|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1007-1571 |
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: 741.47 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1007 LYVLLNAKGVAVCTATCVQLHKRAEKIAAALMERSGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPPH-PQNLS 1085
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1086 ATLPTVRMiiDVSKAACILTTQILTKILRSKEAATSVNIKTWPIIIDTDDLPRKRPPN-----IYKPPSADVIAYLDFSV 1160
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKlkkwgPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1161 STTGMLTGVKISHSAVSALCRSIKLQCELYSSRQLAICLDPYCGLGFVLWCLASVYSGHQSILIPPLELESSLSLWLSTL 1240
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1241 SQYRVRDTFCSYSVMELCTKGLGGQTDMLKARGVNLACVRSCVVVAEERPRLALTQSFSKLFKDLGLSTRAVSTAFGSRV 1320
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1321 NLAICLQGTTGPDPSTVYVDMKSLRHDRVRLVERGAPQSLPLMESGTILPGVRVVIVNPETRGPLGDSHLGEIWVNSPHT 1400
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1401 ASGYYTIYGEESLQADHFN-TKLSFGDPHTLWARTGYLGFVKRTELTDSSGERHDALFIVGSLDETLELRGLRYHPIDIE 1479
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFPsTRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1480 ISVQRAHRSIGESAVFTWTNLLVVVSEL-CGSEQDALDLVPLITNVVLEEHHLIVGVVVIVDPGVIPINSRGEKQRMHLR 1558
Cdd:cd05905 479 ATVMRVHPYRGRCAVFSITGLVVVVAEQpPGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIR 558
|
570
....*....|...
gi 2264466784 1559 DSFLADQLDPIYV 1571
Cdd:cd05905 559 QAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
346-922 |
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: 691.01 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 346 ALTTLDITGKPLYTLTYGKLWSRGVKLAYTLLNKLGtkneqvLKPGDRVALVYPnsDPGMFWVAFYGCLLAEVIPVPIEV 425
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 426 PLsrkdaGSSQVGFLLGSCGVSLALTSEICLKGLPKT-----STGEILQFKGWPRLKWVITDSKYLTKPSKDWQPHIPTA 500
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 501 NIDTAYIEYKASKEGTVVGVAVSKIAMLTHCQALSQACNYCEGETLVNVLDFKKDMGLWHGVLTSVMNRIHTICVPYAVM 580
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 581 KACPLSWVQRVHIHKARVALVKCRDLHWAMM------AHKEQRDISLSSLRMLIVADGaNPWSVSSCDAYLNVFQAHGLK 654
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKdlsstlASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 655 PEVIcpcatSPEAMTVAIRRPGVPGA--PLPARAVLSMTGLSHGVIRVNTEDKNSALTVQDVGHVMPGALMCIVKPDGPP 732
Cdd:cd05905 307 PRAV-----STEFGTRVNPFICWQGTsgPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 733 mLCKTDEIGEIVVNSRAGGTLYYGLQGVTKNTFEVIPVNASGAPIGEIPFVRSGLLGFVGPGS----------LIFVVGK 802
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTKctdlnveehdLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 803 NEGLLVVSGRRHNADDLVATALAVEPvktvYRGRIAVFSVTvfydERIVIVAEQRPdASEEDSFQWMSRVLQAIDSIHQV 882
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 2264466784 883 GLYCLALVPANTLPKTPLGGIHISDTKQLFLEGALHPCNI 922
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
997-1563 |
5.51e-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: 231.36 E-value: 5.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 997 WRAQTDPDHVLYVLLNAKGVAVCTATCVQLHKRAEKIAAALMERSGIsiGENIVLLYPPGIDLIAAFYGCLYAGCIPVTV 1076
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGKP--GDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1077 RPPHPqnlSATLPTVRMIIDVSKAACILTTQILTKILRSKEAATSVNIKTWPIIIDTDDLPRKRPPNIYKPPSADvIAYL 1156
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDD-IAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1157 DFSVSTTGMLTGVKISHSAVSALCRSIKLQCELYSSRQLAICLDPYCGLGFVLWCLASVYSGHQSILIPPLElesslslw 1236
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAA-------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1237 lstlsqY------------RVRDTFcsySVM-----ELCTKGLGGQtdmlKARGVNLACVRSCVVVAEeRPRLALTQSFS 1299
Cdd:cd05931 227 ------FlrrplrwlrlisRYRATI---SAApnfayDLCVRRVRDE----DLEGLDLSSWRVALNGAE-PVRPATLRRFA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1300 KLFKDLGLSTRAVSTAFGsrvnLA-ICLQGTTGP---DPSTVYVDMKSLRHdRVRLVERGAPQSLPLMESGTILPGVRVV 1375
Cdd:cd05931 293 EAFAPFGFRPEAFRPSYG----LAeATLFVSGGPpgtGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQEVR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1376 IVNPETRGPLGDSHLGEIWVNSPHTASGYytiYGEESLQADHFNTKLsfGDPHTLWARTGYLGFVKRteltdssGErhda 1455
Cdd:cd05931 368 IVDPETGRELPDGEVGEIWVRGPSVASGY---WGRPEATAETFGALA--ATDEGGWLRTGDLGFLHD-------GE---- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1456 LFIVGSLDETLELRGLRYHPIDIEISVQRAHRSIGESAVFTWTNL------LVVVSELcGSEQDALDLVPLITNV---VL 1526
Cdd:cd05931 432 LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPGCVAAFSVPddgeerLVVVAEV-ERGADPADLAAIAAAIraaVA 510
|
570 580 590
....*....|....*....|....*....|....*..
gi 2264466784 1527 EEHHLIVGVVVIVDPGVIPINSRGEKQRMHLRDSFLA 1563
Cdd:cd05931 511 REHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYLD 547
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
336-913 |
2.58e-63 |
|
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: 226.35 E-value: 2.58e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 336 RWGATQGKSPALTTLDITGKPLYTLTYGKLWSRGVKLAYTLLnklgtkneQVLKPGDRVALVYPnsdPGM-FWVAFYGCL 414
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAP---PGLdFVAAFLGCL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 415 LAEVIPVPIEVPLSRKDAGssQVGFLLGSCGVSLALTSEICLKGLPKTstgeILQFKGWPRLKWVITDSKyLTKPSKDWQ 494
Cdd:cd05931 70 YAGAIAVPLPPPTPGRHAE--RLAAILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLL-PDTSAADWP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 495 PHIPTANiDTAYIEYKASKEGTVVGVAVSKIAMLTHCQALSQACNYCEGETLVNVLDFKKDMGLWHGVLTSVMNRIHtiC 574
Cdd:cd05931 143 PPSPDPD-DIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGP--S 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 575 V---PYAVMKAcPLSWVQRVHIHKARV------ALVKCrdlhwAMMAHKEQRD-ISLSSLRMLIVadGANPWSVSSCDAY 644
Cdd:cd05931 220 VlmsPAAFLRR-PLRWLRLISRYRATIsaapnfAYDLC-----VRRVRDEDLEgLDLSSWRVALN--GAEPVRPATLRRF 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 645 LNVFQAHGLKPEVICPC-----ATspeaMTVAIRRPGVPgaplPARAVLSMTGLSHGViRVNTEDKNSALTVQDVGHVMP 719
Cdd:cd05931 292 AEAFAPFGFRPEAFRPSyglaeAT----LFVSGGPPGTG----PVVLRVDRDALAGRA-VAVAADDPAARELVSCGRPLP 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 720 GALMCIVKPDGPPmLCKTDEIGEIVVNSRAGGTLYYGLQGVTKNTFEVIPVNASGapigeiPFVRSGLLGFVGPGSLiFV 799
Cdd:cd05931 363 DQEVRIVDPETGR-ELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEG------GWLRTGDLGFLHDGEL-YI 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 800 VGKNEGLLVVSGRRHNADDLVATALAVEPVktVYRGRIAVFSVTVFYDERIVIVAEQRPDASEEDSFQWMSRVLQAIDSI 879
Cdd:cd05931 435 TGRLKDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVARE 512
|
570 580 590
....*....|....*....|....*....|....
gi 2264466784 880 HQVGLYCLALVPANTLPKTPLGGIHISDTKQLFL 913
Cdd:cd05931 513 HGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
995-1469 |
1.14e-45 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 170.96 E-value: 1.14e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 995 LQWRAQTDPDHVlyVLLNAKGVAVctaTCVQLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPV 1074
Cdd:pfam00501 1 LERQAARTPDKT--ALEVGEGRRL---TYRELDERANRLAAGLRAL-GVGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1075 TVRPphpqnlSATLPTVRMIIDVSKAACILTTQILtKILRSKEAATSVNIKTWPIIIDTDDLPRKRPPNIYK-------- 1146
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDDAL-KLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAkpadvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1147 ---PPSADVIAYLDFSVSTTGMLTGVKISHSAVSALCRSIKLQCE----LYSSRQLAICLDPYCGLGFVLWCLASVYSGH 1219
Cdd:pfam00501 148 pppPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1220 QSILIPPlELESSLSLWLSTLSQYRVRDTFCSYSVMELCTKGLGGQTDMLKArgvnlacVRSCVVVAeERPRLALTQSFS 1299
Cdd:pfam00501 228 TVVLPPG-FPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSS-------LRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1300 KLFKdlglstRAVSTAFGSRVNLAICLQGTTGPDpstvyvDMKSLRHdrvrlvergapqslplmeSGTILPGVRVVIVNP 1379
Cdd:pfam00501 299 ELFG------GALVNGYGLTETTGVVTTPLPLDE------DLRSLGS------------------VGRPLPGTEVKIVDD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1380 ETRGPLGDSHLGEIWVNSPHTASGYytiYGEESLQADHFNTKlsfGdphtlWARTGYLGFVkrteltDSSGErhdaLFIV 1459
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAFDED---G-----WYRTGDLGRR------DEDGY----LEIV 407
|
490
....*....|
gi 2264466784 1460 GSLDETLELR 1469
Cdd:pfam00501 408 GRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
987-1569 |
2.54e-37 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 154.94 E-value: 2.54e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 987 MHHYLSEALQWRAQTDPDHV-LYVLLNAKGVAVcTATCVQLHKRAEKIAAALMERSGIsiGENIVLLYPPGIDLIAAFYG 1065
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLaLRFLADDPGEGV-VLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1066 CLYAGCIPVTVRPP------HPQNLSAtlptvrmIIDVSKAACILTTQILTKILRSKEAATSVNIKTWpIIIDTDD---L 1136
Cdd:PRK05691 84 CLYAGVIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANAPEL-LCVDTLDpalA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1137 PRKRPPNIykppSADVIAYLDFSVSTTGMLTGVKISHSAVSAlcrsiklqCELYSSRQLAICLDP----------YCGLG 1206
Cdd:PRK05691 156 EAWQEPAL----QPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1207 FVLWCLASVYSGHQSILIPPLELESSLSLWLSTLSQYRVRDT--------FCSYSVMELCTKGLggqtDMLKARgvnlac 1278
Cdd:PRK05691 224 LIGGLLQPIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTISggpdfayrLCSERVSESALERL----DLSRWR------ 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1279 vrscVVVAEERP-RLALTQSFSKLFKDLGLSTRAVSTAFGSRVNLAICLQGTTGPDPSTVYVDMKSLRHDRvrlVERGAP 1357
Cdd:PRK05691 294 ----VAYSGSEPiRQDSLERFAEKFAACGFDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNR---AEPGTG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1358 QslPLMESGTILPGVRVVIVNPETRGPLGDSHLGEIWVNSPHTASGYYTiYGEESLQA--DHfntklsfgDPHTlWARTG 1435
Cdd:PRK05691 367 S--VLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR-NPEASAKTfvEH--------DGRT-WLRTG 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1436 YLGFVkrteltdssgeRHDALFIVGSLDETLELRGLRYHPIDIEISVQRAHRSI--GESAVFTWTNL----LVVVSELCG 1509
Cdd:PRK05691 435 DLGFL-----------RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVrkGRVAAFAVNHQgeegIGIAAEISR 503
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2264466784 1510 SEQDAL---DLVPLITNVVLEEHHLIVGVVVIVDPGVIPINSRGEKQRMHLRDSFLADQLDPI 1569
Cdd:PRK05691 504 SVQKILppqALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDSY 566
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
995-1567 |
2.46e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 143.93 E-value: 2.46e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 995 LQWRAQTDPDHVLYVLL----NAKGVAVcTATCVQLHKRAEKIAAALMERSgiSIGENIVLLYPPGIDLIAAFYGCLYAG 1070
