|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1015-1579 |
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: 801.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1015 LYMLLNAKGVAVSTATCSQLHKRAEKITAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPH-PQNLA 1093
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1094 ATLPTVRMiiDVSKAACILTTQTLIKILRSKEAAASVNVKTWPNIIDIDDLPRKRPSH-----IYKPPTAEMLAYLDFSV 1168
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKlkkwgPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1169 STTGMLTGVKISHSAVNALCRSIKLQCELYSSRQIAICMDPYCGLGFVLWCMSSVYSGHQSILIPPMELETSLPLWLSTL 1248
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1249 SQYKIRDTFCSYSVMELCTKGLGTQTEALKARGVNLSCVRSCVVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFGARV 1328
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1329 NLAICLQGTAGPDPSTVYVDMKSLRHDRVRLVERGAPQSLPLMESGTILPGVRVIIVNPETRGPLGDSHLGEIWVCSPHN 1408
Cdd:cd05905 319 NPFICWQGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEIGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1409 ASGYYTIYGEESLQADHFN-TRLSFGDTETLWARTGYLGFVRRTELLDASGDRHDALFVVGSLDETLELRGLRYHPIDIE 1487
Cdd:cd05905 399 ASGYFLLDGETNDTFKVFPsTRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVRGLRHHPSDIE 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1488 TSVSRAHRSIAESAVFTWTNLLVVVVELS-GSEQEALDLVPLVTNVVLKEHHLIVGVVVIVDPGVIPINSRGEKQRMHLR 1566
Cdd:cd05905 479 ATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNPLGEKQRMEIR 558
|
570
....*....|...
gi 1025141333 1567 DSFLADQLDPIYV 1579
Cdd:cd05905 559 QAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
354-930 |
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: 729.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 354 ALTALDITGKPLYTLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPnsDPGMFWVAFYGCLLAEVIPVPIEV 433
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVG------LKPGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 434 PLsrkdaGSQQIGFLLGSCGVGLALTSEVCLKGLPKT-----QNGEIMQFKGWPRLKWVVTDTKYLTKPSKDWQPHIPTA 508
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 509 NTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWHGVVTSVMNRIHTISVPYSVM 588
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 589 KACPLSWVQRVHVHKARVALVKCRDLHWAMM------AHRDQKDTNLSSLRMLIVADGaNPWSVSSCDAFLNVFQSHGLK 662
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLKdlsstlASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 663 PEmicpcASSPEAMTVAIRRPGAQGA--PLPARAILSMAGLSHGVIRVNTEDKNSALTVQDVGHVMPGALMCIVKPDGPP 740
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWQGTsgPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 741 mLCKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFEVIPVNSGGTPIGDVPFTRTGLLGFVGPGS----------LVFVVGK 810
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTKctdlnveehdLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 811 IEGLLSVSGRRHNADDLVATALAVEPvktvYRGRIAVFSVTvfydERIVIVAEQRPdANEEDSFQWMSRVLQAIDSIHQV 890
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPP-GSEEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 1025141333 891 GLYCLALVPANTLPKTPLGGIHVSETKQHFLEGSLHPCNI 930
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1005-1571 |
9.25e-76 |
|
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: 262.94 E-value: 9.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1005 WRAQTDPDHVLYMLLNAKGVAVSTATCSQLHKRAEKITAALLERGGinTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTV 1084
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQAVGK--PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1085 RPPHPqnlAATLPTVRMIIDVSKAACILTTQTLIKILRSKEAAASVNVKTWPNIIDIDDLPRKRPSHIyKPPTAEMLAYL 1164
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPP-PSPDPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1165 DFSVSTTGMLTGVKISHSAVNALCRSIKLQCELYSSRQIAICMDPY--CGL-GFVLwcmSSVYSGHQSILIPPMELETSL 1241
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYhdMGLiGGLL---TPLYSGGPSVLMSPAAFLRRP 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1242 PLWLSTLSQYkiRDTFcsySVM-----ELCTKglgtQTEALKARGVNLSCVRScVVIAEERPRLALTQSFSKLFKDLGLS 1316
Cdd:cd05931 232 LRWLRLISRY--RATI---SAApnfayDLCVR----RVRDEDLEGLDLSSWRV-ALNGAEPVRPATLRRFAEAFAPFGFR 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1317 PRAVSTAFG-ARVNLAICLqGTAGPDPSTVYVDMKSLRHdRVRLVERGAPQSLPLMESGTILPGVRVIIVNPETRGPLGD 1395
Cdd:cd05931 302 PEAFRPSYGlAEATLFVSG-GPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQEVRIVDPETGRELPD 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1396 SHLGEIWVCSPHNASGYytiYGEESLQADHFNTRLsfGDTETLWARTGYLGFVRRTElldasgdrhdaLFVVGSLDETLE 1475
Cdd:cd05931 380 GEVGEIWVRGPSVASGY---WGRPEATAETFGALA--ATDEGGWLRTGDLGFLHDGE-----------LYITGRLKDLII 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1476 LRGLRYHPIDIETSVSRAHRSIAESAVFTWTNL------LVVVVELSGSeQEALDLVPLVTNV---VLKEHHLIVGVVVI 1546
Cdd:cd05931 444 VRGRNHYPQDIEATAEEAHPALRPGCVAAFSVPddgeerLVVVAEVERG-ADPADLAAIAAAIraaVAREHGVAPADVVL 522
|
570 580
....*....|....*....|....*
gi 1025141333 1547 VDPGVIPINSRGEKQRMHLRDSFLA 1571
Cdd:cd05931 523 VRPGSIPRTSSGKIQRRACRAAYLD 547
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
344-921 |
1.62e-62 |
|
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: 224.04 E-value: 1.62e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 344 RWGATQAKSPALTALDITGKPLYTLTYGKLWSRSLKLAYTLLnklgtknePVLKPGDRVALVYPnsdPGM-FWVAFYGCL 422
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARLQ--------AVGKPGDRVLLLAP---PGLdFVAAFLGCL 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 423 LAEVIPVPIEVPLSRKDAgsQQIGFLLGSCGVGLALTSEVCLKGLPKTQNGeimqFKGWPRLKWVVTDTKyLTKPSKDWQ 502
Cdd:cd05931 70 YAGAIAVPLPPPTPGRHA--ERLAAILADAGPRVVLTTAAALAAVRAFAAS----RPAAGTPRLLVVDLL-PDTSAADWP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 503 PHIPTANtDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWHGVVTSVMNRIHTIS 582
Cdd:cd05931 143 PPSPDPD-DIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 583 V-PYSVMKAcPLSWVQRVHVHKARV------ALVKCrdlhwAMMAHRDQKDT-NLSSLRMLIVadGANPWSVSSCDAFLN 654
Cdd:cd05931 222 MsPAAFLRR-PLRWLRLISRYRATIsaapnfAYDLC-----VRRVRDEDLEGlDLSSWRVALN--GAEPVRPATLRRFAE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 655 VFQSHGLKPEMICPCASSPEA-MTVAIRRPGAQgaplPARAILSMAGLSHGViRVNTEDKNSALTVQDVGHVMPGALMCI 733
Cdd:cd05931 294 AFAPFGFRPEAFRPSYGLAEAtLFVSGGPPGTG----PVVLRVDRDALAGRA-VAVAADDPAARELVSCGRPLPDQEVRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 734 VKPDGPPmLCKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFEVIpvnsggTPIGDVPFTRTGLLGFVGPGSLvFVVGKIEG 813
Cdd:cd05931 369 VDPETGR-ELPDGEVGEIWVRGPSVASGYWGRPEATAETFGAL------AATDEGGWLRTGDLGFLHDGEL-YITGRLKD 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 814 LLSVSGRRHNADDLVATALAVEPVktVYRGRIAVFSVTVFYDERIVIVAEQRPDANEEDSFQWMSRVLQAIDSIHQVGLY 893
Cdd:cd05931 441 LIIVRGRNHYPQDIEATAEEAHPA--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPA 518
|
570 580
....*....|....*....|....*...
gi 1025141333 894 CLALVPANTLPKTPLGGIHVSETKQHFL 921
Cdd:cd05931 519 DVVLVRPGSIPRTSSGKIQRRACRAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1003-1477 |
2.93e-48 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 178.66 E-value: 2.93e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1003 LQWRAQTDPDHVLYMllnakGVAVSTATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPV 1082
Cdd:pfam00501 1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1083 TVRPphpqnlAATLPTVRMIIDVSKAACILTTQTLiKILRSKEAAASVNVKTWPNIIDIDDLPRKRPSHIYK-------- 1154
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDDAL-KLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAkpadvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1155 ---PPTAEMLAYLDFSVSTTGMLTGVKISHSAVNALCRSIKLQCE----LYSSRQIAICMDPYCGLGFVLWCMSSVYSGH 1227
Cdd:pfam00501 148 pppPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1228 QSILIPPMELeTSLPLWLSTLSQYKIRDTFCSYSVMELCTKGLGTQTEALKArgvnlscVRsCVVIAEERPRLALTQSFS 1307
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSS-------LR-LVLSGGAPLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1308 KLFkdlglsPRAVSTAFGARVNLAIClqgtagpdpstVYVDMKSLRHDRVRLVergapqslplmesGTILPGVRVIIVNP 1387
Cdd:pfam00501 299 ELF------GGALVNGYGLTETTGVV-----------TTPLPLDEDLRSLGSV-------------GRPLPGTEVKIVDD 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1388 ETRGPLGDSHLGEIWVCSPHNASGYytiYGEESLQADHFntrlsfgdTETLWARTGYLGFvrrtelLDASGdrhdALFVV 1467
Cdd:pfam00501 349 ETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGR------RDEDG----YLEIV 407
|
490
....*....|
gi 1025141333 1468 GSLDETLELR 1477
Cdd:pfam00501 408 GRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
999-1577 |
2.23e-40 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 164.96 E-value: 2.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 999 LSEALQWRAQTDPDHV-LYMLLNAKGVAVsTATCSQLHKRAEKITAALLERGGIntGDNVVLLYPPGIDLIASFYGCLYA 1077
Cdd:PRK05691 11 LVQALQRRAAQTPDRLaLRFLADDPGEGV-VLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1078 GCIPVTVRPP------HPQNLAAtlptvrmIIDVSKAACILTTQTLIKILRSKEAAASVNVktwPNIIDIDDLPRKRPSH 1151
Cdd:PRK05691 88 GVIAVPAYPPesarrhHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLDPALAEA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1152 IYKPP-TAEMLAYLDFSVSTTGMLTGVKISHSAVNAlcrsiklqCELYSSRQIAICMDP----------YCGLGFVLWCM 1220
Cdd:PRK05691 158 WQEPAlQPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1221 SSVYSGHQSILIPPMELETSLPLWLSTLSQYkiRDT----------FCSYSVMELCTKGLgtqtealkargvNLSCVRsc 1290
Cdd:PRK05691 230 QPIFSGVPCVLMSPAYFLERPLRWLEAISEY--GGTisggpdfayrLCSERVSESALERL------------DLSRWR-- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1291 VVIAEERP-RLALTQSFSKLFKDLGLSPRAVSTAFG-ARVNLAIClQGTAGPDPSTVYVDMKSLRHDRvrlVERGAPQsl 1368
Cdd:PRK05691 294 VAYSGSEPiRQDSLERFAEKFAACGFDPDSFFASYGlAEATLFVS-GGRRGQGIPALELDAEALARNR---AEPGTGS-- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1369 PLMESGTILPGVRVIIVNPETRGPLGDSHLGEIWVCSPHNASGYYTiYGEESLQAdhFNTRlsfgDTETlWARTGYLGFV 1448
Cdd:PRK05691 368 VLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGYWR-NPEASAKT--FVEH----DGRT-WLRTGDLGFL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1449 RRTElldasgdrhdaLFVVGSLDETLELRGLRYHPIDIETSVSRAHRSIAES--AVFTWTNL----LVVVVELSGSEQEA 1522
Cdd:PRK05691 440 RDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKGrvAAFAVNHQgeegIGIAAEISRSVQKI 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1025141333 1523 L---DLVPLVTNVVLKEHHLIVGVVVIVDPGVIPINSRGEKQRMHLRDSFLADQLDPI 1577
Cdd:PRK05691 509 LppqALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDSY 566
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1003-1575 |
4.82e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 152.02 E-value: 4.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1003 LQWRAQTDPDHVLYMLL----NAKGVAvSTATCSQLHKRAEKITAALLERGGinTGDNVVLLYPPGIDLIASFYGCLYAG 1078
Cdd:PRK05850 7 LRERASLQPDDAAFTFIdyeqDPAGVA-ETLTWSQLYRRTLNVAEELRRHGS--TGDRAVILAPQGLEYIVAFLGALQAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1079 CIPVTVRPPHPqnlAATLPTVRMIIDVSKAACILTTQTLIKILRSKEAAASVNVKtwPNIIDID--DLPRKRPSHIyKPP 1156
Cdd:PRK05850 84 LIAVPLSVPQG---GAHDERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQPGQSA--PPVIEVDllDLDSPRGSDA-RPR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1157 TAEMLAYLDFSVSTTGMLTGVKISHSAVNALCRsiKLQCELYSSRQIAICMD-------P-YCGLGFVLWCMSSVYSGHQ 1228
Cdd:PRK05850 158 DLPSTAYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMGLVLGVCAPILGGCP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1229 SILIPPMELETSLPLWlstlsqykirdtfcsysvMELCTKGLGTQTEA------LKAR--------GVNLSCVRsCVVIA 1294
Cdd:PRK05850 236 AVLTSPVAFLQRPARW------------------MQLLASNPHAFSAApnfafeLAVRktsdddmaGLDLGGVL-GIISG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1295 EERPRLALTQSFSKLFKDLGLSPRAVSTAFG---ARVNLAIclqGTAGPDPSTVYVDMKSLRHDRVR---------LVER 1362
Cdd:PRK05850 297 SERVHPATLKRFADRFAPFNLRETAIRPSYGlaeATVYVAT---REPGQPPESVRFDYEKLSAGHAKrcetgggtpLVSY 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1363 GAPQSlplmesgtilPGVRviIVNPETRGPLGDSHLGEIWVCSPHNASGYytiYGEESLQADHFNTRL---SFGDTETLW 1439
Cdd:PRK05850 374 GSPRS----------PTVR--IVDPDTCIECPAGTVGEIWVHGDNVAAGY---WQKPEETERTFGATLvdpSPGTPEGPW 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1440 ARTGYLGFVrrtelldaSGdrhDALFVVGSLDETLELRGLRYHPIDIETSV---SRAhRSIAESAVFTWTNLLVVVVEL- 1515
Cdd:PRK05850 439 LRTGDLGFI--------SE---GELFIVGRIKDLLIVDGRNHYPDDIEATIqeiTGG-RVAAISVPDDGTEKLVAIIELk 506
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025141333 1516 --SGSEQEALDLVPLVTNVVL----KEHHLIVGVVVIVDPGVIPINSRGEKQR-----MHLRDSFlaDQLD 1575
Cdd:PRK05850 507 krGDSDEEAMDRLRTVKREVTsaisKSHGLSVADLVLVAPGSIPITTSGKIRRaacveQYRQDEF--TRLD 575
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1161-1561 |
1.17e-34 |
|
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: 136.26 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1161 LAYLDFSVSTTGMLTGVKISHSAVNALCRSIkLQCELYSSRQIAICMDPYCGLGFVLWCMSSVYSGHQSILIPPMELEts 1240
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAAL-AASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPE-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1241 lpLWLSTLSQYKIRDTFCSYSVMELCTKglgtqteALKARGVNLSCVRSCVVIAEERPRlALTQSFSKLFKDlglsprAV 1320
Cdd:cd04433 79 --AALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLPP-ELLERFEEAPGI------KL 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1321 STAFGArvnlaiclqgT-AGPDPSTVYVDMKSLRHDrvrlvergapqslplmESGTILPGVRVIIVNPETrGPLGDSHLG 1399
Cdd:cd04433 143 VNGYGL----------TeTGGTVATGPPDDDARKPG----------------SVGRPVPGVEVRIVDPDG-GELPPGEIG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1400 EIWVCSPHNASGYYTiygeeslqadhfNTRLSFGDTETLWARTGYLGFVrrtelldasgDRHDALFVVGSLDETLELRGL 1479
Cdd:cd04433 196 ELVVRGPSVMKGYWN------------NPEATAAVDEDGWYRTGDLGRL----------DEDGYLYIVGRLKDMIKSGGE 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1480 RYHPIDIETSVSRaHRSIAESAVF-----TWTNLLVVVVEL-SGSEQEALDLVPLVTNVVlkEHHLIVGVVVIVDPgvIP 1553
Cdd:cd04433 254 NVYPAEVEAVLLG-HPGVAEAAVVgvpdpEWGERVVAVVVLrPGADLDAEELRAHVRERL--APYKVPRRVVFVDA--LP 328
|
....*...
