|
Name |
Accession |
Description |
Interval |
E-value |
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
988-1562 |
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: 790.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 988 LYTLLNCRGAIANSLTCVQLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPH-PQNIA 1066
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDiSQQLG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1067 TTLPTVKMivEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPA-----QICKPCNPDTLAYLDFSV 1141
Cdd:cd05905 81 FLLGTCKV--RVALTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSklkkwGPHPPTRDGDTAYIEYSF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1142 STTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALWLLAV 1221
Cdd:cd05905 159 SSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELMKTNPLLWLQTL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1222 SQYKVRDTFCSYSVMELCTKGLGSQTESLKARGLDLSRVRTCVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGCRV 1301
Cdd:cd05905 239 SQYKVRDAYVKLRTLHWCLKDLSSTLASLKNRDVNLSSLRMCMVPCENRPRISSCDSFLKLFQTLGLSPRAVSTEFGTRV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1302 NLAICLqphrlwtlaeQGTSGPDPTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGDSHL 1381
Cdd:cd05905 319 NPFICW----------QGTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKGLCKDGEI 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1382 GEIWVHSAHNASGYFTIYGDESLQSDHFNS-RLSFGDTQTIWARTGYLGFLRRTELTDANGERHDALYVVGALDEAMELR 1460
Cdd:cd05905 389 GEIWVNSPANASGYFLLDGETNDTFKVFPStRLSTGITNNSYARTGLLGFLRPTKCTDLNVEEHDLLFVVGSIDETLEVR 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1461 GMRYHPIDIETSVIRAHKSVTECAVFTWTNLLVVVVELD-GSEQEALDLVPLVTNVVLEEHYLIVGVVVVVDIGVIPINS 1539
Cdd:cd05905 469 GLRHHPSDIEATVMRVHPYRGRCAVFSITGLVVVVAEQPpGSEEEALDLVPLVLNAILEEHQVIVDCVALVPPGSLPKNP 548
|
570 580
....*....|....*....|...
gi 530392108 1540 RGEKQRMHLRDGFLADQLDPIYV 1562
Cdd:cd05905 549 LGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
336-912 |
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: 739.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 336 CLTTMDTNGKPLYILTYGKLWTRSMKVAYSILHKLGTKqepmvrPGDRVALVFPnnDPAAFMAAFYGCLLAEVVPVPIEV 415
Cdd:cd05905 1 AYTLLDSKGKEATTLTWGKLLSRAEKIAAVLQKKVGLK------PGDRVALMYP--DPLDFVAAFYGCLYAGVVPIPIEP 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 416 PLtrkdaGSQQIGFLLGSCGVTVALTSDACHKGLPKS-----PTGEIPQFKGWPKLLWFVTESKHLSKPPRDWFPHIKDA 490
Cdd:cd05905 73 PD-----ISQQLGFLLGTCKVRVALTVEACLKGLPKKllkskTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 491 NNDTAYIEYKTCKDGSVLGVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYSLM 570
Cdd:cd05905 148 DGDTAYIEYSFSSDGSLSGVAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLSVYSGHHTILIPPELM 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 571 KVNPLSWIQKVCQYKAKVACVKSRDMHWAL------VAHRDQRDINLSSLRMLIVADGaNPWSISSCDAFLNVFQSKGLR 644
Cdd:cd05905 228 KTNPLLWLQTLSQYKVRDAYVKLRTLHWCLkdlsstLASLKNRDVNLSSLRMCMVPCE-NRPRISSCDSFLKLFQTLGLS 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 645 QEvicpcASSPEALTVAIRRPTD--DSNQPPGRGVLSMHGLTYGVIRVDSEEKLSVLTVQDVGLVMPGAIMCSVKPDGVP 722
Cdd:cd05905 307 PR-----AVSTEFGTRVNPFICWqgTSGPEPSRVYLDMRALRHGVVRLDERDKPNSLPLQDSGKVLPGAQVAIVNPETKG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 723 qLCRTDEIGELCVCAVATGTSYYGLSGMTKNTFEVFPMTSSGAPISEYPFIRTGLLGFVGPG----------GLVFVVGK 792
Cdd:cd05905 382 -LCKDGEIGEIWVNSPANASGYFLLDGETNDTFKVFPSTRLSTGITNNSYARTGLLGFLRPTkctdlnveehDLLFVVGS 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 793 MDGLMVVSGRRHNADDIVATALAVEPmkfvYRGRIAVFSVTvlhdERIVIVAEQRPDStEEDSFQWMSRVLQAIDSIHQV 872
Cdd:cd05905 461 IDETLEVRGLRHHPSDIEATVMRVHP----YRGRCAVFSIT----GLVVVVAEQPPGS-EEEALDLVPLVLNAILEEHQV 531
|
570 580 590 600
....*....|....*....|....*....|....*....|
gi 530392108 873 GVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLHPCNV 912
Cdd:cd05905 532 IVDCVALVPPGSLPKNPLGEKQRMEIRQAFLAGKLHPIYV 571
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
978-1520 |
3.14e-70 |
|
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: 246.77 E-value: 3.14e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 978 WRAQTTPDHILYTLLNCRGAIANSLTCVQLHKRAEKIAVMLmeRGHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITV 1057
Cdd:cd05931 1 RRAAARPDRPAYTFLDDEGGREETLTYAELDRRARAIAARL--QAVGKPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1058 RPPHPqniATTLPTVKMIVEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQICKPcNPDTLAYL 1137
Cdd:cd05931 79 PPPTP---GRHAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSP-DPDDIAYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1138 DFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALW 1217
Cdd:cd05931 155 QYTSGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMSPAAFLRRPLRW 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1218 LLAVSQYkvRDTFcsySVM-----ELCTKglgsQTESLKARGLDLSRVRTCVVVAEeRPRIALTQSFSKLFKDLGLHPRA 1292
Cdd:cd05931 235 LRLISRY--RATI---SAApnfayDLCVR----RVRDEDLEGLDLSSWRVALNGAE-PVRPATLRRFAEAFAPFGFRPEA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1293 VSTSFGcrvnlaiclqphrlwtLAEQ------GTSGPDPTTVYVDMRALRHdRVRLVERGSPHSLPLMESGKILPGVRII 1366
Cdd:cd05931 305 FRPSYG----------------LAEAtlfvsgGPPGTGPVVLRVDRDALAG-RAVAVAADDPAARELVSCGRPLPDQEVR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1367 IANPETKGPLGDSHLGEIWVHSAHNASGYFtiyGDESLQSDHFNSRLSFGDtqTIWARTGYLGFLRRteltdanGErhda 1446
Cdd:cd05931 368 IVDPETGRELPDGEVGEIWVRGPSVASGYW---GRPEATAETFGALAATDE--GGWLRTGDLGFLHD-------GE---- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1447 LYVVGALDEAMELRGMRYHPIDIETSVIRAHKSVTE--CAVFTW----TNLLVVVVELDGSeQEALDLVPLVTNV---VL 1517
Cdd:cd05931 432 LYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRPgcVAAFSVpddgEERLVVVAEVERG-ADPADLAAIAAAIraaVA 510
|
...
gi 530392108 1518 EEH 1520
Cdd:cd05931 511 REH 513
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
350-903 |
8.98e-61 |
|
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: 219.03 E-value: 8.98e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 350 LTYGKLWTRsmkvAYSILHKLGTKQepmvRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEVPLTRKDAgsQQIGF 429
Cdd:cd05931 25 LTYAELDRR----ARAIAARLQAVG----KPGDRVLLLAPPG--LDFVAAFLGCLYAGAIAVPLPPPTPGRHA--ERLAA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 430 LLGSCGVTVALTSDACHKGLPKSptgeIPQFKGWPKLLWFVTESKHLSkPPRDWFPHIKDANnDTAYIEYKTCKDGSVLG 509
Cdd:cd05931 93 ILADAGPRVVLTTAAALAAVRAF----AASRPAAGTPRLLVVDLLPDT-SAADWPPPSPDPD-DIAYLQYTSGSTGTPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 510 VTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISI-PYSLMKvNPLSWIQKVCQYKAKV 588
Cdd:cd05931 167 VVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVLMsPAAFLR-RPLRWLRLISRYRATI 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 589 ACVKsrDMHWALVAHR----DQRDINLSSLRMLIVadGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAIR 663
Cdd:cd05931 246 SAAP--NFAYDLCVRRvrdeDLEGLDLSSWRVALN--GAEPVRPATLRRFAEAFAPFGFRPEAFRPSYGLAEAtLFVSGG 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 664 RPtddsNQPPGRGVLSMHGLTYGVIRVDSEEKLSVLTVQdVGLVMPG---AIMCsvkPDGVpQLCRTDEIGELCVC--AV 738
Cdd:cd05931 322 PP----GTGPVVLRVDRDALAGRAVAVAADDPAARELVS-CGRPLPDqevRIVD---PETG-RELPDGEVGEIWVRgpSV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 739 ATGtsYYGLSGMTKNTFEVFpmtssgAPISEYPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATALAVEP 818
Cdd:cd05931 393 ASG--YWGRPEATAETFGAL------AATDEGGWLRTGDLGFLHDGEL-YITGRLKDLIIVRGRNHYPQDIEATAEEAHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 819 MkfVYRGRIAVFSVTVLHDERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSET 898
Cdd:cd05931 464 A--LRPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREHGVAPADVVLVRPGSIPRTSSGKIQRRAC 541
|
....*
gi 530392108 899 KQLFL 903
Cdd:cd05931 542 RAAYL 546
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
976-1460 |
1.71e-58 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 208.32 E-value: 1.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 976 LQWRAQTTPDHILYTllncrGAIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPI 1055
Cdd:pfam00501 1 LERQAARTPDKTALE-----VGEGRRLTYRELDERANRLAAGLRALG-VGKGDRVAILLPNSPEWVVAFLACLKAGAVYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1056 TVRPphpqniATTLPTVKMIVEVSRSACLMTTQlICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQICK-------- 1127
Cdd:pfam00501 75 PLNP------RLPAEELAYILEDSGAKVLITDD-ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAkpadvppp 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1128 ---PCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCE----LYPSREVAICLDPYCGLGFVLWCLCSVYSGH 1200
Cdd:pfam00501 148 pppPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPrgfgLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGA 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1201 QSILIPPSELeTNPALWLLAVSQYKVRDTFCSYSVMELCtkglgsqTESLKARGLDLSRVRTCVVVAeERPRIALTQSFS 1280
Cdd:pfam00501 228 TVVLPPGFPA-LDPAALLELIERYKVTVLYGVPTLLNML-------LEAGAPKRALLSSLRLVLSGG-APLPPELARRFR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1281 KLFkdlglhPRAVSTSFGcrvnlaiclqphrlwtLAEqgTSGPdptTVYVDMRALRHDRVRLVergsphslplmesGKIL 1360
Cdd:pfam00501 299 ELF------GGALVNGYG----------------LTE--TTGV---VTTPLPLDEDLRSLGSV-------------GRPL 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1361 PGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLrrteltDAN 1440
Cdd:pfam00501 339 PGTEVKIVDDETGEPVPPGEPGELCVRGPGVMKGY---LNDPELTAEAF--------DEDGWYRTGDLGRR------DED 401
|
490 500
....*....|....*....|
gi 530392108 1441 GErhdaLYVVGALDEAMELR 1460
Cdd:pfam00501 402 GY----LEIVGRKKDQIKLG 417
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1133-1507 |
1.73e-38 |
|
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: 147.43 E-value: 1.73e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1133 TLAYLDFSVSTTGMLAGVKMSH---AATSAFCRSIKlqceLYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSe 1209
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHrnlLAAAAALAASG----GLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1210 letNPALWLLAVSQYKVRDTFCSYSVMELCTKglgsqteSLKARGLDLSRVRTCVVVAEERPrIALTQSFSKLfkdlglh 1289
Cdd:cd04433 76 ---DPEAALELIEREKVTILLGVPTLLARLLK-------APESAGYDLSSLRALVSGGAPLP-PELLERFEEA------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1290 pravstsFGCRVnlaiclqpHRLWTLAEqgtSGPDPTTVYVDMRALRhdrvrlveRGSphslplmeSGKILPGVRIIIAN 1369
Cdd:cd04433 138 -------PGIKL--------VNGYGLTE---TGGTVATGPPDDDARK--------PGS--------VGRPVPGVEVRIVD 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1370 PETkGPLGDSHLGEIWVHSAHNASGYFTiygdeslqsdhfNSRLSFGDTQTIWARTGYLGFLrrteltDANGErhdaLYV 1449
Cdd:cd04433 184 PDG-GELPPGEIGELVVRGPSVMKGYWN------------NPEATAAVDEDGWYRTGDLGRL------DEDGY----LYI 240
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530392108 1450 VGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAVF-----TWTNLLVVVVELDGSEQEALD 1507
Cdd:cd04433 241 VGRLKDMIKSGGENVYPAEVEA-VLLGHPGVAEAAVVgvpdpEWGERVVAVVVLRPGADLDAE 302
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
972-1560 |
7.80e-35 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 146.47 E-value: 7.80e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 972 LSEVLQWRAQTTPDHILYTLLNCRGAIANSLTCVQLHKRAEKIAVMLMERGHLqdGDHVALVYPPGIDLIAAFYGCLYAG 1051
Cdd:PRK05691 11 LVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAALQARASF--GDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1052 CV------PITVRPPHPQNIATtlptvkmIVEVSRSACLMTTQLICKLLRSREAAAAVDVrtwPLILDTDDLPKKRPAQI 1125
Cdd:PRK05691 89 VIavpaypPESARRHHQERLLS-------IIADAEPRLLLTVADLRDSLLQMEELAAANA---PELLCVDTLDPALAEAW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1126 CKP-CNPDTLAYLDFSVSTTGMLAGVKMSHAATSAfcrsiklqCELYPSREVAICLDP----------YCGLGFVLWCLC 1194
Cdd:PRK05691 159 QEPaLQPDDIAFLQYTSGSTALPKGVQVSHGNLVA--------NEQLIRHGFGIDLNPddvivswlplYHDMGLIGGLLQ 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1195 SVYSGHQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSVMELCTKGLGsqtESLKARgLDLSRVRtcVVVAEERP-RI 1273
Cdd:PRK05691 231 PIFSGVPCVLMSPAYFLERPLRWLEAISEYGGTISGGPDFAYRLCSERVS---ESALER-LDLSRWR--VAYSGSEPiRQ 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1274 ALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAEQ------GTSGPDPTTVYVDMRALRHDRVRLVErGS 1347
Cdd:PRK05691 305 DSLERFAEKFAACGFDPDSFFASYG----------------LAEAtlfvsgGRRGQGIPALELDAEALARNRAEPGT-GS 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1348 phslPLMESGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFNSRlsfgDTQTiWARTGY 1427
Cdd:PRK05691 368 ----VLMSCGRSQPGHAVLIVDPQSLEVLGDNRVGEIWASGPSIAHGY---WRNPEASAKTFVEH----DGRT-WLRTGD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1428 LGFLRRTEltdangerhdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSVTE--CAVFTWTNL----LVVVVELDGS 1501
Cdd:PRK05691 436 LGFLRDGE-----------LFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVVRKgrVAAFAVNHQgeegIGIAAEISRS 504
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530392108 1502 EQEAL---DLVPLVTNVVLEEHYLIVGVVVVVDIGVIPINSRGEKQRMHLRDGFLADQLDPI 1560
Cdd:PRK05691 505 VQKILppqALIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSLDSY 566
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
975-1516 |
6.22e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 136.23 E-value: 6.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 975 VLQWRAQTTPDHILYTLLNCR---GAIANSLTCVQLHKRAEKIAVMLMERGhlQDGDHVALVYPPGIDLIAAFYGCLYAG 1051
Cdd:PRK05850 6 LLRERASLQPDDAAFTFIDYEqdpAGVAETLTWSQLYRRTLNVAEELRRHG--STGDRAVILAPQGLEYIVAFLGALQAG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1052 CVPITVRPPH----------------PQNIATTLPTVKMIVEVSRSACLMTTQLIckllrsreaaAAVDVrtwpLILDTD 1115
Cdd:PRK05850 84 LIAVPLSVPQggahdervsavlrdtsPSVVLTTSAVVDDVTEYVAPQPGQSAPPV----------IEVDL----LDLDSP 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1116 DLPKKRPAQIckpcnPDTlAYLDFSVSTTGMLAGVKMSHAATSAFCRsiKLQCELYPSREVAICLD-------P-YCGLG 1187
Cdd:PRK05850 150 RGSDARPRDL-----PST-AYLQYTSGSTRTPAGVMVSHRNVIANFE--QLMSDYFGDTGGVPPPDttvvswlPfYHDMG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1188 FVLWCLCSVYSGHQSILIPPSELETNPALW--LLAVSQYkvrdtfcSYSV-----MELCTKglgsQTESLKARGLDLSRV 1260
Cdd:PRK05850 222 LVLGVCAPILGGCPAVLTSPVAFLQRPARWmqLLASNPH-------AFSAapnfaFELAVR----KTSDDDMAGLDLGGV 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1261 RTcVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAE------QGTSGPDPTTVYVDMRA 1334
Cdd:PRK05850 291 LG-IISGSERVHPATLKRFADRFAPFNLRETAIRPSYG----------------LAEatvyvaTREPGQPPESVRFDYEK 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1335 LRHDRVR---------LVERGSPHSlplmesgkilPGVRIIiaNPETKGPLGDSHLGEIWVHSAHNASGYFTiyGDESLQ 1405
Cdd:PRK05850 354 LSAGHAKrcetgggtpLVSYGSPRS----------PTVRIV--DPDTCIECPAGTVGEIWVHGDNVAAGYWQ--KPEETE 419
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1406 SDhFNSRL---SFGDTQTIWARTGYLGFLrrteltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETSVirahKSVT- 1481
Cdd:PRK05850 420 RT-FGATLvdpSPGTPEGPWLRTGDLGFI-------SEGE----LFIVGRIKDLLIVDGRNHYPDDIEATI----QEITg 483
|
570 580 590 600
....*....|....*....|....*....|....*....|...
