|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1137-1752 |
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 442629139 1137 IFTLLNSKGAIAKTLTCSELHKRAEKIAALLQERGRIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPH-PQNLN 1215
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1216 TTLPTVRMivDVSKSGIVLSIQPIIKLLKSREAATSIDPKTWPPILDIDDNPK------RKYAGIATVSFDSSAYLDFSV 1289
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKskrsklKKWGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1290 STCGRLSGVNITHRSLSSLCASLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYEVEANPSLWLSTL 1369
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1370 SQHRVRDTFCSYGVIELCTKALSNSIPSLKQRNIDLRCVRTCVVVAEERPRVQLTQQFCKLFQALGLNTRCVSTSFGCRV 1449
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1450 NPAICVQGASSAESAQVYVDMRALRNNRVALVERGAPNSLCVIESGKLLPGVKVIIANPETKGHCGDSHLGEIWVQAPHN 1529
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1530 ANGYFTIYGDETDYNDHFNA-KLVTGATSELYARTGYLGFLRRTECSQSaslldettpsvasrdsdteslnsisqlqlnf 1608
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFPStRLSTGITNNSYARTGLLGFLRPTKCTDL------------------------------- 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1609 snvslggnsehslvggasnanDQELHDAVYVVGAVDEVISLRGMNYHPIDIENSVMRCHKKIAECAVFTWTNLLVVVVEL 1688
Cdd:cd05905 448 ---------------------NVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQ 506
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442629139 1689 D-GNESEALDLVPLVTNTVLEDHQLIVGVVVVVDPGVVPINSRGEKQRMHLRDGFLADQLDPIYV 1752
Cdd:cd05905 507 PpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
465-1061 |
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 442629139 465 MATVLDPNGKVTTTLTYGKLLSRAQKIAHALSTKIfskgpeqvTLKPGDRVALVYPnnDPLSFITAWYGCMFRGLVPLPI 544
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKV--------GLKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 545 ELPLsssdtPPQQVGFLLSSCGITVALTSEACLKGLPKST----TTGEIAKLKGWPRLQWFVTEHLPKP-PKEFNVGNLR 619
Cdd:cd05905 71 EPPD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKLlkskTAAEIAKKKGWPKILDFVKIPKSKRsKLKKWGPHPP 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 620 ADDSAAAYIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYA 699
Cdd:cd05905 146 TRDGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPE 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 700 LMKLRPSSWMQLITKHRASCCLVKSRDLHWGL------LATKDHKDISLSSLRMLLVADGaNPWSLSSCDQFLSVFQAKG 773
Cdd:cd05905 226 LMKTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 774 LRSDAIcpcasSSEVFTVSLRRPGRGscGFSPSATGRGVLSMAALSHGVVRVDSEDSLTSLTLQDCGQVMPAAQMVVVRS 853
Cdd:cd05905 305 LSPRAV-----STEFGTRVNPFICWQ--GTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 854 EGPPvLCKTDQVGEICVTSGSTSASYFGLDGMTNSTFKVQPlleeleqpkdgngtVNIISKPIGEDFYVRS--------- 924
Cdd:cd05905 378 ETKG-LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFP--------------STRLSTGITNNSYARTgllgflrpt 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 925 -GLLGFLGPGGLVFVCGSRDGLMTVTGRKHNADDIIATVLAVEPmrfiYRGRIAVFSIKvlrdERVCVIAEQRPdCSEEE 1003
Cdd:cd05905 443 kCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSEEE 513
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 442629139 1004 SFQWMSRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRFLEGSLHPANV 1061
Cdd:cd05905 514 ALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1127-1712 |
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 442629139 1127 WRANTSPDHIIFTLLNSKGAIAKTLTCSELHKRAEKIAALLQERGRiePGDHVALIFPPGLDLLCAFYGCLYLGAIPITI 1206
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1207 RPPHPqnlNTTLPTVRMIVDVSKSGIVLSIQPIIKLLKSREAATSIDPKTWPPILDIDDNPKRKYAGIATVSFDSSAYLD 1286
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1287 F-SVSTcGRLSGVNITHRSLSSLCASLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYEVEANPSLW 1365
Cdd:cd05931 156 YtSGST-GTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1366 LSTLSQHRvrdtfcsyGVI--------ELCTKAlsnsIPSLKQRNIDLRCVRTCVVVAeERPRVQLTQQFCKLFQALGLN 1437
Cdd:cd05931 235 LRLISRYR--------ATIsaapnfayDLCVRR----VRDEDLEGLDLSSWRVALNGA-EPVRPATLRRFAEAFAPFGFR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1438 TRCVSTSFGCrvnpAICVQGASSAESAQ----VYVDMRALRnNRVALVERGAPNSLCVIESGKLLPGVKVIIANPETKGH 1513
Cdd:cd05931 302 PEAFRPSYGL----AEATLFVSGGPPGTgpvvLRVDRDALA-GRAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGRE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1514 CGDSHLGEIWVQAPHNANGYFtiyGDETDYNDHFNAKLVTGATSelYARTGYLGFLRrtecsqsaslldettpsvasrds 1593
Cdd:cd05931 377 LPDGEVGEIWVRGPSVASGYW---GRPEATAETFGALAATDEGG--WLRTGDLGFLH----------------------- 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1594 dteslnsisqlqlnfsnvslggnsehslvggasnanDQELhdavYVVGAVDEVISLRGMNYHPIDIENSVMRCHKKIAE- 1672
Cdd:cd05931 429 ------------------------------------DGEL----YITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPg 468
|
570 580 590 600
....*....|....*....|....*....|....*....|....*...
gi 442629139 1673 -CAVFTW----TNLLVVVVELDGNEsEALDLVPLVTN---TVLEDHQL 1712
Cdd:cd05931 469 cVAAFSVpddgEERLVVVAEVERGA-DPADLAAIAAAiraAVAREHGV 515
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
467-1052 |
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 442629139 467 TVLDPNGKVTTTLTYGKLLSRAQKIAHALstkifskgpeQVTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIEL 546
Cdd:cd05931 13 TFLDDEGGREETLTYAELDRRARAIAARL----------QAVGKPGDRVLLLAPPG--LDFVAAFLGCLYAGAIAVPLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 547 PLSSSDTPpqQVGFLLSSCGITVALTSEACLKGLPKSTTTGEiaklkGWPRLQWFVTEHLP-KPPKEFNVGNLRADDsaA 625
Cdd:cd05931 81 PTPGRHAE--RLAAILADAGPRVVLTTAAALAAVRAFAASRP-----AAGTPRLLVVDLLPdTSAADWPPPSPDPDD--I 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 626 AYIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFI-PYALMKlR 704
Cdd:cd05931 152 AYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMsPAAFLR-R 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 705 PSSWMQLITKHRASC----------CLVKSRDLHwglLATKDhkdisLSSLRMLLVadGANPWSLSSCDQFLSVFQAKGL 774
Cdd:cd05931 231 PLRWLRLISRYRATIsaapnfaydlCVRRVRDED---LEGLD-----LSSWRVALN--GAEPVRPATLRRFAEAFAPFGF 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 775 RSDAICPC---ASSSeVFtVSLRRPGRGscgfsPSATgrgVLSMAALSHGVVRVDSEDSlTSLTLQDCGQVMPAAQMVVV 851
Cdd:cd05931 301 RPEAFRPSyglAEAT-LF-VSGGPPGTG-----PVVL---RVDRDALAGRAVAVAADDP-AARELVSCGRPLPDQEVRIV 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 852 RSEGPPVlCKTDQVGEICVTSGSTSASYFGLDGMTNSTFKvqpllEELEQPKDG---NGTVNIISKpiGEdfyvrsgllg 928
Cdd:cd05931 370 DPETGRE-LPDGEVGEIWVRGPSVASGYWGRPEATAETFG-----ALAATDEGGwlrTGDLGFLHD--GE---------- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 929 flgpgglVFVCGSRDGLMTVTGRKHNADDIIATVLAVEPMrfIYRGRIAVFSIKVLRDERVCVIAEQRPDCSEEESFQWM 1008
Cdd:cd05931 432 -------LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIA 502
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 442629139 1009 SRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRFL 1052
Cdd:cd05931 503 AAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1125-1570 |
5.81e-40 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 154.39 E-value: 5.81e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1125 LRWRANTSPDHIIFTllnskGAIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPI 1204
Cdd:pfam00501 1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1205 TIRPphpqnlNTTLPTVRMIVDVSKSGIVLsIQPIIKLLKSREAATSIDPKTWPPILDIDDNPKRKYAGIATVSF----- 1279
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLI-TDDALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPAdvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1280 -------DSSAYLDFSVSTCGRLSGVNITHRSLSSLCASLKLACE----LYPSRHVALCLDPYCGLGFVMWTLIGVYSGH 1348
Cdd:pfam00501 148 pppppdpDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1349 HSILIAPyEVEANPSLWLSTLSQHRVRDTFCSYGVIELCTKALS---NSIPSLKQrnidlrcvrtcVVVAEERPRVQLTQ 1425
Cdd:pfam00501 228 TVVLPPG-FPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGApkrALLSSLRL-----------VLSGGAPLPPELAR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1426 QFCKLFqalglnTRCVSTSFGCRVNPAICvqgassaesaqVYVDMRALRNNRVALVergapnslcviesGKLLPGVKVII 1505
Cdd:pfam00501 296 RFRELF------GGALVNGYGLTETTGVV-----------TTPLPLDEDLRSLGSV-------------GRPLPGTEVKI 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442629139 1506 ANPETKGHCGDSHLGEIWVQAPHNANGYftiYGDETDYNDHFNAKlvtgatsELYaRTGYLGFLR 1570
Cdd:pfam00501 346 VDDETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAFDED-------GWY-RTGDLGRRD 399
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
470-1061 |
1.35e-31 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 132.44 E-value: 1.35e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 470 DPNGKVTTTLTYGKLLSRAQKIAHALSTkifskgpeqVTLKPGDRVALVyPNNDPlSFITAWYGCMFRGLVPLPIELPLS 549
Cdd:PRK09192 41 DRRGQLEEALPYQTLRARAEAGARRLLA---------LGLKPGDRVALI-AETDG-DFVEAFFACQYAGLVPVPLPLPMG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 550 --SSDTPPQQVGFLLSSCGITVALTSEAcLKGLPKSTTTGEIAKLKGWPRlqWFVTehLPKPPKEFNvgnlRADDSAAAY 627
Cdd:PRK09192 110 fgGRESYIAQLRGMLASAQPAAIITPDE-LLPWVNEATHGNPLLHVLSHA--WFKA--LPEADVALP----RPTPDDIAY 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 628 IEYTTdkeGSV---MGVTVTRAAMINHCRALTM-ACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYALMKL 703
Cdd:PRK09192 181 LQYSS---GSTrfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFAR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 704 RPSSWMQLITKHRASC----------CLVKSRDlhwgllatKDHKDISLSSLRmlLVADGANPWSLSSCDQFLSVFQAKG 773
Cdd:PRK09192 258 RPLQWLDLISRNRGTIsysppfgyelCARRVNS--------KDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAG 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 774 LRSDAICPCASSSEVfTVSLrrpgrgscGFSPSATGRGVLSMAA--LSHGVVRVDS-EDSLTSLTLQDCGQVMPAAQmVV 850
Cdd:PRK09192 328 FDDKAFMPSYGLAEA-TLAV--------SFSPLGSGIVVEEVDRdrLEYQGKAVAPgAETRRVRTFVNCGKALPGHE-IE 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 851 VRSEGPPVLCKTdQVGEICVTSGSTSASYFGlDGMTNSTFKVQPLLE--ELEQPKDGNgtvniiskpigedfyvrsgllg 928
Cdd:PRK09192 398 IRNEAGMPLPER-VVGHICVRGPSLMSGYFR-DEESQDVLAADGWLDtgDLGYLLDGY---------------------- 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 929 flgpgglVFVCGSRDGLMTVTGRKHNADDIiatVLAVEPMRFIYRGRIAVFSIKVLRDERVCVIAEQRPDcSEEESFQWM 1008
Cdd:PRK09192 454 -------LYITGRAKDLIIINGRNIWPQDI---EWIAEQEPELRSGDAAAFSIAQENGEKIVLLVQCRIS-DEERRGQLI 522
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 442629139 1009 SRVLQAVDSIHqvGIYCL-ALVPPNHLPKTPLGGIHLCEARRRFLEGSLHPANV 1061
Cdd:PRK09192 523 HALAALVRSEF--GVEAAvELVPPHSLPRTSSGKLSRAKAKKRYLSGAFASLDV 574
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
3-115 |
3.26e-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: 3.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 3 HTASLPGYVREKLAELDLELSEGDITQKGYEKKRAKLLQPFLKKPEgdkvkstpPPPYYNVKNANNSTNHGNINNDGvIV 82
Cdd:pfam06464 1 NPPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLHPE--------TPTKLSAEAQNQLASLETKLRDE-EL 71
|
90 100 110
....*....|....*....|....*....|...
gi 442629139 83 SSEGYSYVTEVPSLSSSQQRHSKKIDFHQQAAM 115
Cdd:pfam06464 72 SEEVYLEKVKALLAKELERENGLNAPTKEQSGL 104
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
477-891 |
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 442629139 477 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIelplsSSDTPPQ 556
Cdd:pfam00501 20 RRLTYRELDERANRLAAGLR----ALG-----VGKGDRVAILLPNS--PEWVVAFLACLKAGAVYVPL-----NPRLPAE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 557 QVGFLLSSCGITVALTSEACL-------KGLPKSTTTGEIAKLKGWPRLQWFVTEHLPKPPKEFNVGNLRADDsaAAYIE 629
Cdd:pfam00501 84 ELAYILEDSGAKVLITDDALKleelleaLGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDD--LAYII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 630 YT-----TDKegsvmGVTVTRAAMINHCRALTMACHY----TEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYAL 700
Cdd:pfam00501 162 YTsgttgKPK-----GVMLTHRNLVANVLSIKRVRPRgfglGPDDRVLSTLPLFHDFGLSLGLLGPLLAGATVVLPPGFP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 701 MkLRPSSWMQLITKHRASC-CLVKSrdLHWGLLATKDHKDISLSSLRMLLVadGANPWSLSSCDQFLSVFqakglrsdai 779
Cdd:pfam00501 237 A-LDPAALLELIERYKVTVlYGVPT--LLNMLLEAGAPKRALLSSLRLVLS--GGAPLPPELARRFRELF---------- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 780 cpcasssevftvslrrPGRGSCGFSPSATGrgvlsmAALSHGVVRVDSEDSLTSltlqdCGQVMPAAQMVVV-RSEGPPV 858
Cdd:pfam00501 302 ----------------GGALVNGYGLTETT------GVVTTPLPLDEDLRSLGS-----VGRPLPGTEVKIVdDETGEPV 354
|
410 420 430
....*....|....*....|....*....|...
