|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1136-1751 |
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: 751.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1136 IFTLLNSKGAIAKTLTCSELHKRAEKIAALLQERGRIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPH-PQNLN 1214
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1215 TTLPTVRMivDVSKSGIVLSIQPIIKLLKSREAATSIDPKTWPPILDIDDNPK------RKYAGIATVSFDSSAYLDFSV 1288
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKskrsklKKWGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1289 STCGRLSGVNITHRSLSSLCASLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYEVEANPSLWLSTL 1368
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1369 SQHRVRDTFCSYGVIELCTKALSNSIPSLKQRNIDLRCVRTCVVVAEERPRVQLTQQFCKLFQALGLNTRCVSTSFGCRV 1448
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1449 NPAICVQGASSAESAQVYVDMRALRNNRVALVERGAPNSLCVIESGKLLPGVKVIIANPETKGHCGDSHLGEIWVQAPHN 1528
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1529 ANGYFTIYGDETDYNDHFNA-KLVTGATSELYARTGYLGFLRRTECSQSaslldettpsvasrdsdteslnsisqlqlnf 1607
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFPStRLSTGITNNSYARTGLLGFLRPTKCTDL------------------------------- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1608 snvslggnsehslvggasnanDQELHDAVYVVGAVDEVISLRGMNYHPIDIENSVMRCHKKIAECAVFTWTNLLVVVVEL 1687
Cdd:cd05905 448 ---------------------NVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQ 506
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386770269 1688 D-GNESEALDLVPLVTNTVLEDHQLIVGVVVVVDPGVVPINSRGEKQRMHLRDGFLADQLDPIYV 1751
Cdd:cd05905 507 PpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
464-1060 |
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: 688.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 464 MATVLDPNGKVTTTLTYGKLLSRAQKIAHALSTKIfskgpeqvTLKPGDRVALVYPnnDPLSFITAWYGCMFRGLVPLPI 543
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKV--------GLKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 544 ELPLsssdtPPQQVGFLLSSCGITVALTSEACLKGLPKST----TTGEIAKLKGWPRLQWFVTEHLPKP-PKEFNVGNLR 618
Cdd:cd05905 71 EPPD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKLlkskTAAEIAKKKGWPKILDFVKIPKSKRsKLKKWGPHPP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 619 ADDSAAAYIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYA 698
Cdd:cd05905 146 TRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 699 LMKLRPSSWMQLITKHRASCCLVKSRDLHWGL------LATKDHKDISLSSLRMLLVADGaNPWSLSSCDQFLSVFQAKG 772
Cdd:cd05905 226 LMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 773 LRSDAIcpcasSSEVFTVSLRRPGRGscGFSPSATGRGVLSMAALSHGVVRVDSEDSLTSLTLQDCGQVMPAAQMVVVRS 852
Cdd:cd05905 305 LSPRAV-----STEFGTRVNPFICWQ--GTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 853 EGPPvLCKTDQVGEICVTSGSTSASYFGLDGMTNSTFKVQPlleeleqpkdgngtVNIISKPIGEDFYVRS--------- 923
Cdd:cd05905 378 ETKG-LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFP--------------STRLSTGITNNSYARTgllgflrpt 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 924 -GLLGFLGPGGLVFVCGSRDGLMTVTGRKHNADDIIATVLAVEPmrfiYRGRIAVFSIKvlrdERVCVIAEQRPdCSEEE 1002
Cdd:cd05905 443 kCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSEEE 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 386770269 1003 SFQWMSRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRFLEGSLHPANV 1060
Cdd:cd05905 514 ALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1126-1711 |
2.74e-59 |
|
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: 214.80 E-value: 2.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1126 WRANTSPDHIIFTLLNSKGAIAKTLTCSELHKRAEKIAALLQERGRiePGDHVALIFPPGLDLLCAFYGCLYLGAIPITI 1205
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1206 RPPHPqnlNTTLPTVRMIVDVSKSGIVLSIQPIIKLLKSREAATSIDPKTWPPILDIDDNPKRKYAGIATVSFDSSAYLD 1285
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1286 F-SVSTcGRLSGVNITHRSLSSLCASLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYEVEANPSLW 1364
Cdd:cd05931 156 YtSGST-GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1365 LSTLSQHRvrdtfcsyGVI--------ELCTKAlsnsIPSLKQRNIDLRCVRTCVVVAeERPRVQLTQQFCKLFQALGLN 1436
Cdd:cd05931 235 LRLISRYR--------ATIsaapnfayDLCVRR----VRDEDLEGLDLSSWRVALNGA-EPVRPATLRRFAEAFAPFGFR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1437 TRCVSTSFGCrvnpAICVQGASSAESAQ----VYVDMRALRnNRVALVERGAPNSLCVIESGKLLPGVKVIIANPETKGH 1512
Cdd:cd05931 302 PEAFRPSYGL----AEATLFVSGGPPGTgpvvLRVDRDALA-GRAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGRE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1513 CGDSHLGEIWVQAPHNANGYFtiyGDETDYNDHFNAKLVTGATSelYARTGYLGFLRrtecsqsaslldettpsvasrds 1592
Cdd:cd05931 377 LPDGEVGEIWVRGPSVASGYW---GRPEATAETFGALAATDEGG--WLRTGDLGFLH----------------------- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1593 dteslnsisqlqlnfsnvslggnsehslvggasnanDQELhdavYVVGAVDEVISLRGMNYHPIDIENSVMRCHKKIAE- 1671
Cdd:cd05931 429 ------------------------------------DGEL----YITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPg 468
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 386770269 1672 -CAVFTW----TNLLVVVVELDGNEsEALDLVPLVTN---TVLEDHQL 1711
Cdd:cd05931 469 cVAAFSVpddgEERLVVVAEVERGA-DPADLAAIAAAiraAVAREHGV 515
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
466-1051 |
1.12e-57 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 210.17 E-value: 1.12e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 466 TVLDPNGKVTTTLTYGKLLSRAQKIAHALstkifskgpeQVTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIEL 545
Cdd:cd05931 13 TFLDDEGGREETLTYAELDRRARAIAARL----------QAVGKPGDRVLLLAPPG--LDFVAAFLGCLYAGAIAVPLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 546 PLSSSDTPpqQVGFLLSSCGITVALTSEACLKGLPKSTTTGEiaklkGWPRLQWFVTEHLP-KPPKEFNVGNLRADDsaA 624
Cdd:cd05931 81 PTPGRHAE--RLAAILADAGPRVVLTTAAALAAVRAFAASRP-----AAGTPRLLVVDLLPdTSAADWPPPSPDPDD--I 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 625 AYIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFI-PYALMKlR 703
Cdd:cd05931 152 AYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMsPAAFLR-R 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 704 PSSWMQLITKHRASC----------CLVKSRDLHwglLATKDhkdisLSSLRMLLVadGANPWSLSSCDQFLSVFQAKGL 773
Cdd:cd05931 231 PLRWLRLISRYRATIsaapnfaydlCVRRVRDED---LEGLD-----LSSWRVALN--GAEPVRPATLRRFAEAFAPFGF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 774 RSDAICPC---ASSSeVFtVSLRRPGRGscgfsPSATgrgVLSMAALSHGVVRVDSEDSlTSLTLQDCGQVMPAAQMVVV 850
Cdd:cd05931 301 RPEAFRPSyglAEAT-LF-VSGGPPGTG-----PVVL---RVDRDALAGRAVAVAADDP-AARELVSCGRPLPDQEVRIV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 851 RSEGPPVlCKTDQVGEICVTSGSTSASYFGLDGMTNSTFKvqpllEELEQPKDG---NGTVNIISKpiGEdfyvrsgllg 927
Cdd:cd05931 370 DPETGRE-LPDGEVGEIWVRGPSVASGYWGRPEATAETFG-----ALAATDEGGwlrTGDLGFLHD--GE---------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 928 flgpgglVFVCGSRDGLMTVTGRKHNADDIIATVLAVEPMrfIYRGRIAVFSIKVLRDERVCVIAEQRPDCSEEESFQWM 1007
Cdd:cd05931 432 -------LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIA 502
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 386770269 1008 SRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRFL 1051
Cdd:cd05931 503 AAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1124-1569 |
5.80e-40 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 154.39 E-value: 5.80e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1124 LRWRANTSPDHIIFTllnskGAIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPI 1203
Cdd:pfam00501 1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1204 TIRPphpqnlNTTLPTVRMIVDVSKSGIVLsIQPIIKLLKSREAATSIDPKTWPPILDIDDNPKRKYAGIATVSF----- 1278
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLI-TDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAdvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1279 -------DSSAYLDFSVSTCGRLSGVNITHRSLSSLCASLKLACE----LYPSRHVALCLDPYCGLGFVMWTLIGVYSGH 1347
Cdd:pfam00501 148 pppppdpDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1348 HSILIAPyEVEANPSLWLSTLSQHRVRDTFCSYGVIELCTKALS---NSIPSLKQrnidlrcvrtcVVVAEERPRVQLTQ 1424
Cdd:pfam00501 228 TVVLPPG-FPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGApkrALLSSLRL-----------VLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1425 QFCKLFqalglnTRCVSTSFGCRVNPAICvqgassaesaqVYVDMRALRNNRVALVergapnslcviesGKLLPGVKVII 1504
Cdd:pfam00501 296 RFRELF------GGALVNGYGLTETTGVV-----------TTPLPLDEDLRSLGSV-------------GRPLPGTEVKI 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386770269 1505 ANPETKGHCGDSHLGEIWVQAPHNANGYftiYGDETDYNDHFNAKlvtgatsELYaRTGYLGFLR 1569
Cdd:pfam00501 346 VDDETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAFDED-------GWY-RTGDLGRRD 399
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
469-1060 |
1.34e-31 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 132.44 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 469 DPNGKVTTTLTYGKLLSRAQKIAHALSTkifskgpeqVTLKPGDRVALVyPNNDPlSFITAWYGCMFRGLVPLPIELPLS 548
Cdd:PRK09192 41 DRRGQLEEALPYQTLRARAEAGARRLLA---------LGLKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPMG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 549 --SSDTPPQQVGFLLSSCGITVALTSEAcLKGLPKSTTTGEIAKLKGWPRlqWFVTehLPKPPKEFNvgnlRADDSAAAY 626
Cdd:PRK09192 110 fgGRESYIAQLRGMLASAQPAAIITPDE-LLPWVNEATHGNPLLHVLSHA--WFKA--LPEADVALP----RPTPDDIAY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 627 IEYTTdkeGSV---MGVTVTRAAMINHCRALTM-ACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYALMKL 702
Cdd:PRK09192 181 LQYSS---GSTrfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFAR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 703 RPSSWMQLITKHRASC----------CLVKSRDlhwgllatKDHKDISLSSLRmlLVADGANPWSLSSCDQFLSVFQAKG 772
Cdd:PRK09192 258 RPLQWLDLISRNRGTIsysppfgyelCARRVNS--------KDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 773 LRSDAICPCASSSEVfTVSLrrpgrgscGFSPSATGRGVLSMAA--LSHGVVRVDS-EDSLTSLTLQDCGQVMPAAQmVV 849
Cdd:PRK09192 328 FDDKAFMPSYGLAEA-TLAV--------SFSPLGSGIVVEEVDRdrLEYQGKAVAPgAETRRVRTFVNCGKALPGHE-IE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 850 VRSEGPPVLCKTdQVGEICVTSGSTSASYFGlDGMTNSTFKVQPLLE--ELEQPKDGNgtvniiskpigedfyvrsgllg 927
Cdd:PRK09192 398 IRNEAGMPLPER-VVGHICVRGPSLMSGYFR-DEESQDVLAADGWLDtgDLGYLLDGY---------------------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 928 flgpgglVFVCGSRDGLMTVTGRKHNADDIiatVLAVEPMRFIYRGRIAVFSIKVLRDERVCVIAEQRPDcSEEESFQWM 1007
Cdd:PRK09192 454 -------LYITGRAKDLIIINGRNIWPQDI---EWIAEQEPELRSGDAAAFSIAQENGEKIVLLVQCRIS-DEERRGQLI 522
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 386770269 1008 SRVLQAVDSIHqvGIYCL-ALVPPNHLPKTPLGGIHLCEARRRFLEGSLHPANV 1060
Cdd:PRK09192 523 HALAALVRSEF--GVEAAvELVPPHSLPRTSSGKLSRAKAKKRYLSGAFASLDV 574
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
3-115 |
3.13e-31 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 118.68 E-value: 3.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 3 HTASLPGYVREKLAELDLELSEGDITQKGYEKKRAKLLQPFLKKPEgdkvkstpPPPYYNVKNANNSTNHGNINNDGvIV 82
Cdd:pfam06464 1 NPPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLHPE--------TPTKLSAEAQNQLASLETKLRDE-EL 71
|
90 100 110
....*....|....*....|....*....|...
gi 386770269 83 SSEGYSYVTEVPSLSSSQQRHSKKIDFHQQAAM 115
Cdd:pfam06464 72 SEEVYLEKVKALLAKELERENGLNAPTKEQSGL 104
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
476-890 |
2.83e-27 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 116.64 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 476 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIelplsSSDTPPQ 555
Cdd:pfam00501 20 RRLTYRELDERANRLAAGLR----ALG-----VGKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPL-----NPRLPAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 556 QVGFLLSSCGITVALTSEACL-------KGLPKSTTTGEIAKLKGWPRLQWFVTEHLPKPPKEFNVGNLRADDsaAAYIE 628
Cdd:pfam00501 84 ELAYILEDSGAKVLITDDALKleelleaLGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDD--LAYII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 629 YT-----TDKegsvmGVTVTRAAMINHCRALTMACHY----TEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYAL 699
Cdd:pfam00501 162 YTsgttgKPK-----GVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 700 MkLRPSSWMQLITKHRASC-CLVKSrdLHWGLLATKDHKDISLSSLRMLLVadGANPWSLSSCDQFLSVFqakglrsdai 778
Cdd:pfam00501 237 A-LDPAALLELIERYKVTVlYGVPT--LLNMLLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF---------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 779 cpcasssevftvslrrPGRGSCGFSPSATGrgvlsmAALSHGVVRVDSEDSLTSltlqdCGQVMPAAQMVVV-RSEGPPV 857
Cdd:pfam00501 302 ----------------GGALVNGYGLTETT------GVVTTPLPLDEDLRSLGS-----VGRPLPGTEVKIVdDETGEPV 354
|
410 420 430
....*....|....*....|....*....|...
