP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1097 DPTTVYvdlkSLRHdRVRLVERGAPqslllseSGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYytiYDSET 1176
Cdd:cd12116 273 TETTIW----STAA-RVTAAAGPIP-------IGRPLANTQVYVLDAALR-PVPPGVPGELYIGGDGVAQGY---LGRPA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1177 LQADHFnTRLSFGDAAQTLWaRTGYLgfVRRteltaatgERHDALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAE 1256
Cdd:cd12116 337 LTAERF-VPDPFAGPGSRLY-RTGDL--VRR--------RADGRLEYLGRADGQVKIRGHRIELGEIEAALAA-HPGVAQ 403
|
490 500
....*....|....*....|....
gi 226823266 1257 CAVFTWTN----LLVVVVELCGSE 1276
Cdd:cd12116 404 AAVVVREDggdrRLVAYVVLKAGA 427
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
789-1185 |
3.07e-09 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 61.59 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTAtLPTVRmvvdvSKAACVL 868
Cdd:PRK06060 35 QIHDGAARLGEVLRNRG-LSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHA-LAARN-----TEPALVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 869 TTQTLMRLLKSREAAAAVDVKTWPAIIDTDDlprkrlpqlYKPPTPEMLAYLDFSVSTTGMLTGVKMSH----SAVNALC 944
Cdd:PRK06060 108 TSDALRDRFQPSRVAEAAELMSEAARVAPGG---------YEPMGGDALAYATYTSGTTGPPKAAIHRHadplTFVDAMC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 945 R-AIKLqcelySSRQIAIC---LDPYCGLGFALWCLCSVYSghqSVLIPPMELENNLFLWLATVNQ----YKIRDTFCsy 1016
Cdd:PRK06060 179 RkALRL-----TPEDTGLCsarMYFAYGLGNSVWFPLATGG---SAVINSAPVTPEAAAILSARFGpsvlYGVPNFFA-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1017 SVMELCTKGlgnqvevlktrgiNLSCIRtCVVVAEERPRVSLQQSFSKLFKDI----GLSPRAVSTTFGSRVnvaiclqg 1092
Cdd:PRK06060 249 RVIDSCSPD-------------SFRSLR-CVVSAGEALELGLAERLMEFFGGIpildGIGSTEVGQTFVSNR-------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1093 tsgpdpttvyvdlkslrhdrvrlVERGAPQSLllsesGKILPGVKVVIVNPE--TKGPVGDshlGEIWVNSPHTASGYYT 1170
Cdd:PRK06060 307 -----------------------VDEWRLGTL-----GRVLPPYEIRVVAPDgtTAGPGVE---GDLWVRGPAIAKGYWN 355
|
410
....*....|....*
gi 226823266 1171 IYDSETLQADHFNTR 1185
Cdd:PRK06060 356 RPDSPVANEGWLDTR 370
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
763-958 |
5.18e-09 |
|
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: 60.44 E-value: 5.18e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 763 AQATPDHVLfmlLNAKGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG--CIPVTV 840
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGaaYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 841 RPPhAQNLTATLPTVRMVvdvskaaCVLTTQTLM-RLLKSREAAAAVDVKTWPAIIDTDDLPrkrlpqlykPPTPEMLAY 919
Cdd:cd17651 78 AYP-AERLAFMLADAGPV-------LVLTHPALAgELAVELVAVTLLDQPGAAAGADAEPDP---------ALDADDLAY 140
|
170 180 190
....*....|....*....|....*....|....*....
gi 226823266 920 LDFSVSTTGMLTGVKMSHSAVNALCRAiklQCELYSSRQ 958
Cdd:cd17651 141 VIYTSGSTGRPKGVVMPHRSLANLVAW---QARASSLGP 176
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
133-603 |
7.97e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 60.74 E-value: 7.97e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 133 LTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNDPVMfmVAFYGCLLA--EVIPVPIEVPltrkdagGQQI 210
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLR-ARG------VGPEVRVAIAAERSFELV--VALLAVLKAggAYVPLDPNYP-------AERL 2092
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 211 GFLLGSCGIALALTSEICLKGLPKTQngeivqfkGWPRLKwvVTDSKYLSKPPkDWQPHISPAGTEPAYIEYKTSKEGSV 290
Cdd:PRK12316 2093 AYMLEDSGAALLLTQRHLLERLPLPA--------GVARLP--LDRDAEWADYP-DTAPAVQLAGENLAYVIYTSGSTGLP 2161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 291 MGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWhGMFANVMNKMHTISVPYSVMKtcPLSWVQRVHAHkaK 370
Cdd:PRK12316 2162 KGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDELWD--PEQLYDEMERH--G 2236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 371 VALVKCRDLHWAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLS------LFQSHGLKPEAICPCATSAEAmTVA 444
Cdd:PRK12316 2237 VTILDFPPVYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEalrpvyLFNGYGPTEAVVTPLLWKCRP-QDP 2313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 445 IRRPGVP-GAPLPGRAilsmnglsygvirvntedknsaltvqdvGHVMPGGMmcivkpdglpQLCRTDEIGEICVSSRTG 523
Cdd:PRK12316 2314 CGAAYVPiGRALGNRR----------------------------AYILDADL----------NLLAPGMAGELYLGGEGL 2355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 524 GMMYFGLAGVTKNTFEVIPVTSSGSPVgdvpfIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIK 603
Cdd:PRK12316 2356 ARGYLNRPGLTAERFVPDPFSASGERL-----YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVR 2430
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
292-676 |
1.60e-08 |
|
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: 58.07 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 292 GVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWhGMFANVMNKMHTISVPysvmKTCPLSWVQRVHAHKAKV 371
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP----KFDPEAALELIEREKVTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 372 ALVKcRDLHWAMMAHRDQRDVSLSSLRMLIVtdGANPWSVSSCDAFLSLF-----QSHGLkPEAICPCATSAEAMtvAIR 446
Cdd:cd04433 92 LLGV-PTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAPgiklvNGYGL-TETGGTVATGPPDD--DAR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 447 RPGVPGAPLPGRAILsmnglsygvirvntedknsaltvqdvghvmpggmmcIVKPDGLPqlCRTDEIGEICVssrTGGMM 526
Cdd:cd04433 166 KPGSVGRPVPGVEVR------------------------------------IVDPDGGE--LPPGEIGELVV---RGPSV 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 527 YFGLAGVTKNTFEVIPvtsSGspvgdvpFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGRRHNADDIVATGLAVESIKTVy 606
Cdd:cd04433 205 MKGYWNNPEATAAVDE---DG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEA- 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 226823266 607 rgriAVFSVsvfYDER------IVVVAEQRPDASEEDSFQWMSRVLQAIDSIHQVgvyclalVPANTLPKTPLGGI 676
Cdd:cd04433 274 ----AVVGV---PDPEwgervvAVVVLRPGADLDAEELRAHVRERLAPYKVPRRV-------VFVDALPRTASGKI 335
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
357-685 |
1.74e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 58.85 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 357 PLSWVQRVHAHKAKVALVKcrDLHWAMMAHR-----DQRDVSLSSLRmlIVTDGANPWSVSSCDAFLSLFQSHGLKPEAI 431
Cdd:PRK07768 235 PLLWAELISKYRGTMTAAP--NFAYALLARRlrrqaKPGAFDLSSLR--FALNGAEPIDPADVEDLLDAGARFGLRPEAI 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 432 CPCATSAEAmTVAIRRPGvPGAPL----PGRAILSMNGlsygviRVNTEDKNSALTVQDVGHVMPGGMMCIVKPDGlpQL 507
Cdd:PRK07768 311 LPAYGMAEA-TLAVSFSP-CGAGLvvdeVDADLLAALR------RAVPATKGNTRRLATLGPPLPGLEVRVVDEDG--QV 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 508 CRTDEIGEICVSSRTggmmyfglagVTKNTfevipVTSSG--SPVGDVPFIRSGLLGFVGPGSLVFVVGKMDGLLMVSGR 585
Cdd:PRK07768 381 LPPRGVGVIELRGES----------VTPGY-----LTMDGfiPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGR 445
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 586 RHNADDIVAtglAVESIKTVYRGRIavfsVSVFYD-----ERIVVVAEQRPDASEEDSFQWMSRVLQAIDSihQVGV--Y 658
Cdd:PRK07768 446 NIYPTDIER---AAARVEGVRPGNA----VAVRLDaghsrEGFAVAVESNAFEDPAEVRRIRHQVAHEVVA--EVGVrpR 516
|
330 340
....*....|....*....|....*..