gi 442629139 859 lcKTDQVGEICVTSGSTSASYFGLDGMTNSTFK 891
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 ... |
1283-1697 |
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 442629139 1283 AYLDFSVSTCGRLSGVNITHRSLSSLCASLkLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYeveaNP 1362
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF----DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1363 SLWLSTLSQHRVRDTFCSYGVIELCTKALsnsipslKQRNIDLRCVRTCVVVAEERPRVqLTQQF-----CKLFQALGLN 1437
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAP-------ESAGYDLSSLRALVSGGAPLPPE-LLERFeeapgIKLVNGYGLT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1438 TRCVSTSFGCRVNPAicvqgassaesaqvyvdmralrnnrvalverGAPNSlcvieSGKLLPGVKVIIANPETkGHCGDS 1517
Cdd:cd04433 150 ETGGTVATGPPDDDA-------------------------------RKPGS-----VGRPVPGVEVRIVDPDG-GELPPG 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1518 HLGEIWVQAPHNANGYFTiygdetdyndhfNAKLVTGATSELYARTGYLGFLrrtecsqsasllDEttpsvasrdsdtes 1597
Cdd:cd04433 193 EIGELVVRGPSVMKGYWN------------NPEATAAVDEDGWYRTGDLGRL------------DE-------------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1598 lnsisqlqlnfsnvslggnsehslvggasnandqelHDAVYVVGAVDEVISLRGMNYHPIDIENSVMRcHKKIAECAVF- 1676
Cdd:cd04433 235 ------------------------------------DGYLYIVGRLKDMIKSGGENVYPAEVEAVLLG-HPGVAEAAVVg 277
|
410 420
....*....|....*....|....*
gi 442629139 1677 ----TWTNLLVVVVELDGNESEALD 1697
Cdd:cd04433 278 vpdpEWGERVVAVVVLRPGADLDAE 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1118-1573 |
6.54e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 117.58 E-value: 6.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1118 PQLITGVLRWRANTSPDHIIFTLLNSKGAIAKTLTCSELHKRAEKIAALLQERGriEPGDHVALIFPPGLDLLCAFYGCL 1197
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARA--SFGDRAVLLFPSGPDYVAAFFGCL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1198 YLGAIPITIRPP------HPQNLNTtlptvrmIVDVSKSGIVLSIQPIIKLLKSREAATSIDPktwPPILDIDDNPkrky 1271
Cdd:PRK05691 86 YAGVIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLD---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1272 AGIA------TVSFDSSAYLDFSVSTCGRLSGVNITHRSLsslcaslkLACELYPSRHVALCLDP----------YCGLG 1335
Cdd:PRK05691 152 PALAeawqepALQPDDIAFLQYTSGSTALPKGVQVSHGNL--------VANEQLIRHGFGIDLNPddvivswlplYHDMG 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1336 FVMWTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRvrdtfcsyGVI--------ELCTKALSNSipSLKQrnIDLRC 1407
Cdd:PRK05691 224 LIGGLLQPIFSGVPCVLMSPAYFLERPLRWLEAISEYG--------GTIsggpdfayRLCSERVSES--ALER--LDLSR 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1408 VRtcVVVAEERP-RVQLTQQFCKLFQALGLNTRCVSTSFGCrVNPAICVQGASSAES-AQVYVDMRALRNNRVALVErGA 1485
Cdd:PRK05691 292 WR--VAYSGSEPiRQDSLERFAEKFAACGFDPDSFFASYGL-AEATLFVSGGRRGQGiPALELDAEALARNRAEPGT-GS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1486 PnslcVIESGKLLPGVKVIIANPETKGHCGDSHLGEIWVQAPHNANGYFTiygdetdyNDHFNAKLVTGATSELYARTGY 1565
Cdd:PRK05691 368 V----LMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR--------NPEASAKTFVEHDGRTWLRTGD 435
|
....*...
gi 442629139 1566 LGFLRRTE 1573
Cdd:PRK05691 436 LGFLRDGE 443
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
477-891 |
6.85e-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: 6.85e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 477 TTLTYGKLLSRAQKIAHALStkifskgpeQVTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIELPLsssdtPPQ 556
Cdd:COG0318 23 RRLTYAELDARARRLAAALR---------ALGVGPGDRVALLLPNS--PEFVVAFLAALRAGAVVVPLNPRL-----TAE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 557 QVGFLLSSCGITVALTseACLkgLPKSTTTGeiaklkgwprlqwfvtehLPKppkefnvgnlraddsaaayieyttdkeg 636
Cdd:COG0318 87 ELAYILEDSGARALVT--ALI--LYTSGTTG------------------RPK---------------------------- 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 637 svmGVTVTRAAMINHCRALTMACHYTEGETIVCVL----DFkrevGLWHSVLTSVLNGMHVIFIPyalmKLRPSSWMQLI 712
Cdd:COG0318 117 ---GVMLTHRNLLANAAAIAAALGLTPGDVVLVALplfhVF----GLTVGLLAPLLAGATLVLLP----RFDPERVLELI 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 713 TKHRAS-CCLVKSrdLHWGLLATKDHKDISLSSLRMLLVadGANPWSLSSCDQFLSVFQAkglrsdAICPCASSSEVFTV 791
Cdd:COG0318 186 ERERVTvLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERFEERFGV------RIVEGYGLTETSPV 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 792 SLRRPGrgscgfspsatgrgvlsmaalSHGVVRVDSedsltsltlqdCGQVMPAAQMVVVRSEGPPVlcKTDQVGEICVT 871
Cdd:COG0318 256 VTVNPE---------------------DPGERRPGS-----------VGRPLPGVEVRIVDEDGREL--PPGEVGEIVVR 301
|
410 420
....*....|....*....|
gi 442629139 872 SGSTSASYFGLDGMTNSTFK 891
Cdd:COG0318 302 GPNVMKGYWNDPEATAEAFR 321
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1121-1699 |
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 442629139 1121 ITGVLRWRANTSPDHIIFTLLNskgaiaKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLG 1200
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGG------RRLTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1201 AIPITIrpphpqNLNTTLPTVRMIVDVSKSGIVLS--IQPiikllksreaaTSidpktwppildiddnpkrkyaGiatvs 1278
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVTalILY-----------TS---------------------G----- 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1279 fdssayldfsvSTcGRLSGVNITHRSLSSLCASLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYev 1358
Cdd:COG0318 111 -----------TT-GRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLPRF-- 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1359 eaNPSLWLSTLSQHRVrdTFcSYGV----IELCTKAlsnsipslKQRNIDLRCVRTCVVVAEerprvQLTQQFCKLFQAL 1434
Cdd:COG0318 177 --DPERVLELIERERV--TV-LFGVptmlARLLRHP--------EFARYDLSSLRLVVSGGA-----PLPPELLERFEER 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1435 glntrcvstsFGCRVnpaicVQGASSAE-SAQVYVDMRALRNNRVALVergapnslcviesGKLLPGVKVIIANPETKGh 1513
Cdd:COG0318 239 ----------FGVRI-----VEGYGLTEtSPVVTVNPEDPGERRPGSV-------------GRPLPGVEVRIVDEDGRE- 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1514 CGDSHLGEIWVQAPHNANGYftiYGDEtdyndhfnaklvtGATSELYA----RTGYLGFLrrtecsqsaslldettpsva 1589
Cdd:COG0318 290 LPPGEVGEIVVRGPNVMKGY---WNDP-------------EATAEAFRdgwlRTGDLGRL-------------------- 333
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1590 srDSDteslnsisqlqlnfsnvslgGNsehslvggasnandqelhdaVYVVGAVDEVISLRGMNYHPIDIENSVMRcHKK 1669
Cdd:COG0318 334 --DED--------------------GY--------------------LYIVGRKKDMIISGGENVYPAEVEEVLAA-HPG 370
|
570 580 590
....*....|....*....|....*....|....*.
gi 442629139 1670 IAECAVF-----TWTNLLVVVVEL-DGNESEALDLV 1699
Cdd:COG0318 371 VAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELR 406
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1121-1569 |
1.71e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 107.34 E-value: 1.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1121 ITGVLRWRANTSPDHIIFTLLN---SKGAIAKTLTCSELHKRAEKIAALLQERGRiePGDHVALIFPPGLDLLCAFYGCL 1197
Cdd:PRK05850 3 VPSLLRERASLQPDDAAFTFIDyeqDPAGVAETLTWSQLYRRTLNVAEELRRHGS--TGDRAVILAPQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1198 YLGAIPITIRPPHPQnlnttlptvrmIVDVSKSGIVLSIQPIIKLLKS------REAATSIDPKTWPPILDID--DNPKR 1269
Cdd:PRK05850 81 QAGLIAVPLSVPQGG-----------AHDERVSAVLRDTSPSVVLTTSavvddvTEYVAPQPGQSAPPVIEVDllDLDSP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1270 KYAGIATVSFDSSAYLDF-SVSTcgRL-SGVNITHRSLSSLCAslKLACELYPSRHVALCLD-------P-YCGLGFVMW 1339
Cdd:PRK05850 150 RGSDARPRDLPSTAYLQYtSGST--RTpAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMGLVLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1340 TLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRVRDTFCSYGVIELCTKALSNSipslKQRNIDLRCVRTCVVVAEerp 1419
Cdd:PRK05850 226 VCAPILGGCPAVLTSPVAFLQRPARWMQLLASNPHAFSAAPNFAFELAVRKTSDD----DMAGLDLGGVLGIISGSE--- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1420 RVQLT--QQFCKLFQALGLNTRCVSTSFGCrvnpAICVQGASSAESAQ----VYVDMRALRNNRV---------ALVERG 1484
Cdd:PRK05850 299 RVHPAtlKRFADRFAPFNLRETAIRPSYGL----AEATVYVATREPGQppesVRFDYEKLSAGHAkrcetgggtPLVSYG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1485 APNSlcviesgkllPGVKviIANPETKGHCGDSHLGEIWVQAPHNANGYFTiYGDETdyNDHFNAKLVT---GATSELYA 1561
Cdd:PRK05850 375 SPRS----------PTVR--IVDPDTCIECPAGTVGEIWVHGDNVAAGYWQ-KPEET--ERTFGATLVDpspGTPEGPWL 439
|
....*...
gi 442629139 1562 RTGYLGFL 1569
Cdd:PRK05850 440 RTGDLGFI 447
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1151-1568 |
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 442629139 1151 LTCSELHKRAEKIAALLQERGRiePGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPP----HPQNLNTTL----PTVR 1222
Cdd:PRK12476 69 LTWTQLGVRLRAVGARLQQVAG--PGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1223 MIVDVSKsgivlsiQPIIKLLKSREAATSidpktwPPILDIDDNPKRKYAGIATVSFDSS--AYLDFSVSTCGRLSGVNI 1300
Cdd:PRK12476 147 LTTTAAA-------EAVEGFLRNLPRLRR------PRVIAIDAIPDSAGESFVPVELDTDdvSHLQYTSGSTRPPVGVEI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1301 THRSLSSLCASLKLACELY-PSRHVALCLDPYCGLGFVMWTLIGVYSGhHSILIAPYEVEANPSLWLSTLSQHrvrdtfC 1379
Cdd:PRK12476 214 THRAVGTNLVQMILSIDLLdRNTHGVSWLPLYHDMGLSMIGFPAVYGG-HSTLMSPTAFVRRPQRWIKALSEG------S 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1380 SYGviELCTKALSNSIPSLKQR-------NIDLRCVrtCVVVAEERPRVQLTQQFCKLFQALGLNTRCVSTSFGCRVNPA 1452
Cdd:PRK12476 287 RTG--RVVTAAPNFAYEWAAQRglpaegdDIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEATL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1453 ICVQGASSAESAQVYVDMRALRNNRVALVERGAPNSLCVIESGKLLPGVKVIIANPETKGHCGDSHLGEIWVQAPHNANG 1532
Cdd:PRK12476 363 FVATIAPDAEPSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRG 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 442629139 1533 YFTiYGDETDYNdhFNAKLVT----------GATSELYARTGYLGF 1568
Cdd:PRK12476 443 YWG-RPEETERT--FGAKLQSrlaegshadgAADDGTWLRTGDLGV 485
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
470-1042 |
3.89e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 100.02 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 470 DPNGkVTTTLTYGKLLSRAQKIAHALStkifSKGpeqvtlKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIELPL- 548
Cdd:PRK05850 28 DPAG-VAETLTWSQLYRRTLNVAEELR----RHG------STGDRAVILAPQG--LEYIVAFLGALQAGLIAVPLSVPQg 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 549 SSSDtppQQVGFLLSSCGITVALTSeaclkglpkSTTTGEIAKLKGWPRLQ---WFVTEHLPKPPKEFNVGNLRADDSAA 625
Cdd:PRK05850 95 GAHD---ERVSAVLRDTSPSVVLTT---------SAVVDDVTEYVAPQPGQsapPVIEVDLLDLDSPRGSDARPRDLPST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 626 AYIEYTTDKEGSVMGVTVTRAAMINHCRALtMACHY-------TEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFI-P 697
Cdd:PRK05850 163 AYLQYTSGSTRTPAGVMVSHRNVIANFEQL-MSDYFgdtggvpPPDTTVVSWLPFYHDMGLVLGVCAPILGGCPAVLTsP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 698 YALMKlRPSSWMQLITKHRAScclvksrdlhWGL-------LATKDHKDISLSSL---RMLLVADGA---NPWSLsscDQ 764
Cdd:PRK05850 242 VAFLQ-RPARWMQLLASNPHA----------FSAapnfafeLAVRKTSDDDMAGLdlgGVLGIISGServHPATL---KR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 765 FLSVFQAKGLRSDAICPCASSSE--VFtVSLRRPGRgscgfsPSATGRgvLSMAALSHGVVRVDSEDSLTSLTlqDCGqv 842
Cdd:PRK05850 308 FADRFAPFNLRETAIRPSYGLAEatVY-VATREPGQ------PPESVR--FDYEKLSAGHAKRCETGGGTPLV--SYG-- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 843 MPAAQMV-VVRSEgPPVLCKTDQVGEICVTSGSTSASYFGLDGMTNSTFKVQplleeLEQPKDG--------NGTVNIIS 913