gi 530392108 1482 -ECAVFT----WTNLLVVVVEL---DGSEQEALDLVPLVTNVV 1516
Cdd:PRK05850 484 gRVAAISvpddGTEKLVAIIELkkrGDSDEEAMDRLRTVKREV 526
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
972-1509 |
1.69e-31 |
|
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: 129.93 E-value: 1.69e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 972 LSEVLQWRAQTTPDHILYTLLNCRgaiansLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1051
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLAAALRALG-VGPGDRVALLLPNSPEFVVAFLAALRAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1052 CVPITVrpphpqNIATTLPTVKMIVEVSRSACLMTtqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnp 1131
Cdd:COG0318 74 AVVVPL------NPRLTAEELAYILEDSGARALVT--------------------------------------------- 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1132 dtlAYLDFSvS-TTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPpsel 1210
Cdd:COG0318 103 ---ALILYT-SgTTGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGATLVLLP---- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1211 ETNPALWLLAVSQYKVrdTFCSYS---VMELCtkglgsqtESLKARGLDLSRVRTCVVVAEerpriALTQSFSKLFKDLg 1287
Cdd:COG0318 175 RFDPERVLELIERERV--TVLFGVptmLARLL--------RHPEFARYDLSSLRLVVSGGA-----PLPPELLERFEER- 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1288 lhpravstsFGCRVnlaiclqpHRLWTLAEqgtSGPDPTTVYVDMRALRHDRVrlvergsphslplmesGKILPGVRIII 1367
Cdd:COG0318 239 ---------FGVRI--------VEGYGLTE---TSPVVTVNPEDPGERRPGSV----------------GRPLPGVEVRI 282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1368 ANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDESLqsdhfnSRLSFGDTqtiWARTGYLGFLrrteltDANGErhdaL 1447
Cdd:COG0318 283 VDEDGR-ELPPGEVGEIVVRGPNVMKGY---WNDPEA------TAEAFRDG---WLRTGDLGRL------DEDGY----L 339
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530392108 1448 YVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF-----TWTNLLVVVVEL-DGSEQEALDLV 1509
Cdd:COG0318 340 YIVGRKKDMIISGGENVYPAEVE-EVLAAHPGVAEAAVVgvpdeKWGERVVAFVVLrPGAELDAEELR 406
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
317-905 |
2.94e-31 |
|
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: 130.87 E-value: 2.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 317 PPSLEAALQRWGTISPKAPClTTMDTNGKPlYILTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNDpaAF 396
Cdd:cd05906 9 PRTLLELLLRAAERGPTKGI-TYIDADGSE-EFQSYQDLLEDARRLA-AGLRQLG------LRPGDSVILQFDDNE--DF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 397 MAAFYGCLLAEVVPVPIEVPLTRKDAGSQ-----QIGFLLGSCgvtVALTSDACHKGLpksptgeIPQFKGWPKLLWFVT 471
Cdd:cd05906 78 IPAFWACVLAGFVPAPLTVPPTYDEPNARlrklrHIWQLLGSP---VVLTDAELVAEF-------AGLETLSGLPGIRVL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 472 ESKHLSKPPRDWFPHIKDAnNDTAYIEYKTCKDGSVLGVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHG 551
Cdd:cd05906 148 SIEELLDTAADHDLPQSRP-DDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVEL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 552 ILTSVMNMMHVISIPYSLMKVNPLSWIQKVCQYKAKV------ACVKSRDmhwaLVAHRDQRDINLSSLRMLIVADGANp 625
Cdd:cd05906 227 HLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTItwapnfAFALLND----LLEEIEDGTWDLSSLRYLVNAGEAV- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 626 wSISSCDAFLNVFQSKGLRQEVICPCASSPEalTVAirrptddsnqppgrgvlsmhGLTYGviRVDSEEKLS-VLTVQDV 704
Cdd:cd05906 302 -VAKTIRRLLRLLEPYGLPPDAIRPAFGMTE--TCS--------------------GVIYS--RSFPTYDHSqALEFVSL 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 705 GLVMPGAIMCSVKPDGvpQLCRTDEIGELCVCavatGTS----YYGLSGMTKNTFevfpmTSSGapiseypFIRTGLLGF 780
Cdd:cd05906 357 GRPIPGVSMRIVDDEG--QLLPEGEVGRLQVR----GPVvtkgYYNNPEANAEAF-----TEDG-------WFRTGDLGF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 781 VGPGGLVFvVGKMDGLMVVSGRRHNADDIVAtalAVEPMKFVYRGRIAVFSVTVLHD--ERIVIVAeqrpdSTEEDSFQW 858
Cdd:cd05906 419 LDNGNLTI-TGRTKDTIIVNGVNYYSHEIEA---AVEEVPGVEPSFTAAFAVRDPGAetEELAIFF-----VPEYDLQDA 489
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 530392108 859 MSRVLQAIDSI--HQVGVYCLALVP--ANTLPKTPLGGIHLSETKQLFLEG 905
Cdd:cd05906 490 LSETLRAIRSVvsREVGVSPAYLIPlpKEEIPKTSLGKIQRSKLKAAFEAG 540
|
|
| DMAP_binding |
pfam06464 |
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor. |
8-118 |
1.60e-30 |
|
DMAP1-binding Domain; This domain binds DMAP1, a transcriptional co-repressor.
Pssm-ID: 368923 [Multi-domain] Cd Length: 104 Bit Score: 116.36 E-value: 1.60e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 8 GMALPLEVRARLAELELELSEGDITQKGYEKKRSKLIGAYLPQPprvdqalpqerRAPVTPSSASRYHR-RRSSGSRDER 86
Cdd:pfam06464 2 PPSLPDDVRERLSELDLDLSEGDITEKGYEKKKLKLLRKFLLHP-----------ETPTKLSAEAQNQLaSLETKLRDEE 70
|
90 100 110
....*....|....*....|....*....|..
gi 530392108 87 YRSDVHTEAVQAALAKHKERKMAVPMPSKRRS 118
Cdd:pfam06464 71 LSEEVYLEKVKALLAKELERENGLNAPTKEQS 102
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
320-907 |
1.41e-29 |
|
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: 124.15 E-value: 1.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 320 LEAALQRWGTISPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdpAAFMAA 399
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRR------LTYAELDARARRLA-AALRALG------VGPGDRVALLLPNS--PEFVVA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 400 FYGCLLAEVVPVPIEVPLTRKdagsqQIGFLLGSCGVTVALTSDACH----KGLPKsptgeipqfkgwpkllwfvteskh 475
Cdd:COG0318 66 FLAALRAGAVVVPLNPRLTAE-----ELAYILEDSGARALVTALILYtsgtTGRPK------------------------ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 476 lskpprdwfphikdanndtayieyktckdgsvlGVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTS 555
Cdd:COG0318 117 ---------------------------------GVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAP 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 556 VMNMMHVISIPyslmKVNPLSWIQKVCQYKA-KVACVKSrdMHWALVAHRDQRDINLSSLRMLIVadGANPWSISSCDAF 634
Cdd:COG0318 164 LLAGATLVLLP----RFDPERVLELIERERVtVLFGVPT--MLARLLRHPEFARYDLSSLRLVVS--GGAPLPPELLERF 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 635 LNVFQSkglrqeVICPC-ASSpEALTVAIRRPTDDSNQPPGRgvlsmhgltygvirvdseeklsvltvqdVGLVMPGAIM 713
Cdd:COG0318 236 EERFGV------RIVEGyGLT-ETSPVVTVNPEDPGERRPGS----------------------------VGRPLPGVEV 280
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 714 CSVKPDGVPqlCRTDEIGELCVC--AVATGtsYYGLSGMTKNTFEVfpmtssgapiseyPFIRTGLLGFVGPGGLVFVVG 791
Cdd:COG0318 281 RIVDEDGRE--LPPGEVGEIVVRgpNVMKG--YWNDPEATAEAFRD-------------GWLRTGDLGRLDEDGYLYIVG 343
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 792 KMDGLMVVSGRRHNADDIVATALAVEPMKfvyrgRIAVFSVTV-LHDERIV--IVAEQRPDSTEEDSFQWMSRVL---QA 865
Cdd:COG0318 344 RKKDMIISGGENVYPAEVEEVLAAHPGVA-----EAAVVGVPDeKWGERVVafVVLRPGAELDAEELRAFLRERLaryKV 418
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 530392108 866 IDSIHQVGvyclalvpanTLPKTPLGGIHLSETKQLFLEGSL 907
Cdd:COG0318 419 PRRVEFVD----------ELPRTASGKIDRRALRERYAAGAL 450
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
350-909 |
1.67e-29 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 125.89 E-value: 1.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 350 LTYGKLWTRSMKVAYSILhKLGtkqepmVRPGDRVALVfPNNDPAaFMAAFYGCLLAEVVPVPIEVP--LTRKDAGSQQI 427
Cdd:PRK09192 50 LPYQTLRARAEAGARRLL-ALG------LKPGDRVALI-AETDGD-FVEAFFACQYAGLVPVPLPLPmgFGGRESYIAQL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 428 GFLLGSCGVTVALTSDACHKGLPKSPTGEIPQFKGWPKLLwfvteskHLSKPPRDWFPHIKDanNDTAYIEYKTckdGSV 507
Cdd:PRK09192 121 RGMLASAQPAAIITPDELLPWVNEATHGNPLLHVLSHAWF-------KALPEADVALPRPTP--DDIAYLQYSS---GST 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 508 ---LGVTVTRTALLTHCQALTQ-ACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYSLMKVNPLSWIQKVCQ 583
Cdd:PRK09192 189 rfpRGVIITHRALMANLRAISHdGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVATQLSVDYLPTRDFARRPLQWLDLISR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 584 YKAKVAcvKSRDMHWALVAHR----DQRDINLSSLRmlIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlT 659
Cdd:PRK09192 269 NRGTIS--YSPPFGYELCARRvnskDLAELDLSCWR--VAGIGADMIRPDVLHQFAEAFAPAGFDDKAFMPSYGLAEA-T 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 660 VAIrrptddSNQPPGRGV----LSMHGLTYGVIRVDSEEK-LSVLTVQDVGLVMPGAIMCSVKPDG--VPQLcrtdEIGE 732
Cdd:PRK09192 344 LAV------SFSPLGSGIvveeVDRDRLEYQGKAVAPGAEtRRVRTFVNCGKALPGHEIEIRNEAGmpLPER----VVGH 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 733 LCVcavatgtsyYGLSGMTkntfEVFPMTSSGAPISEYPFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVAT 812
Cdd:PRK09192 414 ICV---------RGPSLMS----GYFRDEESQDVLAADGWLDTGDLGYLLDGYLY-ITGRAKDLIIINGRNIWPQDIEWI 479
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 813 AlavEPMKFVYRGRIAVFSVTVLHDERIVIVAEQRPdSTEEDSFQWMSRVLQAIDSIHqvGVYCL-ALVPANTLPKTPLG 891
Cdd:PRK09192 480 A---EQEPELRSGDAAAFSIAQENGEKIVLLVQCRI-SDEERRGQLIHALAALVRSEF--GVEAAvELVPPHSLPRTSSG 553
|
570
....*....|....*...
gi 530392108 892 GIHLSETKQLFLEGSLHP 909
Cdd:PRK09192 554 KLSRAKAKKRYLSGAFAS 571
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
379-907 |
2.27e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 113.29 E-value: 2.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 379 RPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEVPltrKDAG-SQQIGFLLGSCGVTVALTSDACHKGLPKSptgei 457
Cdd:PRK07769 77 KPGDRVAILAPQN--LDYLIAFFGALYAGRIAVPLFDP---AEPGhVGRLHAVLDDCTPSAILTTTDSAEGVRKF----- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 458 pqFKGWPKllwfvteskhlSKPPR-------------DWFPhiKDANNDT-AYIEYKTckdGSV---LGVTVTRTALLTH 520
Cdd:PRK07769 147 --FRARPA-----------KERPRviavdavpdevgaTWVP--PEANEDTiAYLQYTS---GSTripAGVQITHLNLPTN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 521 CQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNmmHVISI--PYSLMKvNPLSWIQKVCQYKAKVACVKSRDMHW 598
Cdd:PRK07769 209 VLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLG--HYITFmsPAAFVR-RPGRWIRELARKPGGTGGTFSAAPNF 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 599 A--LVAHR-----DQRDINLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEALTVAIRRPTDDSNQ 671
Cdd:PRK07769 286 AfeHAAARglpkdGEPPLDLSNVKGLL--NGSEPVSPASMRKFNEAFAPYGLPPTAIKPSYGMAEATLFVSTTPMDEEPT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 672 ppgrgvlsmhgltygVIRVDSEEkLSVLTVQDVGLVMPGAI-------------MCSVKPDGVPQLcRTDEIGELCVCAV 738
Cdd:PRK07769 364 ---------------VIYVDRDE-LNAGRFVEVPADAPNAVaqvsagkvgvsewAVIVDPETASEL-PDGQIGEIWLHGN 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 739 ATGTSYYGLSGMTKNTFE------VFPMTSSGAPiSEYPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVAT 812
Cdd:PRK07769 427 NIGTGYWGKPEETAATFQnilksrLSESHAEGAP-DDALWVRTGDYGVYFDGEL-YITGRVKDLVIIDGRNHYPQDLEYT 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 813 ALavEPMKFVYRGRIAVFSV-------TVLHD-------------ERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQV 872
Cdd:PRK07769 505 AQ--EATKALRTGYVAAFSVpanqlpqVVFDDshaglkfdpedtsEQLVIVAERAPGAHKLDPQPIADDIRAAIAVRHGV 582
|
570 580 590
....*....|....*....|....*....|....*
gi 530392108 873 GVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSL 907
Cdd:PRK07769 583 TVRDVLLVPAGSIPRTSSGKIARRACRAAYLDGSL 617
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
972-1495 |
5.76e-25 |
|
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: 111.22 E-value: 5.76e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 972 LSEVLQWRAQTTPDHILYTllncrgaIANSLTCV-----QLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYG 1046
Cdd:cd05906 12 LLELLLRAAERGPTKGITY-------IDADGSEEfqsyqDLLEDARRLAAGLRQLG-LRPGDSVILQFDDNEDFIPAFWA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1047 CLYAGCVPITVRPPHP-QNIATTLPTVKMIVEVSRSA-CLMTTQLICKLLRSREAA--AAVDVRTWPLILDTDDLPKKRP 1122
Cdd:cd05906 84 CVLAGFVPAPLTVPPTyDEPNARLRKLRHIWQLLGSPvVLTDAELVAEFAGLETLSglPGIRVLSIEELLDTAADHDLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1123 AQickpcnPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSiKLQCELYPSREVA---ICLDPYCGLGFVlwCLCSVYSG 1199
Cdd:cd05906 164 SR------PDDLALLMLTSGSTGFPKAVPLTHRNILARSAG-KIQHNGLTPQDVFlnwVPLDHVGGLVEL--HLRAVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1200 HQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSvmeLCTKgLGSQTESLKARGLDLSRVRtCVVVAEERPRIALTQSF 1279
Cdd:cd05906 235 CQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNF---AFAL-LNDLLEEIEDGTWDLSSLR-YLVNAGEAVVAKTIRRL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1280 SKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAEQGtSGpdpTTVYVDMRALRHdrvrlvergsPHSLPLMESGKI 1359
Cdd:cd05906 310 LRLLEPYGLPPDAIRPAFG----------------MTETC-SG---VIYSRSFPTYDH----------SQALEFVSLGRP 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1360 LPGVRIIIANPETKGpLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLRrteltda 1439
Cdd:cd05906 360 IPGVSMRIVDDEGQL-LPEGEVGRLQVRGPVVTKGY---YNNPEANAEAF--------TEDGWFRTGDLGFLD------- 420
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530392108 1440 NGErhdaLYVVGALDEAMELRGMRYHPIDIETSV----IRAHKSVTECAVF---TWTNLLVVV 1495
Cdd:cd05906 421 NGN----LTITGRTKDTIIVNGVNYYSHEIEAAVeevpGVEPSFTAAFAVRdpgAETEELAIF 479
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
999-1480 |
8.84e-25 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 111.37 E-value: 8.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 999 ANSLTCVQLHKRAEKIAVMLMErgHLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNIATTLPTVkmiVEV 1078
Cdd:PRK12476 66 AVELTWTQLGVRLRAVGARLQQ--VAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFAPELPGHAERLDTA---LRD 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1079 SRSACLMTTQLICKLLRSREAAAAVDVRtwPLILDTDDLPKkRPAQICKPCNPDT--LAYLDFSVSTTGMLAGVKMSHAA 1156
Cdd:PRK12476 141 AEPTVVLTTTAAAEAVEGFLRNLPRLRR--PRVIAIDAIPD-SAGESFVPVELDTddVSHLQYTSGSTRPPVGVEITHRA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1157 TSA----FCRSIKLqceLYPSREVAICLDPYCGLGFVLWCLCSVYSGHqSILIPPSELETNPALWLLAVSQ-YKVRDTFC 1231
Cdd:PRK12476 218 VGTnlvqMILSIDL---LDRNTHGVSWLPLYHDMGLSMIGFPAVYGGH-STLMSPTAFVRRPQRWIKALSEgSRTGRVVT 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1232 SYS--VMELCT-KGLGSQTEslkarGLDLSRVrtCVVVAEERPRIALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclq 1308
Cdd:PRK12476 294 AAPnfAYEWAAqRGLPAEGD-----DIDLSNV--VLIIGSEPVSIDAVTTFNKAFAPYGLPRTAFKPSYG---------- 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1309 phrlwtLAEQ----GTSGPD--PTTVYVDMRALRHDRVRLVERGSPHSLPLMESGKILPGVRIIIANPETKGPLGDSHLG 1382
Cdd:PRK12476 357 ------IAEAtlfvATIAPDaePSVVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVARSQWAVIVDPDTGAELPDGEVG 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1383 EIWVHSAHNASGYFTiYGDESLQSDH--FNSRLSFG------DTQTIWARTGYLGFLRrteltdaNGErhdaLYVVGALD 1454
Cdd:PRK12476 431 EIWLHGDNIGRGYWG-RPEETERTFGakLQSRLAEGshadgaADDGTWLRTGDLGVYL-------DGE----LYITGRIA 498
|
490 500
....*....|....*....|....*.