gi 226823266 659 CLALVPANTLPKTPLGGIHISQTKQLF 685
Cdd:PRK07768 517 NVVVLGPGSIPKTPSGKLRRANAAELV 543
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
755-1258 |
2.90e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 57.99 E-value: 2.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 755 LAEILQWRAQATPDHVLFMLLNAKGTTV----CTASCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGC 830
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVAVPGGRGADGklayDELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 831 LYAGCIPVTVRPPHA-QNLTATLPTVR--MVVDVSKAacvlttqTLMRLL-----KSREAAAAVDVKTWPAIIDTDDLPR 902
Cdd:PRK09274 87 FKAGAVPVLVDPGMGiKNLKQCLAEAQpdAFIGIPKA-------HLARRLfgwgkPSVRRLVTVGGRLLWGGTTLATLLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 903 KRLP---QLYKPPTPEMLAYLdFSVSTTGMLTGVKMSHSAVNALCRAIKlqcELYSSRQIAICL---------DPYCGlg 970
Cdd:PRK09274 160 DGAAapfPMADLAPDDMAAIL-FTSGSTGTPKGVVYTHGMFEAQIEALR---EDYGIEPGEIDLptfplfalfGPALG-- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 971 falwcLCSVysghqsvlIPPMELE-----NNLFLWlATVNQYKIRDTFCSYSVMELctkgLGNQvevLKTRGINLSCIRT 1045
Cdd:PRK09274 234 -----MTSV--------IPDMDPTrpatvDPAKLF-AAIERYGVTNLFGSPALLER----LGRY---GEANGIKLPSLRR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1046 cVVVAEERPRVSLQQSFSKLfkdigLSPRA-VSTTFGSRVNVAICLqgtsgpdpttvyVDLKSLRHDRVRLVERGAPQSL 1124
Cdd:PRK09274 293 -VISAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS------------IESREILFATRAATDNGAGICV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1125 llsesGKILPGVKVVIVNPeTKGPVGDSH---------LGEIWVNSPHTASGYYTiYDSETLQAdhfntRLSfgDAAQTL 1195
Cdd:PRK09274 355 -----GRPVDGVEVRIIAI-SDAPIPEWDdalrlatgeIGEIVVAGPMVTRSYYN-RPEATRLA-----KIP--DGQGDV 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226823266 1196 WARTGYLGFVrrteltaatgERHDALYVVGALDETLELRGLRYHPIDIEtSVSRVHRSIAECA 1258
Cdd:PRK09274 421 WHRMGDLGYL----------DAQGRLWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGVKRSA 472
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
752-947 |
2.97e-08 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 58.71 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 752 HQFLAEilqwRAQATPDHV-LfmllnakgttVCTASCL---QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAF 827
Cdd:COG1020 479 HELFEA----QAARTPDAVaV----------VFGDQSLtyaELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVAL 543
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 828 YGCLYAGC--IPvtvrpphaqnLTATLPT--VRMVVDVSKAACVLTTQTLMRLLksreAAAAVDVktwpaiIDTDDLPRK 903
Cdd:COG1020 544 LAVLKAGAayVP----------LDPAYPAerLAYMLEDAGARLVLTQSALAARL----PELGVPV------LALDALALA 603
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 226823266 904 RLPQ--LYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAI 947
Cdd:COG1020 604 AEPAtnPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWM 649
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
124-677 |
3.18e-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: 57.99 E-value: 3.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 124 DVTGKpvyTLTYGKLWSRSLKLAYTLlNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLTRK 203
Cdd:cd05911 5 ADTGK---ELTYAQLRTLSRRLAAGL-RKLG------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAANPIYTAD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 204 DaggqqIGFLLGSCGIALALTSEiclKGLPKTQNgeivQFKGWPRLK--WVVTDSK-YLSKPPKDWQPHISP-------- 272
Cdd:cd05911 73 E-----LAHQLKISKPKVIFTDP---DGLEKVKE----AAKELGPKDkiIVLDDKPdGVLSIEDLLSPTLGEededlppp 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 273 ---AGTEPAYIEYKTSKEGSVMGVTVSR---LAMLSQCQALSQAcNYSEGETVVNVLDFKKDAGLWhGMFANVMNKMHTI 346
Cdd:cd05911 141 lkdGKDDTAAILYSSGTTGLPKGVCLSHrnlIANLSQVQTFLYG-NDGSNDVILGFLPLYHIYGLF-TTLASLLNGATVI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 347 svpysVM-KTCPLSWVQRVHAHKAKVALVKCRdlHWAMMAHRDQRDV-SLSSLRMLIVtdGANPWSVSSCDAFLSLFQSh 424
Cdd:cd05911 219 -----IMpKFDSELFLDLIEKYKITFLYLVPP--IAAALAKSPLLDKyDLSSLRVILS--GGAPLSKELQELLAKRFPN- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 425 glkpeaicPCATSAEAMTVAirrpGVPGAPLPGrailsmnglsygvirvnTEDKNSAltvqdVGHVMPGGMMCIVKPDGl 504
Cdd:cd05911 289 --------ATIKQGYGMTET----GGILTVNPD-----------------GDDKPGS-----VGRLLPNVEAKIVDDDG- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 505 PQLCRTDEIGEICVssRTGGMM--YFGLAGVTKNTFevipvTSSGspvgdvpFIRSGLLGFVGPGSLVFVVGKMDGLLMV 582
Cdd:cd05911 334 KDSLGPNEPGEICV--RGPQVMkgYYNNPEATKETF-----DEDG-------WLHTGDIGYFDEDGYLYIVDRKKELIKY 399
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 583 SGRRHNADDIVATGLAVESIKTVyrgriAVFSVsvfYDE------RIVVVAEQRPDASEEDSFQWMSrvlQAIDSIHQ-- 654
Cdd:cd05911 400 KGFQVAPAELEAVLLEHPGVADA-----AVIGI---PDEvsgelpRAYVVRKPGEKLTEKEVKDYVA---KKVASYKQlr 468
|
570 580
....*....|....*....|...