Cdd:PRK05850 7 LRERASLQPDDAAFTFIdyeqDPAGVAE-TLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGALQAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1071 CIPVTVRPPHPqnlSATLPTVRMIIDVSKAACILTTQILTKILRSKEAATSVNIKTWPIIIDTDDLPRKRPPNIyKPPSA 1150
Cdd:PRK05850 84 LIAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDA-RPRDL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1151 DVIAYLDFSVSTTGMLTGVKISHSAVSA----LCRSIKLQCELYSSRQLAIC--LDPYCGLGFVLWCLASVYSGHQSILI 1224
Cdd:PRK05850 160 PSTAYLQYTSGSTRTPAGVMVSHRNVIAnfeqLMSDYFGDTGGVPPPDTTVVswLPFYHDMGLVLGVCAPILGGCPAVLT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1225 PPLELEsslslwlstlsQYRVR------DTFCSYSV-----MELCTKglggQT---DMlkaRGVNLACVRsCVVVAEERP 1290
Cdd:PRK05850 240 SPVAFL-----------QRPARwmqllaSNPHAFSAapnfaFELAVR----KTsddDM---AGLDLGGVL-GIISGSERV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1291 RLALTQSFSKLFKDLGLSTRAVSTAFG---SRVNLAIclqGTTGPDPSTVYVDMKSLRHDRVR---------LVERGAPQ 1358
Cdd:PRK05850 301 HPATLKRFADRFAPFNLRETAIRPSYGlaeATVYVAT---REPGQPPESVRFDYEKLSAGHAKrcetgggtpLVSYGSPR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1359 SlplmesgtilPGVRvvIVNPETRGPLGDSHLGEIWVNSPHTASGYytiYGEESLQADHFNTKL---SFGDPHTLWARTG 1435
Cdd:PRK05850 378 S----------PTVR--IVDPDTCIECPAGTVGEIWVHGDNVAAGY---WQKPEETERTFGATLvdpSPGTPEGPWLRTG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1436 YLGFVkrteltdSSGErhdaLFIVGSLDETLELRGLRYHPIDIEISVQRAHRsiGESAVFT----WTNLLVVVSEL---C 1508
Cdd:PRK05850 443 DLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATIQEITG--GRVAAISvpddGTEKLVAIIELkkrG 509
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2264466784 1509 GSEQDALDLVPLITNVVL----EEHHLIVGVVVIVDPGVIPINSRGEKQR-----MHLRDSFlaDQLD 1567
Cdd:PRK05850 510 DSDEEAMDRLRTVKREVTsaisKSHGLSVADLVLVAPGSIPITTSGKIRRaacveQYRQDEF--TRLD 575
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
368-917 |
1.16e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 129.85 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 368 RGVKLAYTLLN---------------KLGTKN-------EQVLKPGDRVALVYPNS-DpgmFWVAFYGCLLAEVIPVPIE 424
Cdd:PRK07769 34 RGDKLAYRFLDfsterdgvardltwsQFGARNravgarlQQVTKPGDRVAILAPQNlD---YLIAFFGALYAGRIAVPLF 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 425 VP-----LSRKDAgssqvgfLLGSCGVSLALTSEICLKGLPKTSTGeiLQFKGWPRLKWV--ITDSKYLTkpskdWQPhi 497
Cdd:PRK07769 111 DPaepghVGRLHA-------VLDDCTPSAILTTTDSAEGVRKFFRA--RPAKERPRVIAVdaVPDEVGAT-----WVP-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 498 PTANIDT-AYIEYKASKEGTVVGVAVSKIAMLTHCQALSQACNYCEGETLVNVLDFKKDMGLWHGVLTSVMNRIHTICVP 576
Cdd:PRK07769 175 PEANEDTiAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 577 YAVMKAcPLSWVQRVhihkARVALVKCRDLHWA---MMAHKEQR--------DISLSSLRMLIvaDGANPWSVSSCDAYL 645
Cdd:PRK07769 255 AAFVRR-PGRWIREL----ARKPGGTGGTFSAApnfAFEHAAARglpkdgepPLDLSNVKGLL--NGSEPVSPASMRKFN 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 646 NVFQAHGLKPEVICPCATSPEAmTVAIRRPGVPGAPlpaRAV-LSMTGLSHG-VIRVNTEDKNsALTVQDVGHVMPGALM 723
Cdd:PRK07769 328 EAFAPYGLPPTAIKPSYGMAEA-TLFVSTTPMDEEP---TVIyVDRDELNAGrFVEVPADAPN-AVAQVSAGKVGVSEWA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 724 CIVKPDGPPMLcKTDEIGEIVVNSRAGGTLYYGLQGVTKNTFEVI------PVNASGAPIGEIpFVRSGLLGFVGPGSLi 797
Cdd:PRK07769 403 VIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGKPEETAATFQNIlksrlsESHAEGAPDDAL-WVRTGDYGVYFDGEL- 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 798 FVVGKNEGLLVVSGRRHNADDLVATALavEPVKTVYRGRIAVFSV-------TVFYD-------------ERIVIVAEQR 857
Cdd:PRK07769 480 YITGRVKDLVIIDGRNHYPQDLEYTAQ--EATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERA 557
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 858 PDASEEDSFQWMSRVLQAIDSIHQVGLYCLALVPANTLPKTPLGGIHISDTKQLFLEGAL 917
Cdd:PRK07769 558 PGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1153-1553 |
2.20e-28 |
|
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: 118.16 E-value: 2.20e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1153 IAYLDFSVSTTGMLTGVKISHSAVSALCRSIkLQCELYSSRQLAICLDPYCGLGFVLWCLASVYSGHQSILIPPLELESS 1232
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1233 LSLWLstlsQYRVRDTFCSYSVMELCTKGLggqtdmlKARGVNLACVRSCVVVAEERPRlALTQSFSKLFKDlglstrAV 1312
Cdd:cd04433 81 LELIE----REKVTILLGVPTLLARLLKAP-------ESAGYDLSSLRALVSGGAPLPP-ELLERFEEAPGI------KL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1313 STAFGSrvnlaiclqgT-TGPDPSTVYVDMKSLRHDrvrlvergapqslplmESGTILPGVRVVIVNPETrGPLGDSHLG 1391
Cdd:cd04433 143 VNGYGL----------TeTGGTVATGPPDDDARKPG----------------SVGRPVPGVEVRIVDPDG-GELPPGEIG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1392 EIWVNSPHTASGYYTIYgeeslqadhFNTKLSFGDphtLWARTGYLGFVkrteltdssgERHDALFIVGSLDETLELRGL 1471
Cdd:cd04433 196 ELVVRGPSVMKGYWNNP---------EATAAVDED---GWYRTGDLGRL----------DEDGYLYIVGRLKDMIKSGGE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1472 RYHPIDIEiSVQRAHRSIGESAVF-----TWTNLLVVVSELC-GSEQDALDLVPLITNVVleEHHLIVGVVVIVDPgvIP 1545
Cdd:cd04433 254 NVYPAEVE-AVLLGHPGVAEAAVVgvpdpEWGERVVAVVVLRpGADLDAEELRAHVRERL--APYKVPRRVVFVDA--LP 328
|
....*...
gi 2264466784 1546 INSRGEKQ 1553
Cdd:cd04433 329 RTASGKID 336
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
360-919 |
1.11e-25 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 113.95 E-value: 1.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 360 LTYGKLWSRGVKLAYTLLNkLGtkneqvLKPGDRVALVyPNSDPGmFWVAFYGCLLAEVIPVPIEVPLS--RKDAGSSQV 437
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLA-LG------LKPGDRVALI-AETDGD-FVEAFFACQYAGLVPVPLPLPMGfgGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 438 GFLLGSCGVSLALTSEICLKGLPKTSTGEilqfkgwpRLKWVITDSKYLTKPSKDWQPHIPTANiDTAYIEYKASKEGTV 517
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGN--------PLLHVLSHAWFKALPEADVALPRPTPD-DIAYLQYSSGSTRFP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 518 VGVAVSKIAMLTHCQALSQ-ACNYCEGETLVNVLDFKKDMGLWHGVLTSVMNRIHTICVPYAVMKACPLSWVQRVHIHKA 596
Cdd:PRK09192 192 RGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQWLDLISRNRG 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 597 RVALVKC--RDLHWAMMAHKEQRDISLSSLRmlIVADGANPWSVSSCDAYLNVFQAHGLKPEVICPCATSPEAmTVAirr 674
Cdd:PRK09192 272 TISYSPPfgYELCARRVNSKDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEA-TLA--- 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 675 pgvpgaplparavLSMTGLSHGvIRVNT------EDKNSALTVQD----------VGHVMPGALMCIVKPDGPPMlcKTD 738
Cdd:PRK09192 346 -------------VSFSPLGSG-IVVEEvdrdrlEYQGKAVAPGAetrrvrtfvnCGKALPGHEIEIRNEAGMPL--PER 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 739 EIGEIVVnsrAGGTL---YYGLQGVTKntfeVIPVNAsgapigeipFVRSGLLGFVGPGSlIFVVGKNEGLLVVSGRRHN 815
Cdd:PRK09192 410 VVGHICV---RGPSLmsgYFRDEESQD----VLAADG---------WLDTGDLGYLLDGY-LYITGRAKDLIIINGRNIW 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 816 ADDLVATALAVEPVKTvyrGRIAVFSVTVFYDERIVIVAEQRPdASEEDSFQWMSRVLQAIDSIHqvGLYCL-ALVPANT 894
Cdd:PRK09192 473 PQDIEWIAEQEPELRS---GDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHS 546
|
570 580
....*....|....*....|....*
gi 2264466784 895 LPKTPLGGIHISDTKQLFLEGALHP 919
Cdd:PRK09192 547 LPRTSSGKLSRAKAKKRYLSGAFAS 571
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1025-1568 |
1.80e-25 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 113.68 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1025 QLHKRAEKIAAALMERSGIsiGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPP----HPQNLSATL----PTVrmiid 1096
Cdd:PRK12476 73 QLGVRLRAVGARLQQVAGP--GDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV----- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1097 vskaacILTTQILTKILRSKEAATSVNIKtwPIIIDTDDLPRKRPPN-IYKPPSADVIAYLDFSVSTTGMLTGVKISHSA 1175
Cdd:PRK12476 146 ------VLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPDSAGESfVPVELDTDDVSHLQYTSGSTRPPVGVEITHRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1176 VSALCRSIKLQCELYSSRQLAICLDP-YCGLGFVLWCLASVYSGHQSILIPPLELESSLSLWLSTLSQYRVRDTFCSYS- 1253
Cdd:PRK12476 218 VGTNLVQMILSIDLLDRNTHGVSWLPlYHDMGLSMIGFPAVYGGHSTLMSPTAFVRRPQRWIKALSEGSRTGRVVTAAPn 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1254 -VMELCT-KGLGGQTDMLKARGVNLacvrscvVVAEERPRLALTQSFSKLFKDLGLSTRAVSTAFGsrVNLAICLQGTTG 1331
Cdd:PRK12476 298 fAYEWAAqRGLPAEGDDIDLSNVVL-------IIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG--IAEATLFVATIA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1332 PD--PSTVYVDMKSLRHDRVRLVERGAPQSLPLMESGTILPGVRVVIVNPETRGPLGDSHLGEIWVNSPHTASGYYTIYG 1409
Cdd:PRK12476 369 PDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1410 EeslqadhfnTKLSFG----------------DPHTLWARTGYLGFVKRTEltdssgerhdaLFIVGSLDETLELRGLRY 1473
Cdd:PRK12476 449 E---------TERTFGaklqsrlaegshadgaADDGTWLRTGDLGVYLDGE-----------LYITGRIADLIVIDGRNH 508
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1474 HPIDIEISVQRAHRSI--GESAVFTW----TNLLVVVSELCG--SEQDALDLVPLITNVVLEEHHLIVGVVVIVDPGVIP 1545
Cdd:PRK12476 509 YPQDIEATVAEASPMVrrGYVTAFTVpaedNERLVIVAERAAgtSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIP 588
|
570 580
....*....|....*....|...
gi 2264466784 1546 INSRGEKQRMHLRDSFLADQLDP 1568
Cdd:PRK12476 589 RTTSGKLARRACRAQYLDGRLGV 611
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
359-903 |
3.54e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 112.34 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 359 TLTYGKLWSRGVKLAYTLlNKLGTkneqvlkPGDRVALVYPNsdpGM-FWVAFYGCLLAEVIPVPIEVPLSRkdAGSSQV 437
Cdd:PRK05850 35 TLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQ---GLeYIVAFLGALQAGLIAVPLSVPQGG--AHDERV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 438 GFLLGSCGVSLALTseiclkglpkTST--GEILQFKGWPRLK---WVIT-DSKYLTKPSKdwqPHIPTANI-DTAYIEYK 510
Cdd:PRK05850 102 SAVLRDTSPSVVLT----------TSAvvDDVTEYVAPQPGQsapPVIEvDLLDLDSPRG---SDARPRDLpSTAYLQYT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 511 ASKEGTVVGVAVSKIAMLTHC-QALSQACNYCEGE-----TLVNVLDFKKDMGLWHGVLTSVMNRIHTICV-PYAVMKAc 583
Cdd:PRK05850 169 SGSTRTPAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTsPVAFLQR- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 584 PLSWVQRVHIHKA----------RVALVKCRDlhwAMMAHKEQRDIslsslrmLIVADGANPWSVSSCDAYLNVFQAHGL 653
Cdd:PRK05850 248 PARWMQLLASNPHafsaapnfafELAVRKTSD---DDMAGLDLGGV-------LGIISGSERVHPATLKRFADRFAPFNL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 654 KPEVICPCATSPEAMT-VAIRRPGVPgaplPARAVLSMTGLSHGVIRVNTEDKNSALtvqdVGHVMPGA-LMCIVKPDgP 731
Cdd:PRK05850 318 RETAIRPSYGLAEATVyVATREPGQP----PESVRFDYEKLSAGHAKRCETGGGTPL----VSYGSPRSpTVRIVDPD-T 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 732 PMLCKTDEIGEIVVNSRAGGTLYYGLQGVTKNTFEVIPVNAS-GAPIGeiPFVRSGLLGFVGPGSLiFVVGKNEGLLVVS 810
Cdd:PRK05850 389 CIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATLVDPSpGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIVD 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 811 GRRHNADDLVATalavepVKTVYRGRIAVFSVTVFYDERIVIVAE-QRPDASEEDSFQWM----SRVLQAIDSIHQVGLY 885
Cdd:PRK05850 466 GRNHYPDDIEAT------IQEITGGRVAAISVPDDGTEKLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVA 539
|
570
....*....|....*...