gi 530392108 1455 EAMELRGMRYHPIDIETSVIRAHKSV 1480
Cdd:PRK12476 499 DLIVIDGRNHYPQDIEATVAEASPMV 524
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
962-1505 |
2.55e-24 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 109.71 E-value: 2.55e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 962 DNDQARK---FLFLSEVLQWRAQTTPDHILYTLlncRGAIANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGI 1038
Cdd:PRK09192 10 TSSLPRRyadFPTLVEALDYAALGEAGMNFYDR---RGQLEEALPYQTLRARAEAGARRLLALG-LKPGDRVALIAETDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1039 DLIAAFYGCLYAGCVPITVrpPHPQNI---ATTLPTVKMIVEVSRSACLMTTQLICKLLrsreaAAAVDVRTWPLILDTD 1115
Cdd:PRK09192 86 DFVEAFFACQYAGLVPVPL--PLPMGFggrESYIAQLRGMLASAQPAAIITPDELLPWV-----NEATHGNPLLHVLSHA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1116 DLpKKRPAQICK--PCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQ-CELYPSREVAICLDPYCGLGFVlWC 1192
Cdd:PRK09192 159 WF-KALPEADVAlpRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAISHDgLKVRPGDRCVSWLPFYHDMGLV-GF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1193 LCSVYSGHQSI-LIPPSELETNPALWLLAVSqyKVRDTFcSYSV---MELCTKGLGSQTESlkarGLDLSRVRTCVVVAE 1268
Cdd:PRK09192 237 LLTPVATQLSVdYLPTRDFARRPLQWLDLIS--RNRGTI-SYSPpfgYELCARRVNSKDLA----ELDLSCWRVAGIGAD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1269 E-RPRIalTQSFSKLFKDLGLHPRAVSTSFG-CRVNLAICLQPHrlwtlaEQGtsgpdpttvyvdMRALRHDRVRLVERG 1346
Cdd:PRK09192 310 MiRPDV--LHQFAEAFAPAGFDDKAFMPSYGlAEATLAVSFSPL------GSG------------IVVEEVDRDRLEYQG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1347 spHSLPLMES----------GKILPGVRIIIANpETKGPLGDSHLGEIWVHSAHNASGYFtiyGDESlqsdhfnsrlsfg 1416
Cdd:PRK09192 370 --KAVAPGAEtrrvrtfvncGKALPGHEIEIRN-EAGMPLPERVVGHICVRGPSLMSGYF---RDEE------------- 430
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1417 DTQTI----WARTGYLGFLrrteltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETSV-----IRAHksvtECAVFT 1487
Cdd:PRK09192 431 SQDVLaadgWLDTGDLGYL-------LDGY----LYITGRAKDLIIINGRNIWPQDIEWIAeqepeLRSG----DAAAFS 495
|
570 580
....*....|....*....|..
gi 530392108 1488 WTN----LLVVVVELDGSEQEA 1505
Cdd:PRK09192 496 IAQengeKIVLLVQCRISDEER 517
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
976-1480 |
2.98e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 109.82 E-value: 2.98e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 976 LQWRAQTTPDHILYTLLNC---RGAIANSLTCVQLHKRAEKIAVMLMERGhlQDGDHVALVYPPGIDLIAAFYGCLYAGC 1052
Cdd:PRK07769 27 VERWAKVRGDKLAYRFLDFsteRDGVARDLTWSQFGARNRAVGARLQQVT--KPGDRVAILAPQNLDYLIAFFGALYAGR 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1053 VPITVRPPHPQNIATTLPTVkmIVEVSRSACLMTT---QLICKLLRSREAAAAvdvrtwPLILDTDDLPKKRPAQICKP- 1128
Cdd:PRK07769 105 IAVPLFDPAEPGHVGRLHAV--LDDCTPSAILTTTdsaEGVRKFFRARPAKER------PRVIAVDAVPDEVGATWVPPe 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1129 CNPDTLAYLDFSVSTTGMLAGVKMSH--AATSAF--CRSIKLQcelYPSREVAiCLDPYCGLGFVLWCLCSVYSGHQSIL 1204
Cdd:PRK07769 177 ANEDTIAYLQYTSGSTRIPAGVQITHlnLPTNVLqvIDALEGQ---EGDRGVS-WLPFFHDMGLITVLLPALLGHYITFM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1205 IPPSELEtNPALWLLAVSQyKVRDTFCSYSV-----MELCT-KGLGSQTESlkarGLDLSRVRtCVVVAEERPRIALTQS 1278
Cdd:PRK07769 253 SPAAFVR-RPGRWIRELAR-KPGGTGGTFSAapnfaFEHAAaRGLPKDGEP----PLDLSNVK-GLLNGSEPVSPASMRK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1279 FSKLFKDLGLHPRAVSTSFGcrvnlaiclqphrlwtLAEQ----GTSGPD--PTTVYVDMRALRHDRVRLVERGSPHSLP 1352
Cdd:PRK07769 326 FNEAFAPYGLPPTAIKPSYG----------------MAEAtlfvSTTPMDeePTVIYVDRDELNAGRFVEVPADAPNAVA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1353 LMESGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNASGYftiYG--DESLQSDH--FNSRLSFGDTQ-----TIWA 1423
Cdd:PRK07769 390 QVSAGKVGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGY---WGkpEETAATFQniLKSRLSESHAEgapddALWV 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 530392108 1424 RTGYLGflrrtelTDANGErhdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSV 1480
Cdd:PRK07769 467 RTGDYG-------VYFDGE----LYITGRVKDLVIIDGRNHYPQDLEYTAQEATKAL 512
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
343-905 |
6.10e-24 |
|
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: 107.57 E-value: 6.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 343 NGKPLYIlTYGKLWTRSMKVaysilhkLGTKQEPMVRPGDRValVFPNNDPAAFMAAFYGCLLAEVVPVPievpltrkda 422
Cdd:cd05908 10 DKKEKFV-SYRHLREEALGY-------LGALQELGIKPGQEV--VFQITHNNKFLYLFWACLLGGMIAVP---------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 423 gsqqigfllgscgvtVALTSDACHKglpksptgeIPQFKGWPKLL--WFVTESKHLSKPPrdwfphikdanNDTAYIEYK 500
Cdd:cd05908 70 ---------------VSIGSNEEHK---------LKLNKVWNTLKnpYLITEEEVLCELA-----------DELAFIQFS 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 501 TCKDGSVLGVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHGILTSVMNMMHVISIPYSLMKVNPLSWIQK 580
Cdd:cd05908 115 SGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRLFIRRPILWLKK 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 581 VCQYKAKVACVKSRDMHWALVAHRDQR--DINLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAl 658
Cdd:cd05908 195 ASEHKATIVSSPNFGYKYFLKTLKPEKanDWDLSSIRMIL--NGAEPIDYELCHEFLDHMSKYGLKRNAILPVYGLAEA- 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 659 TVAIRRPTDDSNQPPgrgvLSMH--GLTYG--VIRVDSEEKlSVLTVQDVGLVMPgaiMCSVK-PDGVPQLCRTDEIGEL 733
Cdd:cd05908 272 SVGASLPKAQSPFKT----ITLGrrHVTHGepEPEVDKKDS-ECLTFVEVGKPID---ETDIRiCDEDNKILPDGYIGHI 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 734 CVCAVATGTSYYGLSGMTKNTfevfpMTSSGapiseypFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATA 813
Cdd:cd05908 344 QIRGKNVTPGYYNNPEATAKV-----FTDDG-------WLKTGDLGFIRNGRLV-ITGREKDIIFVNGQNVYPHDIERIA 410
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 814 LAVEPmkfVYRGRIAVFSV--TVLHDERIVIVAEQRpdsTEEDSFQWMSRVLQAID------SIHQVgvyclalVPANTL 885
Cdd:cd05908 411 EELEG---VELGRVVACGVnnSNTRNEEIFCFIEHR---KSEDDFYPLGKKIKKHLnkrggwQINEV-------LPIRRI 477
|
570 580
....*....|....*....|
gi 530392108 886 PKTPLGGIHLSETKQLFLEG 905
Cdd:cd05908 478 PKTTSGKVKRYELAQRYQSG 497
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
324-800 |
2.63e-23 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 104.70 E-value: 2.63e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 324 LQRWGTISPKAPCLTTMDTngkplYILTYGKLWTRSMKVAYSiLHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGC 403
Cdd:pfam00501 1 LERQAARTPDKTALEVGEG-----RRLTYRELDERANRLAAG-LRALG------VGKGDRVAILLPNS--PEWVVAFLAC 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 404 LLAEVVPVPIEVpltrkDAGSQQIGFLLGSCGVTVALTSD--------ACHKGLPKSPTGEIPQFKGWPKLLWFVTESKH 475
Cdd:pfam00501 67 LKAGAVYVPLNP-----RLPAEELAYILEDSGAKVLITDDalkleellEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKP 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 476 LSKPPRdwfPHIKDANNDTAYIEY--------KtckdgsvlGVTVTRTALLTHCQALTQAC----GYTEAETIVNVLDFK 543
Cdd:pfam00501 142 ADVPPP---PPPPPDPDDLAYIIYtsgttgkpK--------GVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLF 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 544 KDVGLWHGILTSVMNMMHVISIPYSLMKvNPLSWIQKVCQYKAKVACVKSRDMHwALVAHRDQRDINLSSLRMLIVadGA 623
Cdd:pfam00501 211 HDFGLSLGLLGPLLAGATVVLPPGFPAL-DPAALLELIERYKVTVLYGVPTLLN-MLLEAGAPKRALLSSLRLVLS--GG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 624 NPWSISSCDAFLNVFqskglrqevicpcasspealtvairrptddsnqppGRGVLSMHGLT--YGVIRVDSEEKLSVLTV 701
Cdd:pfam00501 287 APLPPELARRFRELF-----------------------------------GGALVNGYGLTetTGVVTTPLPLDEDLRSL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 702 QDVGLVMPGAIMCSVKPDGVpQLCRTDEIGELCV--CAVATGtsYYGLSGMTKNTFEvfpmtssgapisEYPFIRTGLLG 779
Cdd:pfam00501 332 GSVGRPLPGTEVKIVDDETG-EPVPPGEPGELCVrgPGVMKG--YLNDPELTAEAFD------------EDGWYRTGDLG 396
|
490 500
....*....|....*....|.
gi 530392108 780 FVGPGGLVFVVGKMDGLMVVS 800
Cdd:pfam00501 397 RRDEDGYLEIVGRKKDQIKLG 417
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1006-1485 |
4.22e-23 |
|
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: 103.88 E-value: 4.22e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1006 QLHKRAEKIAVMLMERGHLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITvrPPHPQN-IATtlptvkmIVEVSRSA 1082
Cdd:TIGR01733 4 ELDERANRLARHLRAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAayVPLD--PAYPAErLAF-------ILEDAGAR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1083 CLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAqickPCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCR 1162
Cdd:TIGR01733 75 LLLTDSALASRLAGLVLPVILLDPLELAALDDAPAPPPPDA----PSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1163 SIklqCELYPSREVAICLDpYCGLGF------VLWCLcsvYSGHQSILIPPSELETNPALWLLAVSQYKVRDTFCSYSVM 1236
Cdd:TIGR01733 151 WL---ARRYGLDPDDRVLQ-FASLSFdasveeIFGAL---LAGATLVVPPEDEERDDAALLAALIAEHPVTVLNLTPSLL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1237 ELCtkglgsqtesLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDLglhpravstsfgcrvnlaiclqphRLWTla 1316
Cdd:TIGR01733 224 ALL----------AAALPPALASLRL-VILGGEALTPALVDRWRARGPGA------------------------RLIN-- 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1317 eqgTSGPDPTTVYVDMRALRHDRVRlvergSPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYF 1396
Cdd:TIGR01733 267 ---LYGPTETTVWSTATLVDPDDAP-----RESPVPI---GRPLANTRLYVLDDDLR-PVPVGVVGELYIGGPGVARGYL 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1397 tiyGDESLQSDHFNSRLSFGDTQTIWARTGYLGflRRteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRA 1476
Cdd:TIGR01733 335 ---NRPELTAERFVPDPFAGGDGARLYRTGDLV--RY----LPDGN----LEFLGRIDDQVKIRGYRIELGEIE-AALLR 400
|
....*....
gi 530392108 1477 HKSVTECAV 1485
Cdd:TIGR01733 401 HPGVREAVV 409
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
319-893 |
4.65e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 105.79 E-value: 4.65e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 319 SLEAALQRWGTISPKAPCLTTMDTNGKPLYI---LTYGKLWTRSMKVAYSiLHKLGtkqepmvRPGDRVALVFPNNdpAA 395
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTFIDYEQDPAGVaetLTWSQLYRRTLNVAEE-LRRHG-------STGDRAVILAPQG--LE 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 396 FMAAFYGCLLAEVVPVPIEVPLTRkdAGSQQIGFLLGSCGVTVALTS----DACHKGLPKSPTGEIPqfkgwpkllWFVT 471
Cdd:PRK05850 72 YIVAFLGALQAGLIAVPLSVPQGG--AHDERVSAVLRDTSPSVVLTTsavvDDVTEYVAPQPGQSAP---------PVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 472 ------ESKHLSKPPRDWFPhikdannDTAYIEYKTCKDGSVLGVTVTRTALLTHC-QALTQACGYTEAE-----TIVNV 539
Cdd:PRK05850 141 vdlldlDSPRGSDARPRDLP-------STAYLQYTSGSTRTPAGVMVSHRNVIANFeQLMSDYFGDTGGVpppdtTVVSW 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 540 LDFKKDVGLWHGILTSVMNMMH-VISIPYSLMKvNPLSWIQKVCQYKAKVACVKSrdmhWAL-VAHRDQRDINLSSL--- 614
Cdd:PRK05850 214 LPFYHDMGLVLGVCAPILGGCPaVLTSPVAFLQ-RPARWMQLLASNPHAFSAAPN----FAFeLAVRKTSDDDMAGLdlg 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 615 RMLIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAIRRPtddsNQPPGrgvlsmhgltygVIRVDSE 693
Cdd:PRK05850 289 GVLGIISGSERVHPATLKRFADRFAPFNLRETAIRPSYGLAEAtVYVATREP----GQPPE------------SVRFDYE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 694 eKLSVLTVQ----DVG--LVMPGAIMCS----VKPDGVPQlCRTDEIGELCVCA--VATGtsYYGLSGMTKNTFE---VF 758
Cdd:PRK05850 353 -KLSAGHAKrcetGGGtpLVSYGSPRSPtvriVDPDTCIE-CPAGTVGEIWVHGdnVAAG--YWQKPEETERTFGatlVD 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 759 PmtSSGAPISeyPFIRTGLLGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATalavepMKFVYRGRIAVFSVTVLHDE 838
Cdd:PRK05850 429 P--SPGTPEG--PWLRTGDLGFISEGEL-FIVGRIKDLLIVDGRNHYPDDIEAT------IQEITGGRVAAISVPDDGTE 497
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 839 RIVIVAE-QRPDSTEEDSFQWM----SRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGI 893
Cdd:PRK05850 498 KLVAIIElKKRGDSDEEAMDRLrtvkREVTSAISKSHGLSVADLVLVAPGSIPITTSGKI 557
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
341-909 |
5.80e-23 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 105.59 E-value: 5.80e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 341 DTNGKPLYiLTYGKLWTRsmkvaysiLHKLGTKQEPMVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPI---EVPl 417
Cdd:PRK12476 61 SAAGCAVE-LTWTQLGVR--------LRAVGARLQQVAGPGDRVAILAPQG--IDYVAGFFAAIKAGTIAVPLfapELP- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 418 trkdAGSQQIGFLLGSCGVTVALTSDAChkglpkspTGEIPQFkgwpkllwfvteskhLSKPPRDWFPH------IKDA- 490
Cdd:PRK12476 129 ----GHAERLDTALRDAEPTVVLTTTAA--------AEAVEGF---------------LRNLPRLRRPRviaidaIPDSa 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 491 ----------NNDTAYIEYKTCKDGSVLGVTVTRTALLTHCQALTQACGYTEAETI-VNVLDFKKDVGLWHGILTSVMNM 559
Cdd:PRK12476 182 gesfvpveldTDDVSHLQYTSGSTRPPVGVEITHRAVGTNLVQMILSIDLLDRNTHgVSWLPLYHDMGLSMIGFPAVYGG 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 560 MHVISIPYSLMKvNPLSWIQKV---CQYKAKVACVKSRDMHWAlvAHR----DQRDINLSSLRMLIvadGANPWSISSCD 632
Cdd:PRK12476 262 HSTLMSPTAFVR-RPQRWIKALsegSRTGRVVTAAPNFAYEWA--AQRglpaEGDDIDLSNVVLII---GSEPVSIDAVT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 633 AFLNVFQSKGLRQEVICPCASSPEA-LTVAirrpTDDSNQPPGRGVLSMHGLTYG-VIRVDSEEKLSVLTVQdVGLVMPG 710
Cdd:PRK12476 336 TFNKAFAPYGLPRTAFKPSYGIAEAtLFVA----TIAPDAEPSVVYLDREQLGAGrAVRVAADAPNAVAHVS-CGQVARS 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 711 AIMCSVKPDGVPQLcRTDEIGELCVCAVATGTSYYGLSGMTKNTFEV-----FPMTS--SGAPISEyPFIRTGLLGFVGP 783
Cdd:PRK12476 411 QWAVIVDPDTGAEL-PDGEVGEIWLHGDNIGRGYWGRPEETERTFGAklqsrLAEGShaDGAADDG-TWLRTGDLGVYLD 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 784 GGLvFVVGKMDGLMVVSGRRHNADDIVATALAVEPMkfVYRGRIAVFSVTVLHDERIVIVAEQRPDSTEEDSFQWMSRVL 863
Cdd:PRK12476 489 GEL-YITGRIADLIVIDGRNHYPQDIEATVAEASPM--VRRGYVTAFTVPAEDNERLVIVAERAAGTSRADPAPAIDAIR 565
|
570 580 590 600
....*....|....*....|....*....|....*....|....*.