gi 226823266 655 VGVYclaLVPAntLPKTPLGGIH 677
Cdd:cd05911 469 GGVV---FVDE--IPKSASGKIL 486
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
789-1259 |
5.28e-08 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 56.93 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGC--IPVTVRPPHAQNltatlptvRMVVDVSKAAC 866
Cdd:cd17643 17 ELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGayVPIDPAYPVERI--------AFILADSGPSL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 867 VLTTqtlmrllksreaaaavdvktwpaiidtddlprkrlpqlykpptPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRA 946
Cdd:cd17643 88 LLTD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 947 IklQCELYSSRQIAICLDPYCGLGFALWCLCSVYSGHQSVLIPPMEL---ENNLFLWLA----TV-NQykirdTFCSYSV 1018
Cdd:cd17643 125 T--QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVarsPEDFARLLRdegvTVlNQ-----TPSAFYQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1019 MelctkglgnqVEVLKTRGINLSCIRTcVVVAEERPRVSLQQSFSKLFKDigLSPRAVSTTfgsrvnvaiclqgtsGPDP 1098
Cdd:cd17643 198 L----------VEAADRDGRDPLALRY-VIFGGEALEAAMLRPWAGRFGL--DRPQLVNMY---------------GITE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1099 TTVYVDLKSLRHDRVRLVERgapqslllSESGKILPGVKVVIVNpETKGPVGDSHLGEIWVNSPHTASGYYtiyDSETLQ 1178
Cdd:cd17643 250 TTVHVTFRPLDAADLPAAAA--------SPIGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAGVARGYL---GRPELT 317
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1179 ADHFNTrLSFGDAAQTLWaRTGYLgfVRRTeltaATGErhdaLYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECA 1258
Cdd:cd17643 318 AERFVA-NPFGGPGSRMY-RTGDL--ARRL----PDGE----LEYLGRADEQVKIRGFRIELGEIEAALAT-HPSVRDAA 384
|
.
gi 226823266 1259 V 1259
Cdd:cd17643 385 V 385
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
788-1259 |
5.84e-08 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 56.70 E-value: 5.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 788 LQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltatlptvrmvvdvskaacV 867
Cdd:cd05919 14 GQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINP------------------------L 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 868 LTTQTLMRLLKSREAAAavdvktwpAIIDTDDlprkrlpqlykpptpemLAYLDFSVSTTGMLTGVKMSHSA----VNAL 943
Cdd:cd05919 69 LHPDDYAYIARDCEARL--------VVTSADD-----------------IAYLLYSSGTTGPPKGVMHAHRDpllfADAM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 944 CR---AIKLQCELYSSRQIAICLdpycGLGFALWclCSVYSGHQSVLIPPMELENNLFlwlATVNQYKIRdTFCSYSVME 1020
Cdd:cd05919 124 ARealGLTPGDRVFSSAKMFFGY----GLGNSLW--FPLAVGASAVLNPGWPTAERVL---ATLARFRPT-VLYGVPTFY 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1021 LCTKGLGNQVEVLktrginLSCIRTCVVVAEERPRVSLQQsfsklFKDIGLSPraVSTTFGSRVNVAICLqgtsgpdptt 1100
Cdd:cd05919 194 ANLLDSCAGSPDA------LRSLRLCVSAGEALPRGLGER-----WMEHFGGP--ILDGIGATEVGHIFL---------- 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1101 vyvdlkSLRHDRVRlvergapqsllLSESGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPHTASGYYTIYDSetlqad 1180
Cdd:cd05919 251 ------SNRPGAWR-----------LGSTGRPVPGYEIRLVDEEGH-TIPPGEEGDLLVRGPSAAVGYWNNPEK------ 306
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226823266 1181 hfnTRLSFGDAaqtlWARTGYLGFVrrteltAATGerhdALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECAV 1259
Cdd:cd05919 307 ---SRATFNGG----WYRTGDKFCR------DADG----WYTHAGRADDMLKVGGQWVSPVEVESLIIQ-HPAVAEAAV 367
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
755-844 |
9.64e-08 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 56.31 E-value: 9.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 755 LAEILQWRAQATPDHVlfmllnAkgtTVCTASCL---QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCL 831
Cdd:COG1021 27 LGDLLRRRAERHPDRI------A---VVDGERRLsyaELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALF 96
|
90
....*....|...
gi 226823266 832 YAGCIPVTVRPPH 844
Cdd:COG1021 97 RAGAIPVFALPAH 109
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
790-1258 |
9.81e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 56.31 E-value: 9.81e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 790 LHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltatlptvRMVVdvskaacvlt 869
Cdd:cd05910 8 LDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP-------------GMGR---------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 870 tQTLMRLLKSREAAAAVDVktwpaiidtddlprkrlpqlykpPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKl 949
Cdd:cd05910 64 -KNLKQCLQEAEPDAFIGI-----------------------PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALR- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 950 qcELYSSRQIAICLDpycglGFALWCLCSVYSGHQSVlIPPMELE-----NNLFLwLATVNQYKIRDTFCSYSVMELCTk 1024
Cdd:cd05910 119 --QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDPTrparaDPQKL-VGAIRQYGVSIVFGSPALLERVA- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1025 glgnqvEVLKTRGINLSCIRtCVVVAEERPRVSLQQSFSKLfkdigLSPRA-VSTTFGSRVNVAICLQGTSgpdpttvyv 1103
Cdd:cd05910 189 ------RYCAQHGITLPSLR-RVLSAGAPVPIALAARLRKM-----LSDEAeILTPYGATEALPVSSIGSR--------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1104 dlkSLRHDRVRLVERGAPQSLllsesGKILPGVKVVIVnPETKGPV---GDSH------LGEIWVNSPHTASGYYTIYDS 1174
Cdd:cd05910 248 ---ELLATTTAATSGGAGTCV-----GRPIPGVRVRII-EIDDEPIaewDDTLelprgeIGEITVTGPTVTPTYVNRPVA 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1175 ETLQADHfntrlsfgDAAQTLWARTGYLGFVrrteltaatgERHDALYVVGALDETLELRGLRYHPIDIEtSVSRVHRSI 1254
Cdd:cd05910 319 TALAKID--------DNSEGFWHRMGDLGYL----------DDEGRLWFCGRKAHRVITTGGTLYTEPVE-RVFNTHPGV 379
|
....