Cdd:PRK05850 375 SPRSPTVrIVDPD-TCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGAT-----LVDPSPGtpegpwlrTGDLGFIS 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 914 KpiGEdfyvrsgllgflgpgglVFVCGSRDGLMTVTGRKHNADDIIATVLAvepmrfIYRGRIAVFSIKVLRDERVCVIA 993
Cdd:PRK05850 449 E--GE-----------------LFIVGRIKDLLIVDGRNHYPDDIEATIQE------ITGGRVAAISVPDDGTEKLVAII 503
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 442629139 994 E-QRPDCSEEESFQWM----SRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGI 1042
Cdd:PRK05850 504 ElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1145-1676 |
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 442629139 1145 GAIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIpitIRPPHPQN--------LNT 1216
Cdd:cd05911 5 ADTGKELTYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGGI---FSAANPIYtadelahqLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1217 TLPTVrMIVD------VSKSG-IVLSIQPIIKLLKSREAATSIDPKTWPPILDIDDN-PKRKYAGIATVsfdssAYLDFS 1288
Cdd:cd05911 81 SKPKV-IFTDpdglekVKEAAkELGPKDKIIVLDDKPDGVLSIEDLLSPTLGEEDEDlPPPLKDGKDDT-----AAILYS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1289 VSTCGRLSGVNITHRslsSLCASLKLAC----ELYPSRHVALCLDPY---CGLgfvMWTLIGVYSGHHSILIAPYEVEan 1361
Cdd:cd05911 155 SGTTGLPKGVCLSHR---NLIANLSQVQtflyGNDGSNDVILGFLPLyhiYGL---FTTLASLLNGATVIIMPKFDSE-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1362 psLWLSTLSQHRVRDTFCSYGVIElctkALSNSiPSLKQrnIDLRCVRTCVVVAEerPrvqLTQQFCKLFQALGLNTRCV 1441
Cdd:cd05911 227 --LFLDLIEKYKITFLYLVPPIAA----ALAKS-PLLDK--YDLSSLRVILSGGA--P---LSKELQELLAKRFPNATIK 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1442 StSFGC-RVNPAICVqgassaesaqvyvdmralrnnrvalvergAPNSLCVIES-GKLLPGVKVIIANPETKGHCGDSHL 1519
Cdd:cd05911 293 Q-GYGMtETGGILTV-----------------------------NPDGDDKPGSvGRLLPNVEAKIVDDDGKDSLGPNEP 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1520 GEIWVQAPHNANGYftiYGDETDYNDHFnaklvtgaTSELYARTGYLGFlrrtecsqsaslLDEttpsvasrdsdtesln 1599
Cdd:cd05911 343 GEICVRGPQVMKGY---YNNPEATKETF--------DEDGWLHTGDIGY------------FDE---------------- 383
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442629139 1600 sisqlqlnfsnvslggnsehslvggasnanDQELhdavYVVGAVDEVISLRGMNYHPIDIEnSVMRCHKKIAECAVF 1676
Cdd:cd05911 384 ------------------------------DGYL----YIVDRKKELIKYKGFQVAPAELE-AVLLEHPGVADAAVI 425
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1147-1567 |
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 442629139 1147 IAKTLTCSELHKRAEKIAALLQERGriEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITI----RPPHPQNLNTTL---- 1218
Cdd:PRK07769 52 VARDLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfdpaEPGHVGRLHAVLddct 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1219 PTVRMIVDVSKSGIVlsiqpiiKLLKSREAatsidpKTWPPILDIDDNPKRKYAGIA--TVSFDSSAYLDF-SVSTcgRL 1295
Cdd:PRK07769 130 PSAILTTTDSAEGVR-------KFFRARPA------KERPRVIAVDAVPDEVGATWVppEANEDTIAYLQYtSGST--RI 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1296 -SGVNITHRSLSSLCASLKLACEL-YPSRHVALcLDPYCGLGFVMwTLIGVYSGHHSILIAPYEVEANPSLWLSTLSqhr 1373
Cdd:PRK07769 195 pAGVQITHLNLPTNVLQVIDALEGqEGDRGVSW-LPFFHDMGLIT-VLLPALLGHYITFMSPAAFVRRPGRWIRELA--- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1374 vRDTFCSYGVIELCTK-----ALSNSIPSLKQRNIDLRCVRtCVVVAEERPRVQLTQQFCKLFQALGLNTRCVSTSFGCr 1448
Cdd:PRK07769 270 -RKPGGTGGTFSAAPNfafehAAARGLPKDGEPPLDLSNVK-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGM- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1449 VNPAICVQGASSAESAQV-YVDMRALRNNRVALVERGAPNSLCVIESGKLLPGVKVIIANPETKGHCGDSHLGEIWVQAP 1527
Cdd:PRK07769 347 AEATLFVSTTPMDEEPTViYVDRDELNAGRFVEVPADAPNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGN 426
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 442629139 1528 HNANGYftiYGDETDYNDHFNAKL--------VTGATSE-LYARTGYLG 1567
Cdd:PRK07769 427 NIGTGY---WGKPEETAATFQNILksrlseshAEGAPDDaLWVRTGDYG 472
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
474-1054 |
9.69e-18 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 88.70 E-value: 9.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 474 KVTTTLTYGKLLSRAQKIAHALstkifskgpEQVTLKPGDRVALVYPNNDplSFITAWYGCMFRGLVPLPIELplSSSDT 553
Cdd:cd05908 11 KKEKFVSYRHLREEALGYLGAL---------QELGIKPGQEVVFQITHNN--KFLYLFWACLLGGMIAVPVSI--GSNEE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 554 PPQQVGFLLSSCGITVALTSEACLKGLPkstttgeiaklkgwprlqwfvtEHLpkppkefnvgnlraddsaaAYIEYTTD 633
Cdd:cd05908 78 HKLKLNKVWNTLKNPYLITEEEVLCELA----------------------DEL-------------------AFIQFSSG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 634 KEGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYALMKLRPSSWMQLIT 713
Cdd:cd05908 117 STGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKAS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 714 KHRAS--CCLVKSRDLHWGLLATKDHKDISLSSLRMLLvaDGANPWSLSSCDQFLSVFQAKGLRSDAICPCASSSEVfTV 791
Cdd:cd05908 197 EHKATivSSPNFGYKYFLKTLKPEKANDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA-SV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 792 SLRRPGRGSCGFSPSATGRGVLsmaaLSHGVVRVDSEDSlTSLTLQDCGQVMPAAQMVVVRSEGPPVlcKTDQVGEICVT 871
Cdd:cd05908 274 GASLPKAQSPFKTITLGRRHVT----HGEPEPEVDKKDS-ECLTFVEVGKPIDETDIRICDEDNKIL--PDGYIGHIQIR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 872 SGSTSASYFgldgmtnstfkvqplleelEQPKDgngTVNIISkpigEDFYVRSGLLGflgpgglvFVcgsRDGLMTVTGR 951
Cdd:cd05908 347 GKNVTPGYY-------------------NNPEA---TAKVFT----DDGWLKTGDLG--------FI---RNGRLVITGR 389
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 952 K--------HNA--DDIIATVLAVEPmrfIYRGRIAVFSI--KVLRDERVCVIAEQRPdcSEEESFQWMSRVLQAVD--- 1016
Cdd:cd05908 390 EkdiifvngQNVypHDIERIAEELEG---VELGRVVACGVnnSNTRNEEIFCFIEHRK--SEDDFYPLGKKIKKHLNkrg 464
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 442629139 1017 --SIHQVgiyclalVPPNHLPKTPLGGIHLCEARRRFLEG 1054
Cdd:cd05908 465 gwQINEV-------LPIRRIPKTTSGKVKRYELAQRYQSG 497
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1118-1570 |
6.71e-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: 6.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1118 PQLITGVLRWRANTSPDHIIfTLLNSKGAiAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCL 1197
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADGS-EEFQSYQDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWACV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1198 YLGAIPITIRPP-----------HPQNLNTTL--PTV----RMIVDVSKSGIVLSIQPIiKLLKSREAATSIDPKTWPPi 1260
Cdd:cd05906 86 LAGFVPAPLTVPptydepnarlrKLRHIWQLLgsPVVltdaELVAEFAGLETLSGLPGI-RVLSIEELLDTAADHDLPQ- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1261 ldiddnpkrkyagiatVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLCASLKLACELYPSR---------HVAlcldpy 1331
Cdd:cd05906 164 ----------------SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDvflnwvpldHVG------ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1332 cglGFVMWTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRVRDTFC-SYgvieLCTKaLSNSIPSLKQRNIDLRCVRt 1410
Cdd:cd05906 222 ---GLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWApNF----AFAL-LNDLLEEIEDGTWDLSSLR- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1411 CVVVAEERPRVQLTQQFCKLFQALGLNTRCVSTSFGCrvnpaicvqgassAESAQVYVDMRALRNNRValvergaPNSLC 1490
Cdd:cd05906 293 YLVNAGEAVVAKTIRRLLRLLEPYGLPPDAIRPAFGM-------------TETCSGVIYSRSFPTYDH-------SQALE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1491 VIESGKLLPGVKVIIANPETKGhCGDSHLGEIWVQAPHNANGYFTiygdetdyNDHFNAKLVtgaTSELYARTGYLGFLR 1570
Cdd:cd05906 353 FVSLGRPIPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGYYN--------NPEANAEAF---TEDGWFRTGDLGFLD 420
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
439-1058 |
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 442629139 439 LSIPAGLprTLECALQRYGTNSFKSPMATVLD---PNGKVTTTLTYGKLLSRAQKIAHALstkifskgpEQVTlKPGDRV 515
Cdd:PRK12476 28 IALPPGT--TLISLIERNIANVGDTVAYRYLDhshSAAGCAVELTWTQLGVRLRAVGARL---------QQVA-GPGDRV 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 516 ALVYPNNdpLSFITAWYGCMFRGLVPLPI---ELPLSSsdtppQQVGFLLSSCGITVALTSEAClkglpKSTTTGEIAKL 592
Cdd:PRK12476 96 AILAPQG--IDYVAGFFAAIKAGTIAVPLfapELPGHA-----ERLDTALRDAEPTVVLTTTAA-----AEAVEGFLRNL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 593 KGWPRLQWFVTEHLPKPPKE-FNVGNLRADDsaAAYIEYTTDKEGSVMGVTVT-RAA------MINHCRALTMACHYteg 664
Cdd:PRK12476 164 PRLRRPRVIAIDAIPDSAGEsFVPVELDTDD--VSHLQYTSGSTRPPVGVEIThRAVgtnlvqMILSIDLLDRNTHG--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 665 etiVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYALMKlRPSSWMQ-LITKHRASCCLVKSRDLHWGLLAT----KDHKD 739
Cdd:PRK12476 239 ---VSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVR-RPQRWIKaLSEGSRTGRVVTAAPNFAYEWAAQrglpAEGDD 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 740 ISLSSLRMLLvadGANPWSLSSCDQFLSVFQAKGLRSDAICPCASSSE--VFTVSLrrpgrgscgfSPSATGRGV-LSMA 816
Cdd:PRK12476 315 IDLSNVVLII---GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEatLFVATI----------APDAEPSVVyLDRE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 817 ALSHG-VVRVDSEDSLTSLTLQdCGQVMPAAQMVVVRSEGPPVLcKTDQVGEICVTSGSTSASYFGLDGMTNSTF--KVQ 893
Cdd:PRK12476 382 QLGAGrAVRVAADAPNAVAHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFgaKLQ 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 894 PLLEELEQPkdGNGTVNIISKPIGE-DFYVRSGllgflgpgglVFVCGSRDGLMTVTGRKHNADDIIATVLAVEPMrfIY 972
Cdd:PRK12476 460 SRLAEGSHA--DGAADDGTWLRTGDlGVYLDGE----------LYITGRIADLIVIDGRNHYPQDIEATVAEASPM--VR 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 973 RGRIAVFSIKVLRDERVCVIAEQRPDCSEEESFQWMSRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRFL 1052
Cdd:PRK12476 526 RGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYL 605
|
....*.
gi 442629139 1053 EGSLHP 1058
Cdd:PRK12476 606 DGRLGV 611
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
476-890 |
3.16e-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: 3.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 476 TTTLTYGKLLSRAQKIAHALStKIFskgpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPI-------ELPL 548
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLR-KLG--------LKKGDVVGIISPNS--TYYPPVFLGCLFAGGIFSAAnpiytadELAH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 549 SSSDTPPQqvgFLLSS-CGITVALTSEACLKGLPKSTTTGeiAKLKGWPR----LQWFVTEHLPKPPKEFNVGnlrADDs 623
Cdd:cd05911 77 QLKISKPK---VIFTDpDGLEKVKEAAKELGPKDKIIVLD--DKPDGVLSiedlLSPTLGEEDEDLPPPLKDG---KDD- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 624 aAAYIEYTTDKEGSVMGVTVTRAAMINHCRALTMA--CHYTEGETIVCVLDFKREVGLWhSVLTSVLNGMHVIFIPyalm 701
Cdd:cd05911 148 -TAAILYSSGTTGLPKGVCLSHRNLIANLSQVQTFlyGNDGSNDVILGFLPLYHIYGLF-TTLASLLNGATVIIMP---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 702 KLRPSSWMQLITKHRASCCLVKSRDLHWgLLATKDHKDISLSSLRMLLVadGANPWSLSSCDQFLSVFQAKGLRSdaicp 781
Cdd:cd05911 222 KFDSELFLDLIEKYKITFLYLVPPIAAA-LAKSPLLDKYDLSSLRVILS--GGAPLSKELQELLAKRFPNATIKQ----- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 782 casssevftvslrrpgrgSCGFSPSAtgrGVLSMAalshgvvrVDSEDSLTSltlqdCGQVMPAAQMVVVRSEGPPVLcK 861
Cdd:cd05911 294 ------------------GYGMTETG---GILTVN--------PDGDDKPGS-----VGRLLPNVEAKIVDDDGKDSL-G 338
|
410 420
....*....|....*....|....*....