gi 1025141333 1554 INSRGEKQ 1561
Cdd:cd04433 329 RTASGKID 336
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
8-129 |
7.60e-33 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 123.30 E-value: 7.60e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 8 LAALPKEVREQLAELELELSEGDITQKGYEKKRAKLLAPFVpqtqnvdvsiqltpgLSSNPTSTPNAipvaAPRQHRAHR 87
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFL---------------LHPETPTKLSA----EAQNQLASL 62
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1025141333 88 SGGTRDDRYRSDIHTEAVQAALARHKEEKMALPMPTKRRSAF 129
Cdd:pfam06464 63 ETKLRDEELSEEVYLEKVKALLAKELERENGLNAPTKEQSGL 104
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
395-925 |
1.44e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 129.85 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 395 VLKPGDRVALVYPNS-DpgmFWVAFYGCLLAEVIPVPIEVP-----LSRKDAgsqqigfLLGSCGVGLALTSEVC----- 463
Cdd:PRK07769 75 VTKPGDRVAILAPQNlD---YLIAFFGALYAGRIAVPLFDPaepghVGRLHA-------VLDDCTPSAILTTTDSaegvr 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 464 --LKGLPKTQNgeimqfkgwPRLKWV--VTDTKYLTkpskdWQPhiPTANTDT-AYIEYKASKEGTVMGVAVSKISMLTH 538
Cdd:PRK07769 145 kfFRARPAKER---------PRVIAVdaVPDEVGAT-----WVP--PEANEDTiAYLQYTSGSTRIPAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 539 CQALTQACNYCEGETLVNVLDFKKDSGLWHGVVTSVMNRIHTISVPYSVMKAcPLSWVQRVhvhkARVALVKCRDL---- 614
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMSPAAFVRR-PGRWIREL----ARKPGGTGGTFsaap 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 615 -----HWAM--MAHRDQKDTNLSSLRMLIvaDGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEAmTVAIRRPGAQG 687
Cdd:PRK07769 284 nfafeHAAArgLPKDGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEA-TLFVSTTPMDE 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 688 APlpaRAI-LSMAGLSHG-VIRVNTEDKNsALTVQDVGHVMPGALMCIVKPDGPPMLcKTDEIGEIVLNSRAGGTMYYGL 765
Cdd:PRK07769 361 EP---TVIyVDRDELNAGrFVEVPADAPN-AVAQVSAGKVGVSEWAVIVDPETASEL-PDGQIGEIWLHGNNIGTGYWGK 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 766 PGVTKNTFEVI------PVNSGGTPiGDVPFTRTGLLGFVGPGSLvFVVGKIEGLLSVSGRRHNADDLVATALavEPVKT 839
Cdd:PRK07769 436 PEETAATFQNIlksrlsESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYTAQ--EATKA 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 840 VYRGRIAVFSV-------TVFYD-------------ERIVIVAEQRPDANEEDSFQWMSRVLQAIDSIHQVGLYCLALVP 899
Cdd:PRK07769 512 LRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGVTVRDVLLVP 591
|
570 580
....*....|....*....|....*.
gi 1025141333 900 ANTLPKTPLGGIHVSETKQHFLEGSL 925
Cdd:PRK07769 592 AGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
999-1576 |
3.96e-30 |
|
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: 125.69 E-value: 3.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 999 LSEALQWRAQTDPDHVlymllnakgvAVSTA----TCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGC 1074
Cdd:COG0318 1 LADLLRRAAARHPDRP----------ALVFGgrrlTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1075 LYAGCIPVTVrpphpqNLAATLPTVRMIIDVSKAACILTtqtlikilrskeaaasvnvktwpniididdlprkrpshiyk 1154
Cdd:COG0318 70 LRAGAVVVPL------NPRLTAEELAYILEDSGARALVT----------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1155 pptaemlAYLDFSvS-TTGMLTGVKISHSAVNALCRSIKLQCELYSSRQIAICMDPYCGLGFVLWCMSSVYSGHQSILIP 1233
Cdd:COG0318 103 -------ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1234 PMELETslplWLSTLSQYKIrdTFCSYS---VMELCtkglgtqtEALKARGVNLSCVRSCVVIAEerprlALTQSFSKLF 1310
Cdd:COG0318 175 RFDPER----VLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLRLVVSGGA-----PLPPELLERF 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1311 KDLglspravstaFGARVnlaicLQG---T-AGPdpsTVYVDMKSLRHDRVRLVergapqslplmesGTILPGVRVIIVN 1386
Cdd:COG0318 236 EER----------FGVRI-----VEGyglTeTSP---VVTVNPEDPGERRPGSV-------------GRPLPGVEVRIVD 284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1387 PETRgPLGDSHLGEIWVCSPHNASGYYTiYGEEslqadhfnTRLSFGDTetlWARTGYLGFvrrtelLDASGDrhdaLFV 1466
Cdd:COG0318 285 EDGR-ELPPGEVGEIVVRGPNVMKGYWN-DPEA--------TAEAFRDG---WLRTGDLGR------LDEDGY----LYI 341
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1467 VGSLDETLELRGLRYHPIDIETSVsRAHRSIAESAVF-----TWTNLLVVVVELsgSEQEALDLVPLVTnvVLKEH---H 1538
Cdd:COG0318 342 VGRKKDMIISGGENVYPAEVEEVL-AAHPGVAEAAVVgvpdeKWGERVVAFVVL--RPGAELDAEELRA--FLRERlarY 416
|
570 580 590
....*....|....*....|....*....|....*...
gi 1025141333 1539 LIVGVVVIVDPgvIPINSRGEKQRMHLRDSFLADQLDP 1576
Cdd:COG0318 417 KVPRRVEFVDE--LPRTASGKIDRRALRERYAAGALEA 452
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1030-1576 |
1.15e-28 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 123.70 E-value: 1.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1030 TCSQLHKRAEKITAALLERGGinTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPP----HPQNLAATL----PTVrm 1101
Cdd:PRK12476 70 TWTQLGVRLRAVGARLQQVAG--PGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPelpgHAERLDTALrdaePTV-- 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1102 iidvskaacILTTQTLIKILRSKEAAASVNVKtwPNIIDIDDLPrKRPSHIYKPPTAEM--LAYLDFSVSTTGMLTGVKI 1179
Cdd:PRK12476 146 ---------VLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIP-DSAGESFVPVELDTddVSHLQYTSGSTRPPVGVEI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1180 SHSAVNALCRSIKLQCELYSSRQIAICMDP-YCGLGFVLWCMSSVYSGHqSILIPPMELETSLPLWLSTLSQ-YKIRDTF 1257
Cdd:PRK12476 214 THRAVGTNLVQMILSIDLLDRNTHGVSWLPlYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWIKALSEgSRTGRVV 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1258 CSYS--VMELCT-KGLGTQTEALKARGVNLscvrscvVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFG-ARVNLAIc 1333
Cdd:PRK12476 293 TAAPnfAYEWAAqRGLPAEGDDIDLSNVVL-------IIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGiAEATLFV- 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1334 lqGTAGPD--PSTVYVDMKSLRHDRVRLVERGAPQSLPLMESGTILPGVRVIIVNPETRGPLGDSHLGEIWVCSPHNASG 1411
Cdd:PRK12476 365 --ATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVGEIWLHGDNIGRG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1412 YYTIYGEeslqadhfnTRLSFGDT----------------ETLWARTGYLGFVRRTElldasgdrhdaLFVVGSLDETLE 1475
Cdd:PRK12476 443 YWGRPEE---------TERTFGAKlqsrlaegshadgaadDGTWLRTGDLGVYLDGE-----------LYITGRIADLIV 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1476 LRGLRYHPIDIETSVSRAHRSIAESAVFTWT------NLLVVVVELSG--SEQEALDLVPLVTNVVLKEHHLIVGVVVIV 1547
Cdd:PRK12476 503 IDGRNHYPQDIEATVAEASPMVRRGYVTAFTvpaednERLVIVAERAAgtSRADPAPAIDAIRAAVSRRHGLAVADVRLV 582
|
570 580
....*....|....*....|....*....
gi 1025141333 1548 DPGVIPINSRGEKQRMHLRDSFLADQLDP 1576
Cdd:PRK12476 583 PAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
327-923 |
2.99e-27 |
|
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: 118.54 E-value: 2.99e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 327 PLGVVSNWPPALQAALARWgATQAKSPALTALDITGKPlYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVY 406
Cdd:cd05906 1 PLHRPEGAPRTLLELLLRA-AERGPTKGITYIDADGSE-EFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 407 P-NSDpgmFWVAFYGCLLAEVIPVPIEVPLSRKDAGSQ-----QIGFLLGSCgvglaltseVCLkglpkTQNGEIMQFKG 480
Cdd:cd05906 72 DdNED---FIPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSP---------VVL-----TDAELVAEFAG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 481 ----WPRLKWVVTDTKYLTKPSKDWQPHIPTAnTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLVN 556
Cdd:cd05906 135 letlSGLPGIRVLSIEELLDTAADHDLPQSRP-DDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLN 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 557 VLDFKKDSGLWHGVVTSVMNRIHTISVPYSVMKACPLSWVQRVHVHKARV------ALVKCRDLhwamMAHRDQKDTNLS 630
Cdd:cd05906 214 WVPLDHVGGLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLNDL----LEEIEDGTWDLS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 631 SLRMLIVADGANpwSVSSCDAFLNVFQSHGLKPEMICPCasspeamtvairrpgaqgaplparaiLSMAGLSHGVI---R 707
Cdd:cd05906 290 SLRYLVNAGEAV--VAKTIRRLLRLLEPYGLPPDAIRPA--------------------------FGMTETCSGVIysrS 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 708 VNTEDKNSALTVQDVGHVMPGALMCIVKPDGPPMLckTDEIGEIVL--NSRAGGtmYYGLPGVTKNTFevipvnsggTPI 785
Cdd:cd05906 342 FPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLP--EGEVGRLQVrgPVVTKG--YYNNPEANAEAF---------TED 408
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 786 GdvpFTRTGLLGFVGPGSLVFvVGKIEGLLSVSGRRHNADDLVAtalAVEPVKTVYRGRIAVFSVTVFYDERIVIVAEQR 865
Cdd:cd05906 409 G---WFRTGDLGFLDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAETEELAIFFV 481
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025141333 866 PDANEEDSfqwMSRVLQAIDSI--HQVGLYCLALVP--ANTLPKTPLGGIHVSETKQHFLEG 923
Cdd:cd05906 482 PEYDLQDA---LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
336-911 |
7.57e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 117.74 E-value: 7.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 336 PALQAALARwgaTQAKSPALTALDITGKP---LYTLTYGKLWSRSLKLAYTLlNKLGTknepvlkPGDRVALVYPNsdpG 412
Cdd:PRK05850 4 PSLLRERAS---LQPDDAAFTFIDYEQDPagvAETLTWSQLYRRTLNVAEEL-RRHGS-------TGDRAVILAPQ---G 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 413 M-FWVAFYGCLLAEVIPVPIEVPLSRkdAGSQQIGFLLGSCGVGLALT-SEVClkglpktqnGEIMQF----KGWPRLKW 486
Cdd:PRK05850 70 LeYIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTtSAVV---------DDVTEYvapqPGQSAPPV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 487 VVTDTKYLTKPSKdwqPHIPTAN-TDTAYIEYKASKEGTVMGVAVSKISMLTHC-QALTQACNYCEGE-----TLVNVLD 559
Cdd:PRK05850 139 IEVDLLDLDSPRG---SDARPRDlPSTAYLQYTSGSTRTPAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSWLP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 560 FKKDSGLWHGVVTSVMNRIHtiSVPYSvmkacPLSWVQRvhvhKAR-VALVKCRDLHWAM-------MAHRDQKDTNLSS 631
Cdd:PRK05850 216 FYHDMGLVLGVCAPILGGCP--AVLTS-----PVAFLQR----PARwMQLLASNPHAFSAapnfafeLAVRKTSDDDMAG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 632 L---RMLIVADGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEAMT-VAIRRPGaqgapLPARAI-LSMAGLSHGVI 706
Cdd:PRK05850 285 LdlgGVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEATVyVATREPG-----QPPESVrFDYEKLSAGHA 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 707 RVNTEDKNSALtvqdVGHVMPGA-LMCIVKPDgPPMLCKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFEVIPVN-SGGTP 784
Cdd:PRK05850 360 KRCETGGGTPL----VSYGSPRSpTVRIVDPD-TCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGATLVDpSPGTP 434
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 785 IGdvPFTRTGLLGFVGPGSLvFVVGKIEGLLSVSGRRHNADDLVATalavepVKTVYRGRIAVFSVTVFYDERIVIVAE- 863
Cdd:PRK05850 435 EG--PWLRTGDLGFISEGEL-FIVGRIKDLLIVDGRNHYPDDIEAT------IQEITGGRVAAISVPDDGTEKLVAIIEl 505
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 1025141333 864 QRPDANEEDSFQWM----SRVLQAIDSIHQVGLYCLALVPANTLPKTPLGGI 911
Cdd:PRK05850 506 KKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
984-1580 |
6.97e-26 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 114.72 E-value: 6.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 984 QSRKLCVWPTnmhqfLSEALQWRAQTDPDHVLYmllNAKGVAVSTATCSQLHKRAEKITAALLERGgINTGDNVVLLYPP 1063
Cdd:PRK09192 13 LPRRYADFPT-----LVEALDYAALGEAGMNFY---DRRGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAET 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1064 GIDLIASFYGCLYAGCIPVTVrpPHPQNL---AATLPTVRMIIDVSKAACILTTQTLIKILrsKEAAASVNVKTWPNIID 1140
Cdd:PRK09192 84 DGDFVEAFFACQYAGLVPVPL--PLPMGFggrESYIAQLRGMLASAQPAAIITPDELLPWV--NEATHGNPLLHVLSHAW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1141 IDDLPRkrPSHIYKPPTAEMLAYLDFSVSTTGMLTGVKISHSAVNALCRSIK---LQCELySSRqiAICMDP-YCGLGFV 1216
Cdd:PRK09192 160 FKALPE--ADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIShdgLKVRP-GDR--CVSWLPfYHDMGLV 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1217 LWCMSSVYSGHQSILIPPMELETSLPLWLSTLSqyKIRDTFcSYSV---MELCTKGLGTQTEAlkarGVNLSCVRSCVVI 1293
Cdd:PRK09192 235 GFLLTPVATQLSVDYLPTRDFARRPLQWLDLIS--RNRGTI-SYSPpfgYELCARRVNSKDLA----ELDLSCWRVAGIG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1294 AEE-RPRlaLTQSFSKLFKDLGLSPRAVSTAFG-ARVNLAICLqgtagPDPSTvyvDMKSLRHDRVRLVERG---APQSL 1368
Cdd:PRK09192 308 ADMiRPD--VLHQFAEAFAPAGFDDKAFMPSYGlAEATLAVSF-----SPLGS---GIVVEEVDRDRLEYQGkavAPGAE 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1369 PLMES-----GTILPGVRVIIVNpETRGPLGDSHLGEIWVCSPHNASGYytiygeeslqadhfntrlsFGDTETL----- 1438
Cdd:PRK09192 378 TRRVRtfvncGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGY-------------------FRDEESQdvlaa 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1439 --WARTGYLGFvrrteLLDasGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVSR--AHRSiAESAVFTWTN----LLV 1510
Cdd:PRK09192 438 dgWLDTGDLGY-----LLD--GY----LYITGRAKDLIIINGRNIWPQDIEWIAEQepELRS-GDAAAFSIAQengeKIV 505
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1025141333 1511 VVVELSGSEQEA-LDLVPLVTNVVLKEHHLIVgVVVIVDPGVIPINSRGEKQRMHLRDSFLADQLDPIYVA 1580
Cdd:PRK09192 506 LLVQCRISDEERrGQLIHALAALVRSEFGVEA-AVELVPPHSLPRTSSGKLSRAKAKKRYLSGAFASLDVA 575
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
368-927 |
1.16e-25 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 113.95 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 368 LTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVyPNSDPGmFWVAFYGCLLAEVIPVPIEVPLS--RKDAGSQQI 445
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLA-LG------LKPGDRVALI-AETDGD-FVEAFFACQYAGLVPVPLPLPMGfgGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 446 GFLLGSCGVGLALTSEVCLKGLPKTQNGEimqfkgwpRLKWVVTDTKYLTKPSKDWQPHIPTANtDTAYIEYKASKEGTV 525
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGN--------PLLHVLSHAWFKALPEADVALPRPTPD-DIAYLQYSSGSTRFP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 526 MGVAVSKISMLTHCQALTQ-ACNYCEGETLVNVLDFKKDSGLWHGVVTSVMNRihtISVPYS-----VMKacPLSWVQRV 599
Cdd:PRK09192 192 RGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQ---LSVDYLptrdfARR--PLQWLDLI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 600 HVHKARVALVKC--RDLHWAMMAHRDQKDTNLSSLRmlIVADGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEAmT 677
Cdd:PRK09192 267 SRNRGTISYSPPfgYELCARRVNSKDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEA-T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 678 VAirrpgaqgaplparaiLSMAGLSHGvIRVNT------EDKNSALTVQD----------VGHVMPGALMCIVKPDGppm 741
Cdd:PRK09192 344 LA----------------VSFSPLGSG-IVVEEvdrdrlEYQGKAVAPGAetrrvrtfvnCGKALPGHEIEIRNEAG--- 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 742 lcktdeigeIVLNSRAGGTMYYGLPGVTKNTFE------VIPVNSggtpigdvpFTRTGLLGFVGPGSLVfVVGKIEGLL 815
Cdd:PRK09192 404 ---------MPLPERVVGHICVRGPSLMSGYFRdeesqdVLAADG---------WLDTGDLGYLLDGYLY-ITGRAKDLI 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 816 SVSGRRHNADDLVATALAVEPVKTvyrGRIAVFSVTVFYDERIVIVAEQRPdANEEDSFQWMSRVLQAIDSIHqvGLYCL 895
Cdd:PRK09192 465 IINGRNIWPQDIEWIAEQEPELRS---GDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAA 538
|
570 580 590
....*....|....*....|....*....|...