gi 386770269 858 lcKTDQVGEICVTSGSTSASYFGLDGMTNSTFK 890
Cdd:pfam00501 355 --PPGEPGELCVRGPGVMKGYLNDPELTAEAFD 385
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1282-1696 |
9.66e-27 |
|
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: 113.53 E-value: 9.66e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1282 AYLDFSVSTCGRLSGVNITHRSLSSLCASLkLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYeveaNP 1361
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF----DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1362 SLWLSTLSQHRVRDTFCSYGVIELCTKALsnsipslKQRNIDLRCVRTCVVVAEERPRVqLTQQF-----CKLFQALGLN 1436
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAP-------ESAGYDLSSLRALVSGGAPLPPE-LLERFeeapgIKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1437 TRCVSTSFGCRVNPAicvqgassaesaqvyvdmralrnnrvalverGAPNSlcvieSGKLLPGVKVIIANPETkGHCGDS 1516
Cdd:cd04433 150 ETGGTVATGPPDDDA-------------------------------RKPGS-----VGRPVPGVEVRIVDPDG-GELPPG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1517 HLGEIWVQAPHNANGYFTiygdetdyndhfNAKLVTGATSELYARTGYLGFLrrtecsqsasllDEttpsvasrdsdtes 1596
Cdd:cd04433 193 EIGELVVRGPSVMKGYWN------------NPEATAAVDEDGWYRTGDLGRL------------DE-------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1597 lnsisqlqlnfsnvslggnsehslvggasnandqelHDAVYVVGAVDEVISLRGMNYHPIDIENSVMRcHKKIAECAVF- 1675
Cdd:cd04433 235 ------------------------------------DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLG-HPGVAEAAVVg 277
|
410 420
....*....|....*....|....*
gi 386770269 1676 ----TWTNLLVVVVELDGNESEALD 1696
Cdd:cd04433 278 vpdpEWGERVVAVVVLRPGADLDAE 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1117-1572 |
5.62e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 117.58 E-value: 5.62e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1117 PQLITGVLRWRANTSPDHIIFTLLNSKGAIAKTLTCSELHKRAEKIAALLQERGriEPGDHVALIFPPGLDLLCAFYGCL 1196
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARA--SFGDRAVLLFPSGPDYVAAFFGCL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1197 YLGAIPITIRPP------HPQNLNTtlptvrmIVDVSKSGIVLSIQPIIKLLKSREAATSIDPktwPPILDIDDNPkrky 1270
Cdd:PRK05691 86 YAGVIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLD---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1271 AGIA------TVSFDSSAYLDFSVSTCGRLSGVNITHRSLsslcaslkLACELYPSRHVALCLDP----------YCGLG 1334
Cdd:PRK05691 152 PALAeawqepALQPDDIAFLQYTSGSTALPKGVQVSHGNL--------VANEQLIRHGFGIDLNPddvivswlplYHDMG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1335 FVMWTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRvrdtfcsyGVI--------ELCTKALSNSipSLKQrnIDLRC 1406
Cdd:PRK05691 224 LIGGLLQPIFSGVPCVLMSPAYFLERPLRWLEAISEYG--------GTIsggpdfayRLCSERVSES--ALER--LDLSR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1407 VRtcVVVAEERP-RVQLTQQFCKLFQALGLNTRCVSTSFGCrVNPAICVQGASSAES-AQVYVDMRALRNNRVALVErGA 1484
Cdd:PRK05691 292 WR--VAYSGSEPiRQDSLERFAEKFAACGFDPDSFFASYGL-AEATLFVSGGRRGQGiPALELDAEALARNRAEPGT-GS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1485 PnslcVIESGKLLPGVKVIIANPETKGHCGDSHLGEIWVQAPHNANGYFTiygdetdyNDHFNAKLVTGATSELYARTGY 1564
Cdd:PRK05691 368 V----LMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR--------NPEASAKTFVEHDGRTWLRTGD 435
|
....*...
gi 386770269 1565 LGFLRRTE 1572
Cdd:PRK05691 436 LGFLRDGE 443
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
476-890 |
6.84e-26 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 113.37 E-value: 6.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 476 TTLTYGKLLSRAQKIAHALStkifskgpeQVTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIELPLsssdtPPQ 555
Cdd:COG0318 23 RRLTYAELDARARRLAAALR---------ALGVGPGDRVALLLPNS--PEFVVAFLAALRAGAVVVPLNPRL-----TAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 556 QVGFLLSSCGITVALTseACLkgLPKSTTTGeiaklkgwprlqwfvtehLPKppkefnvgnlraddsaaayieyttdkeg 635
Cdd:COG0318 87 ELAYILEDSGARALVT--ALI--LYTSGTTG------------------RPK---------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 636 svmGVTVTRAAMINHCRALTMACHYTEGETIVCVL----DFkrevGLWHSVLTSVLNGMHVIFIPyalmKLRPSSWMQLI 711
Cdd:COG0318 117 ---GVMLTHRNLLANAAAIAAALGLTPGDVVLVALplfhVF----GLTVGLLAPLLAGATLVLLP----RFDPERVLELI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 712 TKHRAS-CCLVKSrdLHWGLLATKDHKDISLSSLRMLLVadGANPWSLSSCDQFLSVFQAkglrsdAICPCASSSEVFTV 790
Cdd:COG0318 186 ERERVTvLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFEERFGV------RIVEGYGLTETSPV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 791 SLRRPGrgscgfspsatgrgvlsmaalSHGVVRVDSedsltsltlqdCGQVMPAAQMVVVRSEGPPVlcKTDQVGEICVT 870
Cdd:COG0318 256 VTVNPE---------------------DPGERRPGS-----------VGRPLPGVEVRIVDEDGREL--PPGEVGEIVVR 301
|
410 420
....*....|....*....|
gi 386770269 871 SGSTSASYFGLDGMTNSTFK 890
Cdd:COG0318 302 GPNVMKGYWNDPEATAEAFR 321
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1120-1698 |
1.16e-25 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 112.60 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1120 ITGVLRWRANTSPDHIIFTLLNskgaiaKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLG 1199
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGG------RRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1200 AIPITIrpphpqNLNTTLPTVRMIVDVSKSGIVLS--IQPiikllksreaaTSidpktwppildiddnpkrkyaGiatvs 1277
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVTalILY-----------TS---------------------G----- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1278 fdssayldfsvSTcGRLSGVNITHRSLSSLCASLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYev 1357
Cdd:COG0318 111 -----------TT-GRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRF-- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1358 eaNPSLWLSTLSQHRVrdTFcSYGV----IELCTKAlsnsipslKQRNIDLRCVRTCVVVAEerprvQLTQQFCKLFQAL 1433
Cdd:COG0318 177 --DPERVLELIERERV--TV-LFGVptmlARLLRHP--------EFARYDLSSLRLVVSGGA-----PLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1434 glntrcvstsFGCRVnpaicVQGASSAE-SAQVYVDMRALRNNRVALVergapnslcviesGKLLPGVKVIIANPETKGh 1512
Cdd:COG0318 239 ----------FGVRI-----VEGYGLTEtSPVVTVNPEDPGERRPGSV-------------GRPLPGVEVRIVDEDGRE- 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1513 CGDSHLGEIWVQAPHNANGYftiYGDEtdyndhfnaklvtGATSELYA----RTGYLGFLrrtecsqsaslldettpsva 1588
Cdd:COG0318 290 LPPGEVGEIVVRGPNVMKGY---WNDP-------------EATAEAFRdgwlRTGDLGRL-------------------- 333
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1589 srDSDteslnsisqlqlnfsnvslgGNsehslvggasnandqelhdaVYVVGAVDEVISLRGMNYHPIDIENSVMRcHKK 1668
Cdd:COG0318 334 --DED--------------------GY--------------------LYIVGRKKDMIISGGENVYPAEVEEVLAA-HPG 370
|
570 580 590
....*....|....*....|....*....|....*.
gi 386770269 1669 IAECAVF-----TWTNLLVVVVEL-DGNESEALDLV 1698
Cdd:COG0318 371 VAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELR 406
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1120-1568 |
1.69e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 107.34 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1120 ITGVLRWRANTSPDHIIFTLLN---SKGAIAKTLTCSELHKRAEKIAALLQERGRiePGDHVALIFPPGLDLLCAFYGCL 1196
Cdd:PRK05850 3 VPSLLRERASLQPDDAAFTFIDyeqDPAGVAETLTWSQLYRRTLNVAEELRRHGS--TGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1197 YLGAIPITIRPPHPQnlnttlptvrmIVDVSKSGIVLSIQPIIKLLKS------REAATSIDPKTWPPILDID--DNPKR 1268
Cdd:PRK05850 81 QAGLIAVPLSVPQGG-----------AHDERVSAVLRDTSPSVVLTTSavvddvTEYVAPQPGQSAPPVIEVDllDLDSP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1269 KYAGIATVSFDSSAYLDF-SVSTcgRL-SGVNITHRSLSSLCAslKLACELYPSRHVALCLD-------P-YCGLGFVMW 1338
Cdd:PRK05850 150 RGSDARPRDLPSTAYLQYtSGST--RTpAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMGLVLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1339 TLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRVRDTFCSYGVIELCTKALSNSipslKQRNIDLRCVRTCVVVAEerp 1418
Cdd:PRK05850 226 VCAPILGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVRKTSDD----DMAGLDLGGVLGIISGSE--- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1419 RVQLT--QQFCKLFQALGLNTRCVSTSFGCrvnpAICVQGASSAESAQ----VYVDMRALRNNRV---------ALVERG 1483
Cdd:PRK05850 299 RVHPAtlKRFADRFAPFNLRETAIRPSYGL----AEATVYVATREPGQppesVRFDYEKLSAGHAkrcetgggtPLVSYG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1484 APNSlcviesgkllPGVKviIANPETKGHCGDSHLGEIWVQAPHNANGYFTiYGDETdyNDHFNAKLVT---GATSELYA 1560
Cdd:PRK05850 375 SPRS----------PTVR--IVDPDTCIECPAGTVGEIWVHGDNVAAGYWQ-KPEET--ERTFGATLVDpspGTPEGPWL 439
|
....*...
gi 386770269 1561 RTGYLGFL 1568
Cdd:PRK05850 440 RTGDLGFI 447
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1150-1567 |
1.72e-21 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 101.36 E-value: 1.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1150 LTCSELHKRAEKIAALLQERGRiePGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPP----HPQNLNTTL----PTVR 1221
Cdd:PRK12476 69 LTWTQLGVRLRAVGARLQQVAG--PGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1222 MIVDVSKsgivlsiQPIIKLLKSREAATSidpktwPPILDIDDNPKRKYAGIATVSFDSS--AYLDFSVSTCGRLSGVNI 1299
Cdd:PRK12476 147 LTTTAAA-------EAVEGFLRNLPRLRR------PRVIAIDAIPDSAGESFVPVELDTDdvSHLQYTSGSTRPPVGVEI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1300 THRSLSSLCASLKLACELY-PSRHVALCLDPYCGLGFVMWTLIGVYSGhHSILIAPYEVEANPSLWLSTLSQHrvrdtfC 1378
Cdd:PRK12476 214 THRAVGTNLVQMILSIDLLdRNTHGVSWLPLYHDMGLSMIGFPAVYGG-HSTLMSPTAFVRRPQRWIKALSEG------S 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1379 SYGviELCTKALSNSIPSLKQR-------NIDLRCVrtCVVVAEERPRVQLTQQFCKLFQALGLNTRCVSTSFGCRVNPA 1451
Cdd:PRK12476 287 RTG--RVVTAAPNFAYEWAAQRglpaegdDIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1452 ICVQGASSAESAQVYVDMRALRNNRVALVERGAPNSLCVIESGKLLPGVKVIIANPETKGHCGDSHLGEIWVQAPHNANG 1531
Cdd:PRK12476 363 FVATIAPDAEPSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRG 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 386770269 1532 YFTiYGDETDYNdhFNAKLVT----------GATSELYARTGYLGF 1567
Cdd:PRK12476 443 YWG-RPEETERT--FGAKLQSrlaegshadgAADDGTWLRTGDLGV 485
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
469-1041 |
3.99e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 100.02 E-value: 3.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 469 DPNGkVTTTLTYGKLLSRAQKIAHALStkifSKGpeqvtlKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIELPL- 547
Cdd:PRK05850 28 DPAG-VAETLTWSQLYRRTLNVAEELR----RHG------STGDRAVILAPQG--LEYIVAFLGALQAGLIAVPLSVPQg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 548 SSSDtppQQVGFLLSSCGITVALTSeaclkglpkSTTTGEIAKLKGWPRLQ---WFVTEHLPKPPKEFNVGNLRADDSAA 624
Cdd:PRK05850 95 GAHD---ERVSAVLRDTSPSVVLTT---------SAVVDDVTEYVAPQPGQsapPVIEVDLLDLDSPRGSDARPRDLPST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 625 AYIEYTTDKEGSVMGVTVTRAAMINHCRALtMACHY-------TEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFI-P 696
Cdd:PRK05850 163 AYLQYTSGSTRTPAGVMVSHRNVIANFEQL-MSDYFgdtggvpPPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTsP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 697 YALMKlRPSSWMQLITKHRAScclvksrdlhWGL-------LATKDHKDISLSSL---RMLLVADGA---NPWSLsscDQ 763
Cdd:PRK05850 242 VAFLQ-RPARWMQLLASNPHA----------FSAapnfafeLAVRKTSDDDMAGLdlgGVLGIISGServHPATL---KR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 764 FLSVFQAKGLRSDAICPCASSSE--VFtVSLRRPGRgscgfsPSATGRgvLSMAALSHGVVRVDSEDSLTSLTlqDCGqv 841
Cdd:PRK05850 308 FADRFAPFNLRETAIRPSYGLAEatVY-VATREPGQ------PPESVR--FDYEKLSAGHAKRCETGGGTPLV--SYG-- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 842 MPAAQMV-VVRSEgPPVLCKTDQVGEICVTSGSTSASYFGLDGMTNSTFKVQplleeLEQPKDG--------NGTVNIIS 912