gi 442629139 862 TDQVGEICVTSGSTSASYFGLDGMTNSTF 890
Cdd:cd05911 339 PNEPGEICVRGPQVMKGYYNNPEATKETF 367
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1150-1428 |
6.78e-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: 6.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1150 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQnlnttlPTVRMIVDVSK 1229
Cdd:cd17651 20 RLTYAELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPA------ERLAFMLADAG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1230 SGIVLSIQPIIKLLKSREAATSidPKTWPPILDIDDNPKRkyagiATVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLC 1309
Cdd:cd17651 93 PVLVLTHPALAGELAVELVAVT--LLDQPGAAAGADAEPD-----PALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1310 ASLKLACELYPSRHVALcldpYCGLGF--VMWTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRVRDTFCSYGVIElc 1387
Cdd:cd17651 166 AWQARASSLGPGARTLQ----FAGLGFdvSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR-- 239
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 442629139 1388 tkALSNSIPSLKQRNIDLRcvrtCVVVAEERPRV-QLTQQFC 1428
Cdd:cd17651 240 --ALAEHGRPLGVRLAALR----YLLTGGEQLVLtEDLREFC 275
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
505-1056 |
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 442629139 505 EQVTlKPGDRVALVYPNNdpLSFITAWYGCMFRGlvplPIELPLSSSDTPpQQVGFL---LSSCGITVALTSEAC----- 576
Cdd:PRK07769 73 QQVT-KPGDRVAILAPQN--LDYLIAFFGALYAG----RIAVPLFDPAEP-GHVGRLhavLDDCTPSAILTTTDSaegvr 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 577 --LKGLPKSTTTGEIAkLKGWPRLqwfVTEHLPKPPkefnvgnlrADDSAAAYIEYTTDKEGSVMGVTVT-RAAMINhcr 653
Cdd:PRK07769 145 kfFRARPAKERPRVIA-VDAVPDE---VGATWVPPE---------ANEDTIAYLQYTSGSTRIPAGVQIThLNLPTN--- 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 654 ALTM--ACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPYALMKlRPSSWMQLitkhrasccLVKSRDLHWGL 731
Cdd:PRK07769 209 VLQVidALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVR-RPGRWIRE---------LARKPGGTGGT 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 732 LATK-----DH-------KD----ISLSSLRMLLvaDGANPWSLSSCDQFLSVFQAKGLRSDAICPCASSSE-VFTVSlr 794
Cdd:PRK07769 279 FSAApnfafEHaaarglpKDgeppLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEaTLFVS-- 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 795 rpgrgSCGFSPSATGRGVLSMAALSHGVVRVDsEDSLTSLTLQDCGQVMPAAQMVVV----RSEGPpvlckTDQVGEICV 870
Cdd:PRK07769 355 -----TTPMDEEPTVIYVDRDELNAGRFVEVP-ADAPNAVAQVSAGKVGVSEWAVIVdpetASELP-----DGQIGEIWL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 871 TSGSTSASYFGLDGMTNSTFKvqplleeleqpkdgngtvNIISKPIGE---------DFYVRSGLLGFLGPGGlVFVCGS 941
Cdd:PRK07769 424 HGNNIGTGYWGKPEETAATFQ------------------NILKSRLSEshaegapddALWVRTGDYGVYFDGE-LYITGR 484
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 942 RDGLMTVTGRKHNADDIIATvlAVEPMRFIYRGRIAVFSI-------KVLRD-------------ERVCVIAEQRPDCSE 1001
Cdd:PRK07769 485 VKDLVIIDGRNHYPQDLEYT--AQEATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHK 562
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*
gi 442629139 1002 EESFQWMSRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRFLEGSL 1056
Cdd:PRK07769 563 LDPQPIADDIRAAIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1152-1399 |
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 442629139 1152 TCSELHKRAEKIAALLQERGRIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQnlnttlPTVRMIVDVSKSG 1231
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1232 IVLSIQPIIKLLksREAATSIDPKTWPPILDIDDNPKRKYAGIATVSfDSSAYLDF-SVSTcGRLSGVNITHRSLSSLCA 1310
Cdd:TIGR01733 75 LLLTDSALASRL--AGLVLPVILLDPLELAALDDAPAPPPPDAPSGP-DDLAYVIYtSGST-GRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1311 SLKLACELYPsRHVALCLDPYCGLGFVM---WTLigvYSGHHSILIAPYEVEANPSLWLSTLSQHRVRDTFCSYGVIELC 1387
Cdd:TIGR01733 151 WLARRYGLDP-DDRVLQFASLSFDASVEeifGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALL 226
|
250
....*....|..
gi 442629139 1388 TKALSNSIPSLK 1399
Cdd:TIGR01733 227 AAALPPALASLR 238
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
445-1058 |
3.73e-14 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 78.67 E-value: 3.73e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 445 LPRTLECALQRYGTNSFKSPMATVLDPNGKVTTTLTYGKLLSRAQKIAHALstkifskgpeQVTLKPGDRVALVYPNNDp 524
Cdd:PRK05691 7 LPLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL----------QARASFGDRAVLLFPSGP- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 525 lSFITAWYGCMFRGLVPLPIELPLSSSDTPPQQVGFLLSSCGITVALTSEACLKGLPkstttgEIAKLKGWPRLQWFVTE 604
Cdd:PRK05691 76 -DYVAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLL------QMEELAAANAPELLCVD 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 605 HL-PKPPKEFNVGNLRADDsaAAYIEYTTDKEGSVMGVTVTRA------AMINHCRALTMachyTEGETIVCVLDFKREV 677
Cdd:PRK05691 149 TLdPALAEAWQEPALQPDD--IAFLQYTSGSTALPKGVQVSHGnlvaneQLIRHGFGIDL----NPDDVIVSWLPLYHDM 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 678 GLWHSVLTSVLNGMHVIFIPYALMKLRPSSWMQLITKHRASccLVKSRDLHWGLLatkdHKDISLSSLRML-----LVA- 751
Cdd:PRK05691 223 GLIGGLLQPIFSGVPCVLMSPAYFLERPLRWLEAISEYGGT--ISGGPDFAYRLC----SERVSESALERLdlsrwRVAy 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 752 DGANPWSLSSCDQFLSVFQAKGLRSDAICPCASSSE-VFTVSLRRPGRGscgfsPSATGrgvLSMAALSHGVVRVDSEDS 830
Cdd:PRK05691 297 SGSEPIRQDSLERFAEKFAACGFDPDSFFASYGLAEaTLFVSGGRRGQG-----IPALE---LDAEALARNRAEPGTGSV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 831 LTSltlqdCGQVMPAAQMVVVRSEGPPVLcKTDQVGEICVTSGSTSASYFGLDGMTNSTFkVQplleeleqpKDG----- 905
Cdd:PRK05691 369 LMS-----CGRSQPGHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF-VE---------HDGrtwlr 432
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 906 NGTVNIISKpiGEdfyvrsgllgflgpgglVFVCGSRDGLMTVTGRKHNADDIIATV-LAVEPMRfiyRGRIAVFSIKVL 984
Cdd:PRK05691 433 TGDLGFLRD--GE-----------------LFVTGRLKDMLIVRGHNLYPQDIEKTVeREVEVVR---KGRVAAFAVNHQ 490
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 442629139 985 RDERVCVIAE-----QRPDCSEEesfqWMSRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRFLEGSLHP 1058
Cdd:PRK05691 491 GEEGIGIAAEisrsvQKILPPQA----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDS 565
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1146-1374 |
5.09e-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: 5.09e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1146 AIA-----KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGA--IPitirpphpqnLNTTL 1218
Cdd:COG1020 492 AVAvvfgdQSLTYAELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAY 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1219 PTVR---MIVDvskSGIVLsiqpiikLLKSREAATSIdPKTWPPILDIDDNPKRKYAG---IATVSFDSSAYLDF-SVST 1291
Cdd:COG1020 561 PAERlayMLED---AGARL-------VLTQSALAARL-PELGVPVLALDALALAAEPAtnpPVPVTPDDLAYVIYtSGST 629
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1292 cGRLSGVNITHRSLSSLCASLKLACELYPSRHVALcldpYCGLGF------VMWTLIgvySGhHSILIAPYEVEANPSLW 1365
Cdd:COG1020 630 -GRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQ----FASLSFdasvweIFGALL---SG-ATLVLAPPEARRDPAAL 700
|
....*....
gi 442629139 1366 LSTLSQHRV 1374
Cdd:COG1020 701 AELLARHRV 709
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1149-1431 |
5.66e-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: 5.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1149 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQNLnttlptVRMIVDVS 1228
Cdd:cd05930 11 QSLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER------LAYILEDS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1229 KSGIVLSiqpiikllksreaatsiDPktwppildiddnpkrkyagiatvsfDSSAYLDF-SVSTcGRLSGVNITHRSLSS 1307
Cdd:cd05930 84 GAKLVLT-----------------DP-------------------------DDLAYVIYtSGST-GKPKGVMVEHRGLVN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1308 LCASLKlacELYPSRH--VALCLDPYcglGFVM--WTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRVRDTFCSYGV 1383
Cdd:cd05930 121 LLLWMQ---EAYPLTPgdRVLQFTSF---SFDVsvWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSL 194
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 442629139 1384 IELCTKALSNSipslkqrniDLRCVRTcVVVAEERPRVQLTQQFCKLF 1431
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 ... |
478-891 |
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 442629139 478 TLTYGKLLSRAQKIAHALstkifskgpEQVTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIElPLSssdtPPQQ 557
Cdd:cd05936 24 KLTYRELDALAEAFAAGL---------QNLGVQPGDRVALMLPNC--PQFPIAYFGALKAGAVVVPLN-PLY----TPRE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 558 VGFLLSSCGITVALTSEACLKGLPKSTTTGEIAKLKgwprlqwfvtehlpkppkefnvgnlrADDSAAayIEYTTdkegs 637
Cdd:cd05936 88 LEHILNDSGAKALIVAVSFTDLLAAGAPLGERVALT--------------------------PEDVAV--LQYTS----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 638 vmGVT-VTRAAMINH---------CRALtMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPyalmKLRPSS 707
Cdd:cd05936 135 --GTTgVPKGAMLTHrnlvanalqIKAW-LEDLLEGDDVVLAALPLFHVFGLTVALLLPLALGATIVLIP----RFRPIG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 708 WMQLITKHRASC-CLVKSrdLHWGLLATKDHKDISLSSLRmlLVADGANPWSLSSCDQFLSVFQAK-----GLrsdaicp 781
Cdd:cd05936 208 VLKEIRKHRVTIfPGVPT--MYIALLNAPEFKKRDFSSLR--LCISGGAPLPVEVAERFEELTGVPivegyGL------- 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 782 cassSEVftvslrrpgrgscgfSPSATGRgvlsmaaLSHGVVRVDSedsltsltlqdCGQVMPAAQMVVVRSEGPPVlcK 861
Cdd:cd05936 277 ----TET---------------SPVVAVN-------PLDGPRKPGS-----------IGIPLPGTEVKIVDDDGEEL--P 317
|
410 420 430
....*....|....*....|....*....|
gi 442629139 862 TDQVGEICVTSGSTSASYFGLDGMTNSTFK 891
Cdd:cd05936 318 PGEVGELWVRGPQVMKGYWNRPEETAEAFV 347
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1138-1534 |
7.63e-12 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 70.03 E-value: 7.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1138 FTLLNSKGAIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPItirpPHPqnlntt 1217
Cdd:PRK09192 37 MNFYDRRGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDGDFVEAFFACQYAGLVPV----PLP------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1218 LPTvrmivdvSKSGIVLSIQPIIKLLKSREAATSIDPKTWPPIL-DIDDNPKRKYAG--------------IATVSFDSS 1282
Cdd:PRK09192 106 LPM-------GFGGRESYIAQLRGMLASAQPAAIITPDELLPWVnEATHGNPLLHVLshawfkalpeadvaLPRPTPDDI 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1283 AYLDFSvSTCGRL-SGVNITHRSL-SSLCASLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYEVEA 1360
Cdd:PRK09192 179 AYLQYS-SGSTRFpRGVIITHRALmANLRAISHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFAR 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1361 NPSLWLSTLSQHRVRDTFC-SYGvIELCT-KALSNSIPSLkqrniDLRCVRTCVVVAEE-RPRVqlTQQFCKLFQALGLN 1437
Cdd:PRK09192 258 RPLQWLDLISRNRGTISYSpPFG-YELCArRVNSKDLAEL-----DLSCWRVAGIGADMiRPDV--LHQFAEAFAPAGFD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1438 TRCVSTSFGCRVNpAICVQGASSAESAQV-YVDMRALRNNRVAL--VERGAPNSLCVIeSGKLLPGVKVIIANPETKGhC 1514
Cdd:PRK09192 330 DKAFMPSYGLAEA-TLAVSFSPLGSGIVVeEVDRDRLEYQGKAVapGAETRRVRTFVN-CGKALPGHEIEIRNEAGMP-L 406
|
410 420
....*....|....*....|
gi 442629139 1515 GDSHLGEIWVQAPHNANGYF 1534
Cdd:PRK09192 407 PERVVGHICVRGPSLMSGYF 426
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1150-1312 |
1.89e-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: 1.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1150 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPqnlnttLPTVRMIVDVSK 1229
Cdd:cd12116 12 SLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1230 SGIVLSIQPIIKLLksreaatsidPKTWPPILDIDDNPKRKYAGI-ATVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSL 1308
Cdd:cd12116 85 PALVLTDDALPDRL----------PAGLPVLLLALAAAAAAPAAPrTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
....
gi 442629139 1309 CASL 1312
Cdd:cd12116 155 LHSM 158
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1129-1534 |
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 442629139 1129 ANTSPDHIIFTLLNskgaiaKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPItirp 1208
Cdd:cd05936 9 ARRFPDKTALIFMG------RKLTYRELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAGAVVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1209 phpqNLNT--TLPTVRMIVDVSKSGIVLSIQPIIKLLKSREaatsidPKTWPPILDIDDnpkrkyagIATVSFDSsayld 1286
Cdd:cd05936 78 ----PLNPlyTPRELEHILNDSGAKALIVAVSFTDLLAAGA------PLGERVALTPED--------VAVLQYTS----- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1287 fsvSTCGRLSGVNITHRSLSS-LCASLKLACELYPSRHVALCLDPY---CGLGFVMwtLIGVYSGHHSILIAPYEveanP 1362
Cdd:cd05936 135 ---GTTGVPKGAMLTHRNLVAnALQIKAWLEDLLEGDDVVLAALPLfhvFGLTVAL--LLPLALGATIVLIPRFR----P 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1363 SLWLSTLSQHRVrDTFCsyGVIELCTkALSNSiPSLKQRniDLRCVRTCV-------VVAEERPRvQLTQqfCKLFQALG 1435
Cdd:cd05936 206 IGVLKEIRKHRV-TIFP--GVPTMYI-ALLNA-PEFKKR--DFSSLRLCIsggaplpVEVAERFE-ELTG--VPIVEGYG 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1436 LnTRCVstsfgcrvnPAICVqgassaesaqvyvdmralrnNRVALVERgaPNSLcviesGKLLPGVKVIIANPETKgHCG 1515
Cdd:cd05936 276 L-TETS---------PVVAV--------------------NPLDGPRK--PGSI-----GIPLPGTEVKIVDDDGE-ELP 317
|
410
....*....|....*....