gi 530392108 864 QAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLHP 909
Cdd:PRK12476 566 AAVSRRHGLAVADVRLVPAGAIPRTTSGKLARRACRAQYLDGRLGV 611
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1001-1486 |
3.92e-22 |
|
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: 101.91 E-value: 3.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1001 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVpitVRPPHPQNIATTL--------PTV 1072
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLG-LKKGDVVGIISPNSTYYPPVFLGCLFAGGI---FSAANPIYTADELahqlkiskPKV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1073 kMIVEVSrsaCLMTTQLICK---------LLRSREAAAA--VDVRTWPLILDTDDLPkkrpaqICKPCNPDTLAYLDFSV 1141
Cdd:cd05911 86 -IFTDPD---GLEKVKEAAKelgpkdkiiVLDDKPDGVLsiEDLLSPTLGEEDEDLP------PPLKDGKDDTAAILYSS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1142 STTGMLAGVKMSHaatSAFCRSIKLQC----ELYPSREVAICLDPY---CGLgfvLWCLCSVYSGHQSILIPpselETNP 1214
Cdd:cd05911 156 GTTGLPKGVCLSH---RNLIANLSQVQtflyGNDGSNDVILGFLPLyhiYGL---FTTLASLLNGATVIIMP----KFDS 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1215 ALWLLAVSQYKVRDTFCSYSVMELctkgLGSQTESLKArglDLSRVRTCVVVAEerpriALTQSFSKLFKdlglhpravs 1294
Cdd:cd05911 226 ELFLDLIEKYKITFLYLVPPIAAA----LAKSPLLDKY---DLSSLRVILSGGA-----PLSKELQELLA---------- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1295 tsfgCRVNLAICLQphrLWTLAEqgTSGPDPTTVYVDmralrhdrvrlVERGSphslplmeSGKILPGVRIIIANPETKG 1374
Cdd:cd05911 284 ----KRFPNATIKQ---GYGMTE--TGGILTVNPDGD-----------DKPGS--------VGRLLPNVEAKIVDDDGKD 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1375 PLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLrrteltDANGErhdaLYVVGALD 1454
Cdd:cd05911 336 SLGPNEPGEICVRGPQVMKGY---YNNPEATKETF--------DEDGWLHTGDIGYF------DEDGY----LYIVDRKK 394
|
490 500 510
....*....|....*....|....*....|..
gi 530392108 1455 EAMELRGMRYHPIDIEtSVIRAHKSVTECAVF 1486
Cdd:cd05911 395 ELIKYKGFQVAPAELE-AVLLEHPGVADAAVI 425
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
999-1488 |
1.26e-18 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 91.28 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 999 ANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPItvrpphPQNIATTLPTVKMIVEV 1078
Cdd:cd05959 27 AGSLTYAELEAEARRVAGALRALG-VKREERVLLIMLDTVDFPTAFLGAIRAGIVPV------PVNTLLTPDDYAYYLED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1079 SRSACLMTTQLICKLLRSREAAAAVDVRT----------WPLILDTDDLPKKRPAQICKPCNPDTLAYLDFSVSTTGMLA 1148
Cdd:cd05959 100 SRARVVVVSGELAPVLAAALTKSEHTLVVlivsggagpeAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGRPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1149 GVKMSHAatsafcrSIKLQCELYPSREVAICLDPYC----------GLGFVLWCLCSVysGHQSILIPpsELETnPALWL 1218
Cdd:cd05959 180 GVVHLHA-------DIYWTAELYARNVLGIREDDVCfsaaklffayGLGNSLTFPLSV--GATTVLMP--ERPT-PAAVF 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1219 LAVSQYKvRDTFcsYSVMELCTKGLGSqtESLKARglDLSRVRTCVVVAEerpriALTQSFSKLFKDLglhpravstsFG 1298
Cdd:cd05959 248 KRIRRYR-PTVF--FGVPTLYAAMLAA--PNLPSR--DLSSLRLCVSAGE-----ALPAEVGERWKAR----------FG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1299 CRVnlaiclqphrlwtlaEQGTSGPDPTTVYVDMRAlrhDRVRLverGSphslplmeSGKILPGVRIIIANpETKGPLGD 1378
Cdd:cd05959 306 LDI---------------LDGIGSTEMLHIFLSNRP---GRVRY---GT--------TGKPVPGYEVELRD-EDGGDVAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1379 SHLGEIWVHSAHNASGYFTIYGDeslqsdhfnSRLSFgdtQTIWARTGYlGFLRrteltDANGerhdALYVVGALDEAME 1458
Cdd:cd05959 356 GEPGELYVRGPSSATMYWNNRDK---------TRDTF---QGEWTRTGD-KYVR-----DDDG----FYTYAGRADDMLK 413
|
490 500 510
....*....|....*....|....*....|
gi 530392108 1459 LRGMRYHPIDIEtSVIRAHKSVTECAVFTW 1488
Cdd:cd05959 414 VSGIWVSPFEVE-SALVQHPAVLEAAVVGV 442
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
317-937 |
1.52e-17 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 89.84 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 317 PPSLEAALQRWGTISPKAPCLTTMDTNGKPLYILTYGKLWTRSMKVAYSIlhklgtkqEPMVRPGDRVALVFPNNdpAAF 396
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALRFLADDPGEGVVLSYRDLDLRARTIAAAL--------QARASFGDRAVLLFPSG--PDY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 397 MAAFYGCLLAEVVPVPIEVPLTRKDAGSQQIGFLLGSCGVTVALTSDACHKGLPKSPTGEIPqfkGWPKLLwfvTESKHL 476
Cdd:PRK05691 78 VAAFFGCLYAGVIAVPAYPPESARRHHQERLLSIIADAEPRLLLTVADLRDSLLQMEELAAA---NAPELL---CVDTLD 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 477 SKPPRDWF-PHIKDanNDTAYIEYKTCKDGSVLGVTVTRTALLTHCQALTQACG--YTEAETIVNVLDFKKDVGLWHGIL 553
Cdd:PRK05691 152 PALAEAWQePALQP--DDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMGLIGGLL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 554 TSVMNmmhviSIPYSLMKVN-----PLSWIQKVCQYKAKVAcvKSRDMHWALVAHRdQRDINLSSL---RMLIVADGANP 625
Cdd:PRK05691 230 QPIFS-----GVPCVLMSPAyflerPLRWLEAISEYGGTIS--GGPDFAYRLCSER-VSESALERLdlsRWRVAYSGSEP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 626 WSISSCDAFLNVFQSKGLRQEVICPCASSPEA-LTVAirrptddsNQPPGRGVlsmhgltyGVIRVDSE-------EKLS 697
Cdd:PRK05691 302 IRQDSLERFAEKFAACGFDPDSFFASYGLAEAtLFVS--------GGRRGQGI--------PALELDAEalarnraEPGT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 698 VLTVQDVGLVMPGAIMCSVKPDGVPQLcRTDEIGELCVCAVATGTSYYGLSGMTKNTFevfpMTSSGApiseyPFIRTGL 777
Cdd:PRK05691 366 GSVLMSCGRSQPGHAVLIVDPQSLEVL-GDNRVGEIWASGPSIAHGYWRNPEASAKTF----VEHDGR-----TWLRTGD 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 778 LGFVGPGGLvFVVGKMDGLMVVSGRRHNADDIVATalAVEPMKFVYRGRIAVFSVTVLHDERIVIVAE-----QRPDSTE 852
Cdd:PRK05691 436 LGFLRDGEL-FVTGRLKDMLIVRGHNLYPQDIEKT--VEREVEVVRKGRVAAFAVNHQGEEGIGIAAEisrsvQKILPPQ 512
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 853 EdsfqWMSRVLQAIDSIHQVGVYCLALVPANTLPKTPLGGIHLSETKQLFLEGSLhpcnvlmcphTCVTNLPKPRQKQPE 932
Cdd:PRK05691 513 A----LIKSIRQAVAEACQEAPSVVLLLNPGALPKTSSGKLQRSACRLRLADGSL----------DSYALFPALQAVEAA 578
|
....*
gi 530392108 933 IGPAS 937
Cdd:PRK05691 579 QTAAS 583
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1001-1508 |
2.18e-17 |
|
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: 86.81 E-value: 2.18e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1001 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSR 1080
Cdd:cd05930 12 SLTYAELDARANRLARYLRERG-VGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAE------RLAYILEDSG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1081 SACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1160
Cdd:cd05930 85 AKLVLTD-------------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1161 CRSIKlqcELYP--SREVAICLDPYcglGF------VLWCLCsvySGHQsILIPPSELETNPALWLLAVSQYKVRDTFCS 1232
Cdd:cd05930 122 LLWMQ---EAYPltPGDRVLQFTSF---SFdvsvweIFGALL---AGAT-LVVLPEEVRKDPEALADLLAEEGITVLHLT 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1233 YSVMELCTKGLGSQteslkarglDLSRVRTcVVVAEERPRIALTQSFSKLFKDlglhpravstsfgcrvnlaiclqpHRL 1312
Cdd:cd05930 192 PSLLRLLLQELELA---------ALPSLRL-VLVGGEALPPDLVRRWRELLPG------------------------ARL 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1313 WTLaeqgtSGPDPTTVYVDMRALRHDRVRlvergsPHSLPLmesGKILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNA 1392
Cdd:cd05930 238 VNL-----YGPTEATVDATYYRVPPDDEE------DGRVPI---GRPIPNTRVYVLDENLR-PVPPGVPGELYIGGAGLA 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1393 SGYftiYGDESLQSDHFNsRLSFGDTQTIWaRTGYLGflRRteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIETs 1472
Cdd:cd05930 303 RGY---LNRPELTAERFV-PNPFGPGERMY-RTGDLV--RW----LPDGN----LEFLGRIDDQVKIRGYRIELGEIEA- 366
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 530392108 1473 VIRAHKSVTECAVFTWTN------LLVVVVELDGSEQEALDL 1508
Cdd:cd05930 367 ALLAHPGVREAAVVAREDgdgekrLVAYVVPDEGGELDEEEL 408
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1006-1485 |
1.83e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 75.19 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1006 QLHKRAEKIAVMLMERGhlqDGDHVALVYPPGIDLIAAFYGCLYAG----CVPITVRPPHPQNIA-TTLptvkmivevSR 1080
Cdd:PRK05851 36 EVHGRAENVAARLLDRD---RPGAVGLVGEPTVELVAAIQGAWLAGaavsILPGPVRGADDGRWAdATL---------TR 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1081 SACLMTTQLIC-----KLLRSREAAAAV-DVRTWPlildtddlPKKRPAQIcKPCNPDTLAYLDFSVSTTGMLAGVKMSH 1154
Cdd:PRK05851 104 FAGIGVRTVLShgshlERLRAVDSSVTVhDLATAA--------HTNRSASL-TPPDSGGPAVLQGTAGSTGTPRTAILSP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1155 AATSAFCRSIKLQCELYPSREVAICLDPY---CGLGFVLwclCSVYSGHQSILIPPSELETNPALWLLAVSQykVRDTFC 1231
Cdd:PRK05851 175 GAVLSNLRGLNARVGLDAATDVGCSWLPLyhdMGLAFLL---TAALAGAPLWLAPTTAFSASPFRWLSWLSD--SRATLT 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1232 SYSVMELCTKGLGSQteslKARGLDLSRVRTCVVVAEerP-RIALTQSFSKLFKDLGLHPRAVSTSFGcrvnlaiclqph 1310
Cdd:PRK05851 250 AAPNFAYNLIGKYAR----RVSDVDLGALRVALNGGE--PvDCDGFERFATAMAPFGFDAGAAAPSYG------------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1311 rlwtLAEQ--GTSGPDPTTvyvdmrALRHDRVRLVERGSPHSLPLMesGKILPGVRIIIANPETKGPLGDSHLGEIWVHS 1388
Cdd:PRK05851 312 ----LAEStcAVTVPVPGI------GLRVDEVTTDDGSGARRHAVL--GNPIPGMEVRISPGDGAAGVAGREIGEIEIRG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1389 AHNASGYFtiyGDESLQSDHfnsrlsfgdtqtiWARTGYLGFlrrteLTDangerhDALYVVGALDEAMELRGMRYHPID 1468
Cdd:PRK05851 380 ASMMSGYL---GQAPIDPDD-------------WFPTGDLGY-----LVD------GGLVVCGRAKELITVAGRNIFPTE 432
|
490
....*....|....*..
gi 530392108 1469 IETSVIRAhKSVTECAV 1485
Cdd:PRK05851 433 IERVAAQV-RGVREGAV 448
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1130-1470 |
1.10e-12 |
|
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: 72.52 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1130 NPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYCGLGFVLWCLCSVYSGHQSILIPPSE 1209
Cdd:cd05908 104 LADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLMPTRL 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1210 LETNPALWLLAVSQYKVRDTFCSysvmELCTKGLGSQTESLKARGLDLSRVRTCVVVAEErprIA--LTQSFSKLFKDLG 1287
Cdd:cd05908 184 FIRRPILWLKKASEHKATIVSSP----NFGYKYFLKTLKPEKANDWDLSSIRMILNGAEP---IDyeLCHEFLDHMSKYG 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1288 LHPRAVSTSFGcrvnlaiclqphrlwtLAEQ--GTSGPDP----TTVYVDMRALRH-DRVRLVERGSPHSLPLMESGKIL 1360
Cdd:cd05908 257 LKRNAILPVYG----------------LAEAsvGASLPKAqspfKTITLGRRHVTHgEPEPEVDKKDSECLTFVEVGKPI 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1361 PGVRIIIANPETKGpLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnsrlsfgdTQTIWARTGYLGFLRrteltdaN 1440
Cdd:cd05908 321 DETDIRICDEDNKI-LPDGYIGHIQIRGKNVTPGY---YNNPEATAKVF--------TDDGWLKTGDLGFIR-------N 381
|
330 340 350
....*....|....*....|....*....|
gi 530392108 1441 GErhdaLYVVGALDEAMELRGMRYHPIDIE 1470
Cdd:cd05908 382 GR----LVITGREKDIIFVNGQNVYPHDIE 407
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
363-891 |
3.03e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 70.93 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 363 AYSILHKLGTkqepmvRPGDRVALVFPNNDPA---AFMAAFYGCLLAEVVpvpieVPLTrKDAGSQQIGFLLGSCGVTVA 439
Cdd:cd05922 6 AASALLEAGG------VRGERVVLILPNRFTYielSFAVAYAGGRLGLVF-----VPLN-PTLKESVLRYLVADAGGRIV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 440 LTS----DACHKGLPKSPTGEipqfkgwpklLWFVTESKHLSKPPRDWFPHIKDannDTAYIEYKTCKDGSVLGVTVTRT 515
Cdd:cd05922 74 LADagaaDRLRDALPASPDPG----------TVLDADGIRAARASAPAHEVSHE---DLALLLYTSGSTGSPKLVRLSHQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 516 ALLTHCQALTQACGYTEAETIVNVLDFKKDVGLwhgiltSVMNMmH-------VISIPYSLmkvnPLSWIQKVCQYKAK- 587
Cdd:cd05922 141 NLLANARSIAEYLGITADDRALTVLPLSYDYGL------SVLNT-HllrgatlVLTNDGVL----DDAFWEDLREHGATg 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 588 VACVKSrdmHWALVAHRDQRDINLSSLRMLIVADGANPwsisscDAFLNVFQSKGlrqevicpcasspealtvairrptd 667
Cdd:cd05922 210 LAGVPS---TYAMLTRLGFDPAKLPSLRYLTQAGGRLP------QETIARLRELL------------------------- 255
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 668 dsnqpPGRGVLSMHGLTYGVIR---VDSEEKLSVLTvqDVGLVMPGAIMCSVKPDGvpQLCRTDEIGELcvcaVATGTSY 744
Cdd:cd05922 256 -----PGAQVYVMYGQTEATRRmtyLPPERILEKPG--SIGLAIPGGEFEILDDDG--TPTPPGEPGEI----VHRGPNV 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 745 YgLSGMTKNTFEVFPMTSSGApiseypfIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMkfvyr 824
Cdd:cd05922 323 M-KGYWNDPPYRRKEGRGGGV-------LHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLI----- 389
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530392108 825 GRIAVFSVTVLHDERIVIVAEqRPDSTEEDSfqwMSRVLQAIDSIHQVGVYClalVPANTLPKTPLG 891
Cdd:cd05922 390 IEAAAVGLPDPLGEKLALFVT-APDKIDPKD---VLRSLAERLPPYKVPATV---RVVDELPLTASG 449
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
972-1206 |
5.51e-12 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 69.90 E-value: 5.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 972 LSEVLQWRAQTTPDHilyTLLNCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1051
Cdd:cd05936 1 LADLLEEAARRFPDK---TALIFMGR---KLTYRELDALAEAFAAGLQNLG-VQPGDRVALMLPNCPQFPIAYFGALKAG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1052 CVPITVRPphpqniattlptvkmivevsrsacLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQickpcNP 1131
Cdd:cd05936 74 AVVVPLNP------------------------LYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVAL-----TP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1132 DTLAYLDFSVSTTGMLAGVKMSHAATSAfcrsIKLQC-----ELYPSREVAICLDP-YCGLGFVLWCLCSVYSGHQSILI 1205
Cdd:cd05936 125 EDVAVLQYTSGTTGVPKGAMLTHRNLVA----NALQIkawleDLLEGDDVVLAALPlFHVFGLTVALLLPLALGATIVLI 200
|
.