Cdd:PRK05850 375 SPRSPTVrIVDPD-TCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGAT-----LVDPSPGtpegpwlrTGDLGFIS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 913 KpiGEdfyvrsgllgflgpgglVFVCGSRDGLMTVTGRKHNADDIIATVLAvepmrfIYRGRIAVFSIKVLRDERVCVIA 992
Cdd:PRK05850 449 E--GE-----------------LFIVGRIKDLLIVDGRNHYPDDIEATIQE------ITGGRVAAISVPDDGTEKLVAII 503
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 386770269 993 E-QRPDCSEEESFQWM----SRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGI 1041
Cdd:PRK05850 504 ElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1144-1675 |
2.90e-19 |
|
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: 93.43 E-value: 2.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1144 GAIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIpitIRPPHPQN--------LNT 1215
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGGI---FSAANPIYtadelahqLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1216 TLPTVrMIVD------VSKSG-IVLSIQPIIKLLKSREAATSIDPKTWPPILDIDDN-PKRKYAGIATVsfdssAYLDFS 1287
Cdd:cd05911 81 SKPKV-IFTDpdglekVKEAAkELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDlPPPLKDGKDDT-----AAILYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1288 VSTCGRLSGVNITHRslsSLCASLKLAC----ELYPSRHVALCLDPY---CGLgfvMWTLIGVYSGHHSILIAPYEVEan 1360
Cdd:cd05911 155 SGTTGLPKGVCLSHR---NLIANLSQVQtflyGNDGSNDVILGFLPLyhiYGL---FTTLASLLNGATVIIMPKFDSE-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1361 psLWLSTLSQHRVRDTFCSYGVIElctkALSNSiPSLKQrnIDLRCVRTCVVVAEerPrvqLTQQFCKLFQALGLNTRCV 1440
Cdd:cd05911 227 --LFLDLIEKYKITFLYLVPPIAA----ALAKS-PLLDK--YDLSSLRVILSGGA--P---LSKELQELLAKRFPNATIK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1441 StSFGC-RVNPAICVqgassaesaqvyvdmralrnnrvalvergAPNSLCVIES-GKLLPGVKVIIANPETKGHCGDSHL 1518
Cdd:cd05911 293 Q-GYGMtETGGILTV-----------------------------NPDGDDKPGSvGRLLPNVEAKIVDDDGKDSLGPNEP 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1519 GEIWVQAPHNANGYftiYGDETDYNDHFnaklvtgaTSELYARTGYLGFlrrtecsqsaslLDEttpsvasrdsdtesln 1598
Cdd:cd05911 343 GEICVRGPQVMKGY---YNNPEATKETF--------DEDGWLHTGDIGY------------FDE---------------- 383
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386770269 1599 sisqlqlnfsnvslggnsehslvggasnanDQELhdavYVVGAVDEVISLRGMNYHPIDIEnSVMRCHKKIAECAVF 1675
Cdd:cd05911 384 ------------------------------DGYL----YIVDRKKELIKYKGFQVAPAELE-AVLLEHPGVADAAVI 425
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1146-1566 |
3.02e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 94.03 E-value: 3.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1146 IAKTLTCSELHKRAEKIAALLQERGriEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITI----RPPHPQNLNTTL---- 1217
Cdd:PRK07769 52 VARDLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHAVLddct 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1218 PTVRMIVDVSKSGIVlsiqpiiKLLKSREAatsidpKTWPPILDIDDNPKRKYAGIA--TVSFDSSAYLDF-SVSTcgRL 1294
Cdd:PRK07769 130 PSAILTTTDSAEGVR-------KFFRARPA------KERPRVIAVDAVPDEVGATWVppEANEDTIAYLQYtSGST--RI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1295 -SGVNITHRSLSSLCASLKLACEL-YPSRHVALcLDPYCGLGFVMwTLIGVYSGHHSILIAPYEVEANPSLWLSTLSqhr 1372
Cdd:PRK07769 195 pAGVQITHLNLPTNVLQVIDALEGqEGDRGVSW-LPFFHDMGLIT-VLLPALLGHYITFMSPAAFVRRPGRWIRELA--- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1373 vRDTFCSYGVIELCTK-----ALSNSIPSLKQRNIDLRCVRtCVVVAEERPRVQLTQQFCKLFQALGLNTRCVSTSFGCr 1447
Cdd:PRK07769 270 -RKPGGTGGTFSAAPNfafehAAARGLPKDGEPPLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGM- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1448 VNPAICVQGASSAESAQV-YVDMRALRNNRVALVERGAPNSLCVIESGKLLPGVKVIIANPETKGHCGDSHLGEIWVQAP 1526
Cdd:PRK07769 347 AEATLFVSTTPMDEEPTViYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGN 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 386770269 1527 HNANGYftiYGDETDYNDHFNAKL--------VTGATSE-LYARTGYLG 1566
Cdd:PRK07769 427 NIGTGY---WGKPEETAATFQNILksrlseshAEGAPDDaLWVRTGDYG 472
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
473-1053 |
9.68e-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: 88.70 E-value: 9.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 473 KVTTTLTYGKLLSRAQKIAHALstkifskgpEQVTLKPGDRVALVYPNNDplSFITAWYGCMFRGLVPLPIELplSSSDT 552
Cdd:cd05908 11 KKEKFVSYRHLREEALGYLGAL---------QELGIKPGQEVVFQITHNN--KFLYLFWACLLGGMIAVPVSI--GSNEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 553 PPQQVGFLLSSCGITVALTSEACLKGLPkstttgeiaklkgwprlqwfvtEHLpkppkefnvgnlraddsaaAYIEYTTD 632
Cdd:cd05908 78 HKLKLNKVWNTLKNPYLITEEEVLCELA----------------------DEL-------------------AFIQFSSG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 633 KEGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYALMKLRPSSWMQLIT 712
Cdd:cd05908 117 STGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKAS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 713 KHRAS--CCLVKSRDLHWGLLATKDHKDISLSSLRMLLvaDGANPWSLSSCDQFLSVFQAKGLRSDAICPCASSSEVfTV 790
Cdd:cd05908 197 EHKATivSSPNFGYKYFLKTLKPEKANDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA-SV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 791 SLRRPGRGSCGFSPSATGRGVLsmaaLSHGVVRVDSEDSlTSLTLQDCGQVMPAAQMVVVRSEGPPVlcKTDQVGEICVT 870
Cdd:cd05908 274 GASLPKAQSPFKTITLGRRHVT----HGEPEPEVDKKDS-ECLTFVEVGKPIDETDIRICDEDNKIL--PDGYIGHIQIR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 871 SGSTSASYFgldgmtnstfkvqplleelEQPKDgngTVNIISkpigEDFYVRSGLLGflgpgglvFVcgsRDGLMTVTGR 950
Cdd:cd05908 347 GKNVTPGYY-------------------NNPEA---TAKVFT----DDGWLKTGDLG--------FI---RNGRLVITGR 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 951 K--------HNA--DDIIATVLAVEPmrfIYRGRIAVFSI--KVLRDERVCVIAEQRPdcSEEESFQWMSRVLQAVD--- 1015
Cdd:cd05908 390 EkdiifvngQNVypHDIERIAEELEG---VELGRVVACGVnnSNTRNEEIFCFIEHRK--SEDDFYPLGKKIKKHLNkrg 464
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 386770269 1016 --SIHQVgiyclalVPPNHLPKTPLGGIHLCEARRRFLEG 1053
Cdd:cd05908 465 gwQINEV-------LPIRRIPKTTSGKVKRYELAQRYQSG 497
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1117-1569 |
6.64e-16 |
|
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: 83.10 E-value: 6.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1117 PQLITGVLRWRANTSPDHIIfTLLNSKGAiAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCL 1196
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADGS-EEFQSYQDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWACV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1197 YLGAIPITIRPP-----------HPQNLNTTL--PTV----RMIVDVSKSGIVLSIQPIiKLLKSREAATSIDPKTWPPi 1259
Cdd:cd05906 86 LAGFVPAPLTVPptydepnarlrKLRHIWQLLgsPVVltdaELVAEFAGLETLSGLPGI-RVLSIEELLDTAADHDLPQ- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1260 ldiddnpkrkyagiatVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLCASLKLACELYPSR---------HVAlcldpy 1330
Cdd:cd05906 164 ----------------SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDvflnwvpldHVG------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1331 cglGFVMWTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRVRDTFC-SYgvieLCTKaLSNSIPSLKQRNIDLRCVRt 1409
Cdd:cd05906 222 ---GLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWApNF----AFAL-LNDLLEEIEDGTWDLSSLR- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1410 CVVVAEERPRVQLTQQFCKLFQALGLNTRCVSTSFGCrvnpaicvqgassAESAQVYVDMRALRNNRValvergaPNSLC 1489
Cdd:cd05906 293 YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGM-------------TETCSGVIYSRSFPTYDH-------SQALE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1490 VIESGKLLPGVKVIIANPETKGhCGDSHLGEIWVQAPHNANGYFTiygdetdyNDHFNAKLVtgaTSELYARTGYLGFLR 1569
Cdd:cd05906 353 FVSLGRPIPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGYYN--------NPEANAEAF---TEDGWFRTGDLGFLD 420
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
438-1057 |
1.83e-15 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 82.10 E-value: 1.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 438 LSIPAGLprTLECALQRYGTNSFKSPMATVLD---PNGKVTTTLTYGKLLSRAQKIAHALstkifskgpEQVTlKPGDRV 514
Cdd:PRK12476 28 IALPPGT--TLISLIERNIANVGDTVAYRYLDhshSAAGCAVELTWTQLGVRLRAVGARL---------QQVA-GPGDRV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 515 ALVYPNNdpLSFITAWYGCMFRGLVPLPI---ELPLSSsdtppQQVGFLLSSCGITVALTSEAClkglpKSTTTGEIAKL 591
Cdd:PRK12476 96 AILAPQG--IDYVAGFFAAIKAGTIAVPLfapELPGHA-----ERLDTALRDAEPTVVLTTTAA-----AEAVEGFLRNL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 592 KGWPRLQWFVTEHLPKPPKE-FNVGNLRADDsaAAYIEYTTDKEGSVMGVTVT-RAA------MINHCRALTMACHYteg 663
Cdd:PRK12476 164 PRLRRPRVIAIDAIPDSAGEsFVPVELDTDD--VSHLQYTSGSTRPPVGVEIThRAVgtnlvqMILSIDLLDRNTHG--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 664 etiVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYALMKlRPSSWMQ-LITKHRASCCLVKSRDLHWGLLAT----KDHKD 738
Cdd:PRK12476 239 ---VSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVR-RPQRWIKaLSEGSRTGRVVTAAPNFAYEWAAQrglpAEGDD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 739 ISLSSLRMLLvadGANPWSLSSCDQFLSVFQAKGLRSDAICPCASSSE--VFTVSLrrpgrgscgfSPSATGRGV-LSMA 815
Cdd:PRK12476 315 IDLSNVVLII---GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEatLFVATI----------APDAEPSVVyLDRE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 816 ALSHG-VVRVDSEDSLTSLTLQdCGQVMPAAQMVVVRSEGPPVLcKTDQVGEICVTSGSTSASYFGLDGMTNSTF--KVQ 892
Cdd:PRK12476 382 QLGAGrAVRVAADAPNAVAHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFgaKLQ 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 893 PLLEELEQPkdGNGTVNIISKPIGE-DFYVRSGllgflgpgglVFVCGSRDGLMTVTGRKHNADDIIATVLAVEPMrfIY 971
Cdd:PRK12476 460 SRLAEGSHA--DGAADDGTWLRTGDlGVYLDGE----------LYITGRIADLIVIDGRNHYPQDIEATVAEASPM--VR 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 972 RGRIAVFSIKVLRDERVCVIAEQRPDCSEEESFQWMSRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRFL 1051
Cdd:PRK12476 526 RGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYL 605
|
....*.
gi 386770269 1052 EGSLHP 1057
Cdd:PRK12476 606 DGRLGV 611
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
475-889 |
3.15e-15 |
|
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: 80.72 E-value: 3.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 475 TTTLTYGKLLSRAQKIAHALStKIFskgpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPI-------ELPL 547
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLR-KLG--------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAAnpiytadELAH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 548 SSSDTPPQqvgFLLSS-CGITVALTSEACLKGLPKSTTTGeiAKLKGWPR----LQWFVTEHLPKPPKEFNVGnlrADDs 622
Cdd:cd05911 77 QLKISKPK---VIFTDpDGLEKVKEAAKELGPKDKIIVLD--DKPDGVLSiedlLSPTLGEEDEDLPPPLKDG---KDD- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 623 aAAYIEYTTDKEGSVMGVTVTRAAMINHCRALTMA--CHYTEGETIVCVLDFKREVGLWhSVLTSVLNGMHVIFIPyalm 700
Cdd:cd05911 148 -TAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFlyGNDGSNDVILGFLPLYHIYGLF-TTLASLLNGATVIIMP---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 701 KLRPSSWMQLITKHRASCCLVKSRDLHWgLLATKDHKDISLSSLRMLLVadGANPWSLSSCDQFLSVFQAKGLRSdaicp 780
Cdd:cd05911 222 KFDSELFLDLIEKYKITFLYLVPPIAAA-LAKSPLLDKYDLSSLRVILS--GGAPLSKELQELLAKRFPNATIKQ----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 781 casssevftvslrrpgrgSCGFSPSAtgrGVLSMAalshgvvrVDSEDSLTSltlqdCGQVMPAAQMVVVRSEGPPVLcK 860
Cdd:cd05911 294 ------------------GYGMTETG---GILTVN--------PDGDDKPGS-----VGRLLPNVEAKIVDDDGKDSL-G 338
|
410 420
....*....|....*....|....*....
