|
Name |
Accession |
Description |
Interval |
E-value |
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
191-680 |
0e+00 |
|
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: 664.04 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 191 FERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYP 270
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 271 AQRLALILETAQPFRVVAHPEHAHVAAAERVLPV----EELVADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRM 346
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTlldqPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 347 WANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQR 426
Cdd:cd17651 161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 427 LAEASNALGVRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPAHYPDLPPIGRPLDGV 506
Cdd:cd17651 241 LAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGLPGLRLHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 507 EVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKV 586
Cdd:cd17651 321 RVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 587 RGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEPEA-VDLAELKQALRSELPEHMVPAHFAWVDG 665
Cdd:cd17651 401 RGFRIELGEIEAALA----RHPGVREAVVLAREDRPGEKRLVAYVVGDPEApVDAAELRAALATHLPEYMVPSAFVLLDA 476
|
490
....*....|....*
gi 1395399044 666 FALTPSGKRDDAALR 680
Cdd:cd17651 477 LPLTPNGKLDRRALP 491
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
4-1006 |
3.01e-174 |
|
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: 545.99 E-value: 3.01e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 4 LTLHLFSRSDSVVTGAISNGRPElPDADRMVGLFLNTVPVRSEIAGH-SWIEVADALFRQERDGHAHRRYPLSAIQQIVG 82
Cdd:COG1020 274 LLLARYSGQDDVVVGTPVAGRPR-PELEGLVGFFVNTLPLRVDLSGDpSFAELLARVRETLLAAYAHQDLPFERLVEELQ 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 83 DELS--------SAFNYVNLHVLE---PLWQLRDFRVWEET-NFALLVNVIATPsDGMYLRIDSDGRGISRSQAALIGAT 150
Cdd:COG1020 353 PERDlsrnplfqVMFVLQNAPADElelPGLTLEPLELDSGTaKFDLTLTVVETG-DGLRLTLEYNTDLFDAATIERMAGH 431
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 151 FVELLWRLAEHPDE---------AADFAFLAPRRDAASQPEPL-VDVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVA 220
Cdd:COG1020 432 LVTLLEALAADPDQplgdlplltAAERQQLLAEWNATAAPYPAdATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARA 511
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 221 RCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHVAAAE- 299
Cdd:COG1020 512 NRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELg 591
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 300 -RVLPVEELVADIEPETFAAPQL--DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDM 376
Cdd:COG1020 592 vPVLALDALALAAEPATNPPVPVtpDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDA 671
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 377 AFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNAlgvRPGALRVVVSSGEQLRiTED 456
Cdd:COG1020 672 SVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPE---ALPSLRLVLVGGEALP-PEL 747
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 457 VRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHyPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLAR 535
Cdd:COG1020 748 VRRWRARLPGARLVNLYGPTETTvDSTYYEVTPPDAD-GGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLAR 826
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 536 GYHRAPELTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAA 614
Cdd:COG1020 827 GYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALL----QHPGVREAV 902
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 615 VVARERQGNDAFLAAFLLGEPEAVDLAE-LKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRALPLEHGTniEYL 693
Cdd:COG1020 903 VVAREDAPGDKRLVAYVVPEAGAAAAAAlLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAA--AAA 980
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 694 APRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLRERSAVRA 773
Cdd:COG1020 981 APPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAA 1060
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 774 fDPLVPIRAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGSTPLAVLEDIAASYLAAIRRVQPEGPY 853
Cdd:COG1020 1061 -APLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLR 1139
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 854 YLGGWSFGGFVAYEMARQLRALDPQAVAQLIVLDSITVDRNHAGSASDEALLLFFYWELVWFERSDEEVEPLPEGASLEQ 933
Cdd:COG1020 1140 LLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1219
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395399044 934 KLDHIVERAIEAGVLPAGTPRATVQRLYELFRASWQALIGYRPEVSDQDMTLLRADGPLPLALKPMHDAAGTH 1006
Cdd:COG1020 1220 LLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTA 1292
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
199-679 |
5.93e-160 |
|
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: 480.10 E-value: 5.93e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 278
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 279 ETAQPFRVVAHPEHahvaaaervlpveelvadiepetfaapqldeLAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVA 358
Cdd:cd05930 81 EDSGAKLVLTDPDD-------------------------------LAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 359 SGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEAsnALGVRP 438
Cdd:cd05930 130 PLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQE--LELAAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 439 GALRVVVSSGEQLRiTEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYpDLPPIGRPLDGVEVQVLDAALRP 517
Cdd:cd05930 208 PSLRLVLVGGEALP-PDLVRRWRELLPGARLVNLYGPTEATvDATYYRVPPDDEED-GRVPIGRPIPNTRVYVLDENLRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 518 VPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE 597
Cdd:cd05930 286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 598 LAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFL-LGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDD 676
Cdd:cd05930 366 AALL----AHPGVREAAVVAREDGDGEKRLVAYVvPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDR 441
|
...
gi 1395399044 677 AAL 679
Cdd:cd05930 442 KAL 444
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
6-1053 |
1.21e-147 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 474.53 E-value: 1.21e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 6 LHLFSRSDSVVTGAISNGRPELPdADRMVGLFLNTVPVRSEIAGHSWI-EVADALFRQERDGHAHRRYPLSAIQQ---IV 81
Cdd:PRK10252 263 LGRLCGRMDYAAGFIFMRRLGSA-ALTATGPVLNVLPLRVHIAAQETLpELATRLAAQLKKMRRHQRYDAEQIVRdsgRA 341
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 82 GDELSSAFNYVNLHVLEPLWQLRDFRVWEETNFALLVNVIA-----TPSDGMYLRIDSDGRGISRSQAALIGATFVELLW 156
Cdd:PRK10252 342 AGDEPLFGPVLNIKVFDYQLDFPGVQAQTHTLATGPVNDLElalfpDEHGGLSIEILANPQRYDEATLIAHAERLKALIA 421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 157 RLAEHPD---------EAADFAFLApRRDAASQPEPLVDVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRL 227
Cdd:PRK10252 422 QFAADPAllcgdvdilLPGEYAQLA-QVNATAVEIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLL 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 228 VRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHVAAAERVL----- 302
Cdd:PRK10252 501 RERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLtslcy 580
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 303 PVEELVADIEPETFAAPQldELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIF 382
Cdd:PRK10252 581 NAPLAPQGAAPLQLSQPH--HTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFF 658
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 383 STLCGGGELQLISNRERMDPSALLHVLERRQ------VQRVLLPFVAlqrlAEASNALGVRPGALRVVVSSGEQLRiTED 456
Cdd:PRK10252 659 WPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGvttthfVPSMLAAFVA----SLTPEGARQSCASLRQVFCSGEALP-ADL 733
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 457 VRAFCAAMpGLLLENQYGPTETH-QVTYHSLSG-DPAHYPDLP-PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCL 533
Cdd:PRK10252 734 CREWQQLT-GAPLHNLYGPTEAAvDVSWYPAFGeELAAVRGSSvPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQL 812
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 534 ARGYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGA 613
Cdd:PRK10252 813 AQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQ----ALPDVEQA 888
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 614 AVVAR-----ERQGNDAF-LAAFLLGEP-EAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDaalRALPL-E 685
Cdd:PRK10252 889 VTHACvinqaAATGGDARqLVGYLVSQSgLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDR---KALPLpE 965
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 686 HGTNIEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERL 765
Cdd:PRK10252 966 LKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLL 1045
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 766 RERSAVRA---FDPLVPIRAgGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGqGSTPL-AVLEDIAASYL 841
Cdd:PRK10252 1046 DAEEDESRrlgFGTILPLRE-GDGPTLFCFHPASGFAWQFSVLSRYLDPQWSIYGIQSPRPD-GPMQTaTSLDEVCEAHL 1123
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 842 AAIRRVQPEGPYYLGGWSFGGFVAYEMARQLRALDpQAVAQLIVLDSITVDRNHagsasdealllffywelvWFERSDEE 921
Cdd:PRK10252 1124 ATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARG-EEVAFLGLLDTWPPETQN------------------WREKEANG 1184
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 922 VEP--LPEGASleqkldhivERAIEAGVLPAGTPRATVQRLYELFRASWQALIGYRPEVSDQDMTLLRADGPLPLALkpm 999
Cdd:PRK10252 1185 LDPevLAEIDR---------EREAFLAAQQGSLSTELFTTIEGNYADAVRLLTTAHSVPFDGKATLFVAERTLQEGM--- 1252
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....
gi 1395399044 1000 hdaagthygDPKNGWQHWTSGrLDVIDVPGDHLVLMKEPYVETVAAEIAALLEP 1053
Cdd:PRK10252 1253 ---------SPEQAWSPWIAE-LDVYRQDCAHVDIISPEAFEKIGPILRATLNE 1296
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-968 |
3.52e-144 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 479.27 E-value: 3.52e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 4 LTLHLFSRSDSVVTGAISNGRP-ELPDADRMVGLFLNTVPV----RSEIAGHSWIEVADALFRQERDghaHRRYPLSAIQ 78
Cdd:PRK12467 2893 LLLQRFTGQDTVCFGATVAGRPaQLRGAEQQLGLFINTLPViaspRAEQTVSDWLQQVQAQNLALRE---FEHTPLADIQ 2969
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 79 QIVGDELSSAFNYV----NLHVLEPLWQ-----LRDFRV--WEETNFA--LLVNVIATPS-DGMYLRIDSDGRGISRsqa 144
Cdd:PRK12467 2970 RWAGQGGEALFDSIlvfeNYPISEALKQgapsgLRFGAVssREQTNYPltLAVGLGDTLElEFSYDRQHFDAAAIER--- 3046
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 145 alIGATFVELLWRLAEHPDE---------AADFAFLAPRRDAASQPEPL-VDVVSLFERQVEALPGSAALAFEEQRWTYR 214
Cdd:PRK12467 3047 --LAESFDRLLQAMLNNPAArlgelptlaAHERRQVLHAWNATAAAYPSeRLVHQLIEAQVARTPEAPALVFGDQQLSYA 3124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 215 DLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHP---E 291
Cdd:PRK12467 3125 ELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAhllE 3204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 292 HAHVAAAERVLPVEELVADIEPETFAAPQLD--ELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQF 369
Cdd:PRK12467 3205 QLPAPAGDTALTLDRLDLNGYSENNPSTRVMgeNLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLF 3284
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 370 APLSFDMAFQEIFSTLCGGGELQLISNRERmDPSALLHVLERRQVQRVLLPFVALQRLAEASnalGVRPGA-LRVVVSSG 448
Cdd:PRK12467 3285 MSFSFDGAQERFLWTLICGGCLVVRDNDLW-DPEELWQAIHAHRISIACFPPAYLQQFAEDA---GGADCAsLDIYVFGG 3360
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 449 EQLRITEDVRAFcAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELY 527
Cdd:PRK12467 3361 EAVPPAAFEQVK-RKLKPRGLTNGYGPTEAVvTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELY 3439
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 528 FGGDCLARGYHRAPELTAERFVEHPWR-PGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElAIMRQaer 606
Cdd:PRK12467 3440 IGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIE-ARLLQ--- 3515
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 607 QPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDaalRALPLEH 686
Cdd:PRK12467 3516 HPSVREAVVLARDGAGGKQLVAYVVPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDR---KALPDPD 3592
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 687 GTNI-EYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERL 765
Cdd:PRK12467 3593 AKGSrEYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS 3672
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 766 RERSAvrAFDPLVPI-RAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGSTPLAVLEDIAASYLAAI 844
Cdd:PRK12467 3673 PLGDV--PVNLLLDLnRLETGFPALFCRHEGLGTVFDYEPLAVILEGDRHVLGLTCRHLLDDGWQDTSLQAMAVQYADYI 3750
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 845 RRVQPEGPYYLGGWSFGGFVAYEMARQLRAlDPQAVAQLIVLDSITVDRNHAGSASDEALLLFFYWELVwfERSDEEVEP 924
Cdd:PRK12467 3751 LWQQAKGPYGLLGWSLGGTLARLVAELLER-EGESEAFLGLFDNTLPLPDEFVPQAEFLELLRQLGELI--GRANRLLRG 3827
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*
gi 1395399044 925 LPEGA-SLEQKLDHIVERAIEAGVLPAGTPRATVQRLYELFRASW 968
Cdd:PRK12467 3828 LEEGGvGPDVLVGIAIQRCFDIAPLELYTPLLDAGELAHIFDVAM 3872
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
190-679 |
6.01e-131 |
|
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: 406.28 E-value: 6.01e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 269
Cdd:cd17646 3 LVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 270 PAQRLALILETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPET---FAAPQLDELAMLLFTSGSTGRPKGVELSHRM 346
Cdd:cd17646 83 PADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPAtppLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 347 WANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRV------LLP 420
Cdd:cd17646 163 IVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTChfvpsmLRV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 421 FVALQRLAEAsnalgvrpGALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDpaHYPDLPPI 499
Cdd:cd17646 243 FLAEPAAGSC--------ASLRRVFCSGEAL--PPELAARFLALPGAELHNLYGPTEAAiDVTHWPVRGP--AETPSVPI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 500 GRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGR 579
Cdd:cd17646 311 GRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGR 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 580 ADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEP--EAVDLAELKQALRSELPEHMVP 657
Cdd:cd17646 391 SDDQVKIRGFRVEPGEIEAAL----AAHPAVTHAVVVARAAPAGAARLVGYVVPAAgaAGPDTAALRAHLAERLPEYMVP 466
|
490 500
....*....|....*....|..
gi 1395399044 658 AHFAWVDGFALTPSGKRDDAAL 679
Cdd:cd17646 467 AAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
190-679 |
1.08e-128 |
|
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: 400.04 E-value: 1.08e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 269
Cdd:cd12117 2 LFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPEL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 270 PAQRLALILETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQL--DELAMLLFTSGSTGRPKGVELSHR-- 345
Cdd:cd12117 82 PAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVspDDLAYVMYTSGSTGRPKGVAVTHRgv 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 346 ----MWANYtqwqlrvASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPF 421
Cdd:cd12117 162 vrlvKNTNY-------VTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 422 VALQRLAEAsnalgvRPGA---LRVVVSSGEQLRItEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPAHYPDLPP 498
Cdd:cd12117 235 ALFNQLADE------DPECfagLRELLTGGEVVSP-PHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGSIP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 499 IGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLG 578
Cdd:cd12117 308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 579 RADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEpEAVDLAELKQALRSELPEHMVPA 658
Cdd:cd12117 388 RIDDQVKIRGFRIELGEIEAAL----RAHPGVREAVVVVREDAGGDKRLVAYVVAE-GALDAAELRAFLRERLPAYMVPA 462
|
490 500
....*....|....*....|.
gi 1395399044 659 HFAWVDGFALTPSGKRDDAAL 679
Cdd:cd12117 463 AFVVLDELPLTANGKVDRRAL 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
212-615 |
4.11e-125 |
|
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: 387.78 E-value: 4.11e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDLDHVARCVATRLV-RAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHP 290
Cdd:TIGR01733 1 TYRELDERANRLARHLRaAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 291 EHAHVAAA---ERVLPVEELVADIEPET-----FAAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVP 362
Cdd:TIGR01733 81 ALASRLAGlvlPVILLDPLELAALDDAPappppDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 363 GLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALL-HVLERRQVQRVLLPFVALQRLAEASNAlgvRPGAL 441
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLaALIAEHPVTVLNLTPSLLALLAAALPP---ALASL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 442 RVVVSSGEQLRiTEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPV 520
Cdd:TIGR01733 238 RLVILGGEALT-PALVDRWRARGPGARLINLYGPTETTvWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLRPVPV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 521 GVTGELYFGGDCLARGYHRAPELTAERFVEHPWRP--GARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVEL 598
Cdd:TIGR01733 317 GVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 396
|
410
....*....|....*..
gi 1395399044 599 AIMrqaeRQPGLRGAAV 615
Cdd:TIGR01733 397 ALL----RHPGVREAVV 409
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-775 |
1.23e-118 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 403.95 E-value: 1.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 1 AHCLTLHLFSRSDSVVTGAISNGRP-ELPDADRMVGLFLNTVPVRSEIAGH-SWIEVADALFRQERDGHAHRRYPLSAIQ 78
Cdd:PRK12316 4346 AWLLLLQRYTGQDTVAFGATVAGRPaELPGIEGQIGLFINTLPVIATPRAQqSVVEWLQQVQRQNLALREHEHTPLYEIQ 4425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 79 QIVGDELSSAF----NYVNLHVLEPLWQ-----LRDFRV--WEETNFALLVNViaTPSDGMYLRIDSDGRGISRSQAALI 147
Cdd:PRK12316 4426 RWAGQGGEALFdsllVFENYPVSEALQQgapggLRFGEVtnHEQTNYPLTLAV--GLGETLSLQFSYDRGHFDAATIERL 4503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 148 GATFVELLWRLAEHP------------DEAADFAFLAPRRDAASQPEPLVDvvSLFERQVEALPGSAALAFEEQRWTYRD 215
Cdd:PRK12316 4504 ARHLTNLLEAMAEDPqrrlgelqllekAEQQRIVALWNRTDAGYPATRCVH--QLVAERARMTPDAVAVVFDEEKLTYAE 4581
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 216 LDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAqpfRVVAHPEHAHV 295
Cdd:PRK12316 4582 LNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDS---GAALLLTQSHL 4658
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 296 AAAervLPVEELVA--DIEPE------TFAAPQL----DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPG 363
Cdd:PRK12316 4659 LQR---LPIPDGLAslALDRDedwegfPAHDPAVrlhpDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPD 4735
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 364 LRTLQFAPLSFDMAFQEIFSTLCGGGELqLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGvRPGALRV 443
Cdd:PRK12316 4736 DRVLQFMSFSFDGSHEGLYHPLINGASV-VIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDG-EPPSLRV 4813
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 444 VVSSGEQLRITEDVRAFCAAMPGLLLeNQYGPTETHQVTYH--SLSGDPAHyPDLPPIGRPLDGVEVQVLDAALRPVPVG 521
Cdd:PRK12316 4814 YCFGGEAVAQASYDLAWRALKPVYLF-NGYGPTETTVTVLLwkARDGDACG-AAYMPIGTPLGNRSGYVLDGQLNPLPVG 4891
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 522 VTGELYFGGDCLARGYHRAPELTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElAI 600
Cdd:PRK12316 4892 VAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIE-AR 4970
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 601 MRQaerQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDL--------AELKQALRSELPEHMVPAHFAWVDGFALTPSG 672
Cdd:PRK12316 4971 LRE---HPAVREAVVIAQEGAVGKQLVGYVVPQDPALADAdeaqaelrDELKAALRERLPEYMVPAHLVFLARMPLTPNG 5047
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 673 KRDDAALRALPLEHGTNIeYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAAL 752
Cdd:PRK12316 5048 KLDRKALPQPDASLLQQA-YVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLREL 5126
|
810 820
....*....|....*....|...
gi 1395399044 753 IETPTVEGLAERLRERSAVRAFD 775
Cdd:PRK12316 5127 FQTPTLAAFVELAAAAGSGDDEK 5149
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
199-679 |
8.80e-118 |
|
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes phosphinothricin tripeptide (PTT, phosphinothricylalanylalanine) synthetase, where PTT is a natural-product antibiotic and potent herbicide that is produced by Streptomyces hygroscopicus. This adenylation domain has been confirmed to directly activate beta-tyrosine, and fluorinated chondramides are produced through precursor-directed biosynthesis. Also included in this family is chondramide synthase D (also known as ATP-dependent phenylalanine adenylase or phenylalanine activase or tyrosine activase). Chondramides A-D are depsipeptide antitumor and antifungal antibiotics produced by C. crocatus, are a class of mixed peptide/polyketide depsipeptides comprised of three amino acids (alanine, N-methyltryptophan, plus the unusual amino acid beta-tyrosine or alpha-methoxy-beta-tyrosine) and a polyketide chain ([E]-7-hydroxy-2,4,6-trimethyloct-4-enoic acid).
Pssm-ID: 341307 [Multi-domain] Cd Length: 436 Bit Score: 369.66 E-value: 8.80e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 278
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 279 ETAQPFRVVAHPEHahvaaaervlpveelvadiepetfaapqldeLAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVA 358
Cdd:cd17652 81 ADARPALLLTTPDN-------------------------------LAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAF 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 359 SGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNAlgvrp 438
Cdd:cd17652 130 DVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLP----- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 439 gALRVVVSSGEQLRiTEDVRAFCaamPGLLLENQYGPTEThqvTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPV 518
Cdd:cd17652 205 -DLRTLVVAGEACP-AELVDRWA---PGRRMINAYGPTET---TVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 519 PVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWR-PGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE 597
Cdd:cd17652 277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGaPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 598 LAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEP-EAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDD 676
Cdd:cd17652 357 AAL----TEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPgAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432
|
...
gi 1395399044 677 AAL 679
Cdd:cd17652 433 RAL 435
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
199-679 |
1.42e-117 |
|
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: 370.65 E-value: 1.42e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 278
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 279 ETAQPFRVVAHPEHAHVAAAER--VLPVEELVADIEPETF-AAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQL 355
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLSFNKstILLEDPSISQEDTSNIdYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFER 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 356 RVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALG 435
Cdd:cd17656 162 EKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFIN 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 436 VRPGALRVVVSSGEQLRITEDVRAFCAAMpGLLLENQYGPTETHQVTYHSLSGDPaHYPDLPPIGRPLDGVEVQVLDAAL 515
Cdd:cd17656 242 RFPTCVKHIITAGEQLVITNEFKEMLHEH-NVHLHNHYGPSETHVVTTYTINPEA-EIPELPPIGKPISNTWIYILDQEQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 516 RPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAE 595
Cdd:cd17656 320 QLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 596 VELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEpEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 675
Cdd:cd17656 400 IEAQLL----NHPGVSEAVVLDKADDKGEKYLCAYFVME-QELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVD 474
|
....
gi 1395399044 676 DAAL 679
Cdd:cd17656 475 RKAL 478
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
199-680 |
1.79e-117 |
|
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes pyoverdine biosynthesis protein PvdJ involved in the synthesis of pyoverdine, which consists of a chromophore group attached to a variable peptide chain and comprises around 6-12 amino acids that are specific for each Pseudomonas species, and for which the peptide might be first synthesized before the chromophore assembly. Also included is ornibactin biosynthesis protein OrbI; ornibactin is a tetrapeptide siderophore with an l-ornithine-d-hydroxyaspartate-l-serine-l-ornithine backbone. The adenylation domain at the N-terminal of OrbI possibly initiates the ornibactin with the binding of N5-hydroxyornithine. 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: 341304 [Multi-domain] Cd Length: 450 Bit Score: 369.39 E-value: 1.79e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 278
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 279 ETAQPFRVVAHpehahvaaaervlpveelvadiEPETfaapqldeLAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVA 358
Cdd:cd17649 81 EDSGAGLLLTH----------------------HPRQ--------LAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERY 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 359 SGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVR- 437
Cdd:cd17649 131 GLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRTGDGr 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 438 PGALRVVVSSGEQLRItEDVRAFCAAmpGLLLENQYGPTET--HQVTYHSLSGDPAHYPDLPpIGRPLDGVEVQVLDAAL 515
Cdd:cd17649 211 PPSLRLYIFGGEALSP-ELLRRWLKA--PVRLFNAYGPTEAtvTPLVWKCEAGAARAGASMP-IGRPLGGRSAYILDADL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 516 RPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPA 594
Cdd:cd17649 287 NPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 595 EVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEPE--AVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSG 672
Cdd:cd17649 367 EIEAALL----EHPGVREAAVVALDGAGGKQLVAYVVLRAAAaqPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPNG 442
|
....*...
gi 1395399044 673 KRDDAALR 680
Cdd:cd17649 443 KLDRKALP 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
146-765 |
7.76e-116 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 395.68 E-value: 7.76e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 146 LIGATFVEllwRLAEHPDEAADFAFLAPRR--------DAASQPEPLVD------------VVSLFERQVEALPGSAALA 205
Cdd:PRK12467 456 LFEATTIE---RLATHWRNLLEAIVAEPRRrlgelpllDAEERARELVRwnapateyapdcVHQLIEAQARQHPERPALV 532
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 206 FEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFR 285
Cdd:PRK12467 533 FGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRL 612
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 286 VVAHPEHAH---VAAAERVLPVEELVADIE--PETFAAPQLD--ELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVA 358
Cdd:PRK12467 613 LLTQSHLLAqlpVPAGLRSLCLDEPADLLCgySGHNPEVALDpdNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERL 692
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 359 SGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRP 438
Cdd:PRK12467 693 QLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQASRVALPRP 772
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 439 gaLRVVVSSGEQLRITEDVRAFcAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLPpIGRPLDGVEVQVLDAALRP 517
Cdd:PRK12467 773 --QRALVCGGEALQVDLLARVR-ALGPGARLINHYGPTETTvGVSTYELSDEERDFGNVP-IGQPLANLGLYILDHYLNP 848
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 518 VPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRP-GARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEV 596
Cdd:PRK12467 849 VPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEI 928
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 597 ELAIMrqaeRQPGLRGAAVVARERQGnDAFLAAFLL------GEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTP 670
Cdd:PRK12467 929 EARLL----AQPGVREAVVLAQPGDA-GLQLVAYLVpaavadGAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTP 1003
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 671 SGKRDdaaLRALPLEHGTNIE--YLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLP 748
Cdd:PRK12467 1004 NGKLD---RKALPKPDASAVQatFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVP 1080
|
650
....*....|....*..
gi 1395399044 749 MAALIETPTVEGLAERL 765
Cdd:PRK12467 1081 LRTLFEHQTLAGFAQAV 1097
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
190-683 |
1.01e-115 |
|
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: 366.27 E-value: 1.01e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 269
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 270 PAQRLALILETAQPFRVVAHPEHAH-VAAAERVLPVEELVADIEPETFAAP--QLDELAMLLFTSGSTGRPKGVELSHRM 346
Cdd:cd17655 82 PEERIQYILEDSGADILLTQSHLQPpIAFIGLIDLLDEDTIYHEESENLEPvsKSDDLAYVIYTSGSTGKPKGVMIEHRG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 347 WANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQR 426
Cdd:cd17655 162 VVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 427 LAEASNALGVRpgaLRVVVSSGEQL------RITEDVRAFCAampgllLENQYGPTETH-QVTYHSLSGDPAHYPDlPPI 499
Cdd:cd17655 242 LDAADDSEGLS---LKHLIVGGEALstelakKIIELFGTNPT------ITNAYGPTETTvDASIYQYEPETDQQVS-VPI 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 500 GRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGR 579
Cdd:cd17655 312 GKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 580 ADTQVKVRGFRIEPAEVElAIMRQAerqPGLRGAAVVARERQGNDAFLAAFLLGEPEAvDLAELKQALRSELPEHMVPAH 659
Cdd:cd17655 392 IDHQVKIRGYRIELGEIE-ARLLQH---PDIKEAVVIARKDEQGQNYLCAYIVSEKEL-PVAQLREFLARELPDYMIPSY 466
|
490 500
....*....|....*....|....
gi 1395399044 660 FAWVDGFALTPSGKRDdaaLRALP 683
Cdd:cd17655 467 FIKLDEIPLTPNGKVD---RKALP 487
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
190-679 |
1.91e-113 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene cluster from Streptomyces lavendulae; 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 saframycin A gene cluster from Streptomyces lavendulae which implicates the NRPS system for assembling the unusual tetrapeptidyl skeleton in an iterative manner. It also includes saframycin Mx1 produced by Myxococcus xanthus NRPS.
Pssm-ID: 341280 [Multi-domain] Cd Length: 447 Bit Score: 358.55 E-value: 1.91e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 269
Cdd:cd12115 4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 270 PAQRLALILETAQPFRVVAHPEHahvaaaervlpveelvadiepetfaapqldeLAMLLFTSGSTGRPKGVELSHRMWAN 349
Cdd:cd12115 84 PPERLRFILEDAQARLVLTDPDD-------------------------------LAYVIYTSGSTGRPKGVAIEHRNAAA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 350 YTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNrermdpsaLLHVLERRQVQRVLL----PFVALQ 425
Cdd:cd12115 133 FLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADN--------VLALPDLPAAAEVTLintvPSAAAE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 426 RLAeasnaLGVRPGALRVVVSSGEQLRiTEDVRAFCAAMPGLLLENQYGPTEThqVTYHSLSGDPAHYPDLPPIGRPLDG 505
Cdd:cd12115 205 LLR-----HDALPASVRVVNLAGEPLP-RDLVQRLYARLQVERVVNLYGPSED--TTYSTVAPVPPGASGEVSIGRPLAN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 506 VEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVK 585
Cdd:cd12115 277 TQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVK 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 586 VRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEP-EAVDLAELKQALRSELPEHMVPAHFAWVD 664
Cdd:cd12115 357 VRGFRIELGEIEAAL----RSIPGVREAVVVAIGDAAGERRLVAYIVAEPgAAGLVEDLRRHLGTRLPAYMVPSRFVRLD 432
|
490
....*....|....*
gi 1395399044 665 GFALTPSGKRDDAAL 679
Cdd:cd12115 433 ALPLTPNGKIDRSAL 447
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-793 |
3.29e-113 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 388.16 E-value: 3.29e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 1 AHCLTLHLFSRSDSVVTGAISNGRP-ELPDADRMVGLFLNTVPV----RSEIAGHSWIEVADALFRQERDghaHRRYPLS 75
Cdd:PRK12316 1798 AWLLLLQRYTGQETVAFGATVAGRPaELPGIEQQIGLFINTLPViaapRPDQSVADWLQEVQALNLALRE---HEHTPLY 1874
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 76 AIQQIVGDELSSAFN----YVNLHVLEPLWQ-----LRDFRV--WEETNFALLVNViaTPSDGMYLRIDSDGRGISRSQA 144
Cdd:PRK12316 1875 DIQRWAGQGGEALFDsllvFENYPVAEALKQgapagLVFGRVsnHEQTNYPLTLAV--TLGETLSLQYSYDRGHFDAAAI 1952
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 145 ALIGATFVELLWRLAEHPD---------EAADFAFLAPRRDAASQPEPL-VDVVSLFERQVEALPGSAALAFEEQRWTYR 214
Cdd:PRK12316 1953 ERLDRHLLHLLEQMAEDAQaalgelallDAGERQRILADWDRTPEAYPRgPGVHQRIAEQAARAPEAIAVVFGDQHLSYA 2032
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 215 DLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHP---E 291
Cdd:PRK12316 2033 ELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRhllE 2112
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 292 HAHVAAAERVLPVEElVADIE--PETFAAPQLDE--LAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTL 367
Cdd:PRK12316 2113 RLPLPAGVARLPLDR-DAEWAdyPDTAPAVQLAGenLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCEL 2191
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 368 QFAPLSFDMAFQEIFSTLCGGGELqLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGvRPGALRVVVSS 447
Cdd:PRK12316 2192 QFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDG-RPPAVRVYCFG 2269
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 448 GEQLRiTEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGEL 526
Cdd:PRK12316 2270 GEAVP-AASLRLAWEALRPVYLFNGYGPTEAVvTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGEL 2348
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 527 YFGGDCLARGYHRAPELTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAE 605
Cdd:PRK12316 2349 YLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIE----ARLQ 2424
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 606 RQPGLRGAAVVARERQGNDAfLAAFLLGEPEAVDLA-ELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRAlPL 684
Cdd:PRK12316 2425 AHPAVREAVVVAQDGASGKQ-LVAYVVPDDAAEDLLaELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPK-PD 2502
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 685 EHGTNIEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAER 764
Cdd:PRK12316 2503 VSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAAS 2582
|
810 820
....*....|....*....|....*....
gi 1395399044 765 LRERSAVRAFDPLVPIRAggsrPPLFLVH 793
Cdd:PRK12316 2583 LESGQTSRAPVLQKVTRV----QPLPLSH 2607
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
199-679 |
5.40e-113 |
|
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: 358.14 E-value: 5.40e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 278
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 279 ETAQPFRVVAHPEHAHVAAAErvLPVEELVADIEPETFAAPQ----LDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQ 354
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAG--LPVLLLALAAAAAAPAAPRtpvsPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 355 LRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVqrvllpfvalqrlaeasNAL 434
Cdd:cd12116 159 RERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSI-----------------TVM 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 435 GVRPGALRVVVSSGEQLRitEDVRAFC---AAMPGLL---------LENQYGPTETH-QVTYHSLSGDPAHypdlPPIGR 501
Cdd:cd12116 222 QATPATWRMLLDAGWQGR--AGLTALCggeALPPDLAarllsrvgsLWNLYGPTETTiWSTAARVTAAAGP----IPIGR 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 502 PLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWR-PGARLYRTGDLGRILGNGEIVWLGRA 580
Cdd:cd12116 296 PLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 581 DTQVKVRGFRIEPAEVElAIMRqaeRQPGLRGAAVVARErQGNDAFLAAFL-LGEPEAVDLAELKQALRSELPEHMVPAH 659
Cdd:cd12116 376 DGQVKIRGHRIELGEIE-AALA---AHPGVAQAAVVVRE-DGGDRRLVAYVvLKAGAAPDAAALRAHLRATLPAYMVPSA 450
|
490 500
....*....|....*....|
gi 1395399044 660 FAWVDGFALTPSGKRDDAAL 679
Cdd:cd12116 451 FVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
199-679 |
3.51e-110 |
|
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: 350.07 E-value: 3.51e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 278
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 279 ETAQPFRVVAHPEHahvaaaervlpveelvadiepetfaapqldeLAMLLFTSGSTGRPKGVELSHR-----MWAnyTQW 353
Cdd:cd17643 81 ADSGPSLLLTDPDD-------------------------------LAYVIYTSGSTGRPKGVVVSHAnvlalFAA--TQR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 354 QLRVAsgvPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQrVL--LPfVALQRLAEAS 431
Cdd:cd17643 128 WFGFN---EDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVT-VLnqTP-SAFYQLVEAA 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 432 NALGVRPGALRVVVSSGEQLRITEdVRAFCAAM--PGLLLENQYGPTET--HqVTYHSLSGDPAHYPDLPPIGRPLDGVE 507
Cdd:cd17643 203 DRDGRDPLALRYVIFGGEALEAAM-LRPWAGRFglDRPQLVNMYGITETtvH-VTFRPLDAADLPAAAASPIGRPLPGLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 508 VQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKV 586
Cdd:cd17643 281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFgGPGSRMYRTGDLARRLPDGELEYLGRADEQVKI 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 587 RGFRIEPAEVELAIMrqaeRQPGLRGAAVVARE-RQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDG 665
Cdd:cd17643 361 RGFRIELGEIEAALA----THPSVRDAAVIVREdEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDA 436
|
490
....*....|....
gi 1395399044 666 FALTPSGKRDDAAL 679
Cdd:cd17643 437 LPLTVNGKLDRAAL 450
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
190-683 |
1.07e-109 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. 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: 341299 [Multi-domain] Cd Length: 465 Bit Score: 349.43 E-value: 1.07e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 269
Cdd:cd17644 5 LFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 270 PAQRLALILETAQPFRVVAHPEHahvaaaervlpveelvadiepetfaapqldeLAMLLFTSGSTGRPKGVELSHRMWAN 349
Cdd:cd17644 85 PQERLTYILEDAQISVLLTQPEN-------------------------------LAYVIYTSGSTGKPKGVMIEHQSLVN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 350 YTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLA- 428
Cdd:cd17644 134 LSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLVl 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 429 EASNALGVRPGALRVVVSSGEqlRITEDVRAFCAAMPGLLLE--NQYGPTE-THQVTYHSLSGDPAHYPDLPPIGRPLDG 505
Cdd:cd17644 214 ELLLSTIDLPSSLRLVIVGGE--AVQPELVRQWQKNVGNFIQliNVYGPTEaTIAATVCRLTQLTERNITSVPIGRPIAN 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 506 VEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWR--PGARLYRTGDLGRILGNGEIVWLGRADTQ 583
Cdd:cd17644 292 TQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEYLGRIDNQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 584 VKVRGFRIEPAEVElAIMRQaerQPGLRGAAVVARERQGNDAFLAAFLLGE-PEAVDLAELKQALRSELPEHMVPAHFAW 662
Cdd:cd17644 372 VKIRGFRIELGEIE-AVLSQ---HNDVKTAVVIVREDQPGNKRLVAYIVPHyEESPSTVELRQFLKAKLPDYMIPSAFVV 447
|
490 500
....*....|....*....|.
gi 1395399044 663 VDGFALTPSGKRDDaalRALP 683
Cdd:cd17644 448 LEELPLTPNGKIDR---RALP 465
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
157-773 |
2.22e-106 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 367.75 E-value: 2.22e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 157 RLAEHPD-EAADFAFLAPRRDAASQPEPLV-DVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARR 234
Cdd:PRK12316 481 RVDELPMlDAEERGQLVEGWNATAAEYPLQrGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGP 560
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 235 GDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQpFRVVAHPEHAH----VAAAERVLPVEELVAD 310
Cdd:PRK12316 561 DVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSG-VQLLLSQSHLGrklpLAAGVQVLDLDRPAAW 639
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 311 IEPETFAAPQL----DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLC 386
Cdd:PRK12316 640 LEGYSEENPGTelnpENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLM 719
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 387 GGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPgaLRVVVSSGEQLRITEDVRAFcAAMPG 466
Cdd:PRK12316 720 SGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVASCTS--LRRIVCSGEALPADAQEQVF-AKLPQ 796
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 467 LLLENQYGPTE-THQVTYHSLSGDPAhypDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTA 545
Cdd:PRK12316 797 AGLYNLYGPTEaAIDVTHWTCVEEGG---DSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTA 873
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 546 ERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGnda 625
Cdd:PRK12316 874 ERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLL----EHPWVREAAVLAVDGKQ--- 946
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 626 fLAAFLLGEPEAVDLAE-LKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDaalRALPLEHGTNI--EYLAPRDDYERT 702
Cdd:PRK12316 947 -LVGYVVLESEGGDWREaLKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR---KALPAPEASVAqqGYVAPRNALERT 1022
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395399044 703 LAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRfMLLIEKRYGVDLPMAALIETPTVEGLAERLRERSAVRA 773
Cdd:PRK12316 1023 LAAIWQDVLGVERVGLDDNFFELGGDSIVSIQ-VVSRARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAA 1092
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
190-782 |
6.95e-105 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 362.94 E-value: 6.95e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 269
Cdd:PRK12467 1579 LIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEY 1658
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 270 PAQRLALILETAQPFRVVAHPEHAH---VAAAERVLPVEELVADIEPETFAAPQL----DELAMLLFTSGSTGRPKGVEL 342
Cdd:PRK12467 1659 PRERLAYMIEDSGIELLLTQSHLQArlpLPDGLRSLVLDQEDDWLEGYSDSNPAVnlapQNLAYVIYTSGSTGRPKGAGN 1738
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 343 SHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFV 422
Cdd:PRK12467 1739 RHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPS 1818
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 423 ALQRLAEASNALGvRPGALRVVVSSGEQLRItEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLPPIGR 501
Cdd:PRK12467 1819 MLQQLLQMDEQVE-HPLSLRRVVCGGEALEV-EALRPWLERLPDTGLFNLYGPTETAvDVTHWTCRRKDLEGRDSVPIGQ 1896
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 502 PLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRA 580
Cdd:PRK12467 1897 PIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRI 1976
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 581 DTQVKVRGFRIEPAEVElAIMRQaerQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDL--------AELKQALRSELP 652
Cdd:PRK12467 1977 DHQVKIRGFRIELGEIE-ARLRE---QGGVREAVVIAQDGANGKQLVAYVVPTDPGLVDDdeaqvalrAILKNHLKASLP 2052
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 653 EHMVPAHFAWVDGFALTPSGKRDDAALRALP---LEHGtnieYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTS 729
Cdd:PRK12467 2053 EYMVPAHLVFLARMPLTPNGKLDRKALPAPDaseLQQA----YVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDS 2128
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395399044 730 LSAMRfMLLIEKRYGVDLPMAALIETPTVEGLAERLRE--------RSAVRAFDPLVPIRA 782
Cdd:PRK12467 2129 IISIQ-VVSRARQAGIRFTPKDLFQHQTVQSLAAVAQEgdgtvsidQGPVTGDLPLLPIQQ 2188
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
187-682 |
7.57e-102 |
|
The adenylation (A) domain of siderophore-synthesizing 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 to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. 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: 341242 [Multi-domain] Cd Length: 481 Bit Score: 328.73 E-value: 7.57e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 187 VVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 266
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 267 VSYPAQRLALILETAQpfrvvahpehAHVAAAErvlpveelvadiepetfaapQLDELAMLLFTSGSTGRPKGVELSHRM 346
Cdd:cd05918 81 PSHPLQRLQEILQDTG----------AKVVLTS--------------------SPSDAAYVIFTSGSTGKPKGVVIEHRA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 347 WANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDpsALLHVLERRQVQRVLL-PFVAlq 425
Cdd:cd05918 131 LSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLtPSVA-- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 426 RLaeasnalgVRPGA---LRVVVSSGEQLRiTEDVRAFCaamPGLLLENQYGPTEThqvTYHSLSGDPAHYPDLPPIGRP 502
Cdd:cd05918 207 RL--------LDPEDvpsLRTLVLGGEALT-QSDVDTWA---DRVRLINAYGPAEC---TIAATVSPVVPSTDPRNIGRP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 503 LDGVeVQVLDAA--LRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHP-WR------PGARLYRTGDLGRILGNGE 573
Cdd:cd05918 272 LGAT-CWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPaWLkqegsgRGRRLYRTGDLVRYNPDGS 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 574 IVWLGRADTQVKVRGFRIEPAEVELAImRQAERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVD-------------- 639
Cdd:cd05918 351 LEYVGRKDTQVKIRGQRVELGEIEHHL-RQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGsgdgdslflepsde 429
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1395399044 640 ----LAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRAL 682
Cdd:cd05918 430 fralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRALREL 476
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
199-679 |
2.02e-101 |
|
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: 327.69 E-value: 2.02e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 278
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 279 ETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPETFAA--PQLDELAMLLFTSGSTGRPKGVELSHRMWANY-----T 351
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPvdVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTildinR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 352 QWQLRvasgvPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVqrVLLPFVA--LQRLAE 429
Cdd:cd12114 161 RFAVG-----PDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGV--TLWNSVPalLEMLLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 430 ASNALGVRPGALRVVVSSGEqlRITEDV-RAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAHYPDLpPIGRPLDGVE 507
Cdd:cd12114 234 VLEAAQALLPSLRLVLLSGD--WIPLDLpARLRALAPDARLISLGGATEASiWSIYHPIDEVPPDWRSI-PYGRPLANQR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 508 VQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPwrPGARLYRTGDLGRILGNGEIVWLGRADTQVKVR 587
Cdd:cd12114 311 YRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 588 GFRIEPAEVElaimRQAERQPGLRGAAVVAReRQGNDAFLAAFLLGEPEA--VDLAELKQALRSELPEHMVPAHFAWVDG 665
Cdd:cd12114 389 GYRIELGEIE----AALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGtpIAPDALRAFLAQTLPAYMIPSRVIALEA 463
|
490
....*....|....