gi 226823266 1255 AECA 1258
Cdd:cd05910 380 RRSA 383
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
132-201 |
1.62e-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: 1.62e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 132 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLT 201
Cdd:cd05936 24 KLTYRELDALAEAFAAGLQN-LG------VQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLNPLYT 84
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
762-945 |
2.71e-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: 54.90 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 762 RAQATPDHVLfmlLNAKGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVR 841
Cdd:cd12117 6 QAARTPDAVA---VVYGDRSLTYA---ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 842 PphaqnltaTLPTVRM--VVDVSKAACVLTTqtlmrllksrEAAAAVDVKTWPAIIDTDDLPRKRLPQLYKPPTPEMLAY 919
Cdd:cd12117 79 P--------ELPAERLafMLADAGAKVLLTD----------RSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAY 140
|
170 180
....*....|....*....|....*.
gi 226823266 920 LDFSVSTTGMLTGVKMSHSAVNALCR 945
Cdd:cd12117 141 VMYTSGSTGRPKGVAVTHRGVVRLVK 166
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
789-1259 |
3.35e-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: 54.41 E-value: 3.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltatlptvrmvvdvskaacvl 868
Cdd:cd05958 15 DLLALANRIANVLVGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMP-------------------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 869 ttqtlmrLLKSREAAAAVDvKTWPAIIDTDDlprkrlpqlyKPPTPEMLAYLDFSVSTTGMLTGVKMSHsavnalcRAIK 948
Cdd:cd05958 69 -------LLRPKELAYILD-KARITVALCAH----------ALTASDDICILAFTSGTTGAPKATMHFH-------RDPL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 949 LQCELYsSRQI--AICLDPYCGL-------GFALWCLCSVYSGHQSVLIP---PMELennlflwLATVNQYKIRDTF--- 1013
Cdd:cd05958 124 ASADRY-AVNVlrLREDDRFVGSpplaftfGLGGVLLFPFGVGASGVLLEeatPDLL-------LSAIARYKPTVLFtap 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1014 CSYSVMelctkglgnqVEVLKTRGINLSCIRTCVVVAEERPrvslQQSFSKLFKDIGLSpraVSTTFGSRVNVAICLQGT 1093
Cdd:cd05958 196 TAYRAM----------LAHPDAAGPDLSSLRKCVSAGEALP----AALHRAWKEATGIP---IIDGIGSTEMFHIFISAR 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1094 SGpdpttvyvdlkslrHDRVrlverGApqslllseSGKILPGVKVVIVNPETKgPVGDSHLGEIWVNSPhtaSGYYtiYD 1173
Cdd:cd05958 259 PG--------------DARP-----GA--------TGKPVPGYEAKVVDDEGN-PVPDGTIGRLAVRGP---TGCR--YL 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1174 SETLQADHF-NTRLSFGDAaqTLWARTGYLGFVRRTeltaatgerhDALYVVGaldetlelrGLRYHPIDIEtSVSRVHR 1252
Cdd:cd05958 306 ADKRQRTYVqGGWNITGDT--YSRDPDGYFRHQGRS----------DDMIVSG---------GYNIAPPEVE-DVLLQHP 363
|
....*..
gi 226823266 1253 SIAECAV 1259
Cdd:cd05958 364 AVAECAV 370
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
134-586 |
4.14e-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: 53.81 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 134 TYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEV--PLTRkdaggqqIG 211
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAER-------LA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 212 FLLGSCGIALALTSEiclkglpktQNGEIVQFKGWPRLKWVVTDSKYLSKPPKDWQPHISPAGTEPAYIEYkTSkeGSV- 290
Cdd:TIGR01733 66 FILEDAGARLLLTDS---------ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIY-TS--GSTg 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 291 --MGVTVSRLAMLSQCQALSQACNYSEGETVVNVLDFKKDAGLWHgMFANVMNKMHTISVPYSVMKTCPLSWvQRVHAHK 368
Cdd:TIGR01733 134 rpKGVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL-AALIAEH 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 369 aKVALVKCRDLHWAMMAhrDQRDVSLSSLRMLIVtdganpwsvsscdaflslfqshglkpeaicpcatSAEAMTVA-IRR 447
Cdd:TIGR01733 212 -PVTVLNLTPSLLALLA--AALPPALASLRLVIL----------------------------------GGEALTPAlVDR 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 448 pgvPGAPLPGRAILSMnglsYG---------VIRVnTEDKNSALTVQDVGHVMPGGMMCIVKPDGlpQLCRTDEIGEICV 518
Cdd:TIGR01733 255 ---WRARGPGARLINL----YGptettvwstATLV-DPDDAPRESPVPIGRPLANTRLYVLDDDL--RPVPVGVVGELYI 324
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226823266 519 SSRTGGMMYFGLAGVTKNTFevipVTSSGSPVGDVPFIRSGLLGFVGP-GSLVFvVGKMDGLLMVSGRR 586
Cdd:TIGR01733 325 GGPGVARGYLNRPELTAERF----VPDPFAGGDGARLYRTGDLVRYLPdGNLEF-LGRIDDQVKIRGYR 388
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
731-947 |
4.47e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 54.96 E-value: 4.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 731 RIAQAAGRDLGQI-----EENDLV---------------RKHQFLAEilqwRAQATPDHVlfmllnakgTTVCTASCL-- 788
Cdd:PRK12316 1965 QMAEDAQAALGELalldaGERQRIladwdrtpeayprgpGVHQRIAE----QAARAPEAI---------AVVFGDQHLsy 2031
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 -QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHaqnltatlPTVR---MVVDvSKA 864
Cdd:PRK12316 2032 aELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNY--------PAERlayMLED-SGA 2101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 865 ACVLTTQTLMRLLKSREAAAAVDVKT---WPAIIDTDDLPRKrlpqlykppTPEMLAYLDFSVSTTGMLTGVKMSHSAVN 941
Cdd:PRK12316 2102 ALLLTQRHLLERLPLPAGVARLPLDRdaeWADYPDTAPAVQL---------AGENLAYVIYTSGSTGLPKGVAVSHGALV 2172
|
....*.