gi 386770269 861 TDQVGEICVTSGSTSASYFGLDGMTNSTF 889
Cdd:cd05911 339 PNEPGEICVRGPQVMKGYYNNPEATKETF 367
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1149-1427 |
6.77e-15 |
|
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: 79.70 E-value: 6.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1149 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQnlnttlPTVRMIVDVSK 1228
Cdd:cd17651 20 RLTYAELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPA------ERLAFMLADAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1229 SGIVLSIQPIIKLLKSREAATSidPKTWPPILDIDDNPKRkyagiATVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLC 1308
Cdd:cd17651 93 PVLVLTHPALAGELAVELVAVT--LLDQPGAAAGADAEPD-----PALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1309 ASLKLACELYPSRHVALcldpYCGLGF--VMWTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRVRDTFCSYGVIElc 1386
Cdd:cd17651 166 AWQARASSLGPGARTLQ----FAGLGFdvSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR-- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 386770269 1387 tkALSNSIPSLKQRNIDLRcvrtCVVVAEERPRV-QLTQQFC 1427
Cdd:cd17651 240 --ALAEHGRPLGVRLAALR----YLLTGGEQLVLtEDLREFC 275
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
504-1055 |
1.08e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 79.39 E-value: 1.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 504 EQVTlKPGDRVALVYPNNdpLSFITAWYGCMFRGlvplPIELPLSSSDTPpQQVGFL---LSSCGITVALTSEAC----- 575
Cdd:PRK07769 73 QQVT-KPGDRVAILAPQN--LDYLIAFFGALYAG----RIAVPLFDPAEP-GHVGRLhavLDDCTPSAILTTTDSaegvr 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 576 --LKGLPKSTTTGEIAkLKGWPRLqwfVTEHLPKPPkefnvgnlrADDSAAAYIEYTTDKEGSVMGVTVT-RAAMINhcr 652
Cdd:PRK07769 145 kfFRARPAKERPRVIA-VDAVPDE---VGATWVPPE---------ANEDTIAYLQYTSGSTRIPAGVQIThLNLPTN--- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 653 ALTM--ACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYALMKlRPSSWMQLitkhrasccLVKSRDLHWGL 730
Cdd:PRK07769 209 VLQVidALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR-RPGRWIRE---------LARKPGGTGGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 731 LATK-----DH-------KD----ISLSSLRMLLvaDGANPWSLSSCDQFLSVFQAKGLRSDAICPCASSSE-VFTVSlr 793
Cdd:PRK07769 279 FSAApnfafEHaaarglpKDgeppLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEaTLFVS-- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 794 rpgrgSCGFSPSATGRGVLSMAALSHGVVRVDsEDSLTSLTLQDCGQVMPAAQMVVV----RSEGPpvlckTDQVGEICV 869
Cdd:PRK07769 355 -----TTPMDEEPTVIYVDRDELNAGRFVEVP-ADAPNAVAQVSAGKVGVSEWAVIVdpetASELP-----DGQIGEIWL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 870 TSGSTSASYFGLDGMTNSTFKvqplleeleqpkdgngtvNIISKPIGE---------DFYVRSGLLGFLGPGGlVFVCGS 940
Cdd:PRK07769 424 HGNNIGTGYWGKPEETAATFQ------------------NILKSRLSEshaegapddALWVRTGDYGVYFDGE-LYITGR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 941 RDGLMTVTGRKHNADDIIATvlAVEPMRFIYRGRIAVFSI-------KVLRD-------------ERVCVIAEQRPDCSE 1000
Cdd:PRK07769 485 VKDLVIIDGRNHYPQDLEYT--AQEATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHK 562
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 386770269 1001 EESFQWMSRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRFLEGSL 1055
Cdd:PRK07769 563 LDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1151-1398 |
2.38e-14 |
|
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: 77.31 E-value: 2.38e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1151 TCSELHKRAEKIAALLQERGRIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQnlnttlPTVRMIVDVSKSG 1230
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1231 IVLSIQPIIKLLksREAATSIDPKTWPPILDIDDNPKRKYAGIATVSfDSSAYLDF-SVSTcGRLSGVNITHRSLSSLCA 1309
Cdd:TIGR01733 75 LLLTDSALASRL--AGLVLPVILLDPLELAALDDAPAPPPPDAPSGP-DDLAYVIYtSGST-GRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1310 SLKLACELYPsRHVALCLDPYCGLGFVM---WTLigvYSGHHSILIAPYEVEANPSLWLSTLSQHRVRDTFCSYGVIELC 1386
Cdd:TIGR01733 151 WLARRYGLDP-DDRVLQFASLSFDASVEeifGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL 226
|
250
....*....|..
gi 386770269 1387 TKALSNSIPSLK 1398
Cdd:TIGR01733 227 AAALPPALASLR 238
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
444-1057 |
3.17e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 79.06 E-value: 3.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 444 LPRTLECALQRYGTNSFKSPMATVLDPNGKVTTTLTYGKLLSRAQKIAHALstkifskgpeQVTLKPGDRVALVYPNNDp 523
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL----------QARASFGDRAVLLFPSGP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 524 lSFITAWYGCMFRGLVPLPIELPLSSSDTPPQQVGFLLSSCGITVALTSEACLKGLPkstttgEIAKLKGWPRLQWFVTE 603
Cdd:PRK05691 76 -DYVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLL------QMEELAAANAPELLCVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 604 HL-PKPPKEFNVGNLRADDsaAAYIEYTTDKEGSVMGVTVTRA------AMINHCRALTMachyTEGETIVCVLDFKREV 676
Cdd:PRK05691 149 TLdPALAEAWQEPALQPDD--IAFLQYTSGSTALPKGVQVSHGnlvaneQLIRHGFGIDL----NPDDVIVSWLPLYHDM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 677 GLWHSVLTSVLNGMHVIFIPYALMKLRPSSWMQLITKHRASccLVKSRDLHWGLLatkdHKDISLSSLRML-----LVA- 750
Cdd:PRK05691 223 GLIGGLLQPIFSGVPCVLMSPAYFLERPLRWLEAISEYGGT--ISGGPDFAYRLC----SERVSESALERLdlsrwRVAy 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 751 DGANPWSLSSCDQFLSVFQAKGLRSDAICPCASSSE-VFTVSLRRPGRGscgfsPSATGrgvLSMAALSHGVVRVDSEDS 829
Cdd:PRK05691 297 SGSEPIRQDSLERFAEKFAACGFDPDSFFASYGLAEaTLFVSGGRRGQG-----IPALE---LDAEALARNRAEPGTGSV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 830 LTSltlqdCGQVMPAAQMVVVRSEGPPVLcKTDQVGEICVTSGSTSASYFGLDGMTNSTFkVQplleeleqpKDG----- 904
Cdd:PRK05691 369 LMS-----CGRSQPGHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF-VE---------HDGrtwlr 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 905 NGTVNIISKpiGEdfyvrsgllgflgpgglVFVCGSRDGLMTVTGRKHNADDIIATV-LAVEPMRfiyRGRIAVFSIKVL 983
Cdd:PRK05691 433 TGDLGFLRD--GE-----------------LFVTGRLKDMLIVRGHNLYPQDIEKTVeREVEVVR---KGRVAAFAVNHQ 490
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 386770269 984 RDERVCVIAE-----QRPDCSEEesfqWMSRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRFLEGSLHP 1057
Cdd:PRK05691 491 GEEGIGIAAEisrsvQKILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDS 565
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1145-1373 |
5.08e-14 |
|
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: 77.97 E-value: 5.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1145 AIA-----KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGA--IPitirpphpqnLNTTL 1217
Cdd:COG1020 492 AVAvvfgdQSLTYAELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAY 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1218 PTVR---MIVDvskSGIVLsiqpiikLLKSREAATSIdPKTWPPILDIDDNPKRKYAG---IATVSFDSSAYLDF-SVST 1290
Cdd:COG1020 561 PAERlayMLED---AGARL-------VLTQSALAARL-PELGVPVLALDALALAAEPAtnpPVPVTPDDLAYVIYtSGST 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1291 cGRLSGVNITHRSLSSLCASLKLACELYPSRHVALcldpYCGLGF------VMWTLIgvySGhHSILIAPYEVEANPSLW 1364
Cdd:COG1020 630 -GRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQ----FASLSFdasvweIFGALL---SG-ATLVLAPPEARRDPAAL 700
|
....*....
gi 386770269 1365 LSTLSQHRV 1373
Cdd:COG1020 701 AELLARHRV 709
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1148-1430 |
5.65e-13 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 73.33 E-value: 5.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1148 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQNLnttlptVRMIVDVS 1227
Cdd:cd05930 11 QSLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER------LAYILEDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1228 KSGIVLSiqpiikllksreaatsiDPktwppildiddnpkrkyagiatvsfDSSAYLDF-SVSTcGRLSGVNITHRSLSS 1306
Cdd:cd05930 84 GAKLVLT-----------------DP-------------------------DDLAYVIYtSGST-GKPKGVMVEHRGLVN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1307 LCASLKlacELYPSRH--VALCLDPYcglGFVM--WTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRVRDTFCSYGV 1382
Cdd:cd05930 121 LLLWMQ---EAYPLTPgdRVLQFTSF---SFDVsvWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSL 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 386770269 1383 IELCTKALSNSipslkqrniDLRCVRTcVVVAEERPRVQLTQQFCKLF 1430
Cdd:cd05930 195 LRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELL 232
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
477-890 |
1.83e-12 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 71.83 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 477 TLTYGKLLSRAQKIAHALstkifskgpEQVTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIElPLSssdtPPQQ 556
Cdd:cd05936 24 KLTYRELDALAEAFAAGL---------QNLGVQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLN-PLY----TPRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 557 VGFLLSSCGITVALTSEACLKGLPKSTTTGEIAKLKgwprlqwfvtehlpkppkefnvgnlrADDSAAayIEYTTdkegs 636
Cdd:cd05936 88 LEHILNDSGAKALIVAVSFTDLLAAGAPLGERVALT--------------------------PEDVAV--LQYTS----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 637 vmGVT-VTRAAMINH---------CRALtMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPyalmKLRPSS 706
Cdd:cd05936 135 --GTTgVPKGAMLTHrnlvanalqIKAW-LEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIP----RFRPIG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 707 WMQLITKHRASC-CLVKSrdLHWGLLATKDHKDISLSSLRmlLVADGANPWSLSSCDQFLSVFQAK-----GLrsdaicp 780
Cdd:cd05936 208 VLKEIRKHRVTIfPGVPT--MYIALLNAPEFKKRDFSSLR--LCISGGAPLPVEVAERFEELTGVPivegyGL------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 781 cassSEVftvslrrpgrgscgfSPSATGRgvlsmaaLSHGVVRVDSedsltsltlqdCGQVMPAAQMVVVRSEGPPVlcK 860
Cdd:cd05936 277 ----TET---------------SPVVAVN-------PLDGPRKPGS-----------IGIPLPGTEVKIVDDDGEEL--P 317
|
410 420 430
....*....|....*....|....*....|
gi 386770269 861 TDQVGEICVTSGSTSASYFGLDGMTNSTFK 890
Cdd:cd05936 318 PGEVGELWVRGPQVMKGYWNRPEETAEAFV 347
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1137-1533 |
7.62e-12 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 70.03 E-value: 7.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1137 FTLLNSKGAIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPItirpPHPqnlntt 1216
Cdd:PRK09192 37 MNFYDRRGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDGDFVEAFFACQYAGLVPV----PLP------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1217 LPTvrmivdvSKSGIVLSIQPIIKLLKSREAATSIDPKTWPPIL-DIDDNPKRKYAG--------------IATVSFDSS 1281
Cdd:PRK09192 106 LPM-------GFGGRESYIAQLRGMLASAQPAAIITPDELLPWVnEATHGNPLLHVLshawfkalpeadvaLPRPTPDDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1282 AYLDFSvSTCGRL-SGVNITHRSL-SSLCASLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYEVEA 1359
Cdd:PRK09192 179 AYLQYS-SGSTRFpRGVIITHRALmANLRAISHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFAR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1360 NPSLWLSTLSQHRVRDTFC-SYGvIELCT-KALSNSIPSLkqrniDLRCVRTCVVVAEE-RPRVqlTQQFCKLFQALGLN 1436
Cdd:PRK09192 258 RPLQWLDLISRNRGTISYSpPFG-YELCArRVNSKDLAEL-----DLSCWRVAGIGADMiRPDV--LHQFAEAFAPAGFD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1437 TRCVSTSFGCRVNpAICVQGASSAESAQV-YVDMRALRNNRVAL--VERGAPNSLCVIeSGKLLPGVKVIIANPETKGhC 1513
Cdd:PRK09192 330 DKAFMPSYGLAEA-TLAVSFSPLGSGIVVeEVDRDRLEYQGKAVapGAETRRVRTFVN-CGKALPGHEIEIRNEAGMP-L 406
|
410 420
....*....|....*....|
gi 386770269 1514 GDSHLGEIWVQAPHNANGYF 1533
Cdd:PRK09192 407 PERVVGHICVRGPSLMSGYF 426
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1128-1533 |
1.89e-11 |
|
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: 68.36 E-value: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1128 ANTSPDHIIFTLLNskgaiaKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPItirp 1207
Cdd:cd05936 9 ARRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAGAVVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1208 phpqNLNT--TLPTVRMIVDVSKSGIVLSIQPIIKLLKSREaatsidPKTWPPILDIDDnpkrkyagIATVSFDSsayld 1285
Cdd:cd05936 78 ----PLNPlyTPRELEHILNDSGAKALIVAVSFTDLLAAGA------PLGERVALTPED--------VAVLQYTS----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1286 fsvSTCGRLSGVNITHRSLSS-LCASLKLACELYPSRHVALCLDPY---CGLGFVMwtLIGVYSGHHSILIAPYEveanP 1361
Cdd:cd05936 135 ---GTTGVPKGAMLTHRNLVAnALQIKAWLEDLLEGDDVVLAALPLfhvFGLTVAL--LLPLALGATIVLIPRFR----P 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1362 SLWLSTLSQHRVrDTFCsyGVIELCTkALSNSiPSLKQRniDLRCVRTCV-------VVAEERPRvQLTQqfCKLFQALG 1434
Cdd:cd05936 206 IGVLKEIRKHRV-TIFP--GVPTMYI-ALLNA-PEFKKR--DFSSLRLCIsggaplpVEVAERFE-ELTG--VPIVEGYG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1435 LnTRCVstsfgcrvnPAICVqgassaesaqvyvdmralrnNRVALVERgaPNSLcviesGKLLPGVKVIIANPETKgHCG 1514
Cdd:cd05936 276 L-TETS---------PVVAV--------------------NPLDGPRK--PGSI-----GIPLPGTEVKIVDDDGE-ELP 317
|
410
....*....|....*....
gi 386770269 1515 DSHLGEIWVQAPHNANGYF 1533
Cdd:cd05936 318 PGEVGELWVRGPQVMKGYW 336
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
444-889 |
1.90e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 68.67 E-value: 1.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 444 LPRTLECALQRYGTnsfkspmATVLDPNGKVTTtltYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNDp 523
Cdd:PRK06187 8 IGRILRHGARKHPD-------KEAVYFDGRRTT---YAELDERVNRLANALR----ALG-----VKKGDRVAVFDWNSH- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 524 lSFITAWYGCMFRGLVPLPIELPLSssdtpPQQVGFLLSSCGITVALTSeaclkglpkSTTTGEIAKLKgwPRLQ----W 599
Cdd:PRK06187 68 -EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEDRVVLVD---------SEFVPLLAAIL--PQLPtvrtV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 600 FVTEHLPKPPKEFNVGN---LRAD------------DSAAAYIeYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGE 664
Cdd:PRK06187 131 IVEGDGPAAPLAPEVGEyeeLLAAasdtfdfpdideNDAAAML-YTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 665 T-IVCVLDFkrEVGLWHSVLTSVLNGM-HVI---FIPYALMKlrpsswmqLITKHRASCclvksrdLH-----W-GLLAT 733
Cdd:PRK06187 210 VyLVIVPMF--HVHAWGLPYLALMAGAkQVIprrFDPENLLD--------LIETERVTF-------FFavptiWqMLLKA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 734 KDHKDISLSSLRMLLVadGANPWSLSSCDQFLSVF-----QAKGLrsdaicpcassSEvftvslrrpgrgscgfspsaTG 808
Cdd:PRK06187 273 PRAYFVDFSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGM-----------TE--------------------TS 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 809 rGVLSMAALSHGVVRVDSEDSLTsltlqdcGQVMPAAQMVVVRSEGPPVLCKTDQVGEICVTSGSTSASYFGLDGMTNST 888
Cdd:PRK06187 320 -PVVSVLPPEDQLPGQWTKRRSA-------GRPLPGVEARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAET 391
|
.
