|
Name |
Accession |
Description |
Interval |
E-value |
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
14-1405 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 763.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 14 IPLTKSAQGIYLAAIIDPKNPCYNTAEIMECPPETNLDYLREAFIQLYRENEGFRVQTRVQTGRPEQRViplDEFLTnLE 93
Cdd:PRK10252 8 LPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWV---DPALT-FP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 94 VLPVISLqiqeeTEEQNPVPAAVRGWASELiSEPLRTDAG-VTVRSAVTYYGGKLWV-YHSFSHVVADGFAaFNGLS-RV 170
Cdd:PRK10252 84 LPEIIDL-----RTQPDPHAAAQALMQADL-QQDLRVDSGkPLVFHQLIQLGDNRWYwYQRYHHLLVDGFS-FPAITrRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 171 AAIYRALSAGKPLPTVKRASLMELLR--ADHAAEHAREEDLALWtSEQVEVLSQPdTSLAARSA---SPAPQALREVLTL 245
Cdd:PRK10252 157 AAIYCAWLRGEPTPASPFTPFADVVEeyQRYRASEAWQRDAAFW-AEQRRQLPPP-ASLSPAPLpgrSASADILRLKLEF 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 246 PDKLQRDMLeiGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRifgaqvpaetraLGKTSAQTGTTAVNVLPVQ 325
Cdd:PRK10252 235 TDGAFRQLA--AQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRR------------LGSAALTATGPVLNVLPLR 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 326 VS--GMGSIAQALDSVKNQYARNASHPLARQE----DLERLAQsnDSRLFGAQINVIPFDAALPLGAPTENApasvgyiH 399
Cdd:PRK10252 301 VHiaAQETLPELATRLAAQLKKMRRHQRYDAEqivrDSGRAAG--DEPLFGPVLNIKVFDYQLDFPGVQAQT-------H 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 400 NISAGPVADMTITLRgiPGRGHTISVELDANPNLYTREHVEFHARHLQNWLESWAQA-ALEERSMDTLTtalPHEVELLE 478
Cdd:PRK10252 372 TLATGPVNDLELALF--PDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADpALLCGDVDILL---PGEYAQLA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 479 SFNATAHPIEYKTLLQRFQDALTRYPNEPALyacaPDEDGTLSpqspqayefsqvltYHELDARARALAKAMLEAGVCPG 558
Cdd:PRK10252 447 QVNATAVEIPETTLSALVAQQAAKTPDAPAL----ADARYQFS--------------YREMREQVVALANLLRERGVKPG 508
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 559 TAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALvygsglspIAEAELKPantqSLCGLQQLE 638
Cdd:PRK10252 509 DSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLL--------ITTADQLP----RFADVPDLT 576
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 639 FTS----LTDPVGEPLNLvdvpeaktfpgigTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGAstqdr 714
Cdd:PRK10252 577 SLCynapLAPQGAAPLQL-------------SQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTA----- 638
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 715 aGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSakrtlAEAG 794
Cdd:PRK10252 639 -DDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFVASLT-----PEGA 712
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 795 FGSGEQQRHVrylICSGEALQKDQILSAHNIMGVyPL-NLYGPTEAAVDVTFWDSS----QNPECSTVPIGQPVWNTQTR 869
Cdd:PRK10252 713 RQSCASLRQV---FCSGEALPADLCREWQQLTGA-PLhNLYGPTEAAVDVSWYPAFgeelAAVRGSSVPIGYPVWNTGLR 788
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 870 ILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDN-ATGERLYRTGDLAEWnltatnqepgtlakNPRGVIL 948
Cdd:PRK10252 789 ILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPfAPGERMYRTGDVARW--------------LDDGAVE 854
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 949 YRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVL--LYTKTPEPA-----LTAFLeigdVSETERNRIVAQARQHCE 1021
Cdd:PRK10252 855 YLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHacVINQAAATGgdarqLVGYL----VSQSGLPLDTSALQAQLR 930
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1022 NTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIEFTFDTNTAdGPHGLLEQQISEIIAGVLGRSQFGVTEDFLAAGGNS 1101
Cdd:PRK10252 931 ERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGR-APKTGTETIIAAAFSSLLGCDVVDADADFFALGGHS 1009
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1102 LAALSVIAKIEENLGKMLSIGALFANPTVKGIAAALNEDSPDIE---FAPVLPLREADSTdsatskntvPLFILPPAGGL 1178
Cdd:PRK10252 1010 LLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRrlgFGTILPLREGDGP---------TLFCFHPASGF 1080
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1179 GWCYAAYLPHIPGHPSVYALQHEAFTNPNAgYAQSLRELAEGYLARIRetleERQLPSQFSLMGWSVGGTAAVEVAALAE 1258
Cdd:PRK10252 1081 AWQFSVLSRYLDPQWSIYGIQSPRPDGPMQ-TATSLDEVCEAHLATLL----EQQPHGPYHLLGYSLGGTLAQGIAARLR 1155
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1259 TAGYDVQQVTLLDAYPVEQ--WQGIPEpdeqesfrallrmGGL-PEVSAQtvldlpqtLERLRDAGSAM--GYLPEDKLE 1333
Cdd:PRK10252 1156 ARGEEVAFLGLLDTWPPETqnWREKEA-------------NGLdPEVLAE--------IDREREAFLAAqqGSLSTELFT 1214
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503164607 1334 VCLESMRASAALMRGSNHLNFGGKVVLIGVSHDDQP-YLDAHGWELHVGSFRTVTLkNGTHPDLVNPERIPEI 1405
Cdd:PRK10252 1215 TIEGNYADAVRLLTTAHSVPFDGKATLFVAERTLQEgMSPEQAWSPWIAELDVYRQ-DCAHVDIISPEAFEKI 1286
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
49-1323 |
0e+00 |
|
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: 581.82 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 49 NLDYLREAFIQLYRENEGFRVQTRVQTGRPEQRVIPLDEFLTNLEVLPVISLQIQEETEEQnpvpAAVRGWASELISEPL 128
Cdd:COG1020 53 LVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEA----AAAAEALAPFDLLRG 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 129 RTDAGVTVRSAVTYYGGKLWVYHSFSHVVADGFAAFNGLSRVAAIYRALSAGKPLPTVKRASLMELLRADHAAEhAREED 208
Cdd:COG1020 129 PLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGE-ELARQ 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 209 LALWTSEQVEVLSQPDTSLA-ARSASPAPQALREVLTLPDKLQRDMLEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAF 287
Cdd:COG1020 208 LAYWRQQLAGLPPLLELPTDrPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 288 GVPQMNRifgaQVPAETRALGktsaqtgtTAVNVLP--VQVSGMGSIAQALDSVKNQYARNASH---PLAR-QEDLERLA 361
Cdd:COG1020 288 GTPVAGR----PRPELEGLVG--------FFVNTLPlrVDLSGDPSFAELLARVRETLLAAYAHqdlPFERlVEELQPER 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 362 QSNDSRLFGAQINVIPFDAAlplgaPTENAPASVGYIHNISAGPVADMTITLRGipgRGHTISVELDANPNLYTREHVEF 441
Cdd:COG1020 356 DLSRNPLFQVMFVLQNAPAD-----ELELPGLTLEPLELDSGTAKFDLTLTVVE---TGDGLRLTLEYNTDLFDAATIER 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 442 HARHLQNWLESWAQAalEERSMDTLTTALPHEVE-LLESFNATAHPI-EYKTLLQRFQDALTRYPNEPALyacapdEDGT 519
Cdd:COG1020 428 MAGHLVTLLEALAAD--PDQPLGDLPLLTAAERQqLLAEWNATAAPYpADATLHELFEAQAARTPDAVAV------VFGD 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 520 lspqspqayefsQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSS 599
Cdd:COG1020 500 ------------QSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAY 567
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 600 MMEDAQCSALVYGSGLspiaEAELKPANTQSLCgLQQLEFTSltdpvgeplnlvdvpEAKTFPGIGTALDDTAYILFTSG 679
Cdd:COG1020 568 MLEDAGARLVLTQSAL----AARLPELGVPVLA-LDALALAA---------------EPATNPPVPVTPDDLAYVIYTSG 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 680 STGRPKGVAISHRSIDNRLRWQQSQIPVGAstqdraGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLA 759
Cdd:COG1020 628 STGRPKGVMVEHRALVNLLAWMQRRYGLGP------GDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALA 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 760 RVIAEQNVTCLHFVPTMLTAFLEAPSakrtlaeagfgsgEQQRHVRYLICSGEALQKDQILSAHNIMGVYPL-NLYGPTE 838
Cdd:COG1020 702 ELLARHRVTVLNLTPSLLRALLDAAP-------------EALPSLRLVLVGGEALPPELVRRWRARLPGARLvNLYGPTE 768
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 839 AAVDVTFWD-SSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILD--NATG 915
Cdd:COG1020 769 TTVDSTYYEvTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADpfGFPG 848
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 916 ERLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTP-EPA 994
Cdd:COG1020 849 ARLYRTGDLARW--------------LPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPgDKR 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 995 LTAFLEIGDVSETERNRIVAQARQHcentLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIEFTFDTNTADGPHGLLEQQ 1074
Cdd:COG1020 915 LVAYVVPEAGAAAAAALLRLALALL----LPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEE 990
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1075 ISEIIAGVLGRSQFGVTEDFLAAGGNSLAALSVIAKIEENLGKMLSIGALFANPTVKGIAAALNEDSPDIEFAPVLPLRE 1154
Cdd:COG1020 991 AALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPL 1070
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1155 ADstdsatsknTVPLFILPPAGGLGWCYAAYLPHIPGHPSVYALQHEAFTNPNAGYAQSLRELAEGYLARIRETLEERQL 1234
Cdd:COG1020 1071 PL---------PPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLL 1141
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1235 PSQFSLMGWSVGGTAAVEVAALAETAGYDVQQVTLLDAYPVEQWQGIPEPDEQESFRALLRMGGLPEVSAQTVLDLPQTL 1314
Cdd:COG1020 1142 VALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1221
|
....*....
gi 503164607 1315 ERLRDAGSA 1323
Cdd:COG1020 1222 LLLAAAAAA 1230
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
531-1052 |
4.02e-154 |
|
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: 473.55 E-value: 4.02e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 531 SQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALv 610
Cdd:cd05930 10 DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLV- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 611 ygsglspiaeaelkpantqslcglqqleftsLTDPvgeplnlvdvpeaktfpgigtalDDTAYILFTSGSTGRPKGVAIS 690
Cdd:cd05930 89 -------------------------------LTDP-----------------------DDLAYVIYTSGSTGKPKGVMVE 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 691 HRSIDNRLRWQQSQIPVGAstqdraGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCL 770
Cdd:cd05930 115 HRGLVNLLLWMQEAYPLTP------GDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVL 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 771 HFVPTMLTAFLEAPSAKRtlaeagfgsgeqQRHVRYLICSGEALQKDQILSAHNIM-GVYPLNLYGPTEAAVDVTFWDSS 849
Cdd:cd05930 189 HLTPSLLRLLLQELELAA------------LPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATVDATYYRVP 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 850 QNPECS-TVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILD-NATGERLYRTGDLAEW 927
Cdd:cd05930 257 PDDEEDgRVPIGRPIPNTRVYVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNpFGPGERMYRTGDLVRW 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 928 nltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTP-EPALTAFLeigdVSE 1006
Cdd:cd05930 337 --------------LPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDgEKRLVAYV----VPD 398
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 503164607 1007 TERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd05930 399 EGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
519-1052 |
8.82e-151 |
|
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: 466.37 E-value: 8.82e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 519 TLSPQSPQAYEFSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVS 598
Cdd:cd17646 9 ARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 599 SMMEDAQCSALVYGSGLSPIAEAELKPAntqslcglqqleftsLTDPVGEPLNLVDVPEAKTFPgigtalDDTAYILFTS 678
Cdd:cd17646 89 YMLADAGPAVVLTTADLAARLPAGGDVA---------------LLGDEALAAPPATPPLVPPRP------DNLAYVIYTS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 679 GSTGRPKGVAISHRSIDNRLRWQQSQIPVGAstqdraGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYL 758
Cdd:cd17646 148 GSTGRPKGVMVTHAGIVNRLLWMQDEYPLGP------GDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 759 ARVIAEQNVTCLHFVPTMLTAFLEAPSAkrtlaeagfgsgEQQRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTE 838
Cdd:cd17646 222 AALIREHGVTTCHFVPSMLRVFLAEPAA------------GSCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTE 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 839 AAVDVTFWDSSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDN-ATGER 917
Cdd:cd17646 290 AAIDVTHWPVRGPAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPfGPGSR 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 918 LYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTPE-PALT 996
Cdd:cd17646 370 MYRTGDLARW--------------RPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGaARLV 435
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 503164607 997 AFLEIGDVSETERnriVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd17646 436 GYVVPAAGAAGPD---TAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
114-1328 |
4.09e-140 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 477.35 E-value: 4.09e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 114 AAVRGWASELISEPLrtdagvtVRSAVTYYGGK----LWVYHsfsHVVADGFAAFNGLSRVAAIYRalsaGKPLPTVK-- 187
Cdd:PRK12467 2744 AADRQQGFDLLSAPL-------LRLTLVRTGEDrhhlIYTNH---HILMDGWSGSQLLGEVLQRYF----GQPPPAREgr 2809
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 188 -RASLMELLRADhaaehaREEDLALWtSEQVEVLSQPdTSLAaRSASPAPQALREV-----LTLPDKLQRDMLEIGKMYG 261
Cdd:PRK12467 2810 yRDYIAWLQAQD------AEASEAFW-KEQLAALEEP-TRLA-RALYPAPAEAVAGhgahyLHLDATQTRQLIEFARRHR 2880
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 262 TSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRifgaqvPAETRALgktSAQTGTTaVNVLPVQVS--GMGSIAQALDSV 339
Cdd:PRK12467 2881 VTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGR------PAQLRGA---EQQLGLF-INTLPVIASprAEQTVSDWLQQV 2950
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 340 KNQ--YARNASH-PLArqeDLERLAQSNDSRLFGAqINVI---PFDAALPLGAPTEnapASVGYIHNISAGPVAdMTITL 413
Cdd:PRK12467 2951 QAQnlALREFEHtPLA---DIQRWAGQGGEALFDS-ILVFenyPISEALKQGAPSG---LRFGAVSSREQTNYP-LTLAV 3022
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 414 rgipGRGHTISVELDANPNLYTREHVEFHARHLQNWLESWAQAAleERSMDTLTTALPHEVE-LLESFNAT-AHPIEYKT 491
Cdd:PRK12467 3023 ----GLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNP--AARLGELPTLAAHERRqVLHAWNATaAAYPSERL 3096
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 492 LLQRFQDALTRYPNEPALyACApdedgtlspqspqayefSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQ 571
Cdd:PRK12467 3097 VHQLIEAQVARTPEAPAL-VFG-----------------DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEM 3158
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 572 YIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVygsglspiaeaelkpaNTQSLcgLQQLEF----TSLTdpvg 647
Cdd:PRK12467 3159 IVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLL----------------TQAHL--LEQLPApagdTALT---- 3216
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 648 epLNLVDV-PEAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGastqdrAGDRILHKTPIS 726
Cdd:PRK12467 3217 --LDRLDLnGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELD------ANDRVLLFMSFS 3288
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 727 FDVHVWELYWPLQEGAAVVIAAPDgHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEapsakrtlaeagFGSGEQQRHVRY 806
Cdd:PRK12467 3289 FDGAQERFLWTLICGGCLVVRDND-LWDPEELWQAIHAHRISIACFPPAYLQQFAE------------DAGGADCASLDI 3355
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 807 LICSGEALQKD--QILSAHnIMGVYPLNLYGPTEAAVDVTFW--DSSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGF 882
Cdd:PRK12467 3356 YVFGGEAVPPAafEQVKRK-LKPRGLTNGYGPTEAVVTVTLWkcGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGV 3434
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 883 VGELYLSGAQLAAGYQNNPEATAQAFILD--NATGERLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLH 960
Cdd:PRK12467 3435 AGELYIGGVGLARGYHQRPSLTAERFVADpfSGSGGRLYRTGDLARY--------------RADGVIEYLGRIDHQVKIR 3500
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 961 GQRLELGDIETTLSHVEGVHSAVVLLYTKTPEPALTAFLeigdVSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFP 1040
Cdd:PRK12467 3501 GFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYV----VPADPQGDWRETLRDHLAASLPDYMVPAQLLVLAAMP 3576
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1041 VSPSGKTDRKNLAQIEFTfDTNTADGPHGLLEQQISEIIAGVLGRSQFGVTEDFLAAGGNSLAALSVIAKIEENLGKMLS 1120
Cdd:PRK12467 3577 LGPNGKVDRKALPDPDAK-GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLS 3655
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1121 IGALFANPTVKGIAAALNEdsPDIEFAPVLPLREADSTDSAtskntvpLFILPPAGGLGWCYAAYLPHIPGHPSVYALQH 1200
Cdd:PRK12467 3656 LRDLMSAPTIAELAGYSPL--GDVPVNLLLDLNRLETGFPA-------LFCRHEGLGTVFDYEPLAVILEGDRHVLGLTC 3726
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1201 EAFTNPNAgYAQSLRELAEGYLARIRetleERQLPSQFSLMGWSVGGTAAVEVAALAETAGYDVQQVTLLDAYPVEQWQG 1280
Cdd:PRK12467 3727 RHLLDDGW-QDTSLQAMAVQYADYIL----WQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGLFDNTLPLPDEF 3801
|
1210 1220 1230 1240 1250
....*....|....*....|....*....|....*....|....*....|....*...
gi 503164607 1281 IPEPDEQESFRA----------LLRmgGLPEVSAQTVLDLPQTLERLRDAGSAMGYLP 1328
Cdd:PRK12467 3802 VPQAEFLELLRQlgeligranrLLR--GLEEGGVGPDVLVGIAIQRCFDIAPLELYTP 3857
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
15-1149 |
7.92e-127 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 437.47 E-value: 7.92e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 15 PLTKSAQGIYLAAIIDPKNPCYNTAEIMECPPETNLDYLREAFIQLYRENEGFRvqTRVQTGRPEQ-RVIPLDEFLTnle 93
Cdd:PRK12316 51 RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLR--TVFPRGADDSlAQVPLDRPLE--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 94 vLPVISLQIQEETEEQnpvpAAVRGWASELISEPLRTDAGVTVRSAVTYYGGKLWVYH-SFSHVVADGFAAFNGLSRVAA 172
Cdd:PRK12316 126 -VEFEDCSGLPEAEQE----ARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLlTLHHIVSDGWSMNVLIEEFSR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 173 IYRALSAGK-----PLP------TVKRASLMEllradhAAEHAREedLALWTS---EQVEVLSQPDTSlaARSASPAPQA 238
Cdd:PRK12316 201 FYSAYATGAepglpALPiqyadyALWQRSWLE------AGEQERQ--LEYWRAqlgEEHPVLELPTDH--PRPAVPSYRG 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 239 LREVLTLPDKLQRDMLEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRifgaqVPAETRALGKTSAQTgtta 318
Cdd:PRK12316 271 SRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANR-----NRAEVEGLIGFFVNT---- 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 319 vNVLPVQVSGMGSIAQALDSVKNQYARNASHplarqEDL--ERLAQS-------NDSRLFGAQINVIPFDAALplGAPTE 389
Cdd:PRK12316 342 -QVLRSVFDGRTRVATLLAGVKDTVLGAQAH-----QDLpfERLVEAlkverslSHSPLFQVMYNHQPLVADI--EALDT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 390 NAPASVGYIHNISAGPVADMTITLRGIPGRghtISVELDANPNLYTREHVEFHARHLQNWLESWAQAAlEERSMDTLTTA 469
Cdd:PRK12316 414 VAGLEFGQLEWKSRTTQFDLTLDTYEKGGR---LHAALTYATDLFEARTVERMARHWQNLLRGMVENP-QARVDELPMLD 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 470 LPHEVELLESFNATA--HPIEyKTLLQRFQDALTRYPNEPALyACApdedgtlspqspqayefSQVLTYHELDARARALA 547
Cdd:PRK12316 490 AEERGQLVEGWNATAaeYPLQ-RGVHRLFEEQVERTPEAPAL-AFG-----------------EETLDYAELNRRANRLA 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 548 KAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIAEAelkPAN 627
Cdd:PRK12316 551 HALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPL---AAG 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 628 TQSLCglqqleftsLTDPVGEPLNLVDVPeaktfPGIGTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPV 707
Cdd:PRK12316 628 VQVLD---------LDRPAAWLEGYSEEN-----PGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGL 693
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 708 GAstqdraGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAK 787
Cdd:PRK12316 694 GV------GDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDVA 767
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 788 RTLAeagfgsgeqqrhVRYLICSGEALQKD---QILSAHNIMGVYplNLYGPTEAAVDVTFWdSSQNPECSTVPIGQPVW 864
Cdd:PRK12316 768 SCTS------------LRRIVCSGEALPADaqeQVFAKLPQAGLY--NLYGPTEAAIDVTHW-TCVEEGGDSVPIGRPIA 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 865 NTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDN-ATGERLYRTGDLAEWnltatnqepgtlakNP 943
Cdd:PRK12316 833 NLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPfVAGERMYRTGDLARY--------------RA 898
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 944 RGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTpepALTAFLeigdVSETERNRIVAQARQHCENT 1023
Cdd:PRK12316 899 DGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGK---QLVGYV----VLESEGGDWREALKAHLAAS 971
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1024 LPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIEFTFDTNTADGPHGLLEQQISEIIAGVLGRSQFGVTEDFLAAGGNSLA 1103
Cdd:PRK12316 972 LPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIV 1051
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*..
gi 503164607 1104 ALSVIAKIEENlGKMLSIGALFANPTVKGIA-AALNEDSPDIEFAPV 1149
Cdd:PRK12316 1052 SIQVVSRARQA-GIQLSPRDLFQHQTIRSLAlVAKAGQATAADQGPA 1097
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
14-1142 |
1.38e-126 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 436.51 E-value: 1.38e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 14 IPLTKSAQGIYLAAIIDPKNPCYNTAEIMECPPETNLDYLREAFIQLYRENEGFRVQTRVQTGRPEQRVIPLDEFLTNLE 93
Cdd:PRK12467 50 IPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLD 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 94 VLPVIS-----LQIQEETEEQNPVPAavrgwasELISEPL------RTDAGVTVRSAVTYyggklwvyhsfsHVVADGFA 162
Cdd:PRK12467 130 DLANEQgrareSQIEAYINEEVARPF-------DLANGPLlrvrllRLADDEHVLVVTLH------------HIISDGWS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 163 AFNGLSRVAAIYRALSAGKplptvkRASLMEL--LRADHAAEH-------AREEDLALWTseqvEVLSQPDTSLA----- 228
Cdd:PRK12467 191 MRVLVEELVQLYSAYSQGR------EPSLPALpiQYADYAIWQrswleagERERQLAYWQ----EQLGGEHTVLElptdr 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 229 ARSASPAPQALREVLTLPDKLQRDMLEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRifgaqVPAETRALG 308
Cdd:PRK12467 261 PRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANR-----NRVETERLI 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 309 KTSAQTgttavNVLPVQVSGMGSIAQALDSVKN--------------------QYARNASH-PLAR-----QEDLERLAQ 362
Cdd:PRK12467 336 GFFVNT-----QVLKAEVDPQASFLELLQQVKRtalgaqahqdlpfeqlvealQPERSLSHsPLFQvmfnhQNTATGGRD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 363 SNDSRLFGAQINVIP-------FDAALplgaptenapasvgyihnisagpvaDMTITLRGIpgrGHTISVELDanpnLYT 435
Cdd:PRK12467 411 REGAQLPGLTVEELSwarhtaqFDLAL-------------------------DTYESAQGL---WAAFTYATD----LFE 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 436 REHVEFHARHLQNWLEswAQAALEERSMDTLTTALPHEVE-LLESFNATAHPIEYKTLLQRFQDALTRYPNEPALyacAP 514
Cdd:PRK12467 459 ATTIERLATHWRNLLE--AIVAEPRRRLGELPLLDAEERArELVRWNAPATEYAPDCVHQLIEAQARQHPERPAL---VF 533
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 515 DEdgtlspqspqayefsQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPA 594
Cdd:PRK12467 534 GE---------------QVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQ 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 595 ERVSSMMEDAQCSALVygsGLSPIAEAELKPANTQSLCglqqleftsltdpVGEPLNLVDvPEAKTFPGIGTALDDTAYI 674
Cdd:PRK12467 599 DRLAYMLDDSGVRLLL---TQSHLLAQLPVPAGLRSLC-------------LDEPADLLC-GYSGHNPEVALDPDNLAYV 661
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 675 LFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGAStqdragDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRD 754
Cdd:PRK12467 662 IYTSGSTGQPKGVAISHGALANYVCVIAERLQLAAD------DSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARD 735
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 755 PAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAkrtlaeagfgsgEQQRHVRYLICSGEALQKD-QILSAHNIMGVYPLNL 833
Cdd:PRK12467 736 AEAFAALMADQGVTVLKIVPSHLQALLQASRV------------ALPRPQRALVCGGEALQVDlLARVRALGPGARLINH 803
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 834 YGPTEAAVDVTFWD-SSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILD- 911
Cdd:PRK12467 804 YGPTETTVGVSTYElSDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDp 883
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 912 -NATGERLYRTGDLAEWNLTatnqepgtlaknprGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKT 990
Cdd:PRK12467 884 fGADGGRLYRTGDLARYRAD--------------GVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGD 949
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 991 PEPALTAFLEIGDVSETERNRIVAQA-RQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIEFTFDTNTADGPHG 1069
Cdd:PRK12467 950 AGLQLVAYLVPAAVADGAEHQATRDElKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQT 1029
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503164607 1070 LLEQQISEIIAGVLGRSQFGVTEDFLAAGGNSLAALSVIAKIEENLGKMLSIGALFANPTVKGIAAALNEDSP 1142
Cdd:PRK12467 1030 ELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQ 1102
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
29-1135 |
9.52e-124 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 428.04 E-value: 9.52e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 29 IDPKNPCYNTAEIMECPPETNLDYLREAFIQLYRENEGFRVQTRVQTGRPEQrVIPldefltnlevlPVISLQIQEET-E 107
Cdd:PRK12467 1132 LEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQ-VIH-----------PVGSLTLEEPLlL 1199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 108 EQNPVPAAVRGWASELISEPLRTDAGVTVRSAVTYYGGK----LWVYHsfsHVVADGFAAFNGLSRVAAIYRALSAGKpl 183
Cdd:PRK12467 1200 AADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADehvlVLTLH---HIVSDGWSMQVLVDELVALYAAYSQGQ-- 1274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 184 pTVKRASLmELLRADHAA-------EHAREEDLALWTSEQVevLSQPDTSLAARSASPAPQALREV---LTLPDKLQRDM 253
Cdd:PRK12467 1275 -SLQLPAL-PIQYADYAVwqrqwmdAGERARQLAYWKAQLG--GEQPVLELPTDRPRPAVQSHRGArlaFELPPALAEGL 1350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 254 LEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRIFgaqvpAETRALGKTSAQTgttavNVLPVQVSGMGSIA 333
Cdd:PRK12467 1351 RALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNR-----AETEGLIGFFVNT-----QVLRAEVDGQASFQ 1420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 334 QALDSVKnQYARNASHplarQEDL--ERLAQS-------NDSRLFGAQIN----VIPFDAALPlGAPTEnapaSVGYIHN 400
Cdd:PRK12467 1421 QLLQQVK-QAALEAQA----HQDLpfEQLVEAlqperslSHSPLFQVMFNhqrdDHQAQAQLP-GLSVE----SLSWESQ 1490
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 401 isagpVADMTITLRGIPGRgHTISVELDANPNLYTREHVEFHARHLQNWLESWAQAAleERSMDTLTTALPHEVE-LLES 479
Cdd:PRK12467 1491 -----TAQFDLTLDTYESS-EGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADP--ERRLGELDLLDEAERRqILEG 1562
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 480 FNATAHPIEYKTLL-QRFQDALTRYPNEPALyACApdedgtlspqspqayefSQVLTYHELDARARALAKAMLEAGVCPG 558
Cdd:PRK12467 1563 WNATHTGYPLARLVhQLIEDQAAATPEAVAL-VFG-----------------EQELTYGELNRRANRLAHRLIALGVGPE 1624
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 559 TAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPiaeaELKPANtqslcGLQQLE 638
Cdd:PRK12467 1625 VLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQA----RLPLPD-----GLRSLV 1695
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 639 FtsltDPVGEPLNlvdvPEAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGAStqdragDR 718
Cdd:PRK12467 1696 L----DQEDDWLE----GYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAA------DV 1761
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 719 ILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKrtlaeagfgsg 798
Cdd:PRK12467 1762 VLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQV----------- 1830
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 799 EQQRHVRYLICSGEALQKDQILSAHNIMG-VYPLNLYGPTEAAVDVTFWDSSQNPEC--STVPIGQPVWNTQTRILDQAL 875
Cdd:PRK12467 1831 EHPLSLRRVVCGGEALEVEALRPWLERLPdTGLFNLYGPTETAVDVTHWTCRRKDLEgrDSVPIGQPIANLSTYILDASL 1910
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 876 QPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILD--NATGERLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRT 953
Cdd:PRK12467 1911 NPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADpfGTVGSRLYRTGDLARY--------------RADGVIEYLGRI 1976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 954 DHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTPEPALTAFLEIGDVS-ETERNRIVA---QARQHCENTLPDYMV 1029
Cdd:PRK12467 1977 DHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTDPGlVDDDEAQVAlraILKNHLKASLPEYMV 2056
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1030 PRLWHTTAQFPVSPSGKTDRKNLAQIEFTFDTNTADGPHGLLEQQISEIIAGVLGRSQFGVTEDFLAAGGNSLAALSVIA 1109
Cdd:PRK12467 2057 PAHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVS 2136
|
1130 1140
....*....|....*....|....*.