gi 442629139 1516 DSHLGEIWVQAPHNANGYF 1534
Cdd:cd05936 318 PGEVGELWVRGPQVMKGYW 336
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
445-890 |
1.91e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 68.67 E-value: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 445 LPRTLECALQRYGTnsfkspmATVLDPNGKVTTtltYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNDp 524
Cdd:PRK06187 8 IGRILRHGARKHPD-------KEAVYFDGRRTT---YAELDERVNRLANALR----ALG-----VKKGDRVAVFDWNSH- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 525 lSFITAWYGCMFRGLVPLPIELPLSssdtpPQQVGFLLSSCGITVALTSeaclkglpkSTTTGEIAKLKgwPRLQ----W 600
Cdd:PRK06187 68 -EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEDRVVLVD---------SEFVPLLAAIL--PQLPtvrtV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 601 FVTEHLPKPPKEFNVGN---LRAD------------DSAAAYIeYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGE 665
Cdd:PRK06187 131 IVEGDGPAAPLAPEVGEyeeLLAAasdtfdfpdideNDAAAML-YTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDD 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 666 T-IVCVLDFkrEVGLWHSVLTSVLNGM-HVI---FIPYALMKlrpsswmqLITKHRASCclvksrdLH-----W-GLLAT 734
Cdd:PRK06187 210 VyLVIVPMF--HVHAWGLPYLALMAGAkQVIprrFDPENLLD--------LIETERVTF-------FFavptiWqMLLKA 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 735 KDHKDISLSSLRMLLVadGANPWSLSSCDQFLSVF-----QAKGLrsdaicpcassSEvftvslrrpgrgscgfspsaTG 809
Cdd:PRK06187 273 PRAYFVDFSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGM-----------TE--------------------TS 319
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 810 rGVLSMAALSHGVVRVDSEDSLTsltlqdcGQVMPAAQMVVVRSEGPPVLCKTDQVGEICVTSGSTSASYFGLDGMTNST 889
Cdd:PRK06187 320 -PVVSVLPPEDQLPGQWTKRRSA-------GRPLPGVEARIVDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAET 391
|
.
gi 442629139 890 F 890
Cdd:PRK06187 392 I 392
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1150-1374 |
2.49e-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: 2.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1150 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAI--PITIRPPhPQNLNTTLPTVRMIVDV 1227
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAAyvPVDIDQP-AARREAILADAGARLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1228 SKSGIVLSIQPIIKLLKSREAATSidpkTWPPILDIDDNPkrkyagiatvsfDSSAYLDF-SVSTcGRLSGVNITHRSLS 1306
Cdd:cd12114 90 TDGPDAQLDVAVFDVLILDLDALA----APAPPPPVDVAP------------DDLAYVIFtSGST-GTPKGVMISHRAAL 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1307 SLCASLKLACELYPSRHVaLCLDPycgLGFVM--WTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRV 1374
Cdd:cd12114 153 NTILDINRRFAVGPDDRV-LALSS---LSFDLsvYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGV 218
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1125-1533 |
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 442629139 1125 LRWRANTSPDHIIFTLLNSkgaiakTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIpi 1204
Cdd:cd17631 1 LRRRARRHPDRTALVFGGR------SLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1205 tirpPHPQNLNTTLPTVRMIVDVSKsgivlsiqpiikllksreaatsidpktwppildiddnpkrkyagiATVSFDSSAY 1284
Cdd:cd17631 72 ----FVPLNFRLTPPEVAYILADSG---------------------------------------------AKVLFDDLAL 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1285 LDFSVSTCGRLSGVNITHRSLSSLCASLKLACELyPSRHVALCLDPYC---GLGfvMWTLIGVYSGHHSILIAPYEVEAn 1361
Cdd:cd17631 103 LMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFhigGLG--VFTLPTLLRGGTVVILRKFDPET- 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1362 pslWLSTLSQHRVRDTFCSYGVIElctkALSNSiPSLKQRniDLRCVRtCVVVAEERPRVQLTQQF----CKLFQALGLn 1437
Cdd:cd17631 179 ---VLDLIERHRVTSFFLVPTMIQ----ALLQH-PRFATT--DLSSLR-AVIYGGAPMPERLLRALqargVKFVQGYGM- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1438 TRCVstsfgcrvnPAICVQGASSAE----SAqvyvdmralrnnrvalvergapnslcviesGKLLPGVKVIIANPETKgH 1513
Cdd:cd17631 247 TETS---------PGVTFLSPEDHRrklgSA------------------------------GRPVFFVEVRIVDPDGR-E 286
|
410 420
....*....|....*....|
gi 442629139 1514 CGDSHLGEIWVQAPHNANGY 1533
Cdd:cd17631 287 VPPGEVGEIVVRGPHVMAGY 306
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
477-751 |
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 442629139 477 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIELplsssDTPPQ 556
Cdd:COG1020 500 QSLTYAELNARANRLAHHLR----ALG-----VGPGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLDP-----AYPAE 563
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 557 QVGFLLSSCGITVALTSEACLKGLPKSTTTgeiaklkgWPRLQwfvTEHLPKPPKEFNVGNLRADDsaAAYIEYT----- 631
Cdd:COG1020 564 RLAYMLEDAGARLVLTQSALAARLPELGVP--------VLALD---ALALAAEPATNPPVPVTPDD--LAYVIYTsgstg 630
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 632 TDKegsvmGVTVTRAAMINHCRALTMACHYTEGETI---------VCVLDFkrevglwhsvLTSVLNGMHVIFIPYALMk 702
Cdd:COG1020 631 RPK-----GVMVEHRALVNLLAWMQRRYGLGPGDRVlqfaslsfdASVWEI----------FGALLSGATLVLAPPEAR- 694
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 442629139 703 LRPSSWMQLITKHRASC-CLVKSrdlHWGLLAtkDHKDISLSSLRMLLVA 751
Cdd:COG1020 695 RDPAALAELLARHRVTVlNLTPS---LLRALL--DAAPEALPSLRLVLVG 739
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
480-751 |
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 442629139 480 TYGKLLSRAQKIAHALStkifskgpEQVTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIElplssSDTPPQQVG 559
Cdd:TIGR01733 1 TYRELDERANRLARHLR--------AAGGVGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLD-----PAYPAERLA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 560 FLLSSCGITVALTSEACLKGLPKSTTTGEIaklkgWPRLQWFVTEHLPKPPkefnVGNLRADDSAAAYIEYTTDKEGSVM 639
Cdd:TIGR01733 66 FILEDAGARLLLTDSALASRLAGLVLPVIL-----LDPLELAALDDAPAPP----PPDAPSGPDDLAYVIYTSGSTGRPK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 640 GVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWhSVLTSVLNGMHVIFIPYALMKLRPSSWMQLITKHRASC 719
Cdd:TIGR01733 137 GVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVE-EIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTV 215
|
250 260 270
....*....|....*....|....*....|...
gi 442629139 720 -CLVKSrdlHWGLLAtkDHKDISLSSLRMLLVA 751
Cdd:TIGR01733 216 lNLTPS---LLALLA--AALPPALASLRLVILG 243
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
442-774 |
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 442629139 442 PAGLPRTLECAlQRYGTNSFKSPMATVLDPNGKVtttLTYGKLLSRAQKIAHALSTKifSKGPEQvtlkpgdRVALVYPN 521
Cdd:PRK12316 1996 PEAYPRGPGVH-QRIAEQAARAPEAIAVVFGDQH---LSYAELDSRANRLAHRLRAR--GVGPEV-------RVAIAAER 2062
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 522 NDPLsfITAWYGCMFRG--LVPLPIELPlsssdtpPQQVGFLLSSCGITVALTSEACLKGLPKSTttgeiaklkGWPRLQ 599
Cdd:PRK12316 2063 SFEL--VVALLAVLKAGgaYVPLDPNYP-------AERLAYMLEDSGAALLLTQRHLLERLPLPA---------GVARLP 2124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 600 WFVTEHLPKPPKEFNVGNLRADDsaAAYIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGL 679
Cdd:PRK12316 2125 LDRDAEWADYPDTAPAVQLAGEN--LAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAH 2202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 680 WhSVLTSVLNGMHVIfipyalmkLRPSS-WM--QLI-TKHRASCCLVKSRDLHWGLLATKDHKDISLSSLRMLLVadGAN 755
Cdd:PRK12316 2203 E-QWFHPLLNGARVL--------IRDDElWDpeQLYdEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCF--GGE 2271
|
330
....*....|....*....
gi 442629139 756 PWSLSSCDQFLSVFQAKGL 774
Cdd:PRK12316 2272 AVPAASLRLAWEALRPVYL 2290
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
477-891 |
3.44e-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: 3.44e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 477 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNDplSFITAWYGCMFRGLVPLPIELPLSssdtpPQ 556
Cdd:cd17631 19 RSLTYAELDERVNRLAHALR----ALG-----VAKGDRVAVLSKNSP--EFLELLFAAARLGAVFVPLNFRLT-----PP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 557 QVGFLLSSCGITVALTSEACLkgLPKSTTTGeiaklkgwprlqwfvtehLPKppkefnvgnlraddsaaayieyttdkeg 636
Cdd:cd17631 83 EVAYILADSGAKVLFDDLALL--MYTSGTTG------------------RPK---------------------------- 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 637 svmGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPyalmKLRPSSWMQLITKHR 716
Cdd:cd17631 115 ---GAMLTHRNLLWNAVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILR----KFDPETVLDLIERHR 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 717 A-SCCLVKSrdLHWGLLATKDHKDISLSSLRMLLVADGANPWSLsscdqfLSVFQAKGLRsdaicpcasssevFtvslrr 795
Cdd:cd17631 188 VtSFFLVPT--MIQALLQHPRFATTDLSSLRAVIYGGAPMPERL------LRALQARGVK-------------F------ 240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 796 pgrgscgfspsATGRGvlsMAALSHGVVRVDSEDSLTslTLQDCGQVMPAAQMVVVRSEGPPVlcKTDQVGEICVTSGST 875
Cdd:cd17631 241 -----------VQGYG---MTETSPGVTFLSPEDHRR--KLGSAGRPVFFVEVRIVDPDGREV--PPGEVGEIVVRGPHV 302
|
410
....*....|....*.
gi 442629139 876 SASYFGLDGMTNSTFK 891
Cdd:cd17631 303 MAGYWNRPEATAAAFR 318
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1145-1534 |
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 442629139 1145 GAIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPphpqnlnttLPTVRMI 1224
Cdd:cd05904 27 AATGRALTYAELERRVRRLAAGLAKRG-GRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP---------LSTPAEI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1225 ---VDVSKSGIVLSIQPIIKLLKSREAATSI--DPKT-----WPPILDIDDNPKRKyagiATVSFDSSAYLDFSVSTCGR 1294
Cdd:cd05904 97 akqVKDSGAKLAFTTAELAEKLASLALPVVLldSAEFdslsfSDLLFEADEAEPPV----VVIKQDDVAALLYSSGTTGR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1295 LSGVNITHRSLSSLCASLKLACELYPSRH-VALCLDPYCGL-GFVMWTLIGVYSGHHSILIAPYEVEAnpslWLSTLSQH 1372
Cdd:cd05904 173 SKGVMLTHRNLIAMVAQFVAGEGSNSDSEdVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERY 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1373 RVRDTFCSYGVIelctKALSNSiPSLKQRniDLRCVRTCVVVAEERPRvQLTQQF------CKLFQALGLNTRCvstsfg 1446
Cdd:cd05904 249 KVTHLPVVPPIV----LALVKS-PIVDKY--DLSSLRQIMSGAAPLGK-ELIEAFrakfpnVDLGQGYGMTEST------ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1447 crvnpAICVQGASSAESaqvyvdmralrnnrvalveRGAPNSlcvieSGKLLPGVKVIIANPETKGHCGDSHLGEIWVQA 1526
Cdd:cd05904 315 -----GVVAMCFAPEKD-------------------RAKYGS-----VGRLVPNVEAKIVDPETGESLPPNQTGELWIRG 365
|
....*...
gi 442629139 1527 PHNANGYF 1534
Cdd:cd05904 366 PSIMKGYL 373
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
620-1051 |
5.39e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 60.78 E-value: 5.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 620 ADDSAAAYIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYT-EGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPY 698
Cdd:PRK07768 149 TGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGAELVKVTP 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 699 ALMKLRPSSWMQLITKHRASC--------CLVKSRdlhwgLLATKDHKDISLSSLRMLLvaDGANPWSLSSCDQFLSVFQ 770
Cdd:PRK07768 229 MDFLRDPLLWAELISKYRGTMtaapnfayALLARR-----LRRQAKPGAFDLSSLRFAL--NGAEPIDPADVEDLLDAGA 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 771 AKGLRSDAICPCASSSEV-FTVSLRRPGRG--SCGFSP---SATGRGVLSmaalSHGVVRvdsedSLTSLtlqdcGQVMP 844
Cdd:PRK07768 302 RFGLRPEAILPAYGMAEAtLAVSFSPCGAGlvVDEVDAdllAALRRAVPA----TKGNTR-----RLATL-----GPPLP 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 845 AAQMVVVRSEGPPvlCKTDQVGEICVTSGSTSASYFGLDGMTnstfkvqPLLEEleqpkDG---NGTVNIISKPiGEdfy 921
Cdd:PRK07768 368 GLEVRVVDEDGQV--LPPRGVGVIELRGESVTPGYLTMDGFI-------PAQDA-----DGwldTGDLGYLTEE-GE--- 429
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 922 vrsgllgflgpgglVFVCGSRDGLMTVTGRKHNADDIIATVLAVEPMRfiyRGRIAVFSIKV-LRDERVCVIAEQRPDCS 1000
Cdd:PRK07768 430 --------------VVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVR---PGNAVAVRLDAgHSREGFAVAVESNAFED 492
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 442629139 1001 EEESFQWMSRVLQAVDSIHQVGIYCLALVPPNHLPKTPLGGIHLCEARRRF 1051
Cdd:PRK07768 493 PAEVRRIRHQVAHEVVAEVGVRPRNVVVLGPGSIPKTPSGKLRRANAAELV 543
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1149-1307 |
7.24e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 60.40 E-value: 7.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1149 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPH-PQNL------------- 1214
Cdd:PRK05605 56 ATTTYAELGKQVRRAAAGLRALG-VRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYtAHELehpfedhgarvai 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1215 --NTTLPTVRMIVDVSKSGIVLSIQ---------------PIIKLLKSREAATSIDPKT--WPPILDIDDNPKRKYAGIA 1275
Cdd:PRK05605 135 vwDKVAPTVERLRRTTPLETIVSVNmiaampllqrlalrlPIPALRKARAALTGPAPGTvpWETLVDAAIGGDGSDVSHP 214
|
170 180 190
....*....|....*....|....*....|..
gi 442629139 1276 TVSFDSSAYLDFSVSTCGRLSGVNITHRSLSS 1307
Cdd:PRK05605 215 RPTPDDVALILYTSGTTGKPKGAQLTHRNLFA 246
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
440-754 |
7.87e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 60.30 E-value: 7.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 440 SIPAGLPRTLECALQRYGTNSfkspmATVLDPngkvtTTLTYGKLLSRAQKIAHALstkifskgpEQVTLKPGDRVALVY 519
Cdd:PRK07656 2 NEWMTLPELLARAARRFGDKE-----AYVFGD-----QRLTYAELNARVRRAAAAL---------AALGIGKGDRVAIWA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 520 PNNdpLSFITAWYGCMFRG--LVPL-----PIELP--LSSSDTPPQQV--GFLLSSCGITVALTSEACLKGLPKSTTTGE 588
Cdd:PRK07656 63 PNS--PHWVIAALGALKAGavVVPLntrytADEAAyiLARGDAKALFVlgLFLGVDYSATTRLPALEHVVICETEEDDPH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 589 IAKLKGWPRLqwfvtehLPKPPKEFNVGNLRADDSAAayIEYTTDKEGSVMGVtvtraaMINHCRALTMA---CHY---T 662
Cdd:PRK07656 141 TEKMKTFTDF-------LAAGDPAERAPEVDPDDVAD--ILFTSGTTGRPKGA------MLTHRQLLSNAadwAEYlglT 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 663 EGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPyalmKLRPSSWMQLITKHRAScCLVKSRDLHWGLLATKDHKDISL 742
Cdd:PRK07656 206 EGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP----VFDPDEVFRLIETERIT-VLPGPPTMYNSLLQHPDRSAEDL 280
|
330
....*....|..