gi 386770269 889 F 889
Cdd:PRK06187 392 I 392
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1149-1311 |
1.92e-11 |
|
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: 68.47 E-value: 1.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1149 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPqnlnttLPTVRMIVDVSK 1228
Cdd:cd12116 12 SLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1229 SGIVLSIQPIIKLLksreaatsidPKTWPPILDIDDNPKRKYAGI-ATVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSL 1307
Cdd:cd12116 85 PALVLTDDALPDRL----------PAGLPVLLLALAAAAAAPAAPrTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
....
gi 386770269 1308 CASL 1311
Cdd:cd12116 155 LHSM 158
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1149-1373 |
2.55e-10 |
|
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: 64.98 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1149 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAI--PITIRPPhPQNLNTTLPTVRMIVDV 1226
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAAyvPVDIDQP-AARREAILADAGARLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1227 SKSGIVLSIQPIIKLLKSREAATSidpkTWPPILDIDDNPkrkyagiatvsfDSSAYLDF-SVSTcGRLSGVNITHRSLS 1305
Cdd:cd12114 90 TDGPDAQLDVAVFDVLILDLDALA----APAPPPPVDVAP------------DDLAYVIFtSGST-GTPKGVMISHRAAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1306 SLCASLKLACELYPSRHVaLCLDPycgLGFVM--WTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRV 1373
Cdd:cd12114 153 NTILDINRRFAVGPDDRV-LALSS---LSFDLsvYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGV 218
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1124-1532 |
1.08e-09 |
|
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: 62.63 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1124 LRWRANTSPDHIIFTLLNSkgaiakTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIpi 1203
Cdd:cd17631 1 LRRRARRHPDRTALVFGGR------SLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1204 tirpPHPQNLNTTLPTVRMIVDVSKsgivlsiqpiikllksreaatsidpktwppildiddnpkrkyagiATVSFDSSAY 1283
Cdd:cd17631 72 ----FVPLNFRLTPPEVAYILADSG---------------------------------------------AKVLFDDLAL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1284 LDFSVSTCGRLSGVNITHRSLSSLCASLKLACELyPSRHVALCLDPYC---GLGfvMWTLIGVYSGHHSILIAPYEVEAn 1360
Cdd:cd17631 103 LMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFhigGLG--VFTLPTLLRGGTVVILRKFDPET- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1361 pslWLSTLSQHRVRDTFCSYGVIElctkALSNSiPSLKQRniDLRCVRtCVVVAEERPRVQLTQQF----CKLFQALGLn 1436
Cdd:cd17631 179 ---VLDLIERHRVTSFFLVPTMIQ----ALLQH-PRFATT--DLSSLR-AVIYGGAPMPERLLRALqargVKFVQGYGM- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1437 TRCVstsfgcrvnPAICVQGASSAE----SAqvyvdmralrnnrvalvergapnslcviesGKLLPGVKVIIANPETKgH 1512
Cdd:cd17631 247 TETS---------PGVTFLSPEDHRrklgSA------------------------------GRPVFFVEVRIVDPDGR-E 286
|
410 420
....*....|....*....|
gi 386770269 1513 CGDSHLGEIWVQAPHNANGY 1532
Cdd:cd17631 287 VPPGEVGEIVVRGPHVMAGY 306
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
476-750 |
1.14e-09 |
|
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: 63.72 E-value: 1.14e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 476 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIELplsssDTPPQ 555
Cdd:COG1020 500 QSLTYAELNARANRLAHHLR----ALG-----VGPGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLDP-----AYPAE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 556 QVGFLLSSCGITVALTSEACLKGLPKSTTTgeiaklkgWPRLQwfvTEHLPKPPKEFNVGNLRADDsaAAYIEYT----- 630
Cdd:COG1020 564 RLAYMLEDAGARLVLTQSALAARLPELGVP--------VLALD---ALALAAEPATNPPVPVTPDD--LAYVIYTsgstg 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 631 TDKegsvmGVTVTRAAMINHCRALTMACHYTEGETI---------VCVLDFkrevglwhsvLTSVLNGMHVIFIPYALMk 701
Cdd:COG1020 631 RPK-----GVMVEHRALVNLLAWMQRRYGLGPGDRVlqfaslsfdASVWEI----------FGALLSGATLVLAPPEAR- 694
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 386770269 702 LRPSSWMQLITKHRASC-CLVKSrdlHWGLLAtkDHKDISLSSLRMLLVA 750
Cdd:COG1020 695 RDPAALAELLARHRVTVlNLTPS---LLRALL--DAAPEALPSLRLVLVG 739
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
479-750 |
1.21e-09 |
|
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: 62.67 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 479 TYGKLLSRAQKIAHALStkifskgpEQVTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIElplssSDTPPQQVG 558
Cdd:TIGR01733 1 TYRELDERANRLARHLR--------AAGGVGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLD-----PAYPAERLA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 559 FLLSSCGITVALTSEACLKGLPKSTTTGEIaklkgWPRLQWFVTEHLPKPPkefnVGNLRADDSAAAYIEYTTDKEGSVM 638
Cdd:TIGR01733 66 FILEDAGARLLLTDSALASRLAGLVLPVIL-----LDPLELAALDDAPAPP----PPDAPSGPDDLAYVIYTSGSTGRPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 639 GVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWhSVLTSVLNGMHVIFIPYALMKLRPSSWMQLITKHRASC 718
Cdd:TIGR01733 137 GVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTV 215
|
250 260 270
....*....|....*....|....*....|...
gi 386770269 719 -CLVKSrdlHWGLLAtkDHKDISLSSLRMLLVA 750
Cdd:TIGR01733 216 lNLTPS---LLALLA--AALPPALASLRLVILG 243
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
441-773 |
2.04e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 63.05 E-value: 2.04e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 441 PAGLPRTLECAlQRYGTNSFKSPMATVLDPNGKVtttLTYGKLLSRAQKIAHALSTKifSKGPEQvtlkpgdRVALVYPN 520
Cdd:PRK12316 1996 PEAYPRGPGVH-QRIAEQAARAPEAIAVVFGDQH---LSYAELDSRANRLAHRLRAR--GVGPEV-------RVAIAAER 2062
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 521 NDPLsfITAWYGCMFRG--LVPLPIELPlsssdtpPQQVGFLLSSCGITVALTSEACLKGLPKSTttgeiaklkGWPRLQ 598
Cdd:PRK12316 2063 SFEL--VVALLAVLKAGgaYVPLDPNYP-------AERLAYMLEDSGAALLLTQRHLLERLPLPA---------GVARLP 2124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 599 WFVTEHLPKPPKEFNVGNLRADDsaAAYIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGL 678
Cdd:PRK12316 2125 LDRDAEWADYPDTAPAVQLAGEN--LAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAH 2202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 679 WhSVLTSVLNGMHVIfipyalmkLRPSS-WM--QLI-TKHRASCCLVKSRDLHWGLLATKDHKDISLSSLRMLLVadGAN 754
Cdd:PRK12316 2203 E-QWFHPLLNGARVL--------IRDDElWDpeQLYdEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCF--GGE 2271
|
330
....*....|....*....
gi 386770269 755 PWSLSSCDQFLSVFQAKGL 773
Cdd:PRK12316 2272 AVPAASLRLAWEALRPVYL 2290
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
476-890 |
3.43e-09 |
|
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: 61.09 E-value: 3.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 476 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNDplSFITAWYGCMFRGLVPLPIELPLSssdtpPQ 555
Cdd:cd17631 19 RSLTYAELDERVNRLAHALR----ALG-----VAKGDRVAVLSKNSP--EFLELLFAAARLGAVFVPLNFRLT-----PP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 556 QVGFLLSSCGITVALTSEACLkgLPKSTTTGeiaklkgwprlqwfvtehLPKppkefnvgnlraddsaaayieyttdkeg 635
Cdd:cd17631 83 EVAYILADSGAKVLFDDLALL--MYTSGTTG------------------RPK---------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 636 svmGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPyalmKLRPSSWMQLITKHR 715
Cdd:cd17631 115 ---GAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILR----KFDPETVLDLIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 716 A-SCCLVKSrdLHWGLLATKDHKDISLSSLRMLLVADGANPWSLsscdqfLSVFQAKGLRsdaicpcasssevFtvslrr 794
Cdd:cd17631 188 VtSFFLVPT--MIQALLQHPRFATTDLSSLRAVIYGGAPMPERL------LRALQARGVK-------------F------ 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 795 pgrgscgfspsATGRGvlsMAALSHGVVRVDSEDSLTslTLQDCGQVMPAAQMVVVRSEGPPVlcKTDQVGEICVTSGST 874
Cdd:cd17631 241 -----------VQGYG---MTETSPGVTFLSPEDHRR--KLGSAGRPVFFVEVRIVDPDGREV--PPGEVGEIVVRGPHV 302
|
410
....*....|....*.
gi 386770269 875 SASYFGLDGMTNSTFK 890
Cdd:cd17631 303 MAGYWNRPEATAAAFR 318
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1144-1533 |
3.70e-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: 61.48 E-value: 3.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1144 GAIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPphpqnlnttLPTVRMI 1223
Cdd:cd05904 27 AATGRALTYAELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP---------LSTPAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1224 ---VDVSKSGIVLSIQPIIKLLKSREAATSI--DPKT-----WPPILDIDDNPKRKyagiATVSFDSSAYLDFSVSTCGR 1293
Cdd:cd05904 97 akqVKDSGAKLAFTTAELAEKLASLALPVVLldSAEFdslsfSDLLFEADEAEPPV----VVIKQDDVAALLYSSGTTGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1294 LSGVNITHRSLSSLCASLKLACELYPSRH-VALCLDPYCGL-GFVMWTLIGVYSGHHSILIAPYEVEAnpslWLSTLSQH 1371
Cdd:cd05904 173 SKGVMLTHRNLIAMVAQFVAGEGSNSDSEdVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1372 RVRDTFCSYGVIelctKALSNSiPSLKQRniDLRCVRTCVVVAEERPRvQLTQQF------CKLFQALGLNTRCvstsfg 1445
Cdd:cd05904 249 KVTHLPVVPPIV----LALVKS-PIVDKY--DLSSLRQIMSGAAPLGK-ELIEAFrakfpnVDLGQGYGMTEST------ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1446 crvnpAICVQGASSAESaqvyvdmralrnnrvalveRGAPNSlcvieSGKLLPGVKVIIANPETKGHCGDSHLGEIWVQA 1525
Cdd:cd05904 315 -----GVVAMCFAPEKD-------------------RAKYGS-----VGRLVPNVEAKIVDPETGESLPPNQTGELWIRG 365
|
....*...
gi 386770269 1526 PHNANGYF 1533
Cdd:cd05904 366 PSIMKGYL 373
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
619-1050 |
5.38e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 60.78 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 619 ADDSAAAYIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYT-EGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPY 697
Cdd:PRK07768 149 TGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 698 ALMKLRPSSWMQLITKHRASC--------CLVKSRdlhwgLLATKDHKDISLSSLRMLLvaDGANPWSLSSCDQFLSVFQ 769
Cdd:PRK07768 229 MDFLRDPLLWAELISKYRGTMtaapnfayALLARR-----LRRQAKPGAFDLSSLRFAL--NGAEPIDPADVEDLLDAGA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 770 AKGLRSDAICPCASSSEV-FTVSLRRPGRG--SCGFSP---SATGRGVLSmaalSHGVVRvdsedSLTSLtlqdcGQVMP 843
Cdd:PRK07768 302 RFGLRPEAILPAYGMAEAtLAVSFSPCGAGlvVDEVDAdllAALRRAVPA----TKGNTR-----RLATL-----GPPLP 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 844 AAQMVVVRSEGPPvlCKTDQVGEICVTSGSTSASYFGLDGMTnstfkvqPLLEEleqpkDG---NGTVNIISKPiGEdfy 920
Cdd:PRK07768 368 GLEVRVVDEDGQV--LPPRGVGVIELRGESVTPGYLTMDGFI-------PAQDA-----DGwldTGDLGYLTEE-GE--- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 921 vrsgllgflgpgglVFVCGSRDGLMTVTGRKHNADDIIATVLAVEPMRfiyRGRIAVFSIKV-LRDERVCVIAEQRPDCS 999
Cdd:PRK07768 430 --------------VVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVR---PGNAVAVRLDAgHSREGFAVAVESNAFED 492
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 386770269 1000 EEESFQWMSRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRF 1050
Cdd:PRK07768 493 PAEVRRIRHQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRRANAAELV 543
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1148-1306 |
7.23e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 60.40 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1148 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPH-PQNL------------- 1213
Cdd:PRK05605 56 ATTTYAELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYtAHELehpfedhgarvai 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1214 --NTTLPTVRMIVDVSKSGIVLSIQ---------------PIIKLLKSREAATSIDPKT--WPPILDIDDNPKRKYAGIA 1274
Cdd:PRK05605 135 vwDKVAPTVERLRRTTPLETIVSVNmiaampllqrlalrlPIPALRKARAALTGPAPGTvpWETLVDAAIGGDGSDVSHP 214
|
170 180 190
....*....|....*....|....*....|..
gi 386770269 1275 TVSFDSSAYLDFSVSTCGRLSGVNITHRSLSS 1306
Cdd:PRK05605 215 RPTPDDVALILYTSGTTGKPKGAQLTHRNLFA 246
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
439-753 |
7.86e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 60.30 E-value: 7.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 439 SIPAGLPRTLECALQRYGTNSfkspmATVLDPngkvtTTLTYGKLLSRAQKIAHALstkifskgpEQVTLKPGDRVALVY 518
Cdd:PRK07656 2 NEWMTLPELLARAARRFGDKE-----AYVFGD-----QRLTYAELNARVRRAAAAL---------AALGIGKGDRVAIWA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 519 PNNdpLSFITAWYGCMFRG--LVPL-----PIELP--LSSSDTPPQQV--GFLLSSCGITVALTSEACLKGLPKSTTTGE 587
Cdd:PRK07656 63 PNS--PHWVIAALGALKAGavVVPLntrytADEAAyiLARGDAKALFVlgLFLGVDYSATTRLPALEHVVICETEEDDPH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 588 IAKLKGWPRLqwfvtehLPKPPKEFNVGNLRADDSAAayIEYTTDKEGSVMGVtvtraaMINHCRALTMA---CHY---T 661
Cdd:PRK07656 141 TEKMKTFTDF-------LAAGDPAERAPEVDPDDVAD--ILFTSGTTGRPKGA------MLTHRQLLSNAadwAEYlglT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 662 EGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPyalmKLRPSSWMQLITKHRAScCLVKSRDLHWGLLATKDHKDISL 741
Cdd:PRK07656 206 EGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP----VFDPDEVFRLIETERIT-VLPGPPTMYNSLLQHPDRSAEDL 280
|
330
....*....|..