gi 1025141333 896 -ALVPANTLPKTPLGGIHVSETKQHFLEGSLHP 927
Cdd:PRK09192 539 vELVPPHSLPRTSSGKLSRAKAKKRYLSGAFAS 571
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
335-927 |
1.33e-24 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 110.99 E-value: 1.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 335 PPA--LQAALARWGATQAKSPALTALDITGKPLYT---LTYGKLWSRslklaytlLNKLGTKNEPVLKPGDRVALVYPNs 409
Cdd:PRK12476 31 PPGttLISLIERNIANVGDTVAYRYLDHSHSAAGCaveLTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQ- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 410 dpGMFWVA-FYGCLLAEVIPVPI---EVP--LSRKDAgsqqigfLLGSCGVGLALTSEVC-------LKGLPKTQNgeim 476
Cdd:PRK12476 102 --GIDYVAgFFAAIKAGTIAVPLfapELPghAERLDT-------ALRDAEPTVVLTTTAAaeavegfLRNLPRLRR---- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 477 qfkgwPRLKWV--VTDTKyltkpSKDWQPhIPTANTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETL 554
Cdd:PRK12476 169 -----PRVIAIdaIPDSA-----GESFVP-VELDTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 555 -VNVLDFKKDSGLWHGVVTSVMNRIHTISVPYSVMKAcPLSWVQRVHV--HKARVaLVKCRDLHWAMMAHR----DQKDT 627
Cdd:PRK12476 238 gVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAFVRR-PQRWIKALSEgsRTGRV-VTAAPNFAYEWAAQRglpaEGDDI 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 628 NLSSLRMLIvadGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEA-MTVAIRRPGAQgaplPARAILSMAGLSHG-V 705
Cdd:PRK12476 316 DLSNVVLII---GSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYGIAEAtLFVATIAPDAE----PSVVYLDREQLGAGrA 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 706 IRVNTEDKNSALTVQdVGHVMPGALMCIVKPDGPPMLcKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFEV-----IPVNS 780
Cdd:PRK12476 389 VRVAADAPNAVAHVS-CGQVARSQWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGS 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 781 --GGTPIGDVPFtRTGLLGFVGPGSLvFVVGKIEGLLSVSGRRHNADDLVATALAVEPVktVYRGRIAVFSVTVFYDERI 858
Cdd:PRK12476 467 haDGAADDGTWL-RTGDLGVYLDGEL-YITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERL 542
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1025141333 859 VIVAEQRPDANEEDSFQWMSRVLQAIDSIHQVGLYCLALVPANTLPKTPLGGIHVSETKQHFLEGSLHP 927
Cdd:PRK12476 543 VIVAERAAGTSRADPAPAIDAIRAAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1003-1574 |
5.78e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 109.05 E-value: 5.78e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1003 LQWRAQTDPDHVLYMLLN----AKGVAVSTaTCSQLHKRAEKITAALLERGgiNTGDNVVLLYPPGIDLIASFYGCLYAG 1078
Cdd:PRK07769 27 VERWAKVRGDKLAYRFLDfsteRDGVARDL-TWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAG 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1079 CIPVTV----RPPHPQNLAATLptvrmiiDVSKAACILTTQtlikilrskEAAASVN-------VKTWPNIIDIDDLPRK 1147
Cdd:PRK07769 104 RIAVPLfdpaEPGHVGRLHAVL-------DDCTPSAILTTT---------DSAEGVRkffrarpAKERPRVIAVDAVPDE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1148 RPShIYKPPTA--EMLAYLDFSVSTTGMLTGVKISHSAV--NAL--CRSIKLQcelYSSRQIAiCMDPYCGLGFVLWCMS 1221
Cdd:PRK07769 168 VGA-TWVPPEAneDTIAYLQYTSGSTRIPAGVQITHLNLptNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGLITVLLP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1222 SVYSGHQSILIPPMELETslPL-WLSTLSQyKIRDTFCSYSV-----MELCTkglgtqtealkARGV--------NLSCV 1287
Cdd:PRK07769 243 ALLGHYITFMSPAAFVRR--PGrWIRELAR-KPGGTGGTFSAapnfaFEHAA-----------ARGLpkdgepplDLSNV 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1288 RsCVVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFG-ARVNLAIclqGTAGPD--PSTVYVDMKSLRHDRVRLVERGA 1364
Cdd:PRK07769 309 K-GLLNGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGmAEATLFV---STTPMDeePTVIYVDRDELNAGRFVEVPADA 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1365 PQSLPLMESGTILPGVRVIIVNPETRGPLGDSHLGEIWVCSPHNASGYYTiYGEESLQADH--FNTRLSFGDTE-----T 1437
Cdd:PRK07769 385 PNAVAQVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWG-KPEETAATFQniLKSRLSESHAEgapddA 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1438 LWARTGYLGFVRRTElldasgdrhdaLFVVGSLDETLELRGLRYHPIDIETSVSRAHRSI--------------AESAVF 1503
Cdd:PRK07769 464 LWVRTGDYGVYFDGE-----------LYITGRVKDLVIIDGRNHYPQDLEYTAQEATKALrtgyvaafsvpanqLPQVVF 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1504 TWTNL------------LVVVVELS-GSEQeaLDLVPLVTNV---VLKEHHLIVGVVVIVDPGVIPINSRGEKQRMHLRD 1567
Cdd:PRK07769 533 DDSHAglkfdpedtseqLVIVAERApGAHK--LDPQPIADDIraaIAVRHGVTVRDVLLVPAGSIPRTSSGKIARRACRA 610
|
....*..
gi 1025141333 1568 SFLADQL 1574
Cdd:PRK07769 611 AYLDGSL 617
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1030-1546 |
1.27e-23 |
|
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: 106.53 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1030 TCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIpvtVRPPHPQNLAATLptVRMIiDVSKAA 1109
Cdd:cd05911 12 TYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGGI---FSAANPIYTADEL--AHQL-KISKPK 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1110 CILTTQTLIKILRSKEAAASVNVKTW---------PNIIDIDDLPRKRPSHIYKPP---TAEMLAYLDFSVSTTGMLTGV 1177
Cdd:cd05911 85 VIFTDPDGLEKVKEAAKELGPKDKIIvlddkpdgvLSIEDLLSPTLGEEDEDLPPPlkdGKDDTAAILYSSGTTGLPKGV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1178 KISHS---AVNALCRSIKLQCELYSSRQIA-ICMDPYCGLGFVLWCMssvYSGHQSILIPPMELETslplWLSTLSQYKI 1253
Cdd:cd05911 165 CLSHRnliANLSQVQTFLYGNDGSNDVILGfLPLYHIYGLFTTLASL---LNGATVIIMPKFDSEL----FLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1254 RDTFCSYSVMELctkgLGTQTEALKArgvNLSCVRSCVVIAeerprlaltqsfSKLFKDLGlspravsTAFGARVNLAIC 1333
Cdd:cd05911 238 TFLYLVPPIAAA----LAKSPLLDKY---DLSSLRVILSGG------------APLSKELQ-------ELLAKRFPNATI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1334 LQG---T-AGPdPSTVYVDmkslrhdrvRLVERGApqslplmeSGTILPGVRVIIVNPETRGPLGDSHLGEIWVCSPHNA 1409
Cdd:cd05911 292 KQGygmTeTGG-ILTVNPD---------GDDKPGS--------VGRLLPNVEAKIVDDDGKDSLGPNEPGEICVRGPQVM 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1410 SGYYTiyGEESlqadhfnTRLSFgdTETLWARTGYLGFVrrtelldasgDRHDALFVVGSLDETLELRGLRYHPIDIEtS 1489
Cdd:cd05911 354 KGYYN--NPEA-------TKETF--DEDGWLHTGDIGYF----------DEDGYLYIVDRKKELIKYKGFQVAPAELE-A 411
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025141333 1490 VSRAHRSIAESAVF-----TWTNLLVVVVELSGSEQ-EALDLVPLVTNVVLKEHHLIVGVVVI 1546
Cdd:cd05911 412 VLLEHPGVADAAVIgipdeVSGELPRAYVVRKPGEKlTEKEVKDYVAKKVASYKQLRGGVVFV 474
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
999-1569 |
2.23e-23 |
|
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: 106.60 E-value: 2.23e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 999 LSEALQWRAQTDPD-HVLYMLLNAKGVAVSTAtcsQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYA 1077
Cdd:cd05906 12 LLELLLRAAERGPTkGITYIDADGSEEFQSYQ---DLLEDARRL-AAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1078 GCIPVTVRPPHPQNLAAtlPTVRMIIDVSK---AACILTTQTLIKILRSKEAAASVNVKTwpnIIDIDDLPRKRPSHIYK 1154
Cdd:cd05906 88 GFVPAPLTVPPTYDEPN--ARLRKLRHIWQllgSPVVLTDAELVAEFAGLETLSGLPGIR---VLSIEELLDTAADHDLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1155 PPTAEMLAYLDFSVSTTGMLTGVKISHSAVNALCRSiKLQCELYSSRQIA---ICMDPYCGLGFVlwCMSSVYSGHQSIL 1231
Cdd:cd05906 163 QSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG-KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLGCQQVH 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1232 IPPMELETSLPLWLSTLSQYKIRDTFCSYSvmeLCTKgLGTQTEALKARGVNLSCVRsCVVIAEERPRLALTQSFSKLFK 1311
Cdd:cd05906 240 VPTEEILADPLRWLDLIDRYRVTITWAPNF---AFAL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRLLRLLE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1312 DLGLSPRAVSTAFGARVNLAIClqgtagpdpsTVYVDMKSLRHdrvrlvergaPQSLPLMESGTILPGVRVIIVNPETrG 1391
Cdd:cd05906 315 PYGLPPDAIRPAFGMTETCSGV----------IYSRSFPTYDH----------SQALEFVSLGRPIPGVSMRIVDDEG-Q 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1392 PLGDSHLGEIWVCSPHNASGYytiYGEESLQADHFntrlsfgdTETLWARTGYLGFVrrtelldasgdRHDALFVVGSLD 1471
Cdd:cd05906 374 LLPEGEVGRLQVRGPVVTKGY---YNNPEANAEAF--------TEDGWFRTGDLGFL-----------DNGNLTITGRTK 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1472 ETLELRGLRYHPIDIETSVSRA----HRSIAESAVF---TWTNLLVVVVELSGSEQEALD-LVPLVTNVVLKEHHLIVGV 1543
Cdd:cd05906 432 DTIIVNGVNYYSHEIEAAVEEVpgvePSFTAAFAVRdpgAETEELAIFFVPEYDLQDALSeTLRAIRSVVSREVGVSPAY 511
|
570 580
....*....|....*....|....*.
gi 1025141333 1544 VVIVDPGVIPINSRGEKQRMHLRDSF 1569
Cdd:cd05906 512 LIPLPKEEIPKTSLGKIQRSKLKAAF 537
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
338-925 |
1.07e-22 |
|
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440087 [Multi-domain] Cd Length: 452 Bit Score: 103.35 E-value: 1.07e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 338 LQAALARWGATQAKSPALTALDITgkplytLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNSdPGMFwVA 417
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLA-AALRALG------VGPGDRVALLLPNS-PEFV-VA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 418 FYGCLLAEVIPVPIEVPLSRKdagsqQIGFLLGSCGVGLALTSEVCL----KGLPKtqngeimqfkgwprlkwvvtdtky 493
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSGARALVTALILYtsgtTGRPK------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 494 ltkpskdwqphiptantdtayieykaskegtvmGVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWHGVVTS 573
Cdd:COG0318 117 ---------------------------------GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 574 VMNRIHTISVPYSVmkacPLSWVQRVHVHKA-RVALVKcrDLHWAMMAHRDQKDTNLSSLRMLIVadGANPWSVSSCDAF 652
Cdd:COG0318 164 LLAGATLVLLPRFD----PERVLELIERERVtVLFGVP--TMLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERF 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 653 LNVFQSHglkpemICPC-ASSpEAMTVAIRRPGAQGAPLPARailsmaglshgvirvntedknsaltvqdVGHVMPGALM 731
Cdd:COG0318 236 EERFGVR------IVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEV 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 732 CIVKPDGPPmlCKTDEIGEIVLnsRAGGTM--YYGLPGVTKNTFEvipvnsGGtpigdvpFTRTGLLGFVGPGSLVFVVG 809
Cdd:COG0318 281 RIVDEDGRE--LPPGEVGEIVV--RGPNVMkgYWNDPEATAEAFR------DG-------WLRTGDLGRLDEDGYLYIVG 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 810 KIEGLLSVSGRRHNADDLVATALAVEPVKTVyrgriAVFSVTV-FYDERIV--IVAEQRPDANEEDSFQWMSRVL---QA 883
Cdd:COG0318 344 RKKDMIISGGENVYPAEVEEVLAAHPGVAEA-----AVVGVPDeKWGERVVafVVLRPGAELDAEELRAFLRERLaryKV 418
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 1025141333 884 IDSIHQVGlyclalvpanTLPKTPLGGIHVSETKQHFLEGSL 925
Cdd:COG0318 419 PRRVEFVD----------ELPRTASGKIDRRALRERYAAGAL 450
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1030-1502 |
1.44e-19 |
|
amino acid adenylation domain; This model represents a domain responsible for the specific recognition of amino acids and activation as adenylyl amino acids. The reaction catalyzed is aa + ATP -> aa-AMP + PPi. These domains are usually found as components of multi-domain non-ribosomal peptide synthetases and are usually called "A-domains" in that context. A-domains are almost invariably followed by "T-domains" (thiolation domains, pfam00550) to which the amino acid adenylate is transferred as a thiol-ester to a bound pantetheine cofactor with the release of AMP (these are also called peptide carrier proteins, or PCPs. When the A-domain does not represent the first module (corresponding to the first amino acid in the product molecule) it is usually preceded by a "C-domain" (condensation domain, pfam00668) which catalyzes the ligation of two amino acid thiol-esters from neighboring modules. This domain is a subset of the AMP-binding domain found in Pfam (pfam00501) which also hits substrate--CoA ligases and luciferases. Sequences scoring in between trusted and noise for this model may be ambiguous as to whether they activate amino acids or other molecules lacking an alpha amino group.