gi 2264466784 886 CLALVPANTLPKTPLGGI 903
Cdd:PRK05850 540 DLVLVAPGSIPITTSGKI 557
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
327-919 |
4.85e-24 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 109.06 E-value: 4.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 327 PPA--LQAALARWGATQGKSPALTTLDITGKPLYT---LTYGKLWSRgvklaytlLNKLGTKNEQVLKPGDRVALVYPNs 401
Cdd:PRK12476 31 PPGttLISLIERNIANVGDTVAYRYLDHSHSAAGCaveLTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQ- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 402 dpGMFWVA-FYGCLLAEVIPVPIEVP-----LSRKDAgssqvgfLLGSCGVSLALTSeiclkGLPKTSTGEILqfKGWPR 475
Cdd:PRK12476 102 --GIDYVAgFFAAIKAGTIAVPLFAPelpghAERLDT-------ALRDAEPTVVLTT-----TAAAEAVEGFL--RNLPR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 476 LK--WVITDSKYLTKPSKDWQPhIPTANIDTAYIEYKASKEGTVVGVAVSKIAMLTHCQALSQACNYCEGETL-VNVLDF 552
Cdd:PRK12476 166 LRrpRVIAIDAIPDSAGESFVP-VELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTHgVSWLPL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 553 KKDMGLWHGVLTSVMNRIHTICVPYAVMKAcPLSWVQRVHI--HKARVaLVKCRDLHWAMMAH----KEQRDISLSSLRM 626
Cdd:PRK12476 245 YHDMGLSMIGFPAVYGGHSTLMSPTAFVRR-PQRWIKALSEgsRTGRV-VTAAPNFAYEWAAQrglpAEGDDIDLSNVVL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 627 LIvadGANPWSVSSCDAYLNVFQAHGLKPEVICPCATSPEA-MTVAIRRPgvpgAPLPARAVLSMTGLSHG-VIRVNTED 704
Cdd:PRK12476 323 II---GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEAtLFVATIAP----DAEPSVVYLDREQLGAGrAVRVAADA 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 705 KNSALTVQdVGHVMPGALMCIVKPDGPPMLcKTDEIGEIVVNSRAGGTLYYGLQGVTKNTFEV-----IP--VNASGAPI 777
Cdd:PRK12476 396 PNAVAHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAegSHADGAAD 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 778 GEIpFVRSGLLGFVGPGSLiFVVGKNEGLLVVSGRRHNADDLVATALAVEPVktVYRGRIAVFSVTVFYDERIVIVAEQR 857
Cdd:PRK12476 474 DGT-WLRTGDLGVYLDGEL-YITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERA 549
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2264466784 858 PDASEEDSFQWMSRVLQAIDSIHQVGLYCLALVPANTLPKTPLGGIHISDTKQLFLEGALHP 919
Cdd:PRK12476 550 AGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
330-917 |
4.93e-24 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 107.20 E-value: 4.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 330 LQAALARWGATQGKSPALTTLDITgkplytLTYGKLWSRGVKLAyTLLNKLGtkneqvLKPGDRVALVYPNSdPGMFwVA 409
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLA-AALRALG------VGPGDRVALLLPNS-PEFV-VA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 410 FYGCLLAEVIPVPIEVPLSRKdagssQVGFLLGSCGVSLALTSEICLkglpkTS--TGeilqfkgwprlkwvitdskylt 487
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSGARALVTALILY-----TSgtTG---------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 488 kpskdwqphiptanidtayieykaskegtvvgvaVSKIAMLTH------CQALSQACNYCEGETLVNVLDFKKDMGLWHG 561
Cdd:COG0318 114 ----------------------------------RPKGVMLTHrnllanAAAIAAALGLTPGDVVLVALPLFHVFGLTVG 159
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 562 VLTSVMNRIHTICVPYAVmkacPLSWVQRVHIHKA-RVALVKcrDLHWAMMAHKEQRDISLSSLRMLIVadGANPWSVSS 640
Cdd:COG0318 160 LLAPLLAGATLVLLPRFD----PERVLELIERERVtVLFGVP--TMLARLLRHPEFARYDLSSLRLVVS--GGAPLPPEL 231
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 641 CDAYLNVFQAhglkpeVICPC--ATspEAMTVAIRRPGVPGAPLPARavlsmtglshgvirvntedknsaltvqdVGHVM 718
Cdd:COG0318 232 LERFEERFGV------RIVEGygLT--ETSPVVTVNPEDPGERRPGS----------------------------VGRPL 275
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 719 PGALMCIVKPDGPPmlCKTDEIGEIVV--NSRAGGtlYYGLQGVTKNTFevipvnASGapigeipFVRSGLLGFVGPGSL 796
Cdd:COG0318 276 PGVEVRIVDEDGRE--LPPGEVGEIVVrgPNVMKG--YWNDPEATAEAF------RDG-------WLRTGDLGRLDEDGY 338
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 797 IFVVGKNEGLLVVSGRRHNADDLVATALAVEPVKTVyrgriAVFSVTV-FYDERIV--IVAEQRPDASEEDSFQWMSRVL 873
Cdd:COG0318 339 LYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEA-----AVVGVPDeKWGERVVafVVLRPGAELDAEELRAFLRERL 413
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 2264466784 874 QAIDSIHQVglyclalVPANTLPKTPLGGIHISDTKQLFLEGAL 917
Cdd:COG0318 414 ARYKVPRRV-------EFVDELPRTASGKIDRRALRERYAAGAL 450
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
995-1566 |
7.73e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 108.66 E-value: 7.73e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 995 LQWRAQTDPDHVLYVLLN----AKGVAvCTATCVQLHKRAEKIAAALMERSgiSIGENIVLLYPPGIDLIAAFYGCLYAG 1070
Cdd:PRK07769 27 VERWAKVRGDKLAYRFLDfsteRDGVA-RDLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1071 CIPVTV----RPPHPQNLSATLptvrmiiDVSKAACILTTQiltkilrskEAATSVN--IKTwpiiidtddLPRKRPPNI 1144
Cdd:PRK07769 104 RIAVPLfdpaEPGHVGRLHAVL-------DDCTPSAILTTT---------DSAEGVRkfFRA---------RPAKERPRV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1145 -------------YKPPSA--DVIAYLDFSVSTTGMLTGVKISHSAVSA----LCRSIKLQcelYSSRQLAiCLDPYCGL 1205
Cdd:PRK07769 159 iavdavpdevgatWVPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLPTnvlqVIDALEGQ---EGDRGVS-WLPFFHDM 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1206 GFVLWCLASVYSGHQSILIPplelesslslWLSTLSQYRvrdtfcsySVMELCTKG-LGGQT---------DMLKARGV- 1274
Cdd:PRK07769 235 GLITVLLPALLGHYITFMSP----------AAFVRRPGR--------WIRELARKPgGTGGTfsaapnfafEHAAARGLp 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1275 -------NLACVRsCVVVAEERPRLALTQSFSKLFKDLGLSTRAVSTAFGsrVNLAICLQGTTGPD--PSTVYVDMKSLR 1345
Cdd:PRK07769 297 kdgepplDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYG--MAEATLFVSTTPMDeePTVIYVDRDELN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1346 HDRVRLVERGAPQSLPLMESGTILPGVRVVIVNPETRGPLGDSHLGEIWVNSPHTASGYytiYGEESLQADHFNTKLSFG 1425
Cdd:PRK07769 374 AGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGY---WGKPEETAATFQNILKSR 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1426 DPHT---------LWARTGYLG-FVKrteltdssGErhdaLFIVGSLDETLELRGLRYHPIDIEISVQRAHRSI--GESA 1493
Cdd:PRK07769 451 LSEShaegapddaLWVRTGDYGvYFD--------GE----LYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALrtGYVA 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1494 VF--------------TWTNL----------LVVVSELcGSEQDALDLVPLITNV---VLEEHHLIVGVVVIVDPGVIPI 1546
Cdd:PRK07769 519 AFsvpanqlpqvvfddSHAGLkfdpedtseqLVIVAER-APGAHKLDPQPIADDIraaIAVRHGVTVRDVLLVPAGSIPR 597
|
650 660
....*....|....*....|
gi 2264466784 1547 NSRGEKQRMHLRDSFLADQL 1566
Cdd:PRK07769 598 TSSGKIARRACRAAYLDGSL 617
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
319-915 |
8.49e-24 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 107.75 E-value: 8.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 319 PLGVVSNWPPALQAALARWgATQGKSPALTTLDITGKPlYTLTYGKLWSRGVKLAyTLLNKLGtkneqvLKPGDRVALVY 398
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRA-AERGPTKGITYIDADGSE-EFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 399 P-NSDpgmFWVAFYGCLLAEVIPVPIEVPLSRkDAGSSQVGFLlgsCGVSLALTSEICLkglpkTSTGEILQFKG----W 473
Cdd:cd05906 72 DdNED---FIPAFWACVLAGFVPAPLTVPPTY-DEPNARLRKL---RHIWQLLGSPVVL-----TDAELVAEFAGletlS 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 474 PRLKWVITDSKYLTKPSKDWQPHIPTANiDTAYIEYKASKEGTvvgvavSKIAMLTH------CQALSQACNYCEGETLV 547
Cdd:cd05906 140 GLPGIRVLSIEELLDTAADHDLPQSRPD-DLALLMLTSGSTGF------PKAVPLTHrnilarSAGKIQHNGLTPQDVFL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 548 NVLDFKKDMGLWHGVLTSVMNRIHTICVPYAVMKACPLSWVQRVHIHKARV------ALVKCRDLhwamMAHKEQRDISL 621
Cdd:cd05906 213 NWVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLNDL----LEEIEDGTWDL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 622 SSLRMLIVADGANpwSVSSCDAYLNVFQAHGLKPEVICPCatspeamtvairrpgvpgaplparavLSMTGLSHGVI--- 698
Cdd:cd05906 289 SSLRYLVNAGEAV--VAKTIRRLLRLLEPYGLPPDAIRPA--------------------------FGMTETCSGVIysr 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 699 RVNTEDKNSALTVQDVGHVMPGALMCIVKPDGPPMLckTDEIGEIVV--NSRAGGtlYYGLQGVTKNTFevipvNASGap 776
Cdd:cd05906 341 SFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLP--EGEVGRLQVrgPVVTKG--YYNNPEANAEAF-----TEDG-- 409
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 777 igeipFVRSGLLGFVGPGSLiFVVGKNEGLLVVSGRRHNADDLVAtalAVEPVKTVYRGRIAVFSVTVFYD--ERIVIVA 854
Cdd:cd05906 410 -----WFRTGDLGFLDNGNL-TITGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAetEELAIFF 480
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2264466784 855 eqrpdASEEDSFQWMSRVLQAIDSI--HQVGLYCLALVP--ANTLPKTPLGGIHISDTKQLFLEG 915
Cdd:cd05906 481 -----VPEYDLQDALSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
991-1568 |
1.83e-22 |
|
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: 102.58 E-value: 1.83e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 991 LSEALQWRAQTDPDHVLYVLLNAkgvavcTATCVQLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAG 1070
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGR------RLTYAELDARARRLAAALRAL-GVGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1071 CIPVTVrpphpqNLSATLPTVRMIIDVSKAACILTTQILTkilrskeaaTSvniktwpiiidtddlprkrppniykppsa 1150
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVTALILY---------TS----------------------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1151 dviayldfsvSTTGMLTGVKISHSAVSALCRSIKLQCELYSSRQLAICLDPYCGLGFVLWCLASVYSGHQSILIPplelE 1230
Cdd:COG0318 110 ----------GTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP----R 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1231 SSLSLWLSTLSQYRVrdTFCSYS---VMELCtkglggqtDMLKARGVNLACVRsCVVVAEERPRLALTQSFSKLFKdlgl 1307
Cdd:COG0318 176 FDPERVLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLR-LVVSGGAPLPPELLERFEERFG---- 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1308 stRAVSTAFGSrvnlaiclqgT-TGPdpsTVYVDMKSLRHDRVRLVergapqslplmesGTILPGVRVVIVNPETRgPLG 1386
Cdd:COG0318 241 --VRIVEGYGL----------TeTSP---VVTVNPEDPGERRPGSV-------------GRPLPGVEVRIVDEDGR-ELP 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1387 DSHLGEIWVNSPHTASGYYTiYGEEslqadhfnTKLSFGDPhtlWARTGYLGFVkrteltDSSGErhdaLFIVGSLDETL 1466
Cdd:COG0318 292 PGEVGEIVVRGPNVMKGYWN-DPEA--------TAEAFRDG---WLRTGDLGRL------DEDGY----LYIVGRKKDMI 349
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1467 ELRGLRYHPIDIEiSVQRAHRSIGESAVFTWTN--------LLVVVSElcGSEQDALDLVPLITNVVleEHHLIVGVVVI 1538
Cdd:COG0318 350 ISGGENVYPAEVE-EVLAAHPGVAEAAVVGVPDekwgervvAFVVLRP--GAELDAEELRAFLRERL--ARYKVPRRVEF 424
|
570 580 590
....*....|....*....|....*....|
gi 2264466784 1539 VDPgvIPINSRGEKQRMHLRDSFLADQLDP 1568
Cdd:COG0318 425 VDE--LPRTASGKIDRRALRERYAAGALEA 452
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
1-107 |
6.07e-22 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 92.10 E-value: 6.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1 GDITQKGYEKKRAKLLASFTIQTQNLTPPpqydgeepgpsSATVPSNASSGSSSsrhrrsrrsnrsggTRDERYRSDIHT 80
Cdd:pfam06464 23 GDITEKGYEKKKLKLLRKFLLHPETPTKL-----------SAEAQNQLASLETK--------------LRDEELSEEVYL 77
|
90 100
....*....|....*....|....*..