gi 530392108 1206 P 1206
Cdd:cd05936 201 P 201
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1001-1485 |
1.08e-11 |
|
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: 69.19 E-value: 1.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1001 SLTCVQLHKRAEKIAVMLMERGHLQdGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPphpqniATTLPTVKMIVEVSR 1080
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRK-GDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANP------LSTPAEIAKQVKDSG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1081 SACLMTT-QLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQICKP-CNPDTLAYLDFSVSTTGMLAGVKMSH---- 1154
Cdd:cd05904 105 AKLAFTTaELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEPPVVvIKQDDVAALLYSSGTTGRSKGVMLTHrnli 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1155 AATSAFCRSIKLQCElypSREVAICLDPYCGL-GFVLWCLCSVYSGHQSILIPPSELETnpalWLLAVSQYKVRDTFCSY 1233
Cdd:cd05904 185 AMVAQFVAGEGSNSD---SEDVFLCVLPMFHIyGLSSFALGLLRLGATVVVMPRFDLEE----LLAAIERYKVTHLPVVP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1234 SVMELCTKglgsqteSLKARGLDLSRVRTCVVVAEERPRiALTQSFSKLFKDlglhpravstsfgcrVNLaicLQPHRLW 1313
Cdd:cd05904 258 PIVLALVK-------SPIVDKYDLSSLRQIMSGAAPLGK-ELIEAFRAKFPN---------------VDL---GQGYGMT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1314 TLAEQGTSGPDPTtvyvdmralrHDRVRlveRGSphslplmeSGKILPGVRIIIANPETKGPLGDSHLGEIWVHSAHNAS 1393
Cdd:cd05904 312 ESTGVVAMCFAPE----------KDRAK---YGS--------VGRLVPNVEAKIVDPETGESLPPNQTGELWIRGPSIMK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1394 GYFtiyGDESlqsdhfnsrlsfgDTQ-TI----WARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMRYHPID 1468
Cdd:cd05904 371 GYL---NNPE-------------ATAaTIdkegWLHTGDLCYI------DEDGY----LFIVDRLKELIKYKGFQVAPAE 424
|
490
....*....|....*..
gi 530392108 1469 IEtSVIRAHKSVTECAV 1485
Cdd:cd05904 425 LE-ALLLSHPEILDAAV 440
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
980-1511 |
5.64e-11 |
|
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: 66.89 E-value: 5.64e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 980 AQTTPDHILYTllnCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITV 1057
Cdd:cd05945 1 AAANPDRPAVV---EGGR---TLTYRELKERADALAAALASLG-LDAGDPVVVYGHKSPDAIAAFLAALKAGHayVPLDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1058 RPPHPQniattlptVKMIVEVSRSACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnPDTLAYL 1137
Cdd:cd05945 74 SSPAER--------IREILDAAKPALLIAD-------------------------------------------GDDNAYI 102
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1138 DFSVSTTGMLAGVKMSHAATSAFCRSIkLQCELYPSREVAICLDPYcglGF---VLWCLCSVYSGhQSILIPPSELETNP 1214
Cdd:cd05945 103 IFTSGSTGRPKGVQISHDNLVSFTNWM-LSDFPLGPGDVFLNQAPF---SFdlsVMDLYPALASG-ATLVPVPRDATADP 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1215 ALWLLAVSQYKVRDTFCSYSVMELCTkGLGSQTESLkargldLSRVRTCVVVAEERPrIALTQSFSKLFkdlglhPravs 1294
Cdd:cd05945 178 KQLFRFLAEHGITVWVSTPSFAAMCL-LSPTFTPES------LPSLRHFLFCGEVLP-HKTARALQQRF------P---- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1295 tsfGCRV-NlaiclqphrlwtlaeqgTSGPDPTTVYVdmraLRHDRVRLVERGSPhSLPLmesGKILPGVRIIIANPETK 1373
Cdd:cd05945 240 ---DARIyN-----------------TYGPTEATVAV----TYIEVTPEVLDGYD-RLPI---GYAKPGAKLVILDEDGR 291
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1374 gPLGDSHLGEIWVHSAHNASGYFtiyGDEslqsDHFNSRLSFGDTQTiWARTGYLGFLrrteltDANGErhdaLYVVGAL 1453
Cdd:cd05945 292 -PVPPGEKGELVISGPSVSKGYL---NNP----EKTAAAFFPDEGQR-AYRTGDLVRL------EADGL----LFYRGRL 352
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530392108 1454 DEAMELRGMRYHPIDIETSViRAHKSVTECAVFTWTNL-----LVVVVELDGSEqEALDLVPL 1511
Cdd:cd05945 353 DFQVKLNGYRIELEEIEAAL-RQVPGVKEAVVVPKYKGekvteLIAFVVPKPGA-EAGLTKAI 413
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
980-1485 |
1.79e-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: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 980 AQTTPDHILytlLNCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG--CVPITV 1057
Cdd:cd17651 5 AARTPDAPA---LVAEGR---RLTYAELDRRANRLAHRLRARG-VGPGDLVALCARRSAELVVALLAILKAGaaYVPLDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1058 RPPhPQNIAttlptvkMIVEVSRSACLMTTQlickllrsREAAAAVDVRTWPLILDTDDLPKKRPAQICKPCNPDTLAYL 1137
Cdd:cd17651 78 AYP-AERLA-------FMLADAGPVLVLTHP--------ALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYV 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1138 DFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAicldPYCGLGF--VLWCLCSVYSGHQSILIPPSELETNPA 1215
Cdd:cd17651 142 IYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGARTL----QFAGLGFdvSVQEIFSTLCAGATLVLPPEEVRTDPP 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1216 LWLLAVSQYKVRDTFCSYSVME-LCtkglgsqtESLKARGLDLSRVRtCVVVAEERprialtqsfsklfkdLGLHPRavs 1294
Cdd:cd17651 218 ALAAWLDEQRISRVFLPTVALRaLA--------EHGRPLGVRLAALR-YLLTGGEQ---------------LVLTED--- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1295 tsfgcrvnlaiclqpHRLWTLAEQG-----TSGPDPTTVyVDMRALRHDRVRlveRGSPHSLplmesGKILPGVRIIIAN 1369
Cdd:cd17651 271 ---------------LREFCAGLPGlrlhnHYGPTETHV-VTALSLPGDPAA---WPAPPPI-----GRPIDNTRVYVLD 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1370 PETKgPLGDSHLGEIWVHSAHNASGYFTIYG--DESLQSDHF--NSRLSfgdtqtiwaRTGYLGflRRteltDANGErhd 1445
Cdd:cd17651 327 AALR-PVPPGVPGELYIGGAGLARGYLNRPEltAERFVPDPFvpGARMY---------RTGDLA--RW----LPDGE--- 387
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 530392108 1446 aLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 1485
Cdd:cd17651 388 -LEFLGRADDQVKIRGFRIELGEIE-AALARHPGVREAVV 425
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
979-1508 |
2.18e-10 |
|
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: 66.03 E-value: 2.18e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 979 RAQTTPDHIlytllncrgAI---ANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--V 1053
Cdd:COG1020 485 QAARTPDAV---------AVvfgDQSLTYAELNARANRLAHHLRALG-VGPGDLVGVCLERSLEMVVALLAVLKAGAayV 554
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1054 PITvrPPHPQN-IAttlptvkMIVEVSRSACLMTTQlickLLRSREAAAAVDVrtwpLILDTDDLPKKRPAQICKPCNPD 1132
Cdd:COG1020 555 PLD--PAYPAErLA-------YMLEDAGARLVLTQS----ALAARLPELGVPV----LALDALALAAEPATNPPVPVTPD 617
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1133 TLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAicldPYCGLGF------VLWCLCsvySGHQSILIP 1206
Cdd:COG1020 618 DLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVL----QFASLSFdasvweIFGALL---SGATLVLAP 690
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1207 PsELETNPALWLLAVSQYKVrdtfcsySVMELcTKGLGSQTesLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDL 1286
Cdd:COG1020 691 P-EARRDPAALAELLARHRV-------TVLNL-TPSLLRAL--LDAAPEALPSLRL-VLVGGEALPPELVRRWRARLPGA 758
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1287 GLHpravstsfgcrvNLaiclqphrlwtlaeqgtSGPDPTTVYVDMRALRHDRVrlvergSPHSLPLmesGKILPGVRII 1366
Cdd:COG1020 759 RLV------------NL-----------------YGPTETTVDSTYYEVTPPDA------DGGSVPI---GRPIANTRVY 800
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1367 IAnpetkgplgDSHL--------GEIWVHSAHNASGYFtiyGDESLQSDHF--NsrlSFGDTQTIWARTGYLGflRRTel 1436
Cdd:COG1020 801 VL---------DAHLqpvpvgvpGELYIGGAGLARGYL---NRPELTAERFvaD---PFGFPGARLYRTGDLA--RWL-- 861
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530392108 1437 tdANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVFTWTN-----LLVVVVELDGSEQEALDL 1508
Cdd:COG1020 862 --PDGN----LEFLGRADDQVKIRGFRIELGEIE-AALLQHPGVREAVVVAREDapgdkRLVAYVVPEAGAAAAAAL 931
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
510-902 |
4.52e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 64.25 E-value: 4.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 510 VTVTRTALLTHCQALTQACGYT-EAETIVNVLDFKKDVGLWhGILTSVMNM-MHVISI-PYSLMkVNPLSWIQKVCQYKA 586
Cdd:PRK07768 170 VQITHGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMV-GFLTVPMYFgAELVKVtPMDFL-RDPLLWAELISKYRG 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 587 KVACvkSRDMHWALVAHR-----DQRDINLSSLRmlIVADGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlTVA 661
Cdd:PRK07768 248 TMTA--APNFAYALLARRlrrqaKPGAFDLSSLR--FALNGAEPIDPADVEDLLDAGARFGLRPEAILPAYGMAEA-TLA 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 662 IrrptddSNQPPGRGvlsmhgLTYGVIRVD--SEEKLSVLTVQD-------VGLVMPGAIMCSVKPDGvpQLCRTDEIGE 732
Cdd:PRK07768 323 V------SFSPCGAG------LVVDEVDADllAALRRAVPATKGntrrlatLGPPLPGLEVRVVDEDG--QVLPPRGVGV 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 733 LCVCAVATgTSYYglsgmtkntfevfpMTSSG--APISEYPFIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIV 810
Cdd:PRK07768 389 IELRGESV-TPGY--------------LTMDGfiPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 811 ATALAVEPmkfVYRGRIAVFSVTVLHD-ERIVIVAEQRPDSTEEDSFQWMSRVLQAIDSihQVGV--YCLALVPANTLPK 887
Cdd:PRK07768 454 RAAARVEG---VRPGNAVAVRLDAGHSrEGFAVAVESNAFEDPAEVRRIRHQVAHEVVA--EVGVrpRNVVVLGPGSIPK 528
|
410
....*....|....*
gi 530392108 888 TPLGGIHLSETKQLF 902
Cdd:PRK07768 529 TPSGKLRRANAAELV 543
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
509-893 |
5.11e-10 |
|
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: 63.07 E-value: 5.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 509 GVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMNMMHVISIPyslmKVNPLSWIQKVCQYKAKV 588
Cdd:cd04433 17 GVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLF-GLLGALLAGGTVVLLP----KFDPEAALELIEREKVTI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 589 ACVkSRDMHWALVAHRDQRDINLSSLRMLIVadGANPWSISSCDAFLNVFqskglrqevicpcasspealtvairrptdd 668
Cdd:cd04433 92 LLG-VPTLLARLLKAPESAGYDLSSLRALVS--GGAPLPPELLERFEEAP------------------------------ 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 669 snqppGRGVLSMHGLT-----YGVIRVDSEEKLSVltvqDVGLVMPGAIMCSVKPDGVPqlCRTDEIGELCVcavatgTS 743
Cdd:cd04433 139 -----GIKLVNGYGLTetggtVATGPPDDDARKPG----SVGRPVPGVEVRIVDPDGGE--LPPGEIGELVV------RG 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 744 YYGLSGMTKNTFEVFPMTSSGapiseypFIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVEPMKfvy 823
Cdd:cd04433 202 PSVMKGYWNNPEATAAVDEDG-------WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVA--- 271
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530392108 824 rgRIAVFSVTvlhDER------IVIVAEQRPDSTEEDSFQWMSRVLQAIDSIHQVgvyclalVPANTLPKTPLGGI 893
Cdd:cd04433 272 --EAAVVGVP---DPEwgervvAVVVLRPGADLDAEELRAHVRERLAPYKVPRRV-------VFVDALPRTASGKI 335
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
978-1485 |
1.33e-09 |
|
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: 62.68 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 978 WRAQT--TPDH--ILYTllncrgaiANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCV 1053
Cdd:cd17646 4 VAEQAarTPDApaVVDE--------GRTLTYRELDERANRLAHLLRARG-VGPEDRVAVLLPRSADLVVALLAVLKAGAA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1054 PITVRPPHPQniattlPTVKMIVEVSRSACLMTTQlickllRSREAAAAVDVRTWPLILDTDDLPKKRPAQickPCNPDT 1133
Cdd:cd17646 75 YLPLDPGYPA------DRLAYMLADAGPAVVLTTA------DLAARLPAGGDVALLGDEALAAPPATPPLV---PPRPDN 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1134 LAYLDFSVSTTGMLAGVKMSHAatsAFCRSIKLQCELYP--SREVAICLDPycgLGF------VLWCLCsvySGhQSILI 1205
Cdd:cd17646 140 LAYVIYTSGSTGRPKGVMVTHA---GIVNRLLWMQDEYPlgPGDRVLQKTP---LSFdvsvweLFWPLV---AG-ARLVV 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1206 PPSELETNPALWLLAVSQYKVrdTFCSY--SVMELCtkglgsqteslkargLDLSRVRTC-----VVVAEErpriALTQS 1278
Cdd:cd17646 210 ARPGGHRDPAYLAALIREHGV--TTCHFvpSMLRVF---------------LAEPAAGSCaslrrVFCSGE----ALPPE 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1279 FSKLFKDLglhpravstsFGCRVnlaiclqpHRLWtlaeqgtsGPDPTTVYVDmralrHDRVRlvERGSPHSLPLmesGK 1358
Cdd:cd17646 269 LAARFLAL----------PGAEL--------HNLY--------GPTEAAIDVT-----HWPVR--GPAETPSVPI---GR 312
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1359 ILPGVRIIIANPETKgPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHF-------NSRLSfgdtqtiwaRTGYLGfl 1431
Cdd:cd17646 313 PVPNTRLYVLDDALR-PVPVGVPGELYLGGVQLARGY---LGRPALTAERFvpdpfgpGSRMY---------RTGDLA-- 377
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 530392108 1432 RRTeltdANGErhdaLYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAV 1485
Cdd:cd17646 378 RWR----PDGA----LEFLGRSDDQVKIRGFRVEPGEIEA-ALAAHPAVTHAVV 422
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1001-1502 |
1.99e-09 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A polyketide synthase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the myxovirescin (TA) antibiotic biosynthetic gene in Myxococcus xanthus; TA production plays a role in predation. It also includes the salinosporamide A polyketide synthase which is involved in the biosynthesis of salinosporamide A, a marine microbial metabolite whose chlorine atom is crucial for potent proteasome inhibition and anticancer activity.
Pssm-ID: 341281 [Multi-domain] Cd Length: 470 Bit Score: 61.92 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1001 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPqniattLPTVKMIVEVSR 1080
Cdd:cd12116 12 SLSYAELDERANRLAARLRARG-VGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYP------ADRLRYILEDAE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1081 SACLMTTQlickllrSREAAAAVDVRTWPLILDTDDLPkkrPAQICKPCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1160
Cdd:cd12116 85 PALVLTDD-------ALPDRLPAGLPVLLLALAAAAAA---PAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1161 CRSIklqcelypsREvaicldpycglgfvlwclcsvysghqsilippsELETNPALWLLAVSQYkvrdTFcSYSVMEL-- 1238
Cdd:cd12116 155 LHSM---------RE---------------------------------RLGLGPGDRLLAVTTY----AF-DISLLELll 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1239 ----------CTKGLGSQTESLKARgldLSRVRTCVVVAeerprialTQSFSKLFKDLGLHPRAvstsfGCRV------- 1301
Cdd:cd12116 188 pllagarvviAPRETQRDPEALARL---IEAHSITVMQA--------TPATWRMLLDAGWQGRA-----GLTAlcggeal 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1302 --NLA--ICLQPHRLWTLaeqgtSGPDPTTVYVDMRALrhdrvrlveRGSPHSLPLmesGKILPGVRIIIANPETKgPLG 1377
Cdd:cd12116 252 ppDLAarLLSRVGSLWNL-----YGPTETTIWSTAARV---------TAAAGPIPI---GRPLANTQVYVLDAALR-PVP 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1378 DSHLGEIWVHSAHNASGYftiYGDESLQSDHFnSRLSFGDTQTIWARTGYLgfLRRteltDANGErhdaLYVVGALDEAM 1457
Cdd:cd12116 314 PGVPGELYIGGDGVAQGY---LGRPALTAERF-VPDPFAGPGSRLYRTGDL--VRR----RADGR----LEYLGRADGQV 379
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 530392108 1458 ELRGMRYHPIDIETsVIRAHKSVTECAVFTWTN----LLVVVVELDGSE 1502
Cdd:cd12116 380 KIRGHRIELGEIEA-ALAAHPGVAQAAVVVREDggdrRLVAYVVLKAGA 427
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1001-1226 |
2.29e-09 |
|
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: 61.52 E-value: 2.29e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1001 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITVRPPhPQNIATTLptvkmiveV 1078
Cdd:cd12114 12 TLTYGELAERARRVAGALKAAG-VRPGDLVAVTLPKGPEQVVAVLGILAAGAayVPVDIDQP-AARREAIL--------A 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1079 SRSACLMTTQLICkllrSREAAAAVDVRTWPLILD-TDDLPKKRPAQickpcnPDTLAYLDFSVSTTGMLAGVKMSHAAT 1157
Cdd:cd12114 82 DAGARLVLTDGPD----AQLDVAVFDVLILDLDALaAPAPPPPVDVA------PDDLAYVIFTSGSTGTPKGVMISHRAA 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530392108 1158 SAFCRSIKLQCELYPSREVaICLDPycgLGFVLwclcSVY------SGHQSILIPPSELETNPALWLLAVSQYKV 1226
Cdd:cd12114 152 LNTILDINRRFAVGPDDRV-LALSS---LSFDL----SVYdifgalSAGATLVLPDEARRRDPAHWAELIERHGV 218
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
976-1506 |
2.72e-08 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 58.37 E-value: 2.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 976 LQWRAQTTPDHILYTLLNCRGAIAN----SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAG 1051
Cdd:PRK09274 12 LPRAAQERPDQLAVAVPGGRGADGKlaydELSFAELDARSDAIAHGLNAAG-IGRGMRAVLMVTPSLEFFALTFALFKAG 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1052 CVPITVRP-------------PHPQ--------NIATTL-----PTVKMIVEVSRSACLMTTQLIcKLLRSREAAAAvdv 1105
Cdd:PRK09274 91 AVPVLVDPgmgiknlkqclaeAQPDafigipkaHLARRLfgwgkPSVRRLVTVGGRLLWGGTTLA-TLLRDGAAAPF--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1106 rtwplildtddlpkkrpaqICKPCNPDTLAYLDFSVSTTGMLAGVKMSHaatSAFCRSIKLQCELYPSR--EVAIC---- 1179
Cdd:PRK09274 167 -------------------PMADLAPDDMAAILFTSGSTGTPKGVVYTH---GMFEAQIEALREDYGIEpgEIDLPtfpl 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1180 ---LDPYCGlgfvlwcLCSVysghqsilIPPSEL----ETNPALWLLAVSQYKVRDTFCSYSVMELCTKglgsqteSLKA 1252
Cdd:PRK09274 225 falFGPALG-------MTSV--------IPDMDPtrpaTVDPAKLFAAIERYGVTNLFGSPALLERLGR-------YGEA 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1253 RGLDLSRVRTcVVVAEERPRIALTQSFSKLfkdlgLHPRA-VSTSFGCRVNLAICLqphrlwtlaeqgtsgpdpttvyVD 1331
Cdd:PRK09274 283 NGIKLPSLRR-VISAGAPVPIAVIERFRAM-----LPPDAeILTPYGATEALPISS----------------------IE 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1332 MRALRHDRVRLVERGSPHSLplmesGKILPGVRI-IIA---NP-----ETKgPLGDSHLGEIWVHSAHNASGYFtiygde 1402
Cdd:PRK09274 335 SREILFATRAATDNGAGICV-----GRPVDGVEVrIIAisdAPipewdDAL-RLATGEIGEIVVAGPMVTRSYY------ 402
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1403 slQSDHFN--SRLSFGDTQtIWARTGYLGFLrrteltDANGErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSV 1480
Cdd:PRK09274 403 --NRPEATrlAKIPDGQGD-VWHRMGDLGYL------DAQGR----LWFCGRKAHRVETAGGTLYTIPCE-RIFNTHPGV 468
|
570 580
....*....|....*....|....*.