gi 503164607 1110 KIEENlGKMLSIGALFANPTVKGIAA 1135
Cdd:PRK12467 2137 RARQA-GIRFTPKDLFQHQTVQSLAA 2161
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
535-984 |
1.91e-121 |
|
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: 384.69 E-value: 1.91e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 535 TYHELDARARALAKAMLEA-GVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGS 613
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 GLSPIAEAELKPAntqslcglqqLEFTSLTDPVGEPLNLVDVPEAKTFPgigtalDDTAYILFTSGSTGRPKGVAISHRS 693
Cdd:TIGR01733 81 ALASRLAGLVLPV----------ILLDPLELAALDDAPAPPPPDAPSGP------DDLAYVIYTSGSTGRPKGVVVTHRS 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IDNRLRWQQSQIPVGAstqdraGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRD-PAYLARVIAEQNVTCLHF 772
Cdd:TIGR01733 145 LVNLLAWLARRYGLDP------DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDdAALLAALIAEHPVTVLNL 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 773 VPTMLTAFLEAPsakrtlaeagfgsGEQQRHVRYLICSGEALQKDQILSAHNIMGVYPL-NLYGPTEAAVDVTFW--DSS 849
Cdd:TIGR01733 219 TPSLLALLAAAL-------------PPALASLRLVILGGEALTPALVDRWRARGPGARLiNLYGPTETTVWSTATlvDPD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 850 QNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILD---NATGERLYRTGDLAE 926
Cdd:TIGR01733 286 DAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDpfaGGDGARLYRTGDLVR 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 503164607 927 WnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVV 984
Cdd:TIGR01733 366 Y--------------LPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLRHPGVREAVV 409
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
155-1137 |
4.04e-120 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 417.05 E-value: 4.04e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 155 HVVADGFAAFNGLSRVAAIYRALSAGKPLPTVkRASLMELLRADHAAEHA--REEDLALwtsEQVEVLSQPDTSLAARSA 232
Cdd:PRK12316 4235 HILMDGWSNSQLLGEVLERYSGRPPAQPGGRY-RDYIAWLQRQDAAASEAfwREQLAAL---DEPTRLAQAIARADLRSA 4310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 233 SPAPQALREvltLPDKLQRDMLEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRifgaqvPAEtraLGKTSA 312
Cdd:PRK12316 4311 NGYGEHVRE---LDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGR------PAE---LPGIEG 4378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 313 QTGTTaVNVLPVQVSGMG--SIAQALDSVKNQY--ARNASH-PLarqEDLERLAQSNDSRLFGAQIN--VIPFDAALPLG 385
Cdd:PRK12316 4379 QIGLF-INTLPVIATPRAqqSVVEWLQQVQRQNlaLREHEHtPL---YEIQRWAGQGGEALFDSLLVfeNYPVSEALQQG 4454
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 386 APTENAPASVGyIHNISAGPvadMTITLrgipGRGHTISVELDANPNLYTREHVEFHARHLQNWLESWAQAALEERSmdt 465
Cdd:PRK12316 4455 APGGLRFGEVT-NHEQTNYP---LTLAV----GLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLG--- 4523
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 466 lttalphEVELLEsfnatahPIEYKTLLQRFQDALTRYPNEPALYACAPDEDGtLSPQSPQAYEFSQVLTYHELDARARA 545
Cdd:PRK12316 4524 -------ELQLLE-------KAEQQRIVALWNRTDAGYPATRCVHQLVAERAR-MTPDAVAVVFDEEKLTYAELNRRANR 4588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 546 LAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLS---PIAEae 622
Cdd:PRK12316 4589 LAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLqrlPIPD-- 4666
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 623 lkpantqslcGLQQLEFTSLTDPVGEPLNlvdVPEAKTFPgigtalDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQ 702
Cdd:PRK12316 4667 ----------GLASLALDRDEDWEGFPAH---DPAVRLHP------DNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATG 4727
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 703 SQIPVGAStqdragDRILHKTPISFDVHVWELYWPLQEGAAVVIAaPDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLE 782
Cdd:PRK12316 4728 ERYELTPD------DRVLQFMSFSFDGSHEGLYHPLINGASVVIR-DDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAE 4800
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 783 APSAKRTLAEagfgsgeqqrhVRYLICSGEALQKD-QILSAHNIMGVYPLNLYGPTEAAVDVTFWDSSQNPEC--STVPI 859
Cdd:PRK12316 4801 HAERDGEPPS-----------LRVYCFGGEAVAQAsYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDACgaAYMPI 4869
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 860 GQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILD--NATGERLYRTGDLAEWNltatnqepg 937
Cdd:PRK12316 4870 GTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDpfGAPGGRLYRTGDLARYR--------- 4940
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 938 tlaknPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTPEPALTAFL-----EIGDVSETERNrI 1012
Cdd:PRK12316 4941 -----ADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVvpqdpALADADEAQAE-L 5014
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1013 VAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIEFTFDTNTADGPHGLLEQQISEIIAGVLGRSQFGVTE 1092
Cdd:PRK12316 5015 RDELKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDD 5094
|
970 980 990 1000
....*....|....*....|....*....|....*....|....*
gi 503164607 1093 DFLAAGGNSLAALSVIAKIEENLGKMLSIGALFANPTVKGIAAAL 1137
Cdd:PRK12316 5095 NFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELA 5139
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
95-1235 |
5.04e-117 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 407.81 E-value: 5.04e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 95 LPVISLqiqeETEEQNPVPAAVRGWAS-------ELISEPLrtdagvtVRSAVTYYGGKLW-VYHSFSHVVADGFAAFNG 166
Cdd:PRK12316 1632 LPFAEL----DWRGREDLGQALDALAQaerqkgfDLTRAPL-------LRLVLVRTGEGRHhLIYTNHHILMDGWSNAQL 1700
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 167 LSRVAAIYralsAGKPLPTVK---RASLMELLRADHAAEHAreedlaLWtSEQVEVLSQPdTSLAARSASPAPQA--LRE 241
Cdd:PRK12316 1701 LGEVLQRY----AGQPVAAPGgryRDYIAWLQRQDAAASEA------FW-KEQLAALEEP-TRLAQAARTEDGQVgyGDH 1768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 242 VLTLPDKLQRDMLEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRifgaqvPAEtraLGKTSAQTGTTaVNV 321
Cdd:PRK12316 1769 QQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGR------PAE---LPGIEQQIGLF-INT 1838
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 322 LPVQVSGMG--SIAQALDSVK--NQYARNASH-PLArqeDLERLAQSNDSRLFGAQI--NVIPFDAALPLGAPtenAPAS 394
Cdd:PRK12316 1839 LPVIAAPRPdqSVADWLQEVQalNLALREHEHtPLY---DIQRWAGQGGEALFDSLLvfENYPVAEALKQGAP---AGLV 1912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 395 VGYIHNISAgpvADMTITLrGIpGRGHTISVELDANPNLYTREHVEFHARHLQNWLESWAQAAleERSMDtlttalphEV 474
Cdd:PRK12316 1913 FGRVSNHEQ---TNYPLTL-AV-TLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDA--QAALG--------EL 1977
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 475 ELLEsfnatahPIEYKTLLQRFQDALTRYPNEPALYAcAPDEDGTLSPQSPQAYEFSQVLTYHELDARARALAKAMLEAG 554
Cdd:PRK12316 1978 ALLD-------AGERQRILADWDRTPEAYPRGPGVHQ-RIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARG 2049
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 555 VCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSpiaeAELKPANtqslcGL 634
Cdd:PRK12316 2050 VGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLL----ERLPLPA-----GV 2120
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 635 QQLEFTSltdpvgePLNLVDVPEakTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWqqsqipVGASTQDR 714
Cdd:PRK12316 2121 ARLPLDR-------DAEWADYPD--TAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQA------AGERYELS 2185
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 715 AGDRILHKTPISFDVHVWELYWPLQEGAAVvIAAPDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLE-APSAKRTLAea 793
Cdd:PRK12316 2186 PADCELQFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEhAERDGRPPA-- 2262
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 794 gfgsgeqqrhVRYLICSGEALQKDQILSAHNIM-GVYPLNLYGPTEAAVDVTFWDSSQNPECST--VPIGQPVWNTQTRI 870
Cdd:PRK12316 2263 ----------VRVYCFGGEAVPAASLRLAWEALrPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAayVPIGRALGNRRAYI 2332
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 871 LDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILD--NATGERLYRTGDLAEWNLTatnqepgtlaknprGVIL 948
Cdd:PRK12316 2333 LDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDpfSASGERLYRTGDLARYRAD--------------GVVE 2398
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 949 YRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTPEPALTAFLEIGDVSETERNRIVAQARQhcenTLPDYM 1028
Cdd:PRK12316 2399 YLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDLLAELRAWLAA----RLPAYM 2474
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1029 VPRLWHTTAQFPVSPSGKTDRKNLAQIEFTFDTNTADGPHGLLEQQISEIIAGVLGRSQFGVTEDFLAAGGNSLAALSVI 1108
Cdd:PRK12316 2475 VPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVV 2554
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1109 AKIEENLGKMLSIGALFANPTVKGIAAALNEDSPDIEFAPVLPLREADSTDSATSKNTVPLFILPPaGGLGWCYAAYLpH 1188
Cdd:PRK12316 2555 SRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEP-ESAAYHLPSAL-H 2632
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|....*....
gi 503164607 1189 IPGHPSVYALQH--EAFTNPNAGYAQSLRELAEGYLARIRETLEERQLP 1235
Cdd:PRK12316 2633 LRGVLDQAALEQafDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVL 2681
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
522-1052 |
1.57e-114 |
|
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: 368.98 E-value: 1.57e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 522 PQSPQAYEFSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMM 601
Cdd:cd17651 9 PDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFML 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 602 EDAQCSALVYGSGLSPIAEAELKPantqslcGLQQLEFTSLTDPVGEplnlvdvpeaktfPGIGTALDDTAYILFTSGST 681
Cdd:cd17651 89 ADAGPVLVLTHPALAGELAVELVA-------VTLLDQPGAAAGADAE-------------PDPALDADDLAYVIYTSGST 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 682 GRPKGVAISHRSIDNRLRWQQSQIPVGastqdrAGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARV 761
Cdd:cd17651 149 GRPKGVVMPHRSLANLVAWQARASSLG------PGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAW 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 762 IAEQNVTCLhFVPtmlTAFLEApsakrtLAEAGFGSGEQQRHVRYLICSGEALQKDQILSAHNIMGVYPL--NLYGPTEA 839
Cdd:cd17651 223 LDEQRISRV-FLP---TVALRA------LAEHGRPLGVRLAALRYLLTGGEQLVLTEDLREFCAGLPGLRlhNHYGPTET 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 840 AVdVTFWDSSQNPEC--STVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNA-TGE 916
Cdd:cd17651 293 HV-VTALSLPGDPAAwpAPPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFvPGA 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 917 RLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTP-EPAL 995
Cdd:cd17651 372 RMYRTGDLARW--------------LPDGELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPgEKRL 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 503164607 996 TAFLeigdVSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd17651 438 VAYV----VGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDALPLTPNGKLDRRAL 490
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
14-1154 |
1.11e-112 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 394.32 E-value: 1.11e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 14 IPLTKSAQGIYLAAIIDPKNPCYNTAEIMECPPETNLDYLREAFIQLYRENEGFRVQTRVQTGRPEQrvipldefltnlE 93
Cdd:PRK12316 2603 LPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQ------------V 2670
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 94 VLPVISLQIQEEtEEQNPVPAAVRGWASELISEPLRTDAGVTVRSAVTYYGGKLWVYH-SFSHVVADGFAAFNGLSRVAA 172
Cdd:PRK12316 2671 ILPNMSLRIVLE-DCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLViTQHHIVSDGWSMQVMVDELVQ 2749
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 173 IYRALSAGK--PLPTVK-RASLMELLRADHAAEHAREEDLALWTSEQVEvlSQPDTSLAARSASPAPQ---ALREVLTLP 246
Cdd:PRK12316 2750 AYAGARRGEqpTLPPLPlQYADYAAWQRAWMDSGEGARQLDYWRERLGG--EQPVLELPLDRPRPALQshrGARLDVALD 2827
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 247 DKLQRDMLEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRifgaqVPAETRALGKTSAQTgttavNVLPVQV 326
Cdd:PRK12316 2828 VALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANR-----NRAETERLIGFFVNT-----QVLRAQV 2897
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 327 SGMGSIAQALDSVKNQYARNASHPLARQEDLERLAQSNDSRLFGAQINVIPFDAALPLGAPTENAPASVGYiHNISAGPV 406
Cdd:PRK12316 2898 DAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIESF-AWDGAATQ 2976
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 407 ADMTITLRGIPgrgHTISVELDANPNLYTREHVEFHARHLQNWLESWAQAAleERSMDTLTTALPHEVE-LLESFNATA- 484
Cdd:PRK12316 2977 FDLALDTWESA---EGLGASLTYATDLFDARTVERLARHWQNLLRGMVENP--QRSVDELAMLDAEERGqLLEAWNATAa 3051
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 485 HPIEYKTLLQRFQDALTRYPNEPALYACapdedgtlspqspqayefSQVLTYHELDARARALAKAMLEAGVCPGTAVGLR 564
Cdd:PRK12316 3052 EYPLERGVHRLFEEQVERTPDAVALAFG------------------EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVA 3113
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 565 FHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALvygsglspIAEAELKPANTQslcGLQQLEFTSLTD 644
Cdd:PRK12316 3114 VERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLL--------LSQSHLRLPLAQ---GVQVLDLDRGDE 3182
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 645 PVGEplnlvdvpeakTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGastqdrAGDRILHKTP 724
Cdd:PRK12316 3183 NYAE-----------ANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLG------VGDRVLQFTT 3245
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 725 ISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRtlaeagfgsgeqQRHV 804
Cdd:PRK12316 3246 FSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHR------------CTSL 3313
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 805 RYLICSGEALQKDqiLSAHNIMGVYPLNLYGPTEAAVDVTFWDSSQnPECSTVPIGQPVWNTQTRILDQALQPIPPGFVG 884
Cdd:PRK12316 3314 KRIVCGGEALPAD--LQQQVFAGLPLYNLYGPTEATITVTHWQCVE-EGKDAVPIGRPIANRACYILDGSLEPVPVGALG 3390
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 885 ELYLSGAQLAAGYQNNPEATAQAFILDN-ATGERLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQR 963
Cdd:PRK12316 3391 ELYLGGEGLARGYHNRPGLTAERFVPDPfVPGERLYRTGDLARY--------------RADGVIEYIGRVDHQVKIRGFR 3456
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 964 LELGDIETTLSHVEGVHSAVVLlytKTPEPALTAFLEIGDVSETERNRIVAQARQhcenTLPDYMVPRLWHTTAQFPVSP 1043
Cdd:PRK12316 3457 IELGEIEARLLEHPWVREAVVL---AVDGRQLVAYVVPEDEAGDLREALKAHLKA----SLPEYMVPAHLLFLERMPLTP 3529
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1044 SGKTDRKNLAQIEFTFDTNTADGPHGLLEQQISEIIAGVLGRSQFGVTEDFLAAGGNSLAALSVIAKIEEnLGKMLSIGA 1123
Cdd:PRK12316 3530 NGKLDRKALPRPDAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQ-AGIRFTPKD 3608
|
1130 1140 1150
....*....|....*....|....*....|....*...
gi 503164607 1124 LFANPTVKGIAAALN-------EDSPDIEFAPVLPLRE 1154
Cdd:PRK12316 3609 LFQHQTIQGLARVARvgggvavDQGPVSGETLLLPIQQ 3646
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
534-1052 |
2.41e-112 |
|
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: 362.38 E-value: 2.41e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALvygs 613
Cdd:cd12116 13 LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALV---- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 glspIAEAELkpantqslcglqqlEFTSLTDPVGEPLNLVDVPEAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRS 693
Cdd:cd12116 89 ----LTDDAL--------------PDRLPAGLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IDNRLRwqqsqiPVGASTQDRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNvtclhfv 773
Cdd:cd12116 151 LVNFLH------SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHS------- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 774 PTMLTAfleAPSAKRTLAEAGFgsgEQQRHVRYLiCSGEALqkDQILSAHNIMGVYPL-NLYGPTEAavdvTFWDSSQ-- 850
Cdd:cd12116 218 ITVMQA---TPATWRMLLDAGW---QGRAGLTAL-CGGEAL--PPDLAARLLSRVGSLwNLYGPTET----TIWSTAArv 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 851 NPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNAT--GERLYRTGDLAEWn 928
Cdd:cd12116 285 TAAAGPIPIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgpGSRLYRTGDLVRR- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 929 ltatnQEPGTLaknprgviLYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTPEPALTAFLEIGDVSETE 1008
Cdd:cd12116 364 -----RADGRL--------EYLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGAAPD 430
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 503164607 1009 RNRIvaqaRQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd12116 431 AAAL----RAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
29-1125 |
1.55e-108 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 381.82 E-value: 1.55e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 29 IDPKNPCYNTAEIMECPPETNLDYLREAFIQLYRENEGFRVQTRVQTGRPEQRVIPLDEFltNLEVLPVISLQIQEETEe 108
Cdd:PRK05691 691 LDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEF--ALQRIDLSDLPEAEREA- 767
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 109 qnpvpaavRGWA--SELISEPLRTDAGVTVRSAVTYYGG---KLWVyhSFSHVVADGFAAFNGLSRVAAIYRALSAGKPL 183
Cdd:PRK05691 768 --------RAAQirEEEARQPFDLEKGPLLRVTLVRLDDeehQLLV--TLHHIVADGWSLNILLDEFSRLYAAACQGQTA 837
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 184 ----PTVKRASLMELLRADHAAEHArEEDLALWTSEQVEvlSQPDTSLAA---RSASPAPQALREVLTLPDKLQRDMLEI 256
Cdd:PRK05691 838 elapLPLGYADYGAWQRQWLAQGEA-ARQLAYWKAQLGD--EQPVLELATdhpRSARQAHSAARYSLRVDASLSEALRGL 914
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 257 GKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRifgaqvP-AETRALGKTSAQTgttavNVLPVQVSGMGSIAQA 335
Cdd:PRK05691 915 AQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANR------PrLETQGLVGFFINT-----QVLRAQLDGRLPFTAL 983
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 336 LDSVK-NQYARNASHPLARQEDLERLAQSNDSRLFGAQINVIPFDAA----LPlGAPTENAPAsvgyiHNISAgpvaDMT 410
Cdd:PRK05691 984 LAQVRqATLGAQAHQDLPFEQLVEALPQAREQGLFQVMFNHQQRDLSalrrLP-GLLAEELPW-----HSREA----KFD 1053
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 411 ITLRGIPGRGHTISVELDANPNLYTREHVEFHARHLQNWLESWAQAAleERSMDTLTTALPHEVELLESFNATAHPIEYK 490
Cdd:PRK05691 1054 LQLHSEEDRNGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDP--QRALGDVQLLDAAERAQLAQWGQAPCAPAQA 1131
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 491 TLLQRFQDALTRYPNEPALYAcapdEDGTLspqspqayefsqvlTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLE 570
Cdd:PRK05691 1132 WLPELLNEQARQTPERIALVW----DGGSL--------------DYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQ 1193
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 571 QYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSpiaeAELKPANTQSLCGLQQLEFTSLTDpvgepl 650
Cdd:PRK05691 1194 LLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLL----ERLPQAEGVSAIALDSLHLDSWPS------ 1263
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 651 nlvdvpeakTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQsqipvgASTQDRAGDRILHKTPISFDVH 730
Cdd:PRK05691 1264 ---------QAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQ------ATYALDDSDVLMQKAPISFDVS 1328
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 731 VWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAkrtlaeagfgsgEQQRHVRYLICS 810
Cdd:PRK05691 1329 VWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFIDEPLA------------AACTSLRRLFSG 1396
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 811 GEALQ---KDQILSahNIMGVYPLNLYGPTEAAVDVTFWdSSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELY 887
Cdd:PRK05691 1397 GEALPaelRNRVLQ--RLPQVQLHNRYGPTETAINVTHW-QCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELC 1473
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 888 LSGAQLAAGYQNNPEATAQAFILD--NATGERLYRTGDLAEWNLtatnqepgtlaknpRGVILYRGRTDHQVKLHGQRLE 965
Cdd:PRK05691 1474 IGGAGLARGYLGRPALTAERFVPDplGEDGARLYRTGDRARWNA--------------DGALEYLGRLDQQVKLRGFRVE 1539
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 966 LGDIETTLSHVEGVHSAVVLLYTKTPEPALTAFLEIGDVSETERNRIVAQARQhcenTLPDYMVPRLWHTTAQFPVSPSG 1045
Cdd:PRK05691 1540 PEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAERLKAALAA----ELPEYMVPAQLIRLDQMPLGPSG 1615
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1046 KTDRKNLAQIEFTFDTNTAdgPHGLLEQQISEIIAGVLGRSQFGVTEDFLAAGGNSLAALSVIAKIEENLGKMLSIGALF 1125
Cdd:PRK05691 1616 KLDRRALPEPVWQQREHVE--PRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALF 1693
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
532-1052 |
6.91e-108 |
|
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: 350.73 E-value: 6.91e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVY 611
Cdd:cd12117 21 RSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLLT 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 GSGLSPIAEaelkpantqslcGLQQLEFTSLTDPVGEPLNLVDVPEAktfpgigtalDDTAYILFTSGSTGRPKGVAISH 691
Cdd:cd12117 101 DRSLAGRAG------------GLEVAVVIDEALDAGPAGNPAVPVSP----------DDLAYVMYTSGSTGRPKGVAVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 692 RSIDnRLRWQQSQIPVGastqdrAGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLH 771
Cdd:cd12117 159 RGVV-RLVKNTNYVTLG------PDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 772 fvptmLTAFL------EAPSAKRTLaeagfgsgeqqrhvRYLICSGEALQKDQI---LSAHNimGVYPLNLYGPTEAAVD 842
Cdd:cd12117 232 -----LTAALfnqladEDPECFAGL--------------RELLTGGEVVSPPHVrrvLAACP--GLRLVNGYGPTENTTF 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 843 VTFWDSSQ-NPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNAT-GERLYR 920
Cdd:cd12117 291 TTSHVVTElDEVAGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGpGERLYR 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 921 TGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTP-EPALTAFL 999
Cdd:cd12117 371 TGDLARW--------------LPDGRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGgDKRLVAYV 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 503164607 1000 eigdVSETERNriVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd12117 437 ----VAEGALD--AAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
522-1052 |
2.70e-105 |
|
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: 342.30 E-value: 2.70e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 522 PQSPqAYEF-SQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSM 600
Cdd:cd05945 5 PDRP-AVVEgGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 601 MEDAQCSALvygsglspiaeaelkpantqslcglqqleftsLTDPvgeplnlvdvpeaktfpgigtalDDTAYILFTSGS 680
Cdd:cd05945 84 LDAAKPALL--------------------------------IADG-----------------------DDNAYIIFTSGS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 681 TGRPKGVAISHRSIDNRLRWQQSQIPVGAstqdraGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLAR 760
Cdd:cd05945 109 TGRPKGVQISHDNLVSFTNWMLSDFPLGP------GDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 761 VIAEQNVTCLHFVPTMLTAFLEAPsakrTLAEAGFGSgeqqrhVRYLICSGEALQKDQilsAHNIMGVYP----LNLYGP 836
Cdd:cd05945 183 FLAEHGITVWVSTPSFAAMCLLSP----TFTPESLPS------LRHFLFCGEVLPHKT---ARALQQRFPdariYNTYGP 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 837 TEAAVDVTF--WDSSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNat 914
Cdd:cd05945 250 TEATVAVTYieVTPEVLDGYDRLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 915 GERLYRTGDLAEwnltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVL-LYTKTPEP 993
Cdd:cd05945 328 GQRAYRTGDLVR--------------LEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVpKYKGEKVT 393
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 503164607 994 ALTAFLEIGDVSETERNRIVaqaRQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd05945 394 ELIAFVVPKPGAEAGLTKAI---KAELAERLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
494-1052 |
6.89e-100 |
|
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: 328.90 E-value: 6.89e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 494 QRFQDALTRYPNEPALyACapdEDgtlspqspqayefsQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYI 573
Cdd:cd17655 1 ELFEEQAEKTPDHTAV-VF---ED--------------QTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIV 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 574 ALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGL-SPIAEAELkpantqslcgLQQLEFTSLTDPVGEPLNL 652
Cdd:cd17655 63 GILGILKAGGAYLPIDPDYPEERIQYILEDSGADILLTQSHLqPPIAFIGL----------IDLLDEDTIYHEESENLEP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 653 VDVPeaktfpgigtalDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGAstqdraGDRILHKTPISFDVHVW 732
Cdd:cd17655 133 VSKS------------DDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGE------HLRVALFASISFDASVT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 733 ELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLHFVPTMLtafleapsakRTLAEAGFGSGEQQRHvryLICSGE 812
Cdd:cd17655 195 EIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHL----------KLLDAADDSEGLSLKH---LIVGGE 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 813 ALQKD--QILSAHNIMGVYPLNLYGPTEAAVDVTFWD-SSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLS 889
Cdd:cd17655 262 ALSTElaKKIIELFGTNPTITNAYGPTETTVDASIYQyEPETDQQVSVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 890 GAQLAAGYQNNPEATAQAFILDN-ATGERLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGD 968
Cdd:cd17655 342 GEGVARGYLNRPELTAEKFVDDPfVPGERMYRTGDLARW--------------LPDGNIEFLGRIDHQVKIRGYRIELGE 407
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 969 IETTLSHVEGVHSAVVLLYT-KTPEPALTAFLeigdVSetERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKT 1047
Cdd:cd17655 408 IEARLLQHPDIKEAVVIARKdEQGQNYLCAYI----VS--EKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKV 481
|
....*
gi 503164607 1048 DRKNL 1052
Cdd:cd17655 482 DRKAL 486
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
532-1052 |
1.06e-97 |
|
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: 321.18 E-value: 1.06e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALvy 611
Cdd:cd17643 11 RRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLL-- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 gsglspiaeaelkpantqslcglqqleftsLTDPvgeplnlvdvpeaktfpgigtalDDTAYILFTSGSTGRPKGVAISH 691
Cdd:cd17643 89 ------------------------------LTDP-----------------------DDLAYVIYTSGSTGRPKGVVVSH 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 692 RSIDNRLRWQQSQIPVGAStqdragDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLH 771
Cdd:cd17643 116 ANVLALFAATQRWFGFNED------DVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLN 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 772 fvptmltaflEAPSAKRTLAEAGFGSGEQQRHVRYLICSGEALQKDQILS---AHNIMGVYPLNLYGPTEAAVDVTF--W 846
Cdd:cd17643 190 ----------QTPSAFYQLVEAADRDGRDPLALRYVIFGGEALEAAMLRPwagRFGLDRPQLVNMYGITETTVHVTFrpL 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 847 DSSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNAT--GERLYRTGDL 924
Cdd:cd17643 260 DAADLPAAAASPIGRPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgpGSRMYRTGDL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 925 AEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTP-EPALTAFLEIGD 1003
Cdd:cd17643 340 ARR--------------LPDGELEYLGRADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPgDTRLVAYVVADD 405
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 503164607 1004 VSETERnrivAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd17643 406 GAAADI----AELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
496-959 |
3.93e-97 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 318.49 E-value: 3.93e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 496 FQDALTRYPNEPALYacaPDEDGTLspqspqayefsqvlTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIAL 575
Cdd:pfam00501 1 LERQAARTPDKTALE---VGEGRRL--------------TYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAF 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 576 YAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIAEAELKPANTQSLCGLQQLeftSLTDPVGEPLNLVDV 655
Cdd:pfam00501 64 LACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDDALKLEELLEALGKLEVVKLVLVLD---RDPVLKEEPLPEEAK 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 656 PEAKTF-PGIGTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGAStqDRAGDRILHKTPISFDV-HVWE 733
Cdd:pfam00501 141 PADVPPpPPPPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFG--LGPDDRVLSTLPLFHDFgLSLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 734 LYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRTLaeagFGSgeqqrhVRYLICSGEA 813
Cdd:pfam00501 219 LLGPLLAGATVVLPPGFPALDPAALLELIERYKVTVLYGVPTLLNMLLEAGAPKRAL----LSS------LRLVLSGGAP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 814 LQKDQILSAHNIMGVYPLNLYGPTEAAVDVTFWDSSQNPECSTVPIGQPVWNTQTRILDQA-LQPIPPGFVGELYLSGAQ 892
Cdd:pfam00501 289 LPPELARRFRELFGGALVNGYGLTETTGVVTTPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPG 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503164607 893 LAAGYQNNPEATAQAFIldnatGERLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKL 959
Cdd:pfam00501 369 VMKGYLNDPELTAEAFD-----EDGWYRTGDLGRR--------------DEDGYLEIVGRKKDQIKL 416
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
531-1052 |
4.66e-97 |
|
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: 320.37 E-value: 4.66e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 531 SQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALv 610
Cdd:cd12114 10 DGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLV- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 611 ygsglspiaeaelkpantqslcgLQQLEFTSLTDPVGEPLNLVDVPEA--KTFPGIGTALDDTAYILFTSGSTGRPKGVA 688
Cdd:cd12114 89 -----------------------LTDGPDAQLDVAVFDVLILDLDALAapAPPPPVDVAPDDLAYVIFTSGSTGTPKGVM 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 689 ISHRSIDNRLRWQQSQIPVGAStqdragDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVT 768
Cdd:cd12114 146 ISHRAALNTILDINRRFAVGPD------DRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVT 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 769 CLHFVPT---MLTAFLEAPSAKrtlaeagfgsgeqQRHVRYLICSGEALQKDQILSAHNIM-GVYPLNLYGPTEAAVDVT 844
Cdd:cd12114 220 LWNSVPAlleMLLDVLEAAQAL-------------LPSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEASIWSI 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 845 FWD-SSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDnATGERLYRTGD 923
Cdd:cd12114 287 YHPiDEVPPDWRSIPYGRPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTH-PDGERLYRTGD 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 924 LAEWNltatnqepgtlaknPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTPEPALTAFLeigd 1003
Cdd:cd12114 366 LGRYR--------------PDGTLEFLGRRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFV---- 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 503164607 1004 VSETERNRIVAQA-RQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd12114 428 VPDNDGTPIAPDAlRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
492-1055 |
1.52e-95 |
|
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: 316.41 E-value: 1.52e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 492 LLQRFQDALTRYPNEPALyaCAPDEDgtlspqspqayefsqvLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQ 571
Cdd:cd05918 1 VHDLIEERARSQPDAPAV--CAWDGS----------------LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWA 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 572 YIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCsalvygsglspiaeaelkpantqslcglqqleftsltdpvgePLN 651
Cdd:cd05918 63 VVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGA------------------------------------------KVV 100
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 652 LVDVPeaktfpgigtalDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGASTqdragdRILHKTPISFDVHV 731
Cdd:cd05918 101 LTSSP------------SDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLTSES------RVLQFASYTFDVSI 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 732 WELYWPLQEGAAVVIAAPDGHRDPayLARVIAEQNVTCLHFVPTMltAFLEAPSAKRTLaeagfgsgeqqrhvRYLICSG 811
Cdd:cd05918 163 LEIFTTLAAGGCLCIPSEEDRLND--LAGFINRLRVTWAFLTPSV--ARLLDPEDVPSL--------------RTLVLGG 224
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 812 EALQKDQILS-AHnimGVYPLNLYGPTEAAVDVTfwdSSQNPECSTVP-IGQPVwNTQTRILDQA--LQPIPPGFVGELY 887
Cdd:cd05918 225 EALTQSDVDTwAD---RVRLINAYGPAECTIAAT---VSPVVPSTDPRnIGRPL-GATCWVVDPDnhDRLVPIGAVGELL 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 888 LSGAQLAAGYQNNPEATAQAFILD--------NATGERLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKL 959
Cdd:cd05918 298 IEGPILARGYLNDPEKTAAAFIEDpawlkqegSGRGRRLYRTGDLVRY--------------NPDGSLEYVGRKDTQVKI 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 960 HGQRLELGDIETTL-SHVEGVHSAVVLLYTKT---PEPALTAFLEIGDVSETERN-------------RIVAQARQHCEN 1022
Cdd:cd05918 364 RGQRVELGEIEHHLrQSLPGAKEVVVEVVKPKdgsSSPQLVAFVVLDGSSSGSGDgdslflepsdefrALVAELRSKLRQ 443
|
570 580 590
....*....|....*....|....*....|...