gi 2264466784 81 EAVQAALAKHKEEKMALPMPTKRRSAY 107
Cdd:pfam06464 78 EKVKALLAKELERENGLNAPTKEQSGL 104
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
973-1572 |
1.11e-20 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 98.15 E-value: 1.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 973 DQDLVRKLCMWPTmmhhyLSEALQWRAQTDPDHVLYvllNAKGVAVCTATCVQLHKRAEKIAAALMeRSGISIGENIVLL 1052
Cdd:PRK09192 10 TSSLPRRYADFPT-----LVEALDYAALGEAGMNFY---DRRGQLEEALPYQTLRARAEAGARRLL-ALGLKPGDRVALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1053 YPPGIDLIAAFYGCLYAGCIPVTVrpPHPQNL---SATLPTVRMIIDVSKAACILTTQILTKILrsKEAATSVNIK---T 1126
Cdd:PRK09192 81 AETDGDFVEAFFACQYAGLVPVPL--PLPMGFggrESYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLLhvlS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1127 WpiiIDTDDLPRkrPPNIYKPPSADVIAYLDFSVSTTGMLTGVKISHSAVSALCRSIklqcelySSRQLAICLDPYC--- 1203
Cdd:PRK09192 157 H---AWFKALPE--ADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAI-------SHDGLKVRPGDRCvsw 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1204 -------GL-GFVLWCLASVYS------------GHQSI-LIPplelesslslwlstlsqyRVRDTFcSYSV---MELCT 1259
Cdd:PRK09192 225 lpfyhdmGLvGFLLTPVATQLSvdylptrdfarrPLQWLdLIS------------------RNRGTI-SYSPpfgYELCA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1260 KGLGGQTDMlkarGVNLACVRSCVVVAEE-RPRlaLTQSFSKLFKDLGLSTRAVSTAFG-SRVNLAIclqgtTGPDPSTv 1337
Cdd:PRK09192 286 RRVNSKDLA----ELDLSCWRVAGIGADMiRPD--VLHQFAEAFAPAGFDDKAFMPSYGlAEATLAV-----SFSPLGS- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1338 yvDMKSLRHDRVRLVERG---APQSLPLMES-----GTILPGVRVVIVNpETRGPLGDSHLGEIWVNSPHTASGYYTiyG 1409
Cdd:PRK09192 354 --GIVVEEVDRDRLEYQGkavAPGAETRRVRtfvncGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYFR--D 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1410 EES---LQADHfntklsfgdphtlWARTGYLGFVkrteltdSSGErhdaLFIVGSLDETLELRGLRYHPIDIEISV--QR 1484
Cdd:PRK09192 429 EESqdvLAADG-------------WLDTGDLGYL-------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIAeqEP 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1485 AHRSiGESAVFTWTN-----LLVVVSELCGSEQDALDLVPLITNVVLEEHHLIVgVVVIVDPGVIPINSRGEKQRMHLRD 1559
Cdd:PRK09192 485 ELRS-GDAAAFSIAQengekIVLLVQCRISDEERRGQLIHALAALVRSEFGVEA-AVELVPPHSLPRTSSGKLSRAKAKK 562
|
650
....*....|...
gi 2264466784 1560 SFLADQLDPIYVA 1572
Cdd:PRK09192 563 RYLSGAFASLDVA 575
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1025-1561 |
3.15e-18 |
|
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: 90.42 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1025 QLHKRAEKIAAALmERSGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPPHP-QNLSATLPTVRMIIDVSKAACI 1103
Cdd:cd05906 44 DLLEDARRLAAGL-RQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPVV 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1104 LTTQILTKILRSKEAATSVNIKTWPIIIDTDDLPrkRPPNIYkPPSADVIAYLDFSVSTTGMLTGVKISHSAVSALCRSI 1183
Cdd:cd05906 123 LTDAELVAEFAGLETLSGLPGIRVLSIEELLDTA--ADHDLP-QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1184 KLQCELYS-SRQLA-ICLDPYCGLGFVlwCLASVYSGHQSILIPPLELESSLSLWLSTLSQYRVRDTFCSYSvmeLCTKg 1261
Cdd:cd05906 200 IQHNGLTPqDVFLNwVPLDHVGGLVEL--HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AFAL- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1262 LGGQTDMLKARGVNLACVRsCVVVAEERPRLALTQSFSKLFKDLGLSTRAVSTAFGSRVNLAIClqgttgpdpsTVYVDM 1341
Cdd:cd05906 274 LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGMTETCSGV----------IYSRSF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1342 KSLRHdrvrlvergaPQSLPLMESGTILPGVRVVIVNPETrGPLGDSHLGEIWVNSPHTASGYY-----TiygEESLQAD 1416
Cdd:cd05906 343 PTYDH----------SQALEFVSLGRPIPGVSMRIVDDEG-QLLPEGEVGRLQVRGPVVTKGYYnnpeaN---AEAFTED 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1417 HfntklsfgdphtlWARTGYLGFVkrteltdssgeRHDALFIVGSLDETLELRGLRYHPIDIEISVQR------------ 1484
Cdd:cd05906 409 G-------------WFRTGDLGFL-----------DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEvpgvepsftaaf 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2264466784 1485 AHRSIGESavftwTNLLVVVSELCGSEQDALD-LVPLITNVVLEEHHLIVGVVVIVDPGVIPINSRGEKQRMHLRDSF 1561
Cdd:cd05906 465 AVRDPGAE-----TEELAIFFVPEYDLQDALSeTLRAIRSVVSREVGVSPAYLIPLPKEEIPKTSLGKIQRSKLKAAF 537
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
377-901 |
3.15e-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: 89.85 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 377 LNKLGTKNEQVLKPGDRValVYPNSDPGMFWVAFYGCLLAEVIPVPievplsrkdagssqvgfllgscgVSLALTSEICL 456
Cdd:cd05908 26 LGYLGALQELGIKPGQEV--VFQITHNNKFLYLFWACLLGGMIAVP-----------------------VSIGSNEEHKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 457 KglpktstgeilQFKGWPRLK--WVITDSKYLTKpSKDwqphiptaniDTAYIEYKASKEGTVVGVAVSKIAMLTHCQAL 534
Cdd:cd05908 81 K-----------LNKVWNTLKnpYLITEEEVLCE-LAD----------ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAI 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 535 SQACNYCEGETLVNVLDFKKDMGLWHGVLTSVMNRIHTICVPYAVMKACPLSWVQRVHIHKARValVKCRDLHWAMMAHK 614
Cdd:cd05908 139 LNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATI--VSSPNFGYKYFLKT 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 615 ----EQRDISLSSLRMLIvaDGANPWSVSSCDAYLNVFQAHGLKPEVICPCATSPEAmTVAIrrpGVPGAPLPARAV-LS 689
Cdd:cd05908 217 lkpeKANDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA-SVGA---SLPKAQSPFKTItLG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 690 MTGLSHGVIRVNTEDKNS-ALTVQDVGHVMPGALMCIVKPDGPPMlcKTDEIGEIVVNSRAGGTLYYGLQGVTKNTFevi 768
Cdd:cd05908 291 RRHVTHGEPEPEVDKKDSeCLTFVEVGKPIDETDIRICDEDNKIL--PDGYIGHIQIRGKNVTPGYYNNPEATAKVF--- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 769 pvNASGapigeipFVRSGLLGFVGPGSLIfVVGKNEGLLVVSGRRHNADDLVATALAVEPVKTvyrGRIAVFSV--TVFY 846
Cdd:cd05908 366 --TDDG-------WLKTGDLGFIRNGRLV-ITGREKDIIFVNGQNVYPHDIERIAEELEGVEL---GRVVACGVnnSNTR 432
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 847 DERIVIVAEQRpdASEEDSFQWMSRVLQAID-----SIHQVglyclalVPANTLPKTPLG 901
Cdd:cd05908 433 NEEIFCFIEHR--KSEDDFYPLGKKIKKHLNkrggwQINEV-------LPIRRIPKTTSG 483
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
334-683 |
7.34e-18 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 88.14 E-value: 7.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 334 LARWGATQGKSPALTTLDITgkplyTLTYGKLWSRGVKLAYTLLnKLGtkneqvLKPGDRVALVYPNSdPGMFwVAFYGC 413
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGR-----RLTYRELDERANRLAAGLR-ALG------VGKGDRVAILLPNS-PEWV-VAFLAC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 414 LLAEVIPVPIevplsrkDAGSS--QVGFLLGSCGVSLALTSEI--------CLKGLPKTSTGEILQFKGWPRLKWVITDS 483
Cdd:pfam00501 67 LKAGAVYVPL-------NPRLPaeELAYILEDSGAKVLITDDAlkleelleALGKLEVVKLVLVLDRDPVLKEEPLPEEA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 484 KYLTKPSKdwQPHIPTANiDTAYIEYkASkeGTvvgVAVSKIAMLTHCQALSQACN----------YCEGETLVNVLDFK 553
Cdd:pfam00501 140 KPADVPPP--PPPPPDPD-DLAYIIY-TS--GT---TGKPKGVMLTHRNLVANVLSikrvrprgfgLGPDDRVLSTLPLF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 554 KDMGLWHGVLTSVMNRiHTICVPYAVMKACPLSWVQRVHIHKARV-----ALVKcrdlhwAMMAHKEQRDISLSSLRMLI 628
Cdd:pfam00501 211 HDFGLSLGLLGPLLAG-ATVVLPPGFPALDPAALLELIERYKVTVlygvpTLLN------MLLEAGAPKRALLSSLRLVL 283
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 629 VadGANPWSVSSCDAYLNVF-----QAHGLKpEViCPCATSPEAMTVAIRRPGVPGAPLP 683
Cdd:pfam00501 284 S--GGAPLPPELARRFRELFggalvNGYGLT-ET-TGVVTTPLPLDEDLRSLGSVGRPLP 339
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1022-1538 |
3.08e-17 |
|
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: 86.88 E-value: 3.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1022 TCVQLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGCipvtvrPPHPQNLSATLPTVRMIIDVSKAA 1101
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKL-GLKKGDVVGIISPNSTYYPPVFLGCLFAGG------IFSAANPIYTADELAHQLKISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1102 CILTT-QILTKILRS-KEAATSVNIKT------WPIIIDTDDLPRKRPPNIYKPP----SADVIAYLDFSVSTTGMLTGV 1169
Cdd:cd05911 85 VIFTDpDGLEKVKEAaKELGPKDKIIVlddkpdGVLSIEDLLSPTLGEEDEDLPPplkdGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1170 KISHSAVSALCRSIKLQ---CELYSSRQLA-ICLDPYCGLgfvLWCLASVYSGHQSILIPplelesslslwlstlsqyrv 1245
Cdd:cd05911 165 CLSHRNLIANLSQVQTFlygNDGSNDVILGfLPLYHIYGL---FTTLASLLNGATVIIMP-------------------- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1246 rdTFCSYSVMELCTKglggqtdmlkaRGVNLACVRSCVVVAEERPRLALTQSFSKLfKDLG-----LSTRAVStAFGSRV 1320
Cdd:cd05911 222 --KFDSELFLDLIEK-----------YKITFLYLVPPIAAALAKSPLLDKYDLSSL-RVILsggapLSKELQE-LLAKRF 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1321 NLAICLQ--GTTGPDPSTVYvdmkslrhdrvrlvergAPQSLPLMES-GTILPGVRVVIVNPETRGPLGDSHLGEIWVNS 1397
Cdd:cd05911 287 PNATIKQgyGMTETGGILTV-----------------NPDGDDKPGSvGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1398 PHTASGYYTiyGEESlqadhfnTKLSFgDPHTlWARTGYLGFVkrteltDSSGErhdaLFIVGSLDETLELRGLRYHPID 1477
Cdd:cd05911 350 PQVMKGYYN--NPEA-------TKETF-DEDG-WLHTGDIGYF------DEDGY----LYIVDRKKELIKYKGFQVAPAE 408
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2264466784 1478 IEiSVQRAHRSIGESAVF-----TWTNL---LVVVSElcGSEQDALDLVPLITNVVLEEHHLIVGVVVI 1538
Cdd:cd05911 409 LE-AVLLEHPGVADAAVIgipdeVSGELpraYVVRKP--GEKLTEKEVKDYVAKKVASYKQLRGGVVFV 474
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1025-1494 |
3.21e-17 |
|
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: 85.78 E-value: 3.21e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1025 QLHKRAEKIAAALMERSGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPPHPQnlsatlPTVRMIIDVSKAACIL 1104
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGARLLL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1105 TTQILTkiLRSKEAATSVNIKTWPIIIDTDDLPRKRPPNIykPPSADVIAYLDFSVSTTGMLTGVKISHSAVSALCRSIK 1184