Pssm-ID: 273779 [Multi-domain] Cd Length: 409 Bit Score: 93.10 E-value: 1.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1030 TCSQLHKRAEKITAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQnlaatlPTVRMIIDVSKAA 1109
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPA------ERLAFILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1110 CILTTQTLIKILRSKEAAASVNVKTWPNIIDiDDLPRKRPSHiykPPTAEMLAYLDFSVSTTGMLTGVKISHSAVNALCR 1189
Cdd:TIGR01733 75 LLLTDSALASRLAGLVLPVILLDPLELAALD-DAPAPPPPDA---PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1190 SIKlQCELYSSRQIAICMDPYCGLGFVLWCMSSVYSGHQSILIPPMELETSLPLWLSTLSQYKIRDTFCSYSVMELCTKG 1269
Cdd:TIGR01733 151 WLA-RRYGLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAAA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1270 LGTQTEALKArgvnlscvrscVVIAEERPRLALTQSFSKLFKDLGLspravstafgarVNlaiclqgTAGPDPSTVYVDM 1349
Cdd:TIGR01733 230 LPPALASLRL-----------VILGGEALTPALVDRWRARGPGARL------------IN-------LYGPTETTVWSTA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1350 KSLRHDRVRLVErgapqSLPLmesGTILPGVRVIIVNPETRgPLGDSHLGEIWVCSPHNASGYytiYGEESLQADHFNTR 1429
Cdd:TIGR01733 280 TLVDPDDAPRES-----PVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGY---LNRPELTAERFVPD 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1025141333 1430 LSFGDTETLWARTGYLgfVRRtelldasgdRHD-ALFVVGSLDETLELRGLRYHPIDIEtSVSRAHRSIAESAV 1502
Cdd:TIGR01733 348 PFAGGDGARLYRTGDL--VRY---------LPDgNLEFLGRIDDQVKIRGYRIELGEIE-AALLRHPGVREAVV 409
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
335-927 |
1.37e-18 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 93.31 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 335 PPALQAALARWGATQAKSPALTALDITGKPLYTLTYGKLWSRSLKLAYTLLNKLGtknepvlkPGDRVALVYPnSDPGmF 414
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARAS--------FGDRAVLLFP-SGPD-Y 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 415 WVAFYGCLLAEVIPVPIEVPLSRKDAGSQQIGFLLGSCGVGLALTSEVCLKGLpktQNGEIMQFKGWPrlKWVVTDTkYL 494
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSL---LQMEELAAANAP--ELLCVDT-LD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 495 TKPSKDWQ-PHIPTanTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEG--ETLVNVLDFKKDSGLWHGVV 571
Cdd:PRK05691 152 PALAEAWQePALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNpdDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 572 TSVMNRIHTISVPYSVMKACPLSWVQRVHVHKARVAlvKCRDLHWAMMAHRdQKDTNLSSL---RMLIVADGANPWSVSS 648
Cdd:PRK05691 230 QPIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTIS--GGPDFAYRLCSER-VSESALERLdlsRWRVAYSGSEPIRQDS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 649 CDAFLNVFQSHGLKPEMICPCASSPEA-MTVAIRRPGaQGAPLPAraiLSMAGLSHgvirvNTEDKNSALTVQDVGHVMP 727
Cdd:PRK05691 307 LERFAEKFAACGFDPDSFFASYGLAEAtLFVSGGRRG-QGIPALE---LDAEALAR-----NRAEPGTGSVLMSCGRSQP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 728 GALMCIVKPDGPPMLcKTDEIGEIVLNSRAGGTMYYGLPGVTKNTFevipVNSGGTpigdvPFTRTGLLGFVGPGSLvFV 807
Cdd:PRK05691 378 GHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGDLGFLRDGEL-FV 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 808 VGKIEGLLSVSGRRHNADDLVATalAVEPVKTVYRGRIAVFSVTVFYDERIVIVAE-----QRPDANEEdsfqWMSRVLQ 882
Cdd:PRK05691 447 TGRLKDMLIVRGHNLYPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPPQA----LIKSIRQ 520
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1025141333 883 AIDSIHQVGLYCLALVPANTLPKTPLGGIHVSETKQHFLEGSLHP 927
Cdd:PRK05691 521 AVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDS 565
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
350-828 |
1.64e-18 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 90.06 E-value: 1.64e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 350 AKSPALTALDITGKplYTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNSdPGMFwVAFYGCLLAEVIPV 429
Cdd:pfam00501 6 ARTPDKTALEVGEG--RRLTYRELDERANRLAAGLR-ALG------VGKGDRVAILLPNS-PEWV-VAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 430 PIEVplsrkDAGSQQIGFLLGSCGVGLALTSEVCL--KGLPKTQNGEIMQFKGW-PRLKWVVTDTKYLTKPSKDWQPHIP 506
Cdd:pfam00501 75 PLNP-----RLPAEELAYILEDSGAKVLITDDALKleELLEALGKLEVVKLVLVlDRDPVLKEEPLPEEAKPADVPPPPP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 507 TANT--DTAYIEYKASKEGTVMGVavskisMLTHCQALTQACN----------YCEGETLVNVLDFKKDSGLWHGVVTSV 574
Cdd:pfam00501 150 PPPDpdDLAYIIYTSGTTGKPKGV------MLTHRNLVANVLSikrvrprgfgLGPDDRVLSTLPLFHDFGLSLGLLGPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 575 MNRiHTISVPYSVMKACPLSWVQRVHVHKARV-----ALVKcrdlhwAMMAHRDQKDTNLSSLRMLIVadGANPWSVSSC 649
Cdd:pfam00501 224 LAG-ATVVLPPGFPALDPAALLELIERYKVTVlygvpTLLN------MLLEAGAPKRALLSSLRLVLS--GGAPLPPELA 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 650 DAFLNVF-----QSHGLKpEMiCPCASSPEAMTVAIRRPGAQGAPLParailsmaglshgvirvNTEdknsaltvqdvgh 724
Cdd:pfam00501 295 RRFRELFggalvNGYGLT-ET-TGVVTTPLPLDEDLRSLGSVGRPLP-----------------GTE------------- 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 725 vmpgalMCIVKPDG----PPmlcktDEIGEIVLNSRAGGTMYYGLPGVTKNTFevipVNSGgtpigdvpFTRTGLLGFVG 800
Cdd:pfam00501 343 ------VKIVDDETgepvPP-----GEPGELCVRGPGVMKGYLNDPELTAEAF----DEDG--------WYRTGDLGRRD 399
|
490 500
....*....|....*....|....*...
gi 1025141333 801 PgslvfvvgkiEGLLSVSGRrhnADDLV 828
Cdd:pfam00501 400 E----------DGYLEIVGR---KKDQI 414
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1032-1571 |
2.94e-17 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 87.13 E-value: 2.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1032 SQLHKRAEKITAALLERGGINTgdnVVLLYPPGIDLIASFYGCLYAG----CIPVTVRPPHPQNLAATLPTVRMIIDVSK 1107
Cdd:PRK05851 35 PEVHGRAENVAARLLDRDRPGA---VGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWADATLTRFAGIGVRT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1108 aacILTTQTLIKILRSKEAAASVNvktwpniiDIDDLPRKRPSHIYKPPTAEMLAYLDFSVSTTGMLTGVKISHSAVNAL 1187
Cdd:PRK05851 112 ---VLSHGSHLERLRAVDSSVTVH--------DLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1188 CRSIKLQCELYSSRQIAICMDPY---CGLGFVLwcmSSVYSGHQSILIPPMELETSLPLWLSTLSQYkiRDTFCSYSVME 1264
Cdd:PRK05851 181 LRGLNARVGLDAATDVGCSWLPLyhdMGLAFLL---TAALAGAPLWLAPTTAFSASPFRWLSWLSDS--RATLTAAPNFA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1265 LCTKGlgtqTEALKARGVNLSCVRsCVVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFGarvnLAICLQGTAGPDPST 1344
Cdd:PRK05851 256 YNLIG----KYARRVSDVDLGALR-VALNGGEPVDCDGFERFATAMAPFGFDAGAAAPSYG----LAESTCAVTVPVPGI 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1345 vyvdmkSLRHDRVRLVERGAPQSLPLMesGTILPGVRVIIVNPETRGPLGDSHLGEIWVCSPHNASGYytiYGEESLQAD 1424
Cdd:PRK05851 327 ------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRGASMMSGY---LGQAPIDPD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1425 HfntrlsfgdtetlWARTGYLGFvrrteLLDasgdrhDALFVVGSLDETLELRGLRYHPIDIETSVS--RAHRSIAESAV 1502
Cdd:PRK05851 396 D-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTEIERVAAqvRGVREGAVVAV 451
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1025141333 1503 FTWTNL----LVVVVELSGSEQ-----EALDLVPLVTNVVLKEhhlivgvVVIVDPGVIPINSRGEKQRMHLRDSFLA 1571
Cdd:PRK05851 452 GTGEGSarpgLVIAAEFRGPDEagarsEVVQRVASECGVVPSD-------VVFVAPGSLPRTSSGKLRRLAVKRSLEA 522
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1024-1507 |
1.39e-15 |
|
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: 81.03 E-value: 1.39e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1024 VAV----STATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLaatlptV 1099
Cdd:cd05930 4 VAVvdgdQSLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAER------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1100 RMIIDVSKAACILTTqtlikilrskeaaasvnvktwpniididdlprkrPSHiykpptaemLAYLDFSVSTTGMLTGVKI 1179
Cdd:cd05930 77 AYILEDSGAKLVLTD----------------------------------PDD---------LAYVIYTSGSTGKPKGVMV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1180 SHSAVNALCRSIKLQCELYSSRQIAICMdpycGLGFV--LWCM-SSVYSGHQSILIPPmELETSLPLWLSTLSQYKIRDT 1256
Cdd:cd05930 114 EHRGLVNLLLWMQEAYPLTPGDRVLQFT----SFSFDvsVWEIfGALLAGATLVVLPE-EVRKDPEALADLLAEEGITVL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1257 FCSYSVMELCTKGLGTQtealkargvNLSCVRsCVVIAEERPRLALTQSFSKLFKDLGLspravstafgarVNLAiclqg 1336
Cdd:cd05930 189 HLTPSLLRLLLQELELA---------ALPSLR-LVLVGGEALPPDLVRRWRELLPGARL------------VNLY----- 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1337 taGPDPSTVYVDMKSLRHDRVrlvergAPQSLPLmesGTILPGVRVIIVNPETRgPLGDSHLGEIWVCSPHNASGYytiY 1416
Cdd:cd05930 242 --GPTEATVDATYYRVPPDDE------EDGRVPI---GRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLARGY---L 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1417 GEESLQADHFnTRLSFGDTETLWaRTGYLgfVRRtellDASGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVsRAHRS 1496
Cdd:cd05930 307 NRPELTAERF-VPNPFGPGERMY-RTGDL--VRW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEAAL-LAHPG 373
|
490
....*....|.
gi 1025141333 1497 IAESAVFTWTN 1507
Cdd:cd05930 374 VREAAVVARED 384
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1024-1519 |
9.15e-13 |
|
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: 72.71 E-value: 9.15e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1024 VAVS----TATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPqnlaatLPTV 1099
Cdd:cd12116 4 TAVRdddrSLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1100 RMIIDVSKAACILTTQTLikilrskEAAASVNVKTWPNIIDIDDLPRKRPShiyKPPTAEMLAYLDFSVSTTGMLTGVKI 1179
Cdd:cd12116 77 RYILEDAEPALVLTDDAL-------PDRLPAGLPVLLLALAAAAAAPAAPR---TPVSPDDLAYVIYTSGSTGRPKGVVV 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1180 SHSAVNALCRSIKLQCELYSSRQIA----ICMDpycglgfvlwcMSSvysghqsilippmeLETSLPLWlstlsqykird 1255
Cdd:cd12116 147 SHRNLVNFLHSMRERLGLGPGDRLLavttYAFD-----------ISL--------------LELLLPLL----------- 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1256 tfcSYSVMELCTKGLGTQTEALKARgvnlscvrscvvIAEERPRLA-LTQSFSKLFKDLGLSPRAVSTAF-GAR---VNL 1330
Cdd:cd12116 191 ---AGARVVIAPRETQRDPEALARL------------IEAHSITVMqATPATWRMLLDAGWQGRAGLTALcGGEalpPDL 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1331 AICLQGTA-------GPDPSTVYvdmkSLRHdRVRLVERGAPQSLPlmesgtiLPGVRVIIVNPETRgPLGDSHLGEIWV 1403
Cdd:cd12116 256 AARLLSRVgslwnlyGPTETTIW----STAA-RVTAAAGPIPIGRP-------LANTQVYVLDAALR-PVPPGVPGELYI 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1404 CSPHNASGYytiYGEESLQADHFnTRLSFGDTETLWARTGYLgfVRRtelldasgDRHDALFVVGSLDETLELRGLRYHP 1483
Cdd:cd12116 323 GGDGVAQGY---LGRPALTAERF-VPDPFAGPGSRLYRTGDL--VRR--------RADGRLEYLGRADGQVKIRGHRIEL 388
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1025141333 1484 IDIETSVsRAHRSIAESAVFTWTN----LLVVVVELSGSE 1519
Cdd:cd12116 389 GEIEAAL-AAHPGVAQAAVVVREDggdrRLVAYVVLKAGA 427
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1007-1528 |
2.29e-12 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 71.12 E-value: 2.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1007 AQTDPDHVLYMLLNAkgvavsTATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGC--IPVTV 1084
Cdd:cd05945 1 AAANPDRPAVVEGGR------TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1085 RPPHPQnlaatlptVRMIIDVSKAACILTTQtlikilrskeaaasvnvktwpniidiDDlprkrpshiykpptaemLAYL 1164
Cdd:cd05945 74 SSPAER--------IREILDAAKPALLIADG--------------------------DD-----------------NAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1165 DFSVSTTGMLTGVKISHSAVNALCRSIkLQCELYSSRQIAIC----------MDPYCGL--GFVLWCMSsvysghQSILI 1232
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNqapfsfdlsvMDLYPALasGATLVPVP------RDATA 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1233 PPMELETSLP-----LWLSTLsqykirdtfcsySVMELCTkGLGTQTEAlkargvNLSCVRSCVVIAEERPrLALTQSFS 1307
Cdd:cd05945 176 DPKQLFRFLAehgitVWVSTP------------SFAAMCL-LSPTFTPE------SLPSLRHFLFCGEVLP-HKTARALQ 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1308 KLFkdlglsPravstafGARV-NlaiclqgTAGPDPSTVYVdmksLRHDRVRLVERGAPqSLPLmesGTILPGVRVIIVN 1386
Cdd:cd05945 236 QRF------P-------DARIyN-------TYGPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVILD 287
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1387 PETRgPLGDSHLGEIWVCSPHNASGYytiYGEESLQADHFntrlsFGDTETLWARTGYLGFvrrtelLDASGdrhdALFV 1466
Cdd:cd05945 288 EDGR-PVPPGEKGELVISGPSVSKGY---LNNPEKTAAAF-----FPDEGQRAYRTGDLVR------LEADG----LLFY 348
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1025141333 1467 VGSLDETLELRGLRYHPIDIETSVsRAHRSIAESAVFTWTNL-----LVVVVELSGSEqEALDLVPL 1528
Cdd:cd05945 349 RGRLDFQVKLNGYRIELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKPGA-EAGLTKAI 413
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1030-1502 |
5.52e-12 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 70.34 E-value: 5.52e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1030 TCSQLHKRAEKITAALLERGGINtGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPphpqnlAATLPTVRMIIDVSKAA 1109
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRK-GDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSGAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1110 CILTTQTLIKILRSkeAAASVnvktwpniIDIDDLPrKRPSHIYK---------PPTAEM----LAYLDFSVSTTGMLTG 1176
Cdd:cd05904 107 LAFTTAELAEKLAS--LALPV--------VLLDSAE-FDSLSFSDllfeadeaePPVVVIkqddVAALLYSSGTTGRSKG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1177 VKISH-SAVNALCRSIKLQCELYSSRQIAICMDPYCGL-GFVLWCMSSVYSGHQSILIPPMELETslplWLSTLSQYKIR 1254
Cdd:cd05904 176 VMLTHrNLIAMVAQFVAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERYKVT 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1255 DTFCSYSVMELCTKGlgtqtealkargvnlscvrscvVIAEERPRLALTQSFSklfkdlGLSP--RAVSTAFGARVNLAI 1332
Cdd:cd05904 252 HLPVVPPIVLALVKS----------------------PIVDKYDLSSLRQIMS------GAAPlgKELIEAFRAKFPNVD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1333 CLQG----TAGPDPSTVYVDMKSlrhdrvrlveRGAPQSlplmeSGTILPGVRVIIVNPETRGPLGDSHLGEIWVCSPHN 1408
Cdd:cd05904 304 LGQGygmtESTGVVAMCFAPEKD----------RAKYGS-----VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1409 ASGYytiygeeslqadhfntrlsFGDTE----TL----WARTGYLGFVrrtellDASGDrhdaLFVVGSLDETLELRGLR 1480
Cdd:cd05904 369 MKGY-------------------LNNPEataaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKGFQ 419
|
490 500
....*....|....*....|..
gi 1025141333 1481 YHPIDIEtSVSRAHRSIAESAV 1502
Cdd:cd05904 420 VAPAELE-ALLLSHPEILDAAV 440
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
359-819 |
7.44e-12 |
|
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: 69.55 E-value: 7.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 359 DITGKplyTLTYGKLWSRSLKLAYTLlNKLGtknepvLKPGDRVALVYPNSDpgMFWVAFYGCLLAEVIPVPI------- 431
Cdd:cd05911 5 ADTGK---ELTYAQLRTLSRRLAAGL-RKLG------LKKGDVVGIISPNST--YYPPVFLGCLFAGGIFSAAnpiytad 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 432 EVPLSRKDAGSQqigFLLgscgvglaltseVCLKGLPKTQNgeimQFKGWPRLK--WVVTDTK-YLTKPSKDWQPHIPT- 507
Cdd:cd05911 73 ELAHQLKISKPK---VIF------------TDPDGLEKVKE----AAKELGPKDkiIVLDDKPdGVLSIEDLLSPTLGEe 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 508 ----------ANTDTAYIEYKASKEGTVMGVAVS---KISMLTHCQALTQAcNYCEGETLVNVLDFKKDSGLWhGVVTSV 574
Cdd:cd05911 134 dedlppplkdGKDDTAAILYSSGTTGLPKGVCLShrnLIANLSQVQTFLYG-NDGSNDVILGFLPLYHIYGLF-TTLASL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 575 MNRIHTIsvpysVM-KACPLSWVQRVHVHKARVALVKCRdlHWAMMAHRDQKDT-NLSSLRMLIVadGANPWSVSSCDAF 652
Cdd:cd05911 212 LNGATVI-----IMpKFDSELFLDLIEKYKITFLYLVPP--IAAALAKSPLLDKyDLSSLRVILS--GGAPLSKELQELL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 653 LNVF------QSHGLKpEMICPCASSPEAmtvaIRRPGAqgaplparailsmaglshgvirvntedknsaltvqdVGHVM 726
Cdd:cd05911 283 AKRFpnatikQGYGMT-ETGGILTVNPDG----DDKPGS------------------------------------VGRLL 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 727 PGALMCIVKPDGPPMLcKTDEIGEIVLNsraGGTM---YYGLPGVTKNTFEvipvnSGGtpigdvpFTRTGLLGFVGPGS 803
Cdd:cd05911 322 PNVEAKIVDDDGKDSL-GPNEPGEICVR---GPQVmkgYYNNPEATKETFD-----EDG-------WLHTGDIGYFDEDG 385
|
490
....*....|....*.