gi 530392108 1481 TECAvftwtnllVVVVELDGSEQEAL 1506
Cdd:PRK09274 469 KRSA--------LVGVGVPGAQRPVL 486
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
320-618 |
5.97e-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: 57.19 E-value: 5.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 320 LEAALQRWgtisPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdpAAFMAA 399
Cdd:cd05936 5 LEEAARRF----PDKTALIFMGRK------LTYRELDALAEAFA-AGLQNLG------VQPGDRVALMLPNC--PQFPIA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 400 FYGCLLAEVVPVPIEVPLTrkdagSQQIGFLLGSCGVTVALTsdachkglpksptgeipqfkgwpkLLWFvtesKHLSKP 479
Cdd:cd05936 66 YFGALKAGAVVVPLNPLYT-----PRELEHILNDSGAKALIV------------------------AVSF----TDLLAA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 480 PRDWFPHIKDANNDTAYIEYKTckdgsvlGVT-VTRTALLTH---------CQALTQACGyTEAETIVNVLDFKKDVGLW 549
Cdd:cd05936 113 GAPLGERVALTPEDVAVLQYTS-------GTTgVPKGAMLTHrnlvanalqIKAWLEDLL-EGDDVVLAALPLFHVFGLT 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 550 HGILTSVMNMMHVISIPyslmKVNPLSWIQKVCQYKAKVAC-VKSrdMHWALVAHRDQRDINLSSLRMLI 618
Cdd:cd05936 185 VALLLPLALGATIVLIP----RFRPIGVLKEIRKHRVTIFPgVPT--MYIALLNAPEFKKRDFSSLRLCI 248
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
313-623 |
1.29e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 56.07 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 313 VTNWPPSLEAALQRWgtisPKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNd 392
Cdd:PRK07656 4 WMTLPELLARAARRF----GDKEAYVFGDQR------LTYAELNARVRRAA-AALAALG------IGKGDRVAIWAPNS- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 393 pAAFMAAFYGCLLAEVVPVPIEvplTRKDAGsqQIGFLLGSCGVTVALTSD-------ACHKGLPK----------SPTG 455
Cdd:PRK07656 66 -PHWVIAALGALKAGAVVVPLN---TRYTAD--EAAYILARGDAKALFVLGlflgvdySATTRLPAlehvviceteEDDP 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 456 EIPQFKGWPKLLwfvteskhLSKPPRDWFPHIKDanNDTAYIEYKTCKDGSVLGVTVTRTALLTHCQALTQACGYTEAET 535
Cdd:PRK07656 140 HTEKMKTFTDFL--------AAGDPAERAPEVDP--DDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 536 IVNVLDFKKDVGLWHGILTSVMNMMHVISIPyslmKVNPLSWIQKVCQYKAKV-ACVKSrdMHWALVAHRDQRDINLSSL 614
Cdd:PRK07656 210 YLAANPFFHVFGYKAGVNAPLMRGATILPLP----VFDPDEVFRLIETERITVlPGPPT--MYNSLLQHPDRSAEDLSSL 283
|
....*....
gi 530392108 615 RmLIVADGA 623
Cdd:PRK07656 284 R-LAVTGAA 291
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1002-1510 |
1.46e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.89 E-value: 1.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1002 LTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRS 1081
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPE-VLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRE------RLAYMMEDSGA 4649
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1082 ACLMTTQLICKLLRSREAAAAVDV---RTWplildtDDLPKKRPAqicKPCNPDTLAYLDFSVSTTGMLAGVKMSHAATS 1158
Cdd:PRK12316 4650 ALLLTQSHLLQRLPIPDGLASLALdrdEDW------EGFPAHDPA---VRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLV 4720
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1159 AFCRSIKLQCELYPSREVaICLDPYCGLGFVL---WCLCSvysgHQSILIPPSELeTNPALWLLAVSQYKVRDTFCSYSV 1235
Cdd:PRK12316 4721 NHLHATGERYELTPDDRV-LQFMSFSFDGSHEglyHPLIN----GASVVIRDDSL-WDPERLYAEIHEHRVTVLVFPPVY 4794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1236 MELCTKGlgsqteslKARGLDLSRVRTCVVVAEERPRIALTQSFSKlfkdlglhpravstsfgcrvnlaicLQPHRLWTl 1315
Cdd:PRK12316 4795 LQQLAEH--------AERDGEPPSLRVYCFGGEAVAQASYDLAWRA-------------------------LKPVYLFN- 4840
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1316 aeqgTSGPDPTTVYVDMRALRhdrvrlveRGSPHSLPLMESGKILPGVRIII----ANPETKGPLGDSHLGEIWVhsahn 1391
Cdd:PRK12316 4841 ----GYGPTETTVTVLLWKAR--------DGDACGAAYMPIGTPLGNRSGYVldgqLNPLPVGVAGELYLGGEGV----- 4903
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1392 ASGYFTiygDESLQSDHFNSRlSFGDTQTIWARTGYLGFLRRTELTDangerhdalyVVGALDEAMELRGMRYHPIDIET 1471
Cdd:PRK12316 4904 ARGYLE---RPALTAERFVPD-PFGAPGGRLYRTGDLARYRADGVID----------YLGRVDHQVKIRGFRIELGEIEA 4969
|
490 500 510
....*....|....*....|....*....|....*....
gi 530392108 1472 SvIRAHKSVTECavftwtnlLVVVVELDGSEQEALDLVP 1510
Cdd:PRK12316 4970 R-LREHPAVREA--------VVIAQEGAVGKQLVGYVVP 4999
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1006-1173 |
2.34e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 56.12 E-value: 2.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1006 QLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRSACLM 1085
Cdd:PRK12316 2033 ELDSRANRLAHRLRARG-VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAE------RLAYMLEDSGAALLL 2105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1086 T-TQLICKLLRSREAAAavdvrtwpLILDTD----DLPKKRPAQickPCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAF 1160
Cdd:PRK12316 2106 TqRHLLERLPLPAGVAR--------LPLDRDaewaDYPDTAPAV---QLAGENLAYVIYTSGSTGLPKGVAVSHGALVAH 2174
|
170
....*....|...
gi 530392108 1161 CRSIKLQCELYPS 1173
Cdd:PRK12316 2175 CQAAGERYELSPA 2187
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1001-1485 |
3.45e-07 |
|
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Streptomyces sp. cytotrienin synthetase (CytC1), a relatively promiscuous adenylation enzyme that installs the aminoacyl moieties on the phosphopantetheinyl arm of the holo carrier protein CytC2. Also included are Streptomyces sp Thr1, involved in the biosynthesis of 4-chlorothreonine, Pseudomonas aeruginosa pyoverdine synthetase D (PvdD), involved in the biosynthesis of the siderophore pyoverdine and Pseudomonas syringae syringopeptin synthetase, where syringpeptin is a necrosis-inducing phytotoxin that functions as a virulence determinant in the plant-pathogen interaction. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341298 [Multi-domain] Cd Length: 450 Bit Score: 54.62 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1001 SLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGC--VPITVRPPHPQNIAttlptvkmIVEV 1078
Cdd:cd17643 12 RLTYGELDARANRLARTLRAEG-VGPGDRVALALPRSAELIVALLAILKAGGayVPIDPAYPVERIAF--------ILAD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1079 SRSACLMTTqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnPDTLAYLDFSVSTTGMLAGVKMSHAATS 1158
Cdd:cd17643 83 SGPSLLLTD-------------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1159 AFCRSIKLQCELYPSREVAICldPYCGLGFVLWCLCSVYSGHQSILIPPSELETNPALWLLAVSQYKVrdtfcsySVMel 1238
Cdd:cd17643 120 ALFAATQRWFGFNEDDVWTLF--HSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGV-------TVL-- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1239 ctkglgSQT--------ESLKARGLDLSRVRTcVVVAEERPRIALTQSFSKLFKDlgLHPRAvstsfgcrVNLaiclqph 1310
Cdd:cd17643 189 ------NQTpsafyqlvEAADRDGRDPLALRY-VIFGGEALEAAMLRPWAGRFGL--DRPQL--------VNM------- 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1311 rlwtlaeqgtSGPDPTTVYVDMRALRHDRVRLVErGSPhslplmeSGKILPGVRIIIANpETKGPLGDSHLGEIWVHSAH 1390
Cdd:cd17643 245 ----------YGITETTVHVTFRPLDAADLPAAA-ASP-------IGRPLPGLRVYVLD-ADGRPVPPGVVGELYVSGAG 305
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1391 NASGYFtiyGDESLQSDHFNSrLSFGDTQTIWARTGYLGflRRTeltdANGErhdaLYVVGALDEAMELRGMRYHPIDIE 1470
Cdd:cd17643 306 VARGYL---GRPELTAERFVA-NPFGGPGSRMYRTGDLA--RRL----PDGE----LEYLGRADEQVKIRGFRIELGEIE 371
|
490
....*....|....*
gi 530392108 1471 tSVIRAHKSVTECAV 1485
Cdd:cd17643 372 -AALATHPSVRDAAV 385
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
974-1519 |
3.51e-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: 3.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 974 EVLQWRAQTTPDHILytlLNCRGAianSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCV 1053
Cdd:cd12117 1 ELFEEQAARTPDAVA---VVYGDR---SLTYAELNERANRLARRLRAAG-VGPGDVVGVLAERSPELVVALLAVLKAGAA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1054 PITVRPPHPQNiattlpTVKMIVEVSRSACLMTtqlickllrSREAAAAVDVRTWPLILDTDDLPKKRPAQICkPCNPDT 1133
Cdd:cd12117 74 YVPLDPELPAE------RLAFMLADAGAKVLLT---------DRSLAGRAGGLEVAVVIDEALDAGPAGNPAV-PVSPDD 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1134 LAYLDFSVSTTGMLAGVKMSHAATSAFCRS---IKLQcelypSREVAICLDPYC--GLGFVLWclCSVYSGHQSILIPPS 1208
Cdd:cd12117 138 LAYVMYTSGSTGRPKGVAVTHRGVVRLVKNtnyVTLG-----PDDRVLQTSPLAfdASTFEIW--GALLNGARLVLAPKG 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1209 ELETNPALwLLAVSQYKVrdtfcsySVMELcTKGLGSQteslkargldlsrvrtcvvVAEERPrialtQSFSKLfkdlgl 1288
Cdd:cd12117 211 TLLDPDAL-GALIAEEGV-------TVLWL-TAALFNQ-------------------LADEDP-----ECFAGL------ 251
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1289 hpRAVSTSfGCRVNLAIClqphRLWTLAEQGTS-----GPDPTTVYvdmrALRHdrvrLVERG--SPHSLPLmesGKILP 1361
Cdd:cd12117 252 --RELLTG-GEVVSPPHV----RRVLAACPGLRlvngyGPTENTTF----TTSH----VVTELdeVAGSIPI---GRPIA 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1362 GVRIIIANpETKGPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDHFnSRLSFGDTQTIWaRTGYLgfLRRteltDANG 1441
Cdd:cd12117 314 NTRVYVLD-EDGRPVPPGVPGELYVGGDGLALGY---LNRPALTAERF-VADPFGPGERLY-RTGDL--ARW----LPDG 381
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530392108 1442 ErhdaLYVVGALDEAMELRGMRYHPIDIETsVIRAHKSVTECAvftwtnllVVVVELDGSEQEaldlvpLVTNVVLEE 1519
Cdd:cd12117 382 R----LEFLGRIDDQVKIRGFRIELGEIEA-ALRAHPGVREAV--------VVVREDAGGDKR------LVAYVVAEG 440
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
351-801 |
3.91e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 54.81 E-value: 3.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 351 TYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNDpaAFMAAFYGCLLAEVVPVPIEVPLTrkdagSQQIGFL 430
Cdd:PRK06187 33 TYAELDERVNRLA-NALRALG------VKKGDRVAVFDWNSH--EYLEAYFAVPKIGAVLHPINIRLK-----PEEIAYI 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 431 LGSCGVTVALTSDAcHKGLPKSPTGEIPQFKGW--------PKLLWFVTESKHL--SKPPRDWFPHIKDanNDTAYIEYK 500
Cdd:PRK06187 99 LNDAEDRVVLVDSE-FVPLLAAILPQLPTVRTVivegdgpaAPLAPEVGEYEELlaAASDTFDFPDIDE--NDAAAMLYT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 501 TCKDGSVLGVTVTRTALLTHCQALTQACGYTEaetivnvldfkKDVGLwhgiltSVMNMMHV--ISIPY-SLM------- 570
Cdd:PRK06187 176 SGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSR-----------DDVYL------VIVPMFHVhaWGLPYlALMagakqvi 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 571 --KVNPlswiQKVCQY--KAKV---ACVKSrdMHWALVAHRDQRDINLSSLRMLIVadGANPWSISSCDAFLNVFqskgl 643
Cdd:PRK06187 239 prRFDP----ENLLDLieTERVtffFAVPT--IWQMLLKAPRAYFVDFSSLRLVIY--GGAALPPALLREFKEKF----- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 644 rqevicpcasspealtvairrptddsnqppGRGVLSMHGL--TYGVIRVD--SEEKLSVLTVQ-DVGLVMPG---AImcs 715
Cdd:PRK06187 306 ------------------------------GIDLVQGYGMteTSPVVSVLppEDQLPGQWTKRrSAGRPLPGveaRI--- 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 716 VKPDGVPQLCRTDEIGELCVCAVATGTSYYGLSGMTKNTFEvfpmtsSGapiseypFIRTGLLGFVGPGGLVFVVGKMDG 795
Cdd:PRK06187 353 VDDDGDELPPDGGEVGEIIVRGPWLMQGYWNRPEATAETID------GG-------WLHTGDVGYIDEDGYLYITDRIKD 419
|
....*.