gi 1395399044 666 FALTPSGKRDDAAL 679
Cdd:cd12114 464 LPLTANGKVDRAAL 477
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
195-679 |
7.03e-99 |
|
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: 319.96 E-value: 7.03e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 195 VEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRL 274
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 275 ALILETAQPFRVVAHPehahvaaaervlpveelvadiepetfaapqlDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQ 354
Cdd:cd05945 81 REILDAAKPALLIADG-------------------------------DDNAYIIFTSGSTGRPKGVQISHDNLVSFTNWM 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 355 LRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVL-LP-FVALQRLAEASN 432
Cdd:cd05945 130 LSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVsTPsFAAMCLLSPTFT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 433 ALGVrpGALRVVVSSGEQLRItEDVRAFCAAMPGLLLENQYGPTE-THQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVL 511
Cdd:cd05945 210 PESL--PSLRHFLFCGEVLPH-KTARALQQRFPDARIYNTYGPTEaTVAVTYIEVTPEVLDGYDRLPIGYAKPGAKLVIL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 512 DAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHpwrPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRI 591
Cdd:cd05945 287 DEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPD---EGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 592 EPAEVElaimRQAERQPGLRGAAVVARERQGNDAFLAAFLLGEP--EAVDLAELKQALRSELPEHMVPAHFAWVDGFALT 669
Cdd:cd05945 364 ELEEIE----AALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPgaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLN 439
|
490
....*....|
gi 1395399044 670 PSGKRDDAAL 679
Cdd:cd05945 440 ANGKIDRKAL 449
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-781 |
1.59e-98 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 344.25 E-value: 1.59e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 4 LTLHLFSRSDSVVTGAISNGRpELPDADRMVGLFLNTVPVRSEI-AGHSWIEVADALFRQERDGHAHRRYPL----SAIQ 78
Cdd:PRK12316 2855 VLLHRYSGQSDIRVGVPIANR-NRAETERLIGFFVNTQVLRAQVdAQLAFRDLLGQVKEQALGAQAHQDLPFeqlvEALQ 2933
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 79 QIVGDELSSAFNYVNLH--------VLEPLWQLRDFRVWEETNFALLVNVIATPsDGMYLRIDSDGRGISRSQAALIGAT 150
Cdd:PRK12316 2934 PERSLSHSPLFQVMYNHqsgeraaaQLPGLHIESFAWDGAATQFDLALDTWESA-EGLGASLTYATDLFDARTVERLARH 3012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 151 FVELLWRLAEHPDEAADFAFL-----------APRRDAASQPEPLvDVVSLFERQVEALPGSAALAFEEQRWTYRDLDHV 219
Cdd:PRK12316 3013 WQNLLRGMVENPQRSVDELAMldaeergqlleAWNATAAEYPLER-GVHRLFEEQVERTPDAVALAFGEQRLSYAELNRR 3091
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 220 ARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILET--AQPFRVVAHPEHAHVAA 297
Cdd:PRK12316 3092 ANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDsgAQLLLSQSHLRLPLAQG 3171
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 298 AERVL--PVEELVADIEPETFAAPQldELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFD 375
Cdd:PRK12316 3172 VQVLDldRGDENYAEANPAIRTMPE--NLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFD 3249
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 376 MAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQrvLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRITE 455
Cdd:PRK12316 3250 VFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVD--VLHAYPSMLQAFLEEEDAHRCTSLKRIVCGGEALPADL 3327
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 456 DVRAFCaampGLLLENQYGPTETHQVTYHSLSGDPahYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLAR 535
Cdd:PRK12316 3328 QQQVFA----GLPLYNLYGPTEATITVTHWQCVEE--GKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLAR 3401
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 536 GYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElAIMRQaerQPGLRGAAV 615
Cdd:PRK12316 3402 GYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE-ARLLE---HPWVREAVV 3477
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 616 VARERQGndafLAAFLLGEPEAVDLAE-LKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRAlPLEHGTNIEYLA 694
Cdd:PRK12316 3478 LAVDGRQ----LVAYVVPEDEAGDLREaLKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR-PDAALLQQDYVA 3552
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 695 PRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIeKRYGVDLPMAALIETPTVEGLAERLR-------E 767
Cdd:PRK12316 3553 PVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRA-RQAGIRFTPKDLFQHQTIQGLARVARvgggvavD 3631
|
810
....*....|....
gi 1395399044 768 RSAVRAFDPLVPIR 781
Cdd:PRK12316 3632 QGPVSGETLLLPIQ 3645
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
199-679 |
1.15e-97 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. 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: 341305 [Multi-domain] Cd Length: 447 Bit Score: 316.72 E-value: 1.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 278
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 279 ETAqpfrvvahpehahvaAAERVLpveelvadIEPEtfaapqldELAMLLFTSGSTGRPKGVELSHRMWAN-YTQWQLRV 357
Cdd:cd17650 81 EDS---------------GAKLLL--------TQPE--------DLAYVIYTSGTTGKPKGVMVEHRNVAHaAHAWRREY 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 358 ASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQ-RVLLPFVALQRLAEASNAlGV 436
Cdd:cd17650 130 ELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITlMESTPALIRPVMAYVYRN-GL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 437 RPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQYGPTE-THQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAAL 515
Cdd:cd17650 209 DLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEaTIDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVLDERL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 516 RPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAE 595
Cdd:cd17650 289 QPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGE 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 596 VELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEpEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 675
Cdd:cd17650 369 IESQLA----RHPAIDEAVVAVREDKGGEARLCAYVVAA-ATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVD 443
|
....
gi 1395399044 676 DAAL 679
Cdd:cd17650 444 RRAL 447
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
151-793 |
1.15e-97 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 341.38 E-value: 1.15e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 151 FVELLWRLAEHPDEA-ADFAFL-APRR------DAASQPEPLVDVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARC 222
Cdd:PRK05691 1089 FLALLEQVCEDPQRAlGDVQLLdAAERaqlaqwGQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANR 1168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 223 VATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAH---PEHAHVAAAE 299
Cdd:PRK05691 1169 LAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQshlLERLPQAEGV 1248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 300 RVLPVEELVADIEPETfaAPQL----DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFD 375
Cdd:PRK05691 1249 SAIALDSLHLDSWPSQ--APGLhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFD 1326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 376 MAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVqrVLLPFVA--LQRLAEASNALGVRpgALRVVVSSGEQLRi 453
Cdd:PRK05691 1327 VSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGV--TTLHFVPplLQLFIDEPLAAACT--SLRRLFSGGEALP- 1401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 454 TEDVRAFCAAMPGLLLENQYGPTETH-QVTYHSLSGDPAhypDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDC 532
Cdd:PRK05691 1402 AELRNRVLQRLPQVQLHNRYGPTETAiNVTHWQCQAEDG---ERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAG 1478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 533 LARGYHRAPELTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLR 611
Cdd:PRK05691 1479 LARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLL----AQPGVA 1554
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 612 GAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDaalRALPLEHGTNIE 691
Cdd:PRK05691 1555 QAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDR---RALPEPVWQQRE 1631
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 692 YLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLRERSAV 771
Cdd:PRK05691 1632 HVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAA 1711
|
650 660
....*....|....*....|..
gi 1395399044 772 RAFDPLVPIRAGGSRPPLFLVH 793
Cdd:PRK05691 1712 GERNSQGAIARVDRSQPVPLSY 1733
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
189-680 |
2.22e-96 |
|
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of nonribosomal peptide synthases (NRPS) gliotoxin biosynthesis protein P (GliP), thioclapurine biosynthesis protein P (tcpP) and Sirodesmin biosynthesis protein P (SirP). In the filamentous fungus Aspergillus fumigatus, NRPS GliP is involved in the biosynthesis of gliotoxin, which is initiated by the condensation of serine and phenylalanine. Studies show that GliP is not required for invasive aspergillosis, suggesting that the principal targets of gliotoxin are neutrophils or other phagocytes. SirP is a phytotoxin produced by the fungus Leptosphaeria maculans, which causes blackleg disease of canola (Brassica napus). In the fungus Claviceps purpurea, NRPS tcpP catalyzes condensation of tyrosine and glycine, part of biosynthesis of an unusual class of epipolythiodioxopiperazines (ETPs) that lacks the reactive thiol group for toxicity. 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: 341308 [Multi-domain] Cd Length: 433 Bit Score: 312.71 E-value: 2.22e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 189 SLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVS 268
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 269 YPAQRLALILETAQPFRVVAhpehahvaaaervlpveelvadiepetfaAPQLDELAMLLFTSGSTGRPKGVELSHRMWA 348
Cdd:cd17653 81 LPSARIQAILRTSGATLLLT-----------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPHRGVL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 349 NYTQW-QLRVASGvPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLisnRERMDPSAllHVLERRQVQRVLLPFVALQRL 427
Cdd:cd17653 132 NYVSQpPARLDVG-PGSRVAQVLSIAFDACIGEIFSTLCNGGTLVL---ADPSDPFA--HVARTVDALMSTPSILSTLSP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 428 AEASNalgvrpgaLRVVVSSGEqlritedvrafcAAMPGLL--------LENQYGPTE-THQVTYHSLsgdpahYPDLP- 497
Cdd:cd17653 206 QDFPN--------LKTIFLGGE------------AVPPSLLdrwspgrrLYNAYGPTEcTISSTMTEL------LPGQPv 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 498 PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWL 577
Cdd:cd17653 260 TIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 578 GRADTQVKVRGFRIEPAEVELAIMRQaerQPGLRGAAVVarerQGNDaFLAAFLLgePEAVDLAELKQALRSELPEHMVP 657
Cdd:cd17653 340 GREDNQVKVRGFRINLEEIEEVVLQS---QPEVTQAAAI----VVNG-RLVAFVT--PETVDVDGLRSELAKHLPSYAVP 409
|
490 500
....*....|....*....|...
gi 1395399044 658 AHFAWVDGFALTPSGKRDDAALR 680
Cdd:cd17653 410 DRIIALDSFPLTANGKVDRKALR 432
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
187-686 |
3.84e-96 |
|
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: 312.51 E-value: 3.84e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 187 VVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 266
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 267 VSYPAQRLALILETAQPfRVVahpehahVAAAervlpveelvadiepetfaapqldelamLLFTSGSTGRPKGVELSHRM 346
Cdd:COG0318 81 PRLTAEELAYILEDSGA-RAL-------VTAL----------------------------ILYTSGTTGRPKGVMLTHRN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 347 WANYTQWQLRVASGVPGLRTLQFAPLSFDMAF-QEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRVLLPFVALQ 425
Cdd:COG0318 125 LLANAAAIAAALGLTPGDVVLVALPLFHVFGLtVGLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGVPTMLA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 426 RLAEASNALGVRPGALRVVVSSGEQLRiTEDVRAFCAAMpGLLLENQYGPTETHQVTyhSLSGDPAHYPDLPPIGRPLDG 505
Cdd:COG0318 202 RLLRHPEFARYDLSSLRLVVSGGAPLP-PELLERFEERF-GVRIVEGYGLTETSPVV--TVNPEDPGERRPGSVGRPLPG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 506 VEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEhPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVK 585
Cdd:COG0318 278 VEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD-GW------LRTGDLGRLDEDGYLYIVGRKKDMII 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 586 VRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGnDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWV 663
Cdd:COG0318 351 SGGENVYPAEVEEVLA----AHPGVAEAAVVGVpdEKWG-ERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFV 425
|
490 500
....*....|....*....|...
gi 1395399044 664 DGFALTPSGKRDDAALRALPLEH 686
Cdd:COG0318 426 DELPRTASGKIDRRALRERYAAG 448
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
190-679 |
2.60e-94 |
|
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: 307.17 E-value: 2.60e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 269
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 270 PAQRLALILETAQPFRVVAHPehahvaaaervlpveelvadiepetfaapqlDELAMLLFTSGSTGRPKGVELSHRMWAN 349
Cdd:cd17645 83 PGERIAYMLADSSAKILLTNP-------------------------------DDLAYVIYTSGSTGLPKGVMIEHHNLVN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 350 YTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAE 429
Cdd:cd17645 132 LCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQFMQ 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 430 ASNAlgvrpgALRVVVSSGEQLRITEDvrafcaamPGLLLENQYGPTEtHQVTYHSLSGDPAHYPdlPPIGRPLDGVEVQ 509
Cdd:cd17645 212 LDNQ------SLRVLLTGGDKLKKIER--------KGYKLVNNYGPTE-NTVVATSFEIDKPYAN--IPIGKPIDNTRVY 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 510 VLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGF 589
Cdd:cd17645 275 ILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGY 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 590 RIEPAEVELAIMRQAERQPglrgAAVVARERQGNDAFLAAFLLGePEAVDLAELKQALRSELPEHMVPAHFAWVDGFALT 669
Cdd:cd17645 355 RIEPGEIEPFLMNHPLIEL----AAVLAKEDADGRKYLVAYVTA-PEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLT 429
|
490
....*....|
gi 1395399044 670 PSGKRDDAAL 679
Cdd:cd17645 430 ANGKVDRKAL 439
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
199-683 |
8.50e-89 |
|
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV synthetase (ACVS, EC 6.3.2.26; also known as N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase or delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase) is involved in medically important antibiotic biosynthesis. ACV synthetase is active in an early step in the penicillin G biosynthesis pathway which involves the formation of the tripeptide 6-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine (ACV); each of the constituent amino acids of the tripeptide ACV are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. ACV is then cyclized by the action of isopenicillin N synthase.
Pssm-ID: 341303 [Multi-domain] Cd Length: 453 Bit Score: 292.77 E-value: 8.50e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDA-IGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALI 277
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDDlVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 278 LETAQPFRVVAHPEhahvaaaervlpveelvadiepetfaapqldELAMLLFTSGSTGRPKGVELSHRMWANytqwqLRV 357
Cdd:cd17648 81 LEDTGARVVITNST-------------------------------DLAYAIYTSGTTGKPKGVLVEHGSVVN-----LRT 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 358 A-SGVPGLRT------LQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAea 430
Cdd:cd17648 125 SlSERYFGRDngdeavLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYD-- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 431 snaLGVRPgALRVVVSSGEQLriTEDV-RAFCAAMPGLLLeNQYGPTEThQVTYHSlSGDPAHYPDLPPIGRPLDGVEVQ 509
Cdd:cd17648 203 ---LARLP-HLKRVDAAGEEF--TAPVfEKLRSRFAGLII-NAYGPTET-TVTNHK-RFFPGDQRFDKSLGRPVRNTKCY 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 510 VLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRP--------GARLYRTGDLGRILGNGEIVWLGRAD 581
Cdd:cd17648 274 VLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTeqerargrNARLYKTGDLVRWLPSGELEYLGRND 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 582 TQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGN-----DAFLAAFLLGEPEAVDLAELKQALRSELPEHMV 656
Cdd:cd17648 354 FQVKIRGQRIEPGEVEAALA----SYPGVRECAVVAKEDASQaqsriQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMV 429
|
490 500
....*....|....*....|....*..
gi 1395399044 657 PAHFAWVDGFALTPSGKRDdaaLRALP 683
Cdd:cd17648 430 PARLVRLEGIPVTINGKLD---VRALP 453
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-766 |
1.87e-88 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 313.64 E-value: 1.87e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 1 AHCLTLHLFSRSDSVVTGAISNGRP-ELPDADRMVGLFLNTVPVRSEIAG-------HSWIEvadALFRQERDGHAHRRY 72
Cdd:PRK05691 3512 AWALVLRRYSGDRDVLFGVTVAGRPvSMPQMQRTVGLFINSIALRVQLPAagqrcsvRQWLQ---GLLDSNMELREYEYL 3588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 73 PLSAIQQIV----GDEL-SSAFNYVNLHV-LEPLWQLRDFRVWEE-----TNFALlvNVIATPSDGMYLRIDSDGRGISR 141
Cdd:PRK05691 3589 PLVAIQECSelpkGQPLfDSLFVFENAPVeVSVLDRAQSLNASSDsgrthTNFPL--TAVCYPGDDLGLHLSYDQRYFDA 3666
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 142 SQAALIGATFVELLWRLAEHPD-EAADFAFLAPRR-----DAASQPE---PL-VDVVSLFERQVEALPGSAALAFEEQRW 211
Cdd:PRK05691 3667 PTVERLLGEFKRLLLALVQGFHgDLSELPLLGEQErdfllDGCNRSErdyPLeQSYVRLFEAQVAAHPQRIAASCLDQQW 3746
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILE-TAQPFRVV--A 288
Cdd:PRK05691 3747 SYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIElSRTPVLVCsaA 3826
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 289 HPEHAHVAAAE-------RVLPVEEL----VADIEPETFAAPqlDELAMLLFTSGSTGRPKGVELSHR-MWANytqwQLr 356
Cdd:PRK05691 3827 CREQARALLDElgcanrpRLLVWEEVqageVASHNPGIYSGP--DNLAYVIYTSGSTGLPKGVMVEQRgMLNN----QL- 3899
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 357 vaSGVPGLR------TLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALL-HVLERRQVQRVLLPFVALQRLAE 429
Cdd:PRK05691 3900 --SKVPYLAlseadvIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLaHVQAQGITVLESVPSLIQGMLAE 3977
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 430 ASNALGvrpgALRVVVSSGEQLRiTEDVRAFCAAMPGLLLENQYGPTEThqvtyhslSGDPAHYP-DLP-------PIGR 501
Cdd:PRK05691 3978 DRQALD----GLRWMLPTGEAMP-PELARQWLQRYPQIGLVNAYGPAEC--------SDDVAFFRvDLAstrgsylPIGS 4044
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 502 PLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPW-RPGARLYRTGDLGRILGNGEIVWLGRA 580
Cdd:PRK05691 4045 PTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARRRSDGVLEYVGRI 4124
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 581 DTQVKVRGFRIEPAEVELAIMRQAErqpgLRGAAVVARERQgNDAFLAAFLLGEPEAVDLAEL----KQALRSELPEHMV 656
Cdd:PRK05691 4125 DHQVKIRGYRIELGEIEARLHEQAE----VREAAVAVQEGV-NGKHLVGYLVPHQTVLAQGALleriKQRLRAELPDYMV 4199
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 657 PAHFAWVDGFALTPSGKRDDAALRALPLEHGTNIEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFM 736
Cdd:PRK05691 4200 PLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIA 4279
|
810 820 830
....*....|....*....|....*....|
gi 1395399044 737 LLIEKRYGVDLPMAALIETPTVEGLAERLR 766
Cdd:PRK05691 4280 SRVQKALQRNVPLRAMFECSTVEELAEYIE 4309
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
191-587 |
1.24e-87 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 288.44 E-value: 1.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 191 FERQVEALPGSAALA-FEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 269
Cdd:pfam00501 1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 270 PAQRLALILETAQP--------FRVVAHPEHAHV--------------AAAERVLPVEELVADIEPETFAAPQLDELAML 327
Cdd:pfam00501 81 PAEELAYILEDSGAkvlitddaLKLEELLEALGKlevvklvlvldrdpVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 328 LFTSGSTGRPKGVELSHR--MWANYTQWQLRVASGV--PGLRTLQFAPLSFDMAFQ-EIFSTLCGGGELQLISNRERMDP 402
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRnlVANVLSIKRVRPRGFGlgPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 403 SALLHVLERRQVQrvLLPFV--ALQRLAEASNALGVRPGALRVVVSSGEQLRItEDVRAFCAAMPGLLLeNQYGPTETHQ 480
Cdd:pfam00501 241 AALLELIERYKVT--VLYGVptLLNMLLEAGAPKRALLSSLRLVLSGGAPLPP-ELARRFRELFGGALV-NGYGLTETTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 481 VTYHSLSGDPaHYPDLPPIGRPLDGVEVQVLDAA-LRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarl 559
Cdd:pfam00501 317 VVTTPLPLDE-DLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGW------ 389
|
410 420
....*....|....*....|....*...
gi 1395399044 560 YRTGDLGRILGNGEIVWLGRADTQVKVR 587
Cdd:pfam00501 390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
28-730 |
1.02e-75 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 275.12 E-value: 1.02e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 28 PDADRMVGLFLNTVPVRSEIAGHSwieVADALFRQER----DGHAHRRYPLSAIQQIVGDELSSAFNyvnlhvlePL--- 100
Cdd:PRK05691 2008 PESEGLIGAFLNTQVLRCQLDGQM---SVSELLEQVRqtviEGQSHQDLPFDHLVEALQPPRSAAYN--------PLfqv 2076
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 101 ------WQLRDFRVWEETNFALLVN-VIATPSDgMYLRI-DSDGR---------------GISRSQA---ALIGATFVEL 154
Cdd:PRK05691 2077 mcnvqrWEFQQSRQLAGMTVEYLVNdARATKFD-LNLEVtDLDGRlgccltysrdlfdepRIARMAEhwqNLLEALLGDP 2155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 155 LWRLAEHP--DEAADFAFLAPRRDAASQPEPLVDVVSLFERQVEALPGSAALAFEEQRWTYRDLDhvARcvATRLVRAGA 232
Cdd:PRK05691 2156 QQRLAELPllAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELD--AR--ANRLARALR 2231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 233 RRGDA----IGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAqpfRVVAHPEHAHVAAAERVLPV---- 304
Cdd:PRK05691 2232 ERGVGpqvrVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDS---GIGLLLSDRALFEALGELPAgvar 2308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 305 ----EELVA-----DIEPETFAAPQldELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFD 375
Cdd:PRK05691 2309 wcleDDAAAlaaysDAPLPFLSLPQ--HQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFD 2386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 376 MAFQEIFSTLCGGGELQLisnrermdpsallhvleRRQVQRVLLPFVALQRlAEASNALGVRPG---------------- 439
Cdd:PRK05691 2387 AASERLLVPLLCGARVVL-----------------RAQGQWGAEEICQLIR-EQQVSILGFTPSygsqlaqwlagqgeql 2448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 440 ALRVVVSSGEQLrITEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDpahypDLP------PIGRPLDGVEVQVLDA 513
Cdd:PRK05691 2449 PVRMCITGGEAL-TGEHLQRIRQAFAPQLFFNAYGPTETVVMPLACLAPE-----QLEegaasvPIGRVVGARVAYILDA 2522
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 514 ALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRP-GARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIE 592
Cdd:PRK05691 2523 DLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAdGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIE 2602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 593 PAEVELAIMrqaeRQPGLRGAAVVARERQGNDAfLAAFLLGEPEAVDLAE-------LKQALRSELPEHMVPAHFAWVDG 665
Cdd:PRK05691 2603 LGEIESRLL----EHPAVREAVVLALDTPSGKQ-LAGYLVSAVAGQDDEAqaalreaLKAHLKQQLPDYMVPAHLILLDS 2677
|
730 740 750 760 770 780
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395399044 666 FALTPSGKRDDAALRALPLEHGTNiEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSL 730
Cdd:PRK05691 2678 LPLTANGKLDRRALPAPDPELNRQ-AYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSI 2741
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
177-1056 |
4.96e-73 |
|
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442548 [Multi-domain] Cd Length: 855 Bit Score: 260.02 E-value: 4.96e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 177 AASQPEPLVDVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGIL 256
Cdd:COG3319 1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 257 RAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQLDELAMLLFTSGSTGR 336
Cdd:COG3319 81 LAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 337 PKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQR 416
Cdd:COG3319 161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 417 VLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLlenQYGPTETHQVTYHSLSGDPAHYPDL 496
Cdd:COG3319 241 LLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAG---GTATTAAVTTTAAAAAPGVAGALGP 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 497 PPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRPGARLYRTGDLGRILGNGEIVW 576
Cdd:COG3319 318 IGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 577 LGRADTQVKVRGFRIEPAEVELAimrqAERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMV 656
Cdd:COG3319 398 LGRLRLQRLRRGLREELEEAEAA----LAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLP 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 657 PAHFAWVDGFALTPSGKRDDAALRALPLEHGTniEYLAPRDDYERTLAGLLGELLDRPRVGIRDSFFDLGGTSLSAMRFM 736
Cdd:COG3319 474 PALLLLLLLLLLLLLAALLLAAAAPAAAAAAA--AAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLL 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 737 LLIEKRYGVDLPMAALIETPTVEGLAERLRERSAVRAFDPLVPIRAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVY 816
Cdd:COG3319 552 LLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALGPDRPVY 631
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 817 ALQAAGTGQGSTPLAVLEDIAASYLAAIRRVQPEGPYYLGGWSFGGFVAYEMARQLRALDpQAVAQLIVLDSITVDrnhA 896
Cdd:COG3319 632 GLQAPGLDGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQG-EEVALLVLLDSYAPG---A 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 897 GSASDEALLLFFYWELVWFERSDEEVEPLPEGASLEQKLDHIVERAIEAGvLPAGTPRATVQRLYELFRASWQALIGYRP 976
Cdd:COG3319 708 LARLDEAELLAALLRDLARGVDLPLDAEELRALDPEERLARLLERLREAG-LPAGLDAERLRRLLRVFRANLRALRRYRP 786
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 977 EVSDQDMTLLRADGPLPlalkpmhdaagTHYGDPKNGWQHWTSGRLDVIDVPGDHLVLMKEPYVETVAAEIAALLEPSTS 1056
Cdd:COG3319 787 RPYDGPVLLFRAEEDPP-----------GRADDPALGWRPLVAGGLEVHDVPGDHFSMLREPHVAELAAALRAALAAAEA 855
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
323-675 |
1.61e-62 |
|
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: 216.00 E-value: 1.61e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 323 ELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLisnRERMDP 402
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVL---LPKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 403 SALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRItEDVRAFcAAMPGLLLENQYGPTETHQVT 482
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPP-ELLERF-EEAPGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 483 yhSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEhpwrpgaRLYRT 562
Cdd:cd04433 156 --ATGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GWYRT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 563 GDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVAR--ERQGNDAFlAAFLLGEPEAVDL 640
Cdd:cd04433 227 GDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVL----LGHPGVAEAAVVGVpdPEWGERVV-AVVVLRPGADLDA 301
|
330 340 350
....*....|....*....|....*....|....*
gi 1395399044 641 AELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 675
Cdd:cd04433 302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
186-679 |
5.43e-59 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 211.54 E-value: 5.43e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 186 DVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPL 265
Cdd:TIGR01734 1 KLIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 266 DVSYPAQRLALILETAQP---FRVVAHPEHAHVAAAERVLPVEELVADIEPETFAAP-QLDELAMLLFTSGSTGRPKGVE 341
Cdd:TIGR01734 81 DTSIPSERIEMIIEAAGPelvIHTAELSIDAVGTQIITLSALEQAETSGGPVSFDHAvKGDDNYYIIYTSGSTGNPKGVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 342 LSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQR-VLLP 420
Cdd:TIGR01734 161 ISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVwVSTP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 421 -FVALQRLAEASNAlGVRPGALRVVVsSGEQLrITEDVRAFCAAMPGLLLENQYGPTE-THQVTYHSLSGDP-AHYPDLp 497
Cdd:TIGR01734 241 sFVDMCLLDPNFNQ-ENYPHLTHFLF-CGEEL-PVKTAKALLERFPKATIYNTYGPTEaTVAVTSVKITQEIlDQYPRL- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 498 PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHpwrPGARLYRTGDLGRIlGNGEIVWL 577
Cdd:TIGR01734 317 PIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH---EGQPAYRTGDAGTI-TDGQLFYQ 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 578 GRADTQVKVRGFRIEPAEVELAImRQAERqpgLRGAAVVAR-ERQGNDAFLAAFLLGEPEAVD-----LAELKQALRSEL 651
Cdd:TIGR01734 393 GRLDFQIKLHGYRIELEDIEFNL-RQSSY---IESAVVVPKyNKDHKVEYLIAAIVPETEDFEkefqlTKAIKKELKKSL 468
|
490 500
....*....|....*....|....*...
gi 1395399044 652 PEHMVPAHFAWVDGFALTPSGKRDDAAL 679
Cdd:TIGR01734 469 PAYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
187-680 |
1.95e-58 |
|
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: 208.57 E-value: 1.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 187 VVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 266
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 267 VSYPAQRLALILETAQpfrvvahpehahVAAAERVLPVEELVADIEPETF-AAPQLDELAMLLFTSGSTGRPKGVELSHR 345
Cdd:cd05936 81 PLYTPRELEHILNDSG------------AKALIVAVSFTDLLAAGAPLGErVALTPEDVAVLQYTSGTTGVPKGAMLTHR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 346 -MWANYTQWQLRVA-SGVPGLRTLQFAPL--SFDMAFQeIFSTLCGGGELQLISnreRMDPSALLHVLERRQVQrvLLP- 420
Cdd:cd05936 149 nLVANALQIKAWLEdLLEGDDVVLAALPLfhVFGLTVA-LLLPLALGATIVLIP---RFRPIGVLKEIRKHRVT--IFPg 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 421 ----FVAlqrLAEASNALGVRPGALRVVVSSGEQLRItEDVRAFCAAMPGLLLENqYGPTETHQVTyhslSGDPAHYPDL 496
Cdd:cd05936 223 vptmYIA---LLNAPEFKKRDFSSLRLCISGGAPLPV-EVAERFEELTGVPIVEG-YGLTETSPVV----AVNPLDGPRK 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 497 P-PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHpWrpgarlYRTGDLGRILGNGEIV 575
Cdd:cd05936 294 PgSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG-W------LRTGDIGYMDEDGYFF 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 576 WLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVA--RERQGnDAFLAAFLLGEPEAVDLAELKQALRSELPE 653
Cdd:cd05936 367 IVDRKKDMIIVGGFNVYPREVEEVLY----EHPAVAEAAVVGvpDPYSG-EAVKAFVVLKEGASLTEEEIIAFCREQLAG 441
|
490 500
....*....|....*....|....*..
gi 1395399044 654 HMVPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:cd05936 442 YKVPRQVEFRDELPKSAVGKILRRELR 468
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
186-679 |
1.41e-56 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 204.36 E-value: 1.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 186 DVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPL 265
Cdd:PRK04813 3 DIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 266 DVSYPAQRLALILETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPET---FAAP-QLDELAMLLFTSGSTGRPKGVE 341
Cdd:PRK04813 83 DVSSPAERIEMIIEVAKPSLIIATEELPLEILGIPVITLDELKDIFATGNpydFDHAvKGDDNYYIIFTSGTTGKPKGVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 342 LSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQR-VLLP 420
Cdd:PRK04813 163 ISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVwVSTP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 421 -FVALQRLAEASNAlgVRPGALRVVVSSGEQLRITEdVRAFCAAMPGLLLENQYGPTETH------QVTYHSLsgdpAHY 493
Cdd:PRK04813 243 sFADMCLLDPSFNE--EHLPNLTHFLFCGEELPHKT-AKKLLERFPSATIYNTYGPTEATvavtsiEITDEML----DQY 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 494 PDLPpIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHpwrPGARLYRTGDLGrILGNGE 573
Cdd:PRK04813 316 KRLP-IGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF---DGQPAYHTGDAG-YLEDGL 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 574 IVWLGRADTQVKVRGFRIEPAEVElAIMRQaerQPGLRGAAVVARERQGN-DAFLAAFLLGEPEAVDLAELKQALRSEL- 651
Cdd:PRK04813 391 LFYQGRIDFQIKLNGYRIELEEIE-QNLRQ---SSYVESAVVVPYNKDHKvQYLIAYVVPKEEDFEREFELTKAIKKELk 466
|
490 500 510
....*....|....*....|....*....|.
gi 1395399044 652 ---PEHMVPAHFAWVDGFALTPSGKRDDAAL 679
Cdd:PRK04813 467 erlMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
190-681 |
2.11e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 178.07 E-value: 2.11e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFEEQRWTYRDLD-HVARcVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVS 268
Cdd:PRK06187 11 ILRHGARKHPDKEAVYFDGRRTTYAELDeRVNR-LANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIR 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 269 YPAQRLALILETAQPFRVVAHPEHAHVAAA-----------------------ERVLPVEELVADiEPETFAAPQLDE-- 323
Cdd:PRK06187 90 LKPEEIAYILNDAEDRVVLVDSEFVPLLAAilpqlptvrtvivegdgpaaplaPEVGEYEELLAA-ASDTFDFPDIDEnd 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 324 LAMLLFTSGSTGRPKGVELSHR-MWANytqwqLRVASGVPGLRT----LQFAPLSFDMAFQEIFSTLCGGGELQLIsnrE 398
Cdd:PRK06187 169 AAAMLYTSGTTGHPKGVVLSHRnLFLH-----SLAVCAWLKLSRddvyLVIVPMFHVHAWGLPYLALMAGAKQVIP---R 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 399 RMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGeqlritedvrafcAAMPGLLLEN------- 471
Cdd:PRK06187 241 RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSLRLVIYGG-------------AALPPALLREfkekfgi 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 472 ----QYGPTETHQVTyhSLSGDPAHYPDLPPI----GRPLDGVEVQVLDAALRPVPV--GVTGELYFGGDCLARGYHRAP 541
Cdd:PRK06187 308 dlvqGYGMTETSPVV--SVLPPEDQLPGQWTKrrsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 542 ELTAERFVeHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQaerqPGLRGAAVVAR--E 619
Cdd:PRK06187 386 EATAETID-GGW------LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGH----PAVAEVAVIGVpdE 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395399044 620 RQGnDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRA 681
Cdd:PRK06187 455 KWG-ERPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
208-680 |
6.47e-47 |
|
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: 174.02 E-value: 6.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 208 EQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVV 287
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 288 AHPehahvaaaervlpveelvadiepetfaapqldelAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTL 367
Cdd:cd05934 81 VDP----------------------------------ASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGEDDVYL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 368 QFAPLsFDMAFQE--IFSTLCGGGELQLisnRERMDPSALLHVLERRQVQR-----VLLPFVALQRLAEASNALGVRPGA 440
Cdd:cd05934 127 TVLPL-FHINAQAvsVLAALSVGATLVL---LPRFSASRFWSDVRRYGATVtnylgAMLSYLLAQPPSPDDRAHRLRAAY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 441 LRVVVSsgeqlritEDVRAFCAAMpGLLLENQYGPTETHqvtyHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPV 520
Cdd:cd05934 203 GAPNPP--------ELHEEFEERF-GVRLLEGYGMTETI----VGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPA 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 521 GVTGELY---FGGDCLARGYHRAPELTAERFvEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE 597
Cdd:cd05934 270 GEPGELVirgLRGWGFFKGYYNMPEATAEAM-RNGW------FHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 598 LAIMrqaeRQPGLRGAAVVA-RERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDD 676
Cdd:cd05934 343 RAIL----RHPAVREAAVVAvPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAK 418
|
....
gi 1395399044 677 AALR 680
Cdd:cd05934 419 AQLR 422
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
191-673 |
2.76e-46 |
|
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: 172.41 E-value: 2.76e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 191 FERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDvsyp 270
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLN---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 271 aQRLaliletaqpfrvvahpehahvAAAErvlpVEELVADIEPETFaapqLDELAMLLFTSGSTGRPKGVELSHRMWANY 350
Cdd:cd17631 77 -FRL---------------------TPPE----VAYILADSGAKVL----FDDLALLMYTSGTTGRPKGAMLTHRNLLWN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 351 TQWQLrVASGV-PGLRTLQFAPLS-FDMAFQEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRVLLPFVALQRLA 428
Cdd:cd17631 127 AVNAL-AALDLgPDDVLLVVAPLFhIGGLGVFTLPTLLRGGTVVIL---RKFDPETVLDLIERHRVTSFFLVPTMIQALL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 429 EASNALGVRPGALRVVVSSGEQLRitEDVRAFCAAMpGLLLENQYGPTETHQVTYHSLSGDpaHYPDLPPIGRPLDGVEV 508
Cdd:cd17631 203 QHPRFATTDLSSLRAVIYGGAPMP--ERLLRALQAR-GVKFVQGYGMTETSPGVTFLSPED--HRRKLGSAGRPVFFVEV 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 509 QVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFvEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRG 588
Cdd:cd17631 278 RIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAF-RDGW------FHTGDLGRLDEDGYLYIVDRKKDMIISGG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 589 FRIEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGnDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGF 666
Cdd:cd17631 351 ENVYPAEVEDVLY----EHPAVAEVAVIGVpdEKWG-EAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDAL 425
|
....*..
gi 1395399044 667 ALTPSGK 673
Cdd:cd17631 426 PRNATGK 432
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
102-766 |
8.28e-45 |
|
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), product of the LYS2 gene. It is also called alpha-aminoadipate reductase. In fungi, lysine is synthesized via aminoadipate. Currently, all members of this family are fungal.
Pssm-ID: 274582 [Multi-domain] Cd Length: 1389 Bit Score: 176.79 E-value: 8.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 102 QLRDFRVWEETNFALLVnviATPSDGMYLRIDSDGRGISRSQAALIGATFVELLWRLAEHPDEAADFAFLAPRRDAASQP 181
Cdd:TIGR03443 147 QQTTYSTGSTTDLTVFL---TPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLP 223
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 182 EPLVD---------VVSLFERQVEALP---------GSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALN 243
Cdd:TIGR03443 224 DPTKDldwsgfrgaIHDIFADNAEKHPdrtcvvetpSFLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAY 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 244 RSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAhpehahVAAAERVLP-VE-------ELVADI---- 311
Cdd:TIGR03443 304 RGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIV------IEKAGTLDQlVRdyidkelELRTEIpala 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 312 ---------------EPETFAAPQL------------DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGL 364
Cdd:TIGR03443 378 lqddgslvggsleggETDVLAPYQAlkdtptgvvvgpDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSEND 457
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 365 RTLQFAPLSFDMAFQEIFSTLCGGGELqLISNRERM-DPSALLHVLERRQVQRV-LLPfvALQRL--AEASNALGVRPGA 440
Cdd:TIGR03443 458 KFTMLSGIAHDPIQRDMFTPLFLGAQL-LVPTADDIgTPGRLAEWMAKYGATVThLTP--AMGQLlsAQATTPIPSLHHA 534
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 441 LRVvvssGEQLrITEDVRAFCAAMPGLLLENQYGPTETHQ-VTYH---SLSGDP---AHYPDLPPIGRPLDGVEVQVLDA 513
Cdd:TIGR03443 535 FFV----GDIL-TKRDCLRLQTLAENVCIVNMYGTTETQRaVSYFeipSRSSDStflKNLKDVMPAGKGMKNVQLLVVNR 609
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 514 ALRPVPVGV--TGELYFGGDCLARGYHRAPELTAERFV-----------------EHPWR-----PGARLYRTGDLGRIL 569
Cdd:TIGR03443 610 NDRTQTCGVgeVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfvdpshwidldkenNKPERefwlgPRDRLYRTGDLGRYL 689
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 570 GNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQA--- 646
Cdd:TIGR03443 690 PDGNVECCGRADDQVKIRGFRIELGEIDTHL----SQHPLVRENVTLVRRDKDEEPTLVSYIVPQDKSDELEEFKSEvdd 765
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 647 ------------------------LRSELPEHMVPAHFAWVDGFALTPSGKRDDAalrALPLEHGTNIEYLAPRDD---- 698
Cdd:TIGR03443 766 eessdpvvkglikyrklikdireyLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKP---ALPFPDTAQLAAVAKNRSasaa 842
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395399044 699 ------YERTLAGLLGELL-DRP-RVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLA---ERLR 766
Cdd:TIGR03443 843 deefteTEREIRDLWLELLpNRPaTISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAkevDRLK 921
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
190-682 |
2.22e-44 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 169.91 E-value: 2.22e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFE-----EQRWTYRDL-DHVARcVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCV 263
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEgedgeERTLTYAELrREVNR-FANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 264 PLDVSYPAQRLALILETAQPfRVV-----------AHPEHAHVAAA-------ERVLPV---------------EELVAD 310
Cdd:COG0365 93 PVFPGFGAEALADRIEDAEA-KVLitadgglrggkVIDLKEKVDEAleelpslEHVIVVgrtgadvpmegdldwDELLAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 311 iEPETFAAPQL--DELAMLLFTSGSTGRPKGVELSHR---MWANYT-QWQLRVASG-----------VPGLRTLQFAPLS 373
Cdd:COG0365 172 -ASAEFEPEPTdaDDPLFILYTSGTTGKPKGVVHTHGgylVHAATTaKYVLDLKPGdvfwctadigwATGHSYIVYGPLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 374 FDMAfqeifSTLCGGgelqlisNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPG--ALRVVVSSGEql 451
Cdd:COG0365 251 NGAT-----VVLYEG-------RPDFPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDlsSLRLLGSAGE-- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 452 RITEDVRAFCAAMPGLLLENQYGPTET-HQVTyhslsgdpAHYPDLPP----IGRPLDGVEVQVLDAALRPVPVGVTGEL 526
Cdd:COG0365 317 PLNPEVWEWWYEAVGVPIVDGWGQTETgGIFI--------SNLPGLPVkpgsMGKPVPGYDVAVVDEDGNPVPPGEEGEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 527 YFGGDC--LARGYHRAPELTAERFVEHPwrPGarLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQ- 603
Cdd:COG0365 389 VIKGPWpgMFRGYWNDPERYRETYFGRF--PG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHp 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 604 --AErqpglrgAAVVARERQGNDAFLAAFLL---GEPEAVDLA-ELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDA 677
Cdd:COG0365 465 avAE-------AAVVGVPDEIRGQVVKAFVVlkpGVEPSDELAkELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRR 537
|
....*
gi 1395399044 678 ALRAL 682
Cdd:COG0365 538 LLRKI 542
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
207-673 |
3.63e-44 |
|
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: 167.77 E-value: 3.63e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 207 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRV 286
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 287 VAHPEHAHV--AAAERVLPVEELV------------------ADIEPETFAAPQL----DELAMLLFTSGSTGRPKGVEL 342
Cdd:cd05911 87 FTDPDGLEKvkEAAKELGPKDKIIvlddkpdgvlsiedllspTLGEEDEDLPPPLkdgkDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 343 SHRmwaNYTQWQLRVASGVPGL---RTLQFAPLSFDMAFQeIFSTLCGG--GELQLISNreRMDPSALLHVLERRQVQRV 417
Cdd:cd05911 167 SHR---NLIANLSQVQTFLYGNdgsNDVILGFLPLYHIYG-LFTTLASLlnGATVIIMP--KFDSELFLDLIEKYKITFL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 418 LLPFVALQRLAEASNALGVRPGALRVVVSSGEqlRITEDVRAFCAAMPGLLLENQ-YGPTETHQVTYHSlsgdPAHYPDL 496
Cdd:cd05911 241 YLVPPIAAALAKSPLLDKYDLSSLRVILSGGA--PLSKELQELLAKRFPNATIKQgYGMTETGGILTVN----PDGDDKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 497 PPIGRPLDGVEVQVLDAALRP-VPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIV 575
Cdd:cd05911 315 GSVGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYLY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 576 WLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGNDAflAAFLLGEPEAVDLAElkqalrsELPE 653
Cdd:cd05911 389 IVDRKKELIKYKGFQVAPAELEAVLL----EHPGVADAAVigIPDEVSGELP--RAYVVRKPGEKLTEK-------EVKD 455
|
490 500
....*....|....*....|....*....