gi 1025141333 804 LVFVVGKIEGLLSVSG 819
Cdd:cd05911 386 YLYIVDRKKELIKYKG 401
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1030-1564 |
5.90e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 66.94 E-value: 5.90e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1030 TCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCiPVTV--RPPHPQNLAA----TLPTVRMIi 1103
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAG-VGPGDAVAVLAGAPVEIAPTAQGLWMRGA-SLTMlhQPTPRTDLAVwaedTLRVIGMI- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1104 dvSKAACILTTQTlikilrskEAAASVNVKTWPNIIDIDDLPRKRPshIYKPPTAE-MLAYLDFSVSTTGMLTGVKISH- 1181
Cdd:PRK07768 108 --GAKAVVVGEPF--------LAAAPVLEEKGIRVLTVADLLAADP--IDPVETGEdDLALMQLTSGSTGSPKAVQITHg 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1182 ---SAVNALCRSIKLQCElyssRQIAICMDPYC-GLGFVLWCMSSVYSGHQSILIPPMELETSLPLWLSTLSQYKIRDTF 1257
Cdd:PRK07768 176 nlyANAEAMFVAAEFDVE----TDVMVSWLPLFhDMGMVGFLTVPMYFGAELVKVTPMDFLRDPLLWAELISKYRGTMTA 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1258 CSYSVMELCTKGLGTQTEAlkaRGVNLSCVRsCVVIAEERPRLALTQSFSKLFKDLGLSPRAVSTAFG-ARVNLAICLQG 1336
Cdd:PRK07768 252 APNFAYALLARRLRRQAKP---GAFDLSSLR-FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGmAEATLAVSFSP 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1337 T-AGPDPSTVYVDMKSLRHdRVRLVERGAPQSLPLMesGTILPGVRVIIVNpETRGPLGDSHLGEIWVCSPHNASGYYTI 1415
Cdd:PRK07768 328 CgAGLVVDEVDADLLAALR-RAVPATKGNTRRLATL--GPPLPGLEVRVVD-EDGQVLPPRGVGVIELRGESVTPGYLTM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1416 YGEESLQADHfntrlsfGdtetlWARTGYLGFvrrtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVSRAH- 1494
Cdd:PRK07768 404 DGFIPAQDAD-------G-----WLDTGDLGY------LTEEGE----VVVCGRVKDVIIMAGRNIYPTDIERAAARVEg 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1495 -RSIAESAVFTWTNL----LVVVVE--LSGSEQEALDLVPLVTNVVLKEhhliVGV----VVIVDPGVIPINSRGEKQRM 1563
Cdd:PRK07768 462 vRPGNAVAVRLDAGHsregFAVAVEsnAFEDPAEVRRIRHQVAHEVVAE----VGVrprnVVVLGPGSIPKTPSGKLRRA 537
|
.
gi 1025141333 1564 H 1564
Cdd:PRK07768 538 N 538
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
336-774 |
1.54e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 65.59 E-value: 1.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 336 PALQAALARWGATqaKSPALTALDITGKplyTLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSDpgMFW 415
Cdd:PRK06187 5 PLTIGRILRHGAR--KHPDKEAVYFDGR---RTTYAELDERVNRLANALRA-LG------VKKGDRVAVFDWNSH--EYL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 416 VAFYGCLLAEVIPVPIEVPLSrkdagSQQIGFLLGSCG-----VGLALTSEVC-LKGLPKTQNgeimqfkgwprlKWVVT 489
Cdd:PRK06187 71 EAYFAVPKIGAVLHPINIRLK-----PEEIAYILNDAEdrvvlVDSEFVPLLAaILPQLPTVR------------TVIVE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 490 DTKYLTKPSKDWQ-------------PHIPTANTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEgetlvn 556
Cdd:PRK06187 134 GDGPAAPLAPEVGeyeellaaasdtfDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 557 vldfkKDSGLwhgVVTSvMNRIHTISVPY-SVMKACPLSWVQRVH-------VHKARVALVKCRDLHWAMM-AHRDQKDT 627
Cdd:PRK06187 208 -----DDVYL---VIVP-MFHVHAWGLPYlALMAGAKQVIPRRFDpenlldlIETERVTFFFAVPTIWQMLlKAPRAYFV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 628 NLSSLRMLIVadGANPWSVSSCDAFLNVF-----QSHGLKpEMiCPCASS---PEAMTVAIRRPGAQGAPLParailsma 699
Cdd:PRK06187 279 DFSSLRLVIY--GGAALPPALLREFKEKFgidlvQGYGMT-ET-SPVVSVlppEDQLPGQWTKRRSAGRPLP-------- 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1025141333 700 glshGV-IRvntedknsaltvqdvghvmpgalmcIVKPDGPPMLCKTDEIGEIVLnsRAGGTM--YYGLPGVTKNTFE 774
Cdd:PRK06187 347 ----GVeAR-------------------------IVDDDGDELPPDGGEVGEIIV--RGPWLMqgYWNRPEATAETID 393
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1007-1502 |
1.73e-10 |
|
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: 65.44 E-value: 1.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1007 AQTDPDHVLymlLNAKGVAVSTAtcsQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRP 1086
Cdd:cd17651 5 AARTPDAPA---LVAEGRRLTYA---ELDRRANRL-AHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1087 PHPQnlaatlPTVRMIIDVSKAACILTTQTLIkiLRSKEAAASVNVKTWPNIIDIDDLPRKRPshiykpPTAEMLAYLDF 1166
Cdd:cd17651 78 AYPA------ERLAFMLADAGPVLVLTHPALA--GELAVELVAVTLLDQPGAAAGADAEPDPA------LDADDLAYVIY 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1167 SVSTTGMLTGVKISHSAVNALCRSiklQCELYSsrqiaicMDP------YCGLGF--VLWCMSSVYSGHQSILIPPMELE 1238
Cdd:cd17651 144 TSGSTGRPKGVVMPHRSLANLVAW---QARASS-------LGPgartlqFAGLGFdvSVQEIFSTLCAGATLVLPPEEVR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1239 TSLPLWLSTLSQYKIRDTFCSYSVME-LCtkglgtqtEALKARGVNLSCVRsCVVIAEErpRLALTQSFSKLFKDLGlsp 1317
Cdd:cd17651 214 TDPPALAAWLDEQRISRVFLPTVALRaLA--------EHGRPLGVRLAALR-YLLTGGE--QLVLTEDLREFCAGLP--- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1318 ravstafGARvnlaicLQGTAGPDPSTVyVDMKSLRHDRVRlveRGAPQSLplmesGTILPGVRVIIVNPETRgPLGDSH 1397
Cdd:cd17651 280 -------GLR------LHNHYGPTETHV-VTALSLPGDPAA---WPAPPPI-----GRPIDNTRVYVLDAALR-PVPPGV 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1398 LGEIWVCSPHNASGYYTIYG--EESLQADHFNtrlsfgdTETLWARTGYLgfVRRtellDASGDrhdaLFVVGSLDETLE 1475
Cdd:cd17651 337 PGELYIGGAGLARGYLNRPEltAERFVPDPFV-------PGARMYRTGDL--ARW----LPDGE----LEFLGRADDQVK 399
|
490 500
....*....|....*....|....*..
gi 1025141333 1476 LRGLRYHPIDIETSVsRAHRSIAESAV 1502
Cdd:cd17651 400 IRGFRIELGEIEAAL-ARHPGVREAVV 425
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1011-1487 |
2.15e-10 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 65.20 E-value: 2.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1011 PDHVLYMLLNAKGVAVSTatcSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVtvrpphpq 1090
Cdd:cd05908 1 PEGIIFILGDKKEKFVSY---RHLREEALGYLGALQELG-IKPGQEVVFQITHNNKFLYLFWACLLGGMIAV-------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1091 nlaatlPTVRMIIDVSKAACILTTQTLIKilrskeaaasvnvktwPNIIDIDDLPRKRPSHIykpptaemlAYLDFSVST 1170
Cdd:cd05908 69 ------PVSIGSNEEHKLKLNKVWNTLKN----------------PYLITEEEVLCELADEL---------AFIQFSSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1171 TGMLTGVKISHSAVNALCRSIKLQCELYSSRQIAICMDPYCGLGFVLWCMSSVYSGHQSILIPPMELETSLPLWLSTLSQ 1250
Cdd:cd05908 118 TGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKKASE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1251 YKIRDTFCSYSVMELCTKGLGTQtealKARGVNLSCVRscVVIAEERPRLA-LTQSFSKLFKDLGLSPRAVSTAFG-ARV 1328
Cdd:cd05908 198 HKATIVSSPNFGYKYFLKTLKPE----KANDWDLSSIR--MILNGAEPIDYeLCHEFLDHMSKYGLKRNAILPVYGlAEA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1329 NLAICLQgTAGPDPSTVYVDMKSLRH-DRVRLVERGAPQSLPLMESGTILPGVRVIIVNPETRGpLGDSHLGEIWVCSPH 1407
Cdd:cd05908 272 SVGASLP-KAQSPFKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPIDETDIRICDEDNKI-LPDGYIGHIQIRGKN 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1408 NASGYYTiyGEESlqadhfnTRLSFgdTETLWARTGYLGFVRRTELLdASGDRHDALFVVGSldetlelrglRYHPIDIE 1487
Cdd:cd05908 350 VTPGYYN--NPEA-------TAKVF--TDDGWLKTGDLGFIRNGRLV-ITGREKDIIFVNGQ----------NVYPHDIE 407
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
999-1502 |
8.64e-10 |
|
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: 62.97 E-value: 8.64e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 999 LSEALQWRAQTDPDHVLYMLLNAKgvavstATCSQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAG 1078
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRK------LTYRELDALAEAF-AAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1079 CIPVTVRPphpqnlaatlptvrmiidvskaacILTTQTLIKILRSKEAAASVNVKTWPNIIDIDDLPRKRPshiykPPTA 1158
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERV-----ALTP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1159 EMLAYLDFSVSTTGMLTGVKISHSAV--NAlcrsikLQC-----ELYSSRQIAICMDP-YCGLGFVLWCMSSVYSGHQSI 1230
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLvaNA------LQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1231 LIP---PMELetslplwLSTLSQYKIrDTFCsysvmelctkGLGTQTEAL----KARGVNLSCVRSCvviaeerprlalt 1303
Cdd:cd05936 199 LIPrfrPIGV-------LKEIRKHRV-TIFP----------GVPTMYIALlnapEFKKRDFSSLRLC------------- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1304 qsfsklfkdlgLS-----PRAVSTAFGARVNLAIcLQG----TAGP----DPSTvyvdmkslRHDRVRLVergapqslpl 1370
Cdd:cd05936 248 -----------ISggaplPVEVAERFEELTGVPI-VEGygltETSPvvavNPLD--------GPRKPGSI---------- 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1371 mesGTILPGVRVIIVNPETRgPLGDSHLGEIWVCSPHNASGYYTiYGEEslqadhfnTRLSFGDTetlWARTGYLGFVrr 1450
Cdd:cd05936 298 ---GIPLPGTEVKIVDDDGE-ELPPGEVGELWVRGPQVMKGYWN-RPEE--------TAEAFVDG---WLRTGDIGYM-- 359
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025141333 1451 tellDASG-----DRHDALFVVGsldetlelrGLRYHPIDIEtSVSRAHRSIAESAV 1502
Cdd:cd05936 360 ----DEDGyffivDRKKDMIIVG---------GFNVYPREVE-EVLYEHPAVAEAAV 402
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
396-909 |
9.14e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 62.84 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 396 LKPGDRVALVYPNSDPG---MFWVAFYGCLLAEVIpvpieVPLSrKDAGSQQIGFLLGSCGVGLALTSEVCL----KGLP 468
Cdd:cd05922 15 GVRGERVVLILPNRFTYielSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIVLADAGAAdrlrDALP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 469 KTQNGEimqfkgwprlkwVVTDTKYLTKPSKDWQPHIPtANTDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNY 548
Cdd:cd05922 89 ASPDPG------------TVLDADGIRAARASAPAHEV-SHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 549 CEGETLVNVLDFKKDSGLwhGVVTSVMNR-----IHTISVPysvmkacPLSWVQRVHVHKAR-VALVKCrdlHWAMMAHR 622
Cdd:cd05922 156 TADDRALTVLPLSYDYGL--SVLNTHLLRgatlvLTNDGVL-------DDAFWEDLREHGATgLAGVPS---TYAMLTRL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 623 DQKDTNLSSLRMLIVADGANPwsvsscDAFLNVFQSHGlkpemicpcasspeamtvairrPGAQgaplparaILSMAGLS 702
Cdd:cd05922 224 GFDPAKLPSLRYLTQAGGRLP------QETIARLRELL----------------------PGAQ--------VYVMYGQT 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 703 HGVIRVNTEDKNSALTVQD-VGHVMPGALMCIVKPDGPPmlCKTDEIGEIVLNsraGGTMYYGLPgvtkNTFEVIPvnSG 781
Cdd:cd05922 268 EATRRMTYLPPERILEKPGsIGLAIPGGEFEILDDDGTP--TPPGEPGEIVHR---GPNVMKGYW----NDPPYRR--KE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 782 GTPIGDVpftRTGLLGFVGPGSLVFVVGKIEGLLSVSGRRHNADDLVATALAVEPVKTVyrgriAVFSVTVFYDERIVIV 861
Cdd:cd05922 337 GRGGGVL---HTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEA-----AAVGLPDPLGEKLALF 408
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1025141333 862 AEqRPDANEEDSfqwMSRVLQAIDSIHQVGLYClalVPANTLPKTPLG 909
Cdd:cd05922 409 VT-APDKIDPKD---VLRSLAERLPPYKVPATV---RVVDELPLTASG 449
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
969-1527 |
2.24e-09 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 62.67 E-value: 2.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 969 AQASGRDLGLIDDQEQSRKLCVWPTN---------MHQFLSEalqwRAQTDPDHVLyMLLNAKgvavsTATCSQLHKRAE 1039
Cdd:PRK12316 4518 PQRRLGELQLLEKAEQQRIVALWNRTdagypatrcVHQLVAE----RARMTPDAVA-VVFDEE-----KLTYAELNRRAN 4587
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1040 KITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLAATlptvrMIIDvSKAACILTTQTLIK 1119
Cdd:PRK12316 4588 RLAHALIARG-VGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAY-----MMED-SGAALLLTQSHLLQ 4660
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1120 ILRSKEAAASVnvktwpnIIDIDDLPRKRPSHIYKPPT-AEMLAYLDFSVSTTGMLTGVKISHSAVNALCRSIKLQCELY 1198
Cdd:PRK12316 4661 RLPIPDGLASL-------ALDRDEDWEGFPAHDPAVRLhPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELT 4733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1199 SSRQIAICMdPYCGLGFVLWCMSSVYSGhQSILIPPMELetSLPLWL-STLSQYKIRDTFCSYSVMELCTKGLGTQTEAL 1277
Cdd:PRK12316 4734 PDDRVLQFM-SFSFDGSHEGLYHPLING-ASVVIRDDSL--WDPERLyAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPP 4809
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1278 KARGVnlscvrscvviaeerprlaltqsfskLFKDLGLSPRAVSTAFGARVNLAicLQGTAGPDPSTVYVdmkslRHDRV 1357
Cdd:PRK12316 4810 SLRVY--------------------------CFGGEAVAQASYDLAWRALKPVY--LFNGYGPTETTVTV-----LLWKA 4856
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1358 RLVERGAPQSLPLmesGTILPGVRVIIV----NPETRGPLGDSHLGEIWVcsphnASGYYTiygEESLQADHFNTRlSFG 1433
Cdd:PRK12316 4857 RDGDACGAAYMPI---GTPLGNRSGYVLdgqlNPLPVGVAGELYLGGEGV-----ARGYLE---RPALTAERFVPD-PFG 4924
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1434 DTETLWARTGYLGFVRRTELLDasgdrhdalfVVGSLDETLELRGLRYHPIDIETSVsRAHRSIAESavftwtnlLVVVV 1513
Cdd:PRK12316 4925 APGGRLYRTGDLARYRADGVID----------YLGRVDHQVKIRGFRIELGEIEARL-REHPAVREA--------VVIAQ 4985
|
570
....*....|....