gi 226823266 942 ALCRAI 947
Cdd:PRK12316 2173 AHCQAA 2178
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
132-265 |
6.04e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 53.81 E-value: 6.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 132 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALvYPNNDPvMFMVAFYGCLLAEVIPVPIEvPLTRKDaggqQIG 211
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLL-YMQNSP-QFVIAYYAILRANAVVVPVN-PMNREE----ELA 101
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 226823266 212 FLLGSCGIALAltseICLKGLPktqnGEIVQFKGWPRLKWVVTD--SKYLSKPPKD 265
Cdd:PRK08314 102 HYVTDSGARVA----IVGSELA----PKVAPAVGNLRLRHVIVAqySDYLPAEPEI 149
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
752-1284 |
9.22e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.81 E-value: 9.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 752 HQFLAEilqwRAQATPDHVLfMLLNAKgttvcTASCLQLHKRAERIASVLGDKGhlnAGDNVV--LLYPPGIELIAAFYG 829
Cdd:PRK12316 4554 HQLVAE----RARMTPDAVA-VVFDEE-----KLTYAELNRRANRLAHALIARG---VGPEVLvgIAMERSAEMMVGLLA 4620
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 830 CLYAGCIPVTVRPPHAQNLTATlptvrMVVDvSKAACVLTTQTLMRLLKSREAAAAVDV---KTWPAIIDTDdlprkrlP 906
Cdd:PRK12316 4621 VLKAGGAYVPLDPEYPRERLAY-----MMED-SGAALLLTQSHLLQRLPIPDGLASLALdrdEDWEGFPAHD-------P 4687
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 907 QLykPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELYSSRqiaiCLDPYCGLGF--ALWCLCSVYSGHQ 984
Cdd:PRK12316 4688 AV--RLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDD----RVLQFMSFSFdgSHEGLYHPLINGA 4761
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 985 SVLIPPMELENNLFLwLATVNQYKIRDTFCSYSVMELCTKGLGNQVEVLKTRGINLScirtcvvvAEERPRVSLQQSFSK 1064
Cdd:PRK12316 4762 SVVIRDDSLWDPERL-YAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFG--------GEAVAQASYDLAWRA 4832
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1065 LFKDiglspravsttfgsrvnvaiCLQGTSGPDPTTVYVDLKSLRhdrvrlveRGAPQSLLLSESGKILPGVKVVIV--- 1141
Cdd:PRK12316 4833 LKPV--------------------YLFNGYGPTETTVTVLLWKAR--------DGDACGAAYMPIGTPLGNRSGYVLdgq 4884
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1142 -NPETKGPVGDSHLGEIWVnsphtASGYytiYDSETLQADHFNTRlSFGDAAQTLWaRTGYLgfvrrteltaATGERHDA 1220
Cdd:PRK12316 4885 lNPLPVGVAGELYLGGEGV-----ARGY---LERPALTAERFVPD-PFGAPGGRLY-RTGDL----------ARYRADGV 4944
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226823266 1221 LYVVGALDETLELRGLRYHPIDIETSVsRVHRSIAECavftwtnlLVVVVELCGSEQEALDLVP 1284
Cdd:PRK12316 4945 IDYLGRVDHQVKIRGFRIELGEIEARL-REHPAVREA--------VVIAQEGAVGKQLVGYVVP 4999
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
761-940 |
2.25e-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: 51.89 E-value: 2.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 761 WRAQA--TPDHVlfmllnAKGTTVCTASCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPV 838
Cdd:cd17646 4 VAEQAarTPDAP------AVVDEGRTLTYRELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 839 TVRPPHaqnltatlPTVR---MVVDVskAACVLTTQTLMRLLKSREAAAAVDVKTWPAIIDTDDLPRkrlpqlykPPTPE 915
Cdd:cd17646 77 PLDPGY--------PADRlayMLADA--GPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV--------PPRPD 138
|
170 180
....*....|....*....|....*
gi 226823266 916 MLAYLDFSVSTTGMLTGVKMSHSAV 940
Cdd:cd17646 139 NLAYVIYTSGSTGRPKGVMVTHAGI 163
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
755-950 |
2.93e-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: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 755 LAEILQWRAQATPDHVLFMLLNAKGTTVCTASclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 834
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSLTWA--EFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 835 CIPVTVRPphaqnlTATLPTVRMVVDVSKAACVL--TTQTLMRLLKSREAAAAV---------------DVKTWPAIID- 896
Cdd:COG1022 90 AVTVPIYP------TSSAEEVAYILNDSGAKVLFveDQEQLDKLLEVRDELPSLrhivvldprglrddpRLLSLDELLAl 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 226823266 897 -TDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSH----SAVNALCRAIKLQ 950
Cdd:COG1022 164 gREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHrnllSNARALLERLPLG 222
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
789-947 |
3.63e-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: 51.12 E-value: 3.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaqnltaTLPTVRMVVDVSKAACvl 868
Cdd:cd12114 17 ELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDI--------DQPAARREAILADAGA-- 85
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 226823266 869 ttqtlmRLLKSREAAAAVDVKTWPAIIDTDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVNALCRAI 947
Cdd:cd12114 86 ------RLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
132-406 |
2.03e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 48.75 E-value: 2.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 132 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLTrkdagGQQIG 211
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAA-LG------IGKGDRVAIWAPNS--PHWVIAALGALKAGAVVVPLNTRYT-----ADEAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 212 FLLGSCGIALALTSEICL-------KGLPKTQNGEIVQF-KGWPRLKWVVTDSKYLSKPPKDWQpHISPAGTEPAYIEYk 283
Cdd:PRK07656 96 YILARGDAKALFVLGLFLgvdysatTRLPALEHVVICETeEDDPHTEKMKTFTDFLAAGDPAER-APEVDPDDVADILF- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 284 TSkegsvmGVT-VSRLAMLSQCQALSQA---CNY---SEGETVVNVLDFKKDAGLWHGMFANVMNKMHTISVPysvmKTC 356
Cdd:PRK07656 174 TS------GTTgRPKGAMLTHRQLLSNAadwAEYlglTEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP----VFD 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 226823266 357 PLSWVQRVHAHKAKVaLVKCRDLHWAMMAHRDQRDVSLSSLRmLIVTDGA 406
Cdd:PRK07656 244 PDEVFRLIETERITV-LPGPPTMYNSLLQHPDRSAEDLSSLR-LAVTGAA 291
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
127-228 |
3.36e-05 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 48.13 E-value: 3.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 127 GKPVY-----TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYpnNDPVMFMVAFYGCLLAEVIPVPIEVPLT 201
Cdd:cd05959 19 DKTAFiddagSLTYAELEAEARRVAGALR-ALG------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100
....*....|....*....|....*...