gi 503164607 1023 TLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQI 1055
Cdd:cd05918 444 RLPSYMVPSVFLPLSHLPLTASGKIDRRALREL 476
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
532-1052 |
2.08e-95 |
|
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: 315.08 E-value: 2.08e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVy 611
Cdd:cd17649 11 QSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLL- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 gsglspiaeaelkpanTQslcglqqleftsltdpvgEPLNLvdvpeaktfpgigtalddtAYILFTSGSTGRPKGVAISH 691
Cdd:cd17649 90 ----------------TH------------------HPRQL-------------------AYVIYTSGSTGTPKGVAVSH 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 692 RSIDNRLRWQQSQIPVGAstqdraGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLH 771
Cdd:cd17649 117 GPLAAHCQATAERYGLTP------GDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLD 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 772 FVPTMLTAFLEapsakrtLAEAGfGSGEQQRhVRYLICSGEALQKDqILSAHNIMGVYPLNLYGPTEAAVDVTFWDSSQN 851
Cdd:cd17649 191 LPPAYLQQLAE-------EADRT-GDGRPPS-LRLYIFGGEALSPE-LLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 852 PEC--STVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILD--NATGERLYRTGDLAEW 927
Cdd:cd17649 261 AARagASMPIGRPLGGRSAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDpfGAPGSRLYRTGDLARW 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 928 nltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTPEPALTAFLEIGDVSET 1007
Cdd:cd17649 341 --------------RDDGVIEYLGRVDHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQ 406
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 503164607 1008 ERNRivAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd17649 407 PELR--AQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKAL 449
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
534-1052 |
2.13e-94 |
|
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: 311.94 E-value: 2.13e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALvygs 613
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLV---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 glspiaeaelkpantqslcglqqleftsLTDPvgeplnlvdvpeaktfpgigtalDDTAYILFTSGSTGRPKGVAISHRS 693
Cdd:cd12115 101 ----------------------------LTDP-----------------------DDLAYVIYTSGSTGRPKGVAIEHRN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IDNRLRWQQSQIPvgasTQDRAGdrILHKTPISFDVHVWELYWPLQEGAAVVIAapDGHRDPAYLArviAEQNVTCLHFV 773
Cdd:cd12115 130 AAAFLQWAAAAFS----AEELAG--VLASTSICFDLSVFELFGPLATGGKVVLA--DNVLALPDLP---AAAEVTLINTV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 774 PTMLTAFLEA---PSAKRTLAEAGfgsgeqqrhvrylicsgEALQKDQILSAHNIMGVYPL-NLYGPTEaavDVTFWDSS 849
Cdd:cd12115 199 PSAAAELLRHdalPASVRVVNLAG-----------------EPLPRDLVQRLYARLQVERVvNLYGPSE---DTTYSTVA 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 850 QNPECS--TVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILD-NATGERLYRTGDLAE 926
Cdd:cd12115 259 PVPPGAsgEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDpFGPGARLYRTGDLVR 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 927 WnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLY-TKTPEPALTAFLeigdVS 1005
Cdd:cd12115 339 W--------------RPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIgDAAGERRLVAYI----VA 400
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 503164607 1006 ETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd12115 401 EPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
534-1052 |
6.07e-91 |
|
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: 301.86 E-value: 6.07e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVygs 613
Cdd:cd17652 13 LTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 glspiaeaelkpantqslcglqqleftsltdpvgeplnlvdvpeaktfpgigTALDDTAYILFTSGSTGRPKGVAISHRS 693
Cdd:cd17652 90 ----------------------------------------------------TTPDNLAYVIYTSGSTGRPKGVVVTHRG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IDNRLRWQQSQIPVGAstqdraGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTclhfv 773
Cdd:cd17652 118 LANLAAAQIAAFDVGP------GSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRIT----- 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 774 ptmlTAFLeAPSAKRTLAEAGFGSGeqqrhvRYLICSGEALQKD--QILSAHNIMgvypLNLYGPTEAAVDVTFWDSSqn 851
Cdd:cd17652 187 ----HVTL-PPAALAALPPDDLPDL------RTLVVAGEACPAElvDRWAPGRRM----INAYGPTETTVCATMAGPL-- 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 852 PECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILD--NATGERLYRTGDLAEWnl 929
Cdd:cd17652 250 PGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADpfGAPGSRMYRTGDLARW-- 327
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 930 tatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTP-EPALTAFLeigdVSETE 1008
Cdd:cd17652 328 ------------RADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPgDKRLVAYV----VPAPG 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 503164607 1009 RNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd17652 392 AAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
532-1052 |
2.76e-86 |
|
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: 289.72 E-value: 2.76e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVy 611
Cdd:cd17644 24 QQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 gsglspiaeaelkpanTQslcglqqleftsltdpvgePLNLvdvpeaktfpgigtalddtAYILFTSGSTGRPKGVAISH 691
Cdd:cd17644 103 ----------------TQ-------------------PENL-------------------AYVIYTSGSTGKPKGVMIEH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 692 RSIDNRLRWQQSQIPVGAStqdragDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLH 771
Cdd:cd17644 129 QSLVNLSHGLIKEYGITSS------DRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 772 FVPTMLTAFLEAPS-AKRTLAEagfgsgeqqrHVRYLICSGEALQKDQILSAHNIMGVYP--LNLYGPTEAAVDVTFWDS 848
Cdd:cd17644 203 LPPAYWHLLVLELLlSTIDLPS----------SLRLVIVGGEAVQPELVRQWQKNVGNFIqlINVYGPTEATIAATVCRL 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 849 SQNPECS--TVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFI---LDNATGERLYRTGD 923
Cdd:cd17644 273 TQLTERNitSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFIshpFNSSESERLYKTGD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 924 LAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTP-EPALTAFLeig 1002
Cdd:cd17644 353 LARY--------------LPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPgNKRLVAYI--- 415
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 503164607 1003 dVSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd17644 416 -VPHYEESPSTVELRQFLKAKLPDYMIPSAFVVLEELPLTPNGKIDRRAL 464
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
531-1054 |
4.44e-81 |
|
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: 273.80 E-value: 4.44e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 531 SQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALV 610
Cdd:cd17653 20 GGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 611 YGSglSPiaeaelkpantqslcglqqleftsltdpvgeplnlvdvpeaktfpgigtalDDTAYILFTSGSTGRPKGVAIS 690
Cdd:cd17653 100 TTD--SP---------------------------------------------------DDLAYIIFTSGSTGIPKGVMVP 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 691 HRSIDNRLRWQQSQIPVgastqdRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPdghrdPAYLARVIAEQNVTcl 770
Cdd:cd17653 127 HRGVLNYVSQPPARLDV------GPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADP-----SDPFAHVARTVDAL-- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 771 hfvptMLTafleaPSAKRTLAEAGFGSgeqqrhVRYLICSGEALQKDqiLSAHNIMGVYPLNLYGPTEAAVDVTFwdSSQ 850
Cdd:cd17653 194 -----MST-----PSILSTLSPQDFPN------LKTIFLGGEAVPPS--LLDRWSPGRRLYNAYGPTECTISSTM--TEL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 851 NPEcSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNA-TGERLYRTGDLAEWnl 929
Cdd:cd17653 254 LPG-QPVTIGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFwPGSRMYRTGDYGRW-- 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 930 taTNQepgtlaknprGVILYRGRTDHQVKLHGQRLELGDIETT-LSHVEGVHSAVVLLYtktpEPALTAFLEIGDVSete 1008
Cdd:cd17653 331 --TED----------GGLEFLGREDNQVKVRGFRINLEEIEEVvLQSQPEVTQAAAIVV----NGRLVAFVTPETVD--- 391
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 503164607 1009 rnriVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQ 1054
Cdd:cd17653 392 ----VDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKALRE 433
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
492-1054 |
1.75e-80 |
|
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: 272.84 E-value: 1.75e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 492 LLQRFQDALTRYPNEPALYacapDEDGTLspqspqayefsqvlTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQ 571
Cdd:COG0318 1 LADLLRRAAARHPDRPALV----FGGRRL--------------TYAELDARARRLAAALRALGVGPGDRVALLLPNSPEF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 572 YIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVygsglspiaeaelkpantqslcglqqleftsltdpvgepln 651
Cdd:COG0318 63 VVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALV----------------------------------------- 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 652 lvdvpeaktfpgigtalddTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVgastqdRAGDRILHKTPISFDV-H 730
Cdd:COG0318 102 -------------------TALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGL------TPGDVVLVALPLFHVFgL 156
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 731 VWELYWPLQEGAAVVIAApdgHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRTLAeagfgsgeqqRHVRYLICS 810
Cdd:COG0318 157 TVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDL----------SSLRLVVSG 223
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 811 GEALQKDQILSAHNIMGVYPLNLYGPTEAAVdVTFWDSSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSG 890
Cdd:COG0318 224 GAPLPPELLERFEERFGVRIVEGYGLTETSP-VVTVNPEDPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRG 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 891 AQLAAGYQNNPEATAQAFIldnatgERLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIE 970
Cdd:COG0318 303 PNVMKGYWNDPEATAEAFR------DGWLRTGDLGRL--------------DEDGYLYIVGRKKDMIISGGENVYPAEVE 362
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 971 TTLSHVEGVHSAVVLLytkTPEP----ALTAFLEIGDVSETErnriVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGK 1046
Cdd:COG0318 363 EVLAAHPGVAEAAVVG---VPDEkwgeRVVAFVVLRPGAELD----AEELRAFLRERLARYKVPRRVEFVDELPRTASGK 435
|
....*...
gi 503164607 1047 TDRKNLAQ 1054
Cdd:COG0318 436 IDRRALRE 443
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
532-1052 |
9.96e-80 |
|
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: 271.66 E-value: 9.96e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVy 611
Cdd:cd17656 12 QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVL- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 gsglsPIAEAELKPANTQSLcglQQLEFTSLTDPVGEPLNLVDvpeaktfpgigtALDDTAYILFTSGSTGRPKGVAISH 691
Cdd:cd17656 91 -----TQRHLKSKLSFNKST---ILLEDPSISQEDTSNIDYIN------------NSDDLLYIIYTSGTTGKPKGVQLEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 692 RSIDNRLRWQQSQipvgasTQDRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLh 771
Cdd:cd17656 151 KNMVNLLHFEREK------TNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 772 FVPTmltAFLEAPSAKRTLAEAGFgsgeqqRHVRYLICSGEALQKDQ----ILSAHNimgVYPLNLYGPTEAAVDVTFWD 847
Cdd:cd17656 224 FLPV---AFLKFIFSEREFINRFP------TCVKHIITAGEQLVITNefkeMLHEHN---VHLHNHYGPSETHVVTTYTI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 848 SSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDN-ATGERLYRTGDLAE 926
Cdd:cd17656 292 NPEAEIPELPPIGKPISNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPfDPNERMYRTGDLAR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 927 WnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTP-EPALTAFLeigdVS 1005
Cdd:cd17656 372 Y--------------LPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKgEKYLCAYF----VM 433
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 503164607 1006 ETERNriVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd17656 434 EQELN--ISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
522-1052 |
1.86e-77 |
|
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: 263.94 E-value: 1.86e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 522 PQSPQAYEFSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMM 601
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 602 EDAQCSALvygsglspiaeaelkpantqslcglqqleftsLTDPvgeplnlvdvpeaktfpgigtalDDTAYILFTSGST 681
Cdd:cd17650 81 EDSGAKLL--------------------------------LTQP-----------------------EDLAYVIYTSGTT 105
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 682 GRPKGVAISHRSIDN-RLRWQQSQipvgasTQDRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLAR 760
Cdd:cd17650 106 GKPKGVMVEHRNVAHaAHAWRREY------ELDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYD 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 761 VIAEQNVTCLHFVPTMLtafleapsakRTLAEAGFGSGEQQRHVRYLICSGEALQKD--QILSAHNIMGVYPLNLYGPTE 838
Cdd:cd17650 180 LILKSRITLMESTPALI----------RPVMAYVYRNGLDLSAMRLLIVGSDGCKAQdfKTLAARFGQGMRIINSYGVTE 249
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 839 AAVDVTFWDSSQNPEC--STVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFiLDN--AT 914
Cdd:cd17650 250 ATIDSTYYEEGRDPLGdsANVPIGRPLPNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERF-VENpfAP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 915 GERLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLL-YTKTPEP 993
Cdd:cd17650 329 GERMYRTGDLARW--------------RADGNVELLGRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAVrEDKGGEA 394
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 503164607 994 ALTAFLEIGDVSETernrivAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd17650 395 RLCAYVVAAATLNT------AELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
155-1135 |
8.71e-75 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 276.28 E-value: 8.71e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 155 HVVADGFAAFNGLSRVAAIYRALSAGKPLP-----------TVKRASLMEllradhAAEHAREedLALWTSEQVEvlSQP 223
Cdd:PRK05691 1862 HIVTEGWAMDIFARELGALYEAFLDDRESPleplpvqyldySVWQRQWLE------SGERQRQ--LDYWKAQLGN--EHP 1931
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 224 DTSLAARSASPAPQALREVL---TLPDKLQRDMLEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRIfgaqv 300
Cdd:PRK05691 1932 LLELPADRPRPPVQSHRGELyrfDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRI----- 2006
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 301 PAETRALGKTSAQTgttavNVLPVQVSGMGSIAQALDSVKNQYARNASHPLARQEDLERLAQSNDSR----LFGAQINVI 376
Cdd:PRK05691 2007 RPESEGLIGAFLNT-----QVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAaynpLFQVMCNVQ 2081
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 377 PFDaalpLGAPTENAPASVGYIHNISAGPVADMTITLRGIPGRghtISVELDANPNLYTREHVEFHARHLQNWLEswaqa 456
Cdd:PRK05691 2082 RWE----FQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDGR---LGCCLTYSRDLFDEPRIARMAEHWQNLLE----- 2149
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 457 ALEERSMDTLTtalphEVELLESFNAtahpieyktllQRFQDALTRYPNEPALYACAPD---EDGTLSPQSPQAYEFSQV 533
Cdd:PRK05691 2150 ALLGDPQQRLA-----ELPLLAAAEQ-----------QQLLDSLAGEAGEARLDQTLHGlfaAQAARTPQAPALTFAGQT 2213
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGS 613
Cdd:PRK05691 2214 LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDR 2293
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 GLSPiAEAELkPANTQSLCglqqLE--FTSLTDPVGEPLNLVDVPEAKtfpgigtalddtAYILFTSGSTGRPKGVAISH 691
Cdd:PRK05691 2294 ALFE-ALGEL-PAGVARWC----LEddAAALAAYSDAPLPFLSLPQHQ------------AYLIYTSGSTGKPKGVVVSH 2355
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 692 RSIDNRLRwqqsqiPVGASTQDRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIAApDGHRDPAYLARVIAEQNVTCLH 771
Cdd:PRK05691 2356 GEIAMHCQ------AVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRA-QGQWGAEEICQLIREQQVSILG 2428
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 772 FvptmltafleAPSAKRTLAEAGFGSGeQQRHVRYLICSGEALQKDQIlsaHNIMGVYP----LNLYGPTEAAVDVTfwd 847
Cdd:PRK05691 2429 F----------TPSYGSQLAQWLAGQG-EQLPVRMCITGGEALTGEHL---QRIRQAFApqlfFNAYGPTETVVMPL--- 2491
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 848 SSQNPE-----CSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILD--NATGERLYR 920
Cdd:PRK05691 2492 ACLAPEqleegAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADpfAADGGRLYR 2571
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 921 TGDLAEwnltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTPEPALTAFL- 999
Cdd:PRK05691 2572 TGDLVR--------------LRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLv 2637
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1000 -EIGDVSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIEFTFDTNTADGPHGLLEQQISEI 1078
Cdd:PRK05691 2638 sAVAGQDDEAQAALREALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELEQQLAQI 2717
|
970 980 990 1000 1010
....*....|....*....|....*....|....*....|....*....|....*..
gi 503164607 1079 IAGVLGRSQFGVTEDFLAAGGNSLAALSVIAKIEEnLGKMLSIGALFANPTVKGIAA 1135
Cdd:PRK05691 2718 WREVLNVERVGLGDNFFELGGDSILSIQVVSRARQ-LGIHFSPRDLFQHQTVQTLAA 2773
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
522-1135 |
2.19e-73 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 271.66 E-value: 2.19e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 522 PQSPQAYEFSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMM 601
Cdd:PRK05691 3734 PQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRII 3813
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 602 EDAQCSALVygsglspiaeaelkpanTQSLCGLQQLEFTSLTDPVGEPLNLV-------DVPEAKtfPGIGTALDDTAYI 674
Cdd:PRK05691 3814 ELSRTPVLV-----------------CSAACREQARALLDELGCANRPRLLVweevqagEVASHN--PGIYSGPDNLAYV 3874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 675 LFTSGSTGRPKGVAISHRSIDNRlrwQQSQIPVGASTQdraGDRILHKTPISFDVHVWE-LYWPLQeGAAVVIAAPDGHR 753
Cdd:PRK05691 3875 IYTSGSTGLPKGVMVEQRGMLNN---QLSKVPYLALSE---ADVIAQTASQSFDISVWQfLAAPLF-GARVEIVPNAIAH 3947
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 754 DPAYLARVIAEQNVTCLHFVPTMLTAFLEAPsakrtlaEAGFGSgeqqrhVRYLICSGEALQKDQilsAHNIMGVYP--- 830
Cdd:PRK05691 3948 DPQGLLAHVQAQGITVLESVPSLIQGMLAED-------RQALDG------LRWMLPTGEAMPPEL---ARQWLQRYPqig 4011
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 831 -LNLYGPTEAAVDVTFWD-SSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAF 908
Cdd:PRK05691 4012 lVNAYGPAECSDDVAFFRvDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAF 4091
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 909 ILD--NATGERLYRTGDLAEwnltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLL 986
Cdd:PRK05691 4092 VPHpfGAPGERLYRTGDLAR--------------RRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAV 4157
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 987 YTKTPEPALTAFLEIGDvSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIEFTFDTNTA-D 1065
Cdd:PRK05691 4158 QEGVNGKHLVGYLVPHQ-TVLAQGALLERIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAyL 4236
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1066 GPHGLLEQQISEIIAGVLGRSQFGVTEDFLAAGGNSLAALSVIAKIEENLGKMLSIGALFANPTVKGIAA 1135
Cdd:PRK05691 4237 APRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAE 4306
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
494-1052 |
1.26e-70 |
|
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: 244.00 E-value: 1.26e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 494 QRFQDALTRYPNEPALYacapDEDgtlspqspqayefsQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYI 573
Cdd:cd17645 2 QLFEEQVERTPDHVAVV----DRG--------------QSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIA 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 574 ALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALvygsglspiaeaelkpantqslcglqqleftsLTDPvgeplnlv 653
Cdd:cd17645 64 AILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKIL--------------------------------LTNP-------- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 654 dvpeaktfpgigtalDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGAStqdragDRILHKTPISFDVHVWE 733
Cdd:cd17645 104 ---------------DDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPA------DKSLVYASFSFDASAWE 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 734 LYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTcLHFVPTmltafleapsakrTLAEAgFGSGEQQRhVRYLICSGEA 813
Cdd:cd17645 163 IFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT-ISFLPT-------------GAAEQ-FMQLDNQS-LRVLLTGGDK 226
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 814 LQKDQILSahnimgvYPL-NLYGPTEAAVDVTFWDSsqNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQ 892
Cdd:cd17645 227 LKKIERKG-------YKLvNNYGPTENTVVATSFEI--DKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEG 297
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 893 LAAGYQNNPEATAQAFILD-NATGERLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIET 971
Cdd:cd17645 298 LARGYLNRPELTAEKFIVHpFVPGERMYRTGDLAKF--------------LPDGNIEFLGRLDQQVKIRGYRIEPGEIEP 363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 972 TLSHVEGVHSAVVL-LYTKTPEPALTAFLEIGDVSETErnrivaQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRK 1050
Cdd:cd17645 364 FLMNHPLIELAAVLaKEDADGRKYLVAYVTAPEEIPHE------ELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRK 437
|
..
gi 503164607 1051 NL 1052
Cdd:cd17645 438 AL 439
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
534-1052 |
4.80e-64 |
|
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: 225.36 E-value: 4.80e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAG-VCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVyg 612
Cdd:cd17648 13 LTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 613 sglspiaeaelkpantqslcglqqleftslTDPvgeplnlvdvpeaktfpgigtalDDTAYILFTSGSTGRPKGVAISHR 692
Cdd:cd17648 91 ------------------------------TNS-----------------------TDLAYAIYTSGTTGKPKGVLVEHG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 693 SIDNrLRWQQSQIPVGASTQDRAgdrILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLHF 772
Cdd:cd17648 118 SVVN-LRTSLSERYFGRDNGDEA---VLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSG 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 773 VPTMLTAFleapsakrtlaeaGFGSgeqQRHVRYLICSGEALQKDQIlsaHNIMGVYP---LNLYGPTEAAVD--VTFWD 847
Cdd:cd17648 194 TPSVLQQY-------------DLAR---LPHLKRVDAAGEEFTAPVF---EKLRSRFAgliINAYGPTETTVTnhKRFFP 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 848 SSQNPECStvpIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFIL-------DNATGE--RL 918
Cdd:cd17648 255 GDQRFDKS---LGRPVRNTKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPnpfqteqERARGRnaRL 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 919 YRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVL---LYTKTPEP-- 993
Cdd:cd17648 332 YKTGDLVRW--------------LPSGELEYLGRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVakeDASQAQSRiq 397
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503164607 994 -ALTAF--LEIGDVSETErnrivaqARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd17648 398 kYLVGYylPEPGHVPESD-------LLSFLRAKLPRYMVPARLVRLEGIPVTINGKLDVRAL 452
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
515-1054 |
5.26e-63 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 224.00 E-value: 5.26e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 515 DEDGTLSPQSPqAYEF-SQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLP 593
Cdd:PRK04813 9 EEFAQTQPDFP-AYDYlGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 594 AERVSSMMEDAQCSALvygsglspIAEAELkpantqslcglqqlEFTSLTDPVGEPLNLVDVPEAKTFPGIGTAL--DDT 671
Cdd:PRK04813 88 AERIEMIIEVAKPSLI--------IATEEL--------------PLEILGIPVITLDELKDIFATGNPYDFDHAVkgDDN 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 672 AYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGAstqdraGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDG 751
Cdd:PRK04813 146 YYIIFTSGTTGKPKGVQISHDNLVSFTNWMLEDFALPE------GPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDM 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 752 HRDPAYLARVIAEQNVTClhFVPTmltafleaPS-AKRTLAEAGFgSGEQQRHVRYLICSGEALQKDqilSAHNIMGVYP 830
Cdd:PRK04813 220 TANFKQLFETLPQLPINV--WVST--------PSfADMCLLDPSF-NEEHLPNLTHFLFCGEELPHK---TAKKLLERFP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 831 ----LNLYGPTEAAVDVTFWDSSQN--PECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEAT 904
Cdd:PRK04813 286 satiYNTYGPTEATVAVTSIEITDEmlDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKT 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 905 AQAFILDNatGERLYRTGDLaewnltatnqepGTLAKnprGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVV 984
Cdd:PRK04813 366 AEAFFTFD--GQPAYHTGDA------------GYLED---GLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVV 428
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503164607 985 LLYTKT-PEPALTAFLEIGDVSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQ 1054
Cdd:PRK04813 429 VPYNKDhKVQYLIAYVVPKEEDFEREFELTKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIE 499
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
670-1048 |
1.97e-57 |
|
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: 202.52 E-value: 1.97e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 670 DTAYILFTSGSTGRPKGVAISHRSIDnrlrwqQSQIPVGASTQDRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAP 749
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLL------AAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 750 DghrDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRTlaeagfgsgeQQRHVRYLICSGEALQKDQILSAHNIMGVY 829
Cdd:cd04433 75 F---DPEAALELIEREKVTILLGVPTLLARLLKAPESAGY----------DLSSLRALVSGGAPLPPELLERFEEAPGIK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 830 PLNLYGPTEAAVDVTFWDSSqNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFi 909
Cdd:cd04433 142 LVNGYGLTETGGTVATGPPD-DDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 910 ldnatGERLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGV-HSAVVLLYT 988
Cdd:cd04433 220 -----EDGWYRTGDLGRL--------------DEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVaEAAVVGVPD 280
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 989 KTPEPALTAFLeigdVSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTD 1048
Cdd:cd04433 281 PEWGERVVAVV----VLRPGADLDAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
15-451 |
2.36e-54 |
|
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. While standard C-domains catalyze peptide bond formation between two amino acids, an initial, ('starter') C-domain may instead acylate an amino acid with a fatty acid. 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: 380456 [Multi-domain] Cd Length: 419 Bit Score: 196.05 E-value: 2.36e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 15 PLTKSAQGIYLAAIIDPKNPCYNTAEIMECPPETNLDYLREAFIQLYRENEGFRVQTRVQTGRPEQRVIPLDEFLtnlev 94
Cdd:cd19533 3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVP----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 95 LPVISLqiqeeTEEQNPVpAAVRGWASELISEPLRTDAGVTVRSAV-TYYGGKLWVYHSFSHVVADGFAAFNGLSRVAAI 173
Cdd:cd19533 78 IRHIDL-----SGDPDPE-GAAQQWMQEDLRKPLPLDNDPLFRHALfTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 174 YRALSAGKPLPTVKRASLMELLRAD--HAAEHAREEDLALWTsEQVEVLSQPdTSLAARSASPAPQALREVLTLPDKLQR 251
Cdd:cd19533 152 YTALLKGRPAPPAPFGSFLDLVEEEqaYRQSERFERDRAFWT-EQFEDLPEP-VSLARRAPGRSLAFLRRTAELPPELTR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 252 DMLEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRifgaqvpaetraLGKTSAQTGTTAVNVLPVQ--VSGM 329
Cdd:cd19533 230 TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGR------------LGAAARQTPGMVANTLPLRltVDPQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 330 GSIAQALDSVKNQYARNASHPLARQEDLER---LAQSNDsRLFGAQINVIPFDAALPLGAPtenapasVGYIHNISAGPV 406
Cdd:cd19533 298 QTFAELVAQVSRELRSLLRHQRYRYEDLRRdlgLTGELH-PLFGPTVNYMPFDYGLDFGGV-------VGLTHNLSSGPT 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 503164607 407 ADMTITLRGIPGRGhTISVELDANPNLYTREHVEFHARHLQNWLE 451
Cdd:cd19533 370 NDLSIFVYDRDDES-GLRIDFDANPALYSGEDLARHQERLLRLLE 413
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
489-1052 |
2.20e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 178.46 E-value: 2.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 489 YKTLLQRFQDALTRYPNEPALYAcapDEDGTlspqspqayefsqvlTYHELDARARALAKAMLEAGVCPGTAVGLRFHRG 568
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYF---DGRRT---------------TYAELDERVNRLANALRALGVKKGDRVAVFDWNS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 569 LEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIAEAeLKPAntqslcgLQQLEFTSLTDPVGE 648
Cdd:PRK06187 67 HEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAA-ILPQ-------LPTVRTVIVEGDGPA 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 649 PLNLVDVPE--------AKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSIdnrlrWQQSQIpVGASTQDRAGDRIL 720
Cdd:PRK06187 139 APLAPEVGEyeellaaaSDTFDFPDIDENDAAAMLYTSGTTGHPKGVVLSHRNL-----FLHSLA-VCAWLKLSRDDVYL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 721 HKTPIsFDVHVWEL-YWPLQEGAAVVIAapdGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKrtlaEAGFGSge 799
Cdd:PRK06187 213 VIVPM-FHVHAWGLpYLALMAGAKQVIP---RRFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAY----FVDFSS-- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 800 qqrhVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTF-WDSSQNPECSTVPI--GQPVWNTQTRILDQALQ 876
Cdd:PRK06187 283 ----LRLVIYGGAALPPALLREFKEKFGIDLVQGYGMTETSPVVSVlPPEDQLPGQWTKRRsaGRPLPGVEARIVDDDGD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 877 PIPP--GFVGELYLSGAQLAAGYQNNPEATAQAFILDnatgerLYRTGDLaewnltatnqepGTLakNPRGVILYRGRTD 954
Cdd:PRK06187 359 ELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETIDGG------WLHTGDV------------GYI--DEDGYLYITDRIK 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 955 HQVKLHGQRLELGDIETTLSHVEGVHSAVVLlytKTPEP----ALTAFLEIGDVSETERNRIvaqaRQHCENTLPDYMVP 1030
Cdd:PRK06187 419 DVIISGGENIYPRELEDALYGHPAVAEVAVI---GVPDEkwgeRPVAVVVLKPGATLDAKEL----RAFLRGRLAKFKLP 491
|
570 580
....*....|....*....|..