gi 442629139 743 SSLRmLLVADGA 754
Cdd:PRK07656 281 SSLR-LAVTGAA 291
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
480-720 |
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 442629139 480 TYGKLLSRAQKIAHALSTKifskgpeqvTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIELPLSSSDTPPQqvg 559
Cdd:cd05934 5 TYAELLRESARIAAALAAL---------GIRPGDRVALMLDNC--PEFLFAWFALAKLGAVLVPINTALRGDELAYI--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 560 flLSSCGITVALTSEACLkgLPKSTTTGeiaklkgwprlqwfvtehlpkPPKefnvgnlraddsaaayieyttdkegsvm 639
Cdd:cd05934 71 --IDHSGAQLVVVDPASI--LYTSGTTG---------------------PPK---------------------------- 97
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 640 GVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIFIPyalmKLRPSSWMQLITKHRASC 719
Cdd:cd05934 98 GVVITHANLTFAGYYSARRFGLGEDDVYLTVLPLFHINAQAVSVLAALSVGATLVLLP----RFSASRFWSDVRRYGATV 173
|
.
gi 442629139 720 C 720
Cdd:cd05934 174 T 174
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
509-773 |
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 442629139 509 LKPGDRVALVYPNNDP---LSFITAWYGCMfRGLVPLPIelplsSSDTPPQQVGFLLSSCGITVALTSEACL----KGLP 581
Cdd:cd05922 15 GVRGERVVLILPNRFTyieLSFAVAYAGGR-LGLVFVPL-----NPTLKESVLRYLVADAGGRIVLADAGAAdrlrDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 582 KSTTTGEIAKLKGWPRLQWFVTEHLPKPPkefnvgnlradDSAAayIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHY 661
Cdd:cd05922 89 ASPDPGTVLDADGIRAARASAPAHEVSHE-----------DLAL--LLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 662 TEGETIVCVLDFKREVGLwhSVL-TSVLNGMHVIFIPYALMklrPSSWMQLITKHRA-SCCLVKSrdlHWGLLATKDHKD 739
Cdd:cd05922 156 TADDRALTVLPLSYDYGL--SVLnTHLLRGATLVLTNDGVL---DDAFWEDLREHGAtGLAGVPS---TYAMLTRLGFDP 227
|
250 260 270
....*....|....*....|....*....|....
gi 442629139 740 ISLSSLRMLLVADGANPwslsscDQFLSVFQAKG 773
Cdd:cd05922 228 AKLPSLRYLTQAGGRLP------QETIARLRELL 255
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1149-1534 |
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 442629139 1149 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPP-HPQNLnttlptVRMIVDV 1227
Cdd:cd05919 9 RSVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLlHPDDY------AYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1228 SKSGIVlsiqpiikllksreaatsidpktwppildiddnpkrkyagiatVSFDSSAYLDFSVSTCGRLSGVNITHRSLSs 1307
Cdd:cd05919 82 EARLVV-------------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPL- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1308 lcaslkLACELYPSRhvALCLDP----YC--------GLGFVMWtlIGVYSGHHSILIAPYEVeanPSLWLSTLSQHRVR 1375
Cdd:cd05919 118 ------LFADAMARE--ALGLTPgdrvFSsakmffgyGLGNSLW--FPLAVGASAVLNPGWPT---AERVLATLARFRPT 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1376 dtfCSYGVIELctkaLSNSIPSLKQRNIDLRCVRTCVVVAEERPRvqltqqfcKLFQALglntrcvSTSFGCRVnpaicV 1455
Cdd:cd05919 185 ---VLYGVPTF----YANLLDSCAGSPDALRSLRLCVSAGEALPR--------GLGERW-------MEHFGGPI-----L 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1456 QGASSAESAQVYVdmralrNNRVALVERGApnslcvieSGKLLPGVKVIIANPEtkGH-CGDSHLGEIWVQAPHNANGYF 1534
Cdd:cd05919 238 DGIGATEVGHIFL------SNRPGAWRLGS--------TGRPVPGYEIRLVDEE--GHtIPPGEEGDLLVRGPSAAVGYW 301
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1128-1309 |
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 442629139 1128 RANTSPDHIiftllnskgAI---AKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPI 1204
Cdd:cd12117 6 QAARTPDAV---------AVvygDRSLTYAELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1205 TIRPPHPQNlnttlptvRMIVDVSKSGIVLsiqpiikLLKSREAATSIDPKTWPPILDIDDNPKRKYAGIATVSFDSSAY 1284
Cdd:cd12117 76 PLDPELPAE--------RLAFMLADAGAKV-------LLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAY 140
|
170 180
....*....|....*....|....*
gi 442629139 1285 LDFSVSTCGRLSGVNITHRSLSSLC 1309
Cdd:cd12117 141 VMYTSGSTGRPKGVAVTHRGVVRLV 165
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1133-1573 |
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 442629139 1133 PDHIIFTLLNSKgaiAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIR----P 1208
Cdd:cd05908 1 PEGIIFILGDKK---EKFVSYRHLREEALGYLGALQELG-IKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSigsnE 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1209 PHPQNLNTtlptvrmivdvsksgivlsiqpIIKLLKSreaatsidpktwpPILDIDDNPKRKYAgiatvsfDSSAYLDFS 1288
Cdd:cd05908 77 EHKLKLNK----------------------VWNTLKN-------------PYLITEEEVLCELA-------DELAFIQFS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1289 VSTCGRLSGVNITHRSLSSLCASLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYEVEANPSLWLST 1368
Cdd:cd05908 115 SGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKK 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1369 LSQHRVRDTFC-SYGvielcTKALSNSIPSLKQRNIDLRCVRTCVVVAEerP-RVQLTQQFCKLFQALGLNTRCVSTSFG 1446
Cdd:cd05908 195 ASEHKATIVSSpNFG-----YKYFLKTLKPEKANDWDLSSIRMILNGAE--PiDYELCHEFLDHMSKYGLKRNAILPVYG 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1447 CRVNPAicvqGASSAESAQ----VYVDMRALRNN-RVALVERGAPNSLCVIESGKLLPGVKVIIANPETKGhCGDSHLGE 1521
Cdd:cd05908 268 LAEASV----GASLPKAQSpfktITLGRRHVTHGePEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LPDGYIGH 342
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 442629139 1522 IWVQAPHNANGYFTiygdetdyNDHFNAKLVtgaTSELYARTGYLGFLRRTE 1573
Cdd:cd05908 343 IQIRGKNVTPGYYN--------NPEATAKVF---TDDGWLKTGDLGFIRNGR 383
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1117-1307 |
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 442629139 1117 KPQLITGVLRWRANTSPDHIiftllnskgAIA---KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAF 1193
Cdd:PRK07656 3 EWMTLPELLARAARRFGDKE---------AYVfgdQRLTYAELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAA 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1194 YGCLYLGAIPItirPphpqnLNTTLPT-----------VRMI--------VDVSKSGIVLSIQPIIKLLKSREAATSIDP 1254
Cdd:PRK07656 73 LGALKAGAVVV---P-----LNTRYTAdeaayilargdAKALfvlglflgVDYSATTRLPALEHVVICETEEDDPHTEKM 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 442629139 1255 KTWPPILDIDDNPKRKyagiATVSFDSSAYLDFSVSTCGRLSGVNITHRSLSS 1307
Cdd:PRK07656 145 KTFTDFLAAGDPAERA----PEVDPDDVADILFTSGTTGRPKGAMLTHRQLLS 193
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1128-1491 |
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 442629139 1128 RANTSPDHIiftllnskgAIA---KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPI 1204
Cdd:cd17655 6 QAEKTPDHT---------AVVfedQTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGAYL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1205 TIRPPHPQNlnttlpTVRMIVDVSKSGIVLSIQPIIKLLKSREAATSIDPKTWPPILDIDDNPKRKyagiatvsFDSSAY 1284
Cdd:cd17655 76 PIDPDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSK--------SDDLAY 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1285 LDFSVSTCGRLSGVNITHRSLSSLCASLKLACELYPSRHVALcLDPYCGLGFVMWTLIGVYSGhHSILIAPYEVEANPSL 1364
Cdd:cd17655 142 VIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVAL-FASISFDASVTEIFASLLSG-NTLYIVRKETVLDGQA 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1365 WLSTLSQHRVRDTFCSYGVIELCTKALSNSIPSLKQrnidlrcvrtcVVVAEERPRVQLTQQFCKLFQAlglnTRCVSTS 1444
Cdd:cd17655 220 LTQYIRQNRITIIDLTPAHLKLLDAADDSEGLSLKH-----------LIVGGEALSTELAKKIIELFGT----NPTITNA 284
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1445 FGcrvnPAICVQGAS-----SAESAQVYVDM-RALRNNRVALVER-------GAPNSLCV 1491
Cdd:cd17655 285 YG----PTETTVDASiyqyePETDQQVSVPIgKPLGNTRIYILDQygrpqpvGVAGELYI 340
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1148-1374 |
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 442629139 1148 AKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQNlnttlPTVRMIVDv 1227
Cdd:PRK12316 4574 EEKLTYAELNRRANRLAHALIARG-VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE-----RLAYMMED- 4646
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1228 SKSGIVLSIQPIIKLLKSREAATSIDpktwppiLDIDD--------NPKRKYAGiatvsfDSSAYLDFSVSTCGRLSGVN 1299
Cdd:PRK12316 4647 SGAALLLTQSHLLQRLPIPDGLASLA-------LDRDEdwegfpahDPAVRLHP------DNLAYVIYTSGSTGRPKGVA 4713
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1300 ITHRSLSSLCASLKLACELYPSRHVaLCLDPYCGLGFVmWTLIGVYSGHHSILIAPyeveanPSLWLS-----TLSQHRV 1374
Cdd:PRK12316 4714 VSHGSLVNHLHATGERYELTPDDRV-LQFMSFSFDGSH-EGLYHPLINGASVVIRD------DSLWDPerlyaEIHEHRV 4785
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1121-1206 |
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 442629139 1121 ITGVLRWRANTSPDHiifTLLNSK-GAIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYL 1199
Cdd:COG1022 13 LPDLLRRRAARFPDR---VALREKeDGIWQSLTWAEFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAA 88
|
....*..
gi 442629139 1200 GAIPITI 1206
Cdd:COG1022 89 GAVTVPI 95
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1150-1374 |
1.94e-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: 1.94e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1150 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQNlnttlptvRMIVDVSK 1229
Cdd:cd17643 12 RLTYGELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVE--------RIAFILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1230 SGIVLsiqpiikllksreaatsidpktwppILDIDDNPkrkyagiatvsfdssAYLDFSVSTCGRLSGVNITHRSLSSLC 1309
Cdd:cd17643 83 SGPSL-------------------------LLTDPDDL---------------AYVIYTSGSTGRPKGVVVSHANVLALF 122
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 442629139 1310 ASLKLACELYPSRHVALCldPYCGLGFVMWTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRV 1374
Cdd:cd17643 123 AATQRWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGV 185
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1121-1210 |
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 442629139 1121 ITGVLRWRANTSPDHIiftllnskgAI---AKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCL 1197
Cdd:COG1021 27 LGDLLRRRAERHPDRI---------AVvdgERRLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALF 96
|
90
....*....|...
gi 442629139 1198 YLGAIPITIRPPH 1210
Cdd:COG1021 97 RAGAIPVFALPAH 109
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
476-717 |
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 442629139 476 TTTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIelplsSSDTPP 555
Cdd:cd05926 12 TPALTYADLAELVDDLARQLA----ALG-----IKKGDRVAIALPNG--LEFVVAFLAAARAGAVVAPL-----NPAYKK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 556 QQVGFLLSSCGITVALTSE----ACLKGLPKST-TTGEIAKLKGWPRLQWFVTE---HLPKPPKEFNVGNLRADDSaaAY 627
Cdd:cd05926 76 AEFEFYLADLGSKLVLTPKgelgPASRAASKLGlAILELALDVGVLIRAPSAESlsnLLADKKNAKSEGVPLPDDL--AL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 628 IEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTSVLNGMHVIfIPyalMKLRPSS 707
Cdd:cd05926 154 ILHTSGTTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPLFHVHGLVASLLSTLAAGGSVV-LP---PRFSAST 229
|
250
....*....|
gi 442629139 708 WMQLITKHRA 717
Cdd:cd05926 230 FWPDVRDYNA 239
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
476-751 |
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 442629139 476 TTTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIelplsSSDTPP 555
Cdd:COG0365 37 ERTLTYAELRREVNRFANALR----ALG-----VKKGDRVAIYLPNI--PEAVIAMLACARIGAVHSPV-----FPGFGA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 556 QQVGFLLSSCGITVALTS----------------EACLKGLPKSTT------TGEIAKLKGWprlQWFvTEHLPKPPKEF 613
Cdd:COG0365 101 EALADRIEDAEAKVLITAdgglrggkvidlkekvDEALEELPSLEHvivvgrTGADVPMEGD---LDW-DELLAAASAEF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 614 NVGNLRADDsaAAYIEYTtdkegSvmGVT--------VTRAAMINHcrALTMACHY--TEGETIVCVLDFKREVGLWHSV 683
Cdd:COG0365 177 EPEPTDADD--PLFILYT-----S--GTTgkpkgvvhTHGGYLVHA--ATTAKYVLdlKPGDVFWCTADIGWATGHSYIV 245
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 442629139 684 LTSVLNGMHVIFIPYALMKLRPSSWMQLITKHRASCC---------LVKsrdlhWGLLATKDHkdiSLSSLRMLLVA 751
Cdd:COG0365 246 YGPLLNGATVVLYEGRPDFPDPGRLWELIEKYGVTVFftaptairaLMK-----AGDEPLKKY---DLSSLRLLGSA 314
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1125-1208 |
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 442629139 1125 LRWRANTSPDHIIFTLLNSKGA----IAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLG 1200
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPGGRGAdgklAYDELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
....*...