gi 226823266 202 rkdagGQQIGFLLGSCGI-ALALTSEIC 228
Cdd:cd05959 90 -----PDDYAYYLEDSRArVVVVSGELA 112
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
759-1260 |
3.52e-05 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 47.99 E-value: 3.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 759 LQWRAQATPDHVLFMLLnakGTTVCTAsclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPV 838
Cdd:cd17631 1 LRRRARRHPDRTALVFG---GRSLTYA---ELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 839 tvrpPHAQNLTAtlPTVRMVVDVSKAACVLttqtlmrllksreaaaavdvktwpaiidtDDLprkrlpqlykpptpemlA 918
Cdd:cd17631 74 ----PLNFRLTP--PEVAYILADSGAKVLF-----------------------------DDL-----------------A 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 919 YLDFSVSTTGMLTGVKMSHSAVNALCRAIKLQCELySSRQIAICLDPYCGLGFA-LWCLCSVYSGHQSVLIPPMELENnl 997
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFHIGGLgVFTLPTLLRGGTVVILRKFDPET-- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 998 flWLATVNQYKIRDTFCSYSVME-LCTKGlgnqvevlKTRGINLSCIRtCVVVAEERPRVSLQQSFsklfKDIGLsprAV 1076
Cdd:cd17631 179 --VLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRAL----QARGV---KF 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1077 STTFGsrvnvaiclQGTSGPdPTTVyvdlksLRHDRVRlvergapqSLLLSeSGKILPGVKVVIVNPETKgPVGDSHLGE 1156
Cdd:cd17631 241 VQGYG---------MTETSP-GVTF------LSPEDHR--------RKLGS-AGRPVFFVEVRIVDPDGR-EVPPGEVGE 294
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1157 IWVNSPHTASGYYTiyDSETlqadhfnTRLSFGDAaqtlWARTGYLGFVrrteltaatgeRHDA-LYVVGALDETLELRG 1235
Cdd:cd17631 295 IVVRGPHVMAGYWN--RPEA-------TAAAFRDG----WFHTGDLGRL-----------DEDGyLYIVDRKKDMIISGG 350
|
490 500
....*....|....*....|....*
gi 226823266 1236 LRYHPIDIETSVSRvHRSIAECAVF 1260
Cdd:cd17631 351 ENVYPAEVEDVLYE-HPAVAEVAVI 374
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
132-323 |
3.80e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 48.01 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 132 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNDpvMFMVAFYGCLLAEVIPVPIEVPLTrkdagGQQIG 211
Cdd:PRK08316 36 SWTYAELDAAVNRVAAALLD-LG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLT-----GEELA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 212 FLLGSCGIALALTSEICLKGLPKTQNGEIVQFKGWPRL--------KWVVTDSKYLSKPpkDWQPHISPAGTEPAYIEYK 283
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVlggreapgGWLDFADWAEAGS--VAEPDVELADDDLAQILYT 179
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 226823266 284 TSKEGSVMGVTVSRLAMLSQCQALSQACNYSEGETVVNVL 323
Cdd:PRK08316 180 SGTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHAL 219
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
789-937 |
4.36e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 47.69 E-value: 4.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRP-------------------------- 842
Cdd:PRK05605 62 ELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPlytahelehpfedhgarvaivwdkva 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 843 PHAQNLTATLPtVRMVVDVS-KAACVLTTQTLMRL-----LKSREA--AAAVDVKTWPAIIDTDDLPRKRLPQLYKPpTP 914
Cdd:PRK05605 141 PTVERLRRTTP-LETIVSVNmIAAMPLLQRLALRLpipalRKARAAltGPAPGTVPWETLVDAAIGGDGSDVSHPRP-TP 218
|
170 180
....*....|....*....|...
gi 226823266 915 EMLAYLDFSVSTTGMLTGVKMSH 937
Cdd:PRK05605 219 DDVALILYTSGTTGKPKGAQLTH 241
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
132-402 |
4.58e-05 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 47.93 E-value: 4.58e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 132 TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPI--EVPLTRkdaggqq 209
Cdd:COG1020 501 SLTYAELNARANRLAHHLR-ALG------VGPGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLdpAYPAER------- 564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 210 IGFLLGSCGIALALTSEICLKGLPKTQngeivqfkgwprLKWVVTDSKYLSKPPKDWqPHISPAGTEPAYIEYkTS---- 285
Cdd:COG1020 565 LAYMLEDAGARLVLTQSALAARLPELG------------VPVLALDALALAAEPATN-PPVPVTPDDLAYVIY-TSgstg 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 286 --KegsvmGVTVSRLAMLSQCQALSQACNYSEGETVVNV--LDFkkDAGLWhGMFANVMNKMHTISVPYSVMKTcPLSWV 361
Cdd:COG1020 631 rpK-----GVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW-EIFGALLSGATLVLAPPEARRD-PAALA 701
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 226823266 362 QRVHAHkaKVALVKCRDLHWAMMAHRDQRDvsLSSLRMLIV 402
Cdd:COG1020 702 ELLARH--RVTVLNLTPSLLRALLDAAPEA--LPSLRLVLV 738
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
131-194 |
8.87e-05 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 46.68 E-value: 8.87e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 226823266 131 YTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPV 194
Cdd:COG1021 49 RRLSYAELDRRADRLAAGLL-ALG------LRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
798-1272 |
9.62e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 46.66 E-value: 9.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 798 ASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTATlpTVRMVVDVSKAACVLTTQTLMrll 877
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKES--VLRYLVADAGGRIVLADAGAA--- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 878 kSREAAAAVDVKTWPAIIDTDDLPRKRLPQLYKPPTPEMLAYLDFSVSTTGMLTGVKMSHSAVnalcraiklqceLYSSR 957
Cdd:cd05922 81 -DRLRDALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNL------------LANAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 958 QIAICLDpYCGLGFALWCLCSVYSGHQSVLippmeleNNLFLWLATV---NQYKIRDTFcsysvMELCTKglgnqvevlk 1034
Cdd:cd05922 148 SIAEYLG-ITADDRALTVLPLSYDYGLSVL-------NTHLLRGATLvltNDGVLDDAF-----WEDLRE---------- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1035 TRGINLSCIrtcvvvaeerPrvSLQQSFSKL-FKDIGL-SPRAVSTTFGSRVNVAICLQGTSGPDpTTVYV--------- 1103
Cdd:cd05922 205 HGATGLAGV----------P--STYAMLTRLgFDPAKLpSLRYLTQAGGRLPQETIARLRELLPG-AQVYVmygqteatr 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1104 DLKSLRHDRVRlvERgaPQSLllsesGKILPGVKVVIVNPEtKGPVGDSHLGEIWVNSPHTASGYytiydsetlqadhfn 1183
Cdd:cd05922 272 RMTYLPPERIL--EK--PGSI-----GLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGY--------------- 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1184 trlsfgdaaqtlWARTGYLGFVRRTELTAATGE--RHDA---LYVVGALDETLELRGLRYHPIDIETSVsRVHRSIAECA 1258
Cdd:cd05922 327 ------------WNDPPYRRKEGRGGGVLHTGDlaRRDEdgfLFIVGRRDRMIKLFGNRISPTEIEAAA-RSIGLIIEAA 393
|
490
....*....|....*...