gi 503164607 1031 RLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:PRK06187 492 KRIAFVDELPRTSVGKILKRVL 513
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
492-1052 |
8.65e-47 |
|
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: 175.44 E-value: 8.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 492 LLQRFQDALTRYPNEPALYacapdedgtlspqspqayEFSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQ 571
Cdd:cd05936 1 LADLLEEAARRFPDKTALI------------------FMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQF 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 572 YIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVygsglspiaeaelkpantqslcglqqleftsltdpVGEPLN 651
Cdd:cd05936 63 PIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALI-----------------------------------VAVSFT 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 652 LVDVPEAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLrwQQSQIPVGASTqdRAGDRILHKTPISfdvHV 731
Cdd:cd05936 108 DLLAAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLVANA--LQIKAWLEDLL--EGDDVVLAALPLF---HV 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 732 W----ELYWPLQEGAAVVIAapdgHR-DPAYLARVIAEQNVTCLHFVPTMLTAFLEAPsakrTLAEAGFGSgeqqrhVRY 806
Cdd:cd05936 181 FgltvALLLPLALGATIVLI----PRfRPIGVLKEIRKHRVTIFPGVPTMYIALLNAP----EFKKRDFSS------LRL 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 807 LICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTFwdssqNP-ECSTVP--IGQPVWNTQTRILDQALQPIPPGFV 883
Cdd:cd05936 247 CISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAV-----NPlDGPRKPgsIGIPLPGTEVKIVDDDGEELPPGEV 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 884 GELYLSGAQLAAGYQNNPEATAQAFildnaTGERLyRTGDLaewnltATNQEPGTL-----AKNprgVILyRGrtdhqvk 958
Cdd:cd05936 322 GELWVRGPQVMKGYWNRPEETAEAF-----VDGWL-RTGDI------GYMDEDGYFfivdrKKD---MII-VG------- 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 959 lhGQRLELGDIETTLSHVEGVHSAVVLlytKTPEP----ALTAFL---EIGDVSETErnrIVAQARQHcentLPDYMVPR 1031
Cdd:cd05936 379 --GFNVYPREVEEVLYEHPAVAEAAVV---GVPDPysgeAVKAFVvlkEGASLTEEE---IIAFCREQ----LAGYKVPR 446
|
570 580
....*....|....*....|.
gi 503164607 1032 LWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd05936 447 QVEFRDELPKSAVGKILRREL 467
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
498-1056 |
2.62e-45 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 173.37 E-value: 2.62e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 498 DALTRY----PNEPALYACapDEDGTlspqspqayefSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYI 573
Cdd:COG0365 13 NCLDRHaegrGDKVALIWE--GEDGE-----------ERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 574 ALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALV-YGSGLSPIAEAELKPANTQSLCGLQQLEFTSLTDPVGEPLNL 652
Cdd:COG0365 80 AMLACARIGAVHSPVFPGFGAEALADRIEDAEAKVLItADGGLRGGKVIDLKEKVDEALEELPSLEHVIVVGRTGADVPM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 653 V-DVP-------EAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSidnrlrwqqsqIPVGAST-----QD-RAGDR 718
Cdd:COG0365 160 EgDLDwdellaaASAEFEPEPTDADDPLFILYTSGTTGKPKGVVHTHGG-----------YLVHAATtakyvLDlKPGDV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 719 ILHKTPISFDVHVW-ELYWPLQEGAAVVI--AAPDgHRDPAYLARVIAEQNVTCLHFVPTMLTAFL---EAPSAKRTLae 792
Cdd:COG0365 229 FWCTADIGWATGHSyIVYGPLLNGATVVLyeGRPD-FPDPGRLWELIEKYGVTVFFTAPTAIRALMkagDEPLKKYDL-- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 793 agfgsgeqqRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTfwdsSQNPECSTVP--IGQPVWNTQTRI 870
Cdd:COG0365 306 ---------SSLRLLGSAGEPLNPEVWEWWYEAVGVPIVDGWGQTETGGIFI----SNLPGLPVKPgsMGKPVPGYDVAV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 871 LDQALQPIPPGFVGELYLSGAQ--LAAGYQNNPEATAQAFiLDNATGerLYRTGDLAEwnltatnqepgtlaKNPRGVIL 948
Cdd:COG0365 373 VDEDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETY-FGRFPG--WYRTGDGAR--------------RDEDGYFW 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 949 YRGRTDHQVKLHGQRLELGDIETTLSHVEGVH-SAVVllytktPEP------ALTAF--LEIGdvsETERNRIVAQARQH 1019
Cdd:COG0365 436 ILGRSDDVINVSGHRIGTAEIESALVSHPAVAeAAVV------GVPdeirgqVVKAFvvLKPG---VEPSDELAKELQAH 506
|
570 580 590
....*....|....*....|....*....|....*..
gi 503164607 1020 CENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIE 1056
Cdd:COG0365 507 VREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIA 543
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
514-1054 |
7.51e-41 |
|
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: 158.63 E-value: 7.51e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 514 PDEDGTLSPQSPQAyefsqvLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLP 593
Cdd:cd05926 1 PDAPALVVPGSTPA------LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 594 AERVSSMMEDAQCSALVYGSG-LSPIAEAELKP----ANTQSLCGLQQLEFTSLTDPVGEPLNLVDVPEAKTFPgigtal 668
Cdd:cd05926 75 KAEFEFYLADLGSKLVLTPKGeLGPASRAASKLglaiLELALDVGVLIRAPSAESLSNLLADKKNAKSEGVPLP------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAISHRSIDNRLRwqqsqiPVGASTQDRAGDRILHKTPIsFDVH--VWELYWPLQEGAAVVI 746
Cdd:cd05926 149 DDLALILHTSGTTGRPKGVPLTHRNLAASAT------NITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSVVL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 747 AapdghrdPAYLARV----IAEQNVTCLHFVPTMLTAFLEAPSAKRTLAEAgfgsgeqqrHVRYLICSGEALQKDQILSA 822
Cdd:cd05926 222 P-------PRFSASTfwpdVRDYNATWYTAVPTIHQILLNRPEPNPESPPP---------KLRFIRSCSASLPPAVLEAL 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 823 HNIMGVYPLNLYGPTEAAVDVTfwdssQNPECSTVP----IGQPVwNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQ 898
Cdd:cd05926 286 EATFGAPVLEAYGMTEAAHQMT-----SNPLPPGPRkpgsVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYL 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 899 NNPEATAqafilDNATGERLYRTGDLaewnltatnqepGTLakNPRGVILYRGRTDHQVKLHGQR---LELGDIETTLSH 975
Cdd:cd05926 360 NNPEANA-----EAAFKDGWFRTGDL------------GYL--DADGYLFLTGRIKELINRGGEKispLEVDGVLLSHPA 420
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 976 V--------------EGVHSAVVLlytkTPEPALTAfleigdvseternrivAQARQHCENTLPDYMVPRLWHTTAQFPV 1041
Cdd:cd05926 421 VleavafgvpdekygEEVAAAVVL----REGASVTE----------------EELRAFCRKHLAAFKVPKKVYFVDELPK 480
|
570
....*....|...
gi 503164607 1042 SPSGKTDRKNLAQ 1054
Cdd:cd05926 481 TATGKIQRRKVAE 493
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
531-925 |
3.40e-40 |
|
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: 156.22 E-value: 3.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 531 SQVLTYHELDARARALAKAMLEAGVCPGTAVGLrFHRGLEQYIAL-YAALYAGFVYVPILPDLPAERVSSMMEDAQCSAL 609
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGI-ISPNSTYYPPVfLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 610 -VYGSGLSPIAEAelkpanTQSLCGLQQLE-FTSLTDPVGEPLNLVDVP---EAKTFPGI-GTALDDTAYILFTSGSTGR 683
Cdd:cd05911 87 fTDPDGLEKVKEA------AKELGPKDKIIvLDDKPDGVLSIEDLLSPTlgeEDEDLPPPlKDGKDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 684 PKGVAISHRSIDNRLRWQQSQIPvgasTQDRAGDRILhkTPISFDvHV---WELYWPLQEGAAVVIaapdgHR--DPAYL 758
Cdd:cd05911 161 PKGVCLSHRNLIANLSQVQTFLY----GNDGSNDVIL--GFLPLY-HIyglFTTLASLLNGATVII-----MPkfDSELF 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 759 ARVIAEQNVTCLHFVPTMLTAFLEAPSAKRtlaeagfgsgEQQRHVRYLICSGEALQKD-QILSAHNIMGVYPLNLYGPT 837
Cdd:cd05911 229 LDLIEKYKITFLYLVPPIAAALAKSPLLDK----------YDLSSLRVILSGGAPLSKElQELLAKRFPNATIKQGYGMT 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 838 EAAVDVTfwdssQNPECSTVP--IGQPVWNTQTRILDQALQPI-PPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNat 914
Cdd:cd05911 299 ETGGILT-----VNPDGDDKPgsVGRLLPNVEAKIVDDDGKDSlGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDG-- 371
|
410
....*....|.
gi 503164607 915 gerLYRTGDLA 925
Cdd:cd05911 372 ---WLHTGDIG 379
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
534-1052 |
3.04e-39 |
|
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: 152.63 E-value: 3.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYgS 613
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQ-N 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 GLSPIAEAELKPANTQslcglqqleFTSLTDpvgEPLnlvdvpeaktfpgigtalddtAYILFTSGSTGRPKGVAISHRS 693
Cdd:cd17654 96 KELDNAPLSFTPEHRH---------FNIRTD---ECL---------------------AYVIHTSGTTGTPKIVAVPHKC 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IDNRLrwqqsqipVGASTQ-DRAGDRILHKTPI-SFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQN-VTCL 770
Cdd:cd17654 143 ILPNI--------QHFRSLfNITSEDILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKRHrITVL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 771 HFVPTMLTAFLEAPSAKRTLAeagfgsgeQQRHVRYLICSGEALQKDQILSA--HNIMGVYPLNLYGPTEaavdVTFWDS 848
Cdd:cd17654 215 QATPTLFRRFGSQSIKSTVLS--------ATSSLRVLALGGEPFPSLVILSSwrGKGNRTRIFNIYGITE----VSCWAL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 849 SQ--NPECSTVPIGQPVWNTQTRILDQAlqpippGFVGELYLSGAQLAAG-----YQNNPEATaqafildnatgerLYRT 921
Cdd:cd17654 283 AYkvPEEDSPVQLGSPLLGTVIEVRDQN------GSEGTGQVFLGGLNRVcilddEVTVPKGT-------------MRAT 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 922 GDLAEWNLtatnqepgtlaknprGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTpepALTAFLei 1001
Cdd:cd17654 344 GDFVTVKD---------------GELFFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQ---RLIAFI-- 403
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 503164607 1002 gdVSETERNRIVAQARQHCENT--LPDYMVprlwhTTAQFPVSPSGKTDRKNL 1052
Cdd:cd17654 404 --VGESSSSRIHKELQLTLLSShaIPDTFV-----QIDKLPLTSHGKVDKSEL 449
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
496-1136 |
1.51e-38 |
|
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: 157.92 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 496 FQDALTRYPNEPalyaCAPDEDGTLSPQSPqayefSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIAL 575
Cdd:TIGR03443 242 FADNAEKHPDRT----CVVETPSFLDPSSK-----TRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAV 312
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 576 YAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVY----GSgLSPIAE-------------AELKPANTQSLCG--LQQ 636
Cdd:TIGR03443 313 MGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIViekaGT-LDQLVRdyidkelelrteiPALALQDDGSLVGgsLEG 391
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 637 LEFTSLTDPV---GEPLNLVDVPeaktfpgigtalDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIpvGASTQD 713
Cdd:TIGR03443 392 GETDVLAPYQalkDTPTGVVVGP------------DSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRF--GLSEND 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 714 R----AGdrILHKtPISFDvhvweLYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLHFVPTM---LTAflEAPSA 786
Cdd:TIGR03443 458 KftmlSG--IAHD-PIQRD-----MFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMgqlLSA--QATTP 527
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 787 KRTLAEAGFgsgeqqrhvrylicSGEALQKDQILS----AHNimgVYPLNLYGPTEAAVDVTFWDSSQNPECST------ 856
Cdd:TIGR03443 528 IPSLHHAFF--------------VGDILTKRDCLRlqtlAEN---VCIVNMYGTTETQRAVSYFEIPSRSSDSTflknlk 590
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 857 --VPIGQPVWNTQTRILDQ--ALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFI------------LDNATGE---- 916
Cdd:TIGR03443 591 dvMPAGKGMKNVQLLVVNRndRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVnnwfvdpshwidLDKENNKpere 670
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 917 -------RLYRTGDLAEWNltatnqepgtlaknPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLY-T 988
Cdd:TIGR03443 671 fwlgprdRLYRTGDLGRYL--------------PDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRrD 736
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 989 KTPEPALTAF---------LE--IGDVSETERNRIVAQ-----------ARQHCENTLPDYMVPRLWHTTAQFPVSPSGK 1046
Cdd:TIGR03443 737 KDEEPTLVSYivpqdksdeLEefKSEVDDEESSDPVVKglikyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGK 816
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1047 TDR--------KNLAQIEFTFDTNTADGPHGLLEQQISEIIAGVLGRSQFGVTED--FLAAGGNSLAALSVIAKIEENLG 1116
Cdd:TIGR03443 817 VDKpalpfpdtAQLAAVAKNRSASAADEEFTETEREIRDLWLELLPNRPATISPDdsFFDLGGHSILATRMIFELRKKLN 896
|
730 740
....*....|....*....|
gi 503164607 1117 KMLSIGALFANPTVKGIAAA 1136
Cdd:TIGR03443 897 VELPLGLIFKSPTIKGFAKE 916
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
499-925 |
1.27e-37 |
|
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: 147.76 E-value: 1.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 499 ALTRYPNEPALyacapDEDGTlspqspqayefsqVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAA 578
Cdd:cd17631 4 RARRHPDRTAL-----VFGGR-------------SLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAA 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 579 LYAGFVYVPILPDLPAERVSSMMEDAqcsalvygsglspiaeaelkpantqslcglqqleftsltdpvgeplnlvdvpEA 658
Cdd:cd17631 66 ARLGAVFVPLNFRLTPPEVAYILADS----------------------------------------------------GA 93
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 659 KTFpgigtaLDDTAYILFTSGSTGRPKGVAISHRSidnrLRWQQsqIPVGASTQDRAGDRILHKTPISfdvHVWEL--YW 736
Cdd:cd17631 94 KVL------FDDLALLMYTSGTTGRPKGAMLTHRN----LLWNA--VNALAALDLGPDDVLLVVAPLF---HIGGLgvFT 158
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 737 P--LQEGAAVVIAApdgHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRTlaeaGFGSgeqqrhVRYLICSGEAL 814
Cdd:cd17631 159 LptLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATT----DLSS------LRAVIYGGAPM 225
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 815 QkDQILSAHNIMGVYPLNLYGPTEAAVDVTFWDSSQNPEcSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLA 894
Cdd:cd17631 226 P-ERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRR-KLGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVM 303
|
410 420 430
....*....|....*....|....*....|.
gi 503164607 895 AGYQNNPEATAQAFildnatGERLYRTGDLA 925
Cdd:cd17631 304 AGYWNRPEATAAAF------RDGWFHTGDLG 328
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
534-1049 |
1.11e-36 |
|
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: 146.36 E-value: 1.11e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGS 613
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 GLSPIAEAELKPANTQslcgLQQLEFTSLTDPVGEPLNLVDVP--EAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISH 691
Cdd:cd05959 110 ELAPVLAAALTKSEHT----LVVLIVSGGAGPEAGALLLAELVaaEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 692 RSIdnrlRWQQSQI--PVGASTQDragDRILHKTPISFDVHVWE-LYWPLQEGAAVVIAApdGHRDPAYLARVIAEQNVT 768
Cdd:cd05959 186 ADI----YWTAELYarNVLGIRED---DVCFSAAKLFFAYGLGNsLTFPLSVGATTVLMP--ERPTPAAVFKRIRRYRPT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 769 CLHFVPTMLTAFLEAPSAKRTlaeaGFGSgeqqrhVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAA-VDVTFWD 847
Cdd:cd05959 257 VFFGVPTLYAAMLAAPNLPSR----DLSS------LRLCVSAGEALPAEVGERWKARFGLDILDGIGSTEMLhIFLSNRP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 848 SSQNPECStvpiGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFIldnatGErLYRTGDlaew 927
Cdd:cd05959 327 GRVRYGTT----GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ-----GE-WTRTGD---- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 928 nltatnqepgTLAKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGV-HSAVVLLYTKTPEPALTAFL------E 1000
Cdd:cd05959 393 ----------KYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVlEAAVVGVEDEDGLTKPKAFVvlrpgyE 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 503164607 1001 IGDVSETErnrivaqARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDR 1049
Cdd:cd05959 463 DSEALEEE-------LKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQR 504
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
527-926 |
4.66e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 144.66 E-value: 4.66e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 527 AYEF-SQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQ 605
Cdd:PRK07656 23 AYVFgDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 606 CSALvygsglspIAEAELKPANTQSLCGLQQLE-FTSLTDPVGEPLNLVDV-------PEAKTFPGIGTALDDTAYILFT 677
Cdd:PRK07656 103 AKAL--------FVLGLFLGVDYSATTRLPALEhVVICETEEDDPHTEKMKtftdflaAGDPAERAPEVDPDDVADILFT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 678 SGSTGRPKGVAISHRsidNRLRWQQSqipVGASTQDRAGDRILHKTPIsFDVHVWELYW--PLQEGAAVVIAApdgHRDP 755
Cdd:PRK07656 175 SGTTGRPKGAMLTHR---QLLSNAAD---WAEYLGLTEGDRYLAANPF-FHVFGYKAGVnaPLMRGATILPLP---VFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 756 AYLARVIAEQNVTCLHFVPTMLTAFLEAPsakrTLAEAGFGSgeqqrhVRyLICSGEA-------------LQKDQILSA 822
Cdd:PRK07656 245 DEVFRLIETERITVLPGPPTMYNSLLQHP----DRSAEDLSS------LR-LAVTGAAsmpvallerfeseLGVDIVLTG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 823 hnimgvyplnlYGPTEAAVDVTFwdssqNP---ECSTVP--IGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGY 897
Cdd:PRK07656 314 -----------YGLSEASGVTTF-----NRlddDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGY 377
|
410 420
....*....|....*....|....*....
gi 503164607 898 QNNPEATAQAFILDNAtgerLYrTGDLAE 926
Cdd:PRK07656 378 YDDPEATAAAIDADGW----LH-TGDLGR 401
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
533-987 |
9.50e-34 |
|
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: 135.97 E-value: 9.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 533 VLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYG 612
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 613 SglspiaeaelkpantqslcglqqlEFTSlTDPVGEPlnlvdvpeaktfpgigtalDDTAYILFTSGSTGRPKGVAISHR 692
Cdd:cd05903 81 E------------------------RFRQ-FDPAAMP-------------------DAVALLLFTSGTTGEPKGVMHSHN 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 693 SIDNRLRWQQSQIPVGastqdrAGDRILHKTPIS-FDVHVWELYWPLQEGAAVVIaapDGHRDPAYLARVIAEQNVTCLH 771
Cdd:cd05903 117 TLSASIRQYAERLGLG------PGDVFLVASPMAhQTGFVYGFTLPLLLGAPVVL---QDIWDPDKALALMREHGVTFMM 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 772 FVPTMLTAFLEAPSAkrtlaeagfgSGEQQRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTFWDSSQn 851
Cdd:cd05903 188 GATPFLTDLLNAVEE----------AGEPLSRLRTFVCGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAP- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 852 PECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFildnatGERLYRTGDLAEWnlta 931
Cdd:cd05903 257 EDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAA------PEGWFRTGDLARL---- 326
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 503164607 932 tnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLY 987
Cdd:cd05903 327 ----------DEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGVIEAAVVAL 372
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
537-1407 |
6.08e-33 |
|
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: 138.68 E-value: 6.08e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 537 HELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLS 616
Cdd:COG3319 4 AAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 617 PIAEAELKPANTQSLCGLQQLEFTSLTDPVGEPLNLVD----VPEAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHR 692
Cdd:COG3319 84 LALALAAAAAALLLAALALLLALLAALALALLALLLAAlllaLAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 693 SIDNRLRWQQSQIPVGASTQDRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCLHF 772
Cdd:COG3319 164 LVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 773 VPTMLTAFLEAPSAKRTLAEAGFGSGEQQRHVRYLICSGEALQkdqilsahnimgVYPLNLYGPTEAAVDVTFWDSSQNP 852
Cdd:COG3319 244 LAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAA------------AALAAGGTATTAAVTTTAAAAAPGV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 853 ECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNATGERLYRTGDLAewnltat 932
Cdd:COG3319 312 AGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGG------- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 933 nqepGTLAKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLytktPEPALTAFLEIGDVSETERNRI 1012
Cdd:COG3319 385 ----DRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAA----AAAAAAAAALAAAVVAAAALAA 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1013 VAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIEFTFDTNTADgPHGLLEQQISEIIAGVLGRSQFGVTE 1092
Cdd:COG3319 457 AALLLLLLLLLLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPA-PAAALELALALLLLLLLGLGLVGDDD 535
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1093 DFLAAGGNSLAALSVIAKIEENLGKMLSIGALFANPTVKGIAAALNEDSPDIEFAPVLPLREADSTdsatskntVPLFIL 1172
Cdd:COG3319 536 DFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGGSG--------PPLFCV 607
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1173 PPAGGLGWCYAAYLPHIPGHPSVYALQHEAFTNPNAGYAqSLRELAEGYLARIREtleeRQLPSQFSLMGWSVGGTAAVE 1252
Cdd:COG3319 608 HPAGGNVLCYRPLARALGPDRPVYGLQAPGLDGGEPPPA-SVEEMAARYVEAIRA----VQPEGPYHLLGWSFGGLVAYE 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1253 VAALAETAGYDVQQVTLLDAYPVEQWQGIPEPDEQESFRALLRMGGLPEVSAQTVLDLP------QTLERLRDAGsAMGY 1326
Cdd:COG3319 683 MARQLEAQGEEVALLVLLDSYAPGALARLDEAELLAALLRDLARGVDLPLDAEELRALDpeerlaRLLERLREAG-LPAG 761
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1327 LPEDKLEVCLESMRASAALMRGSNHLNFGGKVVLI--GVSHDDQPYLDAHGWELHVGSFRTVTLKNGTHPDLVNPERIPE 1404
Cdd:COG3319 762 LDAERLRRLLRVFRANLRALRRYRPRPYDGPVLLFraEEDPPGRADDPALGWRPLVAGGLEVHDVPGDHFSMLREPHVAE 841
|
...
gi 503164607 1405 IIA 1407
Cdd:COG3319 842 LAA 844
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
528-1052 |
2.42e-32 |
|
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: 131.82 E-value: 2.42e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 528 YEFSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCS 607
Cdd:cd05919 5 YAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEAR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 608 ALVygsglspiaeaelkpantqslcglqqleftsltdpvgeplnlvdvpeaktfpgigTALDDTAYILFTSGSTGRPKGV 687
Cdd:cd05919 85 LVV-------------------------------------------------------TSADDIAYLLYSSGTTGPPKGV 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 688 AISHRsiDNRLRWQQSQIPVGAStqdRAGDRILHKTPISFDVHVW-ELYWPLQEGAAVVIAapDGHRDPAYLARVIAEQN 766
Cdd:cd05919 110 MHAHR--DPLLFADAMAREALGL---TPGDRVFSSAKMFFGYGLGnSLWFPLAVGASAVLN--PGWPTAERVLATLARFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 767 VTCLHFVPTMLTAFLEAPSakrtlaeagfGSGEQQRHVRYLICSGEALQKD--QILSAHniMGVYPLNLYGPTEaaVDVT 844
Cdd:cd05919 183 PTVLYGVPTFYANLLDSCA----------GSPDALRSLRLCVSAGEALPRGlgERWMEH--FGGPILDGIGATE--VGHI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 845 FWdSSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFIldnatgERLYRTGDL 924
Cdd:cd05919 249 FL-SNRPGAWRLGSTGRPVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN------GGWYRTGDK 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 925 AEwnltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLlytKTPEPA----LTAFLE 1000
Cdd:cd05919 322 FC--------------RDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAAVV---AVPESTglsrLTAFVV 384
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 503164607 1001 IGDvsETERNRIVAQA-RQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd05919 385 LKS--PAAPQESLARDiHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
481-927 |
4.80e-32 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 133.69 E-value: 4.80e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 481 NATAHPIEYKTLLQRFQDALTRYPNEPALYAcaPDEDGtlspqspqayefSQVLTYHELDARARALAKAMLEAGVCPGTA 560
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALRE--KEDGI------------WQSLTWAEFAERVRALAAGLLALGVKPGDR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 561 VGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSG-----LSPIAEA-----------ELK 624
Cdd:COG1022 68 VAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQeqldkLLEVRDElpslrhivvldPRG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 625 PANTQSLCGLQQLEftSLTDPVGEPLNLVDVPEAktfpgigTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQ 704
Cdd:COG1022 148 LRDDPRLLSLDELL--ALGREVADPAELEARRAA-------VKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLER 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 705 IPVGastqdrAGDRIL------HktpiSFDvHVWELYWpLQEGAAVVIAapdghRDPAYLARVIAEQNVTCLHFVP---- 774
Cdd:COG1022 219 LPLG------PGDRTLsflplaH----VFE-RTVSYYA-LAAGATVAFA-----ESPDTLAEDLREVKPTFMLAVPrvwe 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 775 ----TMLTAFLEAPSAKRTLAEAGFGSGEQQRH----------------------------------VRYLICSGEALQK 816
Cdd:COG1022 282 kvyaGIQAKAEEAGGLKRKLFRWALAVGRRYARarlagkspslllrlkhaladklvfsklrealggrLRFAVSGGAALGP 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 817 DqILSAHNIMGVYPLNLYGPTEAAVDVTFWDSSQN-PEcsTVpiGQPVWNTQTRILDQalqpippgfvGELYLSGAQLAA 895
Cdd:COG1022 362 E-LARFFRALGIPVLEGYGLTETSPVITVNRPGDNrIG--TV--GPPLPGVEVKIAED----------GEILVRGPNVMK 426
|
490 500 510
....*....|....*....|....*....|..
gi 503164607 896 GYQNNPEATAQAFildnaTGERLYRTGDLAEW 927
Cdd:COG1022 427 GYYKNPEATAEAF-----DADGWLHTGDIGEL 453
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
541-1053 |
8.92e-32 |
|
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: 130.64 E-value: 8.92e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 541 ARARALAKAMLEAGVCPG--TAVGL-RFHRGLEQYIAL-YAALYAGFVYVPILPDLPAERVSSMMEDAQcSALVYgsgLS 616
Cdd:cd05922 1 LGVSAAASALLEAGGVRGerVVLILpNRFTYIELSFAVaYAGGRLGLVFVPLNPTLKESVLRYLVADAG-GRIVL---AD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 617 PIAEAELKPANTQSlcglqqleftsltdpvGEPLNLVDVPEA----KTFPGIGTALDDTAYILFTSGSTGRPKGVAISHR 692
Cdd:cd05922 77 AGAADRLRDALPAS----------------PDPGTVLDADGIraarASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQ 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 693 SIDNRLRwqqsqiPVGASTQDRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIaAPDGhRDPAYLARVIAEQNVTCLHF 772
Cdd:cd05922 141 NLLANAR------SIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVL-TNDG-VLDDAFWEDLREHGATGLAG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 773 VPT---MLTAFLEAPSAK---RTLAEAGfGSGEQQRhVRYLicsGEALQKDQILsahnIMgvyplnlYGPTEAAVDVTFW 846
Cdd:cd05922 213 VPStyaMLTRLGFDPAKLpslRYLTQAG-GRLPQET-IARL---RELLPGAQVY----VM-------YGQTEATRRMTYL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 847 DSSQ---NPECstvpIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPeataqAFILDNATGERLYRTGD 923
Cdd:cd05922 277 PPERileKPGS----IGLAIPGGEFEILDDDGTPTPPGEPGEIVHRGPNVMKGYWNDP-----PYRRKEGRGGGVLHTGD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 924 LAEwnltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTPEPALTAFLEIGD 1003
Cdd:cd05922 348 LAR--------------RDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPD 413
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 503164607 1004 VSEternriVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLA 1053
Cdd:cd05922 414 KID------PKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAALR 457
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
532-1054 |
1.46e-31 |
|
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: 129.72 E-value: 1.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAG-VCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALV 610
Cdd:cd05941 10 DSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 611 ygsglspiaeaelkpantqslcglqqleftsltdpvgeplnlvdvpeaktfpgigtaldDTAYILFTSGSTGRPKGVAIS 690
Cdd:cd05941 90 -----------------------------------------------------------DPALILYTSGTTGRPKGVVLT 110
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 691 HRSIDNRLR-----WQQSQipvgastqdraGDRILHKTPIsFDVH--VWELYWPLQEGAAVVIAAPDghrDPAYLARVIA 763
Cdd:cd05941 111 HANLAANVRalvdaWRWTE-----------DDVLLHVLPL-HHVHglVNALLCPLFAGASVEFLPKF---DPKEVAISRL 175
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 764 EQNVTCLHFVPTMLTAFLEAPSAKRTlaEAGFGSGEQQRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDV 843
Cdd:cd05941 176 MPSITVFMGVPTIYTRLLQYYEAHFT--DPQFARAAAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMAL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 844 TfwdssqNP-ECSTVP--IGQPVWNTQTRILDQ-ALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFildnaTGERLY 919
Cdd:cd05941 254 S------NPlDGERRPgtVGMPLPGVQARIVDEeTGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF-----TDDGWF 322
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 920 RTGDLAEwnltatnqepgtlaKNPRGVILYRGRT-DHQVKLHGQRLELGDIETTL-SHVEGVHSAVVLLytktPEPAL-- 995
Cdd:cd05941 323 KTGDLGV--------------VDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLlAHPGVSECAVIGV----PDPDWge 384
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503164607 996 --TAFLeigdVSETERNRIVAQA-RQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQ 1054
Cdd:cd05941 385 rvVAVV----VLRAGAAALSLEElKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKELRK 442
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
535-1052 |
3.82e-31 |
|
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: 128.18 E-value: 3.82e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 535 TYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYgsg 614
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 615 lspiaeaelkpantqslcglqqleftsltdpvgeplnlvdvpeaktfpgigtaldDTAYILFTSGSTGRPKGVAISHRSI 694
Cdd:cd05934 82 -------------------------------------------------------DPASILYTSGTTGPPKGVVITHANL 106
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 695 DNRLRWQQSQIPVgastqdRAGDRILHKTPISF-DVHVWELYWPLQEGAAVVIAapdghrdPAYLAR----VIAEQNVTC 769
Cdd:cd05934 107 TFAGYYSARRFGL------GEDDVYLTVLPLFHiNAQAVSVLAALSVGATLVLL-------PRFSASrfwsDVRRYGATV 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 770 LHFVPTMLTAFLEAPSAkrtlaeagfgsgEQQRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTfwdsS 849
Cdd:cd05934 174 TNYLGAMLSYLLAQPPS------------PDDRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIVGVI----G 237
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 850 QNPECSTVP-IGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQ---LAAGYQNNPEATAQAFildnATGerLYRTGDLA 925
Cdd:cd05934 238 PRDEPRRPGsIGRPAPGYEVRIVDDDGQELPAGEPGELVIRGLRgwgFFKGYYNMPEATAEAM----RNG--WFHTGDLG 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 926 EwnltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGV-HSAVVLLYTKTPEPALTAFLEIGDV 1004
Cdd:cd05934 312 Y--------------RDADGFFYFVDRKKDMIRRRGENISSAEVERAILRHPAVrEAAVVAVPDEVGEDEVKAVVVLRPG 377
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 503164607 1005 SETERNRIVAqarqHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd05934 378 ETLDPEELFA----FCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
532-927 |
4.94e-31 |
|
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: 128.48 E-value: 4.94e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVy 611
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALF- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 gsglspiaeaelkpantqslcglqqleftsltdpVGEPlnlvdvpeaktfpgigtalDDTAYILFTSGSTGRPKGVAISH 691
Cdd:cd05907 83 ----------------------------------VEDP-------------------DDLATIIYTSGTTGRPKGVMLSH 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 692 RSIdnrlrWQQSQipvGASTQ--DRAGDRILHKTPISfdvHVWE----LYWPLQEGAAVVIAAPD-------GHRDPAYL 758
Cdd:cd05907 110 RNI-----LSNAL---ALAERlpATEGDRHLSFLPLA---HVFErragLYVPLLAGARIYFASSAetllddlSEVRPTVF 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 759 ARVIaeqnvtcLHFVPTMLTAFLEA-PSAKRTLAEAGFGSGeqqrhVRYLICSGEALQKDQILSAHNImGVYPLNLYGPT 837
Cdd:cd05907 179 LAVP-------RVWEKVYAAIKVKAvPGLKRKLFDLAVGGR-----LRFAASGGAPLPAELLHFFRAL-GIPVYEGYGLT 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 838 E--AAVDVTFWDssqNPECSTVpiGQPVWNTQTRILDQalqpippgfvGELYLSGAQLAAGYQNNPEATAQAFILDNAtg 915
Cdd:cd05907 246 EtsAVVTLNPPG---DNRIGTV--GKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW-- 308
|
410
....*....|..