gi 386770269 742 SSLRmLLVADGA 753
Cdd:PRK07656 281 SSLR-LAVTGAA 291
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
479-719 |
1.16e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 59.61 E-value: 1.16e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 479 TYGKLLSRAQKIAHALSTKifskgpeqvTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIELPLSSSDTPPQqvg 558
Cdd:cd05934 5 TYAELLRESARIAAALAAL---------GIRPGDRVALMLDNC--PEFLFAWFALAKLGAVLVPINTALRGDELAYI--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 559 flLSSCGITVALTSEACLkgLPKSTTTGeiaklkgwprlqwfvtehlpkPPKefnvgnlraddsaaayieyttdkegsvm 638
Cdd:cd05934 71 --IDHSGAQLVVVDPASI--LYTSGTTG---------------------PPK---------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 639 GVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPyalmKLRPSSWMQLITKHRASC 718
Cdd:cd05934 98 GVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP----RFSASRFWSDVRRYGATV 173
|
.
gi 386770269 719 C 719
Cdd:cd05934 174 T 174
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
508-772 |
1.23e-08 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 59.38 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 508 LKPGDRVALVYPNNDP---LSFITAWYGCMfRGLVPLPIelplsSSDTPPQQVGFLLSSCGITVALTSEACL----KGLP 580
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGR-LGLVFVPL-----NPTLKESVLRYLVADAGGRIVLADAGAAdrlrDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 581 KSTTTGEIAKLKGWPRLQWFVTEHLPKPPkefnvgnlradDSAAayIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHY 660
Cdd:cd05922 89 ASPDPGTVLDADGIRAARASAPAHEVSHE-----------DLAL--LLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 661 TEGETIVCVLDFKREVGLwhSVL-TSVLNGMHVIFIPYALMklrPSSWMQLITKHRA-SCCLVKSrdlHWGLLATKDHKD 738
Cdd:cd05922 156 TADDRALTVLPLSYDYGL--SVLnTHLLRGATLVLTNDGVL---DDAFWEDLREHGAtGLAGVPS---TYAMLTRLGFDP 227
|
250 260 270
....*....|....*....|....*....|....
gi 386770269 739 ISLSSLRMLLVADGANPwslsscDQFLSVFQAKG 772
Cdd:cd05922 228 AKLPSLRYLTQAGGRLP------QETIARLRELL 255
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1148-1533 |
1.46e-08 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 59.01 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1148 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPP-HPQNLnttlptVRMIVDV 1226
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLlHPDDY------AYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1227 SKSGIVlsiqpiikllksreaatsidpktwppildiddnpkrkyagiatVSFDSSAYLDFSVSTCGRLSGVNITHRSLSs 1306
Cdd:cd05919 82 EARLVV-------------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPL- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1307 lcaslkLACELYPSRhvALCLDP----YC--------GLGFVMWtlIGVYSGHHSILIAPYEVeanPSLWLSTLSQHRVR 1374
Cdd:cd05919 118 ------LFADAMARE--ALGLTPgdrvFSsakmffgyGLGNSLW--FPLAVGASAVLNPGWPT---AERVLATLARFRPT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1375 dtfCSYGVIELctkaLSNSIPSLKQRNIDLRCVRTCVVVAEERPRvqltqqfcKLFQALglntrcvSTSFGCRVnpaicV 1454
Cdd:cd05919 185 ---VLYGVPTF----YANLLDSCAGSPDALRSLRLCVSAGEALPR--------GLGERW-------MEHFGGPI-----L 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1455 QGASSAESAQVYVdmralrNNRVALVERGApnslcvieSGKLLPGVKVIIANPEtkGH-CGDSHLGEIWVQAPHNANGYF 1533
Cdd:cd05919 238 DGIGATEVGHIFL------SNRPGAWRLGS--------TGRPVPGYEIRLVDEE--GHtIPPGEEGDLLVRGPSAAVGYW 301
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1127-1308 |
1.58e-08 |
|
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: 59.14 E-value: 1.58e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1127 RANTSPDHIiftllnskgAI---AKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPI 1203
Cdd:cd12117 6 QAARTPDAV---------AVvygDRSLTYAELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1204 TIRPPHPQNlnttlptvRMIVDVSKSGIVLsiqpiikLLKSREAATSIDPKTWPPILDIDDNPKRKYAGIATVSFDSSAY 1283
Cdd:cd12117 76 PLDPELPAE--------RLAFMLADAGAKV-------LLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAY 140
|
170 180
....*....|....*....|....*
gi 386770269 1284 LDFSVSTCGRLSGVNITHRSLSSLC 1308
Cdd:cd12117 141 VMYTSGSTGRPKGVAVTHRGVVRLV 165
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1132-1572 |
4.54e-08 |
|
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: 57.88 E-value: 4.54e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1132 PDHIIFTLLNSKgaiAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIR----P 1207
Cdd:cd05908 1 PEGIIFILGDKK---EKFVSYRHLREEALGYLGALQELG-IKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSigsnE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1208 PHPQNLNTtlptvrmivdvsksgivlsiqpIIKLLKSreaatsidpktwpPILDIDDNPKRKYAgiatvsfDSSAYLDFS 1287
Cdd:cd05908 77 EHKLKLNK----------------------VWNTLKN-------------PYLITEEEVLCELA-------DELAFIQFS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1288 VSTCGRLSGVNITHRSLSSLCASLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYEVEANPSLWLST 1367
Cdd:cd05908 115 SGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKK 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1368 LSQHRVRDTFC-SYGvielcTKALSNSIPSLKQRNIDLRCVRTCVVVAEerP-RVQLTQQFCKLFQALGLNTRCVSTSFG 1445
Cdd:cd05908 195 ASEHKATIVSSpNFG-----YKYFLKTLKPEKANDWDLSSIRMILNGAE--PiDYELCHEFLDHMSKYGLKRNAILPVYG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1446 CRVNPAicvqGASSAESAQ----VYVDMRALRNN-RVALVERGAPNSLCVIESGKLLPGVKVIIANPETKGhCGDSHLGE 1520
Cdd:cd05908 268 LAEASV----GASLPKAQSpfktITLGRRHVTHGePEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LPDGYIGH 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 386770269 1521 IWVQAPHNANGYFTiygdetdyNDHFNAKLVtgaTSELYARTGYLGFLRRTE 1572
Cdd:cd05908 343 IQIRGKNVTPGYYN--------NPEATAKVF---TDDGWLKTGDLGFIRNGR 383
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1116-1306 |
5.17e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 57.61 E-value: 5.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1116 KPQLITGVLRWRANTSPDHIiftllnskgAIA---KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAF 1192
Cdd:PRK07656 3 EWMTLPELLARAARRFGDKE---------AYVfgdQRLTYAELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1193 YGCLYLGAIPItirPphpqnLNTTLPT-----------VRMI--------VDVSKSGIVLSIQPIIKLLKSREAATSIDP 1253
Cdd:PRK07656 73 LGALKAGAVVV---P-----LNTRYTAdeaayilargdAKALfvlglflgVDYSATTRLPALEHVVICETEEDDPHTEKM 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 386770269 1254 KTWPPILDIDDNPKRKyagiATVSFDSSAYLDFSVSTCGRLSGVNITHRSLSS 1306
Cdd:PRK07656 145 KTFTDFLAAGDPAERA----PEVDPDDVADILFTSGTTGRPKGAMLTHRQLLS 193
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1127-1490 |
9.44e-08 |
|
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: 56.57 E-value: 9.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1127 RANTSPDHIiftllnskgAIA---KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPI 1203
Cdd:cd17655 6 QAEKTPDHT---------AVVfedQTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGAYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1204 TIRPPHPQNlnttlpTVRMIVDVSKSGIVLSIQPIIKLLKSREAATSIDPKTWPPILDIDDNPKRKyagiatvsFDSSAY 1283
Cdd:cd17655 76 PIDPDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSK--------SDDLAY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1284 LDFSVSTCGRLSGVNITHRSLSSLCASLKLACELYPSRHVALcLDPYCGLGFVMWTLIGVYSGhHSILIAPYEVEANPSL 1363
Cdd:cd17655 142 VIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVAL-FASISFDASVTEIFASLLSG-NTLYIVRKETVLDGQA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1364 WLSTLSQHRVRDTFCSYGVIELCTKALSNSIPSLKQrnidlrcvrtcVVVAEERPRVQLTQQFCKLFQAlglnTRCVSTS 1443
Cdd:cd17655 220 LTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKH-----------LIVGGEALSTELAKKIIELFGT----NPTITNA 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1444 FGcrvnPAICVQGAS-----SAESAQVYVDM-RALRNNRVALVER-------GAPNSLCV 1490
Cdd:cd17655 285 YG----PTETTVDASiyqyePETDQQVSVPIgKPLGNTRIYILDQygrpqpvGVAGELYI 340
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1147-1373 |
1.33e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.27 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1147 AKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQNlnttlPTVRMIVDv 1226
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALIARG-VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE-----RLAYMMED- 4646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1227 SKSGIVLSIQPIIKLLKSREAATSIDpktwppiLDIDD--------NPKRKYAGiatvsfDSSAYLDFSVSTCGRLSGVN 1298
Cdd:PRK12316 4647 SGAALLLTQSHLLQRLPIPDGLASLA-------LDRDEdwegfpahDPAVRLHP------DNLAYVIYTSGSTGRPKGVA 4713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1299 ITHRSLSSLCASLKLACELYPSRHVaLCLDPYCGLGFVmWTLIGVYSGHHSILIAPyeveanPSLWLS-----TLSQHRV 1373
Cdd:PRK12316 4714 VSHGSLVNHLHATGERYELTPDDRV-LQFMSFSFDGSH-EGLYHPLINGASVVIRD------DSLWDPerlyaEIHEHRV 4785
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1120-1205 |
1.35e-07 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 56.26 E-value: 1.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1120 ITGVLRWRANTSPDHiifTLLNSK-GAIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYL 1198
Cdd:COG1022 13 LPDLLRRRAARFPDR---VALREKeDGIWQSLTWAEFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAA 88
|
....*..
gi 386770269 1199 GAIPITI 1205
Cdd:COG1022 89 GAVTVPI 95
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1149-1373 |
1.93e-07 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 55.78 E-value: 1.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1149 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQNlnttlptvRMIVDVSK 1228
Cdd:cd17643 12 RLTYGELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE--------RIAFILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1229 SGIVLsiqpiikllksreaatsidpktwppILDIDDNPkrkyagiatvsfdssAYLDFSVSTCGRLSGVNITHRSLSSLC 1308
Cdd:cd17643 83 SGPSL-------------------------LLTDPDDL---------------AYVIYTSGSTGRPKGVVVSHANVLALF 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 386770269 1309 ASLKLACELYPSRHVALCldPYCGLGFVMWTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRV 1373
Cdd:cd17643 123 AATQRWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGV 185
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1120-1209 |
1.99e-07 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 55.92 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1120 ITGVLRWRANTSPDHIiftllnskgAI---AKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCL 1196
Cdd:COG1021 27 LGDLLRRRAERHPDRI---------AVvdgERRLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALF 96
|
90
....*....|...
gi 386770269 1197 YLGAIPITIRPPH 1209
Cdd:COG1021 97 RAGAIPVFALPAH 109
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
475-716 |
2.39e-07 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL 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. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 55.40 E-value: 2.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 475 TTTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIelplsSSDTPP 554
Cdd:cd05926 12 TPALTYADLAELVDDLARQLA----ALG-----IKKGDRVAIALPNG--LEFVVAFLAAARAGAVVAPL-----NPAYKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 555 QQVGFLLSSCGITVALTSE----ACLKGLPKST-TTGEIAKLKGWPRLQWFVTE---HLPKPPKEFNVGNLRADDSaaAY 626
Cdd:cd05926 76 AEFEFYLADLGSKLVLTPKgelgPASRAASKLGlAILELALDVGVLIRAPSAESlsnLLADKKNAKSEGVPLPDDL--AL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 627 IEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIfIPyalMKLRPSS 706
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVV-LP---PRFSAST 229
|
250
....*....|
gi 386770269 707 WMQLITKHRA 716
Cdd:cd05926 230 FWPDVRDYNA 239
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
475-750 |
3.26e-07 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 55.12 E-value: 3.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 475 TTTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIelplsSSDTPP 554
Cdd:COG0365 37 ERTLTYAELRREVNRFANALR----ALG-----VKKGDRVAIYLPNI--PEAVIAMLACARIGAVHSPV-----FPGFGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 555 QQVGFLLSSCGITVALTS----------------EACLKGLPKSTT------TGEIAKLKGWprlQWFvTEHLPKPPKEF 612
Cdd:COG0365 101 EALADRIEDAEAKVLITAdgglrggkvidlkekvDEALEELPSLEHvivvgrTGADVPMEGD---LDW-DELLAAASAEF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 613 NVGNLRADDsaAAYIEYTtdkegSvmGVT--------VTRAAMINHcrALTMACHY--TEGETIVCVLDFKREVGLWHSV 682
Cdd:COG0365 177 EPEPTDADD--PLFILYT-----S--GTTgkpkgvvhTHGGYLVHA--ATTAKYVLdlKPGDVFWCTADIGWATGHSYIV 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 386770269 683 LTSVLNGMHVIFIPYALMKLRPSSWMQLITKHRASCC---------LVKsrdlhWGLLATKDHkdiSLSSLRMLLVA 750
Cdd:COG0365 246 YGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFftaptairaLMK-----AGDEPLKKY---DLSSLRLLGSA 314
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1124-1207 |
3.47e-07 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 54.90 E-value: 3.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1124 LRWRANTSPDHIIFTLLNSKGA----IAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLG 1199
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPGGRGAdgklAYDELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
....*...
gi 386770269 1200 AIPITIRP 1207
Cdd:PRK09274 91 AVPVLVDP 98
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1148-1306 |
6.35e-07 |
|
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: 53.79 E-value: 6.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1148 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGA--IPITIRPPHPQnlnttlptVRMIVD 1225
Cdd:cd05945 15 RTLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDASSPAER--------IREILD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1226 VSKSGIVLSiqpiikllksreaatsidpktwppilDIDDNpkrkyagiatvsfdssAYLDFSVSTCGRLSGVNITHRSLS 1305
Cdd:cd05945 86 AAKPALLIA--------------------------DGDDN----------------AYIIFTSGSTGRPKGVQISHDNLV 123
|
.