gi 1395399044 654 HM---VPAHFAW------VDGFALTPSGK 673
Cdd:cd05911 456 YVakkVASYKQLrggvvfVDEIPKSASGK 484
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
193-673 |
9.34e-43 |
|
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: 164.72 E-value: 9.34e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 193 RQVEALPGSAALAF------EEQRWTYRDLDHVARCVATRLVRAGaRRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 266
Cdd:cd05931 1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 267 VSYP---AQRLALILETAQPfRVV--AHPEHAHVAAAERVLPVEEL----------VADIEPETFAAPQLDELAMLLFTS 331
Cdd:cd05931 80 PPTPgrhAERLAAILADAGP-RVVltTAAALAAVRAFAASRPAAGTprllvvdllpDTSAADWPPPSPDPDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 332 GSTGRPKGVELSHR-MWANytQWQLRVASGV-PGLRTLQFAPLSFDMA-FQEIFSTLCGGGELQLISNRERM-DPSALLH 407
Cdd:cd05931 159 GSTGTPKGVVVTHRnLLAN--VRQIRRAYGLdPGDVVVSWLPLYHDMGlIGGLLTPLYSGGPSVLMSPAAFLrRPLRWLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 408 VLERRQVQRVLLPFVALQRLAEASNALGVRP---GALRVVVSSGEQLRItEDVRAFCAAMPGLLLENQ-----YG----- 474
Cdd:cd05931 237 LISRYRATISAAPNFAYDLCVRRVRDEDLEGldlSSWRVALNGAEPVRP-ATLRRFAEAFAPFGFRPEafrpsYGlaeat 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 475 -----------------PTETHQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAA-LRPVPVGVTGELYFGGDCLARG 536
Cdd:cd05931 316 lfvsggppgtgpvvlrvDRDALAGRAVAVAADDPAARELVSCGRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVASG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 537 YHRAPELTAERFVEHPWRPGARLYRTGDLGRILGnGEIVWLGRADTQVKVRGFRIEPAEVELAImrqAERQPGLRGAAVV 616
Cdd:cd05931 396 YWGRPEATAETFGALAATDEGGWLRTGDLGFLHD-GELYITGRLKDLIIVRGRNHYPQDIEATA---EEAHPALRPGCVA 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395399044 617 A---RERQGNDAFLAAFLLGEPEAVDLAELKQALRSELP-EHMVPAHFAWV---DGFALTPSGK 673
Cdd:cd05931 472 AfsvPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVArEHGVAPADVVLvrpGSIPRTSSGK 535
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
211-681 |
2.47e-42 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 160.97 E-value: 2.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 211 WTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAhp 290
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 291 ehahvaaaervlpveelvadiepetfaapQLDELAMLLFTSGSTGRPKGVELSHRmwanYTQWQLRVASGVPGLRT--LQ 368
Cdd:cd05972 79 -----------------------------DAEDPALIYFTSGTTGLPKGVLHTHS----YPLGHIPTAAYWLGLRPddIH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 369 FAPLsfDMAFQE-IFSTLCG---GGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGaLRVV 444
Cdd:cd05972 126 WNIA--DPGWAKgAWSSFFGpwlLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSH-LRLV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 445 VSSGEQLRiTEDVRAFCAAMpGLLLENQYGPTETHQVTyhslsgdpAHYPDLPP----IGRPLDGVEVQVLDAALRPVPV 520
Cdd:cd05972 203 VSAGEPLN-PEVIEWWRAAT-GLPIRDGYGQTETGLTV--------GNFPDMPVkpgsMGRPTPGYDVAIIDDDGRELPP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 521 GVTGELYF--GGDCLARGYHRAPELTAERFVEHpwrpgarLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVEL 598
Cdd:cd05972 273 GEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVES 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 599 AIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLL---GEPEAVDLA-ELKQALRSELPEHMVPAHFAWVDGFALTPSGKR 674
Cdd:cd05972 346 ALL----EHPAVAEAAVVGSPDPVRGEVVKAFVVltsGYEPSEELAeELQGHVKKVLAPYKYPREIEFVEELPKTISGKI 421
|
....*..
gi 1395399044 675 DDAALRA 681
Cdd:cd05972 422 RRVELRD 428
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
210-673 |
9.90e-42 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 159.08 E-value: 9.90e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 210 RWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPfrvvah 289
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 290 pehahvaaaeRVLPVEELVADIEPetfaAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGvPGLRTLQ 368
Cdd:cd05903 75 ----------KVFVVPERFRQFDP----AAMPDAVALLLFTSGTTGEPKGVMHSHNtLSASIRQYAERLGLG-PGDVFLV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 369 FAPLSFDMAFqeifstlCGGGELQLISN-----RERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRV 443
Cdd:cd05903 140 ASPMAHQTGF-------VYGFTLPLLLGapvvlQDIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 444 VVSSGEQlrITEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPAH--YPDlppiGRPLDGVEVQVLDAALRPVPVG 521
Cdd:cd05903 213 FVCGGAT--VPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRrlYTD----GRPLPGVEIKVVDDTGATLAPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 522 VTGELYFGGDCLARGYHRAPELTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIM 601
Cdd:cd05903 287 VEGELLSRGPSVFLGYLDRPDLTADAAPEG-W------FRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLL 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395399044 602 rqaeRQPGLRGAAVVA--RERQGNDAflAAFLLGEPEA-VDLAELKQAL-RSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:cd05903 360 ----GHPGVIEAAVVAlpDERLGERA--CAVVVTKSGAlLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGK 429
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
180-682 |
1.91e-40 |
|
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: 157.61 E-value: 1.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 180 QPEPLVDVvslFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAG 259
Cdd:COG1021 23 RGETLGDL---LRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 260 LVCVpldVSYPAQRLALIL---ETAQP-------------FRVVA--------HPEHAHVAA-AERVLPVEELVADIEPE 314
Cdd:COG1021 100 AIPV---FALPAHRRAEIShfaEQSEAvayiipdrhrgfdYRALArelqaevpSLRHVLVVGdAGEFTSLDALLAAPADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 315 TFAAPQLDELAMLLFTSGSTGRPKGVELSHrmwANYTqWQLRVASGVPGL----RTLQFAPLS--FDMAFQEIFSTLCGG 388
Cdd:COG1021 177 SEPRPDPDDVAFFQLSGGTTGLPKLIPRTH---DDYL-YSVRASAEICGLdadtVYLAALPAAhnFPLSSPGVLGVLYAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 389 GELQLISNrerMDPSALLHVLERRQVQRVLL-PFVALqRLAEASNALGVRPGALRVVVSSGEQLrITEDVRAFCAAMpGL 467
Cdd:COG1021 253 GTVVLAPD---PSPDTAFPLIERERVTVTALvPPLAL-LWLDAAERSRYDLSSLRVLQVGGAKL-SPELARRVRPAL-GC 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 468 LLENQYGPTEThQVTYHSLsGDP----AHYpdlppIGRPL-DGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPE 542
Cdd:COG1021 327 TLQQVFGMAEG-LVNYTRL-DDPeeviLTT-----QGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPE 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 543 LTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQaerqPGLRGAAVVARErqg 622
Cdd:COG1021 400 HNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAH----PAVHDAAVVAMP--- 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1395399044 623 nDAFLA----AFLLGEPEAVDLAELKQALRS-ELPEHMVPAHFAWVDGFALTPSGKRDDAALRAL 682
Cdd:COG1021 467 -DEYLGerscAFVVPRGEPLTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKALRAA 530
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
209-681 |
4.60e-40 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 154.51 E-value: 4.60e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 209 QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLdvsypaqrLALILETAQPFRVvA 288
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPL--------FALFGPEALEYRL-S 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 289 HPEhahvAAAervlpveeLVADIEpetfaapqlDELAMLLFTSGSTGRPKGVELSHRMwanytqwqlrVASGVPGLR-TL 367
Cdd:cd05971 76 NSG----ASA--------LVTDGS---------DDPALIIYTSGTTGPPKGALHAHRV----------LLGHLPGVQfPF 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 368 QFAPLSFDMAFQEIFSTLCGG-----------GELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGV 436
Cdd:cd05971 125 NLFPRDGDLYWTPADWAWIGGlldvllpslyfGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 437 RPGALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPahyPDLPPIGRPLDGVEVQVLDAALR 516
Cdd:cd05971 205 AQVKLRAIATGGESL--GEELLGWAREQFGVEVNEFYGQTECNLVIGNCSALFP---IKPGSMGKPIPGHRVAIVDDNGT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 517 PVPVGVTGELYFGGDCLAR--GYHRAPELTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPA 594
Cdd:cd05971 280 PLPPGEVGEIAVELPDPVAflGYWNNPSATEKKMAGD-W------LLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 595 EVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQAL----RSELPEHMVPAHFAWVDGFALTP 670
Cdd:cd05971 353 EIEECLL----KHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDALAREIqelvKTRLAAHEYPREIEFVNELPRTA 428
|
490
....*....|.
gi 1395399044 671 SGKRDDAALRA 681
Cdd:cd05971 429 TGKIRRRELRA 439
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
211-673 |
1.02e-39 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 154.78 E-value: 1.02e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 211 WTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPfRVVAHP 290
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGS-KLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 291 EH----AHVAAAERVLPVEELVAD--------------------IEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRM 346
Cdd:cd05926 94 KGelgpASRAASKLGLAILELALDvgvlirapsaeslsnlladkKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 347 WANYTQWQLRVASGVPGLRTLQFAPLsfdmaFQ------EIFSTLCGGGELQLisnRERMDPSALLHVLERRQV------ 414
Cdd:cd05926 174 LAASATNITNTYKLTPDDRTLVVMPL-----FHvhglvaSLLSTLAAGGSVVL---PPRFSASTFWPDVRDYNAtwytav 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 415 ---QRVLLPFvalqrlaEASNALGVRPGaLRVVVSSGEQLriTEDV-RAFCAAMPGLLLEnQYGPTET-HQVTYHSLsgd 489
Cdd:cd05926 246 ptiHQILLNR-------PEPNPESPPPK-LRFIRSCSASL--PPAVlEALEATFGAPVLE-AYGMTEAaHQMTSNPL--- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 490 PAHYPDLPPIGRPlDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRIL 569
Cdd:cd05926 312 PPGPRKPGSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 570 GNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVA--RERQGnDAFLAAFLLGEPEAVDLAELKQAL 647
Cdd:cd05926 385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLL----SHPAVLEAVAFGvpDEKYG-EEVAAAVVLREGASVTEEELRAFC 459
|
490 500
....*....|....*....|....*.
gi 1395399044 648 RSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:cd05926 460 RKHLAAFKVPKKVYFVDELPKTATGK 485
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
211-679 |
1.99e-38 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 151.52 E-value: 1.99e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 211 WTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAhp 290
Cdd:cd17647 21 FTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV-- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 291 ehahVAAAERVLpveelvadiepetfaAPqlDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFA 370
Cdd:cd17647 99 ----IRAAGVVV---------------GP--DSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 371 PLSFDMAFQEIFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRL-AEASNALGVRPGALRVvvssGE 449
Cdd:cd17647 158 GIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLtAQATTPFPKLHHAFFV----GD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 450 QLrITEDVRAFCAAMPGLLLENQYGPTETHQ-VTYH---SLSGDPAHY---PDLPPIGRPLDGVEVQVLDAALRP--VPV 520
Cdd:cd17647 234 IL-TKRDCLRLQTLAENVRIVNMYGTTETQRaVSYFevpSRSSDPTFLknlKDVMPAGRGMLNVQLLVVNRNDRTqiCGI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 521 GVTGELYFGGDCLARGYHRAPELTAERFV-----------------EHPWR-----PGARLYRTGDLGRILGNGEIVWLG 578
Cdd:cd17647 313 GEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfvepdhwnyldkdnNEPWRqfwlgPRDRLYRTGDLGRYLPNGDCECCG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 579 RADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDL------------------ 640
Cdd:cd17647 393 RADDQVKIRGFRIELGEIDTHI----SQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDesfaqedvpkevstdpiv 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1395399044 641 ----------AELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAAL 679
Cdd:cd17647 469 kgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
183-682 |
3.88e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 151.35 E-value: 3.88e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 183 PLVDVVSLFERQVealPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVC 262
Cdd:PRK06178 34 PLTEYLRAWARER---PQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVH 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 263 VPLDVSYPAQRLALILETAQP---------------------FRVVAHPEHAHVAAAERVLPVEELV----------ADI 311
Cdd:PRK06178 111 VPVSPLFREHELSYELNDAGAevllaldqlapvveqvraetsLRHVIVTSLADVLPAEPTLPLPDSLraprlaaagaIDL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 312 --------EPETFAAPQLDELAMLLFTSGSTGRPKGVELSHR-----MWANYTQWQLRVASGVpglrTLQFAPLsFDMA- 377
Cdd:PRK06178 191 lpalractAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRdmvytAAAAYAVAVVGGEDSV----FLSFLPE-FWIAg 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 378 --FQEIFSTLCgGGELQLISnreRMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRITE 455
Cdd:PRK06178 266 enFGLLFPLFS-GATLVLLA---RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEYDLSSLRQVRVVSFVKKLNP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 456 DVR-AFCAAMPGLLLENQYGPTETH---------QVTYHSLSGDPAHypdlppIGRPLDGVEVQVLD-AALRPVPVGVTG 524
Cdd:PRK06178 342 DYRqRWRALTGSVLAEAAWGMTETHtcdtftagfQDDDFDLLSQPVF------VGLPVPGTEFKICDfETGELLPLGAEG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 525 ELYFGGDCLARGYHRAPELTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqa 604
Cdd:PRK06178 416 EIVVRTPSLLKGYWNKPEATAEALRDG-W------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLG--- 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 605 eRQPGLRGAAVVAR--ERQGNDAFlaAFLLGEPEA-VDLAELKQALRSELPEHMVPaHFAWVDGFALTPSGKRDDAALRA 681
Cdd:PRK06178 486 -QHPAVLGSAVVGRpdPDKGQVPV--AFVQLKPGAdLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDLQA 561
|
.
gi 1395399044 682 L 682
Cdd:PRK06178 562 L 562
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
180-679 |
1.30e-37 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 148.24 E-value: 1.30e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 180 QPEPLVDVVSlfeRQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAG 259
Cdd:cd05920 13 QDEPLGDLLA---RSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 260 LVCVpldVSYPAQRLALIL---ETAQPFRVVAHPEHA---HVAAAervlpvEELVADIEpetfaapqldELAMLLFTSGS 333
Cdd:cd05920 90 AVPV---LALPSHRRSELSafcAHAEAVAYIVPDRHAgfdHRALA------RELAESIP----------EVALFLLSGGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 334 TGRPKGVELSHRMWAnytqWQLRVASGVPGL--RTLQFAPLS----FDMAFQEIFSTLCGGGELQLISNrerMDPSALLH 407
Cdd:cd05920 151 TGTPKLIPRTHNDYA----YNVRASAEVCGLdqDTVYLAVLPaahnFPLACPGVLGTLLAGGRVVLAPD---PSPDAAFP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 408 VLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEqlRITEDVRAFCAAMPGLLLENQYGPTEThQVTYHSLs 487
Cdd:cd05920 224 LIEREGVTVTALVPALVSLWLDAAASRRADLSSLRLLQVGGA--RLSPALARRVPPVLGCTLQQVFGMAEG-LLNYTRL- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 488 GDPA---HYPDlppiGRPLD-GVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTG 563
Cdd:cd05920 300 DDPDeviIHTQ----GRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 564 DLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVARErqgnDAFLA----AFLLGEPEAVD 639
Cdd:cd05920 370 DLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVE----NLLLRHPAVHDAAVVAMP----DELLGerscAFVVLRDPPPS 441
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1395399044 640 LAELKQALRS-ELPEHMVPAHFAWVDGFALTPSGKRDDAAL 679
Cdd:cd05920 442 AAQLRRFLRErGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
222-680 |
3.70e-37 |
|
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: 146.05 E-value: 3.70e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 222 CVATRLVR-AGARRGDAIGVALNRSPEMIATIWGILRAG----LVCVPLDVSYPAQRLALILETAQPFRVVAHPEHA-HV 295
Cdd:cd05922 4 SAAASALLeAGGVRGERVVLILPNRFTYIELSFAVAYAGgrlgLVFVPLNPTLKESVLRYLVADAGGRIVLADAGAAdRL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 296 AAAERVLP-------VEELVADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQ 368
Cdd:cd05922 84 RDALPASPdpgtvldADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRALT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 369 FAPLSFDMAFQEIFSTLCGGGELqLISNRERMDPSALLHVLERRQVQRVLLP--FVALQRLAEASNALgvrpGALRVVVS 446
Cdd:cd05922 164 VLPLSYDYGLSVLNTHLLRGATL-VLTNDGVLDDAFWEDLREHGATGLAGVPstYAMLTRLGFDPAKL----PSLRYLTQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 447 SGEQLRiTEDVRAFCAAMPGLLLENQYGPTE-THQVTYHslsgdPAHYPDLPP--IGRPLDGVEVQVLDAALRPVPVGVT 523
Cdd:cd05922 239 AGGRLP-QETIARLRELLPGAQVYVMYGQTEaTRRMTYL-----PPERILEKPgsIGLAIPGGEFEILDDDGTPTPPGEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 524 GELYFGGDCLARGYHRAP-ELTAERfvehpwRPGARLYrTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMR 602
Cdd:cd05922 313 GEIVHRGPNVMKGYWNDPpYRRKEG------RGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARS 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395399044 603 QAErqpgLRGAAVVARERQGNDAfLAAFLLGEPEaVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:cd05922 386 IGL----IIEAAAVGLPDPLGEK-LALFVTAPDK-IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
207-657 |
1.63e-36 |
|
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: 145.89 E-value: 1.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 207 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDV--SYPAQRLAL-----ILE 279
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVppTYDEPNARLrklrhIWQ 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 280 TAQPFRVVAHPE-HAHVAAAE--------RVLPVEELVADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMWANY 350
Cdd:cd05906 116 LLGSPVVLTDAElVAEFAGLEtlsglpgiRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILAR 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 351 TQWQLRVASGVPGLRTLQFAPLSFDMAFQE--IFSTLCGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLA 428
Cdd:cd05906 196 SAGKIQHNGLTPQDVFLNWVPLDHVGGLVElhLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVTITWAPNFAFALLN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 429 EASNALGVRPG---ALRVVVSSGEQLritedVRAFCAAMPGLLLENQ---------YGPTET-HQVTYHSLSGDPAHYPD 495
Cdd:cd05906 276 DLLEEIEDGTWdlsSLRYLVNAGEAV-----VAKTIRRLLRLLEPYGlppdairpaFGMTETcSGVIYSRSFPTYDHSQA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 496 LP--PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGrILGNGE 573
Cdd:cd05906 351 LEfvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGN 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 574 IVWLGRADTQVKVRGFRIEPAEVELAIMRQAERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSEL-- 651
Cdd:cd05906 424 LTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEYDLQDALSETLRAIRSVVsr 503
|
490
....*....|.
gi 1395399044 652 -----PEHMVP 657
Cdd:cd05906 504 evgvsPAYLIP 514
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
188-673 |
1.79e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 146.30 E-value: 1.79e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 188 VSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCV---P 264
Cdd:PRK05605 35 VDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnP 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 265 LdvsYPAQRLALILE----------------------TAQPFRVV------AHPEHAHVA-----------------AAE 299
Cdd:PRK05605 115 L---YTAHELEHPFEdhgarvaivwdkvaptverlrrTTPLETIVsvnmiaAMPLLQRLAlrlpipalrkaraaltgPAP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 300 RVLPVEELVADIEP-----ETFAAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQ---WqlrvasgVPGL-----R 365
Cdd:PRK05605 192 GTVPWETLVDAAIGgdgsdVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRnLFANAAQgkaW-------VPGLgdgpeR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 366 TLQFAPLsfdmaFQEIFSTLCG------GGELQLISnreRMDPSALLHVLERRQVqrVLLPFVA--LQRLAEASNALGVR 437
Cdd:PRK05605 265 VLAALPM-----FHAYGLTLCLtlavsiGGELVLLP---APDIDLILDAMKKHPP--TWLPGVPplYEKIAEAAEERGVD 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 438 PGALRVVVSSGEQLRiTEDVRAFCAAMPGLLLENqYGPTETHQVtyhsLSGDPAHyPDLPP--IGRPLDGVEVQVLDA-- 513
Cdd:PRK05605 335 LSGVRNAFSGAMALP-VSTVELWEKLTGGLLVEG-YGLTETSPI----IVGNPMS-DDRRPgyVGVPFPDTEVRIVDPed 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 514 ALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEP 593
Cdd:PRK05605 408 PDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-W------FRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYP 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 594 AEVELAImrqaERQPGLRGAAVVARERQ-GNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSG 672
Cdd:PRK05605 481 AEVEEVL----REHPGVEDAAVVGLPREdGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLG 556
|
.
gi 1395399044 673 K 673
Cdd:PRK05605 557 K 557
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
203-680 |
1.82e-36 |
|
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: 143.76 E-value: 1.82e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 203 ALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQ 282
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 283 PFRVVAHPehahvaaaervlpveelvadiepetfaapqlDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGV- 361
Cdd:cd05919 83 ARLVVTSA-------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREALGLt 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 362 PGLRTLQFAPLSF--DMAFQEIFSTLCGGgelQLISNRERMDPSALLHVLERRQvQRVL--LP--FVALQRLAEASNALG 435
Cdd:cd05919 132 PGDRVFSSAKMFFgyGLGNSLWFPLAVGA---SAVLNPGWPTAERVLATLARFR-PTVLygVPtfYANLLDSCAGSPDAL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 436 VrpgALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETHQVTyhsLSGDPAHYpDLPPIGRPLDGVEVQVLDAAL 515
Cdd:cd05919 208 R---SLRLCVSAGEAL--PRGLGERWMEHFGGPILDGIGATEVGHIF---LSNRPGAW-RLGSTGRPVPGYEIRLVDEEG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 516 RPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAE 595
Cdd:cd05919 279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-W------YRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 596 VELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVD---LAE-LKQALRSELPEHMVPAHFAWVDGFALTPS 671
Cdd:cd05919 352 VESLII----QHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPqesLARdIHRHLLERLSAHKVPRRIAFVDELPRTAT 427
|
....*....
gi 1395399044 672 GKRDDAALR 680
Cdd:cd05919 428 GKLQRFKLR 436
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
187-681 |
2.05e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 145.05 E-value: 2.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 187 VVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 266
Cdd:PRK07656 7 LPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 267 VSYPAQRLALILET--------AQPF---------------RVVAHPEHAHVAAAERVLPVEELVADIEPETFAAP-QLD 322
Cdd:PRK07656 87 TRYTADEAAYILARgdakalfvLGLFlgvdysattrlpaleHVVICETEEDDPHTEKMKTFTDFLAAGDPAERAPEvDPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 323 ELAMLLFTSGSTGRPKGVELSHR-MWANYTQW----QLRvasgvPGLRTLQFAPLsfdmafqeiFSTLC-GGGELQLISN 396
Cdd:PRK07656 167 DVADILFTSGTTGRPKGAMLTHRqLLSNAADWaeylGLT-----EGDRYLAANPF---------FHVFGyKAGVNAPLMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 397 RERM------DPSALLHVLERRQVqrVLLPFVA------LQRLAEASNALgvrpGALRVVVSSGeqlritedvrafcAAM 464
Cdd:PRK07656 233 GATIlplpvfDPDEVFRLIETERI--TVLPGPPtmynslLQHPDRSAEDL----SSLRLAVTGA-------------ASM 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 465 PGLLLEN------------QYGPTETHQVTYHSLSGDPAHypDLP-PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGD 531
Cdd:PRK07656 294 PVALLERfeselgvdivltGYGLSEASGVTTFNRLDDDRK--TVAgTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGP 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 532 CLARGYHRAPELTAERFVEHPWrpgarLYrTGDLGRI--LGNGEIVwlGRADTQVKVRGFRIEPAEVELAIMrqaeRQPG 609
Cdd:PRK07656 372 NVMKGYYDDPEATAAAIDADGW-----LH-TGDLGRLdeEGYLYIV--DRKKDMFIVGGFNVYPAEVEEVLY----EHPA 439
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395399044 610 LRGAAV--VARERQGnDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRA 681
Cdd:PRK07656 440 VAEAAVigVPDERLG-EVGKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
212-673 |
5.21e-36 |
|
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: 142.23 E-value: 5.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPE 291
Cdd:cd05935 3 TYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 292 hahvaaaervlpveelvadiepetfaapqLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQwqLRVASGV-PGLRTLQF 369
Cdd:cd05935 83 -----------------------------LDDLALIPYTSGTTGLPKGCMHTHFsAAANALQ--SAVWTGLtPSDVILAC 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 370 APLSFDMAFQEIFST-LCGGGELQLISnreRMDPSALLHVLERRQVQ------RVLLPFVALQRLAEA--SNALGVRPGA 440
Cdd:cd05935 132 LPLFHVTGFVGSLNTaVYVGGTYVLMA---RWDRETALELIEKYKVTfwtnipTMLVDLLATPEFKTRdlSSLKVLTGGG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 441 LRVVVSSGEQLRitedvrafcaAMPGLLLENQYGPTETHQVTyHSlsgDPAHYPDLPPIGRPLDGVEVQVLDA-ALRPVP 519
Cdd:cd05935 209 APMPPAVAEKLL----------KLTGLRFVEGYGLTETMSQT-HT---NPPLRPKLQCLGIP*FGVDARVIDIeTGRELP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 520 VGVTGELYFGGDCLARGYHRAPELTAERFVEhpwRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElA 599
Cdd:cd05935 275 PNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVE-A 350
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395399044 600 IMRQaerQPGLRGAAVVAR--ERQGNDAflAAFLLGEPE---AVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:cd05935 351 KLYK---HPAI*EVCVISVpdERVGEEV--KAFIVLRPEyrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGK 424
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
237-679 |
9.05e-36 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. 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: 341309 [Multi-domain] Cd Length: 449 Bit Score: 141.84 E-value: 9.05e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 237 AIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAhpehahvaaaERVLPVEELVADIEPETF 316
Cdd:cd17654 43 AIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQ----------NKELDNAPLSFTPEHRHF 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 317 AAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQwQLRVASGVPGLRTLQFA-PLSFDMAFQEIFSTLCGGGELQLIS 395
Cdd:cd17654 113 NIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQ-HFRSLFNITSEDILFLTsPLTFDPSVVEIFLSLSSGATLLIVP 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 396 NRERMDPSALLHVL-ERRQVQRVLLPFVALQRLAEASNALGV--RPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQ 472
Cdd:cd17654 192 TSVKVLPSKLADILfKRHRITVLQATPTLFRRFGSQSIKSTVlsATSSLRVLALGGEPFPSLVILSSWRGKGNRTRIFNI 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 473 YGPTETH--QVTYHSLSGDpahypdLP-PIGRPLDGVEVQVLDAALRPVpvgvTGELYFGGdcLARGYHRAPELTaerfv 549
Cdd:cd17654 272 YGITEVScwALAYKVPEED------SPvQLGSPLLGTVIEVRDQNGSEG----TGQVFLGG--LNRVCILDDEVT----- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 550 ehpwRPGARLYRTGDLGRIlGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVARERQGndafLAA 629
Cdd:cd17654 335 ----VPKGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQ----QVIESCLGVESCAVTLSDQQR----LIA 401
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1395399044 630 FLLGEPEAvdlAELKQALRSE-LPEHMVPAHFAWVDGFALTPSGKRDDAAL 679
Cdd:cd17654 402 FIVGESSS---SRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
190-675 |
9.73e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 143.49 E-value: 9.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 269
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 270 PAQRLALILETAQPFRVVAH-----------PEHAHVAAAERV------------LPVEELVADIEPET-FAAPQLDELa 325
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYErefaprvaevlPRLPKLRTLVVVedgsgndllpgaVDYEDALAAGSPERdFGERSPDDL- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 326 MLLFTSGSTGRPKGVelshrMW------------ANY-------TQWQL--RVASGvPGLRTLQFAPLSFDMAFQEIFST 384
Cdd:PRK07798 167 YLLYTGGTTGMPKGV-----MWrqedifrvllggRDFatgepieDEEELakRAAAG-PGMRRFPAPPLMHGAGQWAAFAA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 385 LCGGGELQLISNReRMDPSALLHVLERRQVQRVLLPFVALQR--LAEASNALGVRPGALRVVVSSGEQLriTEDVR-AFC 461
Cdd:PRK07798 241 LFSGQTVVLLPDV-RFDADEVWRTIEREKVNVITIVGDAMARplLDALEARGPYDLSSLFAIASGGALF--SPSVKeALL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 462 AAMPGLLLENQYGPTEThQVTYHSLSGDPAHYPDLPPIGRpldGVEVQVLDAALRPVPVGvTGELYFggdcLAR------ 535
Cdd:PRK07798 318 ELLPNVVLTDSIGSSET-GFGGSGTVAKGAVHTGGPRFTI---GPRTVVLDEDGNPVEPG-SGEIGW----IARrghipl 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 536 GYHRAPELTAERFVEHpwrPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAV 615
Cdd:PRK07798 389 GYYKDPEKTAETFPTI---DGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEAL----KAHPDVADALV 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1395399044 616 VAR--ERQGNdAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 675
Cdd:PRK07798 462 VGVpdERWGQ-EVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
201-681 |
9.53e-34 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 135.88 E-value: 9.53e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 201 SAALAFEEQRWTYRDLDHVARCVATRLVRAGA-RRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILE 279
Cdd:cd05941 2 RIAIVDDGDSITYADLVARAARLANRLLALGKdLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVIT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 280 TAQPFRVVahpehahvaaaervlpveelvadiepetfaapqldELAMLLFTSGSTGRPKGVELSHRMWANYTQ-----WQ 354
Cdd:cd05941 82 DSEPSLVL-----------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRalvdaWR 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 355 LRvasgvPGLRTLQFAPLsFDM--AFQEIFSTLCGGGELQLISnreRMDPSAllhVLERRQVQRVLLpFVAL----QRLA 428
Cdd:cd05941 127 WT-----EDDVLLHVLPL-HHVhgLVNALLCPLFAGASVEFLP---KFDPKE---VAISRLMPSITV-FMGVptiyTRLL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 429 EASNA--------LGVRPGALRVVVSSGEQLrITEDVRAFCAAMPGLLLEnQYGPTETHQVTYHSLSGDPahypdLP-PI 499
Cdd:cd05941 194 QYYEAhftdpqfaRAAAAERLRLMVSGSAAL-PVPTLEEWEAITGHTLLE-RYGMTEIGMALSNPLDGER-----RPgTV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 500 GRPLDGVEVQVLD-AALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLG 578
Cdd:cd05941 267 GMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWILG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 579 R-ADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVV--ARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHM 655
Cdd:cd05941 341 RsSVDIIKSGGYKVSALEIERVL----LAHPGVSECAVIgvPDPDWGERVVAVVVLRAGAAALSLEELKEWAKQRLAPYK 416
|
490 500
....*....|....*....|....*.
gi 1395399044 656 VPAHFAWVDGFALTPSGKRDDAALRA 681
Cdd:cd05941 417 RPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
196-680 |
3.04e-33 |
|
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: 135.57 E-value: 3.04e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 196 EALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLA 275
Cdd:cd05959 15 EGRGDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 276 LILETAQPFRVVAHPEHAHVAAAE--------RVLPV-------------EELVADIEPETFAAP-QLDELAMLLFTSGS 333
Cdd:cd05959 95 YYLEDSRARVVVVSGELAPVLAAAltksehtlVVLIVsggagpeagalllAELVAAEAEQLKPAAtHADDPAFWLYSSGS 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 334 TGRPKGVELSHR----MWANYTQWQLRVASGVPGLRT--LQFA-----PLSFDMAFqeifstlcgGGELQLISnrERMDP 402
Cdd:cd05959 175 TGRPKGVVHLHAdiywTAELYARNVLGIREDDVCFSAakLFFAyglgnSLTFPLSV---------GATTVLMP--ERPTP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 403 SALLHVLERRQvqrvllP--FVALQRLaeaSNALGVRPGA-------LRVVVSSGEQLriTEDVRAFCAAMPGLLLENQY 473
Cdd:cd05959 244 AAVFKRIRRYR------PtvFFGVPTL---YAAMLAAPNLpsrdlssLRLCVSAGEAL--PAEVGERWKARFGLDILDGI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 474 GPTETHQVTYHSLSGDpAHYPDlppIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFvEHPW 553
Cdd:cd05959 313 GSTEMLHIFLSNRPGR-VRYGT---TGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-QGEW 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 554 rpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLL- 632
Cdd:cd05959 388 ------TRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALV----QHPAVLEAAVVGVEDEDGLTKPKAFVVl 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1395399044 633 ---GEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:cd05959 458 rpgYEDSEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKLR 508
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
212-680 |
3.01e-32 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 131.10 E-value: 3.01e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVahpe 291
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVV---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 292 hahVAAAERvlpveelvADIEPETFaapqldelaMLLFTSGSTGRPKGVELSHRM---WANYTQWQLRVASG-------- 360
Cdd:cd05973 78 ---TDAANR--------HKLDSDPF---------VMMFTSGTTGLPKGVPVPLRAlaaFGAYLRDAVDLRPEdsfwnaad 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 361 ---VPGLRTLQFAPLSFDMAfqeifSTLCGGGelqlisnrerMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVR 437
Cdd:cd05973 138 pgwAYGLYYAITGPLALGHP-----TILLEGG----------FSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPAR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 438 P-GALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETHQV--TYHSLsGDPAHYPDLppiGRPLDGVEVQVLDAA 514
Cdd:cd05973 203 PkGRLRRVSSAGEPL--TPEVIRWFDAALGVPIHDHYGQTELGMVlaNHHAL-EHPVHAGSA---GRAMPGWRVAVLDDD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 515 LRPVPVGVTGELyfggdclARGYHRAPELTAERFVEHPWR-PGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEP 593
Cdd:cd05973 277 GDELGPGEPGRL-------AIDIANSPLMWFRGYQLPDTPaIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGP 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 594 AEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLL------GEPEAVDlaELKQALRSELPEHMVPAHFAWVDGFA 667
Cdd:cd05973 350 FDVESALI----EHPAVAEAAVIGVPDPERTEVVKAFVVlrggheGTPALAD--ELQLHVKKRLSAHAYPRTIHFVDELP 423
|
490
....*....|...
gi 1395399044 668 LTPSGKRDDAALR 680
Cdd:cd05973 424 KTPSGKIQRFLLR 436
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
190-664 |
5.34e-32 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 131.54 E-value: 5.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFE---EQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 266
Cdd:PRK07514 5 LFDALRAAFADRDAPFIEtpdGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 267 VSYPAQRLALILETAQPFRVVAHPEH----AHVAAAERVLPVEEL----------VADIEPETFA--APQLDELAMLLFT 330
Cdd:PRK07514 85 TAYTLAELDYFIGDAEPALVVCDPANfawlSKIAAAAGAPHVETLdadgtgslleAAAAAPDDFEtvPRGADDLAAILYT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 331 SGSTGRPKGVELSHRMWANYTQwQLRVASGV-PGLRTLQFAPlsfdmafqeIFST----------LCGGGELQLISnreR 399
Cdd:PRK07514 165 SGTTGRSKGAMLSHGNLLSNAL-TLVDYWRFtPDDVLIHALP---------IFHThglfvatnvaLLAGASMIFLP---K 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 400 MDPSALLHVLERRQV--------QRvLLPFVALQRLAEASnalgvrpgaLRVVVSSGEQLrITEDVRAFCAAMPGLLLEn 471
Cdd:PRK07514 232 FDPDAVLALMPRATVmmgvptfyTR-LLQEPRLTREAAAH---------MRLFISGSAPL-LAETHREFQERTGHAILE- 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 472 QYGPTETHQVTYHSLSGD--PAhypdlpPIGRPLDGVEVQVLD-AALRPVPVGVTGELYFGGDCLARGYHRAPELTAERF 548
Cdd:PRK07514 300 RYGMTETNMNTSNPYDGErrAG------TVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 549 VEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLA 628
Cdd:PRK07514 374 RADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEI----DELPGVVESAVIGVPHPDFGEGVT 443
|
490 500 510
....*....|....*....|....*....|....*..
gi 1395399044 629 AFLLGEPEA-VDLAELKQALRSELPEHMVPAHFAWVD 664
Cdd:PRK07514 444 AVVVPKPGAaLDEAAILAALKGRLARFKQPKRVFFVD 480
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
193-673 |
7.49e-32 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 131.09 E-value: 7.49e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 193 RQVEALPGSAALAFEEQ--RWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYP 270
Cdd:cd05923 9 RAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLK 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 271 AQRLALILETAQPFRVV----AHPEHAHVAAAERVLPVEELVADIEPETFA------APQLDELAMLLFTSGSTGRPKGV 340
Cdd:cd05923 89 AAELAELIERGEMTAAViavdAQVMDAIFQSGVRVLALSDLVGLGEPESAGpliedpPREPEQPAFVFYTSGTTGLPKGA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 341 ELSHRMWAN-----YTQWQLRVASGVpglRTLQFAPLSFDMAFQEIF-STLCGGGELQLIsnrERMDPSALLHVLERRQV 414
Cdd:cd05923 169 VIPQRAAESrvlfmSTQAGLRHGRHN---VVLGLMPLYHVIGFFAVLvAALALDGTYVVV---EEFDPADALKLIEQERV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 415 QRVLLPFVALQRLAEASNALGVRPGALRVVVSSGeqlritedvrafcAAMPGLLLE-----------NQYGPTETHQVTY 483
Cdd:cd05923 243 TSLFATPTHLDALAAAAEFAGLKLSSLRHVTFAG-------------ATMPDAVLErvnqhlpgekvNIYGTTEAMNSLY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 484 hslsgDPAHYPDlpPIGRPLDGVEVQVLDAALRPV---PVGVTGELYF--GGDCLARGYHRAPELTAERFVEhpwrpgaR 558
Cdd:cd05923 310 -----MRDARTG--TEMRPGFFSEVRIVRIGGSPDealANGEEGELIVaaAADAAFTGYLNQPEATAKKLQD-------G 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 559 LYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAV--VARERQGNdaFLAAFLLGEPE 636
Cdd:cd05923 376 WYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIE----RVLSRHPGVTEVVVigVADERWGQ--SVTACVVPREG 449
|
490 500 510
....*....|....*....|....*....|....*...
gi 1395399044 637 AVDLAELKQALR-SELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:cd05923 450 TLSADELDQFCRaSELADFKRPRRYFFLDELPKNAMNK 487
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
173-683 |
1.05e-31 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 131.42 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 173 PRRDAASQPEPLVDVV--SLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIA 250
Cdd:PRK06155 7 GLAARAVDPLPPSERTlpAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 251 TIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEH-AHVAAAE-RVLPVEE--------------------LV 308
Cdd:PRK06155 87 VFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALlAALEAADpGDLPLPAvwlldapasvsvpagwstapLP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 309 ADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRM---WANYTQWQLRVASGVPGLRTLqfaPLSFDMAFQEIFSTL 385
Cdd:PRK06155 167 PLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQfywWGRNSAEDLEIGADDVLYTTL---PLFHTNALNAFFQAL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 386 CGGGELQLisnRERMDPSALLHVLERRQ--VQRVLLPFVA--LQRLAEASNalgvRPGALRVVVSSGEQLRITEDVRAFC 461
Cdd:PRK06155 244 LAGATYVL---EPRFSASGFWPAVRRHGatVTYLLGAMVSilLSQPARESD----RAHRVRVALGPGVPAALHAAFRERF 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 462 aampGLLLENQYGPTETHQVTYHSLSGDPAHYpdlppIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGD---CLARGYH 538
Cdd:PRK06155 317 ----GVDLLDGYGSTETNFVIAVTHGSQRPGS-----MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 539 RAPELTAErfvehPWRpgARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR 618
Cdd:PRK06155 388 GMPEKTVE-----AWR--NLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLL----SHPAVAAAAVFPV 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395399044 619 ERQ-GNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRALP 683
Cdd:PRK06155 457 PSElGEDEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQG 522
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
192-679 |
8.19e-31 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 128.05 E-value: 8.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 192 ERQVEALPGSAALAFEEQRWTYRDL-DHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYP 270
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLhEYVSKVAAYLIYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 271 AQRLALILETAQPFRVVAHPEHAHVAAA-------ERVLPVEEL--VADIEPETFAAPQLDELAMLLFTSGSTGRPKGVE 341
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNMALSmqkvsyvQRVISITSLkeIEDRKIDNFVEKNESASFIICYTSGTTGKPKGAV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 342 L-SHRMWANYTQWQLRVASGVPGlRTLQFAPLsFDMAFQEIFS--TLCGGGELQLisnRERMDPSALLHVLERRQVQRVL 418
Cdd:PRK06839 169 LtQENMFWNALNNTFAIDLTMHD-RSIVLLPL-FHIGGIGLFAfpTLFAGGVIIV---PRKFEPTKALSMIEKHKVTVVM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 419 LPFVALQRLAEASNALGVRPGALRVVVSSGEQLRItEDVRAFCAAmpGLLLENQYGPTETHQVTYHSLSGDPAHYPDlpP 498
Cdd:PRK06839 244 GVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPE-ELMREFIDR--GFLFGQGFGMTETSPTVFMLSEEDARRKVG--S 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 499 IGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERfVEHPWrpgarlYRTGDLGRILGNGEIVWLG 578
Cdd:PRK06839 319 IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW------LCTGDLARVDEDGFVYIVG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 579 RADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDL-AELKQALRSELPEHMVP 657
Cdd:PRK06839 392 RKKEMIISGGENIYPLEVEQVI----NKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIeKDVIEHCRLFLAKYKIP 467
|
490 500
....*....|....*....|..
gi 1395399044 658 AHFAWVDGFALTPSGKRDDAAL 679
Cdd:PRK06839 468 KEIVFLKELPKNATGKIQKAQL 489
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
187-673 |
8.73e-31 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 129.45 E-value: 8.73e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 187 VVSLFERQVEALPGSAALAF----EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVC 262
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 263 VPLDVSYPAQRLALILETAQP-FRVVAHPEHAHVAAA----------------------ERVLPVEELVAD----IEPET 315
Cdd:COG1022 93 VPIYPTSSAEEVAYILNDSGAkVLFVEDQEQLDKLLEvrdelpslrhivvldprglrddPRLLSLDELLALgrevADPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 316 F----AAPQLDELAMLLFTSGSTGRPKGVELSHRmwaNYTqWQLRVASGV----PGLRTLQFAPLS-------------- 373
Cdd:COG1022 173 LearrAAVKPDDLATIIYTSGTTGRPKGVMLTHR---NLL-SNARALLERlplgPGDRTLSFLPLAhvfertvsyyalaa 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 374 -FDMAFQEIFSTLcgGGELQLI-----------------SNRERMDPS--------------ALLHVLERRQVQRVLLPF 421
Cdd:COG1022 249 gATVAFAESPDTL--AEDLREVkptfmlavprvwekvyaGIQAKAEEAgglkrklfrwalavGRRYARARLAGKSPSLLL 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 422 VALQRLAEA------SNALGvrpGALRVVVSSGEQLRitEDVRAFCAAMpGLLLENQYGPTETHQVTyhslSGDPAHYPD 495
Cdd:COG1022 327 RLKHALADKlvfsklREALG---GRLRFAVSGGAALG--PELARFFRAL-GIPVLEGYGLTETSPVI----TVNRPGDNR 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 496 LPPIGRPLDGVEVQvldaalrpvpVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIV 575
Cdd:COG1022 397 IGTVGPPLPGVEVK----------IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGELDEDGFLR 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 576 WLGRA-DTQVKVRGFRIEPAEVELAIMR-----QA----ERQPGLrGAAVV--------ARERQGNDAFLAAFLLGEPEA 637
Cdd:COG1022 461 ITGRKkDLIVTSGGKNVAPQPIENALKAsplieQAvvvgDGRPFL-AALIVpdfealgeWAEENGLPYTSYAELAQDPEV 539
|
570 580 590 600
....*....|....*....|....*....|....*....|....