gi 503164607 916 erlYRTGDLAEW 927
Cdd:cd05907 309 ---LHTGDLGEI 317
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
485-925 |
8.22e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 128.95 E-value: 8.22e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 485 HPIEYKTLLQRfqdALTRYPNEPALYacapDEDGTLspqspqayefsqvlTYHELDARARALAKAMLEAGVCPGTAVGLR 564
Cdd:PRK06188 10 SGATYGHLLVS---ALKRYPDRPALV----LGDTRL--------------TYGQLADRISRYIQAFEALGLGTGDAVALL 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 565 FHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVygsgLSPIAEAELKPANTQSLCGLQQLeFTslTD 644
Cdd:PRK06188 69 SLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLI----VDPAPFVERALALLARVPSLKHV-LT--LG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 645 PVGEPLNLVDvpEAKTFPGI----GTALDDTAYILFTSGSTGRPKGVAISHRSIdnrlrWQQSQIpVGASTQDRAGDRIL 720
Cdd:PRK06188 142 PVPDGVDLLA--AAAKFGPAplvaAALPPDIAGLAYTGGTTGKPKGVMGTHRSI-----ATMAQI-QLAEWEWPADPRFL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 721 HKTPISfdvHV-WELYWP-LQEGAAVVIAApdgHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSakrtLAEAGFGSG 798
Cdd:PRK06188 214 MCTPLS---HAgGAFFLPtLLRGGTVIVLA---KFDPAEVLRAIEEQRITATFLVPTMIYALLDHPD----LRTRDLSSL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 799 EQqrhVRYlicSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTFWDSSQ----NPECSTvPIGQPVWNTQTRILDQA 874
Cdd:PRK06188 284 ET---VYY---GASPMSPVRLAEAIERFGPIFAQYYGQTEAPMVITYLRKRDhdpdDPKRLT-SCGRPTPGLRVALLDED 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 503164607 875 LQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFildnATGerLYRTGDLA 925
Cdd:PRK06188 357 GREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF----RDG--WLHTGDVA 401
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
535-1052 |
8.43e-31 |
|
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: 128.79 E-value: 8.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 535 TYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSsmmedaqcsalVYGSg 614
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQN-----------IYLG- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 615 lspiaeaelkpantqslcglqqleftsltdpVGEPLNLVDVPEAktfpGIGTALDDTAYILFTSGSTGRPKGVAISHRSI 694
Cdd:cd17647 90 -------------------------------VAKPRGLIVIRAA----GVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 695 DNRLRWQQSQIpvGASTQDR----AGdrILHKtPISFDvhvweLYWPLQEGAAVVIAAPDGHRDPAYLARVIAEQNVTCL 770
Cdd:cd17647 135 AYYFPWMAKRF--NLSENDKftmlSG--IAHD-PIQRD-----MFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVT 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 771 HFVPTM---LTAFLEAPSAKrtLAEAGFgsgeqqrhvrylicSGEALQKDQILS----AHNIMGVyplNLYGPTEAAVDV 843
Cdd:cd17647 205 HLTPAMgqlLTAQATTPFPK--LHHAFF--------------VGDILTKRDCLRlqtlAENVRIV---NMYGTTETQRAV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 844 TFWD---SSQNPEC-----STVPIGQPVWNTQTRILDQ--ALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFI---- 909
Cdd:cd17647 266 SYFEvpsRSSDPTFlknlkDVMPAGRGMLNVQLLVVNRndRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwf 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 910 --------LDNATGE-----------RLYRTGDLAEWNltatnqepgtlaknPRGVILYRGRTDHQVKLHGQRLELGDIE 970
Cdd:cd17647 346 vepdhwnyLDKDNNEpwrqfwlgprdRLYRTGDLGRYL--------------PNGDCECCGRADDQVKIRGFRIELGEID 411
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 971 TTLSHVEGVHSAVVLLY-TKTPEPALTAFL------------EIGDVSETERNRIVAQ-----------ARQHCENTLPD 1026
Cdd:cd17647 412 THISQHPLVRENITLVRrDKDEEPTLVSYIvprfdkpddesfAQEDVPKEVSTDPIVKgligyrklikdIREFLKKRLAS 491
|
570 580
....*....|....*....|....*.
gi 503164607 1027 YMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd17647 492 YAIPSLIVVLDKLPLNPNGKVDKPKL 517
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
534-924 |
3.26e-30 |
|
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: 127.35 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVcPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLP---AERVSSMMEDAQCSALv 610
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVGK-PGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPgrhAERLAAILADAGPRVV- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 611 ygsgLSPIAEAELKPANTQSLCGLQQLEFTSLTdpvgeplnLVDVPEAKTFPGIGTALDDTAYILFTSGSTGRPKGVAIS 690
Cdd:cd05931 103 ----LTTAAALAAVRAFAASRPAAGTPRLLVVD--------LLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 691 HRSIDNRLRwqqsQIpvGASTQDRAGDRIL------HK--------------------TPISFdvhvweLYWPLQ----- 739
Cdd:cd05931 171 HRNLLANVR----QI--RRAYGLDPGDVVVswlplyHDmgligglltplysggpsvlmSPAAF------LRRPLRwlrli 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 740 -EGAAVVIAAPDGhrdpAY---LARVIAEQ----NVTCLHFV--------PTMLTAFLEA-------PSAKRT---LAEA 793
Cdd:cd05931 239 sRYRATISAAPNF----AYdlcVRRVRDEDleglDLSSWRVAlngaepvrPATLRRFAEAfapfgfrPEAFRPsygLAEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 794 G----FGSGEQQRHVRYLicSGEALQKDQILSAhnimgvyplnlyGPTEAAVDVtfwdssqnpecstVPIGQPVWNTQTR 869
Cdd:cd05931 315 TlfvsGGPPGTGPVVLRV--DRDALAGRAVAVA------------ADDPAAREL-------------VSCGRPLPDQEVR 367
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 503164607 870 ILDQA-LQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNATGERLY-RTGDL 924
Cdd:cd05931 368 IVDPEtGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWlRTGDL 424
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
502-908 |
6.70e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 126.20 E-value: 6.70e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 502 RYPNEPALYacapDEDgtlspqspqayefsQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYA 581
Cdd:PRK08316 23 RYPDKTALV----FGD--------------RSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 582 GFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIAEAELKPANTQSLCGLQQLeftSLTDPVGEPLNLVD--VPEAK 659
Cdd:PRK08316 85 GAVHVPVNFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVL---GGREAPGGWLDFADwaEAGSV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 660 TFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSidnrLRWQ-QSQIPVGASTqdrAGDRILHKTPI--SFDVHVWELYW 736
Cdd:PRK08316 162 AEPDVELADDDLAQILYTSGTESLPKGAMLTHRA----LIAEyVSCIVAGDMS---ADDIPLHALPLyhCAQLDVFLGPY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 737 PLQEGAAVVIAAPdghrDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPS-AKRTLAeagfgsgeqqrhvrylicsgeALQ 815
Cdd:PRK08316 235 LYVGATNVILDAP----DPELILRTIEAERITSFFAPPTVWISLLRHPDfDTRDLS---------------------SLR 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 816 KDQILSAhnIMGVYPL-------------NLYGPTEAAVDVTfwdsSQNPE--------CstvpiGQPVWNTQTRILDQA 874
Cdd:PRK08316 290 KGYYGAS--IMPVEVLkelrerlpglrfyNCYGQTEIAPLAT----VLGPEehlrrpgsA-----GRPVLNVETRVVDDD 358
|
410 420 430
....*....|....*....|....*....|....
gi 503164607 875 LQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAF 908
Cdd:PRK08316 359 GNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAF 392
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
502-925 |
3.14e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 124.30 E-value: 3.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 502 RYPNEPALYAcapdedgtlspqspqayeFSQVLTYHELDARARALAkAML--EAGVCPGTAVGLrFHRGLEQY-IALYAA 578
Cdd:PRK08314 22 RYPDKTAIVF------------------YGRAISYRELLEEAERLA-GYLqqECGVRKGDRVLL-YMQNSPQFvIAYYAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 579 LYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPiaeaELKPANTQSlcGLQQLEFTSLTD------PVGEPLNL 652
Cdd:PRK08314 82 LRANAVVVPVNPMNREEELAHYVTDSGARVAIVGSELAP----KVAPAVGNL--RLRHVIVAQYSDylpaepEIAVPAWL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 653 VDVPEAKTFPGIGT-----AL-------------DDTAYILFTSGSTGRPKGVAISHRSIdnrlrwqQSQIpVGAST--Q 712
Cdd:PRK08314 156 RAEPPLQALAPGGVvawkeALaaglappphtagpDDLAVLPYTSGTTGVPKGCMHTHRTV-------MANA-VGSVLwsN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 713 DRAGDRILHKTPIsFDV--HVWELYWPLQEGAAVVIAaPDGHRDPAylARVIAEQNVTCLHFVPTMLTAFLEAPsakrTL 790
Cdd:PRK08314 228 STPESVVLAVLPL-FHVtgMVHSMNAPIYAGATVVLM-PRWDREAA--ARLIERYRVTHWTNIPTMVVDFLASP----GL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 791 AEAGFGSgeqqrhVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEaavdvTFWDSSQNP------ECstvpIGQPVW 864
Cdd:PRK08314 300 AERDLSS------LRYIGGGGAAMPEAVAERLKELTGLDYVEGYGLTE-----TMAQTHSNPpdrpklQC----LGIPTF 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503164607 865 NTQTRILD-QALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFI-LDnatGERLYRTGDLA 925
Cdd:PRK08314 365 GVDARVIDpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIeID---GKRFFRTGDLG 424
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
531-1054 |
6.64e-28 |
|
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: 118.69 E-value: 6.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 531 SQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALV 610
Cdd:cd05971 4 PEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 611 ygsglspiaeaelkpantqslcglqqleftslTDpvgeplnlvdvpeaktfpgigtALDDTAYILFTSGSTGRPKGVAIS 690
Cdd:cd05971 84 --------------------------------TD----------------------GSDDPALIIYTSGTTGPPKGALHA 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 691 HRSIdnrlrwqQSQIPVGASTQD---RAGDriLHKTPIS-------FDVHVWELYWplqeGAAVViaapdGHR----DPA 756
Cdd:cd05971 110 HRVL-------LGHLPGVQFPFNlfpRDGD--LYWTPADwawigglLDVLLPSLYF----GVPVL-----AHRmtkfDPK 171
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 757 YLARVIAEQNVTclhfvptmlTAFLeAPSAKRTLAEAGFGSGEQQRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGP 836
Cdd:cd05971 172 AALDLMSRYGVT---------TAFL-PPTALKMMRQQGEQLKHAQVKLRAIATGGESLGEELLGWAREQFGVEVNEFYGQ 241
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 837 TEAAVDVTfwdssqnpECSTV------PIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAA--GYQNNPEATAQAF 908
Cdd:cd05971 242 TECNLVIG--------NCSALfpikpgSMGKPIPGHRVAIVDDNGTPLPPGEVGEIAVELPDPVAflGYWNNPSATEKKM 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 909 ILDnatgerLYRTGDLAEwnltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTL-SHVEGVHSAVVLLy 987
Cdd:cd05971 314 AGD------WLLTGDLGR--------------KDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLlKHPAVLMAAVVGI- 372
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503164607 988 tktPEPALT----AFLEIGDvSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQ 1054
Cdd:cd05971 373 ---PDPIRGeivkAFVVLNP-GETPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRRELRA 439
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
490-1052 |
2.27e-27 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 118.54 E-value: 2.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 490 KTLLQRFQDALTRYPNEpalyacapdedGTLSPQSPQAYEFsqvLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGL 569
Cdd:cd05906 10 RTLLELLLRAAERGPTK-----------GITYIDADGSEEF---QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 570 EQYIALYAALYAGFVYVPiLPDLPA-----------ERVSSMMEDAQCsaLVYGSGLSPIAEAElkpaNTQSLCGLQQLE 638
Cdd:cd05906 76 DFIPAFWACVLAGFVPAP-LTVPPTydepnarlrklRHIWQLLGSPVV--LTDAELVAEFAGLE----TLSGLPGIRVLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 639 FTSLTDPVGEPLNLVDVPeaktfpgigtalDDTAYILFTSGSTGRPKGVAISHRSIDNRLRwqqsqipvGASTQDR--AG 716
Cdd:cd05906 149 IEELLDTAADHDLPQSRP------------DDLALLMLTSGSTGFPKAVPLTHRNILARSA--------GKIQHNGltPQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 717 DRIL------HKTPISFdVHVWELYWPLQEgaaVVIAAPDGHRDPAYLARVIAEQNVTcLHFVPTMLTAFLEAPSAKRTL 790
Cdd:cd05906 209 DVFLnwvpldHVGGLVE-LHLRAVYLGCQQ---VHVPTEEILADPLRWLDLIDRYRVT-ITWAPNFAFALLNDLLEEIED 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 791 AEAGFGSgeqqrhVRYLICSGEALQK---DQILSAHNIMGVYPLNL---YGPTEAAVDVTFWDSSQNPECST----VPIG 860
Cdd:cd05906 284 GTWDLSS------LRYLVNAGEAVVAktiRRLLRLLEPYGLPPDAIrpaFGMTETCSGVIYSRSFPTYDHSQalefVSLG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 861 QPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNatgerLYRTGDLA---EWNLTATnqepg 937
Cdd:cd05906 358 RPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDG-----WFRTGDLGfldNGNLTIT----- 427
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 938 tlaknprgvilyrGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTPEPALTAFLEIGDVSE----TERNRIV 1013
Cdd:cd05906 428 -------------GRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRDPGAETEELAIFFVPEydlqDALSETL 494
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 503164607 1014 AQARQHCENTL---PDYMVPRlwhTTAQFPVSPSGKTDRKNL 1052
Cdd:cd05906 495 RAIRSVVSREVgvsPAYLIPL---PKEEIPKTSLGKIQRSKL 533
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
534-1052 |
2.83e-27 |
|
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: 117.61 E-value: 2.83e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGS 613
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 GLSPIAEAELKPAntqslcglqQLEFTSLTDPVGEPLNLVDVPEAKTfPGIGtaldDTAYILFTSGSTGRPKGVAISHRS 693
Cdd:cd05923 109 DAQVMDAIFQSGV---------RVLALSDLVGLGEPESAGPLIEDPP-REPE----QPAFVFYTSGTTGLPKGAVIPQRA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IDNRLRWQQSQipvgASTQDRAGDRILHKTPIS-----FDVHVWELYWplqEGAAVVIAApdghRDPAYLARVIAEQNVT 768
Cdd:cd05923 175 AESRVLFMSTQ----AGLRHGRHNVVLGLMPLYhvigfFAVLVAALAL---DGTYVVVEE----FDPADALKLIEQERVT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 769 CLHFVPTMLTAfleapsakrtLAEAGFGSGEQQRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAavdvtfWDS 848
Cdd:cd05923 244 SLFATPTHLDA----------LAAAAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEA------MNS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 849 SQNPECSTVPIGQPVWNTQ---TRILDQALQPIPPGFVGELYLSGAQLAA--GYQNNPEATAQAFIldnatgERLYRTGD 923
Cdd:cd05923 308 LYMRDARTGTEMRPGFFSEvriVRIGGSPDEALANGEEGELIVAAAADAAftGYLNQPEATAKKLQ------DGWYRTGD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 924 LAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVL-LYTKTPEPALTAF--LE 1000
Cdd:cd05923 382 VGYV--------------DPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIgVADERWGQSVTACvvPR 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 503164607 1001 IGDVSETERNrivaqarQHCENT-LPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd05923 448 EGTLSADELD-------QFCRASeLADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
535-925 |
9.33e-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: 116.58 E-value: 9.33e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 535 TYHELDARARALAKAMLEAGVCPGTAVG---LRFHRGLEQYialYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVY 611
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVAtlaWNTHRHLELY---YAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 GSGLSPIAEAeLKPANTQ--------------SLCGLQQLEFTSLTDPVGEPLNLVDVPEaktfpgigtalDDTAYILFT 677
Cdd:cd12119 104 DRDFLPLLEA-IAPRLPTvehvvvmtddaampEPAGVGVLAYEELLAAESPEYDWPDFDE-----------NTAAAICYT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 678 SGSTGRPKGVAISHRSIdnrlrWQQSqipVGASTQD----RAGDRILHKTPIsFDVHVWEL-YWPLQEGAAVVIaaPDGH 752
Cdd:cd12119 172 SGTTGNPKGVVYSHRSL-----VLHA---MAALLTDglglSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL--PGPY 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 753 RDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKrtlaeagfgsGEQQRHVRYLICSGEALQKDQILSAHNiMGVYPLN 832
Cdd:cd12119 241 LDPASLAELIEREGVTFAAGVPTVWQGLLDHLEAN----------GRDLSSLRRVVIGGSAVPRSLIEAFEE-RGVRVIH 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 833 LYGPTEAAVDVTF----WDSSQNPECSTVPI----GQPVWNTQTRILDQALQPIP--PGFVGELYLSGAQLAAGYQNNPE 902
Cdd:cd12119 310 AWGMTETSPLGTVarppSEHSNLSEDEQLALrakqGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDE 389
|
410 420
....*....|....*....|...
gi 503164607 903 ATAQAFildnATGerLYRTGDLA 925
Cdd:cd12119 390 ESEALT----EDG--WLRTGDVA 406
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
502-899 |
1.23e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 116.57 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 502 RYPNEPALYacapDEDGTLspqspqayefsqvlTYHELDARARALAKAMLEAGVCPGTAVGL--RFHRGLeqYIALYAAL 579
Cdd:PRK07788 61 RAPDRAALI----DERGTL--------------TYAELDEQSNALARGLLALGVRAGDGVAVlaRNHRGF--VLALYAAG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 580 YAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSglspiaeaelkpantqslcglqqlEFTSLTDPVGEPLN----LVDV 655
Cdd:PRK07788 121 KVGARIILLNTGFSGPQLAEVAAREGVKALVYDD------------------------EFTDLLSALPPDLGrlraWGGN 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 656 PEAKTFPGIGTA-LDDTA----------------YILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVgastqdRAGDR 718
Cdd:PRK07788 177 PDDDEPSGSTDEtLDDLIagsstaplpkppkpggIVILTSGTTGTPKGAPRPEPSPLAPLAGLLSRVPF------RAGET 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 719 ILHKTPI--SFDVHVWELYWPLqeGAAVVIaapdgHR--DPAYLARVIAEQNVTCLHFVPTMLTAFLEAP---SAKRTLA 791
Cdd:PRK07788 251 TLLPAPMfhATGWAHLTLAMAL--GSTVVL-----RRrfDPEATLEDIAKHKATALVVVPVMLSRILDLGpevLAKYDTS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 792 EagfgsgeqqrhVRYLICSGEALQKDQILSAHNIMG--VYplNLYGPTEAAVDV--TFWDSSQNPecSTVpiGQPVWNTQ 867
Cdd:PRK07788 324 S-----------LKIIFVSGSALSPELATRALEAFGpvLY--NLYGSTEVAFATiaTPEDLAEAP--GTV--GRPPKGVT 386
|
410 420 430
....*....|....*....|....*....|..
gi 503164607 868 TRILDQALQPIPPGFVGELYLSGAQLAAGYQN 899
Cdd:PRK07788 387 VKILDENGNEVPRGVVGRIFVGNGFPFEGYTD 418
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
491-1191 |
2.16e-26 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 118.73 E-value: 2.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 491 TLLQRFQDALTRYPNEPALYACAPDEDGTLspqspqayefsqVLTYHELDARARALAkAMLEAGVCPGTAVGLRFHRGLE 570
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALRFLADDPGEGV------------VLSYRDLDLRARTIA-AALQARASFGDRAVLLFPSGPD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 571 QYIALYAALYAGFVYVPILPDLPA-----ERVSSMMEDAQCSALVYGSGLSPiaeaelkpantqslcGLQQLEftSLTDP 645
Cdd:PRK05691 77 YVAAFFGCLYAGVIAVPAYPPESArrhhqERLLSIIADAEPRLLLTVADLRD---------------SLLQME--ELAAA 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 646 VGEPLNLVDVPE---AKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHrsidNRLRWQQSQIPVGASTQDRAGDRILHK 722
Cdd:PRK05691 140 NAPELLCVDTLDpalAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSH----GNLVANEQLIRHGFGIDLNPDDVIVSW 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 723 TPISFDVH-VWELYWPLQEGAAVVIAAP---------------------DGHRDPAY--LARVIAEQNVTCLHfvptmLT 778
Cdd:PRK05691 216 LPLYHDMGlIGGLLQPIFSGVPCVLMSPayflerplrwleaiseyggtiSGGPDFAYrlCSERVSESALERLD-----LS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 779 AFLEAPSAK--------RTLAEAGFGSGeqQRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTFWDSSQ 850
Cdd:PRK05691 291 RWRVAYSGSepirqdslERFAEKFAACG--FDPDSFFASYGLAEATLFVSGGRRGQGIPALELDAEALARNRAEPGTGSV 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 851 NPECSTVPIGQPVwntqtRILD-QALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFIldNATGERLYRTGDLaewnl 929
Cdd:PRK05691 369 LMSCGRSQPGHAV-----LIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFV--EHDGRTWLRTGDL----- 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 930 tatnqepGTLAknpRGVILYRGRTDHQVKLHGQRLELGDIETTL-SHVEGVHSAVVLLYTKTPEPALTafleIGDVSETE 1008
Cdd:PRK05691 437 -------GFLR---DGELFVTGRLKDMLIVRGHNLYPQDIEKTVeREVEVVRKGRVAAFAVNHQGEEG----IGIAAEIS 502
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1009 RNriVAQArqhcenTLPDYMVPRLWHTTAQ----------------FPVSPSGKTDRK----NLAQIEF----------T 1058
Cdd:PRK05691 503 RS--VQKI------LPPQALIKSIRQAVAEacqeapsvvlllnpgaLPKTSSGKLQRSacrlRLADGSLdsyalfpalqA 574
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1059 FDTNTADGPHGLLEQQISEIIAGVLGRSQFGVTEDFLAAGGNSLAALSVIAKIEENLGKMLSIGALFANPTVKGIAAA-- 1136
Cdd:PRK05691 575 VEAAQTAASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAva 654
|
730 740 750 760 770
....*....|....*....|....*....|....*....|....*....|....*..
gi 503164607 1137 --LNEDSPDIEFAPVLPlREADSTDSATSKNTVPLFILPPAGglgwcyAAYlpHIPG 1191
Cdd:PRK05691 655 rqLAGGGAAQAAIARLP-RGQALPQSLAQNRLWLLWQLDPQS------AAY--NIPG 702
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
494-964 |
7.09e-25 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 111.14 E-value: 7.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 494 QRFQDALTRYPNEPALYAcapdedgtlsPQSPQAYEF--SQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQ 571
Cdd:PRK09274 10 RHLPRAAQERPDQLAVAV----------PGGRGADGKlaYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 572 YIALYAALYAGFVyvPILPDlPAERVSSMME---DAQCSALV------YGSGLSPIAEAELKPANT--QSLC-GLQQLEf 639
Cdd:PRK09274 80 FALTFALFKAGAV--PVLVD-PGMGIKNLKQclaEAQPDAFIgipkahLARRLFGWGKPSVRRLVTvgGRLLwGGTTLA- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 640 TSLTDPVGEPLNLVDVPEaktfpgigtalDDTAYILFTSGSTGRPKGVAISHRSIDnrlrwqqSQI-PVGASTQDRAGDR 718
Cdd:PRK09274 156 TLLRDGAAAPFPMADLAP-----------DDMAAILFTSGSTGTPKGVVYTHGMFE-------AQIeALREDYGIEPGEI 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 719 ILHKTPIsFDVHvwelywPLQEGAAVVIAAPDGHR----DPAYLARVIAEQNVTCLhFVptmltafleAPSAKRTLAEAG 794
Cdd:PRK09274 218 DLPTFPL-FALF------GPALGMTSVIPDMDPTRpatvDPAKLFAAIERYGVTNL-FG---------SPALLERLGRYG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 795 FGSGEQQRHVRYLICSGEALQKDQILSAHNIM--GVYPLNLYGPTEA------AVDVTFWDSSQNPECST-VPIGQPVWN 865
Cdd:PRK09274 281 EANGIKLPSLRRVISAGAPVPIAVIERFRAMLppDAEILTPYGATEAlpissiESREILFATRAATDNGAgICVGRPVDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 866 TQTRILDQALQPI---------PPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNATGERlYRTGDLaewnltatnqep 936
Cdd:PRK09274 361 VEVRIIAISDAPIpewddalrlATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVW-HRMGDL------------ 427
|
490 500
....*....|....*....|....*...
gi 503164607 937 GTLakNPRGVILYRGRTDHQVKLHGQRL 964
Cdd:PRK09274 428 GYL--DAQGRLWFCGRKAHRVETAGGTL 453
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
534-925 |
8.68e-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: 110.40 E-value: 8.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGS 613
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 GLSPiaeaELKPANTQSLCgLQQLEFTSLtdPVGEPLNLVDVPEAKtFPGIGTalDDTAYILFTSGSTGRPKGVAISHRS 693
Cdd:cd05904 113 ELAE----KLASLALPVVL-LDSAEFDSL--SFSDLLFEADEAEPP-VVVIKQ--DDVAALLYSSGTTGRSKGVMLTHRN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IDNRLrwqqSQIPVGASTQDRAGDRILHKTPISfdvHVWELYW----PLQEGAAVVIAapdGHRDPAYLARVIAEQNVTC 769
Cdd:cd05904 183 LIAMV----AQFVAGEGSNSDSEDVFLCVLPMF---HIYGLSSfalgLLRLGATVVVM---PRFDLEELLAAIERYKVTH 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 770 LHFVPTMLTAfleapsakrtLAEAGFGSGEQQRHVRYLICSGEALQKDQILS-AHNIMGVYPLNLYGPTE--AAVDVTFw 846
Cdd:cd05904 253 LPVVPPIVLA----------LVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAfRAKFPNVDLGQGYGMTEstGVVAMCF- 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 847 dssqNPECSTVPIGQPVW---NTQTRILD-QALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFildnaTGERLYRTG 922
Cdd:cd05904 322 ----APEKDRAKYGSVGRlvpNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATI-----DKEGWLHTG 392
|
...
gi 503164607 923 DLA 925
Cdd:cd05904 393 DLC 395
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
659-925 |
1.74e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 108.47 E-value: 1.74e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 659 KTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLRwQQSQIpVGAstqdRAGDRILHKTPI--SFDVHVwELYW 736
Cdd:PRK08633 772 KRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIE-QISDV-FNL----RNDDVILSSLPFfhSFGLTV-TLWL 844
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 737 PLQEGAAVVIaapdgHRDP---AYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRTLaeagFGSgeqqrhVRYLICSGEA 813
Cdd:PRK08633 845 PLLEGIKVVY-----HPDPtdaLGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLM----FAS------LRLVVAGAEK 909
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 814 LQKDQILSAHNIMGVYPLNLYGPTE----AAV------DVTFWDSSQNPECStvpIGQPVWNTQTRILD-QALQPIPPGF 882
Cdd:PRK08633 910 LKPEVADAFEEKFGIRILEGYGATEtspvASVnlpdvlAADFKRQTGSKEGS---VGMPLPGVAVRIVDpETFEELPPGE 986
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 503164607 883 VGELYLSGAQLAAGYQNNPEATAQAfiLDNATGERLYRTGDLA 925
Cdd:PRK08633 987 DGLILIGGPQVMKGYLGDPEKTAEV--IKDIDGIGWYVTGDKG 1027
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
669-925 |
8.89e-23 |
|
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: 101.59 E-value: 8.89e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAISHRSIDNRLRWqqsqipVGASTQDRAGDRILHKTPI--SFDVhVWELYWPLQEGAAVVI 746
Cdd:cd05917 2 DDVINIQFTSGTTGSPKGATLTHHNIVNNGYF------IGERLGLTEQDRLCIPVPLfhCFGS-VLGVLACLTHGATMVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 747 AAPDghRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAP-------SAKRTLAEAGfgsgeqqrhvryLICSGEALQKdqI 819
Cdd:cd05917 75 PSPS--FDPLAVLEAIEKEKCTALHGVPTMFIAELEHPdfdkfdlSSLRTGIMAG------------APCPPELMKR--V 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 820 LSAHNIMGVypLNLYGPTEAA--VDVTFWDSSQNPECSTVpiGQPVWNTQTRILDQALQPIPP-GFVGELYLSGAQLAAG 896
Cdd:cd05917 139 IEVMNMKDV--TIAYGMTETSpvSTQTRTDDSIEKRVNTV--GRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKG 214
|
250 260
....*....|....*....|....*....