Cdd:TIGR01733 78 TDSALA--SRLAGLVLPVILLDPLELAALDDAPAPPPPDA--PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1185 lQCELYSSRQLAICLDPYCGLGFVLWCLASVYSGHQSILIPPLELESSLSLWLSTLSQYRVRDTFCSYSVMELCTKGLGG 1264
Cdd:TIGR01733 154 -RRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAALPP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1265 QTDMLKArgvnlacvrscVVVAEERPRLALTQSFSKLFKDLGLstravstafgsrVNlaiclqgTTGPDPSTVYVDMKSL 1344
Cdd:TIGR01733 233 ALASLRL-----------VILGGEALTPALVDRWRARGPGARL------------IN-------LYGPTETTVWSTATLV 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1345 RHDRVRLVErgapqSLPLmesGTILPGVRVVIVNPETRgPLGDSHLGEIWVNSPHTASGYytiYGEESLQADHFNTKLSF 1424
Cdd:TIGR01733 283 DPDDAPRES-----PVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---LNRPELTAERFVPDPFA 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1425 GDPHTLWARTGYLgfVKRteltDSSGErhdaLFIVGSLDETLELRGLRYHPIDIEiSVQRAHRSIGESAV 1494
Cdd:TIGR01733 351 GGDGARLYRTGDL--VRY----LPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLRHPGVREAVV 409
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
327-919 |
6.25e-16 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 84.45 E-value: 6.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 327 PPALQAALARWGATQGKSPALTTLDITGKPLYTLTYGKLWSRGVKLAYTLLNKLGtkneqvlkPGDRVALVYPnSDPGmF 406
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS--------FGDRAVLLFP-SGPD-Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 407 WVAFYGCLLAEVIPVPIEVPLSRKDAGSSQVGFLLGSCGVSLALTSEICLKGLPKTstgEILQFKGWPRLKWVITdskYL 486
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQM---EELAAANAPELLCVDT---LD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 487 TKPSKDWQ-PHIPTANIdtAYIEYKASKEGTVVGVAVSKIAMLTHCQALSQACNYCEG--ETLVNVLDFKKDMGLWHGVL 563
Cdd:PRK05691 152 PALAEAWQePALQPDDI--AFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 564 TSVMNRIHTICVPYAVMKACPLSWVQRvhIHKARVALVKCRDLHWaMMAHKEQRDISLSSL---RMLIVADGANPWSVSS 640
Cdd:PRK05691 230 QPIFSGVPCVLMSPAYFLERPLRWLEA--ISEYGGTISGGPDFAY-RLCSERVSESALERLdlsRWRVAYSGSEPIRQDS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 641 CDAYLNVFQAHGLKPEVICPCATSPEA---MTVAIRRPGVPGAPLPARAVLSmtglshgvirvNTEDKNSALTVQDVGHV 717
Cdd:PRK05691 307 LERFAEKFAACGFDPDSFFASYGLAEAtlfVSGGRRGQGIPALELDAEALAR-----------NRAEPGTGSVLMSCGRS 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 718 MPGALMCIVKPDGPPMLcKTDEIGEIVVNSRAGGTLYYGLQGVTKNTFevipVNASGApigeiPFVRSGLLGFVGPGSLi 797
Cdd:PRK05691 376 QPGHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGDLGFLRDGEL- 444
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 798 FVVGKNEGLLVVSGRRHNADDLVATalAVEPVKTVYRGRIAVFSVTVFYDERIVIVAE-----QRPDASEEdsfqWMSRV 872
Cdd:PRK05691 445 FVTGRLKDMLIVRGHNLYPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPPQA----LIKSI 518
|
570 580 590 600
....*....|....*....|....*....|....*....|....*..
gi 2264466784 873 LQAIDSIHQVGLYCLALVPANTLPKTPLGGIHISDTKQLFLEGALHP 919
Cdd:PRK05691 519 RQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDS 565
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
388-901 |
1.99e-10 |
|
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: 65.15 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 388 LKPGDRVALVYPNSDPG---MFWVAFYGCLLAEVIpvpieVPLSrKDAGSSQVGFLLGSCGVSLALTSEICL----KGLP 460
Cdd:cd05922 15 GVRGERVVLILPNRFTYielSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIVLADAGAAdrlrDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 461 KTS-TGEILQFKGWprlkwviTDSKYLTkpskdwqPHIPTANIDTAYIEYKASKEGTVVGVAVSKIAMLTHCQALSQACN 539
Cdd:cd05922 89 ASPdPGTVLDADGI-------RAARASA-------PAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 540 YCEGETLVNVLDFKKDMGLwhgvltSVMNrIHTIC-----------VPYAVMKACplswvqRVHihkaRVALVKCRDLHW 608
Cdd:cd05922 155 ITADDRALTVLPLSYDYGL------SVLN-THLLRgatlvltndgvLDDAFWEDL------REH----GATGLAGVPSTY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 609 AMMAHKEQRDISLSSLRMLIVADGANPwsvsscdaylnvfqahglkpevicpcatspeAMTVAIRRPGVPGAplpaRAVL 688
Cdd:cd05922 218 AMLTRLGFDPAKLPSLRYLTQAGGRLP-------------------------------QETIARLRELLPGA----QVYV 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 689 sMTGLSHGVIRVNTEDKNSALTVQD-VGHVMPGALMCIVKPDGPPmlCKTDEIGEIVVNsraGGTLYYGlqGVTKNTFEV 767
Cdd:cd05922 263 -MYGQTEATRRMTYLPPERILEKPGsIGLAIPGGEFEILDDDGTP--TPPGEPGEIVHR---GPNVMKG--YWNDPPYRR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 768 IPVNASGApigeipfVRSGLLGFVGPGSLIFVVGKNEGLLVVSGRRHNADDLVATALAVEPVKTVyrgriAVFSVTVFYD 847
Cdd:cd05922 335 KEGRGGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA-----AAVGLPDPLG 402
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2264466784 848 ERIVIVAEqrpdASEEDSFQWMSRVLQAIDSIHQVGLYClalVPANTLPKTPLG 901
Cdd:cd05922 403 EKLALFVT----APDKIDPKDVLRSLAERLPPYKVPATV---RVVDELPLTASG 449
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1025-1499 |
4.35e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 63.85 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1025 QLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPPHPqnlsatLPTVRMIIDVSKAACIL 1104
Cdd:cd12116 17 ELDERANRLAARLRAR-GVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAEPALVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1105 TTQILtkilrskEAATSVNIKTWPIIIDTDDLPRKRPPniyKPPSADVIAYLDFSVSTTGMLTGVKISHSAVSALCRSIK 1184
Cdd:cd12116 90 TDDAL-------PDRLPAGLPVLLLALAAAAAAPAAPR---TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1185 LQCELYSS-RQLAICldPYCglgF---VLWCLASVYSGHQSILIPplelesslslwlstlsqyrvRDTfcSYSVMELctk 1260
Cdd:cd12116 160 ERLGLGPGdRLLAVT--TYA---FdisLLELLLPLLAGARVVIAP--------------------RET--QRDPEAL--- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1261 glggqTDMLKARGVNlacvrscVVVAeerprlalTQSFSKLFKDLGLSTRAVSTAF-GSR---VNLAICLQGTT------ 1330
Cdd:cd12116 210 -----ARLIEAHSIT-------VMQA--------TPATWRMLLDAGWQGRAGLTALcGGEalpPDLAARLLSRVgslwnl 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1331 -GPDPSTVYvdmkSLRHdRVRLVERGAPQSLPlmesgtiLPGVRVVIVNPETRgPLGDSHLGEIWVNSPHTASGYytiYG 1409
Cdd:cd12116 270 yGPTETTIW----STAA-RVTAAAGPIPIGRP-------LANTQVYVLDAALR-PVPPGVPGELYIGGDGVAQGY---LG 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1410 EESLQADHFnTKLSFGDPHTLWARTGYLgfVKRteltdssgERHDALFIVGSLDETLELRGLRYHPIDIEiSVQRAHRSI 1489
Cdd:cd12116 334 RPALTAERF-VPDPFAGPGSRLYRTGDL--VRR--------RADGRLEYLGRADGQVKIRGHRIELGEIE-AALAAHPGV 401
|
490
....*....|
gi 2264466784 1490 GESAVFTWTN 1499
Cdd:cd12116 402 AQAAVVVRED 411
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1025-1563 |
5.70e-10 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 63.63 E-value: 5.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1025 QLHKRAEKIAAALMERSGISIgenIVLLYPPGIDLIAAFYGCLYAG----CIPVTVRPPHPQNLSATlptvrmiiDVSKA 1100
Cdd:PRK05851 36 EVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADA--------TLTRF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1101 ACILTTQILT-----KILRSKEAATSVNiktwpiiiDTDDLPRKRPPNIYKPPSADVIAYLDFSVSTTGMLTGVKISHSA 1175
Cdd:PRK05851 105 AGIGVRTVLShgshlERLRAVDSSVTVH--------DLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1176 VSALCRSIKLQCELYSSRQLAICLDPY---CGLGFVLwclASVYSGHQSILIPPLELESSLSLWLSTLSQYRVRDTFC-- 1250
Cdd:PRK05851 177 VLSNLRGLNARVGLDAATDVGCSWLPLyhdMGLAFLL---TAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATLTAApn 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1251 -SYSVmelctkgLGGQTDmlKARGVNLACVRSCVVVAEerP-RLALTQSFSKLFKDLGLSTRAVSTAFGsrvnLAICLQG 1328
Cdd:PRK05851 254 fAYNL-------IGKYAR--RVSDVDLGALRVALNGGE--PvDCDGFERFATAMAPFGFDAGAAAPSYG----LAESTCA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1329 TTGPDPSTvyvdmkSLRHDRVRLVERGAPQSLPLMesGTILPGVRVVIVNPETRGPLGDSHLGEIWVNSPHTASGYytiY 1408
Cdd:PRK05851 319 VTVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY---L 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1409 GEESLQADHfntklsfgdphtlWARTGYLGFvkrteLTDssgerhDALFIVGSLDETLELRGLRYHPIDIE-ISVQ-RAH 1486
Cdd:PRK05851 388 GQAPIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIErVAAQvRGV 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1487 RSIGESAVFTWTNL----LVVVSELCGSEQDALDlVPLITNVVLEehhliVGV----VVIVDPGVIPINSRGEKQRMHLR 1558
Cdd:PRK05851 444 REGAVVAVGTGEGSarpgLVIAAEFRGPDEAGAR-SEVVQRVASE-----CGVvpsdVVFVAPGSLPRTSSGKLRRLAVK 517
|
....*
gi 2264466784 1559 DSFLA 1563
Cdd:PRK05851 518 RSLEA 522
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1025-1494 |
2.10e-09 |
|
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: 61.87 E-value: 2.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1025 QLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPphpqnlSATLPTVRMIIDVSKAACIL 1104
Cdd:cd05904 37 ELERRVRRLAAGLAKR-GGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSGAKLAF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1105 TTQILTKILRSKEAAT----SVNIKTWPIIIDTDDLPRKRPPNIYKPPSaDVIAYLdFSVSTTGMLTGVKISH-SAVSAL 1179
Cdd:cd05904 110 TTAELAEKLASLALPVvlldSAEFDSLSFSDLLFEADEAEPPVVVIKQD-DVAALL-YSSGTTGRSKGVMLTHrNLIAMV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1180 CRSIKLQCELYSSRQLAICLDPYCGL-GFVLWCLASVYSGHQSILIPplelesslslwlstlsqyrvrdTFCSYSVMELc 1258
Cdd:cd05904 188 AQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMP----------------------RFDLEELLAA- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1259 tkglggqtdmLKARGVNLACVRSCVVVAEERPRLALTQSFSKLFK------DLGlstRAVSTAFGSRVNLAICLQG---- 1328
Cdd:cd05904 245 ----------IERYKVTHLPVVPPIVLALVKSPIVDKYDLSSLRQimsgaaPLG---KELIEAFRAKFPNVDLGQGygmt 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1329 TTGPDPSTVYVDMKSlrhdrvrlveRGAPQSlplmeSGTILPGVRVVIVNPETRGPLGDSHLGEIWVNSPHTASGYytiy 1408
Cdd:cd05904 312 ESTGVVAMCFAPEKD----------RAKYGS-----VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMKGY---- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1409 geeslqadhfntklsFGDPH----TL----WARTGYLGFVkrteltDSSGErhdaLFIVGSLDETLELRGLRYHPIDIEi 1480
Cdd:cd05904 373 ---------------LNNPEataaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKGFQVAPAELE- 426
|
490
....*....|....