gi 1395399044 638 VDL--AELKQAlRSELPEHMVPAHFA-----W-VDGFALTPSGK 673
Cdd:COG1022 540 RALiqEEVDRA-NAGLSRAEQIKRFRllpkeFtIENGELTPTLK 582
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
207-638 |
2.12e-30 |
|
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: 125.79 E-value: 2.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 207 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPL-DVSYPAQrLALILETAQPfr 285
Cdd:cd05907 2 VWQPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIyPTSSAEQ-IAYILNDSEA-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 286 vvahpehahvaaaeRVLPVEELvadiepetfaapqlDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGvPGL 364
Cdd:cd05907 79 --------------KALFVEDP--------------DDLATIIYTSGTTGRPKGVMLSHRnILSNALALAERLPAT-EGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 365 RTLQFAPLS--FDMAFQEIFSTLCGG------GELQLISNRERMDPSALLhvlerrQVQRVLLPFVALQRLAEASNALG- 435
Cdd:cd05907 130 RHLSFLPLAhvFERRAGLYVPLLAGAriyfasSAETLLDDLSEVRPTVFL------AVPRVWEKVYAAIKVKAVPGLKRk 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 436 ----VRPGALRVVVSSGEqlRITEDVRAFCAAMpGLLLENQYGPTETHQVTyhslSGDPAHYPDLPPIGRPLDGVEVQvl 511
Cdd:cd05907 204 lfdlAVGGRLRFAASGGA--PLPAELLHFFRAL-GIPVYEGYGLTETSAVV----TLNPPGDNRIGTVGKPLPGVEVR-- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 512 daalrpvpVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRA-DTQVKVRGFR 590
Cdd:cd05907 275 --------IADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKkDLIITSGGKN 340
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1395399044 591 IEPAEVELAIMrqaeRQPGLRGAAVVARERqgndAFLAAFLLGEPEAV 638
Cdd:cd05907 341 ISPEPIENALK----ASPLISQAVVIGDGR----PFLVALIVPDPEAL 380
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
193-673 |
6.48e-30 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 126.02 E-value: 6.48e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 193 RQVEALPGSAALAFEE-QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPA 271
Cdd:PRK06087 31 QTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 272 QRLALILETAQP--------FRVVAH-----------PEHAHVAAAERVLP------VEELVADIEPETFAAP-QLDELA 325
Cdd:PRK06087 111 AELVWVLNKCQAkmffaptlFKQTRPvdlilplqnqlPQLQQIVGVDKLAPatsslsLSQIIADYEPLTTAITtHGDELA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 326 MLLFTSGSTGRPKGVELSHrmwaNYTQWQLRVASGVPGLRTLQF----APLSFDMAF-QEIFSTLCGGGELQLIsnrERM 400
Cdd:PRK06087 191 AVLFTSGTEGLPKGVMLTH----NNILASERAYCARLNLTWQDVfmmpAPLGHATGFlHGVTAPFLIGARSVLL---DIF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 401 DPSALLHVLERRQVQRVL--LPFV--ALQRLAEAsnalGVRPGALRVVVSSGEQlrITEDVrAFCAAMPGLLLENQYGPT 476
Cdd:PRK06087 264 TPDACLALLEQQRCTCMLgaTPFIydLLNLLEKQ----PADLSALRFFLCGGTT--IPKKV-ARECQQRGIKLLSVYGST 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 477 ETHQVTYHSLsGDPAHYpDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpg 556
Cdd:PRK06087 337 ESSPHAVVNL-DDPLSR-FMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGW--- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 557 arlYRTGDLGRILGNGEIVWLGRaDTQVKVRGFR-IEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGNDAFLAAFLLG 633
Cdd:PRK06087 412 ---YYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILL----QHPKIHDACVVAMpdERLGERSCAYVVLKA 483
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1395399044 634 EPEAVDLAELKQAL-RSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK06087 484 PHHSLTLEEVVAFFsRKRVAKYKYPEHIVVIDKLPRTASGK 524
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
199-681 |
7.93e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 125.48 E-value: 7.93e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGV-ALNRsPEMIATIWGILRAGLVCVPL----------DV 267
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALlSLNR-PEVLMAIGAAQLAGLRRTALhplgslddhaYV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 268 SYPAQRLALILEtAQPFRVVAHPEHAHVAAAERVL---PVEELV------ADIEPETFAAPQL-DELAMLLFTSGSTGRP 337
Cdd:PRK06188 105 LEDAGISTLIVD-PAPFVERALALLARVPSLKHVLtlgPVPDGVdllaaaAKFGPAPLVAAALpPDIAGLAYTGGTTGKP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 338 KGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSfDMAFQEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRV 417
Cdd:PRK06188 184 KGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLS-HAGGAFFLPTLLRGGTVIVL---AKFDPAEVLRAIEEQRITAT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 418 LLPFVALQRLAEAsnalgvrPGALRVVVSSGEQL----------RITEDVRAFcaampGLLLENQYGPTETHQVTYHSLS 487
Cdd:PRK06188 260 FLVPTMIYALLDH-------PDLRTRDLSSLETVyygaspmspvRLAEAIERF-----GPIFAQYYGQTEAPMVITYLRK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 488 GDpaHYPDLPPI----GRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFvEHPWrpgarlYRTG 563
Cdd:PRK06188 328 RD--HDPDDPKRltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGW------LHTG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 564 DLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGnDAFLAAFLLGEPEAVDLA 641
Cdd:PRK06188 399 DVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLA----EHPAVAQVAVigVPDEKWG-EAVTAVVVLRPGAAVDAA 473
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1395399044 642 ELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRA 681
Cdd:PRK06188 474 ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRA 513
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
209-680 |
1.81e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 123.76 E-value: 1.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 209 QRWTYRDLDH-VARCVATrLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPfRVV 287
Cdd:PRK09088 21 RRWTYAELDAlVGRLAAV-LRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEP-RLL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 288 AHpeHAHVAAAE-RVLPVEELVADI---EPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRmwanyTQWQLRVASGVPG 363
Cdd:PRK09088 99 LG--DDAVAAGRtDVEDLAAFIASAdalEPADTPSIPPERVSLILFTSGTSGQPKGVMLSER-----NLQQTAHNFGVLG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 364 L-----RTLQFAPLSFDMAF-QEIFSTLCGGGELQlISNRerMDPSALLHVLERRQVQrVLLPFVALQRLAEASNALGVR 437
Cdd:PRK09088 172 RvdahsSFLCDAPMFHIIGLiTSVRPVLAVGGSIL-VSNG--FEPKRTLGRLGDPALG-ITHYFCVPQMAQAFRAQPGFD 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 438 PGALR--VVVSSGEQLRITEDVRAFCAAmpGLLLENQYGPTETHqvTYHSLSGDPAHYPD-LPPIGRPLDGVEVQVLDAA 514
Cdd:PRK09088 248 AAALRhlTALFTGGAPHAAEDILGWLDD--GIPMVDGFGMSEAG--TVFGMSVDCDVIRAkAGAAGIPTPTVQTRVVDDQ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 515 LRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPA 594
Cdd:PRK09088 324 GNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGDIARRDADGFFWVVDRKKDMFISGGENVYPA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 595 EVELAIMrqaeRQPGLRGAAVV--ARERQGNDAFLAAfLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSG 672
Cdd:PRK09088 398 EIEAVLA----DHPGIRECAVVgmADAQWGEVGYLAI-VPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASG 472
|
....*...
gi 1395399044 673 KRDDAALR 680
Cdd:PRK09088 473 KLQKARLR 480
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
787-1051 |
3.71e-29 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 116.33 E-value: 3.71e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 787 PPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGSTPLAVLEDIAASYLAAIRRVQPEGPYYLGGWSFGGFVAY 866
Cdd:pfam00975 1 RPLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 867 EMARQLRALDPQaVAQLIVLDSITVDRNHAGsASDEALLLFFYWELVWFERSDEEVEPLPEGASLeqkldhiveraieag 946
Cdd:pfam00975 81 EVARRLERQGEA-VRSLFLSDASAPHTVRYE-ASRAPDDDEVVAEFTDEGGTPEELLEDEELLSM--------------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 947 vlpagtpratvqrLYELFRASWQALIGYRPEVSDQDMTLLRADGPLPLALKPMHDAagthygdpknGWQHWTSGRLDVID 1026
Cdd:pfam00975 144 -------------LLPALRADYRALESYSCPPLDAQSATLFYGSDDPLHDADDLAE----------WVRDHTPGEFDVHV 200
|
250 260
....*....|....*....|....*
gi 1395399044 1027 VPGDHLVLMKEPyvETVAAEIAALL 1051
Cdd:pfam00975 201 FDGDHFYLIEHL--EAVLEIIEAKL 223
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
208-602 |
3.81e-29 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 122.47 E-value: 3.81e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 208 EQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPfrvv 287
Cdd:cd17640 3 PKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSES---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 288 ahpehahVAaaervlpveeLVADIEPetfaapqlDELAMLLFTSGSTGRPKGVELSHRmwaNYTqWQLR----VASGVPG 363
Cdd:cd17640 79 -------VA----------LVVENDS--------DDLATIIYTSGTTGNPKGVMLTHA---NLL-HQIRslsdIVPPQPG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 364 LRTLQFAPL--SFDMAFqEIFSTLCGGGEL-----QLISNRERMDPSALLHV-------LERRQVQRVLLPFVAlQRLAE 429
Cdd:cd17640 130 DRFLSILPIwhSYERSA-EYFIFACGCSQAytsirTLKDDLKRVKPHYIVSVprlweslYSGIQKQVSKSSPIK-QFLFL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 430 ASnalgVRPGALRVVVSSGEQLRITEDvRAFCAAmpGLLLENQYGPTETHQVTYHSLSGDPAhypdLPPIGRPLDGVEVQ 509
Cdd:cd17640 208 FF----LSGGIFKFGISGGGALPPHVD-TFFEAI--GIEVLNGYGLTETSPVVSARRLKCNV----RGSVGRPLPGTEIK 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 510 VLDAALR-PVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRA-DTQVKVR 587
Cdd:cd17640 277 IVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAkDTIVLSN 350
|
410
....*....|....*
gi 1395399044 588 GFRIEPAEVELAIMR 602
Cdd:cd17640 351 GENVEPQPIEEALMR 365
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
211-684 |
5.98e-29 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 121.46 E-value: 5.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 211 WTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHP 290
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 291 EhahvaaaervlpveeLVADIEPETfaapqldeLAMLLFTSGSTGRPKGVELSHR-MWANY--TQWQLRV-------ASG 360
Cdd:cd05969 81 E---------------LYERTDPED--------PTLLHYTSGTTGTPKGVLHVHDaMIFYYftGKYVLDLhpddiywCTA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 361 VPGLRTLQFAPlsfdmafqeIFSTLCGGgeLQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVR--P 438
Cdd:cd05969 138 DPGWVTGTVYG---------IWAPWLNG--VTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKydL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 439 GALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETHQVTYhslsgdpAHYPDLP----PIGRPLDGVEVQVLDAA 514
Cdd:cd05969 207 SSLRFIHSVGEPL--NPEAIRWGMEVFGVPIHDTWWQTETGSIMI-------ANYPCMPikpgSMGKPLPGVKAAVVDEN 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 515 LRPVPVGVTGELYFGGD--CLARGYHRAPELTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIE 592
Cdd:cd05969 278 GNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDG-W------YLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 593 PAEVELAIMrqaeRQPGLRGAAVVARE----RQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFAL 668
Cdd:cd05969 351 PFEVESALM----EHPAVAEAGVIGKPdplrGEIIKAFISLKEGFEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPK 426
|
490
....*....|....*.
gi 1395399044 669 TPSGKRDDAALRALPL 684
Cdd:cd05969 427 TRSGKIMRRVLKAKEL 442
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
323-682 |
8.44e-29 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 118.20 E-value: 8.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 323 ELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGVPG--LRTLqfaPLSFDMAFQEIFSTLCGGGELQLISNRer 399
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAAnLLASAAGLHSRLGFGGGDswLLSL---PLYHVGGLAILVRSLLAGAELVLLERN-- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 400 mdpSALLHVLERRQVQRVLLPFVALQRLAEASNALGvRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLlenQYGPTET- 478
Cdd:cd17630 76 ---QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPA-ALKSLRAVLLGGAPIPPELLERAADRGIPLYT---TYGMTETa 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 479 HQVTYHSLSGdpahyPDLPPIGRPLDGVEVQVLDaalrpvpvgvTGELYFGGDCLARGYHRApeltaerfVEHPWRPGAR 558
Cdd:cd17630 149 SQVATKRPDG-----FGRGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRG--------QLVPEFNEDG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 559 LYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVArerQGNDAF---LAAFLLGEP 635
Cdd:cd17630 206 WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAAL----AAHPAVRDAFVVG---VPDEELgqrPVAVIVGRG 278
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1395399044 636 EaVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRAL 682
Cdd:cd17630 279 P-ADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
176-762 |
1.43e-28 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 124.90 E-value: 1.43e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 176 DAASQPEPLVDVVslfERQVEALPGSAALAF-----EEQR-WTYRDLDHVARCVATRLvRAGARRGDAIGVALNRSPEMI 249
Cdd:PRK05691 3 DAFELPLTLVQAL---QRRAAQTPDRLALRFladdpGEGVvLSYRDLDLRARTIAAAL-QARASFGDRAVLLFPSGPDYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 250 ATIWGILRAGLVCVPldvSYPAQ--------RLALILETAQPFRVV---------AHPEHAHVAAAERVLPVEELVADIe 312
Cdd:PRK05691 79 AAFFGCLYAGVIAVP---AYPPEsarrhhqeRLLSIIADAEPRLLLtvadlrdslLQMEELAAANAPELLCVDTLDPAL- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 313 PETFAAPQL--DELAMLLFTSGSTGRPKGVELSH-RMWANytQWQLRVASGV---PGLRTLQFAPLSFDMAF-----QEI 381
Cdd:PRK05691 155 AEAWQEPALqpDDIAFLQYTSGSTALPKGVQVSHgNLVAN--EQLIRHGFGIdlnPDDVIVSWLPLYHDMGLiggllQPI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 382 FS----------------------------TLCGGGELQLISNRERMDPSALlhvlERRQVQRVLLPFV--------ALQ 425
Cdd:PRK05691 233 FSgvpcvlmspayflerplrwleaiseyggTISGGPDFAYRLCSERVSESAL----ERLDLSRWRVAYSgsepirqdSLE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 426 RLAEASNALGVRPGALRVVVSSGE-QLRITEDVRAfcAAMPGLLLENQygptethqvtyhSLSGDPAHYPDLPPI---GR 501
Cdd:PRK05691 309 RFAEKFAACGFDPDSFFASYGLAEaTLFVSGGRRG--QGIPALELDAE------------ALARNRAEPGTGSVLmscGR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 502 PLDGVEVQVLDAA-LRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPwrpGARLYRTGDLGrILGNGEIVWLGRA 580
Cdd:PRK05691 375 SQPGHAVLIVDPQsLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVEHD---GRTWLRTGDLG-FLRDGELFVTGRL 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 581 DTQVKVRGFRIEPAEVELAIMRQAERQPGLRgAAVVARERQGNDAFLAAFLLGE--PEAVDLAELKQALRSELPE--HMV 656
Cdd:PRK05691 451 KDMLIVRGHNLYPQDIEKTVEREVEVVRKGR-VAAFAVNHQGEEGIGIAAEISRsvQKILPPQALIKSIRQAVAEacQEA 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 657 PAHFAWVDGFAL--TPSGKRDDAALRaLPLEHGTNIEY--------------LAPRDDYERTLAGLLGELLDRPRVGIRD 720
Cdd:PRK05691 530 PSVVLLLNPGALpkTSSGKLQRSACR-LRLADGSLDSYalfpalqaveaaqtAASGDELQARIAAIWCEQLKVEQVAADD 608
|
650 660 670 680
....*....|....*....|....*....|....*....|..
gi 1395399044 721 SFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLA 762
Cdd:PRK05691 609 HFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFS 650
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
204-600 |
6.01e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-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. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 118.70 E-value: 6.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 204 LAFEEQRWTYRDL-DHVARcVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQ 282
Cdd:cd05914 1 LYYGGEPLTYKDLaDNIAK-FALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 283 PFRVVAHPEhahvaaaervlpveelvadiepetfaapqlDELAMLLFTSGSTGRPKGVELSHR-MWANYTqWQLRVASGV 361
Cdd:cd05914 80 AKAIFVSDE------------------------------DDVALINYTSGTTGNSKGVMLTYRnIVSNVD-GVKEVVLLG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 362 PGLRTLQFAPLS--FDMAFQEIFSTLCGGGELQLisnrERMdPSALLHVLERRQVQ----------------RVLLPFVA 423
Cdd:cd05914 129 KGDKILSILPLHhiYPLTFTLLLPLLNGAHVVFL----DKI-PSAKIIALAFAQVTptlgvpvplviekifkMDIIPKLT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 424 L----QRLAEASNALGVRP-----------GALRVVVSSGEQL--RITEDVR--AFCAAMpglllenQYGPTETHQVtyh 484
Cdd:cd05914 204 LkkfkFKLAKKINNRKIRKlafkkvheafgGNIKEFVIGGAKInpDVEEFLRtiGFPYTI-------GYGMTETAPI--- 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 485 sLSGDPAHYPDLPPIGRPLDGVEVQVLDaalrPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGD 564
Cdd:cd05914 274 -ISYSPPNRIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGD 342
|
410 420 430
....*....|....*....|....*....|....*..
gi 1395399044 565 LGRILGNGEIVWLGRADTQ-VKVRGFRIEPAEVELAI 600
Cdd:cd05914 343 LGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKI 379
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
161-680 |
9.28e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 119.11 E-value: 9.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 161 HPDEAADFAFLAPRRDAASQpeplvdvvslFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGV 240
Cdd:PRK07786 3 ALTLAQEQPYLARRQNWVNQ----------LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLI 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 241 -ALNRsPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHVAAAER------------------- 300
Cdd:PRK07786 73 lMLNR-TEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAVRdivpllstvvvaggssdds 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 301 VLPVEELVAdiepETFAAPQL-----DELAMLLFTSGSTGRPKGVELSHrmwANYTqwqlrvASGVPGLRTLQF------ 369
Cdd:PRK07786 152 VLGYEDLLA----EAGPAHAPvdipnDSPALIMYTSGTTGRPKGAVLTH---ANLT------GQAMTCLRTNGAdinsdv 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 370 ----APLSFDMAFQEIFSTLCGGGELqLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGvRPGALRVVv 445
Cdd:PRK07786 219 gfvgVPLFHIAGIGSMLPGLLLGAPT-VIYPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQQARP-RDLALRVL- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 446 SSGEQLRITEDVRAFCAAMPGLLLENQYGPTETHQVTYhSLSGDPAhYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGE 525
Cdd:PRK07786 296 SWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTC-MLLGEDA-IRKLGSVGKVIPTVAARVVDENMNDVPVGEVGE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 526 LYFGGDCLARGYHRAPELTAERFvEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqae 605
Cdd:PRK07786 374 IVYRAPTLMSGYWNNPEATAEAF-AGGW------FHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLA---- 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395399044 606 RQPGLRGAAVVAR--ERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:PRK07786 443 SHPDIVEVAVIGRadEKWGEVPVAVAAVRNDDAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELR 519
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
199-673 |
1.18e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 118.56 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 278
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 279 ETAQPFRVVAHPEHAhvaaaERVLPVEELVADIEPETFAA------PQLDELA-MLLFTSGSTGRPKGVELSHRMWANYT 351
Cdd:PRK13383 129 RAHHISTVVADNEFA-----ERIAGADDAVAVIDPATAGAeesggrPAVAAPGrIVLLTSGTTGKPKGVPRAPQLRSAVG 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 352 QW-------QLRVASGVpGLRTLQFAPLSFDMafqeIFSTLCGGGElqlISNRERMDPSALLHVLERRQVQRVLLPFVAL 424
Cdd:PRK13383 204 VWvtildrtRLRTGSRI-SVAMPMFHGLGLGM----LMLTIALGGT---VLTHRHFDAEAALAQASLHRADAFTAVPVVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 425 QRLAEASNALGVRPG--ALRVVVSSGEQLRITEDVRaFCAAMpGLLLENQYGPTEthqVTYHSLSgDPAHYPDLP-PIGR 501
Cdd:PRK13383 276 ARILELPPRVRARNPlpQLRVVMSSGDRLDPTLGQR-FMDTY-GDILYNGYGSTE---VGIGALA-TPADLRDAPeTVGK 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 502 PLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRApelTAERFVEHpwrpgarLYRTGDLGRILGNGEIVWLGRAD 581
Cdd:PRK13383 350 PVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDG---GGKAVVDG-------MTSTGDMGYLDNAGRLFIVGRED 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 582 TQVKVRGFRIEPAEVELAImrqaERQPGLRGAAV--VARERQGNDafLAAFLLGEPEA-VDLAELKQALRSELPEHMVPA 658
Cdd:PRK13383 420 DMIISGGENVYPRAVENAL----AAHPAVADNAVigVPDERFGHR--LAAFVVLHPGSgVDAAQLRDYLKDRVSRFEQPR 493
|
490
....*....|....*
gi 1395399044 659 HFAWVDGFALTPSGK 673
Cdd:PRK13383 494 DINIVSSIPRNPTGK 508
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
210-680 |
1.23e-27 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation 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. The 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. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 118.50 E-value: 1.23e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 210 RWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALI------------ 277
Cdd:cd12119 25 RYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIinhaedrvvfvd 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 278 -------------LETAQPFRVVAHPEHAHVAAAERVLPVEELVADiEPETFAAPQLDE--LAMLLFTSGSTGRPKGVEL 342
Cdd:cd12119 105 rdflplleaiaprLPTVEHVVVMTDDAAMPEPAGVGVLAYEELLAA-ESPEYDWPDFDEntAAAICYTSGTTGNPKGVVY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 343 SHRmwANYTQWQLRVASGVPGLRT----LQFAPLSFDMAFQEIFSTLCGGGELQLISnrERMDPSALLHVLERRQVQRVL 418
Cdd:cd12119 184 SHR--SLVLHAMAALLTDGLGLSEsdvvLPVVPMFHVNAWGLPYAAAMVGAKLVLPG--PYLDPASLAELIEREGVTFAA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 419 -LPFVALQRLAEASnALGVRPGALRVVVSSGeqlritedvrafcAAMPGLLLE----------NQYGPTETHQVTyhSLS 487
Cdd:cd12119 260 gVPTVWQGLLDHLE-ANGRDLSSLRRVVIGG-------------SAVPRSLIEafeergvrviHAWGMTETSPLG--TVA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 488 GDPAHYPDLPP---------IGRPLDGVEVQVLDAALRPVPV-GVT-GELYFGGDCLARGYHRAPElTAERFVEHPWrpg 556
Cdd:cd12119 324 RPPSEHSNLSEdeqlalrakQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDE-ESEALTEDGW--- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 557 arlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR------ERQgndafLAAF 630
Cdd:cd12119 400 ---LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIM----AHPAVAEAAVIGVphpkwgERP-----LAVV 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1395399044 631 LLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:cd12119 468 VLKEGATVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKALR 517
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
191-687 |
2.82e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 117.45 E-value: 2.82e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 191 FERQVEA-LPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 269
Cdd:PRK07470 12 FLRQAARrFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQ 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 270 PAQRLALILETAQPFRVVAH---PEHAhvAAAERVLPVEELVADIEPETF------------------AAPQLDELAMLL 328
Cdd:PRK07470 92 TPDEVAYLAEASGARAMICHadfPEHA--AAVRAASPDLTHVVAIGGARAgldyealvarhlgarvanAAVDHDDPCWFF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 329 FTSGSTGRPKGVELSHRMWA----NytqwqlRVASGVPGL----RTLQFAPLSFDMAFQEIFSTLCGGGELQLISnrERM 400
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMAfvitN------HLADLMPGTteqdASLVVAPLSHGAGIHQLCQVARGAATVLLPS--ERF 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 401 DPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRITEDVRAFcaAMPGLLLENQYGPTE-TH 479
Cdd:PRK07470 242 DPAEVWALVERHRVTNLFTVPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRAL--AKLGKVLVQYFGLGEvTG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 480 QVT-----YHSLSGDPAhyPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVeHPWr 554
Cdd:PRK07470 320 NITvlppaLHDAEDGPD--ARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR-DGW- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 555 pgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGnDAFLAAFLL 632
Cdd:PRK07470 396 -----FRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLL----THPAVSEVAVlgVPDPVWG-EVGVAVCVA 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1395399044 633 GEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRALPLEHG 687
Cdd:PRK07470 466 RDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEERG 520
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
207-617 |
3.12e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 117.79 E-value: 3.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 207 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAG--LVCVPldvsYPAQRLALILETAQPF 284
Cdd:PRK07768 26 APVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGasLTMLH----QPTPRTDLAVWAEDTL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 285 RVVAHPEHAHV-------AAAE-------RVLPVEELVADIEPETFAAPQlDELAMLLFTSGSTGRPKGVELSHR-MWAN 349
Cdd:PRK07768 102 RVIGMIGAKAVvvgepflAAAPvleekgiRVLTVADLLAADPIDPVETGE-DDLALMQLTSGSTGSPKAVQITHGnLYAN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 350 ----YTQWQLRVASGVpglrTLQFAPLSFDMAFQEIFST-LCGGGELQLISNRERM-DPSALLHVLERRQVQRVLLP-F- 421
Cdd:PRK07768 181 aeamFVAAEFDVETDV----MVSWLPLFHDMGMVGFLTVpMYFGAELVKVTPMDFLrDPLLWAELISKYRGTMTAAPnFa 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 422 --VALQRLAEASNALGVRPGALRVVVSSGEQLRITeDVRAFCAA-----MPGLLLENQYGPTET----------HQVTYH 484
Cdd:PRK07768 257 yaLLARRLRRQAKPGAFDLSSLRFALNGAEPIDPA-DVEDLLDAgarfgLRPEAILPAYGMAEAtlavsfspcgAGLVVD 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 485 SLSGD---------PAHYPD---LPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYhrapeLTAERFV--- 549
Cdd:PRK07768 336 EVDADllaalrravPATKGNtrrLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIpaq 410
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395399044 550 -EHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVA 617
Cdd:PRK07768 411 dADGW------LDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE----RAAARVEGVRPGNAVA 469
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
173-685 |
7.32e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 116.38 E-value: 7.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 173 PRRDAASQPEPLVdvvSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATI 252
Cdd:PRK06164 1 TPHDAAPRADTLA---SLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 253 WGILRAGLVCVPLDVSYPAQRLALILETAQP--------------FRVVAHPEHAHVAAAERVLPVEELVADIEPETFAA 318
Cdd:PRK06164 78 LACARLGATVIAVNTRYRSHEVAHILGRGRArwlvvwpgfkgidfAAILAAVPPDALPPLRAIAVVDDAADATPAPAPGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 319 P--------------------QLDELAMLLFTSGSTGRPKGVELSHRMWANYTqWQLRVASGV-PGLRTLQFAPLSFDMA 377
Cdd:PRK06164 158 RvqlfalpdpappaaageraaDPDAGALLFTTSGTTSGPKLVLHRQATLLRHA-RAIARAYGYdPGAVLLAALPFCGVFG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 378 FQEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPgALRVVVSSGEQLRITEDV 457
Cdd:PRK06164 237 FSTLLGALAGGAPLVCE---PVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFP-SARLFGFASFAPALGELA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 458 RAFCAAmpGLLLENQYGPTETHQ-VTYHSLSGDPAHYPDlpPIGRPLDG-VEVQVLDAALRPV-PVGVTGELYFGGDCLA 534
Cdd:PRK06164 313 ALARAR--GVPLTGLYGSSEVQAlVALQPATDPVSVRIE--GGGRPASPeARVRARDPQDGALlPDGESGEIEIRAPSLM 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 535 RGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAA 614
Cdd:PRK06164 389 RGYLDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHAL----EALPGVAAAQ 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1395399044 615 VVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSG---KRDDAALRALPLE 685
Cdd:PRK06164 459 VVGATRDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQA 532
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
199-617 |
2.36e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 115.06 E-value: 2.36e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRA-GARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD----------- 266
Cdd:PRK08314 24 PDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNpmnreeelahy 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 267 -------VSYPAQRLALILETAQPFRVVAH----------PEHAHVAAAERVLPVEELVADIEP------ETFAAPQL-- 321
Cdd:PRK08314 104 vtdsgarVAIVGSELAPKVAPAVGNLRLRHvivaqysdylPAEPEIAVPAWLRAEPPLQALAPGgvvawkEALAAGLApp 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 322 ------DELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVaSGVPGLRTLQFAPLSFDMAFQE-IFSTLCGGGELQL 393
Cdd:PRK08314 184 phtagpDDLAVLPYTSGTTGVPKGCMHTHRtVMANAVGSVLWS-NSTPESVVLAVLPLFHVTGMVHsMNAPIYAGATVVL 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 394 ISnreRMDPSALLHVLERRQVQR------VLLPFVALQRLAEASNAlgvrpgALRVVVSSGeqlritedvrafcAAMP-- 465
Cdd:PRK08314 263 MP---RWDREAAARLIERYRVTHwtniptMVVDFLASPGLAERDLS------SLRYIGGGG-------------AAMPea 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 466 ---------GLLLENQYGPTETHQVTyHSlsgDPAHYPDLPPIGRPLDGVEVQVLDAA-LRPVPVGVTGELYFGGDCLAR 535
Cdd:PRK08314 321 vaerlkeltGLDYVEGYGLTETMAQT-HS---NPPDRPKLQCLGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 536 GYHRAPELTAERFVEhpwRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElAIMRqaeRQPGLRGAAV 615
Cdd:PRK08314 397 GYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVE-NLLY---KHPAIQEACV 469
|
..
gi 1395399044 616 VA 617
Cdd:PRK08314 470 IA 471
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
325-673 |
4.93e-26 |
|
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: 110.43 E-value: 4.93e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 325 AMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGelQLISNRERMDPS 403
Cdd:cd17635 4 LAVIFTSGTTGEPKAVLLANKtFFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGG--LCVTGGENTTYK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 404 ALLHVLERRQVQRVLLPFVALQRLA-EASNALGVRPgALRVVVSSGEqlRITEDVRAFCAAMPGLLLENQYGPTETHQVT 482
Cdd:cd17635 82 SLFKILTTNAVTTTCLVPTLLSKLVsELKSANATVP-SLRLIGYGGS--RAIAADVRFIEATGLTNTAQVYGLSETGTAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 483 YHSLSGDPAhypDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHpWrpgarlYRT 562
Cdd:cd17635 159 CLPTDDDSI---EINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG-W------VNT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 563 GDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAV--VARERQGNDAFLAAFLLGEPEAVDL 640
Cdd:cd17635 229 GDLGERREDGFLFITGRSSESINCGGVKIAPDEVE----RIAEGVSGVQECACyeISDEEFGELVGLAVVASAELDENAI 304
|
330 340 350
....*....|....*....|....*....|...
gi 1395399044 641 AELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:cd17635 305 RALKHTIRRELEPYARPSTIVIVTDIPRTQSGK 337
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
203-680 |
8.13e-26 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 111.80 E-value: 8.13e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 203 ALAFEEQRWTYRDLDHVARCVATRLVRA-GARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETA 281
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLVGElGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 282 QPfrvvahpehAHVAAAERVLPVeelvadiepetfaapqlDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASG 360
Cdd:cd05958 83 RI---------TVALCAHALTAS-----------------DDICILAFTSGTTGAPKATMHFHRdPLASADRYAVNVLRL 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 361 VPGLRTLQFAPLSFDMAF--QEIFSTLCGGGELQLisnrERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRP 438
Cdd:cd05958 137 REDDRFVGSPPLAFTFGLggVLLFPFGVGASGVLL----EEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 439 GALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETHQVTyhsLSGDPAhypDLPP--IGRPLDGVEVQVLDAALR 516
Cdd:cd05958 213 SSLRKCVSAGEAL--PAALHRAWKEATGIPIIDGIGSTEMFHIF---ISARPG---DARPgaTGKPVPGYEAKVVDDEGN 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 517 PVPVGVTGELYFGGDClarGYHRAPELTAERFVEHPWRPgarlyrTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEV 596
Cdd:cd05958 285 PVPDGTIGRLAVRGPT---GCRYLADKRQRTYVQGGWNI------TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 597 ELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEPE----AVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSG 672
Cdd:cd05958 356 EDVLL----QHPAVAECAVVGHPDESRGVVVKAFVVLRPGvipgPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATG 431
|
....*...
gi 1395399044 673 KRDDAALR 680
Cdd:cd05958 432 KLQRFALR 439
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
199-673 |
1.17e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 112.71 E-value: 1.17e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 278
Cdd:PRK07788 63 PDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 279 ETAQPFRVVAHPEHAHVAAA-----ERVLPVEELVADIEPETFAAPQLDELA----------------MLLFTSGSTGRP 337
Cdd:PRK07788 143 AREGVKALVYDDEFTDLLSAlppdlGRLRAWGGNPDDDEPSGSTDETLDDLIagsstaplpkppkpggIVILTSGTTGTP 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 338 KGVELSHrmwanytqwqlrvasgVPGLRTL-QF---APLSFDMAFQ---EIFSTLcGGGELQLISN-------RERMDPS 403
Cdd:PRK07788 223 KGAPRPE----------------PSPLAPLaGLlsrVPFRAGETTLlpaPMFHAT-GWAHLTLAMAlgstvvlRRRFDPE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 404 ALLHVLERRQVQRVLLPFVALQRLAEASNALGVRP--GALRVVVSSGEQLRiTEDVRAFCAAMpGLLLENQYGPTETHQV 481
Cdd:PRK07788 286 ATLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYdtSSLKIIFVSGSALS-PELATRALEAF-GPVLYNLYGSTEVAFA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 482 TY---HSLSGDPAhypdlpPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYhrapelTAERfveHPWRPGAr 558
Cdd:PRK07788 364 TIatpEDLAEAPG------TVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR---DKQIIDG- 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 559 LYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEP-EA 637
Cdd:PRK07788 428 LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLL----AGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPgAA 503
|
490 500 510
....*....|....*....|....*....|....*.
gi 1395399044 638 VDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK07788 504 LDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGK 539
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
209-597 |
1.32e-25 |
|
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: 112.33 E-value: 1.32e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 209 QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVA 288
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 289 HPEHAH--VAAAERVLPVEELVAD---IEPETFAAPQL---------DELAMLLFTSGSTGRPKGVELSHR-MWANYTQW 353
Cdd:cd05904 111 TAELAEklASLALPVVLLDSAEFDslsFSDLLFEADEAeppvvvikqDDVAALLYSSGTTGRSKGVMLTHRnLIAMVAQF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 354 QLRVASGVPGL-RTLQFAPLSFDMAFQEIFSTLCGGGELQLIsnRERMDPSALLHVLERRQVQRvlLPFVALQRLAEASN 432
Cdd:cd05904 191 VAGEGSNSDSEdVFLCVLPMFHIYGLSSFALGLLRLGATVVV--MPRFDLEELLAAIERYKVTH--LPVVPPIVLALVKS 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 433 ALGV--RPGALRVVVSSGEQLRItEDVRAFCAAMPGLLLENQYGPTE-THQVTYHSL-SGDPAHYPDlppIGRPLDGVEV 508
Cdd:cd05904 267 PIVDkyDLSSLRQIMSGAAPLGK-ELIEAFRAKFPNVDLGQGYGMTEsTGVVAMCFApEKDRAKYGS---VGRLVPNVEA 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 509 QVLD-AALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVR 587
Cdd:cd05904 343 KIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW------LHTGDLCYIDEDGYLFIVDRLKELIKYK 416
|
410
....*....|
gi 1395399044 588 GFRIEPAEVE 597
Cdd:cd05904 417 GFQVAPAELE 426
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
170-680 |
1.50e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 112.45 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 170 FLAPRRDAAS-----QPEPLVDvvsLFERQVEALPGSAALA------FEEQRWTYRDLDHVARCVATRLVRAGARRGDAI 238
Cdd:PRK13295 7 LLPPRRAASIaaghwHDRTIND---DLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 239 GVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQP--------FRVVAHPEHA-----------HVAAA- 298
Cdd:PRK13295 84 SCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESkvlvvpktFRGFDHAAMArrlrpelpalrHVVVVg 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 299 -------ERVL--PVEELVADIePETFAAPQL--DELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVasgvpGLRT 366
Cdd:PRK13295 164 gdgadsfEALLitPAWEQEPDA-PAILARLRPgpDDVTQLIYTSGTTGEPKGVMHTANtLMANIVPYAERL-----GLGA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 367 LQFAPLSFDMAFQEIFstlcGGGELQLISNRERM------DPSALLHVLERRQVQRVL--LPFvaLQRLAEASNALGVRP 438
Cdd:PRK13295 238 DDVILMASPMAHQTGF----MYGLMMPVMLGATAvlqdiwDPARAAELIRTEGVTFTMasTPF--LTDLTRAVKESGRPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 439 GALRVVVSSGEQL--RITEDVRAFCaampGLLLENQYGPTETHQVTYHSLSGDP--AHYPDlppiGRPLDGVEVQVLDAA 514
Cdd:PRK13295 312 SSLRTFLCAGAPIpgALVERARAAL----GAKIVSAWGMTENGAVTLTKLDDPDerASTTD----GCPLPGVEVRVVDAD 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 515 LRPVPVGVTGELYFGGDCLARGYHRAPELTAERFveHPWrpgarlYRTGDLGRILGNGEIVWLGRAdTQVKVRGFR-IEP 593
Cdd:PRK13295 384 GAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA--DGW------FDTGDLARIDADGYIRISGRS-KDVIIRGGEnIPV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 594 AEVELAIMrqaeRQPGLRGAAVVA--RERQGNDAflAAFLLGEP-EAVDLAELKQALRSE-LPEHMVPAHFAWVDGFALT 669
Cdd:PRK13295 455 VEIEALLY----RHPAIAQVAIVAypDERLGERA--CAFVVPRPgQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRT 528
|
570
....*....|.
gi 1395399044 670 PSGKRDDAALR 680
Cdd:PRK13295 529 PSGKIQKFRLR 539
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
327-675 |
2.06e-25 |
|
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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 109.39 E-value: 2.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 327 LLFTSGSTGRPKGVELSH----RMWAN----------YTQWQLRVASGVPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQ 392
Cdd:cd05924 8 ILYTGGTTGMPKGVMWRQedifRMLMGgadfgtgeftPSEDAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 393 LIsnRERMDPSALLHVLERRQVQRVLLPFVALQR-LAEASNALGVRP-GALRVVVSSGEQLriTEDVR-AFCAAMPGLLL 469
Cdd:cd05924 88 LP--DDRFDPEEVWRTIEKHKVTSMTIVGDAMARpLIDALRDAGPYDlSSLFAISSGGALL--SPEVKqGLLELVPNITL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 470 ENQYGPTET-HQVTYHSLSGDPAHYPdlppigRPLDGVEVQVLDAALRPVPVGVTGELYFG-GDCLARGYHRAPELTAER 547
Cdd:cd05924 164 VDAFGSSETgFTGSGHSAGSGPETGP------FTRANPDTVVLDDDGRVVPPGSGGVGWIArRGHIPLGYYGDEAKTAET 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 548 FVEhpwRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVAR--ERQGNDa 625
Cdd:cd05924 238 FPE---VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEAL----KSHPAVYDVLVVGRpdERWGQE- 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 1395399044 626 fLAAFL-LGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 675
Cdd:cd05924 310 -VVAVVqLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
202-673 |
2.39e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 111.53 E-value: 2.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 202 AALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETA 281
Cdd:PRK08276 3 VIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 282 QPFRVVAHP---EHAHVAAAERVLPVEELVADIEPETFAAPQLDELA--------------MLLFTSGSTGRPKGV--EL 342
Cdd:PRK08276 83 GAKVLIVSAalaDTAAELAAELPAGVPLLLVVAGPVPGFRSYEEALAaqpdtpiadetagaDMLYSSGTTGRPKGIkrPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 343 SHR---MWANYTQWQL-RVASGVPGLRTL------QFAPLSFDMafqeifSTLCGGGELQLIsnrERMDPSALLHVLERR 412
Cdd:PRK08276 163 PGLdpdEAPGMMLALLgFGMYGGPDSVYLspaplyHTAPLRFGM------SALALGGTVVVM---EKFDAEEALALIERY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 413 QV---QRVLLPFVALQRLAEAsnalgVRPgalRVVVSSgeqLRitedvRAFCAAMP-------------GLLLENQYGPT 476
Cdd:PRK08276 234 RVthsQLVPTMFVRMLKLPEE-----VRA---RYDVSS---LR-----VAIHAAAPcpvevkramidwwGPIIHEYYASS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 477 ETHQVTYHSlSGDPAHYPDlpPIGRPLDGvEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpg 556
Cdd:PRK08276 298 EGGGVTVIT-SEDWLAHPG--SVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGW--- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 557 arlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGND--AFLAAFLL 632
Cdd:PRK08276 371 ---VTVGDVGYLDEDGYLYLTDRKSDMIISGGVNIYPQEIENLLV----THPKVADVAVfgVPDEEMGERvkAVVQPADG 443
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1395399044 633 GEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK08276 444 ADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGK 484
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
187-679 |
3.38e-25 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 111.13 E-value: 3.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 187 VVSLFERQVEALPGSAALAFEEQRW--TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVP 264
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVTADRIaiSYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 265 LDVSYPA--QRLALILETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQLD-------------------E 323
Cdd:PRK05852 98 LDPALPIaeQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTLSVHldaateptpatstpeglrpD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 324 LAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAF-QEIFSTLCGGGELqLISNRER--- 399
Cdd:PRK05852 178 DAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLiAALLATLASGGAV-LLPARGRfsa 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 400 ------MDPSALLHVLERRQVQRVLLPFVALQRLAEASNALG-VRPGALRVVVSSGEQLRITEDVRAFCAampglllenq 472
Cdd:PRK05852 257 htfwddIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRfIRSCSAPLTAETAQALQTEFAAPVVCA---------- 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 473 YGPTE-THQVTYHSLSG-DPAHYPDLP--PIGRPlDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERF 548
Cdd:PRK05852 327 FGMTEaTHQVTTTQIEGiGQTENPVVStgLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 549 VeHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAVVARERQG-NDAFL 627
Cdd:PRK05852 406 T-DGW------LRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVL----ASHPNVMEAAVFGVPDQLyGEAVA 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1395399044 628 AAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAAL 679
Cdd:PRK05852 475 AVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
199-681 |
3.54e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 110.75 E-value: 3.54e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 278
Cdd:PRK06145 16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 279 ETAQPFRVVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQL----------DELAMLLFTSGSTGRPKGVELSHR--M 346
Cdd:PRK06145 96 GDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLeippqaavapTDLVRLMYTSGTTDRPKGVMHSYGnlH 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 347 WANYTQwqlRVASGVPG-LRTLQFAPLSFDMAFQ-EIFSTLCGGGELQLISNrerMDPSALLHVLERRQVQRVLLPFVAL 424
Cdd:PRK06145 176 WKSIDH---VIALGLTAsERLLVVGPLYHVGAFDlPGIAVLWVGGTLRIHRE---FDPEAVLAAIERHRLTCAWMAPVML 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 425 QRLAEASNALGVRPGALRVVVSSGE---QLRItedvRAFCAAMPGLLLENQYGPTEThqVTYHSLSGDPAHYPDLPPIGR 501
Cdd:PRK06145 250 SRVLTVPDRDRFDLDSLAWCIGGGEktpESRI----RDFTRVFTRARYIDAYGLTET--CSGDTLMEAGREIEKIGSTGR 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 502 PLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRAD 581
Cdd:PRK06145 324 ALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-W------FRSGDVGYLDEEGFLYLTDRKK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 582 TQVKVRGFRIEPAEVELAIMRQAErqpgLRGAAVV-ARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHF 660
Cdd:PRK06145 397 DMIISGGENIASSEVERVIYELPE----VAEAAVIgVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQL 472
|
490 500
....*....|....*....|.