gi 503164607 897 YQNNPEATAQAfildnATGERLYRTGDLA 925
Cdd:cd05917 215 YWNDPEKTAEA-----IDGDGWLHTGDLA 238
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
665-1052 |
1.78e-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: 1.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 665 GTALDDTAYILFTSGSTGRPKGVAISHRSI-DNRlrwQQSQIPVGASTQdragDRILHKTPI----SFDVHVWelyWPLQ 739
Cdd:cd05909 143 PVQPDDPAVILFTSGSEGLPKGVVLSHKNLlANV---EQITAIFDPNPE----DVVFGALPFfhsfGLTGCLW---LPLL 212
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 740 EGAAVVIaapdgHRDPAY---LARVIAEQNVTCLHFVPTMLTAFLEAPSAkrtlaeagfgsgEQQRHVRYLICSGEALQK 816
Cdd:cd05909 213 SGIKVVF-----HPNPLDykkIPELIYDKKATILLGTPTFLRGYARAAHP------------EDFSSLRLVVAGAEKLKD 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 817 DQILSAHNIMGVYPLNLYGPTEAA--VDVTFWDSSQNPECstvpIGQPVWNTQTRILD-QALQPIPPGFVGELYLSGAQL 893
Cdd:cd05909 276 TLRQEFQEKFGIRILEGYGTTECSpvISVNTPQSPNKEGT----VGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNV 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 894 AAGYQNNPEATAQAFildnatGERLYRTGDLAewnltatnqepgtlAKNPRGVILYRGRTDHQVKLHGQRLELGDIETTL 973
Cdd:cd05909 352 MLGYLNEPELTSFAF------GDGWYDTGDIG--------------KIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDIL 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 974 SHVEG--VHSAVVLLYTKTPEPALTAFLeigDVSETERNRIVAQARQHcenTLPDYMVPRLWHTTAQFPVSPSGKTDRKN 1051
Cdd:cd05909 412 SEILPedNEVAVVSVPDGRKGEKIVLLT---TTTDTDPSSLNDILKNA---GISNLAKPSYIHQVEEIPLLGTGKPDYVT 485
|
.
gi 503164607 1052 L 1052
Cdd:cd05909 486 L 486
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
534-908 |
2.59e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 102.93 E-value: 2.59e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGS 613
Cdd:PRK07786 43 TTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAHVVVTEA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 GLSPIAEA--ELKPANTQSLC--GLQQ---LEFTSLTDPVGEPLNLVDVPEaktfpgigtalDDTAYILFTSGSTGRPKG 686
Cdd:PRK07786 123 ALAPVATAvrDIVPLLSTVVVagGSSDdsvLGYEDLLAEAGPAHAPVDIPN-----------DSPALIMYTSGTTGRPKG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 687 VAISHRSIDNrlrwqQSQIPVGASTQDRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIaAPDGHRDPAYLARVIAEQN 766
Cdd:PRK07786 192 AVLTHANLTG-----QAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVI-YPLGAFDPGQLLDVLEAEK 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 767 VTCLHFVPTMLTAFLEAPSAK-RTLAEAGFGSGEQQRHVRYLICSGEALQKDQILSAhnimgvyplnlYGPTEAAvDVTF 845
Cdd:PRK07786 266 VTGIFLVPAQWQAVCAEQQARpRDLALRVLSWGAAPASDTLLRQMAATFPEAQILAA-----------FGQTEMS-PVTC 333
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503164607 846 WDSSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAF 908
Cdd:PRK07786 334 MLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF 396
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
534-1052 |
2.63e-22 |
|
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: 101.64 E-value: 2.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGS 613
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 glspiaeaelkpantqslcglqqleftsltdpvgeplnlvdvpeaktfpgigtalDDTAYILFTSGSTGRPKGVAISHrs 693
Cdd:cd05972 81 -------------------------------------------------------EDPALIYFTSGTTGLPKGVLHTH-- 103
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 idnrlRWQQSQIPVGASTQD-RAGDriLHKTPIS--FDVHVW-ELYWPLQEGAAVVIAapDGHR-DPAYLARVIAEQNVt 768
Cdd:cd05972 104 -----SYPLGHIPTAAYWLGlRPDD--IHWNIADpgWAKGAWsSFFGPWLLGATVFVY--EGPRfDAERILELLERYGV- 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 769 clhfvptmlTAFLEAPSAKRTLAEAGFGSGEQQrHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTfwds 848
Cdd:cd05972 174 ---------TSFCGPPTAYRMLIKQDLSSYKFS-HLRLVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVG---- 239
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 849 sqnpECSTVPI-----GQPVWNTQTRILDQALQPIPPGFVGEL--YLSGAQLAAGYQNNPEATAQAFildnatGERLYRT 921
Cdd:cd05972 240 ----NFPDMPVkpgsmGRPTPGYDVAIIDDDGRELPPGEEGDIaiKLPPPGLFLGYVGDPEKTEASI------RGDYYLT 309
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 922 GDLAEwnltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTL-SHVEGVHSAVVllytKTPEPALT---- 996
Cdd:cd05972 310 GDRAY--------------RDEDGYFWFVGRADDIIKSSGYRIGPFEVESALlEHPAVAEAAVV----GSPDPVRGevvk 371
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 503164607 997 AFLEIGDvSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd05972 372 AFVVLTS-GYEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
534-1056 |
4.51e-22 |
|
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: 101.04 E-value: 4.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVygs 613
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLI--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 glspiaeaelkpaNTQSLcglqqLEFTSLTDPvgeplnlvdvpeaktfpgigtalddtAYILFTSGSTGRPKGVAISHRS 693
Cdd:cd05969 78 -------------TTEEL-----YERTDPEDP--------------------------TLLHYTSGTTGTPKGVLHVHDA 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IdnrlrWQQSQipvgastqdragdrilhKTPISFDVHVWELYW-----------------PLQEGAAVVIAapDGHRDPA 756
Cdd:cd05969 114 M-----IFYYF-----------------TGKYVLDLHPDDIYWctadpgwvtgtvygiwaPWLNGVTNVVY--EGRFDAE 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 757 YLARVIAEQNVTCLHFVPT---MLTAFLEAPSAKRTLAeagfgsgeqqrHVRYLICSGEALQKDQILSAHNIMGVYPLNL 833
Cdd:cd05969 170 SWYGIIERVKVTVWYTAPTairMLMKEGDELARKYDLS-----------SLRFIHSVGEPLNPEAIRWGMEVFGVPIHDT 238
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 834 YGPTEAAVDVTfwdssQNPECSTVPIG---QPVWNTQTRILDQALQPIPPGFVGELYLSGA--QLAAGYQNNPEATAQAF 908
Cdd:cd05969 239 WWQTETGSIMI-----ANYPCMPIKPGsmgKPLPGVKAAVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEERYKNSF 313
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 909 IldnaTGerLYRTGDLAEwnltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTL-SHVEGVHSAVVlly 987
Cdd:cd05969 314 I----DG--WYLTGDLAY--------------RDEDGYFWFVGRADDIIKTSGHRVGPFEVESALmEHPAVAEAGVI--- 370
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503164607 988 tKTPEPAL----TAFLEIG---DVSETERNRIVAQARQHcentLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIE 1056
Cdd:cd05969 371 -GKPDPLRgeiiKAFISLKegfEPSDELKEEIINFVRQK----LGAHVAPREIEFVDNLPKTRSGKIMRRVLKAKE 441
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
533-1054 |
5.16e-22 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 101.89 E-value: 5.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 533 VLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSA-LVY 611
Cdd:PRK05852 43 AISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVvLID 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 GSGLSPIAEAELKP-ANTQSLCGLQQLEFTSLT---DPVGEPLNLVDVPEaktfpGIGtalDDTAYILFTSGSTGRPKGV 687
Cdd:PRK05852 123 ADGPHDRAEPTTRWwPLTVNVGGDSGPSGGTLSvhlDAATEPTPATSTPE-----GLR---PDDAMIMFTGGTTGLPKMV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 688 AISHRSIDNRLRwqqsqiPVGASTQDRAGDRILHKTPIsFDVH--VWELYWPLQEGAAVVIAAPDGHRDPAYLARvIAEQ 765
Cdd:PRK05852 195 PWTHANIASSVR------AIITGYRLSPRDATVAVMPL-YHGHglIAALLATLASGGAVLLPARGRFSAHTFWDD-IKAV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 766 NVTCLHFVPTMLTAFLEAPSAKRtlaeagfgSGEQQRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVT- 844
Cdd:PRK05852 267 GATWYTAVPTIHQILLERAATEP--------SGRKPAALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQVTt 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 845 ----FWDSSQNPECSTVPIGQPVwNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFIldnatgERLYR 920
Cdd:PRK05852 339 tqieGIGQTENPVVSTGLVGRST-GAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFT------DGWLR 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 921 TGDLaewnltatnqepGTLAKNprGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVL-----LYTKTpepaL 995
Cdd:PRK05852 412 TGDL------------GSLSAA--GDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFgvpdqLYGEA----V 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 503164607 996 TAFLEIGDVSETERNRIVAQarqhCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQ 1054
Cdd:PRK05852 474 AAVIVPRESAPPTAEELVQF----CRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
490-1046 |
9.18e-22 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 101.28 E-value: 9.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 490 KTLLQRFQDALTRYPNEPALYACApdeDGTLSPQSpqayefsqvLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGL 569
Cdd:PRK13295 24 RTINDDLDACVASCPDKTAVTAVR---LGTGAPRR---------FTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWW 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 570 eQYIALY-AALYAGFVYVPILPDLPAERVSSMMEDAQCSALVY-----GSGLSPIAeAELKPAntqsLCGLQQLEFTSLT 643
Cdd:PRK13295 92 -EFTVLYlACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVpktfrGFDHAAMA-RRLRPE----LPALRHVVVVGGD 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 644 DPVGEPLNLVDvPEAKTFPGIGTAL-------DDTAYILFTSGSTGRPKGVAISH-------RSIDNRLRWQQSQIPVGA 709
Cdd:PRK13295 166 GADSFEALLIT-PAWEQEPDAPAILarlrpgpDDVTQLIYTSGTTGEPKGVMHTAntlmaniVPYAERLGLGADDVILMA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 710 STqdragdrILHKTpiSFdvhVWELYWPLQEGAAVVIaapDGHRDPAYLARVIAEQNVTclhFvpTML-TAFLEapsakr 788
Cdd:PRK13295 245 SP-------MAHQT--GF---MYGLMMPVMLGATAVL---QDIWDPARAAELIRTEGVT---F--TMAsTPFLT------ 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 789 TLAEAGFGSGEQQRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTE-AAVDVTFWDSSqnPECSTVPIGQPVWNTQ 867
Cdd:PRK13295 299 DLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTEnGAVTLTKLDDP--DERASTTDGCPLPGVE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 868 TRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAqafilDNATGerLYRTGDLAEwnltatnqepgtlaKNPRGVI 947
Cdd:PRK13295 377 VRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG-----TDADG--WFDTGDLAR--------------IDADGYI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 948 LYRGRTDHQVKLHGQRLELGDIETtlshvegvhsavvLLYtKTPEPALTAFLEIGDVSETERNRIVAQARQHCENTLPD- 1026
Cdd:PRK13295 436 RISGRSKDVIIRGGENIPVVEIEA-------------LLY-RHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEm 501
|
570 580 590
....*....|....*....|....*....|..
gi 503164607 1027 ------------YMVPRLwHTTAQFPVSPSGK 1046
Cdd:PRK13295 502 veflkaqkvakqYIPERL-VVRDALPRTPSGK 532
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
534-1052 |
1.17e-21 |
|
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: 99.48 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVygs 613
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 glspiaeaelkpantqslcglqqleftsltdpvgeplnlvdvpeaktfpgIGTALDDTAYILFTSGSTGRPKGVAISHRS 693
Cdd:cd05935 79 --------------------------------------------------VGSELDDLALIPYTSGTTGLPKGCMHTHFS 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IdnrlrWQQSQIPVGASTQDrAGDRILHKTPIsfdVHVWE----LYWPLQEGAAVVIAApdgHRDPAYLARVIAEQNVTC 769
Cdd:cd05935 109 A-----AANALQSAVWTGLT-PSDVILACLPL---FHVTGfvgsLNTAVYVGGTYVLMA---RWDRETALELIEKYKVTF 176
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 770 LHFVPTMLTAFLEAPS-AKRTLAeagfgsgeqqrHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTFwDS 848
Cdd:cd05935 177 WTNIPTMLVDLLATPEfKTRDLS-----------SLKVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHT-NP 244
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 849 SQNPECSTvpIGQPVWNTQTRILD-QALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNatGERLYRTGDLAew 927
Cdd:cd05935 245 PLRPKLQC--LGIP*FGVDARVIDiETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK--GRRFFRTGDLG-- 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 928 nltatnqepgtlAKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLlytKTPEP----ALTAFLEI-- 1001
Cdd:cd05935 319 ------------YMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHPAI*EVCVI---SVPDErvgeEVKAFIVLrp 383
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 503164607 1002 ---GDVSETErnrIVAQARQHCENtlpdYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd05935 384 eyrGKVTEED---IIEWAREQMAA----YKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
532-924 |
1.34e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 100.50 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVY 611
Cdd:PRK07470 31 RSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMIC 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 GSGLSPIAEAelkpantqslCGLQQLEFTSLTdPVGEPLNLVDVpEAKTFPGIGTAL-------DDTAYILFTSGSTGRP 684
Cdd:PRK07470 111 HADFPEHAAA----------VRAASPDLTHVV-AIGGARAGLDY-EALVARHLGARVanaavdhDDPCWFFFTSGTTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 685 KGVAISHRS----IDNRLrwqQSQIPvgASTQDragDRILHKTPISFDVHVWELywpLQ--EGAAVVIAAPDgHRDPAYL 758
Cdd:PRK07470 179 KAAVLTHGQmafvITNHL---ADLMP--GTTEQ---DASLVVAPLSHGAGIHQL---CQvaRGAATVLLPSE-RFDPAEV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 759 ARVIAEQNVTCLHFVPTMLTAFLEAPSAkrtlaeagfgsgEQQRH--VRYLICSGEAL-QKDQILsAHNIMGVYPLNLYG 835
Cdd:PRK07470 247 WALVERHRVTNLFTVPTILKMLVEHPAV------------DRYDHssLRYVIYAGAPMyRADQKR-ALAKLGKVLVQYFG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 836 PTEAAVDVT-----FWDSSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFIl 910
Cdd:PRK07470 314 LGEVTGNITvlppaLHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFR- 392
|
410
....*....|....
gi 503164607 911 dnatgERLYRTGDL 924
Cdd:PRK07470 393 -----DGWFRTGDL 401
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
532-1053 |
3.25e-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: 98.69 E-value: 3.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVyvPILPDlPAERVSSMmedAQCsalvy 611
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAV--PVLID-PGMGRKNL---KQC----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 gsglspIAEAElkpantqslcglqqleftsltdpvgeplnlvdvPEAktFPGIGTAlDDTAYILFTSGSTGRPKGVAISH 691
Cdd:cd05910 70 ------LQEAE---------------------------------PDA--FIGIPKA-DEPAAILFTSGSTGTPKGVVYRH 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 692 RSIdnrlrwqQSQIPVGASTQD-RAGDRILHKTPIsfdvhvWELYWPLQeGAAVVIAAPDGHR----DPAYLARVIAEQN 766
Cdd:cd05910 108 GTF-------AAQIDALRQLYGiRPGEVDLATFPL------FALFGPAL-GLTSVIPDMDPTRparaDPQKLVGAIRQYG 173
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 767 VTCLHFVPTMLtafleapsakRTLAEAGFGSGEQQRHVRYLICSGEALQKDQILSAHNIM--GVYPLNLYGPTEAAVDVT 844
Cdd:cd05910 174 VSIVFGSPALL----------ERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKMLsdEAEILTPYGATEALPVSS 243
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 845 FWDSSQNPECSTVP-------IGQPVWNTQTRILDQALQPI---------PPGFVGELYLSGAQLAAGYQNNPEATAQAF 908
Cdd:cd05910 244 IGSRELLATTTAATsggagtcVGRPIPGVRVRIIEIDDEPIaewddtlelPRGEIGEITVTGPTVTPTYVNRPVATALAK 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 909 ILDNATGERlYRTGDLaewnltatnqepGTLakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGV-HSAVVLLY 987
Cdd:cd05910 324 IDDNSEGFW-HRMGDL------------GYL--DDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVrRSALVGVG 388
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 988 TK-TPEPALTafLEIGDVSETERNRIVAQARQHCENTLPDYMVPR-LWHTtaQFPVSP--SGKTDRKNLA 1053
Cdd:cd05910 389 KPgCQLPVLC--VEPLPGTITPRARLEQELRALAKDYPHTQRIGRfLIHP--SFPVDIrhNAKIFREKLA 454
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
535-1054 |
6.61e-21 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 98.67 E-value: 6.61e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 535 TYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEdaQCSALVYgsg 614
Cdd:PRK06087 51 TYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWVLN--KCQAKMF--- 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 615 LSPIAEAELKPAN-----TQSLCGLQQLEFTSLTDPVGEPLNLVDVPEaKTFP---GIGTALDDTAYILFTSGSTGRPKG 686
Cdd:PRK06087 126 FAPTLFKQTRPVDlilplQNQLPQLQQIVGVDKLAPATSSLSLSQIIA-DYEPlttAITTHGDELAAVLFTSGTEGLPKG 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 687 VAISHRSIdnrLRWQQSQIPVGASTQDragDRILHKTPISFDVHVWE-LYWPLQEGAAVVIAApdgHRDPAYLARVIAEQ 765
Cdd:PRK06087 205 VMLTHNNI---LASERAYCARLNLTWQ---DVFMMPAPLGHATGFLHgVTAPFLIGARSVLLD---IFTPDACLALLEQQ 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 766 NVTCLH----FVPTMLTAFLEAPSAKRTLaeagfgsgeqqrhvRYLICSGEALQKDQILSAHNiMGVYPLNLYGPTEAAv 841
Cdd:PRK06087 276 RCTCMLgatpFIYDLLNLLEKQPADLSAL--------------RFFLCGGTTIPKKVARECQQ-RGIKLLSVYGSTESS- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 842 dvtfwdssqnPEcSTVPIGQPV-WNTQT----------RILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAfiL 910
Cdd:PRK06087 340 ----------PH-AVVNLDDPLsRFMHTdgyaaagveiKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA--L 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 911 DNatgERLYRTGDLaewnltATNQEPGTLAKNPRGV-ILYRGrtdhqvklhGQRLELGDIETTLSHVEGVHSAVVL---- 985
Cdd:PRK06087 407 DE---EGWYYSGDL------CRMDEAGYIKITGRKKdIIVRG---------GENISSREVEDILLQHPKIHDACVVampd 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503164607 986 --------LYTKTPEPALTAFLEigDVSEternrivaqarQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQ 1054
Cdd:PRK06087 469 erlgerscAYVVLKAPHHSLTLE--EVVA-----------FFSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
14-469 |
9.21e-21 |
|
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: 97.02 E-value: 9.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 14 IPLTKSAQGIYLAAIIDPKNPCYNTAEIMECPPETNLDYLREAFIQLYRENEGFR-VQTRVQTGRPEQRVIPLDEFltNL 92
Cdd:pfam00668 5 YPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRtVFIRQENGEPVQVILEERPF--EL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 93 EvlpVISLQIQEETEEQNPVPAavrgWASELISEPLRTDAGVTVRSA-VTYYGGKLWVYHSFSHVVADGFaAFNGLSR-V 170
Cdd:pfam00668 83 E---IIDISDLSESEEEEAIEA----FIQRDLQSPFDLEKGPLFRAGlFRIAENRHHLLLSMHHIIVDGV-SLGILLRdL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 171 AAIYRALSAGKPLPtvkraslmeLLR----ADHAAEH-------AREEDLALWTseqvEVLSQ--PDTSLAARSASPAPQ 237
Cdd:pfam00668 155 ADLYQQLLKGEPLP---------LPPktpyKDYAEWLqqylqseDYQKDAAYWL----EQLEGelPVLQLPKDYARPADR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 238 AL---REVLTLPDKLQRDMLEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRifgaQVPAETRALGktsaqt 314
Cdd:pfam00668 222 SFkgdRLSFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR----PSPDIERMVG------ 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 315 gtTAVNVLPV--QVSGMGSIAQALDSVK---NQYARNASHPLAR-QEDLERLAQSNDSRLFGAQINVIPFDaaLPLGAPT 388
Cdd:pfam00668 292 --MFVNTLPLriDPKGGKTFSELIKRVQedlLSAEPHQGYPFGDlVNDLRLPRDLSRHPLFDPMFSFQNYL--GQDSQEE 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 389 ENAPASVGYIHNISAGPVADMTITLRGIPgRGHTISVELDANPNLYTREHVEFHARHLQNWLEswaQAA----LEERSMD 464
Cdd:pfam00668 368 EFQLSELDLSVSSVIEEEAKYDLSLTASE-RGGGLTIKIDYNTSLFDEETIERFAEHFKELLE---QAIahpsQPLSELD 443
|
....*
gi 503164607 465 TLTTA 469
Cdd:pfam00668 444 LLSDA 448
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
520-1052 |
2.12e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 96.41 E-value: 2.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 520 LSPQSPQAYEFS--QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERV 597
Cdd:PRK09088 7 LQPQRLAAVDLAlgRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASEL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 598 SSMMEDAQCSALVYGSGLSPIaeaelkpantqslcGLQQLEFTSLTDPVgEPLNLVDVPEAKTfpgigtalDDTAYILFT 677
Cdd:PRK09088 87 DALLQDAEPRLLLGDDAVAAG--------------RTDVEDLAAFIASA-DALEPADTPSIPP--------ERVSLILFT 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 678 SGSTGRPKGVAISHRSIdnrlrwQQSQIPVGASTQDRAGDRILHKTPIsfdVHVWELYWP----LQEGAAVVIAapDGHr 753
Cdd:PRK09088 144 SGTSGQPKGVMLSERNL------QQTAHNFGVLGRVDAHSSFLCDAPM---FHIIGLITSvrpvLAVGGSILVS--NGF- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 754 DPAYLARVIAEQNVTCLHF--VPTMLTAFLEAPsakrtlaeaGFgSGEQQRHVRYLICSGEALQKDQILsAHNIMGVYPL 831
Cdd:PRK09088 212 EPKRTLGRLGDPALGITHYfcVPQMAQAFRAQP---------GF-DAAALRHLTALFTGGAPHAAEDIL-GWLDDGIPMV 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 832 NLYGPTEA------AVDVTFWDSSQNPEcstvpiGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATA 905
Cdd:PRK09088 281 DGFGMSEAgtvfgmSVDCDVIRAKAGAA------GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 906 QAFildnaTGERLYRTGDLAEwnltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLS-HVEGVHSAVV 984
Cdd:PRK09088 355 RAF-----TGDGWFRTGDIAR--------------RDADGFFWVVDRKKDMFISGGENVYPAEIEAVLAdHPGIRECAVV 415
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503164607 985 LLytktPEPALTAFLEIGDVSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:PRK09088 416 GM----ADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
521-1046 |
4.05e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 95.72 E-value: 4.05e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 521 SPQSPQAYEFSQVLTYHELDARARALAkAMLEA-GVCPGTAVGLrFHRGLEQYIAL-YAALYAGFVYVPILPDLPAERVS 598
Cdd:PRK06145 15 TPDRAALVYRDQEISYAEFHQRILQAA-GMLHArGIGQGDVVAL-LMKNSAAFLELaFAASYLGAVFLPINYRLAADEVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 599 SMMEDAQCSALVYGSGLSPIAEAELKPANTQSLCglqQLEFTSLTDPvGEPLNlvdvpeaktfPGIGTALDDTAYILFTS 678
Cdd:PRK06145 93 YILGDAGAKLLLVDEEFDAIVALETPKIVIDAAA---QADSRRLAQG-GLEIP----------PQAAVAPTDLVRLMYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 679 GSTGRPKGVAISHrsiDNrLRWQQSQ--IPVGAStqdrAGDRILHKTPIsfdVHVWELYWP----LQEGAAVVIaapdgH 752
Cdd:PRK06145 159 GTTDRPKGVMHSY---GN-LHWKSIDhvIALGLT----ASERLLVVGPL---YHVGAFDLPgiavLWVGGTLRI-----H 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 753 R--DPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRtlaeagFGSGEqqrhVRYLICSGEALQKDQILSAHNIM-GVY 829
Cdd:PRK06145 223 RefDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDR------FDLDS----LAWCIGGGEKTPESRIRDFTRVFtRAR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 830 PLNLYGPTEAAVDVTFWDSSQNPE--CSTvpiGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQA 907
Cdd:PRK06145 293 YIDAYGLTETCSGDTLMEAGREIEkiGST---GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 908 FILDnatgerLYRTGDLaewnltatnqepGTLakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLly 987
Cdd:PRK06145 370 FYGD------WFRSGDV------------GYL--DEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVI-- 427
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503164607 988 tKTPEP----ALTAFLEIGDVSETERNRIvaqaRQHCENTLPDYMVPRLWHTTAQFPVSPSGK 1046
Cdd:PRK06145 428 -GVHDDrwgeRITAVVVLNPGATLTLEAL----DRHCRQRLASFKVPRQLKVRDELPRNPSGK 485
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
532-1055 |
7.70e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 94.93 E-value: 7.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAML-EAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALv 610
Cdd:PRK06839 26 EEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVL- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 611 ygsglspIAEAELKpANTQSLCGLQQLE-FTSLTDPVG----EPLNLVDVPEaktfpgigtalDDTAYILFTSGSTGRPK 685
Cdd:PRK06839 105 -------FVEKTFQ-NMALSMQKVSYVQrVISITSLKEiedrKIDNFVEKNE-----------SASFIICYTSGTTGKPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 686 GVAISHRSidnrLRWqqSQIPVGASTQDRAGDRILHKTPIsFDVHVWELY-WP-LQEGAAVVIAapdGHRDPAYLARVIA 763
Cdd:PRK06839 166 GAVLTQEN----MFW--NALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLFaFPtLFAGGVIIVP---RKFEPTKALSMIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 764 EQNVTCLHFVPTMLTAFLEAPSAKRTlaeagfgsgeQQRHVRYLIcSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDV 843
Cdd:PRK06839 236 KHKVTVVMGVPTIHQALINCSKFETT----------NLQSVRWFY-NGGAPCPEELMREFIDRGFLFGQGFGMTETSPTV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 844 tFWDSSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAqafildNATGERLYRTGD 923
Cdd:PRK06839 305 -FMLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATE------ETIQDGWLCTGD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 924 LAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVL--LYTKTPEPALTAFLEI 1001
Cdd:PRK06839 378 LARV--------------DEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVgrQHVKWGEIPIAFIVKK 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 503164607 1002 GDVSETErnrivAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQI 1055
Cdd:PRK06839 444 SSSVLIE-----KDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
532-1052 |
1.86e-19 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 93.59 E-value: 1.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVY 611
Cdd:PRK08008 36 RRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 GSGLSPIAEAELKPANTQslcgLQQLEFTSLTDPVGEP------LNLVDVPEAKTFPGIGTalDDTAYILFTSGSTGRPK 685
Cdd:PRK08008 116 SAQFYPMYRQIQQEDATP----LRHICLTRVALPADDGvssftqLKAQQPATLCYAPPLST--DDTAEILFTSGTTSRPK 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 686 GVAISHRSidnrLR-------WQqsqipvgasTQDRAGDRILHKTPiSF--DVHVWELYWPLQEGAAVVIAApdghrdpA 756
Cdd:PRK08008 190 GVVITHYN----LRfagyysaWQ---------CALRDDDVYLTVMP-AFhiDCQCTAAMAAFSAGATFVLLE-------K 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 757 YLARV----IAEQNVTCLHFVPTML-TAFLEAPSAkrtlaeagfgsGEQQRHVR----YLICSGEalQKDQILSAhniMG 827
Cdd:PRK08008 249 YSARAfwgqVCKYRATITECIPMMIrTLMVQPPSA-----------NDRQHCLRevmfYLNLSDQ--EKDAFEER---FG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 828 VYPLNLYGPTEAAV--------DVTFWDSsqnpecstvpIGQPVWNTQTRILDQALQPIPPGFVGELYLSGA---QLAAG 896
Cdd:PRK08008 313 VRLLTSYGMTETIVgiigdrpgDKRRWPS----------IGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 897 YQNNPEATAQAFildnaTGERLYRTGDlaewnlTATNQEpgtlaknpRGVILYRGRTDHQVKLHGQRLELGDIETTL-SH 975
Cdd:PRK08008 383 YYLDPKATAKVL-----EADGWLHTGD------TGYVDE--------EGFFYFVDRRCNMIKRGGENVSCVELENIIaTH 443
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503164607 976 VEGVHSAVVLLYTKTPEPALTAFLEIGDVSETERNRIVAqarqHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:PRK08008 444 PKIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFA----FCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
531-1046 |
3.47e-19 |
|
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: 93.41 E-value: 3.47e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 531 SQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALV 610
Cdd:cd17634 82 SRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLI 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 611 YGSG---------LSPIAEAELKPANT--QSLCGLQQLEFTSLTDPvGEPLNLVDVPEAKT--FPGIGTALDDTAYILFT 677
Cdd:cd17634 162 TADGgvragrsvpLKKNVDDALNPNVTsvEHVIVLKRTGSDIDWQE-GRDLWWRDLIAKASpeHQPEAMNAEDPLFILYT 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 678 SGSTGRPKGVAISHRSIDNRLRWQQSQI-PVGAstqdraGDRILHKTPISFDV-HVWELYWPLQEGAAVVI--AAPDgHR 753
Cdd:cd17634 241 SGTTGKPKGVLHTTGGYLVYAATTMKYVfDYGP------GDIYWCTADVGWVTgHSYLLYGPLACGATTLLyeGVPN-WP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 754 DPAYLARVIAEQNVTCLHFVPTMLTAFleAPSAKRTLAEAGFGSgeqqrhVRYLICSGEALQKDQILSAHNIMGVYP--- 830
Cdd:cd17634 314 TPARMWQVVDKHGVNILYTAPTAIRAL--MAAGDDAIEGTDRSS------LRILGSVGEPINPEAYEWYWKKIGKEKcpv 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 831 LNLYGPTE---AAVDVTFWDSSQNPECSTVPigqpVWNTQTRILDQALQPIPPGFVGELYLSGA---QLAAGYQNNPEAT 904
Cdd:cd17634 386 VDTWWQTEtggFMITPLPGAIELKAGSATRP----VFGVQPAVVDNEGHPQPGGTEGNLVITDPwpgQTRTLFGDHERFE 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 905 AQAFildnATGERLYRTGDLAewnltatnqepgtlAKNPRGVILYRGRTDHQVKLHGQRLELGDIETTL-SHVEGVHSAV 983
Cdd:cd17634 462 QTYF----STFKGMYFSGDGA--------------RRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLvAHPKVAEAAV 523
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503164607 984 VLLYTKTPEPALTAF--LEIGDV-SETERNRIVAQARQHCENTLpdymVPRLWHTTAQFPVSPSGK 1046
Cdd:cd17634 524 VGIPHAIKGQAPYAYvvLNHGVEpSPELYAELRNWVRKEIGPLA----TPDVVHWVDSLPKTRSGK 585
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
535-1053 |
3.89e-19 |
|
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: 92.16 E-value: 3.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 535 TYHELDARARALAKAMLEAGVC-PGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQcsalvygs 613
Cdd:cd05958 12 TYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKAR-------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 glspiaeaelkpaNTQSLCGLQQleftsltdpvgeplnlvdvpeaktfpgigTALDDTAYILFTSGSTGRPKGVAISHRs 693
Cdd:cd05958 84 -------------ITVALCAHAL-----------------------------TASDDICILAFTSGTTGAPKATMHFHR- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 iDNRLRWQQSQIPVGASTQDragDRILHKTPISFDVHV-WELYWPLQEGAAVVIAApdgHRDPAYLARVIAEQNVTCLHF 772
Cdd:cd05958 121 -DPLASADRYAVNVLRLRED---DRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLE---EATPDLLLSAIARYKPTVLFT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 773 VPTMLTAFLEAPSAkrtlaeagfgSGEQQRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAavdVTFWDSSQNP 852
Cdd:cd05958 194 APTAYRAMLAHPDA----------AGPDLSSLRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEM---FHIFISARPG 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 853 ECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGaqlAAGYQNNPEATAQAFILDnatgerlyrtgdlaEWNLTAT 932
Cdd:cd05958 261 DARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQG--------------GWNITGD 323
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 933 nqepgTLAKNPRGVILYRGRTDHQVKLHGQRLELGDIETTL-SHVEGVHSAVVllytKTPEPA----LTAFLeIGDVSET 1007
Cdd:cd05958 324 -----TYSRDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLlQHPAVAECAVV----GHPDESrgvvVKAFV-VLRPGVI 393
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 503164607 1008 ERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLA 1053
Cdd:cd05958 394 PGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQRFALR 439
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
532-1045 |
4.80e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 92.50 E-value: 4.80e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVY 611
Cdd:PRK06164 34 RPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHILGRGRARWLVV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 GSGLSPI----AEAELKPANTQSLCGLQQLEFTS--LTDPV-GEPLNLVDVPEAKTFPGIGT--ALDDTAYILFT-SGST 681
Cdd:PRK06164 114 WPGFKGIdfaaILAAVPPDALPPLRAIAVVDDAAdaTPAPApGARVQLFALPDPAPPAAAGEraADPDAGALLFTtSGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 682 GRPKGVAISHRSIDNRLRwqqsqiPVGASTQDRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAPdghRDPAYLARV 761
Cdd:PRK06164 194 SGPKLVLHRQATLLRHAR------AIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPV---FDAARTARA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 762 IAEQNVTCLHFVPTMLTAFLEAPSAKRTLAEA---GFGSgeqqrhvrYLICSGEALQKDQIlsahniMGVYPLNLYGPTE 838
Cdd:PRK06164 265 LRRHRVTHTFGNDEMLRRILDTAGERADFPSArlfGFAS--------FAPALGELAALARA------RGVPLTGLYGSSE 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 839 AAVDVTFWDSSQNPECSTVPIGQPVW-NTQTRILD-QALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFildnaTGE 916
Cdd:PRK06164 331 VQALVALQPATDPVSVRIEGGGRPASpEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDATARAL-----TDD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 917 RLYRTGDLAewnltatnqepgtLAKNPRGVIlYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTPEPALT 996
Cdd:PRK06164 406 GYFRTGDLG-------------YTRGDGQFV-YQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 503164607 997 AFLEIGDVSETERNRIVAqarqHCENTLPDYMVPRLWHTTAQFPVSPSG 1045
Cdd:PRK06164 472 AFVIPTDGASPDEAGLMA----ACREALAGFKVPARVQVVEAFPVTESA 516
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
470-1052 |
7.90e-19 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 92.04 E-value: 7.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 470 LPHEVEllesfnATAHPIEYKTLLQRFQDALTRYPNEPALYacapdedgtlspqspqayEFSQVLTYHELDARARALAkA 549
Cdd:PRK08974 9 YPADVP------AEINPDRYQSLVDMFEQAVARYADQPAFI------------------NMGEVMTFRKLEERSRAFA-A 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 550 MLEAGvcpgtavgLRFHRG---------LEQY-IALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALV----YGSGL 615
Cdd:PRK08974 64 YLQNG--------LGLKKGdrvalmmpnLLQYpIALFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVivsnFAHTL 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 616 SPIAEaelkpaNTQslcgLQQLEFTSLTD----PVGEPLNLV-----------DVPEAKTF--------------PGIgt 666
Cdd:PRK08974 136 EKVVF------KTP----VKHVILTRMGDqlstAKGTLVNFVvkyikrlvpkyHLPDAISFrsalhkgrrmqyvkPEL-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 667 ALDDTAYILFTSGSTGRPKGVAISHRSIDNRLrwqqSQIPVGASTQDRAGDRILhKTPIS----FDVHVWELYWPLQEGA 742
Cdd:PRK08974 204 VPEDLAFLQYTGGTTGVAKGAMLTHRNMLANL----EQAKAAYGPLLHPGKELV-VTALPlyhiFALTVNCLLFIELGGQ 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 743 AVVIAAPdghRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKrtlaEAGFGSgeqqrhVRYLICSGEALQKDQILSA 822
Cdd:PRK08974 279 NLLITNP---RDIPGFVKELKKYPFTAITGVNTLFNALLNNEEFQ----ELDFSS------LKLSVGGGMAVQQAVAERW 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 823 HNIMGVYPLNLYGPTEAA-------VDVTFWDSSqnpecstvpIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAA 895
Cdd:PRK08974 346 VKLTGQYLLEGYGLTECSplvsvnpYDLDYYSGS---------IGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVML 416
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 896 GYQNNPEATAQafILDNAtgerLYRTGDLAEWNltatnqEPGTLAKNPR--------GVILYRGRTDHQVKLHGQRLELG 967
Cdd:PRK08974 417 GYWQRPEATDE--VIKDG----WLATGDIAVMD------EEGFLRIVDRkkdmilvsGFNVYPNEIEDVVMLHPKVLEVA 484
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 968 DIettlshveGVHSAVvllytkTPEpALTAFLEIGDVSETERnrivaQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKT 1047
Cdd:PRK08974 485 AV--------GVPSEV------SGE-AVKIFVVKKDPSLTEE-----ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKI 544
|
....*
gi 503164607 1048 DRKNL 1052
Cdd:PRK08974 545 LRREL 549
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
532-907 |
9.70e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 91.50 E-value: 9.70e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALvy 611
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 gsglspIAEAELKPANTQSLCGLqqleftsltdPVGEPLNLVDVPEAKTFPGIGTALDDT-----------AYILFTSGS 680
Cdd:PRK08276 88 ------IVSAALADTAAELAAEL----------PAGVPLLLVVAGPVPGFRSYEEALAAQpdtpiadetagADMLYSSGT 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 681 TGRPKGV--AISHRSIDNRLrwQQSQIPVGASTQDRAGDRIL------HKTPISFDVHVwelywpLQEGAAVVIAApdgH 752
Cdd:PRK08276 152 TGRPKGIkrPLPGLDPDEAP--GMMLALLGFGMYGGPDSVYLspaplyHTAPLRFGMSA------LALGGTVVVME---K 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 753 RDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRTlaeagfgsgeqqRH----VRYLI-----CSGEAlqKDQILsah 823
Cdd:PRK08276 221 FDAEEALALIERYRVTHSQLVPTMFVRMLKLPEEVRA------------RYdvssLRVAIhaaapCPVEV--KRAMI--- 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 824 NIMGVYPLNLYGPTEAAvDVTFWDSSQ---NPecSTVpiGQPvWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNN 900
Cdd:PRK08276 284 DWWGPIIHEYYASSEGG-GVTVITSEDwlaHP--GSV--GKA-VLGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHND 357
|
....*..