gi 2264466784 1481 SVQRAHRSIGESAV 1494
Cdd:cd05904 427 ALLLSHPEILDAAV 440
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
991-1405 |
5.82e-09 |
|
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: 60.27 E-value: 5.82e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 991 LSEALQWRAQTDPDHVLYVLLNAKgvavctATCVQLHKRAEKIAAALMErSGISIGENIVLLYPPGIDLIAAFYGCLYAG 1070
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRK------LTYRELDALAEAFAAGLQN-LGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1071 CIPVTVRPphpqnlsatlptvrmiidvskaacILTTQILTKILRSKEAATSVNIKTWpiiidTDDLPRKRPPNIYKPPSA 1150
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSF-----TDLLAAGAPLGERVALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1151 DVIAYLDFSVSTTGMLTGVKISHSAVSAlcrsIKLQC-----ELYSSRQLAICLDP-YCGLGFVLWCLASVYSGHQSILI 1224
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1225 PplelesslslwlstlsqyRVRDTfcsySVMElctkglggqtDMLKAR-----GVnlacvrscvvvaeerPRL--ALTQS 1297
Cdd:cd05936 201 P------------------RFRPI----GVLK----------EIRKHRvtifpGV---------------PTMyiALLNA 233
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1298 FSKLFKDLglstravstafgSRVNLAIClqgttGPDPSTVYVDMKSLRHDRVRLVE----------------RGAPQslp 1361
Cdd:cd05936 234 PEFKKRDF------------SSLRLCIS-----GGAPLPVEVAERFEELTGVPIVEgygltetspvvavnplDGPRK--- 293
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2264466784 1362 lmeSGTI---LPGVRVVIVNPETRgPLGDSHLGEIWVNSPHTASGYY 1405
Cdd:cd05936 294 ---PGSIgipLPGTEVKIVDDDGE-ELPPGEVGELWVRGPQVMKGYW 336
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
999-1499 |
6.56e-09 |
|
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: 60.34 E-value: 6.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 999 AQTDPDHVLYVLLNAkgvavcTATCVQLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGC--IPVTV 1076
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASL-GLDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1077 RPPHPQnlsatlptVRMIIDVSKAACilttqiltkilrskeaatsvniktwpIIIDTDDLprkrppniykppsadviAYL 1156
Cdd:cd05945 74 SSPAER--------IREILDAAKPAL--------------------------LIADGDDN-----------------AYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1157 DFSVSTTGMLTGVKISHSAVSAlcrsiklqcelyssrqlaicldpycglgFVLWCLAsvysghQSILIPplelesslslw 1236
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVS----------------------------FTNWMLS------DFPLGP----------- 137
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1237 lstlsqyrvRDTFCSY-------SVMEL-CTKGLGG--------QTD-------MLKARGVNL-ACVRSCVVVAEERPRL 1292
Cdd:cd05945 138 ---------GDVFLNQapfsfdlSVMDLyPALASGAtlvpvprdATAdpkqlfrFLAEHGITVwVSTPSFAAMCLLSPTF 208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1293 A------LTQSfskLF--KDLGLST-RAVSTAF-GSRV-NlaiclqgTTGPDPSTVYVdmksLRHDRVRLVERGAPqSLP 1361
Cdd:cd05945 209 TpeslpsLRHF---LFcgEVLPHKTaRALQQRFpDARIyN-------TYGPTEATVAV----TYIEVTPEVLDGYD-RLP 273
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1362 LmesGTILPGVRVVIVNPETRgPLGDSHLGEIWVNSPHTASGYytiYGEESLQADHFntklsFGDPHTLWARTGYLGFVk 1441
Cdd:cd05945 274 I---GYAKPGAKLVILDEDGR-PVPPGEKGELVISGPSVSKGY---LNNPEKTAAAF-----FPDEGQRAYRTGDLVRL- 340
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2264466784 1442 rteltDSSGErhdaLFIVGSLDETLELRGLRYHPIDIEISVqRAHRSIGESAVFTWTN 1499
Cdd:cd05945 341 -----EADGL----LFYRGRLDFQVKLNGYRIELEEIEAAL-RQVPGVKEAVVVPKYK 388
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
999-1173 |
4.21e-08 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 57.60 E-value: 4.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 999 AQTDPDHVLYVLLNAkgvavcTATCVQLHKRAEKIAAALMERsgISIGENIVLLY----PpgiDLIAAFYGCLYAGC--I 1072
Cdd:PRK04813 12 AQTQPDFPAYDYLGE------KLTYGQLKEDSDALAAFIDSL--KLPDKSPIIVFghmsP---EMLATFLGAVKAGHayI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1073 PVTVRPPhpqnlsatLPTVRMIIDVSKAACILTTqiltkilrSKEAATSVNIKtwpiIIDTDDLPR----KRPPNIYKPP 1148
Cdd:PRK04813 81 PVDVSSP--------AERIEMIIEVAKPSLIIAT--------EELPLEILGIP----VITLDELKDifatGNPYDFDHAV 140
|
170 180
....*....|....*....|....*
gi 2264466784 1149 SADVIAYLDFSVSTTGMLTGVKISH 1173
Cdd:PRK04813 141 KGDDNYYIIFTSGTTGKPKGVQISH 165
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
263-653 |
5.90e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 58.04 E-value: 5.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 263 RVSTKIQQLLNTLKRPKRPPLSEFFMDDQEEIVEVPRPDPNTPRPEGRQiipvkgeplgvvsnwpPALQAALARWGATQG 342
Cdd:PRK12316 1954 RLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRG----------------PGVHQRIAEQAARAP 2017
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 343 KSPALTTLDitgkplYTLTYGKLWSRGVKLAYTLLnklgtknEQVLKPGDRVALVYPNSDPGMfwVAFYGCLLA--EVIP 420
Cdd:PRK12316 2018 EAIAVVFGD------QHLSYAELDSRANRLAHRLR-------ARGVGPEVRVAIAAERSFELV--VALLAVLKAggAYVP 2082
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 421 VPIEVPLSRkdagssqVGFLLGSCGVSLALTSEICLKGLPKTStgeilqfkGWPRLKwVITDSKYLTKPSKDwqPHIPTA 500
Cdd:PRK12316 2083 LDPNYPAER-------LAYMLEDSGAALLLTQRHLLERLPLPA--------GVARLP-LDRDAEWADYPDTA--PAVQLA 2144
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 501 NIDTAYIEYKASKEGTVVGVAVSKIAMLTHCQALSQACNYCEGETLVNVLDFKKDMGLWhGVLTSVMNRIHTICVPYAVM 580
Cdd:PRK12316 2145 GENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDELW 2223
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2264466784 581 KACPLSwvqrVHIHKARVALVKCRDLHWAMMAHKEQRDISLSSLRMLIVadGANPWSVSSCDAYLNVFQAHGL 653
Cdd:PRK12316 2224 DPEQLY----DEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEALRPVYL 2290
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1025-1181 |
2.18e-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: 55.28 E-value: 2.18e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1025 QLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPPHPQNlsatlpTVRMIIDVSKAACIL 1104
Cdd:cd12117 27 ELNERANRLARRLRAA-GVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAE------RLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2264466784 1105 TTQILTKILRSKEaatsvniktwPIIIDTDDLPRKRPPNIYKPPSADVIAYLDFSVSTTGMLTGVKISHSAVSALCR 1181
Cdd:cd12117 100 TDRSLAGRAGGLE----------VAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVK 166
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1366-1562 |
3.65e-07 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 54.99 E-value: 3.65e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1366 GTILPGVRVVIVNPETRGPLGDSHLGEIWVNSPHTASGYYTIYGEESLQADHFNtklsfgdphtlWARTGYLGFVkrtel 1445
Cdd:PLN02330 364 GFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDG-----------WLHTGDIGYI----- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1446 tDSSGErhdaLFIVGSLDETLELRGLRYHPIDIEiSVQRAHRSIGESAVFTWTN---------LLVVVSELCGSEQDALD 1516
Cdd:PLN02330 428 -DDDGD----IFIVDRIKELIKYKGFQVAPAELE-AILLTHPSVEDAAVVPLPDeeageipaaCVVINPKAKESEEDILN 501
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2264466784 1517 LVPliTNVVleeHHLIVGVVVIVDPgvIPINSRGEKQRMHLRDSFL 1562
Cdd:PLN02330 502 FVA--ANVA---HYKKVRVVQFVDS--IPKSLSGKIMRRLLKEKML 540
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1025-1183 |
3.93e-07 |
|
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: 55.25 E-value: 3.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1025 QLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGC--IPvtvrpphpqnLSATLPT--VRMIIDVSKA 1100
Cdd:COG1020 506 ELNARANRLAHHLRAL-GVGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAYPAerLAYMLEDAGA 574
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1101 ACILTTQILTKILRSKEAATsvniktwpIIIDTDDLPRKRPPNIYKPPSADVIAYLDFSVSTTGMLTGVKISHSAVSALC 1180
Cdd:COG1020 575 RLVLTQSALAARLPELGVPV--------LALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLL 646
|
...
gi 2264466784 1181 RSI 1183
Cdd:COG1020 647 AWM 649
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1026-1439 |
4.07e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 54.39 E-value: 4.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1026 LHKRAEKIAAALMErSGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPPhpqnlsatlptvrmiIDVSK-AACIl 1104
Cdd:cd05910 8 LDERSDRIAQGLTA-YGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPG---------------MGRKNlKQCL- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1105 ttqiltkilrsKEAATSVNIKTwpiiidtddlprkrppniykpPSADVIAYLDFSVSTTGMLTGVKISHSAVSALCRSIK 1184
Cdd:cd05910 71 -----------QEAEPDAFIGI---------------------PKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1185 lqcELYSSRQLAICLDpycglGFVLWCLASVYSGHQSIlIPPLELESSLSL----WLSTLSQYRVRDTFCSYSVMELCTK 1260
Cdd:cd05910 119 ---QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDPTRPARAdpqkLVGAIRQYGVSIVFGSPALLERVAR 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1261 glggqtdMLKARGVNLACVRsCVVVAEERPRLALTQSFSKLFKDlglsTRAVSTAFGSRVNLAICLQGTtgpdpstvyvd 1340
Cdd:cd05910 190 -------YCAQHGITLPSLR-RVLSAGAPVPIALAARLRKMLSD----EAEILTPYGATEALPVSSIGS----------- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1341 mKSLRHDRVRLVERGAPQSLplmesGTILPGVRVVIVnPETRGP---------LGDSHLGEIWVNSPHTASGYYTiygee 1411
Cdd:cd05910 247 -RELLATTTAATSGGAGTCV-----GRPIPGVRVRII-EIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVN----- 314
|
410 420
....*....|....*....|....*...
gi 2264466784 1412 SLQADHFnTKLSFGDpHTLWARTGYLGF 1439
Cdd:cd05910 315 RPVATAL-AKIDDNS-EGFWHRMGDLGY 340
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
999-1181 |
9.84e-07 |
|
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: 53.12 E-value: 9.84e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 999 AQTDPDHVLyvlLNAKGVAVctaTCVQLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRP 1078
Cdd:cd17651 5 AARTPDAPA---LVAEGRRL---TYAELDRRANRLAHRLRAR-GVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1079 PHPQnlsatlPTVRMIIDVSKAACILTTQILTKilrskEAATSVNiktWPIIIDTDDLPRKRPPNIYKPPSADVIAYLDF 1158
Cdd:cd17651 78 AYPA------ERLAFMLADAGPVLVLTHPALAG-----ELAVELV---AVTLLDQPGAAAGADAEPDPALDADDLAYVIY 143
|
170 180
....*....|....*....|...
gi 2264466784 1159 SVSTTGMLTGVKISHSAVSALCR 1181
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVA 166
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
330-423 |
1.32e-06 |
|
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: 52.95 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 330 LQAALARWGATQGKSPALTTLditGKPLytlTYGKLWSRGVKLAYTLLNkLGtkneqvLKPGDRVALVYPNSdPgMFWVA 409
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFM---GRKL---TYRELDALAEAFAAGLQN-LG------VQPGDRVALMLPNC-P-QFPIA 65
|
90
....*....|....