gi 1025141333 1514 ELSGSEQEALDLVP 1527
Cdd:PRK12316 4986 EGAVGKQLVGYVVP 4999
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1030-1576 |
1.32e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 60.17 E-value: 1.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1030 TCSQLHKRAEKITAALLERG-GINTGDNVVLlyPPGIDLIASFYGCLYAGCIPVTVRPPHPQN-LAAtlptvrMIIDvSK 1107
Cdd:PRK12467 3122 SYAELNRRANRLAHRLIAIGvGPDVLVGVAV--ERSVEMIVALLAVLKAGGAYVPLDPEYPRErLAY------MIED-SG 3192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1108 AACILTTQTLIKILrskEAAASVNVKTwpniIDIDDLPRKRPSHIYKPPTAEMLAYLDFSVSTTGMLTGVKISHSAVNAL 1187
Cdd:PRK12467 3193 VKLLLTQAHLLEQL---PAPAGDTALT----LDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANH 3265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1188 CRSIKLQCELYSSRQIAICMdPYCGLGFVLWCMSSVYSGHQsILIPPMELETSLPLWlSTLSQYKIrdtfcsySVMELCT 1267
Cdd:PRK12467 3266 LCWIAEAYELDANDRVLLFM-SFSFDGAQERFLWTLICGGC-LVVRDNDLWDPEELW-QAIHAHRI-------SIACFPP 3335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1268 KGLgtQTEALKARGVNLSCVRSCVVIAEERPRLALTQSFSKLfkdlglsPRAvstafgarvnlaiCLQGTAGPDPSTVYV 1347
Cdd:PRK12467 3336 AYL--QQFAEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKL-------KPR-------------GLTNGYGPTEAVVTV 3393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1348 DMKSLRHDRVRLvergaPQSLPLmesGTILPGVRVIIV----NPETRGPLGDSHLGEIWVcsphnASGYYTiygEESLQA 1423
Cdd:PRK12467 3394 TLWKCGGDAVCE-----APYAPI---GRPVAGRSIYVLdgqlNPVPVGVAGELYIGGVGL-----ARGYHQ---RPSLTA 3457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1424 DHFNTRLSFGDTETLWaRTGYLGFVRRTELLDasgdrhdalfVVGSLDETLELRGLRYHPIDIETSVsRAHRSIAESAvf 1503
Cdd:PRK12467 3458 ERFVADPFSGSGGRLY-RTGDLARYRADGVIE----------YLGRIDHQVKIRGFRIELGEIEARL-LQHPSVREAV-- 3523
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025141333 1504 twtnllVVVVELSGSEQealdlvplvtnvvlkehhlIVGVVVIVDPGvipiNSRGEKQRMHLRDSfLADQLDP 1576
Cdd:PRK12467 3524 ------VLARDGAGGKQ-------------------LVAYVVPADPQ----GDWRETLRDHLAAS-LPDYMVP 3566
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
992-1501 |
1.36e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 59.53 E-value: 1.36e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 992 PTNMHQFLSEAlqwrAQTDPDHVLYMLLNAKG----VAVSTATCSQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDL 1067
Cdd:PRK09274 5 MANIARHLPRA----AQERPDQLAVAVPGGRGadgkLAYDELSFAELDARSDAI-AHGLNAAGIGRGMRAVLMVTPSLEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1068 IASFYGCLYAGCIPVTVRPPHP-QNLAATLPTVR--MIIDVSKAacilttQTLIKILRSKEAAASVNV----KTWPNIID 1140
Cdd:PRK09274 80 FALTFALFKAGAVPVLVDPGMGiKNLKQCLAEAQpdAFIGIPKA------HLARRLFGWGKPSVRRLVtvggRLLWGGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1141 IDDLPRKRPSHIYKP---PTAEMLAYLdFSVSTTGMLTGVKISHSAVNALCRSIKlqcELYSSRQIAICM---------D 1208
Cdd:PRK09274 154 LATLLRDGAAAPFPMadlAPDDMAAIL-FTSGSTGTPKGVVYTHGMFEAQIEALR---EDYGIEPGEIDLptfplfalfG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1209 PYCGlgfvlwcMSSVysghqsilIPPMELetSLPL------WLSTLSQYKIRDTFCSYSVMElctkglgTQTEALKARGV 1282
Cdd:PRK09274 230 PALG-------MTSV--------IPDMDP--TRPAtvdpakLFAAIERYGVTNLFGSPALLE-------RLGRYGEANGI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1283 NLSCVRsCVVIAEERPRLALTQSFSKLfkdlgLSPRA-VSTAFGARVNLAICLqgtagpdpstvyVDMKSLRHDRVRLVE 1361
Cdd:PRK09274 286 KLPSLR-RVISAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS------------IESREILFATRAATD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1362 RGAPQSLplmesGTILPGVRVIIV----NP-----ETRgPLGDSHLGEIWVCSPHNASGYYTiygeeSLQADHFNtRLSF 1432
Cdd:PRK09274 348 NGAGICV-----GRPVDGVEVRIIaisdAPipewdDAL-RLATGEIGEIVVAGPMVTRSYYN-----RPEATRLA-KIPD 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1025141333 1433 GDTETlWARTGYLGFvrrtelLDASGdrhdALFVVGSLDETLELRGLRYHPIDIEtSVSRAHRSIAESA 1501
Cdd:PRK09274 416 GQGDV-WHRMGDLGY------LDAQG----RLWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGVKRSA 472
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1024-1565 |
2.75e-08 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 58.09 E-value: 2.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1024 VAVS----TATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPqnlaatLPTV 1099
Cdd:cd17643 4 VAVVdedrRLTYGELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYP------VERI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1100 RMIIDVSKAACILTTqtlikilrskeaaasvnvktwpniididdlprkrpshiykpptAEMLAYLDFSVSTTGMLTGVKI 1179
Cdd:cd17643 77 AFILADSGPSLLLTD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVV 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1180 SHSAVNALCRSIklQCELYSSRQIAICMDPYCGLGFVLWCMSSVYSGHQSILIPPMELetslplwlsTLSQYKIRDTFCS 1259
Cdd:cd17643 114 SHANVLALFAAT--QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEV---------ARSPEDFARLLRD 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1260 YSVMELctkglgTQT--------EALKARGVNLSCVRScVVIAEERPRLALTQSFSKLFKDLglSPRAVStAFGArvnla 1331
Cdd:cd17643 183 EGVTVL------NQTpsafyqlvEAADRDGRDPLALRY-VIFGGEALEAAMLRPWAGRFGLD--RPQLVN-MYGI----- 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1332 iclqgtagpDPSTVYVDMKSLRhdrvrlvergaPQSLPLMESGTI---LPGVRVIIVNPETRgPLGDSHLGEIWVCSPHN 1408
Cdd:cd17643 248 ---------TETTVHVTFRPLD-----------AADLPAAAASPIgrpLPGLRVYVLDADGR-PVPPGVVGELYVSGAGV 306
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1409 ASGYYtiyGEESLQADHFNTRLSFGDTETLWaRTGYLgfVRRTelldASGDrhdaLFVVGSLDETLELRGLRYHPIDIET 1488
Cdd:cd17643 307 ARGYL---GRPELTAERFVANPFGGPGSRMY-RTGDL--ARRL----PDGE----LEYLGRADEQVKIRGFRIELGEIEA 372
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1489 SVsRAHRSIAESAVFTWTN------LLVVVVELSGSEQEALDLVPLvtnvvLKEH---HLIVGVVVIVDpgVIPINSRGE 1559
Cdd:cd17643 373 AL-ATHPSVRDAAVIVREDepgdtrLVAYVVADDGAAADIAELRAL-----LKELlpdYMVPARYVPLD--ALPLTVNGK 444
|
....*.
gi 1025141333 1560 KQRMHL 1565
Cdd:cd17643 445 LDRAAL 450
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
527-911 |
3.23e-08 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 57.30 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 527 GVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLWhGVVTSVMNRIHTISVPYSvmkaCPLSWVQRVHVHKARV 606
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLPKF----DPEAALELIEREKVTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 607 ALVKcRDLHWAMMAHRDQKDTNLSSLRMLIVadGANPWSVSSCDAFLNVF-----QSHGLKPEMICPCASSPEAMtvaIR 681
Cdd:cd04433 92 LLGV-PTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAPgiklvNGYGLTETGGTVATGPPDDD---AR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 682 RPGAQGAPLParailsmaglshgvirvNTEDKnsaltvqdvghvmpgalmcIVKPDGPPmlCKTDEIGEIVLNSRAGGTM 761
Cdd:cd04433 166 KPGSVGRPVP-----------------GVEVR-------------------IVDPDGGE--LPPGEIGELVVRGPSVMKG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 762 YYGLPGVTKNTFEvipvnsGGtpigdvpFTRTGLLGFVGPGSLVFVVGKIEGLLSVSGRRHNADDLVATALAVEPVKTVy 841
Cdd:cd04433 208 YWNNPEATAAVDE------DG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEA- 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025141333 842 rgriAVFSVTV-FYDERI--VIVAEQRPDANEEDSFQWMSRVLQAIDSIHQVglyclalVPANTLPKTPLGGI 911
Cdd:cd04433 274 ----AVVGVPDpEWGERVvaVVVLRPGADLDAEELRAHVRERLAPYKVPRRV-------VFVDALPRTASGKI 335
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
974-1191 |
3.84e-08 |
|
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440643 [Multi-domain] Cd Length: 1329 Bit Score: 58.33 E-value: 3.84e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 974 RDLGLIDDQEQSRKLCVW-----PTNMHQFLSEALQWRAQTDPDHVlymllnakgvAVSTA----TCSQLHKRAEKITAA 1044
Cdd:COG1020 448 GDLPLLTAAERQQLLAEWnataaPYPADATLHELFEAQAARTPDAV----------AVVFGdqslTYAELNARANRLAHH 517
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1045 LLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGC--IPvtvrpphpqnLAATLPT--VRMIIDVSKAACILTTQTliki 1120
Cdd:COG1020 518 LRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayVP----------LDPAYPAerLAYMLEDAGARLVLTQSA---- 582
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025141333 1121 LRSKEAAASVNVktwpniIDIDDL-----PRKRPSHiykPPTAEMLAYLDFSVSTTGMLTGVKISHSAVNALCRSI 1191
Cdd:COG1020 583 LAARLPELGVPV------LALDALalaaePATNPPV---PVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWM 649
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
350-431 |
4.62e-08 |
|
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: 57.57 E-value: 4.62e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 350 AKSPALTALDITGKPLytlTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSdPgMFWVAFYGCLLAEVIPV 429
Cdd:cd05936 10 RRFPDKTALIFMGRKL---TYRELDALAEAFAAGLQN-LG------VQPGDRVALMLPNC-P-QFPIAYFGALKAGAVVV 77
|
..
gi 1025141333 430 PI 431
Cdd:cd05936 78 PL 79
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
272-567 |
7.19e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 57.66 E-value: 7.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 272 VSTKIQQLLNTLKRPKRPPLSEFFLDDSEEIVEFPQPDPNTPKPEGRQiipvkgeplgvvsnwpPALQAALARWGATQAK 351
Cdd:PRK12316 1955 LDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRG----------------PGVHQRIAEQAARAPE 2018
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 352 SPALTALDitgkplYTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNSDPGMfwVAFYGCLLA--EVIPV 429
Cdd:PRK12316 2019 AIAVVFGD------QHLSYAELDSRANRLAHRLR-ARG------VGPEVRVAIAAERSFELV--VALLAVLKAggAYVPL 2083
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 430 PIEVPLSRkdagsqqIGFLLGSCGVGLALTSEVCLKGLPKTQngeimqfkGWPRLKwVVTDTKYLTKPSKDwqPHIPTAN 509
Cdd:PRK12316 2084 DPNYPAER-------LAYMLEDSGAALLLTQRHLLERLPLPA--------GVARLP-LDRDAEWADYPDTA--PAVQLAG 2145
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1025141333 510 TDTAYIEYKASKEGTVMGVAVSKISMLTHCQALTQACNYCEGETLVNVLDFKKDSGLW 567
Cdd:PRK12316 2146 ENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE 2203
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1027-1501 |
3.11e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 54.77 E-value: 3.11e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1027 STATCSQLHKRAEKITAALLErGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRP-PHPQNLAatlptvRMIIDV 1105
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTA-YGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPgMGRKNLK------QCLQEA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1106 SKaacilttQTLIKILRSKEAAASVnvktwpniididdlprkrpshiykpptaemlayldFSVSTTGMLTGVKISHSAVN 1185
Cdd:cd05910 74 EP-------DAFIGIPKADEPAAIL-----------------------------------FTSGSTGTPKGVVYRHGTFA 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1186 ALCRSIKlqcELYSSRQIAICMDpycglGFVLWCMSSVYSGHQSIlIPPME----LETSLPLWLSTLSQYKIRDTFCSYS 1261
Cdd:cd05910 112 AQIDALR---QLYGIRPGEVDLA-----TFPLFALFGPALGLTSV-IPDMDptrpARADPQKLVGAIRQYGVSIVFGSPA 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1262 VMELCtkglgtqTEALKARGVNLSCVRsCVVIAEERPRLALTQSFSKLfkdlgLSPRA-VSTAFGARVNLAICLQGTagp 1340
Cdd:cd05910 183 LLERV-------ARYCAQHGITLPSLR-RVLSAGAPVPIALAARLRKM-----LSDEAeILTPYGATEALPVSSIGS--- 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1341 dpstvyvdmKSLRHDRVRLVERGAPQSLplmesGTILPGVRVIIVnPETRGP---------LGDSHLGEIWVCSPHNASG 1411
Cdd:cd05910 247 ---------RELLATTTAATSGGAGTCV-----GRPIPGVRVRII-EIDDEPiaewddtleLPRGEIGEITVTGPTVTPT 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1412 YYTiygeeSLQADHFnTRLSFGDtETLWARTGYLGFvrrtelLDASGdrhdALFVVGSLDETLELRGLRYHPIDIEtSVS 1491
Cdd:cd05910 312 YVN-----RPVATAL-AKIDDNS-EGFWHRMGDLGY------LDDEG----RLWFCGRKAHRVITTGGTLYTEPVE-RVF 373
|
490
....*....|
gi 1025141333 1492 RAHRSIAESA 1501
Cdd:cd05910 374 NTHPGVRRSA 383
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1003-1526 |
3.61e-07 |
|
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: 54.54 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1003 LQWRAQTDPDHVLYMLLNakgvavSTATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPV 1082
Cdd:cd17631 1 LRRRARRHPDRTALVFGG------RSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVFV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1083 tvrpPHPQNLAAtlPTVRMIIDVSKAACIlttqtlikilrskeaaasvnvktwpniidIDDLprkrpshiykpptaemlA 1162
Cdd:cd17631 74 ----PLNFRLTP--PEVAYILADSGAKVL-----------------------------FDDL-----------------A 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1163 YLDFSVSTTGMLTGVKISHSAVNALCRSIKLQCELySSRQIAICMDPYC---GLGfvLWCMSSVYSGHQSILIPPMELET 1239
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFhigGLG--VFTLPTLLRGGTVVILRKFDPET 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1240 SLplwlSTLSQYKIRDTFcsysvmelctkGLGTQTEAL----KARGVNLSCVRsCVVIAEERPRLALTQSFSklfkdlgl 1315
Cdd:cd17631 179 VL----DLIERHRVTSFF-----------LVPTMIQALlqhpRFATTDLSSLR-AVIYGGAPMPERLLRALQ-------- 234
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1316 spravstAFGARVnlaicLQGTAGPDPSTVYVDMKSLRHDRvRLVERGAPqslplmesgtiLPGVRVIIVNPETRgPLGD 1395
Cdd:cd17631 235 -------ARGVKF-----VQGYGMTETSPGVTFLSPEDHRR-KLGSAGRP-----------VFFVEVRIVDPDGR-EVPP 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1396 SHLGEIWVCSPHNASGYYTiyGEESlqadhfnTRLSFGDTetlWARTGYLGFVrrtelldasgDRHDALFVVGSLDETLE 1475
Cdd:cd17631 290 GEVGEIVVRGPHVMAGYWN--RPEA-------TAAAFRDG---WFHTGDLGRL----------DEDGYLYIVDRKKDMII 347
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1025141333 1476 LRGLRYHPIDIETSVSRaHRSIAESAVF-----TWTNLLV-VVVELSGSEQEALDLV 1526
Cdd:cd17631 348 SGGENVYPAEVEDVLYE-HPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELI 403
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
969-1191 |
3.99e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.35 E-value: 3.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 969 AQASGRDLGLIDDQEQSRKLCVW-------PTN--MHQFLSEalqwRAQTDPDHVLymlLNAKGVAVSTAtcsQLHKRAE 1039
Cdd:PRK12316 1970 AQAALGELALLDAGERQRILADWdrtpeayPRGpgVHQRIAE----QAARAPEAIA---VVFGDQHLSYA---ELDSRAN 2039
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1040 KITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLAATlptvrMIIDvSKAACILTTQTLIK 1119
Cdd:PRK12316 2040 RLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAY-----MLED-SGAALLLTQRHLLE 2112
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1025141333 1120 ILRSKEAAASVNVKTwpnIIDIDDLPRKRPSHIYKPptaEMLAYLDFSVSTTGMLTGVKISHSAVNALCRSI 1191
Cdd:PRK12316 2113 RLPLPAGVARLPLDR---DAEWADYPDTAPAVQLAG---ENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAA 2178
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1033-1502 |
4.08e-07 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis termination module Surfactin (SrfA-C); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the adenylation domain of the Bacillus subtilis termination module (Surfactin domain, SrfA-C) which recognizes a specific amino acid building block, which is then activated and transferred to the terminal thiol of the 4'-phosphopantetheine (Ppan) arm of the downstream peptidyl carrier protein (PCP) domain.