gi 503164607 901 PEATAQA 907
Cdd:PRK08276 358 PEKTAAA 364
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
496-1054 |
1.11e-18 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 91.36 E-value: 1.11e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 496 FQDALTRYPNEPALYacapDEDGTLspqspqayefsqvlTYHELDARARALAKAMLEAGVCPGTAVGL--RFHRGLeqYI 573
Cdd:PRK13382 49 FAIAAQRCPDRPGLI----DELGTL--------------TWRELDERSDALAAALQALPIGEPRVVGImcRNHRGF--VE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 574 ALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIAEAEL--KPANTQSLcglqqleftSLTDPVGEPL- 650
Cdd:PRK13382 109 ALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRALadCPQATRIV---------AWTDEDHDLTv 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 651 -NLVDVPEAKTFPGIGTALDdtaYILFTSGSTGRPKGVAISH-------RSIDNRLRWqqsqipvgastqdRAGDRILHK 722
Cdd:PRK13382 180 eVLIAAHAGQRPEPTGRKGR---VILLTSGTTGTPKGARRSGpggigtlKAILDRTPW-------------RAEEPTVIV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 723 TPIsfdVHVWELYwplQEGAAVVIAAPDGHR---DPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRTLAEAgfgsge 799
Cdd:PRK13382 244 APM---FHAWGFS---QLVLAASLACTIVTRrrfDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSG------ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 800 qqRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAvdvtfWDSSQNPE-CSTVP--IGQPVWNTQTRILDQALQ 876
Cdd:PRK13382 312 --RSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAG-----MIATATPAdLRAAPdtAGRPAEGTEIRILDQDFR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 877 PIPPGFVGELYLSGAQLAAGYQNnpeATAQAFIldnatgERLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQ 956
Cdd:PRK13382 385 EVPTGEVGTIFVRNDTQFDGYTS---GSTKDFH------DGFMASGDVGYL--------------DENGRLFVVGRDDEM 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 957 VKLHGQRLELGDIETTL-SHVEGVHSAVVLLYTKTPEPALTAFLeigdVSETERNRIVAQARQHCENTLPDYMVPRLWHT 1035
Cdd:PRK13382 442 IVSGGENVYPIEVEKTLaTHPDVAEAAVIGVDDEQYGQRLAAFV----VLKPGASATPETLKQHVRDNLANYKVPRDIVV 517
|
570
....*....|....*....
gi 503164607 1036 TAQFPVSPSGKTDRKNLAQ 1054
Cdd:PRK13382 518 LDELPRGATGKILRRELQA 536
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
482-925 |
1.16e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 91.41 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 482 ATAHPIEYKTLLQRFQDALTRYPNEPALYACAPDedgtlspqspqayefsQVLTYHELDARARALAKAMLEAGVCPGTAV 561
Cdd:PRK08315 8 PTDVPLLEQTIGQLLDRTAARYPDREALVYRDQG----------------LRWTYREFNEEVDALAKGLLALGIEKGDRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 562 GLRFHRGLEQYIALYAALYAGFVYVPIlpdLPAERVSSM---MEDAQCSALVygsglspIAEA-----------ELKP-A 626
Cdd:PRK08315 72 GIWAPNVPEWVLTQFATAKIGAILVTI---NPAYRLSELeyaLNQSGCKALI-------AADGfkdsdyvamlyELAPeL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 627 NTQSLCGLQQLEFTSL-------------TDPVGEPLNLVDVPEAKTFPGIGTAL--DDTAYILFTSGSTGRPKGVAISH 691
Cdd:PRK08315 142 ATCEPGQLQSARLPELrrviflgdekhpgMLNFDELLALGRAVDDAELAARQATLdpDDPINIQYTSGTTGFPKGATLTH 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 692 RSIDNRLRWqqsqipVGASTQDRAGDRILHKTPisfdvhvweLYW----------PLQEGAAVVIAAPDghRDPAYLARV 761
Cdd:PRK08315 222 RNILNNGYF------IGEAMKLTEEDRLCIPVP---------LYHcfgmvlgnlaCVTHGATMVYPGEG--FDPLATLAA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 762 IAEQNVTCLHFVPTMLTAFLEAP-------SAKRTLAEAgfGSgeqqrhvrylICSGEALQK-------DQILSAhnimg 827
Cdd:PRK08315 285 VEEERCTALYGVPTMFIAELDHPdfarfdlSSLRTGIMA--GS----------PCPIEVMKRvidkmhmSEVTIA----- 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 828 vyplnlYGPTEAAvDVTFWDSSQNPE---CSTVPIGQPvwNTQTRILDQAL-QPIPPGFVGELYLSGAQLAAGYQNNPEA 903
Cdd:PRK08315 348 ------YGMTETS-PVSTQTRTDDPLekrVTTVGRALP--HLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEK 418
|
490 500
....*....|....*....|..
gi 503164607 904 TAQAfiLDnatGERLYRTGDLA 925
Cdd:PRK08315 419 TAEA--ID---ADGWMHTGDLA 435
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
534-1046 |
1.24e-18 |
|
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: 90.82 E-value: 1.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALvygs 613
Cdd:cd12118 30 YTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVL---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 glspIAEAELkpantqslcglQQLEFTSLTDPVGEPLNLVDvpEaktfpgigtalDDTAYILFTSGSTGRPKGVAISHR- 692
Cdd:cd12118 106 ----FVDREF-----------EYEDLLAEGDPDFEWIPPAD--E-----------WDPIALNYTSGTTGRPKGVVYHHRg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 693 ----SIDNRLRWQQSQIPVgastqdragdrILHKTPIsFDVHVWELYWPLQEGAAVVIAAPdgHRDPAYLARVIAEQNVT 768
Cdd:cd12118 158 aylnALANILEWEMKQHPV-----------YLWTLPM-FHCNGWCFPWTVAAVGGTNVCLR--KVDAKAIYDLIEKHKVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 769 clHF--VPTMLTAFLEAPSAKRtlaeagfGSGEQQRHVryliCSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTF- 845
Cdd:cd12118 224 --HFcgAPTVLNMLANAPPSDA-------RPLPHRVHV----MTAGAPPPAAVLAKMEELGFDVTHVYGLTETYGPATVc 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 846 -----WDSSQNPECSTVPIGQPVWN---TQTRILD-QALQPIPPG--FVGELYLSGAQLAAGYQNNPEATAQAFildnAT 914
Cdd:cd12118 291 awkpeWDELPTEERARLKARQGVRYvglEEVDVLDpETMKPVPRDgkTIGEIVFRGNIVMKGYLKNPEATAEAF----RG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 915 GerLYRTGDLAEWNltatnqepgtlaknPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLlytKTPEPA 994
Cdd:cd12118 367 G--WFHSGDLAVIH--------------PDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVV---ARPDEK 427
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 503164607 995 L----TAFLEIGDVSETERNRIVAqarqHCENTLPDYMVPRlwhtTAQF---PVSPSGK 1046
Cdd:cd12118 428 WgevpCAFVELKEGAKVTEEEIIA----FCREHLAGFMVPK----TVVFgelPKTSTGK 478
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
533-1054 |
1.47e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 90.43 E-value: 1.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 533 VLTYHELDARARALAKAMLEAGvcpgtAVGLRFHRGLEQYIALYAALYAGFVYVPILPDL-PAERvSSMMEDaqcsalvy 611
Cdd:PRK07787 25 VLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSgVAER-RHILAD-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 gSGlspiAEAELKPANTqslcglqqleftsltDPVGEPLNLVDVPEAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISH 691
Cdd:PRK07787 91 -SG----AQAWLGPAPD---------------DPAGLPHVPVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPKGVVLSR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 692 RSIDNRL-----RWQQSqipvgastqdrAGDRILHKTPIsFDVH--VWELYWPLQEGAAVVIAapdGHRDPAYLARVIAE 764
Cdd:PRK07787 151 RAIAADLdalaeAWQWT-----------ADDVLVHGLPL-FHVHglVLGVLGPLRIGNRFVHT---GRPTPEAYAQALSE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 765 qNVTCLHFVPTMLTAFLEAPSAKRTLAEAgfgsgeqqrhvRYLIcSGEAlqkdqILSAH------NIMGVYPLNLYGPTE 838
Cdd:PRK07787 216 -GGTLYFGVPTVWSRIAADPEAARALRGA-----------RLLV-SGSA-----ALPVPvfdrlaALTGHRPVERYGMTE 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 839 AAVDV-TFWDSSQNPecSTVpiGQPVWNTQTRILDQALQPIP--PGFVGELYLSGAQLAAGYQNNPEATAQAFildnaTG 915
Cdd:PRK07787 278 TLITLsTRADGERRP--GWV--GLPLAGVETRLVDEDGGPVPhdGETVGELQVRGPTLFDGYLNRPDATAAAF-----TA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 916 ERLYRTGDLAewnltatnqepgtlAKNPRGV--ILYRGRTDhQVKLHGQRLELGDIETTLSHVEGVHSAVVllyTKTPEP 993
Cdd:PRK07787 349 DGWFRTGDVA--------------VVDPDGMhrIVGRESTD-LIKSGGYRIGAGEIETALLGHPGVREAAV---VGVPDD 410
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503164607 994 AL----TAFL-EIGDVSETERNRIVAQArqhcentLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQ 1054
Cdd:PRK07787 411 DLgqriVAYVvGADDVAADELIDFVAQQ-------LSVHKRPREVRFVDALPRNAMGKVLKKQLLS 469
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
492-1057 |
3.27e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 89.64 E-value: 3.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 492 LLQRFQdaLTryPNEPALYacapDEDGTLSpqspqayeFSQVltYHELDARARALAKAmleaGVCPGTAVGLRFHRGLEQ 571
Cdd:PRK03640 8 LKQRAF--LT--PDRTAIE----FEEKKVT--------FMEL--HEAVVSVAGKLAAL----GVKKGDRVALLMKNGMEM 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 572 YIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYgsglSPIAEAELKpantqslcGLQQLEFTSLtdpvgEPLN 651
Cdd:PRK03640 66 ILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLIT----DDDFEAKLI--------PGISVKFAEL-----MNGP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 652 LVDVPEAKTFPgigtaLDDTAYILFTSGSTGRPKGV----------AIShrsidnrlrwqqSQIPVGASTQDR------- 714
Cdd:PRK03640 129 KEEAEIQEEFD-----LDEVATIMYTSGTTGKPKGViqtygnhwwsAVG------------SALNLGLTEDDCwlaavpi 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 715 ---AGDRILHKTPIsfdvhvwelYwplqeGAAVVIAApdgHRDPAYLARVIAEQNVTCLHFVPTMLtafleapsaKRTLA 791
Cdd:PRK03640 192 fhiSGLSILMRSVI---------Y-----GMRVVLVE---KFDAEKINKLLQTGGVTIISVVSTML---------QRLLE 245
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 792 EagFGSGEQQRHVRYLICSGEALQKD--QILSAHNImgvyPL-NLYGPTEAAvdvtfwdsSQ----NPECSTVPI---GQ 861
Cdd:PRK03640 246 R--LGEGTYPSSFRCMLLGGGPAPKPllEQCKEKGI----PVyQSYGMTETA--------SQivtlSPEDALTKLgsaGK 311
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 862 PVWNTQTRILDQaLQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFIlDNatgerLYRTGDLAEWNltatnqEPGTL-A 940
Cdd:PRK03640 312 PLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQ-DG-----WFKTGDIGYLD------EEGFLyV 378
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 941 KNPRGVILYRGrtdhqvklhGQRLELGDIETTLSHVEGVHSAVVL-----LYTKTPepalTAFLeIGDVSETErnrivAQ 1015
Cdd:PRK03640 379 LDRRSDLIISG---------GENIYPAEIEEVLLSHPGVAEAGVVgvpddKWGQVP----VAFV-VKSGEVTE-----EE 439
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 503164607 1016 ARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIEF 1057
Cdd:PRK03640 440 LRHFCEEKLAKYKVPKRFYFVEELPRNASGKLLRHELKQLVE 481
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
519-1049 |
4.53e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 89.86 E-value: 4.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 519 TLSPQSPQAYEFSQVLTYHELDARARALAKAMLEAGVCPGTAV---GLRFHRGLEqyiALYAALYAGFVYVPILPDLPAE 595
Cdd:PLN02860 18 TLRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVaiaALNSDLYLE---WLLAVACAGGIVAPLNYRWSFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 596 RVSSMMEDAQCSALVYGSGLSPIAEaELKPANTQSLCGLQQLEFTSlTDPVGEPLNLVDVPEAKTfPGIGTAL------- 668
Cdd:PLN02860 95 EAKSAMLLVRPVMLVTDETCSSWYE-ELQNDRLPSLMWQVFLESPS-SSVFIFLNSFLTTEMLKQ-RALGTTEldyawap 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAISHRSIdnrlrWQQS--QIPVGASTQDragDRILHKTPIsfdVHVWELYWP---LQEGAA 743
Cdd:PLN02860 172 DDAVLICFTSGTTGRPKGVTISHSAL-----IVQSlaKIAIVGYGED---DVYLHTAPL---CHIGGLSSAlamLMVGAC 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 744 VVIaAPDGHRDPAYlaRVIAEQNVTCLHFVPTMLtAFLEAPSAKRtlaeagfGSGEQQRHVRYLICSGEALQKDQILSAH 823
Cdd:PLN02860 241 HVL-LPKFDAKAAL--QAIKQHNVTSMITVPAMM-ADLISLTRKS-------MTWKVFPSVRKILNGGGSLSSRLLPDAK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 824 NImgvYP----LNLYGPTEAAVDVTF--------------------WDSSQNPECSTVPIGQPVWNTQTRIldqalQPIP 879
Cdd:PLN02860 310 KL---FPnaklFSAYGMTEACSSLTFmtlhdptlespkqtlqtvnqTKSSSVHQPQGVCVGKPAPHVELKI-----GLDE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 880 PGFVGELYLSGAQLAAGYQNNPEATA----QAFILDnatgerlyrTGDLaewnltatnqepGTLAKNprGVILYRGRTDH 955
Cdd:PLN02860 382 SSRVGRILTRGPHVMLGYWGQNSETAsvlsNDGWLD---------TGDI------------GWIDKA--GNLWLIGRSND 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 956 QVKLHGQRLELGDIETTLSHVEGVHSAVVLlytKTPEPALT----AFLEIGD-----VSETE---RNRIVAQA--RQHC- 1020
Cdd:PLN02860 439 RIKTGGENVYPEEVEAVLSQHPGVASVVVV---GVPDSRLTemvvACVRLRDgwiwsDNEKEnakKNLTLSSEtlRHHCr 515
|
570 580 590
....*....|....*....|....*....|..
gi 503164607 1021 ENTLPDYMVPRL---WHTtaQFPVSPSGKTDR 1049
Cdd:PLN02860 516 EKNLSRFKIPKLfvqWRK--PFPLTTTGKIRR 545
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
486-926 |
5.53e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 89.45 E-value: 5.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 486 PIEYKTLLQRFQDALTRYPNEPALYAcapdedgtlspqSPQAYEFsqvlTYHELDARARALAKAMLEAGVCPGTAVGLRF 565
Cdd:PRK12583 14 PLLTQTIGDAFDATVARFPDREALVV------------RHQALRY----TWRQLADAVDRLARGLLALGVQPGDRVGIWA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 566 HRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGS------------GLSP-IAEAELKPANTQSLC 632
Cdd:PRK12583 78 PNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADafktsdyhamlqELLPgLAEGQPGALACERLP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 633 GLQQLEFTSLTDPVG-----EPLNLVDVPEAKTFPGIGTAL--DDTAYILFTSGSTGRPKGVAISHRSIDNRLRWqqsqi 705
Cdd:PRK12583 158 ELRGVVSLAPAPPPGflawhELQARGETVSREALAERQASLdrDDPINIQYTSGTTGFPKGATLSHHNILNNGYF----- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 706 pVGASTQDRAGDRILHKTPI--SFDVHVWELYWpLQEGAAVVIaaPDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEA 783
Cdd:PRK12583 233 -VAESLGLTEHDRLCVPVPLyhCFGMVLANLGC-MTVGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTMFIAELDH 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 784 P-------SAKRTLAEAGfgsgeqqrhvryLICSGEALQK--DQILSAHNIMGvyplnlYGPTEAAvDVTFWDSSQNP-E 853
Cdd:PRK12583 309 PqrgnfdlSSLRTGIMAG------------APCPIEVMRRvmDEMHMAEVQIA------YGMTETS-PVSLQTTAADDlE 369
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503164607 854 CSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFildnaTGERLYRTGDLAE 926
Cdd:PRK12583 370 RRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESI-----DEDGWMHTGDLAT 437
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
673-1049 |
6.74e-18 |
|
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: 86.31 E-value: 6.74e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 673 YILFTSGSTGRPKGVAISHRSidnrlrWQQSQIPVGASTQDRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIaapDGH 752
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERS------WIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 753 RDPAYLARVIAEQNVTCLHFVPTMLTAFLeapsakRTlaeagfgsGEQQRHVRYLICSGEALQKDqilSAHNIMGVYP-L 831
Cdd:cd17633 75 FNPKSWIRKINQYNATVIYLVPTMLQALA------RT--------LEPESKIKSIFSSGQKLFES---TKKKLKNIFPkA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 832 NL---YGPTEAA-VDVTFWDSSQNPEcstvPIGQPVWNTQTRILDQAlqpipPGFVGELYLSGAQLAAGYQNNPEATAQA 907
Cdd:cd17633 138 NLiefYGTSELSfITYNFNQESRPPN----SVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDG 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 908 FildnatgerlYRTGDLAEWnltatnQEPGTLaknprgviLYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLY 987
Cdd:cd17633 209 W----------MSVGDIGYV------DEEGYL--------YLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGI 264
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503164607 988 TKTPEPALTAFLEIGDvSETERnrivaQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDR 1049
Cdd:cd17633 265 PDARFGEIAVALYSGD-KLTYK-----QLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
499-1053 |
1.15e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 88.13 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 499 ALTRYPNEPALYacapDEDGTLSpqspqayefsqvltYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAA 578
Cdd:PRK13383 44 TAARWPGRTAII----DDDGALS--------------YRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 579 LYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSglspiaeaelkpantqslcglqqlEFTSLTDPVGEPLNLVDvpea 658
Cdd:PRK13383 106 GLLGADVVPISTEFRSDALAAALRAHHISTVVADN------------------------EFAERIAGADDAVAVID---- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 659 ktfPGIGTALDDTA---------YILFTSGSTGRPKGVAishrsidnrlRWQQSQIPVGAS------TQDRAGDRILHKT 723
Cdd:PRK13383 158 ---PATAGAEESGGrpavaapgrIVLLTSGTTGKPKGVP----------RAPQLRSAVGVWvtildrTRLRTGSRISVAM 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 724 PISFDVHVWELYWPLQEGAAVVIAApdgHRDP-AYLARViAEQNVTCLHFVPTMLTAFLEAPSAKRtlaeagfgSGEQQR 802
Cdd:PRK13383 225 PMFHGLGLGMLMLTIALGGTVLTHR---HFDAeAALAQA-SLHRADAFTAVPVVLARILELPPRVR--------ARNPLP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 803 HVRYLICSGEALqkDQILsAHNIMGVYP---LNLYGPTEAAVDV--TFWDSSQNPECstvpIGQPVWNTQTRILDQALQP 877
Cdd:PRK13383 293 QLRVVMSSGDRL--DPTL-GQRFMDTYGdilYNGYGSTEVGIGAlaTPADLRDAPET----VGKPVAGCPVRILDRNNRP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 878 IPPGFVGELYLSGAQLAAGYQNNpeatAQAFILDNATGerlyrTGDLaewnltatnqepGTLAKNPRGVILyrGRTDHQV 957
Cdd:PRK13383 366 VGPRVTGRIFVGGELAGTRYTDG----GGKAVVDGMTS-----TGDM------------GYLDNAGRLFIV--GREDDMI 422
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 958 KLHGQRLELGDIETTL-SHVEGVHSAVVLLYTKTPEPALTAFLEIGDVSETErnriVAQARQHCENTLPDYMVPRLWHTT 1036
Cdd:PRK13383 423 ISGGENVYPRAVENALaAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVD----AAQLRDYLKDRVSRFEQPRDINIV 498
|
570
....*....|....*..
gi 503164607 1037 AQFPVSPSGKTDRKNLA 1053
Cdd:PRK13383 499 SSIPRNPTGKVLRKELP 515
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
669-984 |
1.29e-17 |
|
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: 87.93 E-value: 1.29e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAISH-------RSIDNRLRWQQSqipvgastqdragDRILHKTPISFDV-----HVWELYW 736
Cdd:cd05908 106 DELAFIQFSSGSTGDPKGVMLTHenlvhnmFAILNSTEWKTK-------------DRILSWMPLTHDMgliafHLAPLIA 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 737 PLQEgaaVVIAAPDGHRDPAYLARVIAEQNVT---CLHFVPTMLTAFLeapsaKRTLAEAGFGSgeqqrHVRYLICSGEA 813
Cdd:cd05908 173 GMNQ---YLMPTRLFIRRPILWLKKASEHKATivsSPNFGYKYFLKTL-----KPEKANDWDLS-----SIRMILNGAEP 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 814 LQKDQI------LSAHNIMGVYPLNLYGPTEAAVDVTFWD------------------------SSQNPECST-VPIGQP 862
Cdd:cd05908 240 IDYELChefldhMSKYGLKRNAILPVYGLAEASVGASLPKaqspfktitlgrrhvthgepepevDKKDSECLTfVEVGKP 319
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 863 VWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFildnaTGERLYRTGDLAewnltatnqepgtLAKN 942
Cdd:cd05908 320 IDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVF-----TDDGWLKTGDLG-------------FIRN 381
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 503164607 943 PRGVILyrGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVV 984
Cdd:cd05908 382 GRLVIT--GREKDIIFVNGQNVYPHDIERIAEELEGVELGRV 421
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
532-927 |
2.13e-17 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 87.24 E-value: 2.13e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQyIALY-AALYAGFVYVPILPDLPAERVSSMMEDAQCSALV 610
Cdd:PRK07514 27 LRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEA-LALYlATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 611 YGS----GLSPIAEAelkpantqslCGLQQLEfT-------SLTD-PVGEPLNLVDVPEAKtfpgigtalDDTAYILFTS 678
Cdd:PRK07514 106 CDPanfaWLSKIAAA----------AGAPHVE-TldadgtgSLLEaAAAAPDDFETVPRGA---------DDLAAILYTS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 679 GSTGRPKGVAISHrsiDNRL----------RWqqsqipvgastqdRAGDRILHKTPIsFDVH--------VwelywpLQE 740
Cdd:PRK07514 166 GTTGRSKGAMLSH---GNLLsnaltlvdywRF-------------TPDDVLIHALPI-FHTHglfvatnvA------LLA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 741 GAAVVIAApdgHRDPaylARVIAE-QNVTCLHFVPTMLTafleapsakRTLAEAGFGSgEQQRHVRyLICSGEA-LQKD- 817
Cdd:PRK07514 223 GASMIFLP---KFDP---DAVLALmPRATVMMGVPTFYT---------RLLQEPRLTR-EAAAHMR-LFISGSApLLAEt 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 818 ----QILSAHNImgvypLNLYGPTEAAVdvtfwdSSQNP-ECSTVP--IGQPVWNTQTRILD-QALQPIPPGFVGELYLS 889
Cdd:PRK07514 286 hrefQERTGHAI-----LERYGMTETNM------NTSNPyDGERRAgtVGFPLPGVSLRVTDpETGAELPPGEIGMIEVK 354
|
410 420 430
....*....|....*....|....*....|....*...