gi 386770269 1306 S 1306
Cdd:cd05945 124 S 124
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1151-1207 |
1.12e-06 |
|
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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 53.06 E-value: 1.12e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 386770269 1151 TCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRP 1207
Cdd:cd05934 5 TYAELLRESARIAAALAALG-IRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT 60
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1148-1203 |
1.77e-06 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 52.81 E-value: 1.77e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 386770269 1148 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPI 1203
Cdd:COG0365 38 RTLTYAELRREVNRFANALRALG-VKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
464-576 |
4.16e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 51.44 E-value: 4.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 464 MATVLDPNGkvtTTLTYGKLLSRAQKIAHALstkifskgpEQVTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPI 543
Cdd:PRK08276 1 PAVIMAPSG---EVVTYGELEARSNRLAHGL---------RALGLREGDVVAILLENN--PEFFEVYWAARRSGLYYTPI 66
|
90 100 110
....*....|....*....|....*....|...
gi 386770269 544 ELPLsssdTPPqQVGFLLSSCGITVALTSEACL 576
Cdd:PRK08276 67 NWHL----TAA-EIAYIVDDSGAKVLIVSAALA 94
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
476-758 |
5.87e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.50 E-value: 5.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 476 TTLTYGKLLSRAQKIAHALstkifskgpEQVTLKPGDRVALVYPNNDplSFITAWYGCMFRGLVPLPIElplssSDTPPQ 555
Cdd:PRK12316 535 ETLDYAELNRRANRLAHAL---------IERGVGPDVLVGVAMERSI--EMVVALLAILKAGGAYVPLD-----PEYPAE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 556 QVGFLLSSCGITVALTSEACLKGLPKSTTTGEIAklkgWPRLQWFVTEHLPKPPKefnvgnLRADDSAAAYIEYTTDKEG 635
Cdd:PRK12316 599 RLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLD----LDRPAAWLEGYSEENPG------TELNPENLAYVIYTSGSTG 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 636 SVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTsVLNGMHVIFIPYALMKlRPSSWMQLITKHR 715
Cdd:PRK12316 669 KPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAAPGDHR-DPAKLVELINREG 746
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 386770269 716 ASCC-LVKSrdLHWGLLatKDHKDISLSSLRMLLVADGANPWSL 758
Cdd:PRK12316 747 VDTLhFVPS--MLQAFL--QDEDVASCTSLRRIVCSGEALPADA 786
|
|
| ARG80 |
COG5068 |
Regulator of arginine metabolism and related MADS box-containing transcription factors ... |
33-368 |
5.94e-06 |
|
Regulator of arginine metabolism and related MADS box-containing transcription factors [Transcription];
Pssm-ID: 227400 [Multi-domain] Cd Length: 412 Bit Score: 50.78 E-value: 5.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 33 EKKRAKLLQPFLKKPEGDKVKSTPPPPYYNVKNANNSTNHGnINNDG-------------VIVSSEGYSYVTEVPSLSSS 99
Cdd:COG5068 67 IEQTKAQLQKFLISVTGRKIGISYITNKTKRSVTFSKRKHG-INKKAfelsvltgtevllLVISENGLVHTFTTPKLESV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 100 QQRHS--KKIDFHQQAAMSLSSAPQSGNAGAPGY-ENMRPQGgaVGDPGYQNTREPSAFQNQQStnnsQHRQRRTQRKVT 176
Cdd:COG5068 146 VKSLEgkSLIQSPCSNAPSDSSEEPSSSASFSVDpNDNNPMG--SFQHNGSPQTNFIPLQNPQT----QQYQQHSSRKDH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 177 HNEKRYHSvrqeavqqalaaLKGRPkPSLPMpSKRTSVLNRSPGCNDELDSSTDDESIPEETISPDKEYNYPRDHISNSI 256
Cdd:COG5068 220 PTVPHSNT------------NNGRP-PAKFM-IPELHSSHSTLDLPSDFISDSGFPNQSSTSIFPLDSAIIQITPPHLPN 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 257 LPPEPIIKPPIRESSMGSQQHARTDVKQNQiTNQKYTAPNSAP--ERRPPQNLPPLPTSEPLSSDYPPIaykreNDFSDK 334
Cdd:COG5068 286 NPPQENRHELYSNDSSMVSETPPPKNLPNG-SPNQSPLNNLSRgnPASPNSIIRENNQVEDESFNGRQG-----SAIWNA 359
|
330 340 350
....*....|....*....|....*....|....
gi 386770269 335 AFKQKQYNAPDITQFNNAHRAADRVTRYVNVSQN 368
Cdd:COG5068 360 LISTTQPNSGLHTEASTAPSSTIPADPLKNAAQT 393
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
476-697 |
6.11e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 51.09 E-value: 6.11e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 476 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNDplSFITAWYGCMFRGLVPLPIELPLSssdtpPQ 555
Cdd:PRK08316 35 RSWTYAELDAAVNRVAAALL----DLG-----LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLT-----GE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 556 QVGFLLSSCGITVALTSEACLKGLPKSTTTGEIAKLkGWPR--------------LQWFVTEHLPKPPKEfnvgnlrADD 621
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPALAPTAEAALALLPVDTL-ILSLvlggreapggwldfADWAEAGSVAEPDVE-------LAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 622 SAAAYIEYTTDKEGSVMGvtvtraAMINHcRALT-------MACHYTEGETIVCVLDfkrevgLWHSVltsvlnGMHVIF 694
Cdd:PRK08316 171 DDLAQILYTSGTESLPKG------AMLTH-RALIaeyvsciVAGDMSADDIPLHALP------LYHCA------QLDVFL 231
|
...
gi 386770269 695 IPY 697
Cdd:PRK08316 232 GPY 234
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
477-660 |
6.88e-06 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 50.74 E-value: 6.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 477 TLTYGKLLSRAQKIAHALSTKifskgpeqvTLKPGDRVALVYPNNDPLsfITAWYGCMFRGLVPLPIElplssSDTPPQQ 556
Cdd:cd17646 23 TLTYRELDERANRLAHLLRAR---------GVGPEDRVAVLLPRSADL--VVALLAVLKAGAAYLPLD-----PGYPADR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 557 VGFLLSSCGITVALTSEACLKGLPKSTTTGEIaklkgwprLQWFVTEHLPKPPKEFnvgnlrADDSAAAYIEYTTDKEGS 636
Cdd:cd17646 87 LAYMLADAGPAVVLTTADLAARLPAGGDVALL--------GDEALAAPPATPPLVP------PRPDNLAYVIYTSGSTGR 152
|
170 180
....*....|....*....|....
gi 386770269 637 VMGVTVTRAAMINhcRALTMACHY 660
Cdd:cd17646 153 PKGVMVTHAGIVN--RLLWMQDEY 174
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1101-1209 |
7.41e-06 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 50.79 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1101 EAHGRDVGLAEDcerkpQLITGVLRWRANTSPDHIIFTLLNSKgaiaktLTCSELHKRAEKIAALLQERGrIEPGDHVAL 1180
Cdd:cd05920 3 ARRYRAAGYWQD-----EPLGDLLARSAARHPDRIAVVDGDRR------LTYRELDRRADRLAAGLRGLG-IRPGDRVVV 70
|
90 100
....*....|....*....|....*....
gi 386770269 1181 IFPPGLDLLCAFYGCLYLGAIPITIRPPH 1209
Cdd:cd05920 71 QLPNVAEFVVLFFALLRLGAVPVLALPSH 99
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1149-1534 |
1.05e-05 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 50.15 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1149 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPphpqnlnttlptvRMIVdvsk 1228
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP-------------GMGR---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1229 sgivlsiqpiikllksREAATSIDpktwppildiDDNPKrkyAGIATVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLC 1308
Cdd:cd05910 64 ----------------KNLKQCLQ----------EAEPD---AFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1309 ASLKlacELYPSRHVALCLDpycglGFVMWTLIGVYSGHHSIL-----IAPyeVEANPSLWLSTLSQHRVRDTFCSYGVI 1383
Cdd:cd05910 115 DALR---QLYGIRPGEVDLA-----TFPLFALFGPALGLTSVIpdmdpTRP--ARADPQKLVGAIRQYGVSIVFGSPALL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1384 ELCTK---ALSNSIPSLKqrnidlrcvrtCVVVAEERPRVQLTQQFCKLFQalglNTRCVSTSFGCRVNPAICVQGAssa 1460
Cdd:cd05910 185 ERVARycaQHGITLPSLR-----------RVLSAGAPVPIALAARLRKMLS----DEAEILTPYGATEALPVSSIGS--- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1461 esaqvyvdmRALRNNRVALVERGApnSLCViesGKLLPGVKVII--ANPETKGHCGDSH------LGEIWVQAPHNANGY 1532
Cdd:cd05910 247 ---------RELLATTTAATSGGA--GTCV---GRPIPGVRVRIieIDDEPIAEWDDTLelprgeIGEITVTGPTVTPTY 312
|
..
gi 386770269 1533 FT 1534
Cdd:cd05910 313 VN 314
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1118-1207 |
1.32e-05 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 49.81 E-value: 1.32e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1118 QLITGVLRWRANTSPDHIifTLLNSKGAIakTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLY 1197
Cdd:cd05923 1 QTVFEMLRRAASRAPDAC--AIADPARGL--RLTYSELRARIEAVAARLHARG-LRPGQRVAVVLPNSVEAVIALLALHR 75
|
90
....*....|
gi 386770269 1198 LGAIPITIRP 1207
Cdd:cd05923 76 LGAVPALINP 85
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1115-1310 |
1.54e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 49.65 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1115 RKPQL------ITGVLRWRANTSPDH--IIFtllnskgaIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGL 1186
Cdd:PRK06178 24 REPEYphgerpLTEYLRAWARERPQRpaIIF--------YGHVITYAELDELSDRFAALLRQRG-VGAGDRVAVFLPNCP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1187 DLLCAFYGCLYLGAIPITIRP-------PHPQN---------LNTTLPTVRMI--------VDVSKSGIVLSIQPIIKLL 1242
Cdd:PRK06178 95 QFHIVFFGILKLGAVHVPVSPlfrehelSYELNdagaevllaLDQLAPVVEQVraetslrhVIVTSLADVLPAEPTLPLP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386770269 1243 KSREAATSIDPKTWPPILDIDDNPKRKYAGIAtvSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLCAS 1310
Cdd:PRK06178 175 DSLRAPRLAAAGAIDLLPALRACTAPVPLPPP--ALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAA 240
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1149-1207 |
2.25e-05 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 48.92 E-value: 2.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 386770269 1149 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRP 1207
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALG-VGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILP 58
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
478-723 |
5.01e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 48.62 E-value: 5.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 478 LTYGKLLSRAQKIAHALSTKifSKGPEQVtlkpgdrVALVYPNNdpLSFITAWYGCMFRG--LVPLPIELPlsssdtpPQ 555
Cdd:PRK12467 3121 LSYAELNRRANRLAHRLIAI--GVGPDVL-------VGVAVERS--VEMIVALLAVLKAGgaYVPLDPEYP-------RE 3182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 556 QVGFLLSSCGITVALTSEACLKGLPKST--TTGEIAKLKGWPRLqwfvtEHLPKPpkefnvgnlRADDSAAAYIEYTTDK 633
Cdd:PRK12467 3183 RLAYMIEDSGVKLLLTQAHLLEQLPAPAgdTALTLDRLDLNGYS-----ENNPST---------RVMGENLAYVIYTSGS 3248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 634 EGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHsVLTSVLNGMHVIFIPYALMKlrPSSWMQLITK 713
Cdd:PRK12467 3249 TGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDNDLWD--PEELWQAIHA 3325
|
250
....*....|.
gi 386770269 714 HRAS-CCLVKS 723
Cdd:PRK12467 3326 HRISiACFPPA 3336
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1148-1205 |
6.53e-05 |
|
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: 47.59 E-value: 6.53e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 386770269 1148 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITI 1205
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALG-VEPGDRVAILSRNRPEWTIADLAILAIGAVPVPI 60
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
477-649 |
7.73e-05 |
|
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: 47.29 E-value: 7.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 477 TLTYGKLLSRAQKIAHALSTKifskgpeqvTLKPGDRVALVYPNNDPLsfITAWYGCMFRGLVPLPIElplssSDTPPQQ 556
Cdd:cd12116 12 SLSYAELDERANRLAARLRAR---------GVGPGDRVAVYLPRSARL--VAAMLAVLKAGAAYVPLD-----PDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 557 VGFLLSSCGITVALTSEACLKGLPkstttgeiAKLKGWPRLQWFVTEHLPKPPKEfnvgnlrADDSAAAYIEYTTDKEGS 636
Cdd:cd12116 76 LRYILEDAEPALVLTDDALPDRLP--------AGLPVLLLALAAAAAAPAAPRTP-------VSPDDLAYVIYTSGSTGR 140
|
170
....*....|...
gi 386770269 637 VMGVTVTRAAMIN 649
Cdd:cd12116 141 PKGVVVSHRNLVN 153
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
441-748 |
8.33e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 48.03 E-value: 8.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 441 PAGLPRTLeCALQRYGTNSFKSPMATVLDPNGKvttTLTYGKLLSRAQKIAHALSTKifSKGPEQvtlkpgdRVALVYPN 520
Cdd:PRK12316 4544 DAGYPATR-CVHQLVAERARMTPDAVAVVFDEE---KLTYAELNRRANRLAHALIAR--GVGPEV-------LVGIAMER 4610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 521 NdpLSFITAWYGCMFRG--LVPLPIELPlsssdtpPQQVGFLLSSCGITVALTSEACLKGLPKSTTTGEIA-----KLKG 593
Cdd:PRK12316 4611 S--AEMMVGLLAVLKAGgaYVPLDPEYP-------RERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLAldrdeDWEG 4681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 594 WPrlqwfvtEHLPKppkefnvgnLRADDSAAAYIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGEtivCVLDFK 673
Cdd:PRK12316 4682 FP-------AHDPA---------VRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDD---RVLQFM 4742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 674 RevglwHSVLTSVLNGMHVIFIPYALMKLRPSSW-----MQLITKHRASccLVKSRDLHWGLLATKDHKDISLSSLRMLL 748
Cdd:PRK12316 4743 S-----FSFDGSHEGLYHPLINGASVVIRDDSLWdperlYAEIHEHRVT--VLVFPPVYLQQLAEHAERDGEPPSLRVYC 4815
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
476-656 |
1.46e-04 |
|
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: 46.57 E-value: 1.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 476 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIElplssSDTPPQ 555
Cdd:cd17651 19 RRLTYAELDRRANRLAHRLR----ARG-----VGPGDLVALCARRS--AELVVALLAILKAGAAYVPLD-----PAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 556 QVGFLLSSCGITVALTSEACLKGLPkstttGEIAKLKGWPRLQWfVTEHLPKPPKEFNVGNLraddsaaAYIEYTTDKEG 635
Cdd:cd17651 83 RLAFMLADAGPVLVLTHPALAGELA-----VELVAVTLLDQPGA-AAGADAEPDPALDADDL-------AYVIYTSGSTG 149
|
170 180
....*....|....*....|....*
gi 386770269 636 SVMGVTVTRAAMIN----HCRALTM 656
Cdd:cd17651 150 RPKGVVMPHRSLANlvawQARASSL 174
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
476-574 |
1.79e-04 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 46.25 E-value: 1.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 476 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNndplsfITAW----YGCMFRGLVPLPIelplsSSD 551
Cdd:COG1022 39 QSLTWAEFAERVRALAAGLL----ALG-----VKPGDRVAILSDN------RPEWviadLAILAAGAVTVPI-----YPT 98
|
90 100
....*....|....*....|...