gi 1395399044 661 AWVDGFALTPSGKRDDAALRA 681
Cdd:PRK06145 473 KVRDELPRNPSGKVLKRVLRD 493
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
193-673 |
1.45e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 109.25 E-value: 1.45e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 193 RQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQ 272
Cdd:PRK08316 19 RSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 273 RLALILETAQPFRVVAHPEHA-HVAAAERVLPVEELVADI--------------------EPETFAAPQLDE--LAMLLF 329
Cdd:PRK08316 99 ELAYILDHSGARAFLVDPALApTAEAALALLPVDTLILSLvlggreapggwldfadwaeaGSVAEPDVELADddLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 330 TSGSTGRPKGVELSHR--MWanytQWQLRVASG--VPGLRTLQFAPLsFDMAFQEIF---STLCGGGELQLisnrERMDP 402
Cdd:PRK08316 179 TSGTESLPKGAMLTHRalIA----EYVSCIVAGdmSADDIPLHALPL-YHCAQLDVFlgpYLYVGATNVIL----DAPDP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 403 SALLHVLERRQVQRVLLP---FVALQRlaeasnalgvRPGALRVVVSSgeqLR------------ITEDVRafcAAMPGL 467
Cdd:PRK08316 250 ELILRTIEAERITSFFAPptvWISLLR----------HPDFDTRDLSS---LRkgyygasimpveVLKELR---ERLPGL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 468 LLENQYGPTEThqVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAER 547
Cdd:PRK08316 314 RFYNCYGQTEI--APLATVLGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 548 FvEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVA--RERQGnDA 625
Cdd:PRK08316 392 F-RGGW------FHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALY----THPAVAEVAVIGlpDPKWI-EA 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1395399044 626 FLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK08316 460 VTAVVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGK 507
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
172-685 |
1.47e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 109.48 E-value: 1.47e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 172 APRRDAASQPEPLVD--VVSLFERQVEALPGSAALAFEEQ--RWTYRDL-DHVARcVATRLVRAGARRGDAIGVALNRSP 246
Cdd:PRK12583 3 QPSYYQGGGDKPLLTqtIGDAFDATVARFPDREALVVRHQalRYTWRQLaDAVDR-LARGLLALGVQPGDRVGIWAPNCA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 247 EMIATIWGILRAGLVCVPLDVSYPAQRLALILE--------TAQPFR---------------------VVAHPEHAH--- 294
Cdd:PRK12583 82 EWLLTQFATARIGAILVNINPAYRASELEYALGqsgvrwviCADAFKtsdyhamlqellpglaegqpgALACERLPElrg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 295 -----VAAAERVLPVEELVAdiEPETFAAPQLDELAM---------LLFTSGSTGRPKGVELSHRMWANyTQWQLRVASG 360
Cdd:PRK12583 162 vvslaPAPPPGFLAWHELQA--RGETVSREALAERQAsldrddpinIQYTSGTTGFPKGATLSHHNILN-NGYFVAESLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 361 VPGLRTLqFAPLSFDMAFQEIFSTL-CGGGELQLISNRERMDPSALLHVLERRQ---VQRVLLPFVAL----QRLAEASN 432
Cdd:PRK12583 239 LTEHDRL-CVPVPLYHCFGMVLANLgCMTVGACLVYPNEAFDPLATLQAVEEERctaLYGVPTMFIAEldhpQRGNFDLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 433 AL--GVRPGA--LRVVVSsgeqlRITEDVRafcaaMPGLLLenQYGPTETHQVTYHSLSGDPAHYpDLPPIGRPLDGVEV 508
Cdd:PRK12583 318 SLrtGIMAGApcPIEVMR-----RVMDEMH-----MAEVQI--AYGMTETSPVSLQTTAADDLER-RVETVGRTQPHLEV 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 509 QVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRG 588
Cdd:PRK12583 385 KVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW------MHTGDLATMDEQGYVRIVGRSKDMIIRGG 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 589 FRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGNDafLAAFLLGEP-EAVDLAELKQALRSELPEHMVPAHFAWVDG 665
Cdd:PRK12583 459 ENIYPREIEEFLF----THPAVADVQVfgVPDEKYGEE--IVAWVRLHPgHAASEEELREFCKARIAHFKVPRYFRFVDE 532
|
570 580
....*....|....*....|
gi 1395399044 666 FALTPSGKRDDAALRALPLE 685
Cdd:PRK12583 533 FPMTVTGKVQKFRMREISIE 552
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
186-680 |
3.30e-24 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 108.35 E-value: 3.30e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 186 DVVslfERQVEALPGSAALAF-----EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGL 260
Cdd:cd05970 21 DVV---DAMAKEYPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 261 VCVPLDVSYPAQRLALILETAQPFRVVAH-----PEHAHVAAAE-RVLPVEELVADIEPETF---------AAPQL---- 321
Cdd:cd05970 98 IAIPATHQLTAKDIVYRIESADIKMIVAIaedniPEEIEKAAPEcPSKPKLVWVGDPVPEGWidfrkliknASPDFerpt 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 322 -------DELAMLLFTSGSTGRPKGVE------LSHRMWANYtqWQ-LRvasgvPGLRTLQFAPLSFDMA-FQEIFSTLC 386
Cdd:cd05970 178 ansypcgEDILLVYFSSGTTGMPKMVEhdftypLGHIVTAKY--WQnVR-----EGGLHLTVADTGWGKAvWGKIYGQWI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 387 GGGELqLISNRERMDPSALLHVLERRQVQRVLLP-----FVALQRLAEASNAlgvrpgALRVVVSSGEQLriTEDVRAFC 461
Cdd:cd05970 251 AGAAV-FVYDYDKFDPKALLEKLSKYGVTTFCAPptiyrFLIREDLSRYDLS------SLRYCTTAGEAL--NPEVFNTF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 462 AAMPGLLLENQYGPTEThQVTYHSLsgdPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELY--------FGgdcL 533
Cdd:cd05970 322 KEKTGIKLMEGFGQTET-TLTIATF---PWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVirtskgkpVG---L 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 534 ARGYHRAPELTAErfvehPWRPGarLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGA 613
Cdd:cd05970 395 FGGYYKDAEKTAE-----VWHDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALI----QHPAVLEC 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395399044 614 AV--VARERQGNdAFLAAFLLGEPeavdlAELKQALRSELPEHM--------VPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:cd05970 464 AVtgVPDPIRGQ-VVKATIVLAKG-----YEPSEELKKELQDHVkkvtapykYPRIVEFVDELPKTISGKIRRVEIR 534
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
189-673 |
9.29e-24 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation 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. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 106.23 E-value: 9.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 189 SLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVS 268
Cdd:cd12118 8 SFLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTR 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 269 YPAQRLALILETAQPFRVVAHPEHAHvaaaervlpvEELVADIEPETFAAPQLDELAM--LLFTSGSTGRPKGVELSHR- 345
Cdd:cd12118 88 LDAEEIAFILRHSEAKVLFVDREFEY----------EDLLAEGDPDFEWIPPADEWDPiaLNYTSGTTGRPKGVVYHHRg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 346 ----MWANYTQWQLRVAS------------------GVPG-------LRTLQfAPLSFDMAFQEIFSTLCGGGE-LQLIS 395
Cdd:cd12118 158 aylnALANILEWEMKQHPvylwtlpmfhcngwcfpwTVAAvggtnvcLRKVD-AKAIYDLIEKHKVTHFCGAPTvLNMLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 396 NrerMDPSALLHVLERRQVQR--VLLPFVALQRLaeasNALGvrpgaLRVVVSSGeqLRITEDVRAFCAAMP---GLLLE 470
Cdd:cd12118 237 N---APPSDARPLPHRVHVMTagAPPPAAVLAKM----EELG-----FDVTHVYG--LTETYGPATVCAWKPewdELPTE 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 471 NQYGPTETHQVTYHSLSgdpahypdlppigrpldgvEVQVLDAA-LRPVPV-GVT-GELYFGGDCLARGYHRAPELTAER 547
Cdd:cd12118 303 ERARLKARQGVRYVGLE-------------------EVDVLDPEtMKPVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEA 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 548 FvEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGND- 624
Cdd:cd12118 364 F-RGGW------FHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLY----KHPAVLEAAVVARpdEKWGEVp 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1395399044 625 -AFLAaflLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDgFALTPSGK 673
Cdd:cd12118 433 cAFVE---LKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGK 478
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
203-680 |
1.50e-23 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 105.92 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 203 ALAFEE-----QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALI 277
Cdd:PRK08008 25 ALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 278 LETAQPFRVVAHPEHA---------------HVAAAERVLPVEELVADIE-------PETFAAPQL--DELAMLLFTSGS 333
Cdd:PRK08008 105 LQNSQASLLVTSAQFYpmyrqiqqedatplrHICLTRVALPADDGVSSFTqlkaqqpATLCYAPPLstDDTAEILFTSGT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 334 TGRPKGVELSH---RMWANYTQWQ--LRVASgvpglRTLQFAPlSFDMAFQ-----EIFSTlcgGGELQLIsnrERMDPS 403
Cdd:PRK08008 185 TSRPKGVVITHynlRFAGYYSAWQcaLRDDD-----VYLTVMP-AFHIDCQctaamAAFSA---GATFVLL---EKYSAR 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 404 ALLhvlerRQVQR----------VLLPFVALQRLAEASnalgvRPGALRVV-----VSSGEQLritedvrAFCAAMpGLL 468
Cdd:PRK08008 253 AFW-----GQVCKyratitecipMMIRTLMVQPPSAND-----RQHCLREVmfylnLSDQEKD-------AFEERF-GVR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 469 LENQYGPTETHQVTYHSLSGDPAHYPDlppIGRPLDGVEVQVLDAALRPVPVGVTGELYFG---GDCLARGYHRAPELTA 545
Cdd:PRK08008 315 LLTSYGMTETIVGIIGDRPGDKRRWPS---IGRPGFCYEAEIRDDHNRPLPAGEIGEICIKgvpGKTIFKEYYLDPKATA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 546 ERFVEHPWrpgarLYrTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDA 625
Cdd:PRK08008 392 KVLEADGW-----LH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIA----THPKIQDIVVVGIKDSIRDE 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1395399044 626 FLAAF-LLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:PRK08008 462 AIKAFvVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNLK 517
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
211-673 |
1.64e-23 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 104.35 E-value: 1.64e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 211 WTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDvsypaqrlaliletaqpfrvvahp 290
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLN------------------------ 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 291 ehAHVAAAERVLPVEElvadiepetfAAPQLDELAMLLFTSGSTGRPKGVELSHRM-WANYTQWQLRVasgvpGL----R 365
Cdd:cd05912 58 --TRLTPNELAFQLKD----------SDVKLDDIATIMYTSGTTGKPKGVQQTFGNhWWSAIGSALNL-----GLteddN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 366 TLQFAPLSFDMAFQEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNalGVRPGALRVVV 445
Cdd:cd05912 121 WLCALPLFHISGLSILMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILG--EGYPNNLRCIL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 446 SSGEQlrITEDVRAFCAAMpGLLLENQYGPTET-HQVTyhSLSGDPAHyPDLPPIGRPLDGVEVQVLDAALRPVPVgvtG 524
Cdd:cd05912 196 LGGGP--APKPLLEQCKEK-GIPVYQSYGMTETcSQIV--TLSPEDAL-NKIGSAGKPLFPVELKIEDDGQPPYEV---G 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 525 ELYFGGDCLARGYHRAPELTAERFvEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElAIMRQa 604
Cdd:cd05912 267 EILLKGPNVTKGYLNRPDATEESF-ENGW------FKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIE-EVLLS- 337
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395399044 605 erQPGLRGAAVVARERQGNDAFLAAFLLGEPEaVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:cd05912 338 --HPAIKEAGVVGIPDDKWGQVPVAFVVSERP-ISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGK 403
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
181-673 |
1.13e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 103.69 E-value: 1.13e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 181 PEPLVDVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVR-AGARRGDAIGVALNRSPEMIATIWGILRAG 259
Cdd:PRK05677 20 PDEYPNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQhTDLKPGDRIAVQLPNVLQYPVAVFGAMRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 260 LVCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHVAaaERVLP--------VEElVADIEP------------------ 313
Cdd:PRK05677 100 LIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLA--EKVLPktgvkhviVTE-VADMLPplkrllinavvkhvkkmv 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 314 --------------------ETF--AAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGVPGLRTLQFA 370
Cdd:PRK05677 177 payhlpqavkfndalakgagQPVteANPQADDVAVLQYTGGTTGVAKGAMLTHRnLVANMLQCRALMGSNLNEGCEILIA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 371 PLS----FDMAFQEIFSTLCGGGELqLISNRErmDPSALLHVLERRQVQrvllPFVALQRLAEA-SNALGVRP---GALR 442
Cdd:PRK05677 257 PLPlyhiYAFTFHCMAMMLIGNHNI-LISNPR--DLPAMVKELGKWKFS----GFVGLNTLFVAlCNNEAFRKldfSALK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 443 VVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTETHQVTyhslSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGV 522
Cdd:PRK05677 330 LTLSGGMAL--QLATAERWKEVTGCAICEGYGMTETSPVV----SVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 523 TGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE--LAI 600
Cdd:PRK05677 404 VGELCVKGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEdvLAA 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1395399044 601 MrqaerqPG-LRGAAV-VARERQGNDafLAAFLLGEP-EAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK05677 478 L------PGvLQCAAIgVPDEKSGEA--IKVFVVVKPgETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGK 545
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
212-682 |
1.34e-22 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 102.79 E-value: 1.34e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDLdHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD--VSYPAQRLAL-------ILeTAQ 282
Cdd:cd05909 9 TYRKL-LTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNytAGLRELRACIklagiktVL-TSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 283 PF-RVVAHPEHAHVAAAERVLPVEELVADIE--------------PET-----FAAP-QLDELAMLLFTSGSTGRPKGVE 341
Cdd:cd05909 87 QFiEKLKLHHLFDVEYDARIVYLEDLRAKISkadkckaflagkfpPKWllrifGVAPvQPDDPAVILFTSGSEGLPKGVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 342 LSHR-MWANYTQwQLRVASGVPGLRTLQFAPL--SFDMAFQeIFSTLCGGGELQLISNRerMDPSALLHVLERRQVQRVL 418
Cdd:cd05909 167 LSHKnLLANVEQ-ITAIFDPNPEDVVFGALPFfhSFGLTGC-LWLPLLSGIKVVFHPNP--LDYKKIPELIYDKKATILL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 419 LPFVALQRLAEASNALGVRpgALRVVVSSGEQLRitEDVRAFCAAMPGLLLENQYGPTETHQVtyhsLSGDPAHYPDLP- 497
Cdd:cd05909 243 GTPTFLRGYARAAHPEDFS--SLRLVVAGAEKLK--DTLRQEFQEKFGIRILEGYGTTECSPV----ISVNTPQSPNKEg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 498 PIGRPLDGVEVQVLD-AALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFvEHPWrpgarlYRTGDLGRILGNGEIVW 576
Cdd:cd05909 315 TVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF-GDGW------YDTGDIGKIDGEGFLTI 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 577 LGRADTQVKVRGFRIEPAEVELAIMrqaERQPGLRGAAVVAR--ERQGNdaflAAFLLGEPEAVDLAELKQALR-SELPE 653
Cdd:cd05909 388 TGRLSRFAKIAGEMVSLEAIEDILS---EILPEDNEVAVVSVpdGRKGE----KIVLLTTTTDTDPSSLNDILKnAGISN 460
|
490 500
....*....|....*....|....*....
gi 1395399044 654 HMVPAHFAWVDGFALTPSGKRDDAALRAL 682
Cdd:cd05909 461 LAKPSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
199-673 |
4.93e-22 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 100.81 E-value: 4.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALIL 278
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 279 ETAQPFRVVAHPEHAHVAAAERVLPVEELVA----DIEP-ETFaapQLDELAMLLFTSGSTGRPKGVELShrmWANYtqW 353
Cdd:PRK03640 96 DDAEVKCLITDDDFEAKLIPGISVKFAELMNgpkeEAEIqEEF---DLDEVATIMYTSGTTGKPKGVIQT---YGNH--W 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 354 QLRVASGVP-GLRT----LQFAPLSFDMAFQEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRVLLPFVALQRLA 428
Cdd:PRK03640 168 WSAVGSALNlGLTEddcwLAAVPIFHISGLSILMRSVIYGMRVVLV---EKFDAEKINKLLQTGGVTIISVVSTMLQRLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 429 EasnALGVR--PGALRVVVSSGEQlrITEDVRAFCAAMpGLLLENQYGPTET-HQVTyhSLSGDPAHyPDLPPIGRPLDG 505
Cdd:PRK03640 245 E---RLGEGtyPSSFRCMLLGGGP--APKPLLEQCKEK-GIPVYQSYGMTETaSQIV--TLSPEDAL-TKLGSAGKPLFP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 506 VEVQVLDaALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVK 585
Cdd:PRK03640 316 CELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDG-W------FKTGDIGYLDEEGFLYVLDRRSDLII 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 586 VRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGEpEAVDLAELKQALRSELPEHMVPAHFAWVDG 665
Cdd:PRK03640 388 SGGENIYPAEIEEVLL----SHPGVAEAGVVGVPDDKWGQVPVAFVVKS-GEVTEEELRHFCEEKLAKYKVPKRFYFVEE 462
|
....*...
gi 1395399044 666 FALTPSGK 673
Cdd:PRK03640 463 LPRNASGK 470
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
199-680 |
5.69e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 100.85 E-value: 5.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEE--QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY-PAQRLA 275
Cdd:PRK13390 11 PDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLtAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 276 LILETAQPFRVVAHPEHAHVAAAERVLPVE-------ELVADIEPETFAA-PQLDEL---AMLLFTSGSTGRPKGV--EL 342
Cdd:PRK13390 91 IVGDSGARVLVASAALDGLAAKVGADLPLRlsfggeiDGFGSFEAALAGAgPRLTEQpcgAVMLYSSGTTGFPKGIqpDL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 343 SHRmwanytqwqlrvASGVPGLRTLQFAPLSFDMAFQEIFST-----------LCG-----GGELQLIsnrERMDPSALL 406
Cdd:PRK13390 171 PGR------------DVDAPGDPIVAIARAFYDISESDIYYSsapiyhaaplrWCSmvhalGGTVVLA---KRFDAQATL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 407 HVLERRQV---QRVLLPFVALQRL-AEASNALGVrpGALRVVVSSGEQLRIteDVRAFCAAMPGLLLENQYGPTETHQVT 482
Cdd:PRK13390 236 GHVERYRItvtQMVPTMFVRLLKLdADVRTRYDV--SSLRAVIHAAAPCPV--DVKHAMIDWLGPIVYEYYSSTEAHGMT 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 483 YHSlSGDPAHYPDlpPIGRPLDGvEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAErfVEHPWRPgarLYRT 562
Cdd:PRK13390 312 FID-SPDWLAHPG--SVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHP---FWTT 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 563 -GDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGNDAFLAAFLL-GEPEAV 638
Cdd:PRK13390 383 vGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALT----MHPAVHDVAVigVPDPEMGEQVKAVIQLVeGIRGSD 458
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1395399044 639 DLA-ELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:PRK13390 459 ELArELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLLR 501
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
329-673 |
6.29e-22 |
|
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: 341241 [Multi-domain] Cd Length: 349 Bit Score: 98.50 E-value: 6.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 329 FTSGSTGRPKGVELSHRMWAN---YTQWQLRVASG----VPglrtlqfAPL--SFDMAFQeIFSTLCGGGELQLISnrER 399
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNngyFIGERLGLTEQdrlcIP-------VPLfhCFGSVLG-VLACLTHGATMVFPS--PS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 400 MDPSALLHVLERRQ---VQRVLLPFVALQRLAEASNalgVRPGALRVVVSSG------------EQLRITEDVRAfcaam 464
Cdd:cd05917 79 FDPLAVLEAIEKEKctaLHGVPTMFIAELEHPDFDK---FDLSSLRTGIMAGapcppelmkrviEVMNMKDVTIA----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 465 pglllenqYGPTETHQVTYHSLSGDPAHyPDLPPIGRPLDGVEVQVLDAALRPVP-VGVTGELYFGGDCLARGYHRAPEL 543
Cdd:cd05917 151 --------YGMTETSPVSTQTRTDDSIE-KRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEK 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 544 TAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVkVRGFR-IEPAEVELAIMrqaeRQPGLRGAAV--VARER 620
Cdd:cd05917 222 TAEAIDGDGW------LHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLH----THPKVSDVQVvgVPDER 290
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1395399044 621 QGNDafLAAFLLGEPEA-VDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:cd05917 291 YGEE--VCAWIRLKEGAeLTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGK 342
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
209-616 |
1.65e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 99.07 E-value: 1.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 209 QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDvsypaqrlaliletaqPFRVVA 288
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLID----------------PGMGRK 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 289 HpehahvaaaervlpVEELVADIEPETF-AAPQLDELAMLLFTSGSTGRPKGVELSHRMWanytqwqlrvASGVPGLRTL 367
Cdd:cd05910 65 N--------------LKQCLQEAEPDAFiGIPKADEPAAILFTSGSTGTPKGVVYRHGTF----------AAQIDALRQL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 368 -QFAPLSFDMAFQEIFSTLcgGGELQLISNRERMDPSA--------LLHVLERRQVQRVLLPFVALQRLAEASNALGVRP 438
Cdd:cd05910 121 yGIRPGEVDLATFPLFALF--GPALGLTSVIPDMDPTRparadpqkLVGAIRQYGVSIVFGSPALLERVARYCAQHGITL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 439 GALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQYGPTETHQVTY---HSLSGDPAHYPDLPP---IGRPLDGVEVQVLD 512
Cdd:cd05910 199 PSLRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEALPVSSigsRELLATTTAATSGGAgtcVGRPIPGVRVRIIE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 513 AALRP---------VPVGVTGELYFGGDCLARGYHRAPELTAerfVEHPWRPGAR-LYRTGDLGRILGNGEIVWLGRADT 582
Cdd:cd05910 279 IDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATA---LAKIDDNSEGfWHRMGDLGYLDDEGRLWFCGRKAH 355
|
410 420 430
....*....|....*....|....*....|....
gi 1395399044 583 QVKVRGFRIEPAEVElaimRQAERQPGLRGAAVV 616
Cdd:cd05910 356 RVITTGGTLYTEPVE----RVFNTHPGVRRSALV 385
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
192-673 |
1.99e-21 |
|
acetate-CoA ligase; This family 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: 341289 [Multi-domain] Cd Length: 587 Bit Score: 99.96 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 192 ERQVEALPGSAALAFE------EQRWTYRDL-DHVARcVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVP 264
Cdd:cd17634 60 DRHLRENGDRTAIIYEgddtsqSRTISYRELhREVCR-FAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 265 LDVSYPAQRLA--------LILETA----QPFRVVAHPEHAHVAAAERVLPVE-----------------------ELVA 309
Cdd:cd17634 139 IFGGFAPEAVAgriidsssRLLITAdggvRAGRSVPLKKNVDDALNPNVTSVEhvivlkrtgsdidwqegrdlwwrDLIA 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 310 DIEPETFAAP-QLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGV-PGLRTLQFAPLSFDMAFQEIF--STL 385
Cdd:cd17634 219 KASPEHQPEAmNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYVFDYgPGDIYWCTADVGWVTGHSYLLygPLA 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 386 CGGGELQLISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNAL--GVRPGALRVVVSSGEQLRiTEDVRAFCAA 463
Cdd:cd17634 299 CGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAieGTDRSSLRILGSVGEPIN-PEAYEWYWKK 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 464 MPGLL--LENQYGPTETHQVTYHSLSGDPAHYPDLPPigRPLDGVEVQVLDAALRPVPVGVTGELYFGGDC--LARGYHR 539
Cdd:cd17634 378 IGKEKcpVVDTWWQTETGGFMITPLPGAIELKAGSAT--RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPWpgQTRTLFG 455
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 540 APEltaeRFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARE 619
Cdd:cd17634 456 DHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLV----AHPKVAEAAVVGIP 527
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1395399044 620 RQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHM----VPAHFAWVDGFALTPSGK 673
Cdd:cd17634 528 HAIKGQAPYAYVVLNHGVEPSPELYAELRNWVRKEIgplaTPDVVHWVDSLPKTRSGK 585
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
326-675 |
1.99e-21 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. 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: 341291 [Multi-domain] Cd Length: 331 Bit Score: 96.60 E-value: 1.99e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 326 MLLFTSGSTGRPKGVELSHR--MWANYTQWQLRVASgvPGLRTLQFAPLsFDMAFQ-EIFSTLCGGGELQLISnreRMDP 402
Cdd:cd17636 4 LAIYTAAFSGRPNGALLSHQalLAQALVLAVLQAID--EGTVFLNSGPL-FHIGTLmFTLATFHAGGTNVFVR---RVDA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 403 SALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGE-QLRITEDVRAFCAAMPGlllenqYGPTE-THQ 480
Cdd:cd17636 78 EEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEwNDMATVDTSPWGRKPGG------YGQTEvMGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 481 VTYHSLSGdpahyPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVehpwrpgARLY 560
Cdd:cd17636 152 ATFAALGG-----GAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-------GGWH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 561 RTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAImrqaERQPGLRGAAV--VARERQGNDAfLAAFLLGEPEAV 638
Cdd:cd17636 220 HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCL----RQHPAVADAAVigVPDPRWAQSV-KAIVVLKPGASV 294
|
330 340 350
....*....|....*....|....*....|....*..
gi 1395399044 639 DLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 675
Cdd:cd17636 295 TEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
196-680 |
6.72e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 97.54 E-value: 6.72e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 196 EALPGSAALAFEEQRWTYRDLDHVARCVATRLvRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLA 275
Cdd:PRK07638 12 SLQPNKIAIKENDRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 276 LILETAQPFRVVAHPEHAHVAAAE--RVLPVEELVADIEPETFAAPQLDELAM----LLFTSGSTGRPKGVELSHRMW-- 347
Cdd:PRK07638 91 ERLAISNADMIVTERYKLNDLPDEegRVIEIDEWKRMIEKYLPTYAPIENVQNapfyMGFTSGSTGKPKAFLRAQQSWlh 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 348 ---ANYTQWQLRVASGV--PGlrTLqfapLSFDMAFQEIfSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRVLLPFV 422
Cdd:PRK07638 171 sfdCNVHDFHMKREDSVliAG--TL----VHSLFLYGAI-STLYVGQTVHLM---RKFIPNQVLDKLETENISVMYTVPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 423 ALQRLAEASnalGVRPGALRVVvSSGEQLRItEDVRAFCAAMPGLLLENQYGPTETHQVTYHSlSGDPAHYPDlpPIGRP 502
Cdd:PRK07638 241 MLESLYKEN---RVIENKMKII-SSGAKWEA-EAKEKIKNIFPYAKLYEFYGASELSFVTALV-DEESERRPN--SVGRP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 503 LDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGY----HRAPELTAERFVEhpwrpgarlyrTGDLGRILGNGEIVWLG 578
Cdd:PRK07638 313 FHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYiiggVLARELNADGWMT-----------VRDVGYEDEEGFIYIVG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 579 RADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVARErqgnDAFLaafllGE-PEAV-----DLAELKQALRSELP 652
Cdd:PRK07638 382 REKNMILFGGINIFPEEIE----SVLHEHPAVDEIVVIGVP----DSYW-----GEkPVAIikgsaTKQQLKSFCLQRLS 448
|
490 500
....*....|....*....|....*...
gi 1395399044 653 EHMVPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:PRK07638 449 SFKIPKEWHFVDEIPYTNSGKIARMEAK 476
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
217-659 |
9.78e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 97.08 E-value: 9.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 217 DHVARcVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAH------- 289
Cdd:PRK12406 19 QRAAR-AAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHadllhgl 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 290 -------------PEHAHVAAAERVLPV-----------EELVADIEPetFAAPQLDELAMLLFTSGSTGRPKGV----- 340
Cdd:PRK12406 98 asalpagvtvlsvPTPPEIAAAYRISPAlltppagaidwEGWLAQQEP--YDGPPVPQPQSMIYTSGTTGHPKGVrraap 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 341 --ELShrmwANYTQWQLRVASGVPGLRTLQFAPL--SFDMAFQEIFSTLcgGGELQLISnreRMDPSALLHVLERRQVQR 416
Cdd:PRK12406 176 tpEQA----AAAEQMRALIYGLKPGIRALLTGPLyhSAPNAYGLRAGRL--GGVLVLQP---RFDPEELLQLIERHRITH 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 417 V-LLP--FVALQRLAEASNAlgvrpgalRVVVSSgeqLRITEDVRAFCA-----AMP---GLLLENQYGPTETHQVTYHS 485
Cdd:PRK12406 247 MhMVPtmFIRLLKLPEEVRA--------KYDVSS---LRHVIHAAAPCPadvkrAMIewwGPVIYEYYGSTESGAVTFAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 486 lSGDPAHYPDlpPIGRPLDGVEVQVLDAALRPVPVGVTGELYfggdCLARG-----YHRAPELTAErfVEhpwRPGarLY 560
Cdd:PRK12406 316 -SEDALSHPG--TVGKAAPGAELRFVDEDGRPLPQGEIGEIY----SRIAGnpdftYHNKPEKRAE--ID---RGG--FI 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 561 RTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGNDafLAAFLLGEPEA- 637
Cdd:PRK12406 382 TSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLH----AVPGVHDCAVfgIPDAEFGEA--LMAVVEPQPGAt 455
|
490 500
....*....|....*....|..
gi 1395399044 638 VDLAELKQALRSELPEHMVPAH 659
Cdd:PRK12406 456 LDEADIRAQLKARLAGYKVPKH 477
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
209-579 |
9.96e-20 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 94.20 E-value: 9.96e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 209 QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVA 288
Cdd:PRK09274 40 DELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 289 HPEhAHVA---------AAERVLPV-----------EELVADIEPETFAAPQL--DELAMLLFTSGSTGRPKGVELSHRM 346
Cdd:PRK09274 120 IPK-AHLArrlfgwgkpSVRRLVTVggrllwggttlATLLRDGAAAPFPMADLapDDMAAILFTSGSTGTPKGVVYTHGM 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 347 WANYTQwQLRVASG-VPGLRTLQFAPLsfdMAFqeiFSTLCGGGelqliSNRERMDPS--------ALLHVLERRQVQRV 417
Cdd:PRK09274 199 FEAQIE-ALREDYGiEPGEIDLPTFPL---FAL---FGPALGMT-----SVIPDMDPTrpatvdpaKLFAAIERYGVTNL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 418 llpFVA---LQRLAEASNALGVRPGALRVVVSSGEQLriTEDVRAFCAAM--PGLLLENQYGPTET---HQVTYHSLSGD 489
Cdd:PRK09274 267 ---FGSpalLERLGRYGEANGIKLPSLRRVISAGAPV--PIAVIERFRAMlpPDAEILTPYGATEAlpiSSIESREILFA 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 490 PAHYPDLPP---IGRPLDGVEVQVL---DAAL------RPVPVGVTGELYFGGDCLARGYHRAPELTAERFVehpWRPGA 557
Cdd:PRK09274 342 TRAATDNGAgicVGRPVDGVEVRIIaisDAPIpewddaLRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKI---PDGQG 418
|
410 420
....*....|....*....|...
gi 1395399044 558 RLY-RTGDLGRILGNGEIVWLGR 579
Cdd:PRK09274 419 DVWhRMGDLGYLDAQGRLWFCGR 441
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
212-616 |
1.40e-19 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 92.63 E-value: 1.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPldvsypaqrlALILETAQPFRvvahpe 291
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP----------ATTLLTPDDLR------ 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 292 hahvaaaERVLPVEELVADIEPETFAapqlDELAMLLFTSGSTGRPKGVELSHRmwaNYTQWQLRVASGV---PGLRTLQ 368
Cdd:cd05974 66 -------DRVDRGGAVYAAVDENTHA----DDPMLLYFTSGTTSKPKLVEHTHR---SYPVGHLSTMYWIglkPGDVHWN 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 369 FA-PLSFDMAFQEIFSTLCGGGELQLIsNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASnaLGVRPGALRVVVSS 447
Cdd:cd05974 132 ISsPGWAKHAWSCFFAPWNAGATVFLF-NYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQD--LASFDVKLREVVGA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 448 GEQL--RITEDVRAfcaaMPGLLLENQYGPTETHQVTYHSlsgdPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVG---- 521
Cdd:cd05974 209 GEPLnpEVIEQVRR----AWGLTIRDGYGQTETTALVGNS----PGQPVKAGSMGRPLPGYRVALLDPDGAPATEGeval 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 522 VTGELYFGGdcLARGYHRAPELTAERFvehpwrpGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIM 601
Cdd:cd05974 281 DLGDTRPVG--LMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLI 351
|
410
....*....|....*
gi 1395399044 602 rqaeRQPGLRGAAVV 616
Cdd:cd05974 352 ----EHPAVAEAAVV 362
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
329-673 |
4.42e-19 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which 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: 341288 [Multi-domain] Cd Length: 320 Bit Score: 89.39 E-value: 4.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 329 FTSGSTGRPKGVELSHRMWA-----NYTQWQLRVASG--VPGlrtlqfaPLSFDMAFQEIFSTLCGGGELQLISNrerMD 401
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIesfvcNEDLFNISGEDAilAPG-------PLSHSLFLYGAISALYLGGTFIGQRK---FN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 402 PSALLHVLERRQVQRVLLPFVALQRLAEASNalgvrPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQYGPTETHQV 481
Cdd:cd17633 77 PKSWIRKINQYNATVIYLVPTMLQALARTLE-----PESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 482 TYHSL-SGDPAHypdlpPIGRPLDGVEVQVLDAAlrpvpVGVTGELYFGGDCLARGYHRAPELTaerfvEHPWrpgarlY 560
Cdd:cd17633 152 TYNFNqESRPPN-----SVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSN-----PDGW------M 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 561 RTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAAFLLGepEAVDL 640
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLK----AIPGIEEAIVVGIPDARFGEIAVALYSG--DKLTY 284
|
330 340 350
....*....|....*....|....*....|...
gi 1395399044 641 AELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:cd17633 285 KQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGK 317
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
187-673 |
4.76e-19 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 92.13 E-value: 4.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 187 VVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLD 266
Cdd:PRK13382 45 PTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLN 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 267 VSYPAQRLALILE-----------------------TAQPFRVVAHPEHAHVAAAErVLPVEELVADIEPetfaAPQLDE 323
Cdd:PRK13382 125 TSFAGPALAEVVTregvdtviydeefsatvdraladCPQATRIVAWTDEDHDLTVE-VLIAAHAGQRPEP----TGRKGR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 324 laMLLFTSGSTGRPKGVELSHRMWA-------NYTQWQLR--VASGVPGLRTLQFAPLSFDMAFQeifSTlcgggelqlI 394
Cdd:PRK13382 200 --VILLTSGTTGTPKGARRSGPGGIgtlkailDRTPWRAEepTVIVAPMFHAWGFSQLVLAASLA---CT---------I 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 395 SNRERMDPSALLHVLER-RQVQRVLLPfVALQRL----AEASNALGVRpgALRVVVSSGEQLRiTEDVRAFCAAMpGLLL 469
Cdd:PRK13382 266 VTRRRFDPEATLDLIDRhRATGLAVVP-VMFDRImdlpAEVRNRYSGR--SLRFAAASGSRMR-PDVVIAFMDQF-GDVI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 470 ENQYGPTETHQVTYHSLSGDPAHyPDLPpiGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRApelTAERFV 549
Cdd:PRK13382 341 YNNYNATEAGMIATATPADLRAA-PDTA--GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDFH 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 550 EHpwrpgarLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAFLAA 629
Cdd:PRK13382 415 DG-------FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLA----THPDVAEAAVIGVDDEQYGQRLAA 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1395399044 630 FLLGEPEAVDLAE-LKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK13382 484 FVVLKPGASATPEtLKQHVRDNLANYKVPRDIVVLDELPRGATGK 528
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
169-684 |
5.12e-19 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 92.38 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 169 AFLAPRRDAASQPEPLVDvvslFERQVEALP----GSAALAFEEQR------WTYRDLDHVARCVATRLVRAGARRGDAI 238
Cdd:PRK09192 2 VTMSPTPTTSSLPRRYAD----FPTLVEALDyaalGEAGMNFYDRRgqleeaLPYQTLRARAEAGARRLLALGLKPGDRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 239 GVALNRSPEMIATIWGILRAGLVCVPLDV--------SYPAQrLALILETAQPFRVVAHPEHAHVAAAerVLPVEELVAD 310
Cdd:PRK09192 78 ALIAETDGDFVEAFFACQYAGLVPVPLPLpmgfggreSYIAQ-LRGMLASAQPAAIITPDELLPWVNE--ATHGNPLLHV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 311 IEPETFAA----------PQLDELAMLLFTSGSTGRPKGVELSHR-MWAN---YTQWQLRVasgVPGLRTLQFAPLSFDM 376
Cdd:PRK09192 155 LSHAWFKAlpeadvalprPTPDDIAYLQYSSGSTRFPRGVIITHRaLMANlraISHDGLKV---RPGDRCVSWLPFYHDM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 377 AFQEIFST---------LCGGGE--------LQLIS-NRERM--DPSALLHVLERRQVQRVLLPF------VA------- 423
Cdd:PRK09192 232 GLVGFLLTpvatqlsvdYLPTRDfarrplqwLDLISrNRGTIsySPPFGYELCARRVNSKDLAELdlscwrVAgigadmi 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 424 ----LQRLAEASNALGVRPGALrvVVSSGeqlrITEDVRAFCAAMPGlllenqyGPTETHQVTYHSLSGD---------P 490
Cdd:PRK09192 312 rpdvLHQFAEAFAPAGFDDKAF--MPSYG----LAEATLAVSFSPLG-------SGIVVEEVDRDRLEYQgkavapgaeT 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 491 AHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHpWrpgarlYRTGDLGRILg 570
Cdd:PRK09192 379 RRVRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADG-W------LDTGDLGYLL- 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 571 NGEIVWLGRADTQVKVRGFRIEPAEVELAimrqAERQPGLRG----AAVVARERQGNDAFLAAFLLGEPEAvdlaelKQA 646
Cdd:PRK09192 451 DGYLYITGRAKDLIIINGRNIWPQDIEWI----AEQEPELRSgdaaAFSIAQENGEKIVLLVQCRISDEER------RGQ 520
|
570 580 590 600
....*....|....*....|....*....|....*....|....*
gi 1395399044 647 LRSELPE-----HMVPAHFAWVDGFAL--TPSGKRDDAALRALPL 684
Cdd:PRK09192 521 LIHALAAlvrseFGVEAAVELVPPHSLprTSSGKLSRAKAKKRYL 565
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
180-682 |
1.49e-18 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 90.43 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 180 QPEPLVDVVSlfeRQVEalPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAG 259
Cdd:PRK10946 23 QDLPLTDILT---RHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 260 LVcvPLDVSYPAQRLALILETAQ--PFRVVAHPEHAHVAAAERVlpvEELVADI-----------------------EPE 314
Cdd:PRK10946 98 VA--PVNALFSHQRSELNAYASQiePALLIADRQHALFSDDDFL---NTLVAEHsslrvvlllnddgehslddainhPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 315 TFAA--PQLDELAMLLFTSGSTGRPKGVELSHrmwaNYTQWQLRVASGVPGL----RTLQF--APLSFDMAFQEIFSTLC 386
Cdd:PRK10946 173 DFTAtpSPADEVAFFQLSGGSTGTPKLIPRTH----NDYYYSVRRSVEICGFtpqtRYLCAlpAAHNYPMSSPGALGVFL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 387 GGGELQLISnrermDPSALL--HVLERRQVQRVLL--PFVA--LQRLAEASNALGVRpgALRVVVSSGEqlRITEDVRAF 460
Cdd:PRK10946 249 AGGTVVLAP-----DPSATLcfPLIEKHQVNVTALvpPAVSlwLQAIAEGGSRAQLA--SLKLLQVGGA--RLSETLARR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 461 CAAMPGLLLENQYGPTEThQVTYHSLSGDPAHYpdLPPIGRPL-DGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHR 539
Cdd:PRK10946 320 IPAELGCQLQQVFGMAEG-LVNYTRLDDSDERI--FTTQGRPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 540 APELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARE 619
Cdd:PRK10946 397 SPQHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLL----RHPAVIHAALVSME 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395399044 620 rqgnDAFLA----AFLLGEpEAVDLAELKQALRSE-LPEHMVPAHFAWVDGFALTPSGKRDDAALRAL 682
Cdd:PRK10946 467 ----DELMGekscAFLVVK-EPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQW 529
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
196-681 |
2.34e-18 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 89.36 E-value: 2.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 196 EALPGSAALAFEEQRWTYRDLDHVARCVATRLVRA-GARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRL 274
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAeGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 275 ALILETAQPFRVVAHPEhahVAAAERVLPVEELVADIEPETFAAPQLDELAMLLfTSGSTGRPKGVE--LSHRMWANYTQ 352
Cdd:cd05929 82 CAIIEIKAAALVCGLFT---GGGALDGLEDYEAAEGGSPETPIEDEAAGWKMLY-SGGTTGRPKGIKrgLPGGPPDNDTL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 353 --WQLRVASGvPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLIsnrERMDPSALLHVLERRQVQRV-LLP--FVALQRL 427
Cdd:cd05929 158 maAALGFGPG-ADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLM---EKFDPEEFLRLIERYRVTFAqFVPtmFVRLLKL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 428 AEA-SNALGVrpGALRVVVSSGEQLRIteDVRAFCAAMPGLLLENQYGPTETHQVTYHSlSGDPAHYPDlpPIGRPLDGv 506
Cdd:cd05929 234 PEAvRNAYDL--SSLKRVIHAAAPCPP--WVKEQWIDWGGPIIWEYYGGTEGQGLTIIN-GEEWLTHPG--SVGRAVLG- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 507 EVQVLDAALRPVPVGVTGELYF-GGDclARGYHRAPELTAERFVEHPWRpgarlyRTGDLGRILGNGEIVWLGRADTQVK 585
Cdd:cd05929 306 KVHILDEDGNEVPPGEIGEVYFaNGP--GFEYTNDPEKTAAARNEGGWS------TLGDVGYLDEDGYLYLTDRRSDMII 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 586 VRGFRIEPAEVELAIMrqaeRQPGLRGAAVVA--RERQGND--AFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFA 661
Cdd:cd05929 378 SGGVNIYPQEIENALI----AHPKVLDAAVVGvpDEELGQRvhAVVQPAPGADAGTALAEELIAFLRDRLSRYKCPRSIE 453
|
490 500
....*....|....*....|
gi 1395399044 662 WVDGFALTPSGKRDDAALRA 681
Cdd:cd05929 454 FVAELPRDDTGKLYRRLLRD 473
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
203-616 |
3.85e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 88.89 E-value: 3.85e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 203 ALAFEEQRWTYRDLDHVARCVATRLvrAGARRgdaigVALNRSPEM--IATIWGILRAGLVCVPLDVSYPAQRLALILET 280
Cdd:PRK07787 18 AVRIGGRVLSRSDLAGAATAVAERV--AGARR-----VAVLATPTLatVLAVVGALIAGVPVVPVPPDSGVAERRHILAD 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 281 AQPFRVVAHPEHAhvAAAERVLPVEELVAdiEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHR-------MWANYTQW 353
Cdd:PRK07787 91 SGAQAWLGPAPDD--PAGLPHVPVRLHAR--SWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRaiaadldALAEAWQW 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 354 QLR--VASGVP-----GLRTLQFAPLSFdmafqeifstlcGGGELQLIsnreRMDPSALLHVLERRQVQRVLLPFVaLQR 426
Cdd:PRK07787 167 TADdvLVHGLPlfhvhGLVLGVLGPLRI------------GNRFVHTG----RPTPEAYAQALSEGGTLYFGVPTV-WSR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 427 LAEASNALGVRPGAlRVVVSSGEQLRITEDVRafCAAMPGLLLENQYGPTETHQVTyhSLSGDPAHYPDLppIGRPLDGV 506
Cdd:PRK07787 230 IAADPEAARALRGA-RLLVSGSAALPVPVFDR--LAALTGHRPVERYGMTETLITL--STRADGERRPGW--VGLPLAGV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 507 EVQVLDAALRPVPVGV--TGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQ- 583
Cdd:PRK07787 303 ETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGRESTDl 376
|
410 420 430
....*....|....*....|....*....|...