Pssm-ID: 341282 [Multi-domain] Cd Length: 483 Bit Score: 54.51 E-value: 4.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1033 QLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNlaatlpTVRMIIDVSKAACIL 1112
Cdd:cd12117 27 ELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAE------RLAFMLADAGAKVLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1113 TtqtlikilrSKEAAASVNVKTWPNIIDIDDLPRKrPSHIYKPPTAEMLAYLDFSVSTTGMLTGVKISHSAVNALCRS-- 1190
Cdd:cd12117 100 T---------DRSLAGRAGGLEVAVVIDEALDAGP-AGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVRLVKNtn 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1191 -IKLQCELYSSRQIAICMDpycGLGFVLWcmSSVYSGHQSILIPPMELETSLPLwlstlsqykirdtfcsysvmelctkg 1269
Cdd:cd12117 170 yVTLGPDDRVLQTSPLAFD---ASTFEIW--GALLNGARLVLAPKGTLLDPDAL-------------------------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1270 lgtqTEALKARGVNLSCVRSCV--VIAEERPrlaltQSFSKLFKDL-G---LSPRAVSTAfgarvnLAIC----LQGTAG 1339
Cdd:cd12117 219 ----GALIAEEGVTVLWLTAALfnQLADEDP-----ECFAGLRELLtGgevVSPPHVRRV------LAACpglrLVNGYG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1340 PDPSTVYvdmkSLRHdrvrLVERGAPQ--SLPLmesGTILPGVRVIIVNpETRGPLGDSHLGEIWVCSPHNASGYytiYG 1417
Cdd:cd12117 284 PTENTTF----TTSH----VVTELDEVagSIPI---GRPIANTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGY---LN 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1418 EESLQADHFnTRLSFGDTETLWaRTGYLgfVRRTElldasgdrhDALFV-VGSLDETLELRGLRYHPIDIETSVsRAHRS 1496
Cdd:cd12117 349 RPALTAERF-VADPFGPGERLY-RTGDL--ARWLP---------DGRLEfLGRIDDQVKIRGFRIELGEIEAAL-RAHPG 414
|
....*.
gi 1025141333 1497 IAESAV 1502
Cdd:cd12117 415 VREAVV 420
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1374-1570 |
1.34e-06 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 53.06 E-value: 1.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1374 GTILPGVRVIIVNPETRGPLGDSHLGEIWVCSPHNASGYYTIYGEESLQADhfntrlsfgdtETLWARTGYLGFVrrtel 1453
Cdd:PLN02330 364 GFILPNLEVKFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTID-----------EDGWLHTGDIGYI----- 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1454 lDASGDrhdaLFVVGSLDETLELRGLRYHPIDIEtSVSRAHRSIAESAVFTWTN-------LLVVVVELSGSEQEAlDLV 1526
Cdd:PLN02330 428 -DDDGD----IFIVDRIKELIKYKGFQVAPAELE-AILLTHPSVEDAAVVPLPDeeageipAACVVINPKAKESEE-DIL 500
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1025141333 1527 PLVTNVVlkEHHLIVGVVVIVDPgvIPINSRGEKQRMHLRDSFL 1570
Cdd:PLN02330 501 NFVAANV--AHYKKVRVVQFVDS--IPKSLSGKIMRRLLKEKML 540
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
999-1088 |
1.87e-06 |
|
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: 52.46 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 999 LSEALQWRAQTDPDHVlymllnakgvAV----STATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGC 1074
Cdd:COG1021 27 LGDLLRRRAERHPDRI----------AVvdgeRRLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFAL 95
|
90
....*....|....
gi 1025141333 1075 LYAGCIPVTVRPPH 1088
Cdd:COG1021 96 FRAGAIPVFALPAH 109
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1043-1566 |
2.10e-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.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 52.06 E-value: 2.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1043 AALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLAATlpTVRMIIDVSKAACILTTQTLIKILR 1122
Cdd:cd05922 7 ASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRLGLVFVPLNPTLKES--VLRYLVADAGGRIVLADAGAADRLR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1123 sKEAAASVNVKTWPNIIDIDDLPRKRPSHiykPPTAEMLAYLDFSVSTTGMLTGVKISHSAVNALCRSIKLQCELYSSRQ 1202
Cdd:cd05922 85 -DALPASPDPGTVLDADGIRAARASAPAH---EVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1203 IAICMdP--YC-GLGFVLwcmSSVYSGHQSILIPPMELETSlplwlstlsqykirdtfcsysVMELCTKglgtqtealkA 1279
Cdd:cd05922 161 ALTVL-PlsYDyGLSVLN---THLLRGATLVLTNDGVLDDA---------------------FWEDLRE----------H 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1280 RGVNLSCVRScvvIAEERPRLAltqsfsklFKDLGL-SPRAVSTAFGARVNLAICLQGTAGPDpSTVYVdMKSLRHDRVR 1358
Cdd:cd05922 206 GATGLAGVPS---TYAMLTRLG--------FDPAKLpSLRYLTQAGGRLPQETIARLRELLPG-AQVYV-MYGQTEATRR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1359 LVERGAPQSLPLMES-GTILPGVRVIIVNPETrGPLGDSHLGEIWVCSPHNASGYYTIYGEEsLQADHFNTRLsfgdtet 1437
Cdd:cd05922 273 MTYLPPERILEKPGSiGLAIPGGEFEILDDDG-TPTPPGEPGEIVHRGPNVMKGYWNDPPYR-RKEGRGGGVL------- 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1438 lwaRTGYLGFvrrtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDIETSVsRAHRSIAESAVF----TWTNLLVVVV 1513
Cdd:cd05922 344 ---HTGDLAR------RDEDGF----LFIVGRRDRMIKLFGNRISPTEIEAAA-RSIGLIIEAAAVglpdPLGEKLALFV 409
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1025141333 1514 ELSgSEQEALDLVPLVTNVVlkEHHLIVGVVVIVDPgvIPINSRGEKQRMHLR 1566
Cdd:cd05922 410 TAP-DKIDPKDVLRSLAERL--PPYKVPATVRVVDE--LPLTASGKVDYAALR 457
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
325-429 |
3.59e-06 |
|
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: 51.68 E-value: 3.59e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 325 GEPLGvvsnwppalqAALARWGATQAKSPALTALDitgkplYTLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVAL 404
Cdd:COG1021 24 GETLG----------DLLRRRAERHPDRIAVVDGE------RRLSYAELDRRADRLAAGLL-ALG------LRPGDRVVV 80
|
90 100
....*....|....*....|....*
gi 1025141333 405 VYPNSdpGMFWVAFYGCLLAEVIPV 429
Cdd:COG1021 81 QLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
369-544 |
4.32e-06 |
|
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: 51.11 E-value: 4.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 369 TYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNSDPGMfwVAFYGCLLAEVIPVPIEV--PLSRkdagsqqIG 446
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERSAELV--VAILAVLKAGAAYVPLDPayPAER-------LA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 447 FLLGSCGVGLALTSEvclkglpktQNGEIMQFKGWPRLKWVVTDTKYLTKPSKDWQPHIPTANTDTAYIEYKASKEGTVM 526
Cdd:TIGR01733 66 FILEDAGARLLLTDS---------ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPK 136
|
170
....*....|....*...
gi 1025141333 527 GVAVSKISMLTHCQALTQ 544
Cdd:TIGR01733 137 GVVVTHRSLVNLLAWLAR 154
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
967-1502 |
6.54e-06 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 51.50 E-value: 6.54e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 967 RIAQASGRDLGLIDDQEQSRKL-------CVWPTN--MHQFLSEALQwraqtdpdhvlymlLNAKGVAVS----TATCSQ 1033
Cdd:PRK12316 476 ENPQARVDELPMLDAEERGQLVegwnataAEYPLQrgVHRLFEEQVE--------------RTPEAPALAfgeeTLDYAE 541
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1034 LHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPPHPQNLAATLptvrmiIDVSKAACILT 1113
Cdd:PRK12316 542 LNRRANRLAHALIERG-VGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYM------LEDSGVQLLLS 614
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1114 TQTLIKILrskEAAASVNVktwpniIDIDDLPRKRPSHIYKPP----TAEMLAYLDFSVSTTGMLTGVKISHSAVNALCR 1189
Cdd:PRK12316 615 QSHLGRKL---PLAAGVQV------LDLDRPAAWLEGYSEENPgtelNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLC 685
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1190 SIKLQCELYSSRQIAIcMDPYCGLGFVLWCMSSVYSGHQSILIPPMELETSLPLWlSTLSQYKIRdtfcsysVMELCTKG 1269
Cdd:PRK12316 686 WMQQAYGLGVGDTVLQ-KTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLV-ELINREGVD-------TLHFVPSM 756
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1270 LgtqtEALKARGVNLSC--VRSCVVIAEERPRLALTQSFSKLFKdlglspravstafGARVNLaiclqgtAGPDPSTVYV 1347
Cdd:PRK12316 757 L----QAFLQDEDVASCtsLRRIVCSGEALPADAQEQVFAKLPQ-------------AGLYNL-------YGPTEAAIDV 812
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1348 DMKSLRHDRVRLVERGAPqslplmesgtiLPGVRVIIVNPETrGPLGDSHLGEIWVCSPHNASGYytiYGEESLQADHFn 1427
Cdd:PRK12316 813 THWTCVEEGGDSVPIGRP-----------IANLACYILDANL-EPVPVGVLGELYLAGRGLARGY---HGRPGLTAERF- 876
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1025141333 1428 TRLSFGDTETLWaRTGYLGFVRRTELLDasgdrhdalfVVGSLDETLELRGLRYHPIDIETSVSRaHRSIAESAV 1502
Cdd:PRK12316 877 VPSPFVAGERMY-RTGDLARYRADGVIE----------YAGRIDHQVKLRGLRIELGEIEARLLE-HPWVREAAV 939
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
367-488 |
9.98e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 49.96 E-value: 9.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 367 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNSdPgMFWVAFYGCLLAEVIPVPIEvPLSRkdagSQQIG 446
Cdd:PRK08314 35 AISYRELLEEAERLAGYLQQECG------VRKGDRVLLYMQNS-P-QFVIAYYAILRANAVVVPVN-PMNR----EEELA 101
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1025141333 447 FLLGSCGVGLALTSEVCLkglpktqnGEIMQFKGWPRLKWVV 488
Cdd:PRK08314 102 HYVTDSGARVAIVGSELA--------PKVAPAVGNLRLRHVI 135
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
558-924 |
1.26e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 49.76 E-value: 1.26e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 558 LDFKKDSG-----LWHG-----VVTSVMNRIHTISVPYSVMKACPLSWVQrvHVHKARVALVKCRDLHWAMMAH--RDQK 625
Cdd:PRK05851 190 LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLS--WLSDSRATLTAAPNFAYNLIGKyaRRVS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 626 DTNLSSLRMLIvaDGANPWSVSSCDAFLNVFQSHGLKPEMICPCASSPEAM-TVAIRRPGAqgaplparailsmaGLShg 704
Cdd:PRK05851 268 DVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAESTcAVTVPVPGI--------------GLR-- 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 705 VIRVNTEDKNSALTVQDVGHVMPGALMCIVKPDGPPMLcKTDEIGEIVLNsraGGTMYYGLpgvtkntfevipvnSGGTP 784
Cdd:PRK05851 330 VDEVTTDDGSGARRHAVLGNPIPGMEVRISPGDGAAGV-AGREIGEIEIR---GASMMSGY--------------LGQAP 391
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 785 IGDVPFTRTGLLGFVGPGSLVfVVGKIEGLLSVSGRRHNADDLVATALAVEPVKtvyRGRIavfsVTVFYDE-----RIV 859
Cdd:PRK05851 392 IDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRGVR---EGAV----VAVGTGEgsarpGLV 463
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025141333 860 IVAEQR-PDaneEDSFQwmSRVLQAIDSIHQVGLYCLALVPANTLPKTPLGGIHVSETKqHFLEGS 924
Cdd:PRK05851 464 IAAEFRgPD---EAGAR--SEVVQRVASECGVVPSDVVFVAPGSLPRTSSGKLRRLAVK-RSLEAA 523
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1007-1181 |
1.79e-05 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 49.12 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1007 AQTDPDHVLYMLLNAkgvavsTATCSQLHKRAEKITAALLERGgiNTGDNVVLLY----PpgiDLIASFYGCLYAGC--I 1080
Cdd:PRK04813 12 AQTQPDFPAYDYLGE------KLTYGQLKEDSDALAAFIDSLK--LPDKSPIIVFghmsP---EMLATFLGAVKAGHayI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1081 PVTVRPPhpqnlaatLPTVRMIIDVSKAACILTT------QTLIKILRSKEAAASVNVKTWPNiididdlprkrPSHIYK 1154
Cdd:PRK04813 81 PVDVSSP--------AERIEMIIEVAKPSLIIATeelpleILGIPVITLDELKDIFATGNPYD-----------FDHAVK 141
|
170 180
....*....|....*....|....*..
gi 1025141333 1155 pptAEMLAYLDFSVSTTGMLTGVKISH 1181
Cdd:PRK04813 142 ---GDDNYYIIFTSGTTGKPKGVQISH 165
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
350-437 |
2.56e-05 |
|
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: 48.78 E-value: 2.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 350 AKSPALTALDITGKplyTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVAlVYPNSDPGMFwVAFYGCLLA--EVI 427
Cdd:cd05945 2 AANPDRPAVVEGGR---TLTYRELKERADALA-AALASLG------LDAGDPVV-VYGHKSPDAI-AAFLAALKAghAYV 69
|
90
....*....|
gi 1025141333 428 PVPIEVPLSR 437
Cdd:cd05945 70 PLDASSPAER 79
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
341-431 |
3.25e-05 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 48.57 E-value: 3.25e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 341 ALARWGATQAKSPALTALDITGKPlYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNSdPgMFWVAFYG 420
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGEDGEE-RTLTYAELRREVNRFA-NALRALG------VKKGDRVAIYLPNI-P-EAVIAMLA 83
|
90
....*....|.
gi 1025141333 421 CLLAEVIPVPI 431
Cdd:COG0365 84 CARIGAVHSPV 94
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
366-531 |
3.80e-05 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 48.04 E-value: 3.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 366 YTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNSDPGMfwVAFYGCLLAEVIPVPIEV--PLSRKDAgsq 443
Cdd:cd12114 11 GTLTYGELAERARRVA-GALKAAG------VRPGDLVAVTLPKGPEQV--VAVLGILAAGAAYVPVDIdqPAARREA--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 444 qigfLLGSCGVGLALTSEVCLKGLPktqngeimqfkgWPRLkwVVTDTKYLTKPSKDwQPHIPTANTDTAYIEYKASKEG 523
Cdd:cd12114 79 ----ILADAGARLVLTDGPDAQLDV------------AVFD--VLILDLDALAAPAP-PPPVDVAPDDLAYVIFTSGSTG 139
|
....*...
gi 1025141333 524 TVMGVAVS 531
Cdd:cd12114 140 TPKGVMIS 147
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
343-453 |
4.80e-05 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 47.60 E-value: 4.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 343 ARWGATQakSPALTALDITGKplyTLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSDPgmFWVAFYGCL 422
Cdd:cd17631 1 LRRRARR--HPDRTALVFGGR---SLTYAELDERVNRLAHALRA-LG------VAKGDRVAVLSKNSPE--FLELLFAAA 66
|
90 100 110
....*....|....*....|....*....|.
gi 1025141333 423 LAEVIPVPIEVPLSRKDagsqqIGFLLGSCG 453
Cdd:cd17631 67 RLGAVFVPLNFRLTPPE-----VAYILADSG 92
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1042-1503 |
7.11e-05 |
|
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: 47.31 E-value: 7.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1042 TAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPvtvrppHPQNLAATLPTVRMIIDVSKAACILT-TQTLIKI 1120
Cdd:cd05926 27 LARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVV------APLNPAYKKAEFEFYLADLGSKLVLTpKGELGPA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1121 LRSKE------AAASVNVKTWPNIIDIDDLPRKRPSHIY----KPPTAEMLAYLDFSVSTTGMLTGVKISH----SAVNA 1186
Cdd:cd05926 101 SRAASklglaiLELALDVGVLIRAPSAESLSNLLADKKNakseGVPLPDDLALILHTSGTTGRPKGVPLTHrnlaASATN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1187 LCRSIKLqcelySSRQIAICMDP-YCGLGFVLWCMSSVYSGhQSILIPPMELETSL--------PLWLS---TLSQYKIR 1254
Cdd:cd05926 181 ITNTYKL-----TPDDRTLVVMPlFHVHGLVASLLSTLAAG-GSVVLPPRFSASTFwpdvrdynATWYTavpTIHQILLN 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1255 DTfcsysvmelctkglGTQTEALKARgvnLSCVRSCvviaeerprlaltqSFSklfkdlgLSP---RAVSTAFGARVNLA 1331
Cdd:cd05926 255 RP--------------EPNPESPPPK---LRFIRSC--------------SAS-------LPPavlEALEATFGAPVLEA 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1332 I-----CLQGTAGPdpstvyvdmksLRHDRVRLVERGAPQslplmesgtilpGVRVIIVNpETRGPLGDSHLGEIWVCSP 1406
Cdd:cd05926 297 YgmteaAHQMTSNP-----------LPPGPRKPGSVGKPV------------GVEVRILD-EDGEILPPGVVGEICLRGP 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1407 HNASGYYtiygeeslqADHFNTRLSFgdTETLWARTGYLGFvrrtelLDASGDrhdaLFVVGSLDETLELRGLRYHPIDI 1486
Cdd:cd05926 353 NVTRGYL---------NNPEANAEAA--FKDGWFRTGDLGY------LDADGY----LFLTGRIKELINRGGEKISPLEV 411
|
490
....*....|....*..