gi 2264466784 410 FYGCLLAEVIPVPI 423
Cdd:cd05936 66 YFGALKAGAVVVPL 79
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
359-625 |
2.15e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 53.04 E-value: 2.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 359 TLTYGKLWSRGVKLAYTLLnklgtknEQVLKPGDRVALVYPNSDPGMfwVAFYGCLLA--EVIPVPIEVPLSRkdagssq 436
Cdd:PRK12316 4576 KLTYAELNRRANRLAHALI-------ARGVGPEVLVGIAMERSAEMM--VGLLAVLKAggAYVPLDPEYPRER------- 4639
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 437 VGFLLGSCGVSLALTSEICLKGLPKTSTGEILQFkgwprlkwvitdskyltKPSKDWQ------PHIPTANIDTAYIEYK 510
Cdd:PRK12316 4640 LAYMMEDSGAALLLTQSHLLQRLPIPDGLASLAL-----------------DRDEDWEgfpahdPAVRLHPDNLAYVIYT 4702
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 511 ASKEGTVVGVAVSKIAMLTHCQALSQACNYCEGETLVNVLDFKKDMglwhgvltSVMNRIHTICVPYAVMKACPLSWVQR 590
Cdd:PRK12316 4703 SGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDG--------SHEGLYHPLINGASVVIRDDSLWDPE 4774
|
250 260 270
....*....|....*....|....*....|....*...
gi 2264466784 591 VH---IHKARVALVKCRDLHWAMMAHKEQRDISLSSLR 625
Cdd:PRK12316 4775 RLyaeIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLR 4812
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1003-1479 |
3.27e-06 |
|
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: 51.72 E-value: 3.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1003 PDHVLYVLLNAKGVAVctaTCVQLHKRAEKIAAALMErSGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVtvrpphpq 1082
Cdd:cd05908 1 PEGIIFILGDKKEKFV---SYRHLREEALGYLGALQE-LGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAV-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1083 nlsatlPTVRMIIDVSKaacilttQILTKIlrskeaatsVNIKTWPIIIDTDDLPRKRPpniykppsaDVIAYLDFSVST 1162
Cdd:cd05908 69 ------PVSIGSNEEHK-------LKLNKV---------WNTLKNPYLITEEEVLCELA---------DELAFIQFSSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1163 TGMLTGVKISHSAVSALCRSIKLQCELYSSRQLAICLDPYCGLGFVLWCLASVYSGHQSILIPPLELESSLSLWLSTLSQ 1242
Cdd:cd05908 118 TGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1243 YRVRDTFCSYSVMELCTKGLGGQtdmlKARGVNLACVRSCVVVAEerPRLA-LTQSFSKLFKDLGLSTRAVSTAFGsrvn 1321
Cdd:cd05908 198 HKATIVSSPNFGYKYFLKTLKPE----KANDWDLSSIRMILNGAE--PIDYeLCHEFLDHMSKYGLKRNAILPVYG---- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1322 LAICLQGTTGPDPS----TVYVDMKSLRH-DRVRLVERGAPQSLPLMESGTILPGVRVVIVNPETRGpLGDSHLGEIWVN 1396
Cdd:cd05908 268 LAEASVGASLPKAQspfkTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LPDGYIGHIQIR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1397 SPHTASGYYT--IYGEESLQADHfntklsfgdphtlWARTGYLGFVKRTELTdSSGERHDALFIVGSldetlelrglRYH 1474
Cdd:cd05908 347 GKNVTPGYYNnpEATAKVFTDDG-------------WLKTGDLGFIRNGRLV-ITGREKDIIFVNGQ----------NVY 402
|
....*
gi 2264466784 1475 PIDIE 1479
Cdd:cd05908 403 PHDIE 407
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
995-1078 |
8.93e-06 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 50.28 E-value: 8.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 995 LQWRAQTDPDHVLYVLLNAKG----VAVCTATCVQLHKRAEKIAAALmERSGISIGENIVLLYPPGIDLIAAFYGCLYAG 1070
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPGGRGadgkLAYDELSFAELDARSDAIAHGL-NAAGIGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
....*...
gi 2264466784 1071 CIPVTVRP 1078
Cdd:PRK09274 91 AVPVLVDP 98
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
359-480 |
1.13e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 49.96 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 359 TLTYGKLWSRGVKLAYTLLNKLGtkneqvLKPGDRVALVYPNSdPgMFWVAFYGCLLAEVIPVPIEvPLSRKDagssQVG 438
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLLYMQNS-P-QFVIAYYAILRANAVVVPVN-PMNREE----ELA 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 2264466784 439 FLLGSCGVSLAltseICLKGLpktsTGEILQFKGWPRLKWVI 480
Cdd:PRK08314 102 HYVTDSGARVA----IVGSEL----APKVAPAVGNLRLRHVI 135
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
991-1080 |
1.19e-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: 49.76 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 991 LSEALQWRAQTDPDHVlyvllnakgvAVCTA----TCVQLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGC 1066
Cdd:COG1021 27 LGDLLRRRAERHPDRI----------AVVDGerrlSYAELDRRADRLAAGLLAL-GLRPGDRVVVQLPNVAEFVIVFFAL 95
|
90
....*....|....
gi 2264466784 1067 LYAGCIPVTVRPPH 1080
Cdd:COG1021 96 FRAGAIPVFALPAH 109
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
961-1494 |
1.27e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 50.34 E-value: 1.27e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 961 AQAAGRDLGLIEDQDLVRKLCMWPTMMHHY-----LSEALQWRAQTDPDHVLyVLLNAKgvavcTATCVQLHKRAEKIAA 1035
Cdd:PRK12316 4518 PQRRLGELQLLEKAEQQRIVALWNRTDAGYpatrcVHQLVAERARMTPDAVA-VVFDEE-----KLTYAELNRRANRLAH 4591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1036 ALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPPHPQNLSATlptvrMIIDvSKAACILTTQILTKILRS 1115
Cdd:PRK12316 4592 ALIAR-GVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAY-----MMED-SGAALLLTQSHLLQRLPI 4664
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1116 KEAATSVNI---KTWPIIIDTDDLPRKRPPNIykppsadviAYLDFSVSTTGMLTGVKISHSAVSALCRSIKLQCELYSS 1192
Cdd:PRK12316 4665 PDGLASLALdrdEDWEGFPAHDPAVRLHPDNL---------AYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPD 4735
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1193 RQLaICLDPYCGLGFVlWCLASVYSGHQSILIPPLELESSLSLWLSTLSQyRVRDTFCSYSVMELCTKGlggqtdmlKAR 1272
Cdd:PRK12316 4736 DRV-LQFMSFSFDGSH-EGLYHPLINGASVVIRDDSLWDPERLYAEIHEH-RVTVLVFPPVYLQQLAEH--------AER 4804
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1273 GVNLACVRSCVVVAEERPRLALTQSFSKLFKDlglstravstafgsrvnlaiCLQGTTGPDPSTVYVdmkslRHDRVRLV 1352
Cdd:PRK12316 4805 DGEPPSLRVYCFGGEAVAQASYDLAWRALKPV--------------------YLFNGYGPTETTVTV-----LLWKARDG 4859
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1353 ERGAPQSLPLmesGTILPGVRVVIVNPETrGPLGDSHLGEIWVNSPHTASGYYTiygEESLQADHFNTKlSFGDPHTLWA 1432
Cdd:PRK12316 4860 DACGAAYMPI---GTPLGNRSGYVLDGQL-NPLPVGVAGELYLGGEGVARGYLE---RPALTAERFVPD-PFGAPGGRLY 4931
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2264466784 1433 RTGylgfvkrteltDSSGERHDALF-IVGSLDETLELRGLRYHPIDIEISVqRAHRSIGESAV 1494
Cdd:PRK12316 4932 RTG-----------DLARYRADGVIdYLGRVDHQVKIRGFRIELGEIEARL-REHPAVREAVV 4982
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1025-1183 |
1.94e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 49.96 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1025 QLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPPHPQNLSATlptvrMIIDvSKAACIL 1104
Cdd:PRK12316 2033 ELDSRANRLAHRLRAR-GVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAY-----MLED-SGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1105 TTQILTKILRSKEAATSVNIKT---WPiiidtdDLPRKRPPNIYKPpsaDVIAYLDFSVSTTGMLTGVKISHSAVSALCR 1181
Cdd:PRK12316 2106 TQRHLLERLPLPAGVARLPLDRdaeWA------DYPDTAPAVQLAG---ENLAYVIYTSGSTGLPKGVAVSHGALVAHCQ 2176
|
..
gi 2264466784 1182 SI 1183
Cdd:PRK12316 2177 AA 2178
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1016-1183 |
2.84e-05 |
|
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: 48.42 E-value: 2.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1016 VAVCTA----TCVQLHKRAEKIAAALmERSGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVrpphpqnlSATLPTV 1091
Cdd:cd12114 4 TAVICGdgtlTYGELAERARRVAGAL-KAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPV--------DIDQPAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1092 RM--IIDVSKAACILTTQILtkilrskeAATSVNIKTWPIIIDTDDLPRKRPPNIykPPSADVIAYLDFSVSTTGMLTGV 1169
Cdd:cd12114 75 RReaILADAGARLVLTDGPD--------AQLDVAVFDVLILDLDALAAPAPPPPV--DVAPDDLAYVIFTSGSTGTPKGV 144
|
170
....*....|....
gi 2264466784 1170 KISHSAVSALCRSI 1183
Cdd:cd12114 145 MISHRAALNTILDI 158
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1025-1189 |
5.66e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 48.23 E-value: 5.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1025 QLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPPHPQNLSATlptvrMIIDvSKAACIL 1104
Cdd:PRK12467 3125 ELNRRANRLAHRLIAI-GVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAY-----MIED-SGVKLLL 3197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1105 TTQILTKILrskEAATSVNIktwpIIIDTDDLPRKRPPNIYKPPSADVIAYLDFSVSTTGMLTGVKISHSAVSALCRSIK 1184
Cdd:PRK12467 3198 TQAHLLEQL---PAPAGDTA----LTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIA 3270
|
....*
gi 2264466784 1185 LQCEL 1189
Cdd:PRK12467 3271 EAYEL 3275
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
317-421 |
5.86e-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: 47.45 E-value: 5.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 317 GEPLGvvsnwppalqAALARWGATQGKSPALttldITGKplYTLTYGKLWSRGVKLAYTLLnKLGtkneqvLKPGDRVAL 396
Cdd:COG1021 24 GETLG----------DLLRRRAERHPDRIAV----VDGE--RRLSYAELDRRADRLAAGLL-ALG------LRPGDRVVV 80
|
90 100
....*....|....*....|....*
gi 2264466784 397 VYPNSdpGMFWVAFYGCLLAEVIPV 421
Cdd:COG1021 81 QLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
361-630 |
6.13e-05 |
|
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: 47.26 E-value: 6.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 361 TYGKLWSRGVKLAYTLLNKLGtkneqvLKPGDRVALVYPNSDPGMfwVAFYGCLLAEVIPVPIEV--PLSRKDagssqvg 438
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERSAELV--VAILAVLKAGAAYVPLDPayPAERLA------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 439 FLLGSCGVSLALTSEiclkglpktSTGEILQFKGWPRLKWVITDSKYLTKPSKDWQPHIPTANIDTAYIEYKASKEGTVV 518
Cdd:TIGR01733 66 FILEDAGARLLLTDS---------ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 519 GVAVSKIAMLTHCQALSQACNYCEGETLVNVLDFKKDMGLWHgVLTSVMNRIHTICVPYAVMKACPLSWvqRVHIHKARV 598
Cdd:TIGR01733 137 GVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALL--AALIAEHPV 213
|
250 260 270
....*....|....*....|....*....|..