gi 1395399044 584 VKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVV 616
Cdd:PRK07787 377 IKSGGYRIGAGEIETALL----GHPGVREAAVV 405
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1-162 |
5.17e-18 |
|
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal fungal CT domains and Dual Epimerization/Condensation (E/C) domains; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type [D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L))], which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380459 [Multi-domain] Cd Length: 419 Bit Score: 87.89 E-value: 5.17e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 1 AHCLTLHLFSRSDSVVTGAISNGRPE-LPDADRMVGLFLNTVPVRSEIAGHSWIEVADALFRQERDGHAHRRYPLSAIQQ 79
Cdd:cd19536 248 AWALVLSRHSGSDDVVFGTVVHGRSEeTTGAERLLGLFLNTLPLRVTLSEETVEDLLKRAQEQELESLSHEQVPLADIQR 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 80 IVGDE--LSSAFNYVNLHVLE--PLWQL------RDFRVWEETNFALLVNViATPSDGMYLRIDSDGRGISRSQAALIGA 149
Cdd:cd19536 328 CSEGEplFDSIVNFRHFDLDFglPEWGSdegmrrGLLFSEFKSNYDVNLSV-LPKQDRLELKLAYNSQVLDEEQAQRLAA 406
|
170
....*....|...
gi 1395399044 150 TFVELLWRLAEHP 162
Cdd:cd19536 407 YYKSAIAELATAP 419
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
173-673 |
5.26e-18 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 88.88 E-value: 5.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 173 PRRDAASQPEPLVDVVSLFERQV---EALPGSAalafeeqrWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMI 249
Cdd:PLN02330 23 PVPDKLTLPDFVLQDAELYADKVafvEAVTGKA--------VTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 250 ATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEH-AHVAAAErvLPV--------------EELV--ADIE 312
Cdd:PLN02330 95 IVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNyGKVKGLG--LPVivlgeekiegavnwKELLeaADRA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 313 PETFAAPQL--DELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGVPG-LRTLQFAPLSFDMAFQEI-FSTLCG 387
Cdd:PLN02330 173 GDTSDNEEIlqTDLCALPFSSGTTGISKGVMLTHRnLVANLCSSLFSVGPEMIGqVVTLGLIPFFHIYGITGIcCATLRN 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 388 GGELQLISnreRMDPSALLHVLERRQVQrvLLPFVALQRLAEASNAL----GVRPGALRVVVSSGEQLrITEDVRAFCAA 463
Cdd:PLN02330 253 KGKVVVMS---RFELRTFLNALITQEVS--FAPIVPPIILNLVKNPIveefDLSKLKLQAIMTAAAPL-APELLTAFEAK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 464 MPGLLLENQYGPTETHQVTYhsLSGDPAHYPDLP---PIGRPLDGVEVQVLDAAL-RPVPVGVTGELYFGGDCLARGYHR 539
Cdd:PLN02330 327 FPGVQVQEAYGLTEHSCITL--THGDPEKGHGIAkknSVGFILPNLEVKFIDPDTgRSLPKNTPGELCVRSQCVMQGYYN 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 540 APELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARE 619
Cdd:PLN02330 405 NKEETDRTIDEDGW------LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILL----THPSVEDAAVVPLP 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1395399044 620 RQGNDAFLAAFLLGEPEAVDLAE-LKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PLN02330 475 DEEAGEIPAACVVINPKAKESEEdILNFVAANVAHYKKVRVVQFVDSIPKSLSGK 529
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
326-675 |
1.60e-17 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. 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: 341292 [Multi-domain] Cd Length: 333 Bit Score: 85.01 E-value: 1.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 326 MLLFTSGSTGRPKGVELSHR--MWANYtqwQLRVASGV-PGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLIsnrERMDP 402
Cdd:cd17637 4 VIIHTAAVAGRPRGAVLSHGnlIAANL---QLIHAMGLtEADVYLNMLPLFHIAGLNLALATFHAGGANVVM---EKFDP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 403 SALLHVLERRQVQrVLLPFVA-LQRLAEASNALGVRPGALRVVVSsgeqLRITEDVRAFCAAMPGLLLeNQYGPTETHQ- 480
Cdd:cd17637 78 AEALELIEEEKVT-LMGSFPPiLSNLLDAAEKSGVDLSSLRHVLG----LDAPETIQRFEETTGATFW-SLYGQTETSGl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 481 VTYHSLSGDPAhypdlpPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFvehpwRPGarLY 560
Cdd:cd17637 152 VTLSPYRERPG------SAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-----RNG--WH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 561 RTGDLGRILGNGEIVWLGRADTQ--VKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVA-RERQGNDAFLAAFLLGEPEA 637
Cdd:cd17637 219 HTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVIL----EHPAIAEVCVIGvPDPKWGEGIKAVCVLKPGAT 294
|
330 340 350
....*....|....*....|....*....|....*...
gi 1395399044 638 VDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 675
Cdd:cd17637 295 LTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSID 332
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
321-673 |
2.00e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 87.18 E-value: 2.00e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 321 LDELAMLLFTSGSTGRPKGVELSH-----RMWANYTQWQLRVASGVPGLRTLQ---FAPLSFDMAFQEIFSTLC---GGG 389
Cdd:PRK12492 206 LDDIAVLQYTGGTTGLAKGAMLTHgnlvaNMLQVRACLSQLGPDGQPLMKEGQevmIAPLPLYHIYAFTANCMCmmvSGN 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 390 ELQLISNRErmDPSALLHVLERRQvqrvllpFVALQRLAEASNALGVRPG-------ALRVVVSSGEQLritedVRAFC- 461
Cdd:PRK12492 286 HNVLITNPR--DIPGFIKELGKWR-------FSALLGLNTLFVALMDHPGfkdldfsALKLTNSGGTAL-----VKATAe 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 462 --AAMPGLLLENQYGPTETHQVTYHSLSGDPAHypdLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHR 539
Cdd:PRK12492 352 rwEQLTGCTIVEGYGLTETSPVASTNPYGELAR---LGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQ 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 540 APELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VA 617
Cdd:PRK12492 429 QPEATAEALDAEGW------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVM----AHPKVANCAAigVP 498
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1395399044 618 RERQGNDAFLaaFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK12492 499 DERSGEAVKL--FVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGK 552
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
187-655 |
2.09e-17 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 87.16 E-value: 2.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 187 VVSLFERQVEALPGSAALAFEEQR-----WTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLV 261
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 262 CVPLDVSYPAQRLALILE--------TAQPF----RVVAHPEHAHVAAA-----ERVLPVEEL--------VADIEPETF 316
Cdd:cd05968 143 VVPIFSGFGKEAAATRLQdaeakaliTADGFtrrgREVNLKEEADKACAqcptvEKVVVVRHLgndftpakGRDLSYDEE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 317 AAPQLDELA--------MLLFTSGSTGRPKGVELSHRMWA------NYTQWQLRvasgvPGLRTLQFAPLSFDMAFQEIF 382
Cdd:cd05968 223 KETAGDGAErtesedplMIIYTSGTTGKPKGTVHVHAGFPlkaaqdMYFQFDLK-----PGDLLTWFTDLGWMMGPWLIF 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 383 STLCGGGELQLISNR-ERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPG--ALRVVVSSGEQlrITEDVRA 459
Cdd:cd05968 298 GGLILGATMVLYDGApDHPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDlsSLRVLGSTGEP--WNPEPWN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 460 FCAAMPG---LLLENQYGPTEthqvtyhsLSGDPAHYPDLPPI-----GRPLDGVEVQVLDAALRPVPVGVtGEL----- 526
Cdd:cd05968 376 WLFETVGkgrNPIINYSGGTE--------ISGGILGNVLIKPIkpssfNGPVPGMKADVLDESGKPARPEV-GELvllap 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 527 YFGgdcLARGYHRAPeltaERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeR 606
Cdd:cd05968 447 WPG---MTRGFWRDE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLN----A 515
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1395399044 607 QPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHM 655
Cdd:cd05968 516 HPAVLESAAIGVPHPVKGEAIVCFVVLKPGVTPTEALAEELMERVADEL 564
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
212-579 |
2.26e-17 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 87.13 E-value: 2.26e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDL-DHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHP 290
Cdd:cd17632 69 TYAELwERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVSA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 291 EHAHVA-------------------------------AAERVLPV------EELVADIEPETFAAPQL------DELAML 327
Cdd:cd17632 149 EHLDLAveavleggtpprlvvfdhrpevdahraalesARERLAAVgipvttLTLIAVRGRDLPPAPLFrpepddDPLALL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 328 LFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLR-TLQFAPLSFDMAFQEIFSTLCGGGELQLISnreRMDPSALL 406
Cdd:cd17632 229 IYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASiTLNFMPMSHIAGRISLYGTLARGGTAYFAA---ASDMSTLF 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 407 HVL-ERRQVQRVLLPFVA------LQRLAEASNALGVRPGALRVVVssGEQLR-----------------ITEDVRAFCA 462
Cdd:cd17632 306 DDLaLVRPTELFLVPRVCdmlfqrYQAELDRRSVAGADAETLAERV--KAELRervlggrllaavcgsapLSAEMKAFME 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 463 AMPGLLLENQYGPTETHQVTyhslsgdpahypdlppigrpLDGVEV--QVLDAALRPVP-VG--VT------GELYFGGD 531
Cdd:cd17632 384 SLLDLDLHDGYGSTEAGAVI--------------------LDGVIVrpPVLDYKLVDVPeLGyfRTdrphprGELLVKTD 443
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1395399044 532 CLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGR 579
Cdd:cd17632 444 TLFPGYYKRPEVTAEVFDEDGF------YRTGDVMAELGPDRLVYVDR 485
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
190-673 |
4.48e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 86.02 E-value: 4.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFEEQ--RWTYRDLDHVARCVATRLVRAGARRGDAIGV-ALNRsPEMIATIWGILRAGLVCVPLD 266
Cdd:PRK08315 21 LLDRTAARYPDREALVYRDQglRWTYREFNEEVDALAKGLLALGIEKGDRVGIwAPNV-PEWVLTQFATAKIGAILVTIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 267 VSYPAQRLALILE--------TAQPFRVVAH--------PEHAHVAA----AERV-----------------LPVEELVA 309
Cdd:PRK08315 100 PAYRLSELEYALNqsgckaliAADGFKDSDYvamlyelaPELATCEPgqlqSARLpelrrviflgdekhpgmLNFDELLA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 310 DiePETFAAPQLDELAMLL---------FTSGSTGRPKGVELSHRMWAN----------YTQwQLRVASGVPglrtlqfa 370
Cdd:PRK08315 180 L--GRAVDDAELAARQATLdpddpiniqYTSGTTGFPKGATLTHRNILNngyfigeamkLTE-EDRLCIPVP-------- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 371 plsfdmafqeifstL--CGG---GELQLISNR-------ERMDPsalLHVLERRQVQR------VLLPFVALQRLAE--- 429
Cdd:PRK08315 249 --------------LyhCFGmvlGNLACVTHGatmvypgEGFDP---LATLAAVEEERctalygVPTMFIAELDHPDfar 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 430 ---ASNALGVRPGAL-------RVVvssgEQLRITEDVRAfcaampglllenqYGPTETHQVTYHSLSGDPAhypDL--P 497
Cdd:PRK08315 312 fdlSSLRTGIMAGSPcpievmkRVI----DKMHMSEVTIA-------------YGMTETSPVSTQTRTDDPL---EKrvT 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 498 PIGRPLDGVEVQVLDAAL-RPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNG--EI 574
Cdd:PRK08315 372 TVGRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW------MHTGDLAVMDEEGyvNI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 575 VwlGRadtqVK---VRGFR-IEPAEVElaimrqaE---RQPGLRGAAV--VARERQGNDafLAAFL-LGEPEAVDLAELK 644
Cdd:PRK08315 446 V--GR----IKdmiIRGGEnIYPREIE-------EflyTHPKIQDVQVvgVPDEKYGEE--VCAWIiLRPGATLTEEDVR 510
|
570 580
....*....|....*....|....*....
gi 1395399044 645 QALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK08315 511 DFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
4-162 |
5.84e-17 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 84.56 E-value: 5.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 4 LTLHLFSRSDSVVTGAISNGRP-ELPDADRMVGLFLNTVPVRSEIAGH-SWIEVADALFRQERDGHAHRRYPLSAIQQIV 81
Cdd:cd19543 254 LLLSRYSGRDDVVFGTTVSGRPaELPGIETMVGLFINTLPVRVRLDPDqTVLELLKDLQAQQLELREHEYVPLYEIQAWS 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 82 --GDEL-SSAFNYVNLHVLEPL--------WQLRDFRVWEETNFALlvNVIATPSDGMYLRIDSDGRGISRSQAALIGAT 150
Cdd:cd19543 334 egKQALfDHLLVFENYPVDESLeeeqdedgLRITDVSAEEQTNYPL--TVVAIPGEELTIKLSYDAEVFDEATIERLLGH 411
|
170
....*....|..
gi 1395399044 151 FVELLWRLAEHP 162
Cdd:cd19543 412 LRRVLEQVAANP 423
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
210-574 |
1.41e-16 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-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. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to 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.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 84.19 E-value: 1.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 210 RW-TYRDLDHVARCVATRLVRAGARRGDA--IGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRV 286
Cdd:cd05927 4 EWiSYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 287 VahpehahVAAAERVLPVEELV----ADIEPETFAAPqlDELAMLLFTSGSTGRPKGVELSHRMWANYTQ---WQLRVAS 359
Cdd:cd05927 84 F-------CDAGVKVYSLEEFEklgkKNKVPPPPPKP--EDLATICYTSGTTGNPKGVMLTHGNIVSNVAgvfKILEILN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 360 GV-PGLRTLQFAPLS--FDMAFQEifSTLCGGGELQLIS--NRERMDPSALL---------HVLER------------RQ 413
Cdd:cd05927 155 KInPTDVYISYLPLAhiFERVVEA--LFLYHGAKIGFYSgdIRLLLDDIKALkptvfpgvpRVLNRiydkifnkvqakGP 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 414 VQRVLLPFVALQRLAEASN-------------------ALGvrpGALRVVVSSGEQlrITEDVRAFCAAMPGLLLENQYG 474
Cdd:cd05927 233 LKRKLFNFALNYKLAELRSgvvraspfwdklvfnkikqALG---GNVRLMLTGSAP--LSPEVLEFLRVALGCPVLEGYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 475 PTETHQVTYHSLSGDPahypDLPPIGRPLDGVEVQVLDA------ALRPVPvgvTGELYFGGDCLARGYHRAPELTAERF 548
Cdd:cd05927 308 QTECTAGATLTLPGDT----SVGHVGGPLPCAEVKLVDVpemnydAKDPNP---RGEVCIRGPNVFSGYYKDPEKTAEAL 380
|
410 420
....*....|....*....|....*.
gi 1395399044 549 VEHPWrpgarlYRTGDLGRILGNGEI 574
Cdd:cd05927 381 DEDGW------LHTGDIGEWLPNGTL 400
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
323-673 |
4.26e-16 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 80.62 E-value: 4.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 323 ELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQE-IFSTLCGGGElqlISNRERMD 401
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAgIVACLLTGAT---VVPVAVFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 402 PSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRItEDVRAFCAAMPGLLLENQYGPTETHQV 481
Cdd:cd17638 78 VDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPV-ELVRRMRSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 482 TYHSLSGDPAHYPDlpPIGRPLDGVEVQVLDAalrpvpvgvtGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYR 561
Cdd:cd17638 157 TMCRPGDDAETVAT--TCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW------LH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 562 TGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGNDAflAAFLLG-EPEAV 638
Cdd:cd17638 219 TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALA----EHPGVAQVAVigVPDERMGEVG--KAFVVArPGVTL 292
|
330 340 350
....*....|....*....|....*....|....*
gi 1395399044 639 DLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:cd17638 293 TEEDVIAWCRERLANYKVPRFVRFLDELPRNASGK 327
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
175-353 |
4.48e-16 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 83.00 E-value: 4.48e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 175 RDAASQPEPLVDVvslFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWG 254
Cdd:PRK08279 30 LITPDSKRSLGDV---FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 255 ILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHV---AAAERVLPVEELVADIE------------------- 312
Cdd:PRK08279 107 LAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAfeeARADLARPPRLWVAGGDtlddpegyedlaaaaagap 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1395399044 313 ---PETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQW 353
Cdd:PRK08279 187 ttnPASRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGG 230
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
207-680 |
5.53e-16 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 82.51 E-value: 5.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 207 EEQRWTYRDLDHVARCVATRLVRA-GARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFR 285
Cdd:cd05928 38 DEVKWSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKC 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 286 VVAH----PEHAHVAAAERVLPVEELVADIEPE---------TFAAPQ--------LDELAmLLFTSGSTGRPKGVELSH 344
Cdd:cd05928 118 IVTSdelaPEVDSVASECPSLKTKLLVSEKSRDgwlnfkellNEASTEhhcvetgsQEPMA-IYFTSGTTGSPKMAEHSH 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 345 rmwanyTQWQLRVASGVPGLRTLQFAPLSFDM--------AFQEIFSTLCGGGELqLISNRERMDPSALLHVLERRQVQr 416
Cdd:cd05928 197 ------SSLGLGLKVNGRYWLDLTASDIMWNTsdtgwiksAWSSLFEPWIQGACV-FVHHLPRFDPLVILKTLSSYPIT- 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 417 VLLPFVALQRLAEASNALGVRPGALRVVVSSGEQlrITEDVRAFCAAMPGLLLENQYGPTETHQV--TYHSLSGDPAHyp 494
Cdd:cd05928 269 TFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEP--LNPEVLEKWKAQTGLDIYEGYGQTETGLIcaNFKGMKIKPGS-- 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 495 dlppIGRPLDGVEVQVLDAALRPVPVGVTGELY--------FggdCLARGYHRAPELTAERFVehpwrpgARLYRTGDLG 566
Cdd:cd05928 345 ----MGKASPPYDVQIIDDNGNVLPPGTEGDIGirvkpirpF---GLFSGYVDNPEKTAATIR-------GDFYLTGDRG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 567 RILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQ--GN--DAFL---AAFLLGEPEAVd 639
Cdd:cd05928 411 IMDEDGYFWFMGRADDVINSSGYRIGPFEVESALI----EHPAVVESAVVSSPDPirGEvvKAFVvlaPQFLSHDPEQL- 485
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 1395399044 640 LAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:cd05928 486 TKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELR 526
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
212-673 |
5.90e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 82.05 E-value: 5.90e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPE 291
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 292 HAHVAAA--------------------ERVLPVEELVADIePETfaaPQLDEL--AMLLFTSGSTGRPKGV--------- 340
Cdd:PRK13391 106 KLDVARAllkqcpgvrhrlvldgdgelEGFVGYAEAVAGL-PAT---PIADESlgTDMLYSSGTTGRPKGIkrplpeqpp 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 341 -------ELSHRMWaNYTQwQLRVASGVPGLRTlqfAPLSFDMAFQEIfstlcgGGELQLIsnrERMDPSALLHVLERRQ 413
Cdd:PRK13391 182 dtplpltAFLQRLW-GFRS-DMVYLSPAPLYHS---APQRAVMLVIRL------GGTVIVM---EHFDAEQYLALIEEYG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 414 V---QRVLLPFVALQRLAEAsnalgVRpgaLRVVVSSGEqlritedvRAFCAAMP-------------GLLLENQYGPTE 477
Cdd:PRK13391 248 VthtQLVPTMFSRMLKLPEE-----VR---DKYDLSSLE--------VAIHAAAPcppqvkeqmidwwGPIIHEYYAATE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 478 THQVTYhslsGDPAHYPDLP-PIGRPLDGVeVQVLDAALRPVPVGVTGELYFGGDcLARGYHRAPELTAERFVEHP-WRp 555
Cdd:PRK13391 312 GLGFTA----CDSEEWLAHPgTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEGG-RPFEYLNDPAKTAEARHPDGtWS- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 556 garlyRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGND--AFLAAFL 631
Cdd:PRK13391 385 -----TVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLI----THPKVADAAVfgVPNEDLGEEvkAVVQPVD 455
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1395399044 632 LGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK13391 456 GVDPGPALAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGK 497
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
207-601 |
8.12e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 81.87 E-value: 8.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 207 EEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYP----AQRL------AL 276
Cdd:PRK04319 70 RKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMeeavRDRLedseakVL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 277 ILETAQPFRVVA----HPEH-----AHVAAAERVLPVEELVADiEPETFAAP--QLDELAMLLFTSGSTGRPKGVELSHR 345
Cdd:PRK04319 150 ITTPALLERKPAddlpSLKHvllvgEDVEEGPGTLDFNALMEQ-ASDEFDIEwtDREDGAILHYTSGSTGKPKGVLHVHN 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 346 -MWANY--TQWQLRVASG-----------VPGLRTLQFAPLsfdmafqeifstLCGggeLQLISNRERMDPSALLHVLER 411
Cdd:PRK04319 229 aMLQHYqtGKYVLDLHEDdvywctadpgwVTGTSYGIFAPW------------LNG---ATNVIDGGRFSPERWYRILED 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 412 rqvQRVLLPF---VALQRLAEASNAL--GVRPGALRVVVSSGEQLR---ITEDVRAFcaampGLLLENQYGPTET--HQV 481
Cdd:PRK04319 294 ---YKVTVWYtapTAIRMLMGAGDDLvkKYDLSSLRHILSVGEPLNpevVRWGMKVF-----GLPIHDNWWMTETggIMI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 482 tyhslsgdpAHYP--DLPP--IGRPLDGVEVQVLDAALRPVPVGVTGELYF--GGDCLARGYHRAPELTAERFVEHpWrp 555
Cdd:PRK04319 366 ---------ANYPamDIKPgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAGD-W-- 433
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1395399044 556 garlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIM 601
Cdd:PRK04319 434 ----YVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLM 475
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
311-685 |
8.19e-16 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 82.66 E-value: 8.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 311 IEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQW-QL-------RVASGVP-----GLRTLQFAPLSF-- 374
Cdd:PRK08633 771 LKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHnILSNIEQIsDVfnlrnddVILSSLPffhsfGLTVTLWLPLLEgi 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 375 ---------------DMAFQEIFSTLCGGGE-LQLISNRERMDPsallhvlerrqvqrvlLPFvalqrlaeasnalgvrp 438
Cdd:PRK08633 851 kvvyhpdptdalgiaKLVAKHRATILLGTPTfLRLYLRNKKLHP----------------LMF----------------- 897
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 439 GALRVVVSSGEQLRitEDVR-AFCAAMPGLLLENqYGPTETHQVTyhSLSGDPAHYPDLPP--------IGRPLDGVEVQ 509
Cdd:PRK08633 898 ASLRLVVAGAEKLK--PEVAdAFEEKFGIRILEG-YGATETSPVA--SVNLPDVLAADFKRqtgskegsVGMPLPGVAVR 972
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 510 VLDA-ALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEhpwRPGARLYRTGDLGRILGNGEIVWLGRADTQVKVRG 588
Cdd:PRK08633 973 IVDPeTFEELPPGEDGLILIGGPQVMKGYLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGG 1049
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 589 FRIEPAEVELAIMRQAERQPGLRGAAVVARERQGNdaflAAFLLGEPEAVDLAELKQAL-RSELPEHMVPAHFAWVDGFA 667
Cdd:PRK08633 1050 EMVPLGAVEEELAKALGGEEVVFAVTAVPDEKKGE----KLVVLHTCGAEDVEELKRAIkESGLPNLWKPSRYFKVEALP 1125
|
410
....*....|....*...
gi 1395399044 668 LTPSGKRDDAALRALPLE 685
Cdd:PRK08633 1126 LLGSGKLDLKGLKELALA 1143
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
203-681 |
8.32e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 81.65 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 203 ALAFEEQRWTYRDLDHVARCVATRLV-RAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETA 281
Cdd:PRK07867 21 GLYFEDSFTSWREHIRGSAARAAALRaRLDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 282 QPFRVVAHPEHAHVAAAE----RVLPVE-----ELVADI--EPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMWAny 350
Cdd:PRK07867 101 DCQLVLTESAHAELLDGLdpgvRVINVDspawaDELAAHrdAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 351 tqwqlrvASGVP-----GLRTLQFAPLSFDMafqeiFST----------LCGGGELQLisnRERMDPSALLHVLER---- 411
Cdd:PRK07867 179 -------SAGVMlaqrfGLGPDDVCYVSMPL-----FHSnavmagwavaLAAGASIAL---RRKFSASGFLPDVRRygat 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 412 ------RQVQRVLlpfVALQRLAEASNalgvrpgALRVVVSSGEQLRiteDVRAFcAAMPGLLLENQYGPTETHQVTYHS 485
Cdd:PRK07867 244 yanyvgKPLSYVL---ATPERPDDADN-------PLRIVYGNEGAPG---DIARF-ARRFGCVVVDGFGSTEGGVAITRT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 486 lsgdpahyPDLPP--IGRPLDGveVQVLDAA-LRPVPVGV------------TGELY-FGGDCLARGYHRAPELTAERFv 549
Cdd:PRK07867 310 --------PDTPPgaLGPLPPG--VAIVDPDtGTECPPAEdadgrllnadeaIGELVnTAGPGGFEGYYNDPEADAERM- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 550 ehpwRPGarLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR-ERQGNDAFLA 628
Cdd:PRK07867 379 ----RGG--VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILL----RYPDATEVAVYAVpDPVVGDQVMA 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1395399044 629 AFLLGEPEAVDLAELKQAL--RSELPEHMVPAHFAWVDGFALTPSGKRDDAALRA 681
Cdd:PRK07867 449 ALVLAPGAKFDPDAFAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
485-773 |
2.39e-14 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 74.79 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 485 SLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEH--PWRPGARLYRT 562
Cdd:COG3433 2 AIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPfiPVPYPAQPGRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 563 GDLGRILGNGEIVWLGRADTQVKVRGFRIEPaEVELAIMRQAERQPGLRGAAVVARERQGNDAFLAAfLLGEPEAVDLAE 642
Cdd:COG3433 82 ADDLRLLLRRGLGPGGGLERLVQQVVIRAER-GEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIV-GAVAALDGLAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 643 LKQALRSELPEHMVPAHFAW-VDGFALTPSGKRDDAALRALPLEHGTNIEYLAPRDDYERTLAGL---LGELLDRP--RV 716
Cdd:COG3433 160 AALAALDKVPPDVVAASAVVaLDALLLLALKVVARAAPALAAAEALLAAASPAPALETALTEEELradVAELLGVDpeEI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1395399044 717 GIRDSFFDLGGTSLSAMRFMLLIEKRyGVDLPMAALIETPTVEGLAERLRERSAVRA 773
Cdd:COG3433 240 DPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
500-682 |
3.08e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 75.47 E-value: 3.08e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 500 GRPLDGVEVQVLDaalrpvpvgvtGELYFGGDCLARGYHRAPELTAerFVEHPWrpgarlYRTGDLGrILGNGEIVWLGR 579
Cdd:PRK07824 195 GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVDPDP--FAEPGW------FRTDDLG-ALDDGVLTVLGR 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 580 ADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV--VARERQGNdAFLAAFLLGEPEAVDLAELKQALRSELPEHMVP 657
Cdd:PRK07824 255 ADDAISTGGLTVLPQVVEAALA----THPAVADCAVfgLPDDRLGQ-RVVAAVVGDGGPAPTLEALRAHVARTLDRTAAP 329
|
170 180
....*....|....*....|....*
gi 1395399044 658 AHFAWVDGFALTPSGKRDDAALRAL 682
Cdd:PRK07824 330 RELHVVDELPRRGIGKVDRRALVRR 354
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
694-770 |
3.36e-14 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 68.73 E-value: 3.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 694 APRDDYERTLAGLLGELLDRP--RVGIRDSFF-DLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLRERSA 770
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDpeEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
212-618 |
5.51e-14 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 76.17 E-value: 5.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLA----------LILETA 281
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAkqakasgaklIITQSC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 282 QPFRVVAHPEHAHV------AAAERVLPVEELVADIE---PETFAAPqlDELAMLLFTSGSTGRPKGVELSHR-MWANYT 351
Cdd:PLN02246 132 YVDKLKGLAEDDGVtvvtidDPPEGCLHFSELTQADEnelPEVEISP--DDVVALPYSSGTTGLPKGVMLTHKgLVTSVA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 352 QwqlRVASGVPGL------RTLQFAPLsfdmaFQeIFS----TLCG---GGELQLISnreRMDPSALLHVLERRQVqrVL 418
Cdd:PLN02246 210 Q---QVDGENPNLyfhsddVILCVLPM-----FH-IYSlnsvLLCGlrvGAAILIMP---KFEIGALLELIQRHKV--TI 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 419 LPFVALQRLAEASNALGVRP--GALRVVVSS----GEQLritEDvrAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPAH 492
Cdd:PLN02246 276 APFVPPIVLAIAKSPVVEKYdlSSIRMVLSGaaplGKEL---ED--AFRAKLPNAVLGQGYGMTEAGPVLAMCLAFAKEP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 493 YPDLP-PIGRPLDGVEVQVLD----AALrpvPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGR 567
Cdd:PLN02246 351 FPVKSgSCGTVVRNAELKIVDpetgASL---PRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGW------LHTGDIGY 421
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1395399044 568 ILGNGEIVWLGRADTQVKVRGFRIEPAEVE-LAImrqaeRQPGLRGAAVVAR 618
Cdd:PLN02246 422 IDDDDELFIVDRLKELIKYKGFQVAPAELEaLLI-----SHPSIADAAVVPM 468
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
209-638 |
7.17e-14 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-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. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 75.92 E-value: 7.17e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 209 QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIatiWGILRA---GLVCVPLDVSYPAQRLALILETAQPFR 285
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWV---WAELAAqaiGALSLGIYQDSMAEEVAYLLNYTGARV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 286 VVAHPE-------------------------------HAHVAAAERVLPVEELVADIEPETF----AAPQLDELAMLLFT 330
Cdd:cd17641 87 VIAEDEeqvdklleiadripsvryviycdprgmrkydDPRLISFEDVVALGRALDRRDPGLYerevAAGKGEDVAVLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 331 SGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMafQEIFST----LCGGG----------------- 389
Cdd:cd17641 167 SGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWIG--EQMYSVgqalVCGFIvnfpeepetmmedlrei 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 390 ------------ELQLISNRERMDPS-------------ALLHVLERRQVQRVLLPFVALQR-LAEA------SNALGVR 437
Cdd:cd17641 245 gptfvllpprvwEGIAADVRARMMDAtpfkrfmfelgmkLGLRALDRGKRGRPVSLWLRLASwLADAllfrplRDRLGFS 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 438 pgALRVVVSSGEQLriTEDVRAFCAAMpGLLLENQYGPTETHQV-TYHslsgdPAHYPDLPPIGRPLDGVEVQVLDaalr 516
Cdd:cd17641 325 --RLRSAATGGAAL--GPDTFRFFHAI-GVPLKQLYGQTELAGAyTVH-----RDGDVDPDTVGVPFPGTEVRIDE---- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 517 pvpvgvTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRA-DTQVKVRGFRIEPAE 595
Cdd:cd17641 391 ------VGEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQF 458
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1395399044 596 VElaimRQAERQPGLRGAAVVARERQgndaFLAAFLLGEPEAV 638
Cdd:cd17641 459 IE----NKLKFSPYIAEAVVLGAGRP----YLTAFICIDYAIV 493
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
212-569 |
1.34e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 75.08 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPA-----QRLALILETAQPFRV 286
Cdd:PRK12582 82 TYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPRVV 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 287 VAH----------------PEHAHVAAA---ERVLPVEELVA-----DIEpETFAAPQLDELAMLLFTSGSTGRPKGVEL 342
Cdd:PRK12582 162 FAQsgapfaralaaldlldVTVVHVTGPgegIASIAFADLAAtpptaAVA-AAIAAITPDTVAKYLFTSGSTGMPKAVIN 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 343 SHRMWANYTQWQLRVASGVPGLR---TLQFAPLSFDMAFQEIFS-TLCGGGELQL-------------ISNRERMDP--- 402
Cdd:PRK12582 241 TQRMMCANIAMQEQLRPREPDPPppvSLDWMPWNHTMGGNANFNgLLWGGGTLYIddgkplpgmfeetIRNLREISPtvy 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 403 -------SALLHVLERRQVQRVLLpFVALQRLA-----------EASNALGVRPGALRVVVSSGeqlritedvrafcaam 464
Cdd:PRK12582 321 gnvpagyAMLAEAMEKDDALRRSF-FKNLRLMAyggatlsddlyERMQALAVRTTGHRIPFYTG---------------- 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 465 pglllenqYGPTETHQVTYhslsgdPAHYPDLPP--IGRPLDGVEVQVldaalrpVPVGVTGELYFGGDCLARGYHRAPE 542
Cdd:PRK12582 384 --------YGATETAPTTT------GTHWDTERVglIGLPLPGVELKL-------APVGDKYEVRVKGPNVTPGYHKDPE 442
|
410 420
....*....|....*....|....*..
gi 1395399044 543 LTAERFVEHPWrpgarlYRTGDLGRIL 569
Cdd:PRK12582 443 LTAAAFDEEGF------YRLGDAARFV 463
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
173-660 |
2.39e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 73.83 E-value: 2.39e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 173 PRRDAASQP-EPLvdvvSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIAT 251
Cdd:PRK08162 9 DRNAANYVPlTPL----SFLERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 252 IWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHVA-AAERVLPV------------------------EE 306
Cdd:PRK08162 85 HFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIVDTEFAEVArEALALLPGpkplvidvddpeypggrfigaldyEA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 307 LVADIEPETFAAPQLDEL-AMLL-FTSGSTGRPKGVELSHRMWAnytqwqLRVASGVpglrtlqfapLSFDMAFQEIF-S 383
Cdd:PRK08162 165 FLASGDPDFAWTLPADEWdAIALnYTSGTTGNPKGVVYHHRGAY------LNALSNI----------LAWGMPKHPVYlW 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 384 TL----CGGGelqliSNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNAlgvrPGALRVVVSSGEQLR--ITEDV 457
Cdd:PRK08162 229 TLpmfhCNGW-----CFPWTVAARAGTNVCLRKVDPKLIFDLIREHGVTHYCGA----PIVLSALINAPAEWRagIDHPV 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 458 RAFCAAMP------------GLLLENQYGPTETHQVTyhSLSGDPAHYPDLPPIGRP----LDGV------EVQVLDAA- 514
Cdd:PRK08162 300 HAMVAGAAppaaviakmeeiGFDLTHVYGLTETYGPA--TVCAWQPEWDALPLDERAqlkaRQGVryplqeGVTVLDPDt 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 515 LRPVPV-GVT-GELYFGGDCLARGYHRAPELTAERFvEHPWrpgarlYRTGDLGRILGNGEIvwlgradtQVKVR----- 587
Cdd:PRK08162 378 MQPVPAdGETiGEIMFRGNIVMKGYLKNPKATEEAF-AGGW------FHTGDLAVLHPDGYI--------KIKDRskdii 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 588 ---GFRIEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGND--AFLAaflLGEPEAVDLAELKQALRSELPEHMVPAHF 660
Cdd:PRK08162 443 isgGENISSIEVEDVLY----RHPAVLVAAVVAKpdPKWGEVpcAFVE---LKDGASATEEEIIAHCREHLAGFKVPKAV 515
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
192-673 |
2.84e-13 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 73.75 E-value: 2.84e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 192 ERQVEALPGSAALAFE------EQRWTYRDL-DHVARCvATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVP 264
Cdd:cd05966 60 DRHLKERGDKVAIIWEgdepdqSRTITYRELlREVCRF-ANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 265 LDVSYPAQRLA---------LILETAQPFR-------------------------VVAHPEHAHVAAAERVLPVEELVAD 310
Cdd:cd05966 139 VFAGFSAESLAdrindaqckLVITADGGYRggkviplkeivdealekcpsvekvlVVKRTGGEVPMTEGRDLWWHDLMAK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 311 IEPETFAAPqLDELAML--LFTSGSTGRPKGVELSHRMWANYTQwqlrvasgvpglRTLQFAplsFDMAFQEIF------ 382
Cdd:cd05966 219 QSPECEPEW-MDSEDPLfiLYTSGSTGKPKGVVHTTGGYLLYAA------------TTFKYV---FDYHPDDIYwctadi 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 383 ------STLCGG----GELQLIsnRERM----DPSALLHVLERRQVqrvllpfvalqrlaeasNALGVRPGALRVVVSSG 448
Cdd:cd05966 283 gwitghSYIVYGplanGATTVM--FEGTptypDPGRYWDIVEKHKV-----------------TIFYTAPTAIRALMKFG 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 449 EQ---------LRITEDV------RAF-----------CAAMpgllleNQYGPTET--HQVTyhslsgdpaHYPDLPPI- 499
Cdd:cd05966 344 DEwvkkhdlssLRVLGSVgepinpEAWmwyyevigkerCPIV------DTWWQTETggIMIT---------PLPGATPLk 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 500 ----GRPLDGVEVQVLDAALRPVPVGVTGELYF-----GgdcLARGYHRAPEltaeRFVEHPWRPGARLYRTGDLGRILG 570
Cdd:cd05966 409 pgsaTRPFFGIEPAILDEEGNEVEGEVEGYLVIkrpwpG---MARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDE 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 571 NGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGNdaFLAAFLL---GEPEAVDLA-ELK 644
Cdd:cd05966 482 DGYYWITGRVDDVINVSGHRLGTAEVESALV----AHPAVAEAAVVGRphDIKGE--AIYAFVTlkdGEEPSDELRkELR 555
|
570 580
....*....|....*....|....*....