gi 1025141333 1487 EtSVSRAHRSIAESAVF 1503
Cdd:cd05926 412 D-GVLLSHPAVLEAVAF 427
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1005-1184 |
1.07e-04 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 46.88 E-value: 1.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1005 WRAQTD--PDHVLymlLNAKGVAVSTAtcsQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPV 1082
Cdd:cd17646 4 VAEQAArtPDAPA---VVDEGRTLTYR---ELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAAYL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1083 TVRPPHPQnlaatlPTVRMIIDVSKAACILTTQTLIKILRSKEAAASVNVKTWPNIIDIDDLPRKRPSHiykpptaemLA 1162
Cdd:cd17646 77 PLDPGYPA------DRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDN---------LA 141
|
170 180
....*....|....*....|..
gi 1025141333 1163 YLDFSVSTTGMLTGVKISHSAV 1184
Cdd:cd17646 142 YVIYTSGSTGRPKGVMVTHAGI 163
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
334-437 |
1.42e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 46.57 E-value: 1.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 334 WPP-------------ALQAALARWGATQAKSPALtalDITGkplYTLTYGKLWSRSLKLAyTLLNKLGtknepvLKPGD 400
Cdd:PRK06178 18 WPAgiprepeyphgerPLTEYLRAWARERPQRPAI---IFYG---HVITYAELDELSDRFA-ALLRQRG------VGAGD 84
|
90 100 110
....*....|....*....|....*....|....*..
gi 1025141333 401 RVALVYPNSdPgMFWVAFYGCLLAEVIPVPIEvPLSR 437
Cdd:PRK06178 85 RVAVFLPNC-P-QFHIVFFGILKLGAVHVPVS-PLFR 118
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
999-1187 |
1.74e-04 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 46.58 E-value: 1.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 999 LSEALQWRAQTDPDhvlymllnAKGVAVSTATCSQLHKRAEKIT-AALLERGGINTGDNVVLLYPPGIDLIASFYGCLYA 1077
Cdd:PRK10252 460 LSALVAQQAAKTPD--------APALADARYQFSYREMREQVVAlANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEA 531
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1078 GCIPVTVRPPHPQNlaatlpTVRMIIDVSKAACILTTQTLIKILRSKEAAASVNVKTWPNIIDIDDLPRKRPSHiykppt 1157
Cdd:PRK10252 532 GAAWLPLDTGYPDD------RLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLSQPHH------ 599
|
170 180 190
....*....|....*....|....*....|.
gi 1025141333 1158 aemLAYLDFSVSTTGMLTGVKISHSA-VNAL 1187
Cdd:PRK10252 600 ---TAYIIFTSGSTGRPKGVMVGQTAiVNRL 627
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
367-542 |
4.10e-04 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 44.92 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 367 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSDpgMFWVAFYGCLLAEVIPVPIEVPLSRKDagsqqIG 446
Cdd:PRK08316 36 SWTYAELDAAVNRVAAALLD-LG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 447 FLLGSCGVGLALTSEVCLKGLPKTQNGEIMQFKGWPRL--------KWVVTDTKYLTKPSKDWQPHIptANTDTAYIEYK 518
Cdd:PRK08316 102 YILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVlggreapgGWLDFADWAEAGSVAEPDVEL--ADDDLAQILYT 179
|
170 180
....*....|....*....|....
gi 1025141333 519 ASKEGTVMGVavskisMLTHcQAL 542
Cdd:PRK08316 180 SGTESLPKGA------MLTH-RAL 196
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
999-1194 |
4.75e-04 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 44.71 E-value: 4.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 999 LSEALQWRAQTDPDHVLYMLLNAkGVAVSTaTCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAG 1078
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKED-GIWQSL-TWAEFAERVRALAAGLLALG-VKPGDRVAILSDNRPEWVIADLAILAAG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1079 CIPVTVrppHPQNLAAtlpTVRMIIDVSKA-ACILTTQTLI-KILRSKEAAASV---------------NVKTWPNIIDI 1141
Cdd:COG1022 90 AVTVPI---YPTSSAE---EVAYILNDSGAkVLFVEDQEQLdKLLEVRDELPSLrhivvldprglrddpRLLSLDELLAL 163
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1025141333 1142 ------DDLPRKRPSHIykppTAEMLAYLDFSVSTTGMLTGVKISH----SAVNALCRSIKLQ 1194
Cdd:COG1022 164 grevadPAELEARRAAV----KPDDLATIIYTSGTTGRPKGVMLTHrnllSNARALLERLPLG 222
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1374-1567 |
5.22e-04 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 44.59 E-value: 5.22e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1374 GTILPGVRVIIVNPETRGPLGDSHLGEIWVCSPHNASGYY-----TiygEESLQADHfntrlsfgdtetlWARTGYLGFV 1448
Cdd:cd05941 267 GMPLPGVQARIVDEETGEPLPRGEVGEIQVRGPSVFKEYWnkpeaT---KEEFTDDG-------------WFKTGDLGVV 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1449 rrtellDASGdrhdALFVVG-SLDETLELRGLRYHPIDIEtSVSRAHRSIAESAVF-----TWTNLLVVVVELSgSEQEA 1522
Cdd:cd05941 331 ------DEDG----YYWILGrSSVDIIKSGGYKVSALEIE-RVLLAHPGVSECAVIgvpdpDWGERVVAVVVLR-AGAAA 398
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1025141333 1523 LDLVPLVTNvvLKEH---HLIVGVVVIVDpgVIPINSRGEKQRMHLRD 1567
Cdd:cd05941 399 LSLEELKEW--AKQRlapYKRPRRLILVD--ELPRNAMGKVNKKELRK 442
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1028-1113 |
5.79e-04 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 44.37 E-value: 5.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1028 TATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPP-HPQNLA--ATLPTVRMIID 1104
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLG-VSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLlHPDDYAyiARDCEARLVVT 88
|
....*....
gi 1025141333 1105 VSKAACILT 1113
Cdd:cd05919 89 SADDIAYLL 97
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
367-641 |
7.04e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 44.12 E-value: 7.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 367 TLTYGKLWSRSLKLAYTLLNkLGtknepvLKPGDRVALVYPNSdpGMFWVAFYGCLLAEVIPVPIEvPLSRKDagsqQIG 446
Cdd:PRK07656 30 RLTYAELNARVRRAAAALAA-LG------IGKGDRVAIWAPNS--PHWVIAALGALKAGAVVVPLN-TRYTAD----EAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 447 FLLGSCGVGLAL-------TSEVCLKGLPKTQNGEIMQF-KGWPRLKWVVTDTKYLTKPSKDWQpHIPTANTDTAYIEYK 518
Cdd:PRK07656 96 YILARGDAKALFvlglflgVDYSATTRLPALEHVVICETeEDDPHTEKMKTFTDFLAAGDPAER-APEVDPDDVADILFT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 519 ASKEGTVMGVavskisMLTHCQALTQA---CNYC---EGETLVNVLDFKKDSGLWHGVVTSVMNRIHTISVPysvmKACP 592
Cdd:PRK07656 175 SGTTGRPKGA------MLTHRQLLSNAadwAEYLgltEGDRYLAANPFFHVFGYKAGVNAPLMRGATILPLP----VFDP 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1025141333 593 LSWVQRVHVHKARVaLVKCRDLHWAMMAHRDQKDTNLSSLRmLIVADGA 641
Cdd:PRK07656 245 DEVFRLIETERITV-LPGPPTMYNSLLQHPDRSAEDLSSLR-LAVTGAA 291
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1374-1493 |
7.70e-04 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 43.79 E-value: 7.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1374 GTILPGVRVIIVNPETRGPLGDSHlGEIWVCSPHNASGYYTiygEESLQADHFNTRlsfgdtetlWARTGYLGFVRrtel 1453
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGYWN---NPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1025141333 1454 ldasgdRHDALFVVGSLDETLELRGLRYHPIDIETSVSRA 1493
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVERIAEGV 269
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1006-1265 |
8.42e-04 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 43.86 E-value: 8.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1006 RAQTDPDHVlymllnakgvAV----STATCSQLHKRAEKITAALLERGgINTGDNVVLLYPPGIDLIASFYGCLYAGCIP 1081
Cdd:cd17655 6 QAEKTPDHT----------AVvfedQTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKAGGAY 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1082 VTVRPPHPQNlaatlpTVRMIIDVSKAACILTTQTLIKILRSKEAAasvnvktwpNIIDIDDLPRKRPSHIYKPPTAEML 1161
Cdd:cd17655 75 LPIDPDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLI---------DLLDEDTIYHEESENLEPVSKSDDL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1162 AYLDFSVSTTGMLTGVKISH--------SAVNALCRSIKLQCELYSSrqiaICMDpycglGFVLWCMSSVYSGHqSILIP 1233
Cdd:cd17655 140 AYVIYTSGSTGKPKGVMIEHrgvvnlveWANKVIYQGEHLRVALFAS----ISFD-----ASVTEIFASLLSGN-TLYIV 209
|
250 260 270
....*....|....*....|....*....|..
gi 1025141333 1234 PMELETSLPLWLSTLSQYKIRDTFCSYSVMEL 1265
Cdd:cd17655 210 RKETVLDGQALTQYIRQNRITIIDLTPAHLKL 241
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
997-1088 |
1.84e-03 |
|
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: 42.70 E-value: 1.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 997 QFLSEALQWRAQTDPDHVlymllnakgvAVSTA----TCSQLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFY 1072
Cdd:cd05920 15 EPLGDLLARSAARHPDRI----------AVVDGdrrlTYRELDRRADRL-AAGLRGLGIRPGDRVVVQLPNVAEFVVLFF 83
|
90
....*....|....*.
gi 1025141333 1073 GCLYAGCIPVTVRPPH 1088
Cdd:cd05920 84 ALLRLGAVPVLALPSH 99
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1373-1450 |
2.10e-03 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 42.35 E-value: 2.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1373 SGTILPGVRVIIVNPETRGPLGDSHLGEIWVCSPHNASGYY-----TiygEESLQADH-FNTrlsfGDTETlWARTGYLG 1446
Cdd:cd17640 266 VGRPLPGTEIKIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYknpeaT---SKVLDSDGwFNT----GDLGW-LTCGGELV 337
|
....
gi 1025141333 1447 FVRR 1450
Cdd:cd17640 338 LTGR 341
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
367-461 |
2.91e-03 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 42.20 E-value: 2.91e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 367 TLTYGKLWSRSLKLAYTLLnKLGtknepvLKPGDRVALVYPNSDPgmFWVAFYGCLLAEVIPVPIEVPLSrkdagSQQIG 446
Cdd:cd05907 5 PITWAEFAEEVRALAKGLI-ALG------VEPGDRVAILSRNRPE--WTIADLAILAIGAVPVPIYPTSS-----AEQIA 70
|
90
....*....|....*
gi 1025141333 447 FLLGSCGVGLALTSE 461
Cdd:cd05907 71 YILNDSEAKALFVED 85
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
367-445 |
4.67e-03 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 41.58 E-value: 4.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 367 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPN--SDPgmfwVAFYGCLLAEVIPV-------PIEVPLSR 437
Cdd:PRK08974 48 VMTFRKLEERSRAFAAYLQNGLG------LKKGDRVALMMPNllQYP----IALFGILRAGMIVVnvnplytPRELEHQL 117
|
....*...
gi 1025141333 438 KDAGSQQI 445
Cdd:PRK08974 118 NDSGAKAI 125
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1033-1184 |
4.75e-03 |
|
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: 41.49 E-value: 4.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1033 QLHKRAEKItAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPphpqnlaaTLPTVRM--IIDVSKAAC 1110
Cdd:cd12114 17 ELAERARRV-AGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDI--------DQPAARReaILADAGARL 87
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1025141333 1111 ILTTqtlikilrskEAAASVNVKTWPNIIDIDDL--PRKRPSHIykPPTAEMLAYLDFSVSTTGMLTGVKISHSAV 1184
Cdd:cd12114 88 VLTD----------GPDAQLDVAVFDVLILDLDAlaAPAPPPPV--DVAPDDLAYVIFTSGSTGTPKGVMISHRAA 151
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1007-1117 |
5.38e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 41.30 E-value: 5.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1007 AQTDPDHVLYMLLNAkgvavsTATCSQLHKRAEKITAALLERgGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVtvrp 1086
Cdd:PRK07786 27 ALMQPDAPALRFLGN------TTTWRELDDRVAALAGALSRR-GVGFGDRVLILMLNRTEFVESVLAANMLGAIAV---- 95
|
90 100 110
....*....|....*....|....*....|.
gi 1025141333 1087 phPQNLAATLPTVRMIIDVSKAACILTTQTL 1117
Cdd:PRK07786 96 --PVNFRLTPPEIAFLVSDCGAHVVVTEAAL 124
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1379-1503 |
5.45e-03 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 41.41 E-value: 5.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1379 GVRVIIVNPETrGPLGDSHLGEIWVCSPHNASGYYtiygeeslqADHFNTRLSFGDTetlWARTGYLGfvrrteLLDASG 1458
Cdd:PRK05852 362 GAQIRIVGSDG-LPLPAGAVGEVWLRGTTVVRGYL---------GDPTITAANFTDG---WLRTGDLG------SLSAAG 422
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1025141333 1459 DrhdaLFVVGSLDETLELRGLRYHPIDIEtSVSRAHRSIAESAVF 1503
Cdd:PRK05852 423 D----LSIRGRIKELINRGGEKISPERVE-GVLASHPNVMEAAVF 462
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
367-531 |
6.07e-03 |
|
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: 41.12 E-value: 6.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 367 TLTYGKLWSRSLKLAYTLLNKLGtknepvlKPGDRVALVYPNSDPGMfwVAFYGCLLAEVIPVPIEvplsrKDAGSQQIG 446
Cdd:cd12116 12 SLSYAELDERANRLAARLRARGV-------GPGDRVAVYLPRSARLV--AAMLAVLKAGAAYVPLD-----PDYPADRLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 447 FLLGSCGVGLALTSEVCLKGLPktqngeiMQFKGWPRLKWvvtdtkylTKPSKDWQPHIPTANTDTAYIEYKASKEGTVM 526
Cdd:cd12116 78 YILEDAEPALVLTDDALPDRLP-------AGLPVLLLALA--------AAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPK 142
|
....*
gi 1025141333 527 GVAVS 531
Cdd:cd12116 143 GVVVS 147
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1032-1181 |
7.85e-03 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 40.60 E-value: 7.85e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1032 SQLHKRAEKITAALLERGGINTGDNVVLLYPPGIDLIASFYGCLYAGCIPVTVRPphpqnLAATLPTVRMIIDVSKAACI 1111
Cdd:PLN02574 70 SELQPLVKSMAAGLYHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNP-----SSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 1112 LTTQTLIKIlrskeAAASVNVKTWPNIIDIDDLPRKRP---SHIY-------KPPTAEM-LAYLDFSVSTTGMLTGVKIS 1180
Cdd:PLN02574 145 TSPENVEKL-----SPLGVPVIGVPENYDFDSKRIEFPkfyELIKedfdfvpKPVIKQDdVAAIMYSSGTTGASKGVVLT 219
|
.
gi 1025141333 1181 H 1181
Cdd:PLN02574 220 H 220
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
367-538 |
8.42e-03 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 40.63 E-value: 8.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 367 TLTYGKLWSRSLKLAYTLLNKLGtknepvLKPGDRVALVYPNSdpGMFWVAFYGCLLAEVIPV---PIEVPLSRK----D 439
Cdd:PRK08751 50 TITYREADQLVEQFAAYLLGELQ------LKKGDRVALMMPNC--LQYPIATFGVLRAGLTVVnvnPLYTPRELKhqliD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1025141333 440 AGSQQIGFLLGSCGVGLALTSEVCLKGLPKTQNGEIMQFKGWPRLKWVVtdtKYLTKPSKDWQ----------------- 502
Cdd:PRK08751 122 SGASVLVVIDNFGTTVQQVIADTPVKQVITTGLGDMLGFPKAALVNFVV---KYVKKLVPEYRingairfrealalgrkh 198
|
170 180 190
....*....|....*....|....*....|....*...
gi 1025141333 503 --PHIPTANTDTAYIEYKASKEGtvmgvaVSKISMLTH 538
Cdd:PRK08751 199 smPTLQIEPDDIAFLQYTGGTTG------VAKGAMLTH 230
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
368-431 |
8.74e-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: 40.54 E-value: 8.74e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1025141333 368 LTYGKLWSRSLKLAyTLLNKLGtknepvLKPGDRVALVYPNSDpgMFWVAFYGCLLAEVIPVPI 431
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKG------VRKGDRVGICLQNSP--QYVIAYFAIWRANAVVVPI 56
|
|
| |