gi 2264466784 599 ALVKCRDLHWAMMAhkEQRDISLSSLRMLIVA 630
Cdd:TIGR01733 214 TVLNLTPSLLALLA--AALPPALASLRLVILG 243
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1352-1556 |
8.34e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 47.30 E-value: 8.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1352 VERGAPQSLPLMesGTILPGVRVVIVNpETRGPLGDSHLGEIWVNSPHTASGYYTIYGEESLQADHfntklsfGdphtlW 1431
Cdd:PRK07768 351 ATKGNTRRLATL--GPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYLTMDGFIPAQDAD-------G-----W 415
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1432 ARTGYLGFvkrteLTDsSGErhdaLFIVGSLDETLELRGLRYHPIDIEISVQRAH--RSIGESAVFTWTNL------LVV 1503
Cdd:PRK07768 416 LDTGDLGY-----LTE-EGE----VVVCGRVKDVIIMAGRNIYPTDIERAAARVEgvRPGNAVAVRLDAGHsregfaVAV 485
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 2264466784 1504 VSELCGSEQDALDLVPLITNVVLEEhhliVGV----VVIVDPGVIPINSRGEKQRMH 1556
Cdd:PRK07768 486 ESNAFEDPAEVRRIRHQVAHEVVAE----VGVrprnVVVLGPGSIPKTPSGKLRRAN 538
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1034-1558 |
1.30e-04 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 46.28 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1034 AAALMERSGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPPHPQNLSATlpTVRMIIDVSKAACILTTQILTKIL 1113
Cdd:cd05922 6 AASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKES--VLRYLVADAGGRIVLADAGAADRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1114 RSKEAATSVNIktwpIIIDTDDLPRKRPPNIYKPPSADVIAYLDFSVSTTGMLTGVKISHSAVSALCRSIKLQCELYSSR 1193
Cdd:cd05922 84 RDALPASPDPG----TVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1194 QLAICLdP--YC-GLGFVLwclASVYSGHQSILIPplelesslslwlstlsQYRVRDTFcsysvMELCTKGlgGQTDMlk 1270
Cdd:cd05922 160 RALTVL-PlsYDyGLSVLN---THLLRGATLVLTN----------------DGVLDDAF-----WEDLREH--GATGL-- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1271 aRGV--NLACVRSCVVVAEERPRL-ALTQSFSKL-------FKDLGLSTRAVstafgsrvnlaiCLQGTTGPDPSTVYVD 1340
Cdd:cd05922 211 -AGVpsTYAMLTRLGFDPAKLPSLrYLTQAGGRLpqetiarLRELLPGAQVY------------VMYGQTEATRRMTYLP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1341 MKslrhdrvRLVERgaPQSLplmesGTILPGVRVVIVNPETrGPLGDSHLGEIWVNSPHTASGYYTIYGEEsLQADHFNT 1420
Cdd:cd05922 278 PE-------RILEK--PGSI-----GLAIPGGEFEILDDDG-TPTPPGEPGEIVHRGPNVMKGYWNDPPYR-RKEGRGGG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1421 KLsfgdphtlwaRTGYLGFVkrteltDSSGErhdaLFIVGSLDETLELRGLRYHPIDIEISVqRAHRSIGESAVF----T 1496
Cdd:cd05922 342 VL----------HTGDLARR------DEDGF----LFIVGRRDRMIKLFGNRISPTEIEAAA-RSIGLIIEAAAVglpdP 400
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2264466784 1497 WTNLLVVVSElcGSEQDALDLVPLITNVVLEEHHLIVGVVVIVDpgvIPINSRGEKQRMHLR 1558
Cdd:cd05922 401 LGEKLALFVT--APDKIDPKDVLRSLAERLPPYKVPATVRVVDE---LPLTASGKVDYAALR 457
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
997-1176 |
1.34e-04 |
|
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: 46.50 E-value: 1.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 997 WRAQTD--PDHVLYVllnAKGVAVctaTCVQLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPV 1074
Cdd:cd17646 4 VAEQAArtPDAPAVV---DEGRTL---TYRELDERANRLAHLLRAR-GVGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1075 TVRPPHPQnlsatlPTVRMIIDVSKAACILTTQILTKILRSKEAATSVNIKTWPIIIDTDDLPRKRPpniykppsaDVIA 1154
Cdd:cd17646 77 PLDPGYPA------DRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRP---------DNLA 141
|
170 180
....*....|....*....|..
gi 2264466784 1155 YLDFSVSTTGMLTGVKISHSAV 1176
Cdd:cd17646 142 YVIYTSGSTGRPKGVMVTHAGI 163
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1366-1494 |
1.61e-04 |
|
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: 46.15 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1366 GTILPGVRVVIVNPETRgPLGDSHLGEIWVNSPHTASGYYtiyGEESLQADHFNTkLSFGDPHTLWARTGYLgfVKRTel 1445
Cdd:cd17643 273 GRPLPGLRVYVLDADGR-PVPPGVVGELYVSGAGVARGYL---GRPELTAERFVA-NPFGGPGSRMYRTGDL--ARRL-- 343
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 2264466784 1446 tdSSGErhdaLFIVGSLDETLELRGLRYHPIDIEISVqRAHRSIGESAV 1494
Cdd:cd17643 344 --PDGE----LEYLGRADEQVKIRGFRIELGEIEAAL-ATHPSVRDAAV 385
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
335-461 |
2.14e-04 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 45.68 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 335 ARWGATQ-GKSPALTTLDITgkplytLTYGKLWSRGVKLAYTLLnklgtknEQVLKPGDRVALVYPNSDPgmFWVAFYGC 413
Cdd:cd17631 1 LRRRARRhPDRTALVFGGRS------LTYAELDERVNRLAHALR-------ALGVAKGDRVAVLSKNSPE--FLELLFAA 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 2264466784 414 LLAEVIPVPIEVPLSRKDagssqVGFLLGSCGVSLALtSEICL-------KGLPK 461
Cdd:cd17631 66 ARLGAVFVPLNFRLTPPE-----VAYILADSGAKVLF-DDLALlmytsgtTGRPK 114
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
998-1179 |
2.57e-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: 45.40 E-value: 2.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 998 RAQTDPDHVLYVLLNAkgvavcTATCVQLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVR 1077
Cdd:cd17655 6 QAEKTPDHTAVVFEDQ------TLTYRELNERANQLARTLREK-GVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPID 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1078 PPHPQNlsatlpTVRMIIDVSKAACILTTQILTKILRSKEAAtsvniktwpIIIDTDDLPRKRPPNIYKPPSADVIAYLD 1157
Cdd:cd17655 79 PDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLI---------DLLDEDTIYHEESENLEPVSKSDDLAYVI 143
|
170 180
....*....|....*....|..
gi 2264466784 1158 FSVSTTGMLTGVKISHSAVSAL 1179
Cdd:cd17655 144 YTSGSTGKPKGVMIEHRGVVNL 165
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
333-423 |
2.80e-04 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 45.49 E-value: 2.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 333 ALARWGATQGKSPALTTLDITGKPlYTLTYGKLWSRGVKLAyTLLNKLGtkneqvLKPGDRVALVYPNSdPgMFWVAFYG 412
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGEDGEE-RTLTYAELRREVNRFA-NALRALG------VKKGDRVAIYLPNI-P-EAVIAMLA 83
|
90
....*....|.
gi 2264466784 413 CLLAEVIPVPI 423
Cdd:COG0365 84 CARIGAVHSPV 94
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
359-534 |
4.56e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 44.54 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 359 TLTYGKLWSRGVKLAYTLLNkLGtkneqvLKPGDRVALVYPNSDpgMFWVAFYGCLLAEVIPVPIEVPLSRKDagssqVG 438
Cdd:PRK08316 36 SWTYAELDAAVNRVAAALLD-LG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 439 FLLGSCGVSLALTSEICLKGLPKTSTGEILQFKGWPRL--------KWVITDSKYLTKPSKDWQPHIptANIDTAYIEYK 510
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVlggreapgGWLDFADWAEAGSVAEPDVEL--ADDDLAQILYT 179
|
170 180
....*....|....*....|....
gi 2264466784 511 ASKEgtvvgvAVSKIAMLTHcQAL 534
Cdd:PRK08316 180 SGTE------SLPKGAMLTH-RAL 196
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1020-1105 |
4.56e-04 |
|
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: 44.76 E-value: 4.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1020 TATCVQLHKRAEKIAAALmERSGISIGENIVLLYPPGIDLIAAFYGCLYAGCIPVTVRPP-HPQNLS--ATLPTVRMIID 1096
Cdd:cd05919 10 SVTYGQLHDGANRLGSAL-RNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLlHPDDYAyiARDCEARLVVT 88
|
....*....
gi 2264466784 1097 VSKAACILT 1105
Cdd:cd05919 89 SADDIAYLL 97
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1365-1484 |
5.97e-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: 44.27 E-value: 5.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1365 SGTILPGVRVVIVNPETRGPLGDSHLGEIWVNSPHTASGYY-----TiygEESLQADH-FNTklsfGDPHTlWARTGYLG 1438
Cdd:cd17640 266 VGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYknpeaT---SKVLDSDGwFNT----GDLGW-LTCGGELV 337
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2264466784 1439 FVKRTELTdssgerhdalfIVGSLDETLElrglryhPIDIEISVQR 1484
Cdd:cd17640 338 LTGRAKDT-----------IVLSNGENVE-------PQPIEEALMR 365
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
358-536 |
7.81e-04 |
|
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: 43.80 E-value: 7.81e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 358 YTLTYGKLWSRGVKLAyTLLNKLGtkneqvLKPGDRVALVYPNSDPGMfwVAFYGCLLAEVIPVPIEV--PLSRKDAgss 435
Cdd:cd12114 11 GTLTYGELAERARRVA-GALKAAG------VRPGDLVAVTLPKGPEQV--VAVLGILAAGAAYVPVDIdqPAARREA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 436 qvgfLLGSCGVSLALTSEICLKGLPKTSTgeilqfkgwprlkwVITDSKYLTKPSKDwQPHIPTANIDTAYIEYKASKEG 515
Cdd:cd12114 79 ----ILADAGARLVLTDGPDAQLDVAVFD--------------VLILDLDALAAPAP-PPPVDVAPDDLAYVIFTSGSTG 139
|
170 180
....*....|....*....|.
gi 2264466784 516 TVVGVAVSKIAMLTHCQALSQ 536
Cdd:cd12114 140 TPKGVMISHRAALNTILDINR 160
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
359-530 |
1.51e-03 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 42.94 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 359 TLTYGKLWSRGVKLAYTLLNKLGtkneqvLKPGDRVALVYPNSDpgMFWVAFYGCLLAEVIPV---PIEVPLSRK----D 431
Cdd:PRK08751 50 TITYREADQLVEQFAAYLLGELQ------LKKGDRVALMMPNCL--QYPIATFGVLRAGLTVVnvnPLYTPRELKhqliD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 432 AGSSQVGFLLGSCGVSLALTSEICLKGLPKTSTGEILQFKGWPRLKWVItdsKYLTKPSKDWQ----------------- 494
Cdd:PRK08751 122 SGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGFPKAALVNFVV---KYVKKLVPEYRingairfrealalgrkh 198
|
170 180 190
....*....|....*....|....*....|....*...
gi 2264466784 495 --PHIPTANIDTAYIEYKASKEGtvvgvaVSKIAMLTH 530
Cdd:PRK08751 199 smPTLQIEPDDIAFLQYTGGTTG------VAKGAMLTH 230
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
991-1076 |
1.86e-03 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 42.78 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 991 LSEALQWRAQTDPDHVLYVLLNAKGVAVCTATcvQLHKRAEKIAAALMERsGISIGENIVLLYPPGIDLIAAFYGCLYAG 1070
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEDGIWQSLTWA--EFAERVRALAAGLLAL-GVKPGDRVAILSDNRPEWVIADLAILAAG 89
|
....*.
gi 2264466784 1071 CIPVTV 1076
Cdd:COG1022 90 AVTVPI 95
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
326-429 |
2.48e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 42.34 E-value: 2.48e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 326 WPP-------------ALQAALARWGATQGKSPALttlDITGkplYTLTYGKLWSRGVKLAyTLLNKLGtkneqvLKPGD 392
Cdd:PRK06178 18 WPAgiprepeyphgerPLTEYLRAWARERPQRPAI---IFYG---HVITYAELDELSDRFA-ALLRQRG------VGAGD 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 2264466784 393 RVALVYPNSdPgMFWVAFYGCLLAEVIPVPIEvPLSR 429
Cdd:PRK06178 85 RVAVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFR 118
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
359-453 |
3.07e-03 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. 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. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 41.81 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 359 TLTYGKLWSRGVKLAYTLLnKLGtkneqvLKPGDRVALVYPNSDPgmFWVAFYGCLLAEVIPVPIEVPLSrkdagSSQVG 438
Cdd:cd05907 5 PITWAEFAEEVRALAKGLI-ALG------VEPGDRVAILSRNRPE--WTIADLAILAIGAVPVPIYPTSS-----AEQIA 70
|
90
....*....|....*
gi 2264466784 439 FLLGSCGVSLALTSE 453
Cdd:cd05907 71 YILNDSEAKALFVED 85
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1366-1495 |
3.24e-03 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 41.89 E-value: 3.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1366 GTILPGVRVVIVNPETRGPLGDSHLGEIWVNSPHTASGYY-----TiygEESLQADHfntklsfgdphtlWARTGYLGFV 1440
Cdd:cd05941 267 GMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWnkpeaT---KEEFTDDG-------------WFKTGDLGVV 330
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2264466784 1441 krteltDSSGerhdALFIVG-SLDETLELRGLRYHPIDIEiSVQRAHRSIGESAVF 1495
Cdd:cd05941 331 ------DEDG----YYWILGrSSVDIIKSGGYKVSALEIE-RVLLAHPGVSECAVI 375
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1366-1479 |
3.25e-03 |
|
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: 41.48 E-value: 3.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1366 GTILPGVRVVIVNPETRGPLGDSHlGEIWVNSPHTASGYYTiygEESLQADHFNTKlsfgdphtlWARTGYLGFVKrtel 1445
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGYWN---NPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110
....*....|....*....|....*....|....
gi 2264466784 1446 tdssgeRHDALFIVGSLDETLELRGLRYHPIDIE 1479
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE 263
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1357-1494 |
3.68e-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: 41.70 E-value: 3.68e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2264466784 1357 PQSLPLMESGTILPGVRVVIVNPETRGPLGDSHLGEIWVNSPHTASGYYtiygeeslQADHFNTKLSFGDPHTLWARTGY 1436
Cdd:cd05935 245 PLRPKLQCLGIP*FGVDARVIDIETGRELPPNEVGEIVVRGPQIFKGYW--------NRPEETEESFIEIKGRRFFRTGD 316
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 2264466784 1437 LGFVkrteltDSSGerhdALFIVGSLDETLELRGLRYHPIDIEiSVQRAHRSIGESAV 1494
Cdd:cd05935 317 LGYM------DEEG----YFFFVDRVKRMINVSGFKVWPAEVE-AKLYKHPAI*EVCV 363
|
|
| |