gi 1395399044 645 QALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:cd05966 556 KHVRKEIGPIATPDKIQFVPGLPKTRSGK 584
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
183-617 |
4.85e-13 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 73.24 E-value: 4.85e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 183 PLVDVVSLFERQVEALPGSAAlafeeqrwtYRDLDHVA------------------RCVATRLVRAgARRGDAIGVALNR 244
Cdd:PRK12476 32 PGTTLISLIERNIANVGDTVA---------YRYLDHSHsaagcaveltwtqlgvrlRAVGARLQQV-AGPGDRVAILAPQ 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 245 SPEMIATIWGILRAGLVCVPL---DVSYPAQRLALILETAQPFRV-----VAHPEHAHVAA-----AERVLPVEElVADI 311
Cdd:PRK12476 102 GIDYVAGFFAAIKAGTIAVPLfapELPGHAERLDTALRDAEPTVVltttaAAEAVEGFLRNlprlrRPRVIAIDA-IPDS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 312 EPETFAAPQL--DELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGVPGLRTLQFAPLSFDMAFQEI-FSTLCg 387
Cdd:PRK12476 181 AGESFVPVELdtDDVSHLQYTSGSTRPPVGVEITHRaVGTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIgFPAVY- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 388 GGELQLisnrerMDPSALLhvleRRqvqrvllPFVALQRLAEAS---NALGVRP------GALRVVVSSGEQLRIT---- 454
Cdd:PRK12476 260 GGHSTL------MSPTAFV----RR-------PQRWIKALSEGSrtgRVVTAAPnfayewAAQRGLPAEGDDIDLSnvvl 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 455 ---------EDVRAFCAA-----MPGLLLENQYG------------PTETHQVTY---------HSLSGDPAHyPDLPP- 498
Cdd:PRK12476 323 iigsepvsiDAVTTFNKAfapygLPRTAFKPSYGiaeatlfvatiaPDAEPSVVYldreqlgagRAVRVAADA-PNAVAh 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 499 -----IGRPLDGVEVQvlDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFV----------EHPWR--PGARLYR 561
Cdd:PRK12476 402 vscgqVARSQWAVIVD--PDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegSHADGaaDDGTWLR 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1395399044 562 TGDLGRILGnGEIVWLGRADTQVKVRGFRIEPAEVELAImrqAERQPGLRGAAVVA 617
Cdd:PRK12476 480 TGDLGVYLD-GELYITGRIADLIVIDGRNHYPQDIEATV---AEASPMVRRGYVTA 531
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
220-686 |
5.58e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 72.88 E-value: 5.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 220 ARCVATRLVRAGarRGDAIGVALNRSPEMIATIWGILRAG--LVCVPLDV-SYPAQRLALilETAQPF------RVVAHP 290
Cdd:PRK05851 41 AENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGaaVSILPGPVrGADDGRWAD--ATLTRFagigvrTVLSHG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 291 EH-AHVAAAERVLPVEELV---ADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELS-HRMWANYTQWQLRVASGVPGLR 365
Cdd:PRK05851 117 SHlERLRAVDSSVTVHDLAtaaHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSpGAVLSNLRGLNARVGLDAATDV 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 366 TLQFAPLSFDMAFQEIFSTLCGGGELQLI-SNRERMDPSALLHVLERRQVQRVLLPFVALQRLAE-ASNALGVRPGALRV 443
Cdd:PRK05851 197 GCSWLPLYHDMGLAFLLTAALAGAPLWLApTTAFSASPFRWLSWLSDSRATLTAAPNFAYNLIGKyARRVSDVDLGALRV 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 444 VVSSGEQLRItEDVRAFCAAM------PGLLLENqYGPTE-THQVTY----HSLSGDPAHYPD------LPPIGRPLDGV 506
Cdd:PRK05851 277 ALNGGEPVDC-DGFERFATAMapfgfdAGAAAPS-YGLAEsTCAVTVpvpgIGLRVDEVTTDDgsgarrHAVLGNPIPGM 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 507 EVQVldaALRPVPVGVT----GELYFGGDCLARGYhrapeltaerFVEHPWRPGArLYRTGDLGrILGNGEIVWLGRADT 582
Cdd:PRK05851 355 EVRI---SPGDGAAGVAgreiGEIEIRGASMMSGY----------LGQAPIDPDD-WFPTGDLG-YLVDGGLVVCGRAKE 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 583 QVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVARERQGNDA----FLAAFLLGEPEAVDLAELKQALRSELpeHMVPA 658
Cdd:PRK05851 420 LITVAGRNIFPTEIE----RVAAQVRGVREGAVVAVGTGEGSArpglVIAAEFRGPDEAGARSEVVQRVASEC--GVVPS 493
|
490 500 510
....*....|....*....|....*....|
gi 1395399044 659 HFAWVDGFAL--TPSGKrddaaLRALPLEH 686
Cdd:PRK05851 494 DVVFVAPGSLprTSSGK-----LRRLAVKR 518
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
198-682 |
8.81e-13 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 72.30 E-value: 8.81e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 198 LPGSAALAfEEQRWTYRDL-DHVARCvATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCvPLDVSYPAQRLAL 276
Cdd:PRK07529 47 LLDADPLD-RPETWTYAELlADVTRT-ANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIAN-PINPLLEPEQIAE 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 277 ILE--------TAQPF----------RVVAH-PEHAHVA----------------------AAERVLPVEELVA---DIE 312
Cdd:PRK07529 124 LLRaagakvlvTLGPFpgtdiwqkvaEVLAAlPELRTVVevdlarylpgpkrlavplirrkAHARILDFDAELArqpGDR 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 313 PETFAAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANytQWQLRVASGVPGLRTLQFA-PLsFDM--AFQEIFSTLCGG 388
Cdd:PRK07529 204 LFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGnEVAN--AWLGALLLGLGPGDTVFCGlPL-FHVnaLLVTGLAPLARG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 389 GELQLISNRERMDPSALLH---VLERRQVQR-VLLPFV---ALQRLAEASNAlgvrpGALRVVVSSGEQLRItEDVRAFC 461
Cdd:PRK07529 281 AHVVLATPQGYRGPGVIANfwkIVERYRINFlSGVPTVyaaLLQVPVDGHDI-----SSLRYALCGAAPLPV-EVFRRFE 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 462 AAMpGLLLENQYGPTETHQVtyHSLSgdpahYPDLPP----IGRPLDGVEVQVL-----DAALRPVPVGVTGELYFGGDC 532
Cdd:PRK07529 355 AAT-GVRIVEGYGLTEATCV--SSVN-----PPDGERrigsVGLRLPYQRVRVVilddaGRYLRDCAVDEVGVLCIAGPN 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 533 LARGYhrapeLTAERfvEHPWRPGARLYRTGDLGRILGNGeIVWL-GRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLR 611
Cdd:PRK07529 427 VFSGY-----LEAAH--NKGLWLEDGWLNTGDLGRIDADG-YFWLtGRAKDLIIRGGHNIDPAAIEEALL----RHPAVA 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 612 GAAVVARErqgnDAF-----LAAFLLGEPEAVDLAELKQALRSELPEH-MVPAHFAWVDGFALTPSGK------RDDAAL 679
Cdd:PRK07529 495 LAAAVGRP----DAHagelpVAYVQLKPGASATEAELLAFARDHIAERaAVPKHVRILDALPKTAVGKifkpalRRDAIR 570
|
...
gi 1395399044 680 RAL 682
Cdd:PRK07529 571 RVL 573
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1-163 |
1.34e-12 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 71.21 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 1 AHCLTLHLFSRSDSVVTGAISNGRPElPDADRMVGLFLNTVPVRSEIAGH-SWIEVADALFRQERDGHAHRRYPL----- 74
Cdd:pfam00668 258 AYGLLLSRYTGQDDIVVGTPGSGRPS-PDIERMVGMFVNTLPLRIDPKGGkTFSELIKRVQEDLLSAEPHQGYPFgdlvn 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 75 -SAIQQIVGDE--LSSAFNYVNL---HVLEPLWQLRDFRV------WEETNFALlvNVIATPSDG-MYLRIDSDGRGISR 141
Cdd:pfam00668 337 dLRLPRDLSRHplFDPMFSFQNYlgqDSQEEEFQLSELDLsvssviEEEAKYDL--SLTASERGGgLTIKIDYNTSLFDE 414
|
170 180
....*....|....*....|..
gi 1395399044 142 SQAALIGATFVELLWRLAEHPD 163
Cdd:pfam00668 415 ETIERFAEHFKELLEQAIAHPS 436
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
198-616 |
1.36e-12 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; 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: 341297 [Multi-domain] Cd Length: 532 Bit Score: 71.40 E-value: 1.36e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 198 LPGSAAL--AFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLA 275
Cdd:cd17642 30 VPGTIAFtdAHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 276 LILETAQPFRVVAHPEhahvaAAERVLPVEELVADIEP----------------ETF-----------------AAPQLD 322
Cdd:cd17642 110 HSLNISKPTIVFCSKK-----GLQKVLNVQKKLKIIKTiiildskedykgyqclYTFitqnlppgfneydfkppSFDRDE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 323 ELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASG---VPGLRTLQFAPLSFDMAFQEIFSTLCGGGELQLISnreR 399
Cdd:cd17642 185 QVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGnqiIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMY---K 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 400 MDPSALLHVLERRQVQRVLL-----PFVALQRLAEA---SNalgvrpgaLRVVVSSGEQL-RITEDVRAFCAAMPGllLE 470
Cdd:cd17642 262 FEEELFLRSLQDYKVQSALLvptlfAFFAKSTLVDKydlSN--------LHEIASGGAPLsKEVGEAVAKRFKLPG--IR 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 471 NQYGPTETHQVTYHSLSGDpahypDLP-PIGRPLDGVEVQVLDAAL-RPVPVGVTGELYFGGDCLARGYHRAPELTAERF 548
Cdd:cd17642 332 QGYGLTETTSAILITPEGD-----DKPgAVGKVVPFFYAKVVDLDTgKTLGPNERGELCVKGPMIMKGYVNNPEATKALI 406
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395399044 549 VEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElAIMRQaerQPGLRGAAVV 616
Cdd:cd17642 407 DKDGW------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELE-SILLQ---HPKIFDAGVA 464
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
322-653 |
1.45e-12 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 71.45 E-value: 1.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 322 DELAMLLFTSGSTGRPKGVELSHR-MWANYTQ---WQLRVASGVPGLRTLQ--------FAPLSFDMAFQEIfstlcgGG 389
Cdd:PRK08751 208 DDIAFLQYTGGTTGVAKGAMLTHRnLVANMQQahqWLAGTGKLEEGCEVVItalplyhiFALTANGLVFMKI------GG 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 390 ELQLISNRERMdPSALlhvlerRQVQRVllPFVALQRLAEASNALGVRPGALRVVVSS-----GEQLRITEDVRAFCAAM 464
Cdd:PRK08751 282 CNHLISNPRDM-PGFV------KELKKT--RFTAFTGVNTLFNGLLNTPGFDQIDFSSlkmtlGGGMAVQRSVAERWKQV 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 465 PGLLLENQYGPTETHQvtyhSLSGDPAHYPDLP-PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPEL 543
Cdd:PRK08751 353 TGLTLVEAYGLTETSP----AACINPLTLKEYNgSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEE 428
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 544 TAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE--LAIMrqaerqPG-LRGAAV-VARE 619
Cdd:PRK08751 429 TAKVMDADGW------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEdvIAMM------PGvLEVAAVgVPDE 496
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1395399044 620 RQG---------NDAFLAAFLLGEPEAVDLAELKQA----LRSELPE 653
Cdd:PRK08751 497 KSGeivkvvivkKDPALTAEDVKAHARANLTGYKQPriieFRKELPK 543
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
781-1055 |
1.55e-12 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 68.34 E-value: 1.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 781 RAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGST--PLAVLEDIAASYLAAIRRvQPEGPYYLGGW 858
Cdd:COG3208 1 PRPDARLRLFCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGRGDRLGepPLTSLEELADDLAEELAP-LLDRPFALFGH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 859 SFGGFVAYEMARQLRALDPQAVAQLIVldS------ITVDRNHAGSASDEALLlffyWELVWFERSDEEVEPLPEGASLe 932
Cdd:COG3208 80 SMGALLAFELARRLERRGRPLPAHLFV--SgrraphLPRRRRPLHDLSDAELL----AELRRLGGTPEEVLADPELLEL- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 933 qkldhiveraieagVLPAgtpratvqrlyelFRASWQALIGYRPevsdqdmtllRADGPLPLalkPMHDAAGTHygDPK- 1011
Cdd:COG3208 153 --------------FLPI-------------LRADFRLLETYRY----------TPGPPLDC---PITALGGDD--DPLv 190
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1395399044 1012 -----NGWQHWTSGRLDVIDVPGDHLVLMKEPyvETVAAEIAALLEPST 1055
Cdd:COG3208 191 speelAAWREHTTGPFRLRVFPGGHFFLRDHP--AELLALIRAALAALA 237
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
182-637 |
2.33e-12 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 71.03 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 182 EPLVDVVS-LFERQveALPGSAAL--AFEEQRWTYRDLDHVARCVATRLVRA-GARRGDAIGVALNRSPEMIATIWGILR 257
Cdd:PLN02574 37 DPNLDAVSfIFSHH--NHNGDTALidSSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLS 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 258 AGLVCVPLD-VSYPAQRLALILETA--------------QPFR--VVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQ 320
Cdd:PLN02574 115 LGGIVTTMNpSSSLGEIKKRVVDCSvglaftspenveklSPLGvpVIGVPENYDFDSKRIEFPKFYELIKEDFDFVPKPV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 321 L--DELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGV---PGLRTLQFAPLS-FDMAFQEIFSTlcggGELQLI 394
Cdd:PLN02574 195 IkqDDVAAIMYSSGTTGASKGVVLTHRNLIAMVELFVRFEASQyeyPGSDNVYLAALPmFHIYGLSLFVV----GLLSLG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 395 SN---RERMDPSALLHVLERRQVQRvlLPFVA--LQRLAEASNALGVRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLL 469
Cdd:PLN02574 271 STivvMRRFDASDMVKVIDRFKVTH--FPVVPpiLMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 470 ENQYGPTETHQVTYHSLSGDpaHYPDLPPIGRPLDGVEVQVLD---AALrpVPVGVTGELYFGGDCLARGYHRAPELTAE 546
Cdd:PLN02574 349 IQGYGMTESTAVGTRGFNTE--KLSKYSSVGLLAPNMQAKVVDwstGCL--LPPGNCGELWIQGPGVMKGYLNNPKATQS 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 547 RFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGNDAF 626
Cdd:PLN02574 425 TIDKDGW------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLI----SHPEIIDAAVTAVPDKECGEI 494
|
490
....*....|.
gi 1395399044 627 LAAFLLGEPEA 637
Cdd:PLN02574 495 PVAFVVRRQGS 505
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
224-681 |
3.26e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 70.42 E-value: 3.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 224 ATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVV----------AHPEHA 293
Cdd:PRK05857 55 AADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALvapgskmassAVPEAL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 294 HVAAAERV-LPVEELVADIEPET-FAAPQL-----DELAMLlFTSGSTGRPKGVELSHRMW-----------ANYTQWql 355
Cdd:PRK05857 135 HSIPVIAVdIAAVTRESEHSLDAaSLAGNAdqgseDPLAMI-FTSGTTGEPKAVLLANRTFfavpdilqkegLNWVTW-- 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 356 rvasgVPGLRTLQFAPLSFDMAFQEIFSTLCGGGelQLISNRERMdpSALLHVLERRQVQRVLLPFVALQRLAEASNALG 435
Cdd:PRK05857 212 -----VVGETTYSPLPATHIGGLWWILTCLMHGG--LCVTGGENT--TSLLEILTTNAVATTCLVPTLLSKLVSELKSAN 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 436 VRPGALRVVVSSGEQLrITEDVRAFCAAmpGLLLENQYGPTEThQVTYHSLSGDPAHYPDLP--PIGRPLDGVEVQVLDA 513
Cdd:PRK05857 283 ATVPSLRLVGYGGSRA-IAADVRFIEAT--GVRTAQVYGLSET-GCTALCLPTDDGSIVKIEagAVGRPYPGVDVYLAAT 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 514 ------ALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHpWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVR 587
Cdd:PRK05857 359 dgigptAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLIDG-W------VNTGDLLERREDGFFYIKGRSSEMIICG 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 588 GFRIEPAEVElaimRQAERQPGLRGAAV--VARERQGNDAFLAAFLLGEPEAVDLAELKQAL----RSELPEHMVPAHFA 661
Cdd:PRK05857 432 GVNIAPDEVD----RIAEGVSGVREAACyeIPDEEFGALVGLAVVASAELDESAARALKHTIaarfRRESEPMARPSTIV 507
|
490 500
....*....|....*....|
gi 1395399044 662 WVDGFALTPSGKRDDAALRA 681
Cdd:PRK05857 508 IVTDIPRTQSGKVMRASLAA 527
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
203-681 |
8.19e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 68.90 E-value: 8.19e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 203 ALAFEEQRWTYRDldHVARCVATRLVRAGARRGDA---IGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILE 279
Cdd:PRK13388 19 AVRYGDRTWTWRE--VLAEAAARAAALIALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 280 TAQPFRVVAHPEHAHV-----AAAERVLPVE-----ELVA---DIEPETFAAPqlDELAMLLFTSGSTGRPKGVELSHRM 346
Cdd:PRK13388 97 RADCQLLVTDAEHRPLldgldLPGVRVLDVDtpayaELVAaagALTPHREVDA--MDPFMLIFTSGTTGAPKAVRCSHGR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 347 W-----------------------------ANYTQWQLRVASGVPGLRTLQFAPLSF--DMA-FQEIFSTLCGGGELQLI 394
Cdd:PRK13388 175 LafagralterfgltrddvcyvsmplfhsnAVMAGWAPAVASGAAVALPAKFSASGFldDVRrYGATYFNYVGKPLAYIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 395 SNRERMDpsallhvlerrqvqrvllpfvalqrlaEASNALGVRPGalrvvvSSGEQLRITEDVRAFcaampGLLLENQYG 474
Cdd:PRK13388 255 ATPERPD---------------------------DADNPLRVAFG------NEASPRDIAEFSRRF-----GCQVEDGYG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 475 PTEThqvtyhslSGDPAHYPDLPP--IGRPLDGVEVQVLDaALRPVPVGV-------------TGELY-FGGDCLARGYH 538
Cdd:PRK13388 297 SSEG--------AVIVVREPGTPPgsIGRGAPGVAIYNPE-TLTECAVARfdahgallnadeaIGELVnTAGAGFFEGYY 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 539 RAPELTAERfVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElAIMRqaeRQPGLRGAAV--V 616
Cdd:PRK13388 368 NNPEATAER-MRHGM------YWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIE-RILL---RHPAINRVAVyaV 436
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395399044 617 ARERQGnDAFLAAFLLGEPEAVDLAELKQALRS--ELPEHMVPAHFAWVDGFALTPSGKRDDAALRA 681
Cdd:PRK13388 437 PDERVG-DQVMAALVLRDGATFDPDAFAAFLAAqpDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
701-759 |
1.13e-11 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 61.04 E-value: 1.13e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395399044 701 RTLAGLLGELLDRP--RVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVE 759
Cdd:pfam00550 1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
227-681 |
1.31e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 68.91 E-value: 1.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 227 LVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPL-------DVSYPAQrlalilETAQPFRVVAHPEHAHVAAAE 299
Cdd:PRK06060 47 LRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLAnpelhrdDHALAAR------NTEPALVVTSDALRDRFQPSR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 300 RVLPVEEL--VADIEPETFAAPQLDELAMLLFTSGSTGRPKGVelSHRMWANYT------QWQLRVASGVPGLRT--LQF 369
Cdd:PRK06060 121 VAEAAELMseAARVAPGGYEPMGGDALAYATYTSGTTGPPKAA--IHRHADPLTfvdamcRKALRLTPEDTGLCSarMYF 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 370 A-----PLSFDMAF--QEIFSTLCGGGELQLISNrERMDPSALLHVLErrqvqrvllpFVAlqRLAEASNALGVRpgALR 442
Cdd:PRK06060 199 AyglgnSVWFPLATggSAVINSAPVTPEAAAILS-ARFGPSVLYGVPN----------FFA--RVIDSCSPDSFR--SLR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 443 VVVSSGEQLR--ITEDVRAFCAAMPGLlleNQYGPTETHQvTYHSLSGDPAHYPDLppiGRPLDGVEVQVLDAALRPVPV 520
Cdd:PRK06060 264 CVVSAGEALElgLAERLMEFFGGIPIL---DGIGSTEVGQ-TFVSNRVDEWRLGTL---GRVLPPYEIRVVAPDGTTAGP 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 521 GVTGELYFGGDCLARGYHRAPE--LTAERFVEhpwrpgarlyrTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVEL 598
Cdd:PRK06060 337 GVEGDLWVRGPAIAKGYWNRPDspVANEGWLD-----------TRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVER 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 599 AIMrqaERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVD---LAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRD 675
Cdd:PRK06060 406 LII---EDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDgsvMRDLHRGLLNRLSAFKVPHRFAVVDRLPRTPNGKLV 482
|
....*.
gi 1395399044 676 DAALRA 681
Cdd:PRK06060 483 RGALRK 488
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
209-597 |
2.97e-11 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-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. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 67.11 E-value: 2.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 209 QRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVV- 287
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 288 ----AHPEHAHVAAAE---RVLPV----------EELVADIEPETFAAPQLDE-LAMLLFTSGSTGRPKGVELSHRMWAN 349
Cdd:cd05932 85 gkldDWKAMAPGVPEGlisISLPPpsaancqyqwDDLIAQHPPLEERPTRFPEqLATLIYTSGTTGQPKGVMLTFGSFAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 350 YTQWQLRVASGVPGLRTLQFAPLS--FDMAFQEIfSTLCGGGEL-------QLISNRERMDPSALLHV--LERRQVQRVL 418
Cdd:cd05932 165 AAQAGIEHIGTEENDRMLSYLPLAhvTERVFVEG-GSLYGGVLVafaesldTFVEDVQRARPTLFFSVprLWTKFQQGVQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 419 --LPFVALQRLAEAS--NALGVRpgalRVVVSSG-EQLRItedvrAFCAAMP------------GLLLENQYGPTETHQV 481
Cdd:cd05932 244 dkIPQQKLNLLLKIPvvNSLVKR----KVLKGLGlDQCRL-----AGCGSAPvppallewyrslGLNILEAYGMTENFAY 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 482 TYHSLSGDPahypDLPPIGRPLDGVEVQVLDaalrpvpvgvTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYR 561
Cdd:cd05932 315 SHLNYPGRD----KIGTVGNAGPGVEVRISE----------DGEILVRSPALMMGYYKDPEATAEAFTADGF------LR 374
|
410 420 430
....*....|....*....|....*....|....*..
gi 1395399044 562 TGDLGRILGNGEIVWLGRADTQVKV-RGFRIEPAEVE 597
Cdd:cd05932 375 TGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIE 411
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
174-685 |
3.08e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 67.68 E-value: 3.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 174 RRDAASQPepLVDVVS------------LFERQVEAL----PGSAALA-FEEQRWTYRDLDHVARcVATRLVRAGARRGD 236
Cdd:PRK06814 607 RRSAAGAA--LYDIMSdmmfetsdydrtLFEALIEAAkihgFKKLAVEdPVNGPLTYRKLLTGAF-VLGRKLKKNTPPGE 683
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 237 AIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVVA----------HPEHAHVAAAERVLPVEE 306
Cdd:PRK06814 684 NVGVMLPNANGAAVTFFALQSAGRVPAMINFSAGIANILSACKAAQVKTVLTsrafiekarlGPLIEALEFGIRIIYLED 763
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 307 LVADIEPE--------------TFAAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGvpglrtlqfap 371
Cdd:PRK06814 764 VRAQIGLAdkikgllagrfplvYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRnLLANRAQVAARIDFS----------- 832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 372 lSFDMAFQ--EIFST--LCGGGELQLISN-RERMDPSAlLHVlerRQVQRVLLPFVA---------LQRLAEASNALGVR 437
Cdd:PRK06814 833 -PEDKVFNalPVFHSfgLTGGLVLPLLSGvKVFLYPSP-LHY---RIIPELIYDTNAtilfgtdtfLNGYARYAHPYDFR 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 438 pgALRVVVSSGEQLRitEDVRAFCAAMPGLLLENQYGPTETHQVTyhSLSgDPAHYpDLPPIGRPLDGVEvqvldAALRP 517
Cdd:PRK06814 908 --SLRYVFAGAEKVK--EETRQTWMEKFGIRILEGYGVTETAPVI--ALN-TPMHN-KAGTVGRLLPGIE-----YRLEP 974
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 518 VPvGVT--GELYFGGDCLARGYHRApelTAERFVEHP---WrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIE 592
Cdd:PRK06814 975 VP-GIDegGRLFVRGPNVMLGYLRA---ENPGVLEPPadgW------YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMIS 1044
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 593 PAEVELAImrqAERQPGLRGAAV-VARERQGNDAFLaafLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPS 671
Cdd:PRK06814 1045 LAAVEELA---AELWPDALHAAVsIPDARKGERIIL---LTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGT 1118
|
570
....*....|....
gi 1395399044 672 GKRDDAALRALPLE 685
Cdd:PRK06814 1119 GKIDYVAVTKLAEE 1132
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
212-651 |
3.38e-11 |
|
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: 67.13 E-value: 3.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRlalILETAQPFRVVAHPe 291
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEH---KLKLNKVWNTLKNP- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 292 hahvaaaerVLPVEELVADIEPetfaapqlDELAMLLFTSGSTGRPKGVELSH-------RMWANYTQWQLRVasgvpgl 364
Cdd:cd05908 93 ---------YLITEEEVLCELA--------DELAFIQFSSGSTGDPKGVMLTHenlvhnmFAILNSTEWKTKD------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 365 RTLQFAPLSFDM---AFQeiFSTLCGGGELQLISNRERM-DPSALLHVLERRQVQRVLLPFVA----LQRLaEASNALGV 436
Cdd:cd05908 149 RILSWMPLTHDMgliAFH--LAPLIAGMNQYLMPTRLFIrRPILWLKKASEHKATIVSSPNFGykyfLKTL-KPEKANDW 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 437 RPGALRVVVSSGEQLrITEDVRAFCAAMP--GL----------LLENQYG----PTETHQVTY-----HSLSGDPAHYPD 495
Cdd:cd05908 226 DLSSIRMILNGAEPI-DYELCHEFLDHMSkyGLkrnailpvygLAEASVGaslpKAQSPFKTItlgrrHVTHGEPEPEVD 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 496 --------LPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGR 567
Cdd:cd05908 305 kkdsecltFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW------LKTGDLGF 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 568 ILgNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVA----RERQGNDAFLaAFLLGEPEAVDLAEL 643
Cdd:cd05908 379 IR-NGRLVITGREKDIIFVNGQNVYPHDIE----RIAEELEGVELGRVVAcgvnNSNTRNEEIF-CFIEHRKSEDDFYPL 452
|
....*...
gi 1395399044 644 KQALRSEL 651
Cdd:cd05908 453 GKKIKKHL 460
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
212-673 |
3.44e-11 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 66.97 E-value: 3.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLA-----------LILE- 279
Cdd:PRK07059 50 TYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEhqlkdsgaeaiVVLEn 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 280 ---TAQpfRVVAHPEHAHVAAA--------------------ERVLPVEEL---------VADIEPETFAAPQL--DELA 325
Cdd:PRK07059 130 fatTVQ--QVLAKTAVKHVVVAsmgdllgfkghivnfvvrrvKKMVPAWSLpghvrfndaLAEGARQTFKPVKLgpDDVA 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 326 MLLFTSGSTGRPKGVELSHR-MWANYTQ---WqLRVASGVPG----LRTLQFAPLsfdmafQEIFS-TLCG------GGE 390
Cdd:PRK07059 208 FLQYTGGTTGVSKGATLLHRnIVANVLQmeaW-LQPAFEKKPrpdqLNFVCALPL------YHIFAlTVCGllgmrtGGR 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 391 LQLISNRErmDPSALLHVLERRQVQRvllpFVALQRLAeasNALGVRPGALRV-----VVSSGEQLRITEDVRAFCAAMP 465
Cdd:PRK07059 281 NILIPNPR--DIPGFIKELKKYQVHI----FPAVNTLY---NALLNNPDFDKLdfsklIVANGGGMAVQRPVAERWLEMT 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 466 GLLLENQYGPTETHQVtyhsLSGDPAHYPDLP-PIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELT 544
Cdd:PRK07059 352 GCPITEGYGLSETSPV----ATCNPVDATEFSgTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDET 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 545 AERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPG-LRGAAV-VARERQG 622
Cdd:PRK07059 428 AKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIE----EVVASHPGvLEVAAVgVPDEHSG 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1395399044 623 NdaFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK07059 498 E--AVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGK 546
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
206-680 |
9.11e-11 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 65.53 E-value: 9.11e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 206 FEEQRWTYRDLDHVARCVATRLVRA-GARRGDAIGVALNRSPEMIATIWGILRAGlvCVPLDVSYPAQRLALIletaqpf 284
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIG--AAPAFINYNLSGDPLI------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 285 rvvahpehaHVAaaeRVLPVEELVADIepetfaapqlDELAMLLFTSGSTGRPKGVELSHRMwaNYTQWQLR--VASGVP 362
Cdd:cd05937 72 ---------HCL---KLSGSRFVIVDP----------DDPAILIYTSGTTGLPKAAAISWRR--TLVTSNLLshDLNLKN 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 363 GLRTLQFAPLSFDMAFQEIF-STLCGGGELQL-----ISN--RERMDPSALlHVLERRQVQRVLL-----PFVALQRLAE 429
Cdd:cd05937 128 GDRTYTCMPLYHGTAAFLGAcNCLMSGGTLALsrkfsASQfwKDVRDSGAT-IIQYVGELCRYLLstppsPYDRDHKVRV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 430 ASNAlGVRP---GALR---VVVSSGEQLRITEDVRAF-----------CAAMPGLL----LENQYGPtethqVTYHSLSG 488
Cdd:cd05937 207 AWGN-GLRPdiwERFRerfNVPEIGEFYAATEGVFALtnhnvgdfgagAIGHHGLIrrwkFENQVVL-----VKMDPETD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 489 DPahypdlppIGRPLDGVEVQVldaalrpvPVGVTGE----LYFGGDCLARGYHRAPELTAERFVEHPWRPGARLYRTGD 564
Cdd:cd05937 281 DP--------IRDPKTGFCVRA--------PVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGD 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 565 LGRILGNGEIVWLGRADTQVKVRGFRIEPAEVElaimRQAERQPGLRGAAVVARERQGND--AFLAAFLLGE----PEAV 638
Cdd:cd05937 345 LLRQDADGRWYFLDRLGDTFRWKSENVSTTEVA----DVLGAHPDIAEANVYGVKVPGHDgrAGCAAITLEEssavPTEF 420
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1395399044 639 DLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:cd05937 421 TKSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVLR 462
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
192-673 |
1.38e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 65.05 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 192 ERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPA 271
Cdd:PRK06710 31 EQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 272 QRLA---------------LILETAQPFRVVAHPEHAHVAAAERVLP--------------------VEE-----LVADI 311
Cdd:PRK06710 111 RELEyqlhdsgakvilcldLVFPRVTNVQSATKIEHVIVTRIADFLPfpknllypfvqkkqsnlvvkVSEsetihLWNSV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 312 EPETFAAPQL-----DELAMLLFTSGSTGRPKGVELSHRMWANYT----QWQLRVASGVPG-LRTLQFAPLSFDMAFQEI 381
Cdd:PRK06710 191 EKEVNTGVEVpcdpeNDLALLQYTGGTTGFPKGVMLTHKNLVSNTlmgvQWLYNCKEGEEVvLGVLPFFHVYGMTAVMNL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 382 fsTLCGGGELQLISnreRMDPSALLHVLERRQVqrVLLPFVALQRLAEASNAL--GVRPGALRVVVSSGEQLRItEDVRA 459
Cdd:PRK06710 271 --SIMQGYKMVLIP---KFDMKMVFEAIKKHKV--TLFPGAPTIYIALLNSPLlkEYDISSIRACISGSAPLPV-EVQEK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 460 FCAAMPGLLLENqYGPTETHQVTYHSLSGDPAhypdLP-PIGRPLDGVEVQVLD----AALRPvpvGVTGELYFGGDCLA 534
Cdd:PRK06710 343 FETVTGGKLVEG-YGLTESSPVTHSNFLWEKR----VPgSIGVPWPDTEAMIMSletgEALPP---GEIGEIVVKGPQIM 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 535 RGYHRAPELTAErFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQAERQpglRGAA 614
Cdd:PRK06710 415 KGYWNKPEETAA-VLQDGW------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQ---EVVT 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1395399044 615 VVARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK06710 485 IGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGK 543
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
199-631 |
3.70e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 63.35 E-value: 3.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAFEEQRWTYRDL-DHVARcVATRLVRAGARRGDaiGVAL---NrSPEMIATIWGILRAGLVCVPLDVSYPAQRL 274
Cdd:PRK09029 17 PQAIALRLNDEVLTWQQLcARIDQ-LAAGFAQQGVVEGS--GVALrgkN-SPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 275 ALILETAQpFRVVAHPEHAHVAAAERVLPVEELVADIEpetfAAPQLDELAMLLFTSGSTGRPKGVELSHRMwanytqwQ 354
Cdd:PRK09029 93 EELLPSLT-LDFALVLEGENTFSALTSLHLQLVEGAHA----VAWQPQRLATMTLTSGSTGLPKAAVHTAQA-------H 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 355 LRVASGVpgLRTLQFAP-----LS---FDMAFQEIF-STLCGGGELQLisnRERMD-PSALLHV----LERRQVQRVL-- 418
Cdd:PRK09029 161 LASAEGV--LSLMPFTAqdswlLSlplFHVSGQGIVwRWLYAGATLVV---RDKQPlEQALAGCthasLVPTQLWRLLdn 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 419 --LPfVALQR-----------LAEASNALGvrpgalrvvvssgeqlritedVRAFCAampglllenqYGPTE---ThqVT 482
Cdd:PRK09029 236 rsEP-LSLKAvllggaaipveLTEQAEQQG---------------------IRCWCG----------YGLTEmasT--VC 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 483 ---YHSLSGdpahypdlppIGRPLDGVEVQVldaalrpvpvgVTGELYFGGDCLARGYHRAPELTAerFV-EHPWrpgar 558
Cdd:PRK09029 282 akrADGLAG----------VGSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLVP--LVnDEGW----- 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 559 lYRTGDLGRILGnGEIVWLGRADTQVKVRGFRIEPAEVELAIM-----RQA------ERQPGLRGAAVVARERQGNDAFL 627
Cdd:PRK09029 334 -FATRDRGEWQN-GELTILGRLDNLFFSGGEGIQPEEIERVINqhplvQQVfvvpvaDAEFGQRPVAVVESDSEAAVVNL 411
|
....
gi 1395399044 628 AAFL 631
Cdd:PRK09029 412 AEWL 415
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
208-567 |
4.35e-10 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 63.60 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 208 EQRW---TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQ-----RLALILE 279
Cdd:cd05921 20 NGGWrrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLMsqdlaKLKHLFE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 280 TAQPFRVVA----------------HPEHAHV---AAAERVLPVEELVADIE----PETFAAPQLDELAMLLFTSGSTGR 336
Cdd:cd05921 100 LLKPGLVFAqdaapfaralaaifplGTPLVVSrnaVAGRGAISFAELAATPPtaavDAAFAAVGPDTVAKFLFTSGSTGL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 337 PKGVELSHRMWANyTQWQLRVASGVPG---LRTLQFAPLSFDMAFQEIFS-TLCGGGEL-------------QLISNRER 399
Cdd:cd05921 180 PKAVINTQRMLCA-NQAMLEQTYPFFGeepPVLVDWLPWNHTFGGNHNFNlVLYNGGTLyiddgkpmpggfeETLRNLRE 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 400 MDPSALLHV----------------LERRQVQRVLLPFVALQRLA----EASNALGVRPGALRVVVSSGeqlritedvra 459
Cdd:cd05921 259 ISPTVYFNVpagwemlvaalekdeaLRRRFFKRLKLMFYAGAGLSqdvwDRLQALAVATVGERIPMMAG----------- 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 460 fcaampglllenqYGPTETHQVTY--HSLSGDPAHypdlppIGRPLDGVEVQVldaalrpVPVGVTGELYFGGDCLARGY 537
Cdd:cd05921 328 -------------LGATETAPTATftHWPTERSGL------IGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGY 381
|
410 420 430
....*....|....*....|....*....|
gi 1395399044 538 HRAPELTAERFVEHPWrpgarlYRTGDLGR 567
Cdd:cd05921 382 WRQPELTAQAFDEEGF------YCLGDAAK 405
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
187-388 |
4.72e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 63.59 E-value: 4.72e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 187 VVSLFERQVEALPGSAALAF---------EEQRWTYRDLDHVARCVATRLVRAGaRRGDAIGVALNRSPEMIATIWGILR 257
Cdd:PRK07769 23 LVRHVERWAKVRGDKLAYRFldfsterdgVARDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 258 AGLVCVPL-DVSYP--AQRLALILETAQPFRVVAHPEHA--------HVAAAER--VLPVEElVADIEPETFAAPQLDE- 323
Cdd:PRK07769 102 AGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAegvrkffrARPAKERprVIAVDA-VPDEVGATWVPPEANEd 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395399044 324 -LAMLLFTSGSTGRPKGVELSHRMWANYTQWQLRVASGVPGLRTLQFAPLSFDMAF-QEIFSTLCGG 388
Cdd:PRK07769 181 tIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLiTVLLPALLGH 247
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1-162 |
5.21e-10 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 62.71 E-value: 5.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 1 AHCLTLHLFSRSDSVVTGAISNGR--PeLPDADRMVGLFLNTVPVRSEIAGHSWI-EVADALFRQERDGHAHRRYPLSAI 77
Cdd:cd19542 229 AWALVLARYTGSRDVVFGYVVSGRdlP-VPGIDDIVGPCINTLPVRVKLDPDWTVlDLLRQLQQQYLRSLPHQHLSLREI 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 78 QQIVGDELS-----SAFNYVNL--HVLEPLWQLRDFRVWEETN---FALLVNVIATPsDGMYLRIDSDGRGISRSQAALI 147
Cdd:cd19542 308 QRALGLWPSgtlfnTLVSYQNFeaSPESELSGSSVFELSAAEDpteYPVAVEVEPSG-DSLKVSLAYSTSVLSEEQAEEL 386
|
170
....*....|....*
gi 1395399044 148 GATFVELLWRLAEHP 162
Cdd:cd19542 387 LEQFDDILEALLANP 401
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
181-601 |
5.56e-10 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 63.15 E-value: 5.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 181 PEPLVDVVSLFERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRA-GARRGDAigVAL---NRSPEMIAtIWGIL 256
Cdd:PRK08974 19 PDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDR--VALmmpNLLQYPIA-LFGIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 257 RAGLVCVPLDVSYPAQRL------------------ALILEtaqpfRVVAHPEHAHV---------AAAERVLP------ 303
Cdd:PRK08974 96 RAGMIVVNVNPLYTPRELehqlndsgakaivivsnfAHTLE-----KVVFKTPVKHViltrmgdqlSTAKGTLVnfvvky 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 304 VEELVADIE-PET--------------FAAPQL--DELAMLLFTSGSTGRPKGVELSHR-MWANYTQwqlrvASGV--PG 363
Cdd:PRK08974 171 IKRLVPKYHlPDAisfrsalhkgrrmqYVKPELvpEDLAFLQYTGGTTGVAKGAMLTHRnMLANLEQ-----AKAAygPL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 364 LRTLQ------------FAPLSFDMAFQEIfstlcgGGELQLISNRErmDPSALLHVLERRqvqrvllPFVALQRLAEAS 431
Cdd:PRK08974 246 LHPGKelvvtalplyhiFALTVNCLLFIEL------GGQNLLITNPR--DIPGFVKELKKY-------PFTAITGVNTLF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 432 NAL-------GVRPGALRVVVSSGeqLRITEDVRAFCAAMPGLLLENQYGPTE--------THQVTYHSLSgdpahypdl 496
Cdd:PRK08974 311 NALlnneefqELDFSSLKLSVGGG--MAVQQAVAERWVKLTGQYLLEGYGLTEcsplvsvnPYDLDYYSGS--------- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 497 ppIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAErFVEHPWrpgarlYRTGDLGRILGNGEIVW 576
Cdd:PRK08974 380 --IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGW------LATGDIAVMDEEGFLRI 450
|
490 500
....*....|....*....|....*
gi 1395399044 577 LGRADTQVKVRGFRIEPAEVELAIM 601
Cdd:PRK08974 451 VDRKKDMILVSGFNVYPNEIEDVVM 475
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
322-585 |
9.57e-10 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-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. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to 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. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 62.23 E-value: 9.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 322 DELAMLLFTSGSTGRPKGVELSHRmwaNYTQWQLRVASGVPGL-----RTLQFAPLS--FDMAFQEIF----STLCGGGE 390
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHG---NLVAGIAGLGDRVPELlgpddRYLAYLPLAhiFELAAENVClyrgGTIGYGSP 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 391 LQLISNR-----------------------ERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALG-----------V 436
Cdd:cd17639 165 RTLTDKSkrgckgdltefkptlmvgvpaiwDTIRKGVLAKLNPMGGLKRTLFWTAYQSKLKALKEGPGtplldelvfkkV 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 437 RP---GALRVVVSSGEQLriTEDVRAF-----CAAMPGlllenqYGPTEThqvtyhSLSGDPAHYPDLPP--IGRPLDGV 506
Cdd:cd17639 245 RAalgGRLRYMLSGGAPL--SADTQEFlnivlCPVIQG------YGLTET------CAGGTVQDPGDLETgrVGPPLPCC 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 507 EVQVLD------AALRPVPvgvTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRA 580
Cdd:cd17639 311 EIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYYKNPEKTKEAFDGDGW------FHTGDIGEFHPDGTLKIIDRK 381
|
....*
gi 1395399044 581 DTQVK 585
Cdd:cd17639 382 KDLVK 386
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
781-889 |
1.00e-09 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 59.63 E-value: 1.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 781 RAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQGSTPLAV--LEDIAASYLAAIRRVQPEgPYYLGGW 858
Cdd:COG0596 18 EAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPAGGytLDDLADDLAALLDALGLE-RVVLVGH 96
|
90 100 110
....*....|....*....|....*....|.
gi 1395399044 859 SFGGFVAYEMARQLraldPQAVAQLIVLDSI 889
Cdd:COG0596 97 SMGGMVALELAARH----PERVAGLVLVDEV 123
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
208-657 |
1.17e-09 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 61.99 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 208 EQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPFRVV 287
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 288 AhpehahvaaaervlpveelvadiepetfaapqldELAMLLFTSGSTGRPKGVELSHRMWANYTQWqlrVASGVPGLRTL 367
Cdd:cd05940 81 V----------------------------------DAALYIYTSGTTGLPKAAIISHRRAWRGGAF---FAGSGGALPSD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 368 QF---APLSFDMAFQEIFST-LCGGGELQLisnRERMDPSALLHvlERRQVQRVLLPFVA--LQRLAEASNALGVRPGAL 441
Cdd:cd05940 124 VLytcLPLYHSTALIVGWSAcLASGATLVI---RKKFSASNFWD--DIRKYQATIFQYIGelCRYLLNQPPKPTERKHKV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 442 RVVVSSGEQLRITED---------VRAFcaampglllenqYGPTE--THQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQV 510
Cdd:cd05940 199 RMIFGNGLRPDIWEEfkerfgvprIAEF------------YAATEgnSGFINFFGKPGAIGRNPSLLRKVAPLALVKYDL 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 511 -LDAALRP-------VPVGVTGELYFGGDCLAR--GYHRAPElTAERFVEHPWRPGARLYRTGDLGRILGNGEIVWLGRA 580
Cdd:cd05940 267 eSGEPIRDaegrcikVPRGEPGLLISRINPLEPfdGYTDPAA-TEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRL 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1395399044 581 DTQVKVRGFRIEPAEVElAIMRQAerqPGLRGAAV--VARERQGNDAFLAAFLLGEPEAVDLAELKQALRSELPEHMVP 657
Cdd:cd05940 346 GDTFRWKGENVSTTEVA-AVLGAF---PGVEEANVygVQVPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYARP 420
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
210-680 |
1.20e-09 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 62.08 E-value: 1.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 210 RWTYRDLDHVARCVATRLVRAGARRGDAIG-VALNRSPEMiATIWGILRAGLVCVPLDVSYPAQRLALILETAQ------ 282
Cdd:PRK06018 39 RTTYAQIHDRALKVSQALDRDGIKLGDRVAtIAWNTWRHL-EAWYGIMGIGAICHTVNPRLFPEQIAWIINHAEdrvvit 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 283 -----PF------------RVVAHPEHAHVAAA--ERVLPVEELVADIEPEtFAAPQLDE--LAMLLFTSGSTGRPKGVE 341
Cdd:PRK06018 118 dltfvPIlekiadklpsveRYVVLTDAAHMPQTtlKNAVAYEEWIAEADGD-FAWKTFDEntAAGMCYTSGTTGDPKGVL 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 342 LSHRmwANYTQWQLRVASGVPGLRT----LQFAPLSFDMAFQEIFSTLCGGGelQLISNRERMDPSALLHVLERRQVQ-R 416
Cdd:PRK06018 197 YSHR--SNVLHALMANNGDALGTSAadtmLPVVPLFHANSWGIAFSAPSMGT--KLVMPGAKLDGASVYELLDTEKVTfT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 417 VLLPFVALQrLAEASNALGVRPGALRVVVSSGeqlritedvrafcAAMPGLLLE----------NQYGPTETHQVTyhSL 486
Cdd:PRK06018 273 AGVPTVWLM-LLQYMEKEGLKLPHLKMVVCGG-------------SAMPRSMIKafedmgvevrHAWGMTEMSPLG--TL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 487 SGDPAHYPDLPP---------IGRPLDGVEVQVLDAALRPVPVG--VTGELYFGGDCLARGYHRApelTAERFVEHPWrp 555
Cdd:PRK06018 337 AALKPPFSKLPGdarldvlqkQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYRV---DGEILDDDGF-- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 556 garlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE-LAImrqaeRQPGLRGAAVVA------RERQgndafLA 628
Cdd:PRK06018 412 ----FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLEnLAV-----GHPKVAEAAVIGvyhpkwDERP-----LL 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1395399044 629 AFLLGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:PRK06018 478 IVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALR 529
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
296-567 |
1.24e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 62.20 E-value: 1.24e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 296 AAAERVLPVEELVADIEP----ETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMW-ANytQWQLRVASGVPGLRT---L 367
Cdd:PRK08180 179 VPGRAATPFAALLATPPTaavdAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLcAN--QQMLAQTFPFLAEEPpvlV 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 368 QFAPLS--------FDMAfqeifstLCGGGEL-------------QLISNRERMDP----------SALLHVLERRQV-- 414
Cdd:PRK08180 257 DWLPWNhtfggnhnLGIV-------LYNGGTLyiddgkptpggfdETLRNLREISPtvyfnvpkgwEMLVPALERDAAlr 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 415 ----QRVLLPFVA-----------LQRLAEAsnalgvrpgalrvvvSSGEQLRitedvraFCAAmpglllenqYGPTETh 479
Cdd:PRK08180 330 rrffSRLKLLFYAgaalsqdvwdrLDRVAEA---------------TCGERIR-------MMTG---------LGMTET- 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 480 qvtyhSLSGDPAHYPDLPP--IGRPLDGVEVQVldaalrpVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWrpga 557
Cdd:PRK08180 378 -----APSATFTTGPLSRAgnIGLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY---- 441
|
330
....*....|
gi 1395399044 558 rlYRTGDLGR 567
Cdd:PRK08180 442 --YRSGDAVR 449
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
171-657 |
2.20e-09 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 61.40 E-value: 2.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 171 LAPRRDAASQPEPLVDVVSL-----FERQVEALPGSAALAFEEQRWTYRDLDHVARCVATRLVRAGARRGDAIGVALNRS 245
Cdd:PLN02479 1 MAKERDIDDLPKNAANYTALtplwfLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 246 PEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQ-------------------------------PFRVVA-----H 289
Cdd:PLN02479 81 PAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHSKsevvmvdqefftlaeealkilaekkkssfkpPLLIVIgdptcD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 290 PEHAHVAAAERVLPVEELVADIEPETFAAPQLDELA--MLLFTSGSTGRPKGVELSHR-----MWANYTQWQLRvaSGVP 362
Cdd:PLN02479 161 PKSLQYALGKGAIEYEKFLETGDPEFAWKPPADEWQsiALGYTSGTTASPKGVVLHHRgaylmALSNALIWGMN--EGAV 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 363 GLRTLqfaPLSF--DMAFQEIFSTLCGGGelqlISNRErMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGA 440
Cdd:PLN02479 239 YLWTL---PMFHcnGWCFTWTLAALCGTN----ICLRQ-VTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 441 lRVVvssgeqlriteDVRAFCAAMP----------GLLLENQYGPTETHQVTyhSLSGDPAHYPDLPPIGRP-------- 502
Cdd:PLN02479 311 -RVV-----------HVMTAGAAPPpsvlfamsekGFRVTHTYGLSETYGPS--TVCAWKPEWDSLPPEEQArlnarqgv 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 503 ----LDGVEVqVLDAALRPVPV-GVT-GELYFGGDCLARGYHRAPELTAERFvEHPWrpgarlYRTGDLGRILGNGEIVW 576
Cdd:PLN02479 377 ryigLEGLDV-VDTKTMKPVPAdGKTmGEIVMRGNMVMKGYLKNPKANEEAF-ANGW------FHSGDLGVKHPDGYIEI 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 577 LGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVAR--ERQGNDAFLAAFLLGEPEAVDLAELKQAL----RSE 650
Cdd:PLN02479 449 KDRSKDIIISGGENISSLEVENVVY----THPAVLEASVVARpdERWGESPCAFVTLKPGVDKSDEAALAEDImkfcRER 524
|
....*..