gi 226823266 1259 VF----TWTNLLVVVVEL 1272
Cdd:cd05922 394 AVglpdPLGEKLALFVTA 411
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1125-1216 |
1.05e-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: 1.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1125 LLSESGKILPGVKVVIVNPETKGPVGDSHLGEIWVNSPHTASGYY-----TiydSETLQADH-FNTrlsfGDAAQtlWAR 1198
Cdd:cd17640 262 VRGSVGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYknpeaT---SKVLDSDGwFNT----GDLGW--LTC 332
|
90 100
....*....|....*....|
gi 226823266 1199 TGYLGFVRRTELTA--ATGE 1216
Cdd:cd17640 333 GGELVLTGRAKDTIvlSNGE 352
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
789-1259 |
1.65e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 45.76 E-value: 1.65e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAGCiPVTV--RPPHAQNLTA----TLPTVRMV---- 858
Cdd:PRK07768 34 EVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGA-SLTMlhQPTPRTDLAVwaedTLRVIGMIgaka 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 859 VDVSK----AACVLTTQ--TLMRLLKSREAAAAVDVKTwpaiiDTDDLprkrlpqlykpptpemlAYLDFSVSTTGMLTG 932
Cdd:PRK07768 112 VVVGEpflaAAPVLEEKgiRVLTVADLLAADPIDPVET-----GEDDL-----------------ALMQLTSGSTGSPKA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 933 VKMSHSAVNALCRAIKLQCELYSSRQIAICLDPYC---GL-GFalwcLCS-VYSGHQSVLIPPMELENNLFLWLATVNQY 1007
Cdd:PRK07768 170 VQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFhdmGMvGF----LTVpMYFGAELVKVTPMDFLRDPLLWAELISKY 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1008 KIRDT----FcSYSVmelctkgLGNQVEVLKTRG-INLSCIRtCVVVAEERPRVSLQQSFSKLFKDIGLSPRAVSTTFG- 1081
Cdd:PRK07768 246 RGTMTaapnF-AYAL-------LARRLRRQAKPGaFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGm 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1082 --SRVNVAICLQGTsGPDPTTVYVDLKSLRHdRVRLVERGAPQSLLLSesGKILPGVKVVIVNpETKGPVGDSHLGEIWV 1159
Cdd:PRK07768 317 aeATLAVSFSPCGA-GLVVDEVDADLLAALR-RAVPATKGNTRRLATL--GPPLPGLEVRVVD-EDGQVLPPRGVGVIEL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1160 NSPHTASGYYTIYDSETLQADHfntrlsfGdaaqtlWARTGYLGFVrrTELtaatGErhdaLYVVGALDETLELRGLRYH 1239
Cdd:PRK07768 392 RGESVTPGYLTMDGFIPAQDAD-------G------WLDTGDLGYL--TEE----GE----VVVCGRVKDVIIMAGRNIY 448
|
490 500
....*....|....*....|
gi 226823266 1240 PIDIETSVSRVHRSIAECAV 1259
Cdd:PRK07768 449 PTDIERAAARVEGVRPGNAV 468
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
755-937 |
1.92e-04 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 45.90 E-value: 1.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 755 LAEILQWRAQATPDHVLFMLlnakGTTVCTASclQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYAG 834
Cdd:PRK06155 23 LPAMLARQAERYPDRPLLVF----GGTRWTYA--EAARAAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAWLG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 835 CIPVTV----RPPHaqnLTATLPTVRMVVDVSKAACVLTTQTLMRLLKSREAAAAVD---VKTWPAIIDTDDLPRKRLPQ 907
Cdd:PRK06155 96 AIAVPIntalRGPQ---LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLDapaSVSVPAGWSTAPLPPLDAPA 172
|
170 180 190
....*....|....*....|....*....|.
gi 226823266 908 LYKPPTP-EMLAYLDFSvSTTGMLTGVKMSH 937
Cdd:PRK06155 173 PAAAVQPgDTAAILYTS-GTTGPSKGVCCPH 202
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1130-1259 |
2.00e-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: 2.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1130 GKILPGVKVVIVNPETKGPVGDSHlGEIWVNSPHTASGYytiYDSETLQADHFNTRlsfgdaaqtlWARTGYLGFVRrte 1209
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGY---WNNPERTAEVLIDG----------WVNTGDLGERR--- 235
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 226823266 1210 ltaatgeRHDALYVVGALDETLELRGLRYHPIDIETSVSRVhRSIAECAV 1259
Cdd:cd17635 236 -------EDGFLFITGRSSESINCGGVKIAPDEVERIAEGV-SGVQECAC 277
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
753-846 |
2.45e-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: 45.40 E-value: 2.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 753 QFLAEILQWRAQATPDHVlfMLLNAKGTTvctaSCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLY 832
Cdd:cd05920 15 EPLGDLLARSAARHPDRI--AVVDGDRRL----TYRELDRRADRLAAGLRGLG-IRPGDRVVVQLPNVAEFVVLFFALLR 87
|
90
....*....|....
gi 226823266 833 AGCIPVTVRPPHAQ 846
Cdd:cd05920 88 LGAVPVLALPSHRR 101
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
789-1259 |
3.91e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.15 E-value: 3.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGhlnAGDNVV--LLYPPGIELIAAFYGCLYAGCIPVTVRPPHAQNLTATlptvrMVVDvSKAAC 866
Cdd:PRK12467 3125 ELNRRANRLAHRLIAIG---VGPDVLvgVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY-----MIED-SGVKL 3195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 867 VLTTQtlmRLLKSREAAAAVDVKTwpaiIDTDDLPrkrlPQLYKPPT----PEMLAYLDFSVSTTGMLTGVKMSHSAVNA 942
Cdd:PRK12467 3196 LLTQA---HLLEQLPAPAGDTALT----LDRLDLN----GYSENNPStrvmGENLAYVIYTSGSTGKPKGVGVRHGALAN 3264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 943 LCRAIKLQCELySSRQIAICLDPYCGLGFA---LWCLCsvySGHQsVLIPPMELENNLFLWlATVNQYKIrdtfcsySVM 1019
Cdd:PRK12467 3265 HLCWIAEAYEL-DANDRVLLFMSFSFDGAQerfLWTLI---CGGC-LVVRDNDLWDPEELW-QAIHAHRI-------SIA 3331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1020 ELCTKGLGNQVEVLKTRgiNLSCIRTCVVVAEERPRVSLQQSFSKLfkdiglsPRAvsttfgsrvnvaiCLQGTSGPDPT 1099
Cdd:PRK12467 3332 CFPPAYLQQFAEDAGGA--DCASLDIYVFGGEAVPPAAFEQVKRKL-------KPR-------------GLTNGYGPTEA 3389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1100 TVYVDLKSLRHDRVRLVErGAPqslllseSGKILPGVKVVIVNPETkGPVGDSHLGEIWVNSPHTASGYytiYDSETLQA 1179
Cdd:PRK12467 3390 VVTVTLWKCGGDAVCEAP-YAP-------IGRPVAGRSIYVLDGQL-NPVPVGVAGELYIGGVGLARGY---HQRPSLTA 3457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1180 DHFNTRlSFGDAAQTLWaRTGYLGFVRRTELtaatgerhdaLYVVGALDETLELRGLRYHPIDIETSVsRVHRSIAECAV 1259
Cdd:PRK12467 3458 ERFVAD-PFSGSGGRLY-RTGDLARYRADGV----------IEYLGRIDHQVKIRGFRIELGEIEARL-LQHPSVREAVV 3524
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
757-1021 |
8.81e-04 |
|
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: 8.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 757 EILQWRAQATPDHVlfmllnakgTTVC---TASCLQLHKRAERIASVLGDKGhLNAGDNVVLLYPPGIELIAAFYGCLYA 833
Cdd:cd17655 1 ELFEEQAEKTPDHT---------AVVFedqTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 834 GCIPVTVRPPHAQNltatlpTVRMVVDVSKAACVLTTQTLMRLLKSREAAAAvdvktwpaiIDTDDLPRKRLPQLYKPPT 913
Cdd:cd17655 71 GGAYLPIDPDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLIDL---------LDEDTIYHEESENLEPVSK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 914 PEMLAYLDFSVSTTGMLTGVKMSH--------SAVNALCRAIKLQCELYSSrqiaICLDPYCGLGFAlwclcSVYSGHQS 985
Cdd:cd17655 136 SDDLAYVIYTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFDASVTEIFA-----SLLSGNTL 206
|
250 260 270
....*....|....*....|....*....|....*.