gi 530392108 796 lMVVSG 801
Cdd:PRK06187 420 -VIISG 424
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
281-817 |
4.32e-07 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 55.35 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 281 FEELLEVQQPDPNQPKPEGAqmLAMRGEQLGVVTNWPPSLEAALQRWGT---------ISPKAPCLTTMDTNgkplyiLT 351
Cdd:PRK12316 1959 LLHLLEQMAEDAQAALGELA--LLDAGERQRILADWDRTPEAYPRGPGVhqriaeqaaRAPEAIAVVFGDQH------LS 2030
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 352 YGKLWTRSMKVAYSILhKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLA--EVVPVPIEVPLTRkdagsqqIGF 429
Cdd:PRK12316 2031 YAELDSRANRLAHRLR-ARG------VGPEVRVAIAAERS--FELVVALLAVLKAggAYVPLDPNYPAER-------LAY 2094
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 430 LLGSCGVTVALTSDACHKGLPksPTGEIPQFKGWPKLLWFVTESKHlskpprdwfPHIKDANNDTAYIEYKTCKDGSVLG 509
Cdd:PRK12316 2095 MLEDSGAALLLTQRHLLERLP--LPAGVARLPLDRDAEWADYPDTA---------PAVQLAGENLAYVIYTSGSTGLPKG 2163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 510 VTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMNMMHVISIPYSLMkvNPLSWIQKVCQYKAKVA 589
Cdd:PRK12316 2164 VAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHE-QWFHPLLNGARVLIRDDELW--DPEQLYDEMERHGVTIL 2240
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 590 CVKSrdMHWALVAHRDQRDINLSSLRMLIVadGANPWSISSCDAFLN------VFQSKGLRQEVICP-----CASSPE-A 657
Cdd:PRK12316 2241 DFPP--VYLQQLAEHAERDGRPPAVRVYCF--GGEAVPAASLRLAWEalrpvyLFNGYGPTEAVVTPllwkcRPQDPCgA 2316
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 658 LTVAIRRPTDDsnqppgrgvlsmhgltygvirvdseEKLSVLtvqDVGLvmpgaimcsvkpdgvpQLCRTDEIGELCVCA 737
Cdd:PRK12316 2317 AYVPIGRALGN-------------------------RRAYIL---DADL----------------NLLAPGMAGELYLGG 2352
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 738 VATGTSYYGLSGMTKNTFEVFPMTSSGAPIseypfIRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNADDIVATALAVE 817
Cdd:PRK12316 2353 EGLARGYLNRPGLTAERFVPDPFSASGERL-----YRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHP 2427
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
976-1509 |
4.58e-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: 54.15 E-value: 4.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 976 LQWRAQTTPDHilyTLLNCRGaiaNSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPi 1055
Cdd:cd17631 1 LRRRARRHPDR---TALVFGG---RSLTYAELDERVNRLAHALRALG-VAKGDRVAVLSKNSPEFLELLFAAARLGAVF- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1056 tvrppHPQNIATTLPTVKMIVEVSRSACLMttqlickllrsreaaaavdvrtwplildtddlpkkrpaqickpcnpDTLA 1135
Cdd:cd17631 73 -----VPLNFRLTPPEVAYILADSGAKVLF----------------------------------------------DDLA 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1136 YLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELyPSREVAICLDPYC---GLGfvLWCLCSVYSGHQSILIPpselET 1212
Cdd:cd17631 102 LLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDL-GPDDVLLVVAPLFhigGLG--VFTLPTLLRGGTVVILR----KF 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1213 NPALWLLAVSQYKVRDTFCSYSVME-LCTKGlgsqteslKARGLDLSRVRtCVVVAEERPRIALTQSFSKlfkdlglhpr 1291
Cdd:cd17631 175 DPETVLDLIERHRVTSFFLVPTMIQaLLQHP--------RFATTDLSSLR-AVIYGGAPMPERLLRALQA---------- 235
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1292 avstsFGCRvnlaiclqphrLWTLAEQGTSGPdPTTVyvdMRALRHDRvRLVERGSPHslplmesgkilPGVRIIIANPE 1371
Cdd:cd17631 236 -----RGVK-----------FVQGYGMTETSP-GVTF---LSPEDHRR-KLGSAGRPV-----------FFVEVRIVDPD 283
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1372 TKgPLGDSHLGEIWVHSAHNASGYftiYGDESLQSDhfnsrlSFGDTqtiWARTGYLGFLrrteltDANGerhdALYVVG 1451
Cdd:cd17631 284 GR-EVPPGEVGEIVVRGPHVMAGY---WNRPEATAA------AFRDG---WFHTGDLGRL------DEDG----YLYIVD 340
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530392108 1452 ALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF-----TWTNLLV-VVVELDGSEQEALDLV 1509
Cdd:cd17631 341 RKKDMIISGGENVYPAEVE-DVLYEHPAVAEVAVIgvpdeKWGEAVVaVVVPRPGAELDEDELI 403
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
344-446 |
4.71e-07 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 54.30 E-value: 4.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 344 GKPLYI-----LTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFpnNDPAAFMAAFYGCLLAEVVPVPIEVPLT 418
Cdd:cd05959 19 DKTAFIddagsLTYAELEAEARRVA-GALRALG------VKREERVLLIM--LDTVDFPTAFLGAIRAGIVPVPVNTLLT 89
|
90 100
....*....|....*....|....*...
gi 530392108 419 rkdagSQQIGFLLGSCGVTVALTSDACH 446
Cdd:cd05959 90 -----PDDYAYYLEDSRARVVVVSGELA 112
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
974-1154 |
7.31e-07 |
|
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: 53.87 E-value: 7.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 974 EVLQWRAQTTPDHIlytllncrgAIA---NSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYA 1050
Cdd:cd17655 1 ELFEEQAEKTPDHT---------AVVfedQTLTYRELNERANQLARTLREKG-VGPDTIVGIMAERSLEMIVGILGILKA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1051 GC--VPITvrPPHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLRSREAAaavdvrtwpLILDTDDLPKKRPAQICKP 1128
Cdd:cd17655 71 GGayLPID--PDYPEE------RIQYILEDSGADILLTQSHLQPPIAFIGLI---------DLLDEDTIYHEESENLEPV 133
|
170 180
....*....|....*....|....*.
gi 530392108 1129 CNPDTLAYLDFSVSTTGMLAGVKMSH 1154
Cdd:cd17655 134 SKSDDLAYVIYTSGSTGKPKGVMIEH 159
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
350-444 |
3.75e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 51.47 E-value: 3.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 350 LTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNDpaAFMAAFYGCLLAEVVPVPIEVPLTRKDagsqqIGF 429
Cdd:PRK08316 37 WTYAELDAAVNRVA-AALLDLG------LKKGDRVAALGHNSD--AYALLWLACARAGAVHVPVNFMLTGEE-----LAY 102
|
90
....*....|....*
gi 530392108 430 LLGSCGVTVALTSDA 444
Cdd:PRK08316 103 ILDHSGARAFLVDPA 117
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1128-1485 |
7.12e-06 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 50.76 E-value: 7.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1128 PCNPDTLAYLDFSVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAICLDPYC-GLGFVLWCLCSVYSGHQSILIP 1206
Cdd:PRK07768 148 ETGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAAEFDVETDVMVSWLPLFhDMGMVGFLTVPMYFGAELVKVT 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1207 PSELETNPALWLLAVSQYKVRDTFCSYSVMELCTKGLGSQTESlkaRGLDLSRVRtCVVVAEERPRIALTQSFSKLFKDL 1286
Cdd:PRK07768 228 PMDFLRDPLLWAELISKYRGTMTAAPNFAYALLARRLRRQAKP---GAFDLSSLR-FALNGAEPIDPADVEDLLDAGARF 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1287 GLHPRAVSTSFG-CRVNLAICLQPhrlwtlaeqgtSGPDPTTVYVDMRALRHDRvRLVERGSPHSLPLMESGKILPG--V 1363
Cdd:PRK07768 304 GLRPEAILPAYGmAEATLAVSFSP-----------CGAGLVVDEVDADLLAALR-RAVPATKGNTRRLATLGPPLPGleV 371
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1364 RIIIANPEtkgPLGDSHLGEIWVHSAHNASGYFTIYGDESLQSDHfnsrlsfGdtqtiWARTGYLGFLrrTEltdaNGEr 1443
Cdd:PRK07768 372 RVVDEDGQ---VLPPRGVGVIELRGESVTPGYLTMDGFIPAQDAD-------G-----WLDTGDLGYL--TE----EGE- 429
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 530392108 1444 hdaLYVVGALDEAMELRGMRYHPIDIETSVIRAHKSVTECAV 1485
Cdd:PRK07768 430 ---VVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAV 468
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
350-441 |
1.18e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 49.96 E-value: 1.18e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 350 LTYGKLWTRSMKVAYSILHKLGtkqepmVRPGDRVALvFPNNDPaAFMAAFYGCLLAEVVPVPIEvPLTRkdagSQQIGF 429
Cdd:PRK08314 36 ISYRELLEEAERLAGYLQQECG------VRKGDRVLL-YMQNSP-QFVIAYYAILRANAVVVPVN-PMNR----EEELAH 102
|
90
....*....|..
gi 530392108 430 LLGSCGVTVALT 441
Cdd:PRK08314 103 YVTDSGARVAIV 114
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
930-1156 |
1.41e-05 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 50.04 E-value: 1.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 930 QPEIGPASVmvgNLVSGKRIAQasgrdLGQIEDNDQARKFLFLSEVLQWRAQTTPDhilytllncRGAIA---NSLTCVQ 1006
Cdd:PRK10252 426 DPALLCGDV---DILLPGEYAQ-----LAQVNATAVEIPETTLSALVAQQAAKTPD---------APALAdarYQFSYRE 488
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1007 LHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRPPHPQNiattlpTVKMIVEVSRSACLMT 1086
Cdd:PRK10252 489 MREQVVALANLLRERG-VKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDD------RLKMMLEDARPSLLIT 561
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1087 TQlickLLRSREAAAAVDVRTWPLILDTDdlPKKRPAQICKPCNPdtlAYLDFSVSTTGMLAGVKMSHAA 1156
Cdd:PRK10252 562 TA----DQLPRFADVPDLTSLCYNAPLAP--QGAAPLQLSQPHHT---AYIIFTSGSTGRPKGVMVGQTA 622
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
324-440 |
1.54e-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: 49.15 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 324 LQRWGTISPKAPCLTTMDTngkplyILTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNDpaAFMAAFYGC 403
Cdd:cd17631 1 LRRRARRHPDRTALVFGGR------SLTYAELDERVNRLA-HALRALG------VAKGDRVAVLSKNSP--EFLELLFAA 65
|
90 100 110
....*....|....*....|....*....|....*..
gi 530392108 404 LLAEVVPVPIEVPLTRKDagsqqIGFLLGSCGVTVAL 440
Cdd:cd17631 66 ARLGAVFVPLNFRLTPPE-----VAYILADSGAKVLF 97
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
540-905 |
2.13e-05 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 48.99 E-value: 2.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 540 LDFKKDVG-----LWHG-----ILTSVMNMMHVISIPYSLMKVNPLSWIQKVCQYKAKVacVKSRDMHWALVAH--RDQR 607
Cdd:PRK05851 190 LDAATDVGcswlpLYHDmglafLLTAALAGAPLWLAPTTAFSASPFRWLSWLSDSRATL--TAAPNFAYNLIGKyaRRVS 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 608 DINLSSLRMLIvaDGANPWSISSCDAFLNVFQSKGLRQEVICPCASSPEAlTVAIRRPTddsnqpPGRGVLsmhgltygV 687
Cdd:PRK05851 268 DVDLGALRVAL--NGGEPVDCDGFERFATAMAPFGFDAGAAAPSYGLAES-TCAVTVPV------PGIGLR--------V 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 688 IRVDSEEKLSVLTVQDVGLVMPGA---IMCSVKPDGVPQlcrtDEIGELCVCAVATGTSYYGlsgmtkntfevfpmtssG 764
Cdd:PRK05851 331 DEVTTDDGSGARRHAVLGNPIPGMevrISPGDGAAGVAG----REIGEIEIRGASMMSGYLG-----------------Q 389
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 765 APISEYPFIRTGLLGFVGPGGLVfVVGKMDGLMVVSGRRHNADDIVATALAVEPmkfVYRGRIavfsVTVLHDE-----R 839
Cdd:PRK05851 390 APIDPDDWFPTGDLGYLVDGGLV-VCGRAKELITVAGRNIFPTEIERVAAQVRG---VREGAV----VAVGTGEgsarpG 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530392108 840 IVIVAEQRpdSTEEDSFQwmSRVLQAIDSihQVGVyclalVPAN-------TLPKTPLGGIHLSETKQLFLEG 905
Cdd:PRK05851 462 LVIAAEFR--GPDEAGAR--SEVVQRVAS--ECGV-----VPSDvvfvapgSLPRTSSGKLRRLAVKRSLEAA 523
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
972-1061 |
2.72e-05 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 48.60 E-value: 2.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 972 LSEVLQWRAQTTPDHIlytllncrgAI---ANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCL 1048
Cdd:COG1021 27 LGDLLRRRAERHPDRI---------AVvdgERRLSYAELDRRADRLAAGLLALG-LRPGDRVVVQLPNVAEFVIVFFALF 96
|
90
....*....|...
gi 530392108 1049 YAGCVPITVRPPH 1061
Cdd:COG1021 97 RAGAIPVFALPAH 109
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
972-1160 |
2.78e-05 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 48.75 E-value: 2.78e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 972 LSEVLQWRAQTTPDHIlytllncrgAIA---NSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCL 1048
Cdd:PRK07656 7 LPELLARAARRFGDKE---------AYVfgdQRLTYAELNARVRRAAAALAALG-IGKGDRVAIWAPNSPHWVIAALGAL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1049 YAGCVPITVRPPH-PQNIATTLPT--VKMI--------VEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDl 1117
Cdd:PRK07656 77 KAGAVVVPLNTRYtADEAAYILARgdAKALfvlglflgVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFLAAGD- 155
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 530392108 1118 PKKRPAQIckpcNPDTLAYLDFSVSTTGMLAGVKMSHAAT-SAF 1160
Cdd:PRK07656 156 PAERAPEV----DPDDVADILFTSGTTGRPKGAMLTHRQLlSNA 195
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
316-444 |
5.48e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 47.73 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 316 WPP-------------SLEAALQRWGTISPKAPCLttmDTNGkplYILTYGKLWTRSMKVAySILHKLGtkqepmVRPGD 382
Cdd:PRK06178 18 WPAgiprepeyphgerPLTEYLRAWARERPQRPAI---IFYG---HVITYAELDELSDRFA-ALLRQRG------VGAGD 84
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530392108 383 RVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEvPLTRKdagsQQIGFLLGSCGVTVALTSDA 444
Cdd:PRK06178 85 RVAVFLPNC--PQFHIVFFGILKLGAVHVPVS-PLFRE----HELSYELNDAGAEVLLALDQ 139
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
974-1161 |
6.22e-05 |
|
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes linear gramicidin synthetase (LgrA) in Brevibacillus brevis. LgrA has a formylation domain fused to the N-terminal end that formylates its substrate for linear gramicidin synthesis to proceed. This formyl group is essential for the clinically important antibacterial activity of gramicidin by enabling head-to-head gramicidin dimers to make a beta-helical pore in gram-positive bacterial membranes, allowing free passage of monovalent cations, destroying the ion gradient and killing bacteria. This family also includes bacitracin synthetase 1 (known as ATP-dependent cysteine adenylase or BA1); it activates cysteine, incorporates two D-amino acids, releases and cyclizes the mature bacitracin, an antibiotic that is a mixture of related cyclic peptides that disrupt gram positive bacteria by interfering with cell wall and peptidoglycan synthesis. Also included is surfactin synthetase which activates and polymerizes the amino acids Leu, Glu, Asp, and Val to form the antibiotic surfactin.
Pssm-ID: 341300 [Multi-domain] Cd Length: 440 Bit Score: 47.55 E-value: 6.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 974 EVLQWRAQTTPDHILYTLlncRGaiaNSLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCV 1053
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD---RG---QSLTYKQLNEKANQLARHLRGKGVKPD-DQVGIMLDKSLDMIAAILGVLKAGGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1054 PITVRPPHPQniattlptvkmivevsrsaclmttQLICKLLRSREAAaavdvrtwpLILDtddlpkkrpaqickpcNPDT 1133
Cdd:cd17645 75 YVPIDPDYPG------------------------ERIAYMLADSSAK---------ILLT----------------NPDD 105
|
170 180
....*....|....*....|....*...
gi 530392108 1134 LAYLDFSVSTTGMLAGVKMSHAATSAFC 1161
Cdd:cd17645 106 LAYVIYTSGSTGLPKGVMIEHHNLVNLC 133
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
321-444 |
6.36e-05 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 47.41 E-value: 6.36e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 321 EAALQRWGTISPKAPCLTTMDTNGKPlYILTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdPAAfMAAF 400
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGEDGEE-RTLTYAELRREVNRFA-NALRALG------VKKGDRVAIYLPNI-PEA-VIAM 81
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 530392108 401 YGCLLAEVVPVPIeVPLTRKDAgsqqIGFLLGSCGVTVALTSDA 444
Cdd:COG0365 82 LACARIGAVHSPV-FPGFGAEA----LADRIEDAEAKVLITADG 120
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
980-1155 |
1.67e-04 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 46.04 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 980 AQTTPDHILYtllNCRGAianSLTCVQLHKRAEKIAVMLMERgHLQDGDHVaLVY----PpgiDLIAAFYGCLYAGC--V 1053
Cdd:PRK04813 12 AQTQPDFPAY---DYLGE---KLTYGQLKEDSDALAAFIDSL-KLPDKSPI-IVFghmsP---EMLATFLGAVKAGHayI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1054 PITVRPPhpqniattLPTVKMIVEVSRSACLMTTqlickllrSREAAAAVDVRTwpLILD--TDDLPKKRPAQICKPCNP 1131
Cdd:PRK04813 81 PVDVSSP--------AERIEMIIEVAKPSLIIAT--------EELPLEILGIPV--ITLDelKDIFATGNPYDFDHAVKG 142
|
170 180
....*....|....*....|....