gi 1395399044 651 LPEHMVP 657
Cdd:PLN02479 525 LPAYWVP 531
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
318-616 |
2.22e-09 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 61.35 E-value: 2.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 318 APqlDELAMLLFTSGSTGRPKGVELSHRmwANYTQWQLRVAsgVPGLRT----LQFAPLSFDMAFQEIFSTLCGGGELQL 393
Cdd:PLN02860 170 AP--DDAVLICFTSGTTGRPKGVTISHS--ALIVQSLAKIA--IVGYGEddvyLHTAPLCHIGGLSSALAMLMVGACHVL 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 394 ISnreRMDPSALLHVLERRQ------VQRVLLPFVALQRLAEASNalgVRPGALRVVVSSGE-QLRITEDVRAFcaaMPG 466
Cdd:PLN02860 244 LP---KFDAKAALQAIKQHNvtsmitVPAMMADLISLTRKSMTWK---VFPSVRKILNGGGSlSSRLLPDAKKL---FPN 314
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 467 LLLENQYGPTET-------------------HQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQV-LDAALRpvpvgvTGEL 526
Cdd:PLN02860 315 AKLFSAYGMTEAcssltfmtlhdptlespkqTLQTVNQTKSSSVHQPQGVCVGKPAPHVELKIgLDESSR------VGRI 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 527 YFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeR 606
Cdd:PLN02860 389 LTRGPHVMLGYWGQNSETASVLSNDGW------LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLS----Q 458
|
330
....*....|
gi 1395399044 607 QPGLRGAAVV 616
Cdd:PLN02860 459 HPGVASVVVV 468
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
494-680 |
4.34e-09 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 60.36 E-value: 4.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 494 PDLP----PIGRPLDGVEVQVLDAALRPVpVGVTGEL-----------YFGGDCLARGYHRApeltaeRFVEHP--WRpg 556
Cdd:cd05943 417 PLLPvyrgEIQCRGLGMAVEAFDEEGKPV-WGEKGELvctkpfpsmpvGFWNDPDGSRYRAA------YFAKYPgvWA-- 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 557 arlyrTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEvelaIMRQAERQPGLRGAAVVARERQGNDAFLAAFL-LGEP 635
Cdd:cd05943 488 -----HGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAE----IYRVVEKIPEVEDSLVVGQEWKDGDERVILFVkLREG 558
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 1395399044 636 EAVDLA---ELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALR 680
Cdd:cd05943 559 VELDDElrkRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKKVEVAVK 606
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
190-586 |
1.17e-08 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 59.06 E-value: 1.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 190 LFERQVEALPGSAALAFEE--------QRW-TYRDLDHVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGL 260
Cdd:PLN02430 47 IFSKSVEKYPDNKMLGWRRivdgkvgpYMWkTYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVAMEACAAHSL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 261 VCVPLDVSYPAQRLALILETAQ-PFRVVAHPE-----HAHVAAAERVL-------PVEEL---VADI------------- 311
Cdd:PLN02430 127 ICVPLYDTLGPGAVDYIVDHAEiDFVFVQDKKikellEPDCKSAKRLKaivsftsVTEEEsdkASQIgvktyswidflhm 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 312 ---EPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRmwanytqwqlRVASGVPGLRT---------------LQFAPLS 373
Cdd:PLN02430 207 gkeNPSETNPPKPLDICTIMYTSGTSGDPKGVVLTHE----------AVATFVRGVDLfmeqfedkmthddvyLSFLPLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 374 --FDMAFQEIF-------------------------STLCGG-------------GELQLISNRERMDPSAL----LHVL 409
Cdd:PLN02430 277 hiLDRMIEEYFfrkgasvgyyhgdlnalrddlmelkPTLLAGvprvferihegiqKALQELNPRRRLIFNALykykLAWM 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 410 ERRQVQRVLLPFVALQRLAEASNALGvrpGALRVVVSSGEQL--RITEDVRAFCAAmpglLLENQYGPTEThqvtyhsLS 487
Cdd:PLN02430 357 NRGYSHKKASPMADFLAFRKVKAKLG---GRLRLLISGGAPLstEIEEFLRVTSCA----FVVQGYGLTET-------LG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 488 GDPAHYPD----LPPIGRPLDGVEV---QVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAErFVEHPWrpgarlY 560
Cdd:PLN02430 423 PTTLGFPDemcmLGTVGAPAVYNELrleEVPEMGYDPLGEPPRGEICVRGKCLFSGYYKNPELTEE-VMKDGW------F 495
|
490 500
....*....|....*....|....*.
gi 1395399044 561 RTGDLGRILGNGEIVWLGRADTQVKV 586
Cdd:PLN02430 496 HTGDIGEILPNGVLKIIDRKKNLIKL 521
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
4-162 |
4.01e-08 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 56.92 E-value: 4.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 4 LTLHLFSRSDSVVTGAISNGR--PeLPDADRMVGLFLNTVPVRSEIAGHSwiEVADALFRQERDGHAHRRYPLSAIQQI- 80
Cdd:cd19545 225 LVLSRYTGSDDVVFGVTLSGRnaP-VPGIEQIVGPTIATVPLRVRIDPEQ--SVEDFLQTVQKDLLDMIPFEHTGLQNIr 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 81 -VGDELSSAFNYVNLHVLEP-----LWQLRDFRVWEE-------TNFALLVnVIATPSDGMYLRIDSDGRGISRSQAALI 147
Cdd:cd19545 302 rLGPDARAACNFQTLLVVQPalpssTSESLELGIEEEsedledfSSYGLTL-ECQLSGSGLRVRARYDSSVISEEQVERL 380
|
170
....*....|....*
gi 1395399044 148 GATFVELLWRLAEHP 162
Cdd:cd19545 381 LDQFEHVLQQLASAP 395
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
556-673 |
7.47e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 55.81 E-value: 7.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 556 GARLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAV------VARERqgndafLAA 629
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVML----RLPGVQEAVVyrgkdpVAGER------VKA 358
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 1395399044 630 FLLGEpEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK08308 359 KVISH-EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGK 401
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
199-579 |
7.96e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 56.49 E-value: 7.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 199 PGSAALAF--EEQRW-------TYRDLDHVARCVATRLVRAGARrGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSY 269
Cdd:PRK05850 15 PDDAAFTFidYEQDPagvaetlTWSQLYRRTLNVAEELRRHGST-GDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVPQ 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 270 PAQ---RLALILETAQPF----------RVVAHPEHAHVAAAERVLPVEELVADIEPETFAAPQ-LDELAMLLFTSGSTG 335
Cdd:PRK05850 94 GGAhdeRVSAVLRDTSPSvvlttsavvdDVTEYVAPQPGQSAPPVIEVDLLDLDSPRGSDARPRdLPSTAYLQYTSGSTR 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 336 RPKGVELSHR-MWANYTQWQ---LRVASGVP--GLRTLQFAPLSFDMAF-QEIFSTLCGGGELQLISnrermdPSALLhv 408
Cdd:PRK05850 174 TPAGVMVSHRnVIANFEQLMsdyFGDTGGVPppDTTVVSWLPFYHDMGLvLGVCAPILGGCPAVLTS------PVAFL-- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 409 lerrqvQRvllPFVALQRLAEASNA----------LGVRP-----------GALRVVVSSGEQL------RITEDVRAFc 461
Cdd:PRK05850 246 ------QR---PARWMQLLASNPHAfsaapnfafeLAVRKtsdddmagldlGGVLGIISGSERVhpatlkRFADRFAPF- 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 462 aAMPGLLLENQYG---------------PTETHQVTYHSLSGDPAHyPDLPPIGRPL------DGVEVQVLDA-ALRPVP 519
Cdd:PRK05850 316 -NLRETAIRPSYGlaeatvyvatrepgqPPESVRFDYEKLSAGHAK-RCETGGGTPLvsygspRSPTVRIVDPdTCIECP 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1395399044 520 VGVTGELYFGGDCLARGYHRAPELTAERF-----------VEHPWrpgarlYRTGDLGRILGnGEIVWLGR 579
Cdd:PRK05850 394 AGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvdpspgtPEGPW------LRTGDLGFISE-GELFIVGR 457
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
701-768 |
9.24e-08 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 50.71 E-value: 9.24e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1395399044 701 RTLAGLLGeLLDRPRVGIRDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLRER 768
Cdd:smart00823 19 EQVAAVLG-HAAAEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
200-586 |
1.41e-07 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 55.59 E-value: 1.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 200 GSAALAFEEQ--RWTYRDLDHVARCVATRLVRAGarrGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALI 277
Cdd:PRK06334 33 TTATVCWDEQlgKLSYNQVRKAVIALATKVSKYP---DQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTAC 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 278 LE--------TAQPFrvVAHPEHAHVAAAE---------------------RV-----LPVEEL-----VADIEPEtfaa 318
Cdd:PRK06334 110 ANlvgvthvlTSKQL--MQHLAQTHGEDAEypfsliymeevrkelsfwekcRIgiymsIPFEWLmrwfgVSDKDPE---- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 319 pqldELAMLLFTSGSTGRPKGVELSHrmwANYTQWQ---LRVASGVPGLRTLQFAPLSFDMAFQ--EIFSTLCGggeLQL 393
Cdd:PRK06334 184 ----DVAVILFTSGTEKLPKGVPLTH---ANLLANQracLKFFSPKEDDVMMSFLPPFHAYGFNscTLFPLLSG---VPV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 394 ISNRERMDPSALLHVLERRQVQRVLLPFVALQRLAEASNALGVRPGALRVVVSSGEQLRIT---EDVRAFcaamPGLLLE 470
Cdd:PRK06334 254 VFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSlyqEALKTF----PHIQLR 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 471 NQYGPTETHQVTYHSLSGDPAHYPdlpPIGRPLDGVEVQVLDAALR-PVPVGVTGELYFGGDCLARGYHRAPEltAERFV 549
Cdd:PRK06334 330 QGYGTTECSPVITINTVNSPKHES---CVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDF--GQGFV 404
|
410 420 430
....*....|....*....|....*....|....*..
gi 1395399044 550 EhpwRPGARLYRTGDLGRILGNGEIVWLGRADTQVKV 586
Cdd:PRK06334 405 E---LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKI 438
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
322-685 |
1.49e-07 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 54.79 E-value: 1.49e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 322 DELAMLLFTSGSTGRPKGVELSHrmwANytqwqlRVASGVPGLRTLQFAPLSFDMAFQEIF----------STLCGGGEL 391
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTH---SN------EVYNAWMLALNSLFDPDDVLLCGLPLFhvngsvvtllTPLASGAHV 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 392 QLISNRERMDPSA---LLHVLERRQVQrvllpfvALQRLAEASNALGVRP-----GALRVVVSSGEQLRItEDVRAFCAA 463
Cdd:cd05944 73 VLAGPAGYRNPGLfdnFWKLVERYRIT-------SLSTVPTVYAALLQVPvnadiSSLRFAMSGAAPLPV-ELRARFEDA 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 464 MpGLLLENQYGPTETHQVtyHSLSgdpahYPDLPP----IGRPL--DGVEVQVLDA---ALRPVPVGVTGELYFGGDCLA 534
Cdd:cd05944 145 T-GLPVVEGYGLTEATCL--VAVN-----PPDGPKrpgsVGLRLpyARVRIKVLDGvgrLLRDCAPDEVGEICVAGPGVF 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 535 RGYHRApELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAA 614
Cdd:cd05944 217 GGYLYT-EGNKNAFVADGW------LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALL----RHPAVAFAG 285
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395399044 615 VVARERQGNDAFLAAFLLGEPEA-VDLAELKQALRSELPEH-MVPAHFAWVDGFALTPSGKRDDAALRALPLE 685
Cdd:cd05944 286 AVGQPDAHAGELPVAYVQLKPGAvVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRADAIH 358
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
192-682 |
3.20e-07 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 54.24 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 192 ERQVEA-LPGSAALAFE------EQRWTYRDL-DHVARcVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCV 263
Cdd:cd05967 57 DRHVEAgRGDQIALIYDspvtgtERTYTYAELlDEVSR-LAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 264 PLDVSYPAQRLALILETAQPFRVVA--------------------------HPEH----------AHVAAAERVLPVEEL 307
Cdd:cd05967 136 VVFGGFAAKELASRIDDAKPKLIVTascgiepgkvvpykplldkalelsghKPHHvlvlnrpqvpADLTKPGRDLDWSEL 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 308 VADIEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHRMWANYTQWQLR----VASG-----------VPGLRTLQFAPL 372
Cdd:cd05967 216 LAKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSMRniygIKPGdvwwaasdvgwVVGHSYIVYGPL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 373 sfdmafqeifstLCGGGELQLISNRERM-DPSALLHVLERRQVQRVLLPFVALQRL----AEASNALGVRPGALRVVVSS 447
Cdd:cd05967 296 ------------LHGATTVLYEGKPVGTpDPGAFWRVIEKYQVNALFTAPTAIRAIrkedPDGKYIKKYDLSSLRTLFLA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 448 GEqlRITEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELY 527
Cdd:cd05967 364 GE--RLDPPTLEWAENTLGVPVIDHWWQTETGWPITANPVGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 528 FGG----DCLARGYhrapeLTAERFVEHPWR--PGarLYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIM 601
Cdd:cd05967 442 IKLplppGCLLTLW-----KNDERFKKLYLSkfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVL 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 602 rqaeRQPGLRGAAVVARErqgnDAF-----LAAFLLGEPEAVDLAELKQALRSELPEHMVP----AHFAWVDGFALTPSG 672
Cdd:cd05967 515 ----SHPAVAECAVVGVR----DELkgqvpLGLVVLKEGVKITAEELEKELVALVREQIGPvaafRLVIFVKRLPKTRSG 586
|
570
....*....|
gi 1395399044 673 KRDDAALRAL 682
Cdd:cd05967 587 KILRRTLRKI 596
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
210-345 |
4.61e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 53.94 E-value: 4.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 210 RWTYRDLDHVARCVATRLVRAGARRGDAIG-VALN--RSPEMiatIWGILRAGLVCVPLDVSYPAQRLALILETAQ---- 282
Cdd:PRK07008 39 RYTYRDCERRAKQLAQALAALGVEPGDRVGtLAWNgyRHLEA---YYGVSGSGAVCHTINPRLFPEQIAYIVNHAEdryv 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 283 -------PFRVVAHP------------EHAHV-AAAERVLPVEELVaDIEPETFAAPQLDE--LAMLLFTSGSTGRPKGV 340
Cdd:PRK07008 116 lfdltflPLVDALAPqcpnvkgwvamtDAAHLpAGSTPLLCYETLV-GAQDGDYDWPRFDEnqASSLCYTSGTTGNPKGA 194
|
....*
gi 1395399044 341 ELSHR 345
Cdd:PRK07008 195 LYSHR 199
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
206-348 |
4.92e-07 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 53.83 E-value: 4.92e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 206 FEEQRWTYRDLDHVARCVATRLVR-AGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQPF 284
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 285 RVVAHPEhaHVAAAERVLP---------------------------VEELVADIEPETFAAPQ-LDELAMLLFTSGSTGR 336
Cdd:cd05938 81 VLVVAPE--LQEAVEEVLPalradgvsvwylshtsntegvislldkVDAASDEPVPASLRAHVtIKSPALYIYTSGTTGL 158
|
170
....*....|...
gi 1395399044 337 PKGVELSH-RMWA 348
Cdd:cd05938 159 PKAARISHlRVLQ 171
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
500-673 |
5.50e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 53.61 E-value: 5.50e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 500 GRPLDGVEVQVLDAALRPVPVGVTGELyfggdCLAR----------GYHrapeltaERFVEHPWRPGARLYRTGDLGRIL 569
Cdd:PRK00174 427 TRPLPGIQPAVVDEEGNPLEGGEGGNL-----VIKDpwpgmmrtiyGDH-------ERFVKTYFSTFKGMYFTGDGARRD 494
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 570 GNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQ---AErqpglrgAAVVAR--ERQGNDAFlaAFLL---GEPEAVDLA 641
Cdd:PRK00174 495 EDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHpkvAE-------AAVVGRpdDIKGQGIY--AFVTlkgGEEPSDELR 565
|
170 180 190
....*....|....*....|....*....|...
gi 1395399044 642 -ELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PRK00174 566 kELRNWVRKEIGPIAKPDVIQFAPGLPKTRSGK 598
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
500-682 |
5.88e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 53.07 E-value: 5.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 500 GRPLDGVEVQVLDAAlrpvpvgvTGELYFGGDCLARGYHraPELtaerfvehpwRPGARLYRTGDLGRILGNGEIVWLGR 579
Cdd:PRK07445 286 GQVLPHAQITIPANQ--------TGNITIQAQSLALGYY--PQI----------LDSQGIFETDDLGYLDAQGYLHILGR 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 580 ADTQVKVRGFRIEPAEVELAImrqaeRQPGL-RGAAV--VARERQGNdaFLAAFLLGEPEAVDLAELKQALRSELPEHMV 656
Cdd:PRK07445 346 NSQKIITGGENVYPAEVEAAI-----LATGLvQDVCVlgLPDPHWGE--VVTAIYVPKDPSISLEELKTAIKDQLSPFKQ 418
|
170 180
....*....|....*....|....*.
gi 1395399044 657 PAHFAWVDGFALTPSGKRDDAALRAL 682
Cdd:PRK07445 419 PKHWIPVPQLPRNPQGKINRQQLQQI 444
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
595-673 |
1.75e-06 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 46.77 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 595 EVELAIMRQaerqPGLRGAAVVARERQGNDAFLAAFL-LGEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:pfam13193 1 EVESALVSH----PAVAEAAVVGVPDELKGEAPVAFVvLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
320-682 |
1.97e-06 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 52.02 E-value: 1.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 320 QLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQlRVASGVPGLRTLQFAPL--SFDMAFQeIFSTLCGGGELQLIsn 396
Cdd:PRK08043 363 QPEDAALILFTSGSEGHPKGVVHSHKsLLANVEQIK-TIADFTPNDRFMSALPLfhSFGLTVG-LFTPLLTGAEVFLY-- 438
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 397 rermdPSALLHvlerrqvqRVlLPFVALQR----LAEASNALG-----VRP---GALRVVVSSGEQLriTEDVRAFCAAM 464
Cdd:PRK08043 439 -----PSPLHY--------RI-VPELVYDRnctvLFGTSTFLGnyarfANPydfARLRYVVAGAEKL--QESTKQLWQDK 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 465 PGLLLENQYGPTETHQVTyhSLSGDPAHYPDlpPIGRPLDGvevqvLDAALRPVPvGVT--GELYFGGDCLARGYHRape 542
Cdd:PRK08043 503 FGLRILEGYGVTECAPVV--SINVPMAAKPG--TVGRILPG-----MDARLLSVP-GIEqgGRLQLKGPNIMNGYLR--- 569
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 543 ltaerfVEHPWR---PGAR---------LYRTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVE-LAIMRQAERQpg 609
Cdd:PRK08043 570 ------VEKPGVlevPTAEnargemergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEqLALGVSPDKQ-- 641
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395399044 610 lrgAAVVARERQGNDAFLAAFLLgEPEAVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRAL 682
Cdd:PRK08043 642 ---HATAIKSDASKGEALVLFTT-DSELTREKLQQYAREHGVPELAVPRDIRYLKQLPLLGSGKPDFVTLKSM 710
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
787-1038 |
2.63e-06 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 49.81 E-value: 2.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 787 PPLFLVHPLGGHVLCYLPLVRALPPD-QPVYALQAAGTGQGSTPLAVLEDIAASYLAAIRRVQ---PEGPYYLGGWSFGG 862
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPKAQDDYRTDDLAEDLEYILealGLEKVNLVGHSMGG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 863 FVAYEMArqlrALDPQAVAQLIVLDSItvDRNHAGSASDEALLLFFYWelvWFERSDEEVEPLPEGASLEQKLDHIVERA 942
Cdd:pfam00561 81 LIALAYA----AKYPDRVKALVLLGAL--DPPHELDEADRFILALFPG---FFDGFVADFAPNPLGRLVAKLLALLLLRL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 943 IEAGVLPAGTPRATVQRLY---ELFRASWQALIGYRPEVSDQDmtLLRADGPLpLALKPMHDaagtHYGDPKNGWQ--HW 1017
Cdd:pfam00561 152 RLLKALPLLNKRFPSGDYAlakSLVTGALLFIETWSTELRAKF--LGRLDEPT-LIIWGDQD----PLVPPQALEKlaQL 224
|
250 260
....*....|....*....|.
gi 1395399044 1018 TSGRLDVIDVPGDHLVLMKEP 1038
Cdd:pfam00561 225 FPNARLVVIPDAGHFAFLEGP 245
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
302-651 |
5.68e-06 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.15 E-value: 5.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 302 LPV---EELVADIEPETFAAPQlDELAMLLFTSGSTGRPKGVELSHRMWANytqWQLRVA-----SGV-PGLRtLQFAP- 371
Cdd:COG1541 61 LPFttkEDLRDNYPFGLFAVPL-EEIVRIHASSGTTGKPTVVGYTRKDLDR---WAELFArslraAGVrPGDR-VQNAFg 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 372 -------LSFDMAFQEIFSTLC--GGGE----LQLIsnrERMDPSALlhvlerrqvqrVLLPFVALqRLAEASNALGVRP 438
Cdd:COG1541 136 yglftggLGLHYGAERLGATVIpaGGGNterqLRLM---QDFGPTVL-----------VGTPSYLL-YLAEVAEEEGIDP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 439 GA--LRVVVSSGEqlRITEDVRAFCAAMPGLLLENQYGPTET-HQVTYHSLSGDPAHYPDlppigrplDGVEVQVLD-AA 514
Cdd:COG1541 201 RDlsLKKGIFGGE--PWSEEMRKEIEERWGIKAYDIYGLTEVgPGVAYECEAQDGLHIWE--------DHFLVEIIDpET 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 515 LRPVPVGVTGELYFGGdclargyhrapeLTAE-----RfvehpwrpgarlYRTGDLGRIL--------GNGEIV-WLGRA 580
Cdd:COG1541 271 GEPVPEGEEGELVVTT------------LTKEampliR------------YRTGDLTRLLpepcpcgrTHPRIGrILGRA 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1395399044 581 DTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARERQGN-DAFLaafLLGEP-EAVDLAELKQALRSEL 651
Cdd:COG1541 327 DDMLIIRGVNVFPSQIEEVLL----RIPEVGPEYQIVVDREGGlDELT---VRVELaPGASLEALAEAIAAAL 392
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
412-908 |
5.91e-06 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 50.64 E-value: 5.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 412 RQVQRVLLPFVALQR-----------LAEASNALGVRPGALRVVVSSGEQLRITEDVRAFCAAMPGLLLENQYGPTETHQ 480
Cdd:COG3321 856 RGRRRVPLPTYPFQRedaaaallaaaLAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAAALAALLALVAL 935
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 481 VTYHSLSGDPAHYPDLPPIGRPLDGVEVQVLDAALRPVPVGVTGELYFGGDCLARGYHRAPELTAERFVEHPWRPGARLY 560
Cdd:COG3321 936 AAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALALLAAAALLLAAA 1015
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 561 RTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQAERQPGLRGAAVVARERQGNDAFLAAFLLGEPEAVDL 640
Cdd:COG3321 1016 AAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAALALAAALAAAAL 1095
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 641 AELKQALRSE--LPEHMVPAHFAWVDGFALTPSGKRDDAALRALPLEHGTNIEYLAPRDDYERTLAGLLGELLDRPRVGI 718
Cdd:COG3321 1096 ALALAALAAAllLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALAAALLAAAALLL 1175
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 719 RDSFFDLGGTSLSAMRFMLLIEKRYGVDLPMAALIETPTVEGLAERLRERSAVRAFDPLVPIRAGGSRPPLFLVHPLGGH 798
Cdd:COG3321 1176 ALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAAVAALAAAAAAL 1255
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 799 VLCYLPLVRALPPDQPVYALQAAGTGQGSTPLAVLEDIAASYLAAIRRVQPEGPYYLGGWSFGGFVAYEMARQLRALDPQ 878
Cdd:COG3321 1256 LAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAALLAAALAALAA 1335
|
490 500 510
....*....|....*....|....*....|
gi 1395399044 879 AVAQLIVLDSITVDRNHAGSASDEALLLFF 908
Cdd:COG3321 1336 AVAAALALAAAAAAAAAAAAAAAAAAALAA 1365
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
1-162 |
1.48e-05 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 48.85 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 1 AHCLTLHLFSRSDSVVTGAISNGRP-ELPDADRMVGLFLNTVPVRSEI-AGHSWIEVADALFRQERDGHAHRRYPLSAIQ 78
Cdd:cd19547 249 AWSMLLALQTGARDVVHGLTIAGRPpELEGSEHMVGIFINTIPLRIRLdPDQTVTGLLETIHRDLATTAAHGHVPLAQIK 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 79 QIVG----------DELSSAFNYV--NLHVLEPLWQLRDFRVWEETNFAllVNVIATPSDGMYLRIDSDGRGISRSQAAL 146
Cdd:cd19547 329 SWASgerlsggrvfDNLVAFENYPedNLPGDDLSIQIIDLHAQEKTEYP--IGLIVLPLQKLAFHFNYDTTHFTRAQVDR 406
|
170
....*....|....*.
gi 1395399044 147 IGATFVELLWRLAEHP 162
Cdd:cd19547 407 FIEVFRLLTEQLCRRP 422
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
322-579 |
1.79e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 48.82 E-value: 1.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 322 DELAMLLFTSGSTGRPKGVELSHRmwanytqwqlRVASGVPGL---------------RTLQFAPLSFDMAF--QEIF-- 382
Cdd:PTZ00216 264 DDLALIMYTSGTTGDPKGVMHTHG----------SLTAGILALedrlndligppeedeTYCSYLPLAHIMEFgvTNIFla 333
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 383 --STLCGGGELQLISN--RERMD-----PSALLHVLE-----RRQVQRVLLPFVALQR-------------LAEA----- 430
Cdd:PTZ00216 334 rgALIGFGSPRTLTDTfaRPHGDltefrPVFLIGVPRifdtiKKAVEAKLPPVGSLKRrvfdhayqsrlraLKEGkdtpy 413
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 431 ------SNALGVRPGALRVVVSSGEQLriTEDVRAFCAAMPGLLLeNQYGPTETHQVTYHSLSGDpahypdLPP--IGRP 502
Cdd:PTZ00216 414 wnekvfSAPRAVLGGRVRAMLSGGGPL--SAATQEFVNVVFGMVI-QGWGLTETVCCGGIQRTGD------LEPnaVGQL 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 503 LDGVEVQVLDA-----ALRPVPvgvTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILGNGEIVWL 577
Cdd:PTZ00216 485 LKGVEMKLLDTeeykhTDTPEP---RGEILLRGPFLFKGYYKQEELTREVLDEDGW------FHTGDVGSIAANGTLRII 555
|
..
gi 1395399044 578 GR 579
Cdd:PTZ00216 556 GR 557
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
300-597 |
3.72e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 47.79 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 300 RVLPVEELVAD--IEPETFAAPQLDELAMLLFTSGSTGRPKGVELSHR-MWANYTQWQLRVASGvPGLRTLQFAPLS--F 374
Cdd:PLN02736 197 EIVTYSKLLAQgrSSPQPFRPPKPEDVATICYTSGTTGTPKGVVLTHGnLIANVAGSSLSTKFY-PSDVHISYLPLAhiY 275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 375 DMAFQeIFSTLCG-------GGELQLISNRERMDPSALLHV--LERRQVQRVLLPFVA----LQRLAEAS-----NAL-- 434
Cdd:PLN02736 276 ERVNQ-IVMLHYGvavgfyqGDNLKLMDDLAALRPTIFCSVprLYNRIYDGITNAVKEsgglKERLFNAAynakkQALen 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 435 GVRPGAL--RVVVSS-----GEQLR--------ITEDVRAFCAAMPGLLLENQYGPTETHQVTYHSLSGD--PAHypdlp 497
Cdd:PLN02736 355 GKNPSPMwdRLVFNKikaklGGRVRfmssgaspLSPDVMEFLRICFGGRVLEGYGMTETSCVISGMDEGDnlSGH----- 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 498 pIGRPLDGVEVQVLD-------AALRPVPvgvTGELYFGGDCLARGYHRAPELTAERFVEHPWrpgarlYRTGDLGRILG 570
Cdd:PLN02736 430 -VGSPNPACEVKLVDvpemnytSEDQPYP---RGEICVRGPIIFKGYYKDEVQTREVIDEDGW------LHTGDIGLWLP 499
|
330 340
....*....|....*....|....*...
gi 1395399044 571 NGEIVWLGRADTQVKV-RGFRIEPAEVE 597
Cdd:PLN02736 500 GGRLKIIDRKKNIFKLaQGEYIAPEKIE 527
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
782-888 |
1.54e-04 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 44.22 E-value: 1.54e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 782 AGGSRPPLFLVHPLGGHVLCYLPLVRALP--------PDQPVYALQAAGTGQGSTPLAVLEDIAAsyLAAIRRVQPEGPY 853
Cdd:COG2267 24 AGSPRGTVVLVHGLGEHSGRYAELAEALAaagyavlaFDLRGHGRSDGPRGHVDSFDDYVDDLRA--ALDALRARPGLPV 101
|
90 100 110
....*....|....*....|....*....|....*
gi 1395399044 854 YLGGWSFGGFVAYEMArqlrALDPQAVAQLIVLDS 888
Cdd:COG2267 102 VLLGHSMGGLIALLYA----ARYPDRVAGLVLLAP 132
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
290-682 |
1.62e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 45.54 E-value: 1.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 290 PEHAHVAAAERVLpveelvaDIEPETFAAPQLDE--LAMLLFTSGSTGRPKGVELSHRmwANYTQWQlrvasgvpGLRTL 367
Cdd:PRK05620 154 PEGIKVYSYEALL-------DGRSTVYDWPELDEttAAAICYSTGTTGAPKGVVYSHR--SLYLQSL--------SLRTT 216
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 368 QFAPLSFDMAFQ---EIFSTLCGGGELQ-------LISNRERMDPSALLHVLErrqvqrvllpfVALQRLAEASNALGVR 437
Cdd:PRK05620 217 DSLAVTHGESFLccvPIYHVLSWGVPLAafmsgtpLVFPGPDLSAPTLAKIIA-----------TAMPRVAHGVPTLWIQ 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 438 pgaLRV--VVSSGEQLRITEdVRAFCAAMPGLLL---ENQYGPTETH--QVTYHSLSGDPAHypdlPPIG---------- 500
Cdd:PRK05620 286 ---LMVhyLKNPPERMSLQE-IYVGGSAVPPILIkawEERYGVDVVHvwGMTETSPVGTVAR----PPSGvsgearwayr 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 501 ----RPLDGVEV------QVLDAALRPvpvgvTGELYFGGDCLARGYHRAPELT----AERFVEHPWRPGARLY------ 560
Cdd:PRK05620 358 vsqgRFPASLEYrivndgQVMESTDRN-----EGEIQVRGNWVTASYYHSPTEEgggaASTFRGEDVEDANDRFtadgwl 432
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 561 RTGDLGRILGNGEIVWLGRADTQVKVRGFRIEPAEVELAIMRQaerqPGLRGAAVVA-RERQGNDAFLAAFLLG---EPE 636
Cdd:PRK05620 433 RTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAA----PEVVECAVIGyPDDKWGERPLAVTVLApgiEPT 508
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1395399044 637 AVDLAELKQALRSELPEHMVPAHFAWVDGFALTPSGKRDDAALRAL 682
Cdd:PRK05620 509 RETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQH 554
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
546-673 |
2.62e-04 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 44.89 E-value: 2.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 546 ERFVEHPWRPGARLYRTGDLGRILGNGeIVWL-GRADTQVKVRGFRIEPAEVELAIMrqaeRQPGLRGAAVVARER---- 620
Cdd:PLN02654 501 ERYETTYFKPFAGYYFSGDGCSRDKDG-YYWLtGRVDDVINVSGHRIGTAEVESALV----SHPQCAEAAVVGIEHevkg 575
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1395399044 621 QGNDAFLaAFLLGEPEAVDL-AELKQALRSELPEHMVPAHFAWVDGFALTPSGK 673
Cdd:PLN02654 576 QGIYAFV-TLVEGVPYSEELrKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGK 628
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
319-575 |
8.59e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 43.18 E-value: 8.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 319 PQLDELAMLLFTSGSTGRPKGVELSHRmwaNYTQWQLRVASGVPGLRT----LQFAPLS--FDMAFQeifSTLCG----- 387
Cdd:PLN02387 247 PSPNDIAVIMYTSGSTGLPKGVMMTHG---NIVATVAGVMTVVPKLGKndvyLAYLPLAhiLELAAE---SVMAAvgaai 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 388 --GGELQLI--SNR----ERMDPSALLHVLE--------------RRQVQ------RVLLPFVALQRLA--EAS------ 431
Cdd:PLN02387 321 gyGSPLTLTdtSNKikkgTKGDASALKPTLMtavpaildrvrdgvRKKVDakgglaKKLFDIAYKRRLAaiEGSwfgawg 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 432 ------NALGVRP------GALRVVVSSGEQLriTEDVRAFCAAMPGLLLENQYGPTEThqvtyhsLSGDPAHYPDLPPI 499
Cdd:PLN02387 401 lekllwDALVFKKiravlgGRIRFMLSGGAPL--SGDTQRFINICLGAPIGQGYGLTET-------CAGATFSEWDDTSV 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 500 GR---PLDGVEVQVLD-------AALRPVPvgvTGELYFGGDCLARGYHRAPELTAERF-VEhpwRPGARLYRTGDLGRI 568
Cdd:PLN02387 472 GRvgpPLPCCYVKLVSweeggylISDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYkVD---ERGMRWFYTGDIGQF 545
|
....*....
gi 1395399044 569 LGNG--EIV 575
Cdd:PLN02387 546 HPDGclEII 554
|
|
| PRK14875 |
PRK14875 |
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional |
781-883 |
1.18e-03 |
|
acetoin dehydrogenase E2 subunit dihydrolipoyllysine-residue acetyltransferase; Provisional
Pssm-ID: 184875 [Multi-domain] Cd Length: 371 Bit Score: 42.62 E-value: 1.18e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 781 RAGGSRPPLFLVHPLGGHVLCYLPLVRALPPDQPVYALQAAGTGQgSTPLAV---LEDIAASYLA-----AIRRVQpegp 852
Cdd:PRK14875 126 LGEGDGTPVVLIHGFGGDLNNWLFNHAALAAGRPVIALDLPGHGA-SSKAVGagsLDELAAAVLAfldalGIERAH---- 200
|
90 100 110
....*....|....*....|....*....|.
gi 1395399044 853 yyLGGWSFGGFVAYEMARQlralDPQAVAQL 883
Cdd:PRK14875 201 --LVGHSMGGAVALRLAAR----APQRVASL 225
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
188-345 |
2.14e-03 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation 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. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 42.03 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 188 VSLFERqvealpgsAALAFEEQrwTYRDLDHV-----ARCV--ATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGL 260
Cdd:cd05915 5 AALFGR--------KEVVSRLH--TGEVHRTTyaevyQRARrlMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 261 VCVPLDVSYPAQRLALILETAQPFRVVAHPEHAHVAAAERVL-------PVEE--------LVADIEPETFAAPQLDEL- 324
Cdd:cd05915 75 VLHTANPRLSPKEIAYILNHAEDKVLLFDPNLLPLVEAIRGElktvqhfVVMDekapegylAYEEALGEEADPVRVPERa 154
|
170 180
....*....|....*....|..
gi 1395399044 325 -AMLLFTSGSTGRPKGVELSHR 345
Cdd:cd05915 155 aCGMAYTTGTTGLPKGVVYSHR 176
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
212-421 |
2.36e-03 |
|
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: 41.95 E-value: 2.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 212 TYRDLD-HVARCVATRLVRAGARRGDAIGVALNRSPEMIATIWGILRAGLVCVPLDVSYPAQRLALILETAQ---PFRVV 287
Cdd:cd05905 16 TWGKLLsRAEKIAAVLQKKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKvrvALTVE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 288 A-HPEH-----AHVAAAERVLPV---EELVADIEPETFAAPQLD----------ELAMLLFTSGSTGRPKGVELSHRMWA 348
Cdd:cd05905 96 AcLKGLpkkllKSKTAAEIAKKKgwpKILDFVKIPKSKRSKLKKwgphpptrdgDTAYIEYSFSSDGSLSGVAVSHSSLL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1395399044 349 NYTQwQLRVASGVPGLRTLqFAPLSFDMAFQEIFSTLCG---GGELQLISNRE-RMDPSALLHVLERRQVQRVLLPF 421
Cdd:cd05905 176 AHCR-ALKEACELYESRPL-VTVLDFKSGLGLWHGCLLSvysGHHTILIPPELmKTNPLLWLQTLSQYKVRDAYVKL 250
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1-44 |
2.96e-03 |
|
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- bond forming activity and similar C-domains of modular NRPSs; SgcC5 is a free-standing NRPS condensation enzyme (rather than a modular NRPS), which catalyzes the condensation between the SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and (R)-1phenyl-1,2-ethanediol, forming an ester bond, during the synthesis of the chromoprotein enediyne antitumor antibiotic C-1027. It has some acceptor substrate promiscuity as it has been shown to also catalyze the formation of an amide bond between SgcC2-tethered (S)-3-chloro-5-hydroxy-beta-tyrosine and a mimic of the enediyne core acceptor substrate having an amine at its C-2 position. This subfamily also includes similar C-domains of modular NRPSs such as Penicillium chrysogenum N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase PCBAB. Condensation (C) domains of NRPSs normally catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380462 [Multi-domain] Cd Length: 427 Bit Score: 41.21 E-value: 2.96e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1395399044 1 AHCLTLHLFSRSDSVVTGAISNGRPElPDADRMVGLFLNTVPVR 44
Cdd:cd19539 254 AYCVLLRRYTGQTDIVVGTPVAGRNH-PRFESTVGFFVNLLPLR 296
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
4-92 |
3.27e-03 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 41.15 E-value: 3.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 4 LTLHLFSRSDSVVTGAISNGRPElPDADRMVGLFLNTVPVRSEIAG-HSWIEVADALFRQERDGHAHRRYPLSAIQQIVG 82
Cdd:cd20484 254 LLLHRYTGQEDIIVGMPTMGRPE-ERFDSLIGYFINMLPIRSRILGeETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLN 332
|
90
....*....|
gi 1395399044 83 DELSSAFNYV 92
Cdd:cd20484 333 IPRSQANSPV 342
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
802-1051 |
9.14e-03 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 38.75 E-value: 9.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 802 YLPLVRALPPDQPVYALQAAGTGQGsTPLAVLEDIAASYLA-AIRRVQPEGPYYLGGWSFGGFVAYEMARQLRALD--PQ 878
Cdd:smart00824 15 YARLAAALRGRRDVSALPLPGFGPG-EPLPASADALVEAQAeAVLRAAGGRPFVLVGHSSGGLLAHAVAARLEARGipPA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 879 AVaqlIVLDsiTVDRNHAGSASDEALLLFFYWELVWFERSDEEVEPLPEGASLEQkLDHIVERAIEAGVLpagtpratvq 958
Cdd:smart00824 94 AV---VLLD--TYPPGDPAPEGWLPELLRGVFEREDSFVPMDDARLTAMGAYLRL-FGGWTPGPVAAPTL---------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1395399044 959 rlyelfraswqaligyrpevsdqdmtLLRADGPLPLALkpmhdaagthyGDPKNGWQ-HWTSGRlDVIDVPGDHLVLMKE 1037
Cdd:smart00824 158 --------------------------LVRASEPLAEWP-----------DEDPDGWRaHWPLPH-TVVDVPGDHFTMMEE 199
|
250
....*....|....
gi 1395399044 1038 pYVETVAAEIAALL 1051
Cdd:smart00824 200 -HAAATARAVHDWL 212
|
|
| |