gi 442629139 1201 AIPITIRP 1208
Cdd:PRK09274 91 AVPVLVDP 98
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1149-1307 |
6.36e-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: 6.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1149 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGA--IPITIRPPHPQnlnttlptVRMIVD 1226
Cdd:cd05945 15 RTLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDASSPAER--------IREILD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1227 VSKSGIVLSiqpiikllksreaatsidpktwppilDIDDNpkrkyagiatvsfdssAYLDFSVSTCGRLSGVNITHRSLS 1306
Cdd:cd05945 86 AAKPALLIA--------------------------DGDDN----------------AYIIFTSGSTGRPKGVQISHDNLV 123
|
.
gi 442629139 1307 S 1307
Cdd:cd05945 124 S 124
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1152-1208 |
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 442629139 1152 TCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRP 1208
Cdd:cd05934 5 TYAELLRESARIAAALAALG-IRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINT 60
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1149-1204 |
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 442629139 1149 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPI 1204
Cdd:COG0365 38 RTLTYAELRREVNRFANALRALG-VKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
465-577 |
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 442629139 465 MATVLDPNGkvtTTLTYGKLLSRAQKIAHALstkifskgpEQVTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPI 544
Cdd:PRK08276 1 PAVIMAPSG---EVVTYGELEARSNRLAHGL---------RALGLREGDVVAILLENN--PEFFEVYWAARRSGLYYTPI 66
|
90 100 110
....*....|....*....|....*....|...
gi 442629139 545 ELPLsssdTPPqQVGFLLSSCGITVALTSEACL 577
Cdd:PRK08276 67 NWHL----TAA-EIAYIVDDSGAKVLIVSAALA 94
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
477-759 |
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 442629139 477 TTLTYGKLLSRAQKIAHALstkifskgpEQVTLKPGDRVALVYPNNDplSFITAWYGCMFRGLVPLPIElplssSDTPPQ 556
Cdd:PRK12316 535 ETLDYAELNRRANRLAHAL---------IERGVGPDVLVGVAMERSI--EMVVALLAILKAGGAYVPLD-----PEYPAE 598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 557 QVGFLLSSCGITVALTSEACLKGLPKSTTTGEIAklkgWPRLQWFVTEHLPKPPKefnvgnLRADDSAAAYIEYTTDKEG 636
Cdd:PRK12316 599 RLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLD----LDRPAAWLEGYSEENPG------TELNPENLAYVIYTSGSTG 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 637 SVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHSVLTsVLNGMHVIFIPYALMKlRPSSWMQLITKHR 716
Cdd:PRK12316 669 KPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWP-LMSGARLVVAAPGDHR-DPAKLVELINREG 746
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 442629139 717 ASCC-LVKSrdLHWGLLatKDHKDISLSSLRMLLVADGANPWSL 759
Cdd:PRK12316 747 VDTLhFVPS--MLQAFL--QDEDVASCTSLRRIVCSGEALPADA 786
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
477-698 |
6.12e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 51.09 E-value: 6.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 477 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNDplSFITAWYGCMFRGLVPLPIELPLSssdtpPQ 556
Cdd:PRK08316 35 RSWTYAELDAAVNRVAAALL----DLG-----LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLT-----GE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 557 QVGFLLSSCGITVALTSEACLKGLPKSTTTGEIAKLkGWPR--------------LQWFVTEHLPKPPKEfnvgnlrADD 622
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPALAPTAEAALALLPVDTL-ILSLvlggreapggwldfADWAEAGSVAEPDVE-------LAD 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 623 SAAAYIEYTTDKEGSVMGvtvtraAMINHcRALT-------MACHYTEGETIVCVLDfkrevgLWHSVltsvlnGMHVIF 695
Cdd:PRK08316 171 DDLAQILYTSGTESLPKG------AMLTH-RALIaeyvsciVAGDMSADDIPLHALP------LYHCA------QLDVFL 231
|
...
gi 442629139 696 IPY 698
Cdd:PRK08316 232 GPY 234
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
478-661 |
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 442629139 478 TLTYGKLLSRAQKIAHALSTKifskgpeqvTLKPGDRVALVYPNNDPLsfITAWYGCMFRGLVPLPIElplssSDTPPQQ 557
Cdd:cd17646 23 TLTYRELDERANRLAHLLRAR---------GVGPEDRVAVLLPRSADL--VVALLAVLKAGAAYLPLD-----PGYPADR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 558 VGFLLSSCGITVALTSEACLKGLPKSTTTGEIaklkgwprLQWFVTEHLPKPPKEFnvgnlrADDSAAAYIEYTTDKEGS 637
Cdd:cd17646 87 LAYMLADAGPAVVLTTADLAARLPAGGDVALL--------GDEALAAPPATPPLVP------PRPDNLAYVIYTSGSTGR 152
|
170 180
....*....|....*....|....
gi 442629139 638 VMGVTVTRAAMINhcRALTMACHY 661
Cdd:cd17646 153 PKGVMVTHAGIVN--RLLWMQDEY 174
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1102-1210 |
7.42e-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: 7.42e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1102 EAHGRDVGLAEDcerkpQLITGVLRWRANTSPDHIIFTLLNSKgaiaktLTCSELHKRAEKIAALLQERGrIEPGDHVAL 1181
Cdd:cd05920 3 ARRYRAAGYWQD-----EPLGDLLARSAARHPDRIAVVDGDRR------LTYRELDRRADRLAAGLRGLG-IRPGDRVVV 70
|
90 100
....*....|....*....|....*....
gi 442629139 1182 IFPPGLDLLCAFYGCLYLGAIPITIRPPH 1210
Cdd:cd05920 71 QLPNVAEFVVLFFALLRLGAVPVLALPSH 99
|
|
| ARG80 |
COG5068 |
Regulator of arginine metabolism and related MADS box-containing transcription factors ... |
33-369 |
7.71e-06 |
|
Regulator of arginine metabolism and related MADS box-containing transcription factors [Transcription];
Pssm-ID: 227400 [Multi-domain] Cd Length: 412 Bit Score: 50.40 E-value: 7.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 33 EKKRAKLLQPFLKKPEGDKVKSTPPPPYYNVKNANNSTNHGnINNDG-------------VIVSSEGYSYVTEVPSLSSS 99
Cdd:COG5068 67 IEQTKAQLQKFLISVTGRKIGISYITNKTKRSVTFSKRKHG-INKKAfelsvltgtevllLVISENGLVHTFTTPKLESV 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 100 QQRHS--KKIDFHQQAAMSLSSAPQSGNAGAPGY-ENMRPQGgaVGDPGYQNTREPSAFQNQQStnnsQHRQRRTQRKVT 176
Cdd:COG5068 146 VKSLEgkSLIQSPCSNAPSDSSEEPSSSASFSVDpNDNNPMG--SFQHNGSPQTNFIPLQNPQT----QQYQQHSSRKDH 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 177 HNEKRYHSevrqeavqqalaaLKGRPkPSLPMpSKRTSVLNRSPGCNDELDSSTDDESIPEETISPDKEYNYPRDHISNS 256
Cdd:COG5068 220 PTVPHSNT-------------NNGRP-PAKFM-IPELHSSHSTLDLPSDFISDSGFPNQSSTSIFPLDSAIIQITPPHLP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 257 ILPPEPIIKPPIRESSMGSQQHARTDVKQNQiTNQKYTAPNSAP--ERRPPQNLPPLPTSEPLSSDYPPIaykreNDFSD 334
Cdd:COG5068 285 NNPPQENRHELYSNDSSMVSETPPPKNLPNG-SPNQSPLNNLSRgnPASPNSIIRENNQVEDESFNGRQG-----SAIWN 358
|
330 340 350
....*....|....*....|....*....|....*
gi 442629139 335 KAFKQKQYNAPDITQFNNAHRAADRVTRYVNVSQN 369
Cdd:COG5068 359 ALISTTQPNSGLHTEASTAPSSTIPADPLKNAAQT 393
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1150-1535 |
1.04e-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: 1.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1150 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPphpqnlnttlptvRMIVdvsk 1229
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYG-IRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDP-------------GMGR---- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1230 sgivlsiqpiikllksREAATSIDpktwppildiDDNPKrkyAGIATVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLC 1309
Cdd:cd05910 64 ----------------KNLKQCLQ----------EAEPD---AFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQI 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1310 ASLKlacELYPSRHVALCLDpycglGFVMWTLIGVYSGHHSIL-----IAPyeVEANPSLWLSTLSQHRVRDTFCSYGVI 1384
Cdd:cd05910 115 DALR---QLYGIRPGEVDLA-----TFPLFALFGPALGLTSVIpdmdpTRP--ARADPQKLVGAIRQYGVSIVFGSPALL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1385 ELCTK---ALSNSIPSLKqrnidlrcvrtCVVVAEERPRVQLTQQFCKLFQalglNTRCVSTSFGCRVNPAICVQGAssa 1461
Cdd:cd05910 185 ERVARycaQHGITLPSLR-----------RVLSAGAPVPIALAARLRKMLS----DEAEILTPYGATEALPVSSIGS--- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1462 esaqvyvdmRALRNNRVALVERGApnSLCViesGKLLPGVKVII--ANPETKGHCGDSH------LGEIWVQAPHNANGY 1533
Cdd:cd05910 247 ---------RELLATTTAATSGGA--GTCV---GRPIPGVRVRIieIDDEPIAEWDDTLelprgeIGEITVTGPTVTPTY 312
|
..
gi 442629139 1534 FT 1535
Cdd:cd05910 313 VN 314
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1119-1208 |
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 442629139 1119 QLITGVLRWRANTSPDHIifTLLNSKGAIakTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLY 1198
Cdd:cd05923 1 QTVFEMLRRAASRAPDAC--AIADPARGL--RLTYSELRARIEAVAARLHARG-LRPGQRVAVVLPNSVEAVIALLALHR 75
|
90
....*....|
gi 442629139 1199 LGAIPITIRP 1208
Cdd:cd05923 76 LGAVPALINP 85
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1116-1311 |
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 442629139 1116 RKPQL------ITGVLRWRANTSPDH--IIFtllnskgaIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGL 1187
Cdd:PRK06178 24 REPEYphgerpLTEYLRAWARERPQRpaIIF--------YGHVITYAELDELSDRFAALLRQRG-VGAGDRVAVFLPNCP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1188 DLLCAFYGCLYLGAIPITIRP-------PHPQN---------LNTTLPTVRMI--------VDVSKSGIVLSIQPIIKLL 1243
Cdd:PRK06178 95 QFHIVFFGILKLGAVHVPVSPlfrehelSYELNdagaevllaLDQLAPVVEQVraetslrhVIVTSLADVLPAEPTLPLP 174
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442629139 1244 KSREAATSIDPKTWPPILDIDDNPKRKYAGIAtvSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLCAS 1311
Cdd:PRK06178 175 DSLRAPRLAAAGAIDLLPALRACTAPVPLPPP--ALDALAALNYTGGTTGMPKGCEHTQRDMVYTAAA 240
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1150-1208 |
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 442629139 1150 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRP 1208
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALG-VGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILP 58
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
479-724 |
5.02e-05 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 48.62 E-value: 5.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 479 LTYGKLLSRAQKIAHALSTKifSKGPEQVtlkpgdrVALVYPNNdpLSFITAWYGCMFRG--LVPLPIELPlsssdtpPQ 556
Cdd:PRK12467 3121 LSYAELNRRANRLAHRLIAI--GVGPDVL-------VGVAVERS--VEMIVALLAVLKAGgaYVPLDPEYP-------RE 3182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 557 QVGFLLSSCGITVALTSEACLKGLPKST--TTGEIAKLKGWPRLqwfvtEHLPKPpkefnvgnlRADDSAAAYIEYTTDK 634
Cdd:PRK12467 3183 RLAYMIEDSGVKLLLTQAHLLEQLPAPAgdTALTLDRLDLNGYS-----ENNPST---------RVMGENLAYVIYTSGS 3248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 635 EGSVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWHsVLTSVLNGMHVIFIPYALMKlrPSSWMQLITK 714
Cdd:PRK12467 3249 TGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQER-FLWTLICGGCLVVRDNDLWD--PEELWQAIHA 3325
|
250
....*....|.
gi 442629139 715 HRAS-CCLVKS 724
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 ... |
1149-1206 |
6.54e-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: 6.54e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 442629139 1149 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITI 1206
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALG-VEPGDRVAILSRNRPEWTIADLAILAIGAVPVPI 60
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
478-650 |
7.67e-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: 7.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 478 TLTYGKLLSRAQKIAHALSTKifskgpeqvTLKPGDRVALVYPNNDPLsfITAWYGCMFRGLVPLPIElplssSDTPPQQ 557
Cdd:cd12116 12 SLSYAELDERANRLAARLRAR---------GVGPGDRVAVYLPRSARL--VAAMLAVLKAGAAYVPLD-----PDYPADR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 558 VGFLLSSCGITVALTSEACLKGLPkstttgeiAKLKGWPRLQWFVTEHLPKPPKEfnvgnlrADDSAAAYIEYTTDKEGS 637
Cdd:cd12116 76 LRYILEDAEPALVLTDDALPDRLP--------AGLPVLLLALAAAAAAPAAPRTP-------VSPDDLAYVIYTSGSTGR 140
|
170
....*....|...
gi 442629139 638 VMGVTVTRAAMIN 650
Cdd:cd12116 141 PKGVVVSHRNLVN 153
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
442-749 |
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 442629139 442 PAGLPRTLeCALQRYGTNSFKSPMATVLDPNGKvttTLTYGKLLSRAQKIAHALSTKifSKGPEQvtlkpgdRVALVYPN 521
Cdd:PRK12316 4544 DAGYPATR-CVHQLVAERARMTPDAVAVVFDEE---KLTYAELNRRANRLAHALIAR--GVGPEV-------LVGIAMER 4610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 522 NdpLSFITAWYGCMFRG--LVPLPIELPlsssdtpPQQVGFLLSSCGITVALTSEACLKGLPKSTTTGEIA-----KLKG 594
Cdd:PRK12316 4611 S--AEMMVGLLAVLKAGgaYVPLDPEYP-------RERLAYMMEDSGAALLLTQSHLLQRLPIPDGLASLAldrdeDWEG 4681
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 595 WPrlqwfvtEHLPKppkefnvgnLRADDSAAAYIEYTTDKEGSVMGVTVTRAAMINHCRALTMACHYTEGEtivCVLDFK 674
Cdd:PRK12316 4682 FP-------AHDPA---------VRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDD---RVLQFM 4742
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 675 RevglwHSVLTSVLNGMHVIFIPYALMKLRPSSW-----MQLITKHRASccLVKSRDLHWGLLATKDHKDISLSSLRMLL 749
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) ... |
477-657 |
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 442629139 477 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIElplssSDTPPQ 556
Cdd:cd17651 19 RRLTYAELDRRANRLAHRLR----ARG-----VGPGDLVALCARRS--AELVVALLAILKAGAAYVPLD-----PAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 557 QVGFLLSSCGITVALTSEACLKGLPkstttGEIAKLKGWPRLQWfVTEHLPKPPKEFNVGNLraddsaaAYIEYTTDKEG 636
Cdd:cd17651 83 RLAFMLADAGPVLVLTHPALAGELA-----VELVAVTLLDQPGA-AAGADAEPDPALDADDL-------AYVIYTSGSTG 149
|
170 180
....*....|....*....|....*
gi 442629139 637 SVMGVTVTRAAMIN----HCRALTM 657
Cdd:cd17651 150 RPKGVVMPHRSLANlvawQARASSL 174
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
477-575 |
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 442629139 477 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNndplsfITAW----YGCMFRGLVPLPIelplsSSD 552
Cdd:COG1022 39 QSLTWAEFAERVRALAAGLL----ALG-----VKPGDRVAILSDN------RPEWviadLAILAAGAVTVPI-----YPT 98
|
90 100
....*....|....*....|...