gi 530392108 1132 DTLAYLDFSVSTTGMLAGVKMSHA 1155
Cdd:PRK04813 143 DDNYYIIFTSGTTGKPKGVQISHD 166
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
350-444 |
2.24e-04 |
|
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: 45.66 E-value: 2.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 350 LTYGKLWTRSMKVAYSiLHKLGtkqepmVRPGDRVALvFPNNDPAAFMAAFyGCLLAEVVPVPIevpltRKDAGSQQIGF 429
Cdd:cd05907 6 ITWAEFAEEVRALAKG-LIALG------VEPGDRVAI-LSRNRPEWTIADL-AILAIGAVPVPI-----YPTSSAEQIAY 71
|
90
....*....|....*
gi 530392108 430 LLGSCGVTVALTSDA 444
Cdd:cd05907 72 ILNDSEAKALFVEDP 86
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
351-803 |
2.35e-04 |
|
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: 45.33 E-value: 2.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 351 TYGKLWTRSMKVAYSILHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEV--PLTRkdagsqqIG 428
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAGG------VGPGDRVAVLLERS--AELVVAILAVLKAGAAYVPLDPayPAER-------LA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 429 FLLGSCGVTVALTSDACHKGLPKSPTGEIPqfkgwPKLLWFVTESKHLSKPPRDWFPHikdaNNDTAYIEY--------K 500
Cdd:TIGR01733 66 FILEDAGARLLLTDSALASRLAGLVLPVIL-----LDPLELAALDDAPAPPPPDAPSG----PDDLAYVIYtsgstgrpK 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 501 tckdgsvlGVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWHgILTSVMNMMHVISIPYSLMKVNPLSWIQK 580
Cdd:TIGR01733 137 --------GVVVTHRSLVNLLAWLARRYGLDPDDRVLQFASLSFDASVEE-IFGALLAGATLVVPPEDEERDDAALLAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 581 VCQYKAKVAC-VKSrdmHWALVAhrDQRDINLSSLRMLIVAdGanpwsisscdaflnvfqskglrqevicpcasspEALT 659
Cdd:TIGR01733 208 IAEHPVTVLNlTPS---LLALLA--AALPPALASLRLVILG-G---------------------------------EALT 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 660 VA-IRRPtddSNQPPGRGVLSMHGLTYGVI-----RVDSEEkLSVLTVQDVGLVMPGAIMCSVKPDGvpQLCRTDEIGEL 733
Cdd:TIGR01733 249 PAlVDRW---RARGPGARLINLYGPTETTVwstatLVDPDD-APRESPVPIGRPLANTRLYVLDDDL--RPVPVGVVGEL 322
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530392108 734 CVCA--VATGtsYYGLSGMTKNTF-EVFPMTSSGAPIseYpfiRTGLLGFVGPGGLVFVVGKMDGLMVVSGRR 803
Cdd:TIGR01733 323 YIGGpgVARG--YLNRPELTAERFvPDPFAGGDGARL--Y---RTGDLVRYLPDGNLEFLGRIDDQVKIRGYR 388
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
350-411 |
2.49e-04 |
|
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: 45.52 E-value: 2.49e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530392108 350 LTYGKLWTRSMKVAYSiLHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPV 411
Cdd:COG1021 51 LSYAELDRRADRLAAG-LLALG------LRPGDRVVVQLPNV--AEFVIVFFALFRAGAIPV 103
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
350-539 |
2.67e-04 |
|
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: 45.36 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 350 LTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEvpltrKDAGSQQIGF 429
Cdd:cd12116 13 LSYAELDERANRLA-ARLRARG------VGPGDRVAVYLPRS--ARLVAAMLAVLKAGAAYVPLD-----PDYPADRLRY 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 430 LLGSCGVTVALTSDACHKGLPKSPTgeipqfkGWPKLLWFVTESKHLSKPPrdwfphikDANNDTAYIEYKTCKDGSVLG 509
Cdd:cd12116 79 ILEDAEPALVLTDDALPDRLPAGLP-------VLLLALAAAAAAPAAPRTP--------VSPDDLAYVIYTSGSTGRPKG 143
|
170 180 190
....*....|....*....|....*....|
gi 530392108 510 VTVTRTALLTHCQALTQACGYTEAETIVNV 539
Cdd:cd12116 144 VVVSHRNLVNFLHSMRERLGLGPGDRLLAV 173
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
983-1154 |
3.43e-04 |
|
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains gramicidin S synthase 2 (also known as ATP-dependent proline adenylase or proline activase or ProA). ProA is a multifunctional enzyme involved in synthesis of the cyclic peptide antibiotic gramicidin S and able to activate and polymerize the amino acids proline, valine, ornithine and leucine. 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: 341311 [Multi-domain] Cd Length: 479 Bit Score: 45.16 E-value: 3.43e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 983 TPDHILYTLLNCrgaianSLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAG--CVPITvrpP 1060
Cdd:cd17656 1 TPDAVAVVFENQ------KLTYRELNERSNQLARFLREKGVKKD-SIVAIMMERSAEMIVGILGILKAGgaFVPID---P 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1061 HpqniattLPTVKMIVEVSRSAC-LMTTQLICKLLRSREAAaaVDVRTWPLILDTDDlpkkrpAQICKPCNPDTLAYLDF 1139
Cdd:cd17656 71 E-------YPEERRIYIMLDSGVrVVLTQRHLKSKLSFNKS--TILLEDPSISQEDT------SNIDYINNSDDLLYIIY 135
|
170
....*....|....*
gi 530392108 1140 SVSTTGMLAGVKMSH 1154
Cdd:cd17656 136 TSGTTGKPKGVQLEH 150
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
332-542 |
3.44e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 44.95 E-value: 3.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 332 PKAPCLTTMDTNgkplyiLTYGKLWTRSMKVAYSiLHKLGtkqepmVRPGDRVALVFPNNDPAafMAAFYGCLLAEVVPV 411
Cdd:cd12114 1 PDATAVICGDGT------LTYGELAERARRVAGA-LKAAG------VRPGDLVAVTLPKGPEQ--VVAVLGILAAGAAYV 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 412 PIEV--PLTRKDAgsqqigfLLGSCGVTVALTSDACHKGLPKSPTgeipqfkgwpkllwFVTESKHLSKPPRDwFPHIKD 489
Cdd:cd12114 66 PVDIdqPAARREA-------ILADAGARLVLTDGPDAQLDVAVFD--------------VLILDLDALAAPAP-PPPVDV 123
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 530392108 490 ANNDTAYIEYKTCKDGSVLGVTVTRTALLTHCQALTQACGYTEAETIVNV--LDF 542
Cdd:cd12114 124 APDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVGPDDRVLALssLSF 178
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
980-1485 |
4.15e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 45.54 E-value: 4.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 980 AQTTPDHILYTLLNCRgaiansLTCVQLHKRAEKIAVMLMERGHLQDgDHVALVYPPGIDLIAAFYGCLYAGCVPITVRP 1059
Cdd:PRK12467 522 ARQHPERPALVFGEQV------LSYAELNRQANRLAHVLIAAGVGPD-VLVGIAVERSIEMVVGLLAVLKAGGAYVPLDP 594
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1060 PHPQNiattlpTVKMIVEVSRSACLMTTQLICKLLrsreaAAAVDVRTWPLILDTDDLPKKRPAQICKPCNPDTLAYLDF 1139
Cdd:PRK12467 595 EYPQD------RLAYMLDDSGVRLLLTQSHLLAQL-----PVPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIY 663
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1140 SVSTTGMLAGVKMSHAATSAFCRSIKLQCELYPSREVAIcLDPYCGLGFVLWCLCSVYSGHQSILIPPSEletnpalwll 1219
Cdd:PRK12467 664 TSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLM-VSTFAFDLGVTELFGALASGATLHLLPPDC---------- 732
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1220 avsqykVRDTFCSYSVMelCTKGLG--SQTES-----LKARGLDLSRVRTCVVVAEErpriALTQSFSKLFKDLGLhpra 1292
Cdd:PRK12467 733 ------ARDAEAFAALM--ADQGVTvlKIVPShlqalLQASRVALPRPQRALVCGGE----ALQVDLLARVRALGP---- 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1293 vstsfGCrvnlaiclqphRLWTLaeqgtSGPDPTTVYVDMRALRHDRVrlVERGSPHSLPLMESgkilpGVRIIIA--NP 1370
Cdd:PRK12467 797 -----GA-----------RLINH-----YGPTETTVGVSTYELSDEER--DFGNVPIGQPLANL-----GLYILDHylNP 848
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1371 ETKGPLGDSHLGeiwvhSAHNASGYftiYGDESLQSDHFNSRLSFGDTQTIWaRTGYLGflRRTeltdANGErhdaLYVV 1450
Cdd:PRK12467 849 VPVGVVGELYIG-----GAGLARGY---HRRPALTAERFVPDPFGADGGRLY-RTGDLA--RYR----ADGV----IEYL 909
|
490 500 510
....*....|....*....|....*....|....*
gi 530392108 1451 GALDEAMELRGMRYHPIDIETSvIRAHKSVTECAV 1485
Cdd:PRK12467 910 GRMDHQVKIRGFRIELGEIEAR-LLAQPGVREAVV 943
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
350-549 |
5.67e-04 |
|
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: 44.85 E-value: 5.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 350 LTYGKLWTRSMKVAYSiLHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPI--EVPLTRkdagsqqI 427
Cdd:COG1020 502 LTYAELNARANRLAHH-LRALG------VGPGDLVGVCLERS--LEMVVALLAVLKAGAAYVPLdpAYPAER-------L 565
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 428 GFLLGSCGVTVALTSDACHKGLPKSptgeipqfkgwpKLLWFVTESKHLSKPPRDWfPHIKDANNDTAYIEY-------- 499
Cdd:COG1020 566 AYMLEDAGARLVLTQSALAARLPEL------------GVPVLALDALALAAEPATN-PPVPVTPDDLAYVIYtsgstgrp 632
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 530392108 500 KtckdgsvlGVTVTRTALLTHCQALTQACGYTEAETIVNV--LDFkkDVGLW 549
Cdd:COG1020 633 K--------GVMVEHRALVNLLAWMQRRYGLGPGDRVLQFasLSF--DASVW 674
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
350-444 |
6.49e-04 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 44.32 E-value: 6.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 350 LTYGKLWTRSMKVAYSiLHKLGtkqepmVRPGDRVALvFPNNDPAAFMAAFyGCLLAEVVPVPIEVpltrkDAGSQQIGF 429
Cdd:COG1022 41 LTWAEFAERVRALAAG-LLALG------VKPGDRVAI-LSDNRPEWVIADL-AILAAGAVTVPIYP-----TSSAEEVAY 106
|
90
....*....|....*
gi 530392108 430 LLGSCGVTVALTSDA 444
Cdd:COG1022 107 ILNDSGAKVLFVEDQ 121
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
350-889 |
7.60e-04 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 44.06 E-value: 7.60e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 350 LTYGKLWTRSMKVAYSILHKLgtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEV--PLTRkdagsqqI 427
Cdd:cd05930 13 LTYAELDARANRLARYLRERG-------VGPGDLVAVLLERS--LEMVVAILAVLKAGAAYVPLDPsyPAER-------L 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 428 GFLLGSCGVTVALTSDachkglpksptgeipqfkgwpkllwfvteskhlskpprdwfphikdanNDTAYIEY-------- 499
Cdd:cd05930 77 AYILEDSGAKLVLTDP------------------------------------------------DDLAYVIYtsgstgkp 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 500 KtckdgsvlGVTVTRTALLTHCQALTQACGYTEAETIVNVLDFKKDVGLWhGILTSVMN--MMHVISipySLMKVNPLSW 577
Cdd:cd05930 109 K--------GVMVEHRGLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVW-EIFGALLAgaTLVVLP---EEVRKDPEAL 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 578 IQKVCQYKAKVA-CVKSrdmHW-ALVAHRDQRDinLSSLRMLIVAdGanpwsisscdaflnvfqskglrqevicpcassp 655
Cdd:cd05930 177 ADLLAEEGITVLhLTPS---LLrLLLQELELAA--LPSLRLVLVG-G--------------------------------- 217
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 656 EALTVAIRRPTDDSNqpPGRGVLSMHGLT-------YGVIRVDSEEKLSVltvqDVGLVMPGAIMCSVKPDGvpQLCRTD 728
Cdd:cd05930 218 EALPPDLVRRWRELL--PGARLVNLYGPTeatvdatYYRVPPDDEEDGRV----PIGRPIPNTRVYVLDENL--RPVPPG 289
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 729 EIGELCVC--AVATGtsYYGLSGMTKntfEVFPMTSSGAPISEYpfiRTGLLGFVGPGGLVFVVGKMDGLMVVSGRRHNA 806
Cdd:cd05930 290 VPGELYIGgaGLARG--YLNRPELTA---ERFVPNPFGPGERMY---RTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIEL 361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 807 DDIVATALAVEPMkfvyrgRIAVfsVTVLHD----ERIV--IVAEQRPDSTEEDSFQWMSRVLQAidsihqvgvYCL--A 878
Cdd:cd05930 362 GEIEAALLAHPGV------REAA--VVAREDgdgeKRLVayVVPDEGGELDEEELRAHLAERLPD---------YMVpsA 424
|
570
....*....|.
gi 530392108 879 LVPANTLPKTP 889
Cdd:cd05930 425 FVVLDALPLTP 435
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
998-1226 |
9.17e-04 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 43.87 E-value: 9.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 998 IANSLTCVQLHKRAEKIAVMLMERGhLQDGDHVALVYPPGIDLIAAFYGCLYAGCVPITVRP------------------ 1059
Cdd:PRK06710 46 LGKDITFSVFHDKVKRFANYLQKLG-VEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPlytereleyqlhdsgakv 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1060 --------PHPQNIATTLPTVKMIVEVSRSACLMTTQLICKLLRSREAAAAVDVRTWPLILDTDDLPKKRPAQICKPCNP 1131
Cdd:PRK06710 125 ilcldlvfPRVTNVQSATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCDP 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1132 DT-LAYLDFSVSTTGMLAGVKMSHA-ATSAFCRSIKLQCELYPSREVAICLDPYCGL-GFVLWCLCSVYSGHQSILIPPS 1208
Cdd:PRK06710 205 ENdLALLQYTGGTTGFPKGVMLTHKnLVSNTLMGVQWLYNCKEGEEVVLGVLPFFHVyGMTAVMNLSIMQGYKMVLIPKF 284
|
250
....*....|....*...
gi 530392108 1209 ELEtnpaLWLLAVSQYKV 1226
Cdd:PRK06710 285 DMK----MVFEAIKKHKV 298
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
350-441 |
1.13e-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: 43.24 E-value: 1.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 350 LTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEvPLTRKDagsqQIGF 429
Cdd:cd05935 2 LTYLELLEVVKKLA-SFLSNKG------VRKGDRVGICLQNS--PQYVIAYFAIWRANAVVVPIN-PMLKER----ELEY 67
|
90
....*....|..
gi 530392108 430 LLGSCGVTVALT 441
Cdd:cd05935 68 ILNDSGAKVAVV 79
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
350-421 |
1.31e-03 |
|
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: 43.22 E-value: 1.31e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530392108 350 LTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPnnDPAAFMAAFYGCLLAEVVPVPIEVPLTRKD 421
Cdd:cd05919 11 VTYGQLHDGANRLG-SALRNLG------VSSGDRVLLLML--DSPELVQLFLGCLARGAIAVVINPLLHPDD 73
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1357-1499 |
2.62e-03 |
|
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: 42.04 E-value: 2.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1357 GKILPGVRIIIANPEtKGPLGDSHLGEIWVHSAHNASGYFTIYGDEsLQSDHFNSRLsfgdtqtiwaRTGYLGFLrrtel 1436
Cdd:cd05922 289 GLAIPGGEFEILDDD-GTPTPPGEPGEIVHRGPNVMKGYWNDPPYR-RKEGRGGGVL----------HTGDLARR----- 351
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530392108 1437 tDANGErhdaLYVVGALDEAMELRGMRYHPIDIETSvIRAHKSVTECAVF----TWTNLLVVVVELD 1499
Cdd:cd05922 352 -DEDGF----LFIVGRRDRMIKLFGNRISPTEIEAA-ARSIGLIIEAAAVglpdPLGEKLALFVTAP 412
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
351-411 |
3.05e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 41.91 E-value: 3.05e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530392108 351 TYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdPaAFMAAFYGCLLAEVVPV 411
Cdd:PRK05605 59 TYAELGKQVRRAA-AGLRALG------VRPGDRVAIVLPNC-P-QHIVAFYAVLRLGAVVV 110
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1357-1485 |
3.58e-03 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 41.48 E-value: 3.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1357 GKILPGVRIIIANPETKGPLGDSHlGEIWVHSAHNASGYftiYGDESLQSDHFNSRlsfgdtqtiWARTGYLGFLRrtel 1436
Cdd:cd17635 173 GRPYPGVDVYLAATDGIAGPSASF-GTIWIKSPANMLGY---WNNPERTAEVLIDG---------WVNTGDLGERR---- 235
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 530392108 1437 tdangeRHDALYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAV 1485
Cdd:cd17635 236 ------EDGFLFITGRSSESINCGGVKIAPDEVE-RIAEGVSGVQECAC 277
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
350-467 |
4.64e-03 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 41.43 E-value: 4.64e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 350 LTYGKLWTRSMKVAySILHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEVPLTRKDagsqqIGF 429
Cdd:PRK08276 12 VTYGELEARSNRLA-HGLRALG------LREGDVVAILLENN--PEFFEVYWAARRSGLYYTPINWHLTAAE-----IAY 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 530392108 430 LLGSCGVTVALTS----DACHKGLPKSP---------TGEIPQFKGWPKLL 467
Cdd:PRK08276 78 IVDDSGAKVLIVSaalaDTAAELAAELPagvplllvvAGPVPGFRSYEEAL 128
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1362-1486 |
5.16e-03 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 41.41 E-value: 5.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 1362 GVRIIIANPEtKGPLGDSHLGEIWVHSAHNASGYFtiyGDESLQSDHFNSRlsfgdtqtiWARTGYLGFLrrteltDANG 1441
Cdd:PRK05852 362 GAQIRIVGSD-GLPLPAGAVGEVWLRGTTVVRGYL---GDPTITAANFTDG---------WLRTGDLGSL------SAAG 422
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 530392108 1442 ErhdaLYVVGALDEAMELRGMRYHPIDIEtSVIRAHKSVTECAVF 1486
Cdd:PRK05852 423 D----LSIRGRIKELINRGGEKISPERVE-GVLASHPNVMEAAVF 462
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
350-499 |
8.88e-03 |
|
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: 40.65 E-value: 8.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 350 LTYGKLWTRSMKVAYSILHKlGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLA--EVVPVPIEVPLTRkdagsqqI 427
Cdd:cd12117 23 LTYAELNERANRLARRLRAA-G------VGPGDVVGVLAERS--PELVVALLAVLKAgaAYVPLDPELPAER-------L 86
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530392108 428 GFLLGSCGVTVALTsdacHKGLPKSPTGEIPqfkgwpkLLWFVTESKHLSKPPrdwfPHIKDANNDTAYIEY 499
Cdd:cd12117 87 AFMLADAGAKVLLT----DRSLAGRAGGLEV-------AVVIDEALDAGPAGN----PAVPVSPDDLAYVMY 143
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
351-445 |
9.57e-03 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 40.35 E-value: 9.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530392108 351 TYGKLWTRSMKVAYSiLHKLGtkqepmVRPGDRVALVFPNNdpAAFMAAFYGCLLAEVVPVPIEVplTRKDAGSQQIgfl 430
Cdd:cd05934 5 TYAELLRESARIAAA-LAALG------IRPGDRVALMLDNC--PEFLFAWFALAKLGAVLVPINT--ALRGDELAYI--- 70
|
90
....*....|....*
gi 530392108 431 LGSCGVTVALTSDAC 445
Cdd:cd05934 71 IDHSGAQLVVVDPAS 85
|
|
| |