gi 226823266 986 VLIPPMELENNLFLwLATVNQYKIRDTFCSYSVMEL 1021
Cdd:cd17655 207 YIVRKETVLDGQAL-TQYIRQNRITIIDLTPAHLKL 241
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
106-196 |
9.97e-04 |
|
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: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 106 ALQRWGSTQAKCPCLTGLDVTGKPVyTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYG 185
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGEDGEER-TLTYAELRREVNRFA-NALRALG------VKKGDRVAIYLPNI--PEAVIAMLA 83
|
90
....*....|.
gi 226823266 186 CLLAEVIPVPI 196
Cdd:COG0365 84 CARIGAVHSPV 94
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1130-1260 |
1.35e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 42.72 E-value: 1.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1130 GKILPGVKVVIVNpetkgpvgdshlGEIWVNSPHTASGYYTIYDsetlqadhfntrlsFGDAAQTLWARTGYLGFVrrte 1209
Cdd:PRK07824 195 GVPLDGVRVRVED------------GRIALGGPTLAKGYRNPVD--------------PDPFAEPGWFRTDDLGAL---- 244
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 226823266 1210 ltaatgerHD-ALYVVGALDETLELRGLRYHPIDIETSVSRvHRSIAECAVF 1260
Cdd:PRK07824 245 --------DDgVLTVLGRADDAISTGGLTVLPQVVEAALAT-HPAVADCAVF 287
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
133-224 |
1.47e-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: 1.47e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 133 LTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEvPLTRKDaggqQIGF 212
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKG------VRKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90
....*....|..
gi 226823266 213 LLGSCGIALALT 224
Cdd:cd05935 68 ILNDSGAKVAVV 79
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
132-234 |
1.62e-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: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 132 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNNDPvmFMVAFYGCLLAEVIPVPIEVPLTRKDaggqqIG 211
Cdd:cd17631 20 SLTYAELDERVNRLAHALRA-LG------VAKGDRVAVLSKNSPE--FLELLFAAARLGAVFVPLNFRLTPPE-----VA 85
|
90 100 110
....*....|....*....|....*....|
gi 226823266 212 FLLGSCGiALALTSEICL-------KGLPK 234
Cdd:cd17631 86 YILADSG-AKVLFDDLALlmytsgtTGRPK 114
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
115-202 |
1.71e-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: 42.62 E-value: 1.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 115 AKCPCLTGLDVTGKpvyTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVAlVYPNNDPVMFmVAFYGCLLA--EVI 192
Cdd:cd05945 2 AANPDRPAVVEGGR---TLTYRELKERADALA-AALASLG------LDAGDPVV-VYGHKSPDAI-AAFLAALKAghAYV 69
|
90
....*....|
gi 226823266 193 PVPIEVPLTR 202
Cdd:cd05945 70 PLDASSPAER 79
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
132-210 |
1.99e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 42.35 E-value: 1.99e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 132 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNndPVMFMVAFYGCLLAEVIPV-------PIEVPLTRKD 204
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPN--LLQYPIALFGILRAGMIVVnvnplytPRELEHQLND 119
|
....*.
gi 226823266 205 AGGQQI 210
Cdd:PRK08974 120 SGAKAI 125
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1126-1259 |
2.51e-03 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 41.95 E-value: 2.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 1126 LSESGKILPGVKVVIVNPETKgPVGDshlGEIWVNSPHTASGYY--TIYDSETLQADHFNTrlsfGDaaqtlwarTGYL- 1202
Cdd:cd05912 241 IGSAGKPLFPVELKIEDDGQP-PYEV---GEILLKGPNVTKGYLnrPDATEESFENGWFKT----GD--------IGYLd 304
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 226823266 1203 --GFV----RRTELTAATGERhdaLYvvgaldetlelrglryhPIDIETSVSRvHRSIAECAV 1259
Cdd:cd05912 305 eeGFLyvldRRSDLIISGGEN---IY-----------------PAEIEEVLLS-HPAIKEAGV 346
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
80-224 |
4.17e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 41.57 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 80 PEGRQMTPVKgePLGVIcnwppALESALQRWGSTQAKCPcltGLDVTGkpvYTLTYGKLWSRSLKLAyTLLNKLGtknep 159
Cdd:PRK06178 19 PAGIPREPEY--PHGER-----PLTEYLRAWARERPQRP---AIIFYG---HVITYAELDELSDRFA-ALLRQRG----- 79
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 226823266 160 vLKPGDRVALVYPNNdPvMFMVAFYGCLLAEVIPVPIEvPLTRkdagGQQIGFLLGSCGIALALT 224
Cdd:PRK06178 80 -VGAGDRVAVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFR----EHELSYELNDAGAEVLLA 136
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
128-202 |
4.70e-03 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 41.03 E-value: 4.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 128 KPVY-----TLTYGKLWSRSLKLAYTLLNKLGTKNEPVlkpgdrvaLVYPNNDPVMfMVAFYGCLLA--EVIPVPIEVPL 200
Cdd:PRK04813 18 FPAYdylgeKLTYGQLKEDSDALAAFIDSLKLPDKSPI--------IVFGHMSPEM-LATFLGAVKAghAYIPVDVSSPA 88
|
..
gi 226823266 201 TR 202
Cdd:PRK04813 89 ER 90
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
132-218 |
9.43e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 40.27 E-value: 9.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 132 TLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNNdpVMFMVAFYGCLLAEVIPVPIEVPLTrkdagGQQIG 211
Cdd:PRK08276 11 VVTYGELEARSNRLA-HGLRALG------LREGDVVAILLENN--PEFFEVYWAARRSGLYYTPINWHLT-----AAEIA 76
|
....*..
gi 226823266 212 FLLGSCG 218
Cdd:PRK08276 77 YIVDDSG 83
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
789-873 |
9.70e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 40.33 E-value: 9.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 226823266 789 QLHKRAERIASVLGDKGHLNAGDNVVLLYPPGIELIAAFYGCLYAGCIPVTVRPphaQNLTATLptvRMVVDVSKAACVL 868
Cdd:PRK08314 40 ELLEEAERLAGYLQQECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNP---MNREEEL---AHYVTDSGARVAI 113
|
....*
gi 226823266 869 TTQTL 873
Cdd:PRK08314 114 VGSEL 118
|
|
| |