gi 386770269 552 TPPQQVGFLLSSCGITVALTSEA 574
Cdd:COG1022 99 SSAEEVAYILNDSGAKVLFVEDQ 121
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
645-880 |
1.89e-04 |
|
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: 45.74 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 645 AAMINHCRALTMA------CHYTEGETIVCVLDFKrEVGLWHSVLTSVLNGMHVIFIPyalmKLRPSSWMQLITKHRAsC 718
Cdd:cd04433 17 GVVLSHRNLLAAAaalaasGGLTEGDVFLSTLPLF-HIGGLFGLLGALLAGGTVVLLP----KFDPEAALELIEREKV-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 719 CLVKSRDLHWGLLATKDHKDISLSSLRMLLVadGANPWSLSSCDQFLSVFQAKGLRsdaicpcasssevftvslrrpgrg 798
Cdd:cd04433 91 ILLGVPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAPGIKLVN------------------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 799 scGFSPSATGRGVLSMAALSHGVVRVDsedsltsltlqdCGQVMPAAQMVVVRSEGPPvlCKTDQVGEICVTSGSTSASY 878
Cdd:cd04433 145 --GYGLTETGGTVATGPPDDDARKPGS------------VGRPVPGVEVRIVDPDGGE--LPPGEIGELVVRGPSVMKGY 208
|
..
gi 386770269 879 FG 880
Cdd:cd04433 209 WN 210
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
477-574 |
2.16e-04 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 45.93 E-value: 2.16e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 477 TLTYGKLLSRAQKIAHALSTKIfskgpeqvTLKPGDRVALVYPNNDplSFITAWYGCMFRGLVPLPIeLPLsssdTPPQQ 556
Cdd:cd05958 10 EWTYRDLLALANRIANVLVGEL--------GIVPGNRVLLRGSNSP--ELVACWFGIQKAGAIAVAT-MPL----LRPKE 74
|
90
....*....|....*...
gi 386770269 557 VGFLLSSCGITVALTSEA 574
Cdd:cd05958 75 LAYILDKARITVALCAHA 92
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
476-758 |
2.68e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 45.60 E-value: 2.68e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 476 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIELplsssDTPPQ 555
Cdd:cd05930 11 QSLTYAELDARANRLARYLR----ERG-----VGPGDLVAVLLERS--LEMVVAILAVLKAGAAYVPLDP-----SYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 556 QVGFLLSSCGITVALTseaclkglpkstttgeiaklkgwprlqwfvtehlpkppkefnvgnlraDDSAAAYIEYTTDKEG 635
Cdd:cd05930 75 RLAYILEDSGAKLVLT------------------------------------------------DPDDLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 636 SVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWhSVLTSVLNGMHVIFIPYALMKLrPSSWMQLITKHR 715
Cdd:cd05930 107 KPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVW-EIFGALLAGATLVVLPEEVRKD-PEALADLLAEEG 184
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 386770269 716 ASC-CLVKSrdlHWGLLAtKDHKDISLSSLRMLLVADGANPWSL 758
Cdd:cd05930 185 ITVlHLTPS---LLRLLL-QELELAALPSLRLVLVGGEALPPDL 224
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1128-1378 |
5.11e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 44.77 E-value: 5.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1128 ANTSPDHIIFTLLnskgaiAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPItirp 1207
Cdd:PRK07786 27 ALMQPDAPALRFL------GNTTTWRELDDRVAALAGALSRRG-VGFGDRVLILMLNRTEFVESVLAANMLGAIAV---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1208 phPQNLNTTLPTVRMIVDVSKSGIVLS-------------IQPIIKLLKSREAATSIDPKTWPPILDIDDNPKrkyaGIA 1274
Cdd:PRK07786 96 --PVNFRLTPPEIAFLVSDCGAHVVVTeaalapvatavrdIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAH----APV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1275 TVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLCASLKLACELYPSRHVALCLDPY---CGLGFVmwtLIGVYSGHHSIL 1351
Cdd:PRK07786 170 DIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLfhiAGIGSM---LPGLLLGAPTVI 246
|
250 260
....*....|....*....|....*...
gi 386770269 1352 iapYEVEA-NPSLWLSTLSQHRVRDTFC 1378
Cdd:PRK07786 247 ---YPLGAfDPGQLLDVLEAEKVTGIFL 271
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1147-1374 |
6.03e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.95 E-value: 6.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1147 AKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQNlnttlpTVRMIVDV 1226
Cdd:PRK12316 534 EETLDYAELNRRANRLAHALIERG-VGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAE------RLAYMLED 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1227 SKSGIVLSIQPIIKLLKSREAATSID---PKTWPPILDiDDNPKRKYAGiatvsfDSSAYLDFSVSTCGRLSGVNITHRS 1303
Cdd:PRK12316 607 SGVQLLLSQSHLGRKLPLAAGVQVLDldrPAAWLEGYS-EENPGTELNP------ENLAYVIYTSGSTGKPKGAGNRHRA 679
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770269 1304 LSSLCASLKLACELYPSRHVaLCLDPYCgLGFVMWTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRVR 1374
Cdd:PRK12316 680 LSNRLCWMQQAYGLGVGDTV-LQKTPFS-FDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVD 748
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1150-1320 |
6.35e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.95 E-value: 6.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1150 LTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGA--IPitirpphpqnLNTTLPTVRMIVDVS 1227
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGayVP----------LDPNYPAERLAYMLE 2097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1228 KSGIVLsiqpiikLLKSREAATSIDPKTWPPILDIDD----------NPKRKYAGiatvsfDSSAYLDFSVSTCGRLSGV 1297
Cdd:PRK12316 2098 DSGAAL-------LLTQRHLLERLPLPAGVARLPLDRdaewadypdtAPAVQLAG------ENLAYVIYTSGSTGLPKGV 2164
|
170 180
....*....|....*....|...
gi 386770269 1298 NITHRSLSSLCASLKLACELYPS 1320
Cdd:PRK12316 2165 AVSHGALVAHCQAAGERYELSPA 2187
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1150-1201 |
7.81e-04 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 44.05 E-value: 7.81e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 386770269 1150 LTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAI 1201
Cdd:cd05973 1 LTFGELRALSARFANALQELG-VGPGDVVAGLLPRTPELVVTILGIWRLGAV 51
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1136-1304 |
1.03e-03 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 43.68 E-value: 1.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1136 IFTLLNSKGAIAKT-------LTCSELHKRAEKIAALLQERGRIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPp 1208
Cdd:PLN02574 46 IFSHHNHNGDTALIdsstgfsISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1209 hpqnLNTTLPTVRMIVDVSKSGIVLSIQPIIKLLKSREAATSIdpktwPPILDIDDNPKRKYAGIATVSFDS-------- 1280
Cdd:PLN02574 125 ----SSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGV-----PENYDFDSKRIEFPKFYELIKEDFdfvpkpvi 195
|
170 180
....*....|....*....|....*...
gi 386770269 1281 ----SAYLDFSVSTCGRLSGVNITHRSL 1304
Cdd:PLN02574 196 kqddVAAIMYSSGTTGASKGVVLTHRNL 223
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1149-1304 |
1.05e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 44.26 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1149 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQNlnttlpTVRMIVDVSK 1228
Cdd:PRK10252 483 QFSYREMREQVVALANLLRERG-VKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDAR 555
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 386770269 1229 SGIVLSIQPIIKLLKSREAATSIDPKTWPPilDIDDNPKRKYAGiatvsfDSSAYLDFSVSTCGRLSGVNITHRSL 1304
Cdd:PRK10252 556 PSLLITTADQLPRFADVPDLTSLCYNAPLA--PQGAAPLQLSQP------HHTAYIIFTSGSTGRPKGVMVGQTAI 623
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
476-609 |
1.14e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 43.80 E-value: 1.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 476 TTLTYGKLLSRAQKIAHALStkifskgpEQVTLKPGDRVALvYPNNDPlSFITAWYGCMFRGLVPLPIElPLSSSDtppq 555
Cdd:PRK08314 34 RAISYRELLEEAERLAGYLQ--------QECGVRKGDRVLL-YMQNSP-QFVIAYYAILRANAVVVPVN-PMNREE---- 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 386770269 556 QVGFLLSSCGITVALTSeACLkglpksttTGEIAKLKGWPRLQWFVTEH----LPKPP 609
Cdd:PRK08314 99 ELAHYVTDSGARVAIVG-SEL--------APKVAPAVGNLRLRHVIVAQysdyLPAEP 147
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
478-571 |
1.80e-03 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 42.85 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 478 LTYGKLLSRAQKIAHALSTKifskgpeqvTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIElPLSSSDtppqQV 557
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNK---------GVRKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----EL 65
|
90
....*....|....
gi 386770269 558 GFLLSSCGITVALT 571
Cdd:cd05935 66 EYILNDSGAKVAVV 79
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1150-1363 |
2.56e-03 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 42.47 E-value: 2.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1150 LTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPphpqnlnttlptvrmivdvsks 1229
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKG-VRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINP---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1230 givlsiqpiikLLKSREAATsidpktwppILDiDDNPKrkyAGIATVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLCA 1309
Cdd:cd05935 59 -----------MLKERELEY---------ILN-DSGAK---VAVVGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANAL 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 386770269 1310 SLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYEVEANPSL 1363
Cdd:cd05935 115 QSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALEL 168
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
477-672 |
2.63e-03 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 42.24 E-value: 2.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 477 TLTYGKLLSRAQKIAHALSTKIFskGPEQVtlkpgdrVALVYPNNDPLsfITAWYGCMFRGLVPLPIElplssSDTPPQQ 556
Cdd:cd17652 12 TLTYAELNARANRLARLLAARGV--GPERL-------VALALPRSAEL--VVAILAVLKAGAAYLPLD-----PAYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 557 VGFLLSSCGITVALTSEaclkglpkstttgeiaklkgwprlqwfvtehlpkppkefnvgnlraddSAAAYIEYTTDKEGS 636
Cdd:cd17652 76 IAYMLADARPALLLTTP------------------------------------------------DNLAYVIYTSGSTGR 107
|
170 180 190
....*....|....*....|....*....|....*.
gi 386770269 637 VMGVTVTRAAMINHCRALTMACHYTEGEtivCVLDF 672
Cdd:cd17652 108 PKGVVVTHRGLANLAAAQIAAFDVGPGS---RVLQF 140
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1118-1252 |
3.42e-03 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 42.05 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1118 QLITGVLRWRANTSPDHiifTLLNSKGaiaKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLY 1197
Cdd:PRK06155 21 RTLPAMLARQAERYPDR---PLLVFGG---TRWTYAEAARAAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAW 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 386770269 1198 LGAI--PITIRPPHPQnLNTTLPTVRMIVDVSKSGIVLSIQPIIKLLKSREAATSID 1252
Cdd:PRK06155 94 LGAIavPINTALRGPQ-LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLD 149
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
477-647 |
3.42e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 3.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 477 TLTYGKLLSRAQKIAHALSTKifSKGPEQVTLKPGDR-----VALvypnndpLSFITAwyGCMFrglVPLpielplsSSD 551
Cdd:PRK05691 1156 SLDYAELHAQANRLAHYLRDK--GVGPDVCVAIAAERspqllVGL-------LAILKA--GGAY---VPL-------DPD 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 552 TPPQQVGFLLSSCGITVALTSEACLKGLPKSTTTGEIA----KLKGWPrlqwfvtehlPKPPkefnvgNLRADDSAAAYI 627
Cdd:PRK05691 1215 YPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIAldslHLDSWP----------SQAP------GLHLHGDNLAYV 1278
|
170 180
....*....|....*....|
gi 386770269 628 EYTTDKEGSVMGVTVTRAAM 647
Cdd:PRK05691 1279 IYTSGSTGQPKGVGNTHAAL 1298
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1124-1201 |
3.49e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 41.87 E-value: 3.49e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 386770269 1124 LRWRANTSPDHIIFTLLNskgaiaKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAI 1201
Cdd:PRK03640 8 LKQRAFLTPDRTAIEFEE------KKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAV 78
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1148-1233 |
3.70e-03 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 41.96 E-value: 3.70e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1148 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIrpphpqNLNTTLPTVRMIVDVS 1227
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLG-LKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI------NYNLRGESLAHCLNVS 74
|
....*.
gi 386770269 1228 KSGIVL 1233
Cdd:cd05940 75 SAKHLV 80
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1147-1205 |
6.06e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 41.41 E-value: 6.06e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 386770269 1147 AKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITI 1205
Cdd:PRK07798 26 DRRLTYAELEERANRLAHYLIAQG-LGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1149-1253 |
6.22e-03 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 41.01 E-value: 6.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 386770269 1149 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGA--IPITIRPPHPQnLNTTLP--TVRMIV 1224
Cdd:PRK09029 28 VLTWQQLCARIDQLAAGFAQQG-VVEGSGVALRGKNSPETLLAYLALLQCGArvLPLNPQLPQPL-LEELLPslTLDFAL 105
|
90 100
....*....|....*....|....*....
gi 386770269 1225 DVSKSGIVLSIQPIIKLLKSREAATSIDP 1253
Cdd:PRK09029 106 VLEGENTFSALTSLHLQLVEGAHAVAWQP 134
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1132-1202 |
7.23e-03 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 41.19 E-value: 7.23e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 386770269 1132 PDHIIFTLLNSKGAIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIP 1202
Cdd:PRK13295 38 PDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLG-VGRGDVVSCQLPNWWEFTVLYLACSRIGAVL 107
|
|
| |