gi 442629139 553 TPPQQVGFLLSSCGITVALTSEA 575
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 ... |
646-881 |
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 442629139 646 AAMINHCRALTMA------CHYTEGETIVCVLDFKrEVGLWHSVLTSVLNGMHVIFIPyalmKLRPSSWMQLITKHRAsC 719
Cdd:cd04433 17 GVVLSHRNLLAAAaalaasGGLTEGDVFLSTLPLF-HIGGLFGLLGALLAGGTVVLLP----KFDPEAALELIEREKV-T 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 720 CLVKSRDLHWGLLATKDHKDISLSSLRMLLVadGANPWSLSSCDQFLSVFQAKGLRsdaicpcasssevftvslrrpgrg 799
Cdd:cd04433 91 ILLGVPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAPGIKLVN------------------------ 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 800 scGFSPSATGRGVLSMAALSHGVVRVDsedsltsltlqdCGQVMPAAQMVVVRSEGPPvlCKTDQVGEICVTSGSTSASY 879
Cdd:cd04433 145 --GYGLTETGGTVATGPPDDDARKPGS------------VGRPVPGVEVRIVDPDGGE--LPPGEIGELVVRGPSVMKGY 208
|
..
gi 442629139 880 FG 881
Cdd:cd04433 209 WN 210
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
478-575 |
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 442629139 478 TLTYGKLLSRAQKIAHALSTKIfskgpeqvTLKPGDRVALVYPNNDplSFITAWYGCMFRGLVPLPIeLPLsssdTPPQQ 557
Cdd:cd05958 10 EWTYRDLLALANRIANVLVGEL--------GIVPGNRVLLRGSNSP--ELVACWFGIQKAGAIAVAT-MPL----LRPKE 74
|
90
....*....|....*...
gi 442629139 558 VGFLLSSCGITVALTSEA 575
Cdd:cd05958 75 LAYILDKARITVALCAHA 92
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
477-759 |
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 442629139 477 TTLTYGKLLSRAQKIAHALStkifSKGpeqvtLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIELplsssDTPPQ 556
Cdd:cd05930 11 QSLTYAELDARANRLARYLR----ERG-----VGPGDLVAVLLERS--LEMVVAILAVLKAGAAYVPLDP-----SYPAE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 557 QVGFLLSSCGITVALTseaclkglpkstttgeiaklkgwprlqwfvtehlpkppkefnvgnlraDDSAAAYIEYTTDKEG 636
Cdd:cd05930 75 RLAYILEDSGAKLVLT------------------------------------------------DPDDLAYVIYTSGSTG 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 637 SVMGVTVTRAAMINHCRALTMACHYTEGETIVCVLDFKREVGLWhSVLTSVLNGMHVIFIPYALMKLrPSSWMQLITKHR 716
Cdd:cd05930 107 KPKGVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVW-EIFGALLAGATLVVLPEEVRKD-PEALADLLAEEG 184
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 442629139 717 ASC-CLVKSrdlHWGLLAtKDHKDISLSSLRMLLVADGANPWSL 759
Cdd:cd05930 185 ITVlHLTPS---LLRLLL-QELELAALPSLRLVLVGGEALPPDL 224
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1129-1379 |
5.12e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 44.77 E-value: 5.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1129 ANTSPDHIIFTLLnskgaiAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPItirp 1208
Cdd:PRK07786 27 ALMQPDAPALRFL------GNTTTWRELDDRVAALAGALSRRG-VGFGDRVLILMLNRTEFVESVLAANMLGAIAV---- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1209 phPQNLNTTLPTVRMIVDVSKSGIVLS-------------IQPIIKLLKSREAATSIDPKTWPPILDIDDNPKrkyaGIA 1275
Cdd:PRK07786 96 --PVNFRLTPPEIAFLVSDCGAHVVVTeaalapvatavrdIVPLLSTVVVAGGSSDDSVLGYEDLLAEAGPAH----APV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1276 TVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLCASLKLACELYPSRHVALCLDPY---CGLGFVmwtLIGVYSGHHSIL 1352
Cdd:PRK07786 170 DIPNDSPALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLfhiAGIGSM---LPGLLLGAPTVI 246
|
250 260
....*....|....*....|....*...
gi 442629139 1353 iapYEVEA-NPSLWLSTLSQHRVRDTFC 1379
Cdd:PRK07786 247 ---YPLGAfDPGQLLDVLEAEKVTGIFL 271
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1148-1375 |
6.04e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 44.95 E-value: 6.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1148 AKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQNlnttlpTVRMIVDV 1227
Cdd:PRK12316 534 EETLDYAELNRRANRLAHALIERG-VGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAE------RLAYMLED 606
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1228 SKSGIVLSIQPIIKLLKSREAATSID---PKTWPPILDiDDNPKRKYAGiatvsfDSSAYLDFSVSTCGRLSGVNITHRS 1304
Cdd:PRK12316 607 SGVQLLLSQSHLGRKLPLAAGVQVLDldrPAAWLEGYS-EENPGTELNP------ENLAYVIYTSGSTGKPKGAGNRHRA 679
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 442629139 1305 LSSLCASLKLACELYPSRHVaLCLDPYCgLGFVMWTLIGVYSGHHSILIAPYEVEANPSLWLSTLSQHRVR 1375
Cdd:PRK12316 680 LSNRLCWMQQAYGLGVGDTV-LQKTPFS-FDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVD 748
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1151-1321 |
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 442629139 1151 LTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGA--IPitirpphpqnLNTTLPTVRMIVDVS 1228
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGayVP----------LDPNYPAERLAYMLE 2097
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1229 KSGIVLsiqpiikLLKSREAATSIDPKTWPPILDIDD----------NPKRKYAGiatvsfDSSAYLDFSVSTCGRLSGV 1298
Cdd:PRK12316 2098 DSGAAL-------LLTQRHLLERLPLPAGVARLPLDRdaewadypdtAPAVQLAG------ENLAYVIYTSGSTGLPKGV 2164
|
170 180
....*....|....*....|...
gi 442629139 1299 NITHRSLSSLCASLKLACELYPS 1321
Cdd:PRK12316 2165 AVSHGALVAHCQAAGERYELSPA 2187
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1151-1202 |
7.82e-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: 7.82e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 442629139 1151 LTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAI 1202
Cdd:cd05973 1 LTFGELRALSARFANALQELG-VGPGDVVAGLLPRTPELVVTILGIWRLGAV 51
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1137-1305 |
1.00e-03 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 43.68 E-value: 1.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1137 IFTLLNSKGAIAKT-------LTCSELHKRAEKIAALLQERGRIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPp 1209
Cdd:PLN02574 46 IFSHHNHNGDTALIdsstgfsISYSELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1210 hpqnLNTTLPTVRMIVDVSKSGIVLSIQPIIKLLKSREAATSIdpktwPPILDIDDNPKRKYAGIATVSFDS-------- 1281
Cdd:PLN02574 125 ----SSSLGEIKKRVVDCSVGLAFTSPENVEKLSPLGVPVIGV-----PENYDFDSKRIEFPKFYELIKEDFdfvpkpvi 195
|
170 180
....*....|....*....|....*...
gi 442629139 1282 ----SAYLDFSVSTCGRLSGVNITHRSL 1305
Cdd:PLN02574 196 kqddVAAIMYSSGTTGASKGVVLTHRNL 223
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1150-1305 |
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 442629139 1150 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPPHPQNlnttlpTVRMIVDVSK 1229
Cdd:PRK10252 483 QFSYREMREQVVALANLLRERG-VKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDAR 555
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 442629139 1230 SGIVLSIQPIIKLLKSREAATSIDPKTWPPilDIDDNPKRKYAGiatvsfDSSAYLDFSVSTCGRLSGVNITHRSL 1305
Cdd:PRK10252 556 PSLLITTADQLPRFADVPDLTSLCYNAPLA--PQGAAPLQLSQP------HHTAYIIFTSGSTGRPKGVMVGQTAI 623
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
477-610 |
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 442629139 477 TTLTYGKLLSRAQKIAHALStkifskgpEQVTLKPGDRVALvYPNNDPlSFITAWYGCMFRGLVPLPIElPLSSSDtppq 556
Cdd:PRK08314 34 RAISYRELLEEAERLAGYLQ--------QECGVRKGDRVLL-YMQNSP-QFVIAYYAILRANAVVVPVN-PMNREE---- 98
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 442629139 557 QVGFLLSSCGITVALTSeACLkglpksttTGEIAKLKGWPRLQWFVTEH----LPKPP 610
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 ... |
479-572 |
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 442629139 479 LTYGKLLSRAQKIAHALSTKifskgpeqvTLKPGDRVALVYPNNdpLSFITAWYGCMFRGLVPLPIElPLSSSDtppqQV 558
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNK---------GVRKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----EL 65
|
90
....*....|....
gi 442629139 559 GFLLSSCGITVALT 572
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 ... |
1151-1364 |
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 442629139 1151 LTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIRPphpqnlnttlptvrmivdvsks 1230
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKG-VRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINP---------------------- 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1231 givlsiqpiikLLKSREAATsidpktwppILDiDDNPKrkyAGIATVSFDSSAYLDFSVSTCGRLSGVNITHRSLSSLCA 1310
Cdd:cd05935 59 -----------MLKERELEY---------ILN-DSGAK---VAVVGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANAL 114
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 442629139 1311 SLKLACELYPSRHVALCLDPYCGLGFVMWTLIGVYSGHHSILIAPYEVEANPSL 1364
Cdd:cd05935 115 QSAVWTGLTPSDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALEL 168
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
478-673 |
2.59e-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: 2.59e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 478 TLTYGKLLSRAQKIAHALSTKIFskGPEQVtlkpgdrVALVYPNNDPLsfITAWYGCMFRGLVPLPIElplssSDTPPQQ 557
Cdd:cd17652 12 TLTYAELNARANRLARLLAARGV--GPERL-------VALALPRSAEL--VVAILAVLKAGAAYLPLD-----PAYPAER 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 558 VGFLLSSCGITVALTSEaclkglpkstttgeiaklkgwprlqwfvtehlpkppkefnvgnlraddSAAAYIEYTTDKEGS 637
Cdd:cd17652 76 IAYMLADARPALLLTTP------------------------------------------------DNLAYVIYTSGSTGR 107
|
170 180 190
....*....|....*....|....*....|....*.
gi 442629139 638 VMGVTVTRAAMINHCRALTMACHYTEGEtivCVLDF 673
Cdd:cd17652 108 PKGVVVTHRGLANLAAAQIAAFDVGPGS---RVLQF 140
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1119-1253 |
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 442629139 1119 QLITGVLRWRANTSPDHiifTLLNSKGaiaKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLY 1198
Cdd:PRK06155 21 RTLPAMLARQAERYPDR---PLLVFGG---TRWTYAEAARAAAAAAHALAAAG-VKRGDRVALMCGNRIEFLDVFLGCAW 93
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 442629139 1199 LGAI--PITIRPPHPQnLNTTLPTVRMIVDVSKSGIVLSIQPIIKLLKSREAATSID 1253
Cdd:PRK06155 94 LGAIavPINTALRGPQ-LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAVWLLD 149
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1125-1202 |
3.50e-03 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 41.87 E-value: 3.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 442629139 1125 LRWRANTSPDHIIFTLLNskgaiaKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAI 1202
Cdd:PRK03640 8 LKQRAFLTPDRTAIEFEE------KKVTFMELHEAVVSVAGKLAALG-VKKGDRVALLMKNGMEMILVIHALQQLGAV 78
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
478-648 |
3.57e-03 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 42.46 E-value: 3.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 478 TLTYGKLLSRAQKIAHALSTKifSKGPEQVTLKPGDR-----VALvypnndpLSFITAwyGCMFrglVPLpielplsSSD 552
Cdd:PRK05691 1156 SLDYAELHAQANRLAHYLRDK--GVGPDVCVAIAAERspqllVGL-------LAILKA--GGAY---VPL-------DPD 1214
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 553 TPPQQVGFLLSSCGITVALTSEACLKGLPKSTTTGEIA----KLKGWPrlqwfvtehlPKPPkefnvgNLRADDSAAAYI 628
Cdd:PRK05691 1215 YPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSAIAldslHLDSWP----------SQAP------GLHLHGDNLAYV 1278
|
170 180
....*....|....*....|
gi 442629139 629 EYTTDKEGSVMGVTVTRAAM 648
Cdd:PRK05691 1279 IYTSGSTGQPKGVGNTHAAL 1298
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1149-1234 |
3.71e-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: 3.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 442629139 1149 KTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITIrpphpqNLNTTLPTVRMIVDVS 1228
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLG-LKPGDVVALFMENRPEYVLLWLGLVKIGAVAALI------NYNLRGESLAHCLNVS 74
|
....*.
gi 442629139 1229 KSGIVL 1234
Cdd:cd05940 75 SAKHLV 80
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1148-1206 |
6.07e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 41.41 E-value: 6.07e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 442629139 1148 AKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIPITI 1206
Cdd:PRK07798 26 DRRLTYAELEERANRLAHYLIAQG-LGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1150-1254 |
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 442629139 1150 TLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGA--IPITIRPPHPQnLNTTLP--TVRMIV 1225
Cdd:PRK09029 28 VLTWQQLCARIDQLAAGFAQQG-VVEGSGVALRGKNSPETLLAYLALLQCGArvLPLNPQLPQPL-LEELLPslTLDFAL 105
|
90 100
....*....|....*....|....*....
gi 442629139 1226 DVSKSGIVLSIQPIIKLLKSREAATSIDP 1254
Cdd:PRK09029 106 VLEGENTFSALTSLHLQLVEGAHAVAWQP 134
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1133-1203 |
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 442629139 1133 PDHIIFTLLNSKGAIAKTLTCSELHKRAEKIAALLQERGrIEPGDHVALIFPPGLDLLCAFYGCLYLGAIP 1203
Cdd:PRK13295 38 PDKTAVTAVRLGTGAPRRFTYRELAALVDRVAVGLARLG-VGRGDVVSCQLPNWWEFTVLYLACSRIGAVL 107
|
|
| |