gi 503164607 890 GAQLAAGYQNNPEATAQAFildnaTGERLYRTGDLAEW 927
Cdd:PRK07514 355 GPNVFKGYWRMPEKTAEEF-----RADGFFITGDLGKI 387
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
483-1050 |
2.36e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 87.36 E-value: 2.36e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 483 TAHPIEY--KTLLQRFQDALTRYPNEPALYAcapdedgtlspqspqayeFSQVLTYHELDARARALAKAMLEAGVCPGTA 560
Cdd:PRK05605 23 TPHDLDYgdTTLVDLYDNAVARFGDRPALDF------------------FGATTTYAELGKQVRRAAAGLRALGVRPGDR 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 561 VGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIAEaELkPANTQ----------- 629
Cdd:PRK05605 85 VAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYTAHELEHPFEDHGARVAIVWDKVAPTVE-RL-RRTTPletivsvnmia 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 630 SLCGLQQL------------------------EFTSLTD-PVGEPLNLVDVPEaktfpgigTALDDTAYILFTSGSTGRP 684
Cdd:PRK05605 163 AMPLLQRLalrlpipalrkaraaltgpapgtvPWETLVDaAIGGDGSDVSHPR--------PTPDDVALILYTSGTTGKP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 685 KGVAISHRSIDNRLRWQQSQIPvGASTQDragDRILHKTPIsfdVHVWEL-----YWPLQEGAAVVIAAPDghrdPAYLA 759
Cdd:PRK05605 235 KGAQLTHRNLFANAAQGKAWVP-GLGDGP---ERVLAALPM---FHAYGLtlcltLAVSIGGELVLLPAPD----IDLIL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 760 RVIAEQNVTCLHFVPTMLTAFLEApSAKRTLAEAGfgsgeqqrhVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEA 839
Cdd:PRK05605 304 DAMKKHPPTWLPGVPPLYEKIAEA-AEERGVDLSG---------VRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTET 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 840 AVDVTfwdssQNPECSTVP---IGQPVWNTQTRILDQ--ALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFIldnat 914
Cdd:PRK05605 374 SPIIV-----GNPMSDDRRpgyVGVPFPDTEVRIVDPedPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFL----- 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 915 gERLYRTGDLAEwnltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGV-HSAVVLLYTKTPEP 993
Cdd:PRK05605 444 -DGWFRTGDVVV--------------MEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVeDAAVVGLPREDGSE 508
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*....
gi 503164607 994 ALTA--FLEIGDVSETErnrivaQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRK 1050
Cdd:PRK05605 509 EVVAavVLEPGAALDPE------GLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
669-973 |
3.77e-17 |
|
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: 86.26 E-value: 3.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAISHRSidnrLRWQQSQIPVGASTQdrAGDRILHKTPIsfdvhvWELYWPLQEGAAVVIAA 748
Cdd:cd17640 88 DDLATIIYTSGTTGNPKGVMLTHAN----LLHQIRSLSDIVPPQ--PGDRFLSILPI------WHSYERSAEYFIFACGC 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 749 PDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLE--------APSAKRTLAEAGFGSGEqqrhVRYLICSGEALqKDQIL 820
Cdd:cd17640 156 SQAYTSIRTLKDDLKRVKPHYIVSVPRLWESLYSgiqkqvskSSPIKQFLFLFFLSGGI----FKFGISGGGAL-PPHVD 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 821 SAHNIMGVYPLNLYGPTEAAVDVTFWDSSQNPECStvpIGQPVWNTQTRILD-QALQPIPPGFVGELYLSGAQLAAGYQN 899
Cdd:cd17640 231 TFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGS---VGRPLPGTEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYK 307
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503164607 900 NPEATAQAFILDNatgerLYRTGDLaewnltatnqepGTLAKNprGVILYRGRT-DHQVKLHGQRLELGDIETTL 973
Cdd:cd17640 308 NPEATSKVLDSDG-----WFNTGDL------------GWLTCG--GELVLTGRAkDTIVLSNGENVEPQPIEEAL 363
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
532-1048 |
7.95e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 85.71 E-value: 7.95e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVY 611
Cdd:PRK07798 27 RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLLDDSDAVALVY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 GSGLSPIAeAELKPantqSLCGLQQLefTSLTDPVGEPLNLVDVP------EAKTFPGIGTALDDTAYILFTSGSTGRPK 685
Cdd:PRK07798 107 EREFAPRV-AEVLP----RLPKLRTL--VVVEDGSGNDLLPGAVDyedalaAGSPERDFGERSPDDLYLLYTGGTTGMPK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 686 GVAISHRSI-------DNRLRWQQSQIPVGASTQDRAGD--RILhktPISFDVH---VWELYWPLQEGAAVVIaAPDGHR 753
Cdd:PRK07798 180 GVMWRQEDIfrvllggRDFATGEPIEDEEELAKRAAAGPgmRRF---PAPPLMHgagQWAAFAALFSGQTVVL-LPDVRF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 754 DPAYLARVIAEQNVTCLHFV------PtMLTAfLEAP-----SAKRTLAEAGfgsgeqqrhvryLICSGEAlqKDQILSA 822
Cdd:PRK07798 256 DADEVWRTIEREKVNVITIVgdamarP-LLDA-LEARgpydlSSLFAIASGG------------ALFSPSV--KEALLEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 823 -HNIMGVyplNLYGPTEAAV--DVTFWDSSQNPECSTVPIGQpvwntQTRILDQALQPIPPG--FVGELYLSGAqLAAGY 897
Cdd:PRK07798 320 lPNVVLT---DSIGSSETGFggSGTVAKGAVHTGGPRFTIGP-----RTVVLDEDGNPVEPGsgEIGWIARRGH-IPLGY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 898 QNNPEATAQAFILDNatGERLYRTGDLAEWnltatnQEPGTlaknprgVILYrGRTDHQVKLHGQRLELGDIETTLSHVE 977
Cdd:PRK07798 391 YKDPEKTAETFPTID--GVRYAIPGDRARV------EADGT-------ITLL-GRGSVCINTGGEKVFPEEVEEALKAHP 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 978 GVHSAVVllytktpepaltafleIGDVSETERNRIVA-------------QARQHCENTLPDYMVPRLWHTTAQFPVSPS 1044
Cdd:PRK07798 455 DVADALV----------------VGVPDERWGQEVVAvvqlregarpdlaELRAHCRSSLAGYKVPRAIWFVDEVQRSPA 518
|
....
gi 503164607 1045 GKTD 1048
Cdd:PRK07798 519 GKAD 522
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
534-1052 |
8.77e-17 |
|
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: 85.07 E-value: 8.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGS 613
Cdd:cd05920 41 LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPD 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 GLSPIAEAELkpantqslcgLQQLeftsltdpvgeplnLVDVPeaktfpgigtaldDTAYILFTSGSTGRPKGVAISHRS 693
Cdd:cd05920 121 RHAGFDHRAL----------AREL--------------AESIP-------------EVALFLLSGGTTGTPKLIPRTHND 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IDNRLRWQQSQIPVGASTQDRAGDRILHKTPIS----FDVhvwelywpLQEGAAVVIAAPDghrDPAYLARVIAEQNVTC 769
Cdd:cd05920 164 YAYNVRASAEVCGLDQDTVYLAVLPAAHNFPLAcpgvLGT--------LLAGGRVVLAPDP---SPDAAFPLIEREGVTV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 770 LHFVPTMLTAFLEAPSAKRtlaeAGFGSgeqqrhVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTFWDSS 849
Cdd:cd05920 233 TALVPALVSLWLDAAASRR----ADLSS------LRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLDDP 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 850 QNPECSTVpiGQPVW-NTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNatgerLYRTGDLAEwn 928
Cdd:cd05920 303 DEVIIHTQ--GRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDG-----FYRTGDLVR-- 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 929 ltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLlytKTPEPAL----TAFLeigdV 1004
Cdd:cd05920 374 ------------RTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVV---AMPDELLgersCAFV----V 434
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 503164607 1005 SETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd05920 435 LRDPPPSAAQLRRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
669-1055 |
1.02e-16 |
|
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: 85.44 E-value: 1.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAishRsiDN-----RLRWQQSQIPVGAstqdrAGDRILHKTPISFDV-HVWELYWPLQEGA 742
Cdd:cd05967 230 TDPLYILYTSGTTGKPKGVV---R--DNgghavALNWSMRNIYGIK-----PGDVWWAASDVGWVVgHSYIVYGPLLHGA 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 743 AVVI--AAPDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPsakrtlAEAGFGSGEQQRHVRYLICSGEALQKDQIL 820
Cdd:cd05967 300 TTVLyeGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRKED------PDGKYIKKYDLSSLRTLFLAGERLDPPTLE 373
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 821 SAHNIMGVYPLNLYGPTEaavdvTFWDSSQNP---ECSTVPIGQ---PVWNTQTRILDQALQPIPPGFVGELYLSG---A 891
Cdd:cd05967 374 WAENTLGVPVIDHWWQTE-----TGWPITANPvglEPLPIKAGSpgkPVPGYQVQVLDEDGEPVGPNELGNIVIKLplpP 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 892 QLAAGYQNNPEATAQAFiLDNATGerLYRTGDLAewnltatnqepgtlAKNPRGVILYRGRTDHQVKLHGQRLELGDIE- 970
Cdd:cd05967 449 GCLLTLWKNDERFKKLY-LSKFPG--YYDTGDAG--------------YKDEDGYLFIMGRTDDVINVAGHRLSTGEMEe 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 971 TTLSHVEGVHSAVVLLY--TKTPEPALTAFLE--IGDVSETERNRIVAQARQhcenTLPDYMVPRLWHTTAQFPVSPSGK 1046
Cdd:cd05967 512 SVLSHPAVAECAVVGVRdeLKGQVPLGLVVLKegVKITAEELEKELVALVRE----QIGPVAAFRLVIFVKRLPKTRSGK 587
|
....*....
gi 503164607 1047 TDRKNLAQI 1055
Cdd:cd05967 588 ILRRTLRKI 596
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
657-1049 |
1.69e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 84.06 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 657 EAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSidnrlrWQQSQIPVGASTQDRAGDRILhkTPISFdVHVWELYW 736
Cdd:PRK07638 131 YLPTYAPIENVQNAPFYMGFTSGSTGKPKAFLRAQQS------WLHSFDCNVHDFHMKREDSVL--IAGTL-VHSLFLYG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 737 P---LQEGAAVVIAApdgHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEApsaKRTLaeagfgsgeqqRHVRYLICSG-- 811
Cdd:PRK07638 202 AistLYVGQTVHLMR---KFIPNQVLDKLETENISVMYTVPTMLESLYKE---NRVI-----------ENKMKIISSGak 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 812 -EALQKDQILSAHNIMGVYplNLYGPTEAAVdVTFW---DSSQNPECstvpIGQPVWNTQTRILDQALQPIPPGFVGELY 887
Cdd:PRK07638 265 wEAEAKEKIKNIFPYAKLY--EFYGASELSF-VTALvdeESERRPNS----VGRPFHNVQVRICNEAGEEVQKGEIGTVY 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 888 LSGAQLAAGYQNnpeataqafildnatGERLYRTGDLAEWnltATNQEPGTLAKNprGVILYRGRTDHQVKLHGQRLELG 967
Cdd:PRK07638 338 VKSPQFFMGYII---------------GGVLARELNADGW---MTVRDVGYEDEE--GFIYIVGREKNMILFGGINIFPE 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 968 DIETTLSHVEGVHSAVVLlytKTPEPALTAFLE-IGDVSETERnrivaQARQHCENTLPDYMVPRLWHTTAQFPVSPSGK 1046
Cdd:PRK07638 398 EIESVLHEHPAVDEIVVI---GVPDSYWGEKPVaIIKGSATKQ-----QLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGK 469
|
...
gi 503164607 1047 TDR 1049
Cdd:PRK07638 470 IAR 472
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
490-1054 |
6.18e-16 |
|
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: 82.89 E-value: 6.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 490 KTLLQRFQDALTRYPNEPALYacapDEDGTLspqspqayefsqvlTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGL 569
Cdd:COG1021 25 ETLGDLLRRRAERHPDRIAVV----DGERRL--------------SYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 570 EQYIALYAALYAGFvyVPILPdLPAER---VSSMMEDAQCSALVYG---SGLSPIAEA-ELKpANTQSL-----CGLQQl 637
Cdd:COG1021 87 EFVIVFFALFRAGA--IPVFA-LPAHRraeISHFAEQSEAVAYIIPdrhRGFDYRALArELQ-AEVPSLrhvlvVGDAG- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 638 EFTSLTDPVGEPlnlVDVPEAKTFPgigtalDDTAYILFTSGSTGRPKGVAISHRsiDNRLRWQQSQIPVGAStqdrAGD 717
Cdd:COG1021 162 EFTSLDALLAAP---ADLSEPRPDP------DDVAFFQLSGGTTGLPKLIPRTHD--DYLYSVRASAEICGLD----ADT 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 718 RILHKTPISfdvHVWELYWP-----LQEGAAVVIaAPDGHRDPAYlaRVIAEQNVTCLHFVPTMLTAFLEAPSAKRtlae 792
Cdd:COG1021 227 VYLAALPAA---HNFPLSSPgvlgvLYAGGTVVL-APDPSPDTAF--PLIERERVTVTALVPPLALLWLDAAERSR---- 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 793 AGFGSgeqqrhVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTFWDSSQNPECSTVpiGQPV--WNtQTRI 870
Cdd:COG1021 297 YDLSS------LRVLQVGGAKLSPELARRVRPALGCTLQQVFGMAEGLVNYTRLDDPEEVILTTQ--GRPIspDD-EVRI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 871 LDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFildnaTGERLYRTGDLAEWnltatnqepgtlakNPRGVILYR 950
Cdd:COG1021 368 VDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAF-----TPDGFYRTGDLVRR--------------TPDGYLVVE 428
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 951 GRTDHQVKLHGQRLELGDIETTLSHVEGVHS----------------AVVLLYTKTPEP-ALTAFLeigdvseteRNRIV 1013
Cdd:COG1021 429 GRAKDQINRGGEKIAAEEVENLLLAHPAVHDaavvampdeylgerscAFVVPRGEPLTLaELRRFL---------RERGL 499
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 503164607 1014 AqarqhcentlpDYMVP-RLwHTTAQFPVSPSGKTDRKNLAQ 1054
Cdd:COG1021 500 A-----------AFKLPdRL-EFVDALPLTAVGKIDKKALRA 529
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
670-1054 |
8.16e-16 |
|
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: 80.45 E-value: 8.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 670 DTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGAstqdraGDRILHKTPIsfdVHVWELY----WpLQEGAAVV 745
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGG------GDSWLLSLPL---YHVGGLAilvrS-LLAGAELV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 746 IaapDGHRDPAYLARviAEQNVTCLHFVPTMLTAFLEAPSAKRTLAEagfgsgeqqrhVRYLICSGEALQKDqILSAHNI 825
Cdd:cd17630 71 L---LERNQALAEDL--APPGVTHVSLVPTQLQRLLDSGQGPAALKS-----------LRAVLLGGAPIPPE-LLERAAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 826 MGVYPLNLYGPTEAAVDVTFWDSSQNPECStvpIGQPVWNTQTRILDQalqpippgfvGELYLSGAQLAAGYQNNPeata 905
Cdd:cd17630 134 RGIPLYTTYGMTETASQVATKRPDGFGRGG---VGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 906 qafILDNATGERLYRTGDLAEWNLTatnqepgtlaknprGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVL 985
Cdd:cd17630 197 ---LVPEFNEDGWFTTKDLGELHAD--------------GRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVV 259
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503164607 986 lytktPEP------ALTAFLEIGDvseterNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQ 1054
Cdd:cd17630 260 -----GVPdeelgqRPVAVIVGRG------PADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRA 323
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
519-984 |
9.56e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 82.40 E-value: 9.56e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 519 TLSPQSPqAYEF-SQVLTYHELDARARALAKAMLEAGVCPGTAVGL------RFHrgleqyIALYAALYAGFVYVPILPD 591
Cdd:PRK06178 44 RERPQRP-AIIFyGHVITYAELDELSDRFAALLRQRGVGAGDRVAVflpncpQFH------IVFFGILKLGAVHVPVSPL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 592 LPAERVSSMMEDAQCSALVYGSGLSPIAEAelkpanTQSLCGLQQLEFTSLTD-----PVGEPLNLVDVP---------- 656
Cdd:PRK06178 117 FREHELSYELNDAGAEVLLALDQLAPVVEQ------VRAETSLRHVIVTSLADvlpaePTLPLPDSLRAPrlaaagaidl 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 657 ------EAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSIdnrlrwqqsqIPVGASTQDRAGDRILHKTPISFDVH 730
Cdd:PRK06178 191 lpalraCTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDM----------VYTAAAAYAVAVVGGEDSVFLSFLPE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 731 VW------ELYWPLQEGAAVVIAApdghR-DPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAK----RTLAEAGFGSge 799
Cdd:PRK06178 261 FWiagenfGLLFPLFSGATLVLLA----RwDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAeydlSSLRQVRVVS-- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 800 qqrHVRYLicSGEALQKDQILSAHNIMGVYplnlYGPTEAAVDVTF--------WDSSQNPecstVPIGQPVWNTQTRIL 871
Cdd:PRK06178 335 ---FVKKL--NPDYRQRWRALTGSVLAEAA----WGMTETHTCDTFtagfqdddFDLLSQP----VFVGLPVPGTEFKIC 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 872 D-QALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFIldnatgERLYRTGDLaewnltatnqepGTLakNPRGVILYR 950
Cdd:PRK06178 402 DfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR------DGWLHTGDI------------GKI--DEQGFLHYL 461
|
490 500 510
....*....|....*....|....*....|....*
gi 503164607 951 GRTDHQVKLHGQRLELGDIETTLS-HVEGVHSAVV 984
Cdd:PRK06178 462 GRRKEMLKVNGMSVFPSEVEALLGqHPAVLGSAVV 496
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
488-1052 |
1.02e-15 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 82.23 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 488 EYKTLLQRFQDALTRYPNEPALYAcapdedgtlspqspqayeFSQVLTYHELDARARALAKAML-EAGVCPGTAVGLRFH 566
Cdd:PRK08751 23 QFRTVAEVFATSVAKFADRPAYHS------------------FGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 567 RGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIAEAELkpANTQslcgLQQLEFTSLTDPV 646
Cdd:PRK08751 85 NCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQVI--ADTP----VKQVITTGLGDML 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 647 GEP----LNLVD------VPEAK-----------------TFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLR 699
Cdd:PRK08751 159 GFPkaalVNFVVkyvkklVPEYRingairfrealalgrkhSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 700 wQQSQIPVGASTQDRAGDRILHKTPIS--FDVHVWELYWPLQEGAAVVIAAPdghRDPAYLARVIAEQNVTCLHFVPTML 777
Cdd:PRK08751 239 -QAHQWLAGTGKLEEGCEVVITALPLYhiFALTANGLVFMKIGGCNHLISNP---RDMPGFVKELKKTRFTAFTGVNTLF 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 778 TAFLEAPSakrtLAEAGFGSgeqqrhVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAvdvtfwdssqnPECSTV 857
Cdd:PRK08751 315 NGLLNTPG----FDQIDFSS------LKMTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETS-----------PAACIN 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 858 P---------IGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFildNATGerLYRTGDLAEwn 928
Cdd:PRK08751 374 PltlkeyngsIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVM---DADG--WLHTGDIAR-- 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 929 ltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGV------------HSAVVLLYTKTPEPALT 996
Cdd:PRK08751 447 ------------MDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVlevaavgvpdekSGEIVKVVIVKKDPALT 514
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*.
gi 503164607 997 AfleigdvseternrivAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:PRK08751 515 A----------------EDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
491-925 |
1.76e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 81.54 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 491 TLLQRFQDALTRYPNEPALyACAPDEDgtlspqspqAYEFSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLE 570
Cdd:PRK07529 26 STYELLSRAAARHPDAPAL-SFLLDAD---------PLDRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPE 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 571 QYIALYAALYAGFVyVPILPDLPAERVSSMMEDAQCSALV-YGS------------------GLSPIAEAELKPAntqsL 631
Cdd:PRK07529 96 THFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKVLVtLGPfpgtdiwqkvaevlaalpELRTVVEVDLARY----L 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 632 CGLQQLEFTSLTDPVGEPLN-----LVDVPEAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRS-IDNRlrWQqsqi 705
Cdd:PRK07529 171 PGPKRLAVPLIRRKAHARILdfdaeLARQPGDRLFSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNeVANA--WL---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 706 pVGASTQDRAGDRILHKTPIsFdvHVWELY----WPLQEGAAVVIAAPDGHRDPAYLAR---VIAEQNVTCLHFVPTMLT 778
Cdd:PRK07529 245 -GALLLGLGPGDTVFCGLPL-F--HVNALLvtglAPLARGAHVVLATPQGYRGPGVIANfwkIVERYRINFLSGVPTVYA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 779 AFLEAPSAKRTLAEagfgsgeqqrhVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVdvtfwDSSQNP---ECS 855
Cdd:PRK07529 321 ALLQVPVDGHDISS-----------LRYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATC-----VSSVNPpdgERR 384
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503164607 856 TVPIGQPVWNTQTRIL-----DQALQPIPPGFVGELYLSGAQLAAGYQNnpEATAQAFILDnatgERLYRTGDLA 925
Cdd:PRK07529 385 IGSVGLRLPYQRVRVVilddaGRYLRDCAVDEVGVLCIAGPNVFSGYLE--AAHNKGLWLE----DGWLNTGDLG 453
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
533-907 |
2.14e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 80.89 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 533 VLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYG 612
Cdd:PRK13391 24 VVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 613 SGLSPIAEAELK--PANTQSLcglqqleftsLTDPVGEPLNLVDVPEA-KTFPgiGTALDDT---AYILFTSGSTGRPKG 686
Cdd:PRK13391 104 AAKLDVARALLKqcPGVRHRL----------VLDGDGELEGFVGYAEAvAGLP--ATPIADEslgTDMLYSSGTTGRPKG 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 687 V--AISHRSIDnrlrwqqSQIPVGASTQDRAGDR----------ILHKTPISFDVHVWELywplqeGAAVVIAApdgHRD 754
Cdd:PRK13391 172 IkrPLPEQPPD-------TPLPLTAFLQRLWGFRsdmvylspapLYHSAPQRAVMLVIRL------GGTVIVME---HFD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 755 PAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRTlaeagfgsgeqqrhvRYLICSGEA-----------LQKDQILSAH 823
Cdd:PRK13391 236 AEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRD---------------KYDLSSLEVaihaaapcppqVKEQMIDWWG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 824 NIMGVYplnlYGPTEaAVDVTFWDSSQ---NPecSTVpiGQPVWNTqTRILDQALQPIPPGFVGELYLSGAqLAAGYQNN 900
Cdd:PRK13391 301 PIIHEY----YAATE-GLGFTACDSEEwlaHP--GTV--GRAMFGD-LHILDDDGAELPPGEPGTIWFEGG-RPFEYLND 369
|
....*..
gi 503164607 901 PEATAQA 907
Cdd:PRK13391 370 PAKTAEA 376
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
534-1049 |
2.85e-15 |
|
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: 80.18 E-value: 2.85e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALvygs 613
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAI---- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 glspiaeaelkpantqslcglqqleFTSltDPvgeplnlvdvpeaktfpgigtalDDTAYILFTSGSTGRPKGVAISHRS 693
Cdd:cd05914 84 -------------------------FVS--DE-----------------------DDVALINYTSGTTGNSKGVMLTYRN 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IDNRLRWQQSQIPVGastqdrAGDRILHKTPISfdvHVWELYW----PLQEGAAVVIAApdghRDPAYLARVIAEQNVTC 769
Cdd:cd05914 114 IVSNVDGVKEVVLLG------KGDKILSILPLH---HIYPLTFtlllPLLNGAHVVFLD----KIPSAKIIALAFAQVTP 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 770 LHFVPTMLTAF-------------------LEAP--------SAKRTLAEAgFGSgeqqrHVRYLICSGEALQKDqILSA 822
Cdd:cd05914 181 TLGVPVPLVIEkifkmdiipkltlkkfkfkLAKKinnrkirkLAFKKVHEA-FGG-----NIKEFVIGGAKINPD-VEEF 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 823 HNIMGVYPLNLYGPTEAAVDVTFwdssqNPECSTV--PIGQPVWNTQTRILDqalqPIPPGFVGELYLSGAQLAAGYQNN 900
Cdd:cd05914 254 LRTIGFPYTIGYGMTETAPIISY-----SPPNRIRlgSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKN 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 901 PEATAQAFILDNatgerLYRTGDLaewnltatnqepGTLAKNprGVILYRGRTDHQVKL-HGQRLELGDIETTLSHVEGV 979
Cdd:cd05914 325 PEATAEAFDKDG-----WFHTGDL------------GKIDAE--GYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFV 385
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503164607 980 --------HSAVVLLYTKTPEPALTAFLEIGDVSETernrIVAQARQHCENTLPDY-MVPRLWHTTAQFPVSPSGKTDR 1049
Cdd:cd05914 386 leslvvvqEKKLVALAYIDPDFLDVKALKQRNIIDA----IKWEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
533-718 |
5.47e-15 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 80.05 E-value: 5.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 533 VLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPiLPdLPA---------ERVSSMMED 603
Cdd:PRK09192 49 ALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVP-LP-LPMgfggresyiAQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 604 AQCSALVYGSGLSPIAEAelkPANTQSLC-GLQQLEFTSLTDPVgeplnlVDVPEAKTfpgigtalDDTAYILFTSGSTG 682
Cdd:PRK09192 127 AQPAAIITPDELLPWVNE---ATHGNPLLhVLSHAWFKALPEAD------VALPRPTP--------DDIAYLQYSSGSTR 189
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 503164607 683 RPKGVAISHRSIDNRLRwqqsqipvgASTQD----RAGDR 718
Cdd:PRK09192 190 FPRGVIITHRALMANLR---------AISHDglkvRPGDR 220
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
486-1052 |
1.99e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 77.88 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 486 PIEYKTLLQRFQDALTRYPNEPALYAcapdedgtlspqspqayeFSQVLTYHELDARARALAkAML--EAGVCPGTAVGL 563
Cdd:PRK05677 20 PDEYPNIQAVLKQSCQRFADKPAFSN------------------LGKTLTYGELYKLSGAFA-AWLqqHTDLKPGDRIAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 564 RFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIAEAELKPAntqslcGLQQLEFTSLT 643
Cdd:PRK05677 81 QLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCLANMAHLAEKVLPKT------GVKHVIVTEVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 644 DPVGEPLNLV---------------DVPEA------------KTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRS-ID 695
Cdd:PRK05677 155 DMLPPLKRLLinavvkhvkkmvpayHLPQAvkfndalakgagQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNlVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 696 NRLRWQqsqiPVGASTQDRAGDRILHKTPI----SFDVHVweLYWPLQEGAAVVIAAPdghRDPAYLARVIAEQNVTCLH 771
Cdd:PRK05677 235 NMLQCR----ALMGSNLNEGCEILIAPLPLyhiyAFTFHC--MAMMLIGNHNILISNP---RDLPAMVKELGKWKFSGFV 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 772 FVPTMLTAF--------LEAPSAKRTLaeagfgSGeqqrhvrylicsGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDV 843
Cdd:PRK05677 306 GLNTLFVALcnneafrkLDFSALKLTL------SG------------GMALQLATAERWKEVTGCAICEGYGMTETSPVV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 844 TFwDSSQNPECSTvpIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFildnaTGERLYRTGD 923
Cdd:PRK05677 368 SV-NPSQAIQVGT--IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEIL-----DSDGWLKTGD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 924 LAewnltatnqepgtlAKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVH--SAVVLLYTKTPEpALTAFLei 1001
Cdd:PRK05677 440 IA--------------LIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLqcAAIGVPDEKSGE-AIKVFV-- 502
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|.
gi 503164607 1002 gdVSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:PRK05677 503 --VVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
484-790 |
2.24e-14 |
|
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: 77.92 E-value: 2.24e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 484 AHPIEYKTLLQRFQDALTRYPNEpalyacapdeDGTlspqspqayefSQVLTYHELDARARALAKAMLEAGVCPGTAVGL 563
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRWEGE----------DGT-----------SRTLTYGELLYEVKRLANGLRALGVGKGDRVGI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 564 RFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIA-EAELKPANTQSLCGLQQLEFTSL 642
Cdd:cd05968 122 YLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGrEVNLKEEADKACAQCPTVEKVVV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 643 TDPVGEPLNLVDV-----PEAKTFPGIG---TALDDTAYILFTSGSTGRPKGVAISHrsidnrlrwqqSQIPVGAStQD- 713
Cdd:cd05968 202 VRHLGNDFTPAKGrdlsyDEEKETAGDGaerTESEDPLMIIYTSGTTGKPKGTVHVH-----------AGFPLKAA-QDm 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 714 ------RAGDRILHKTPISFDVHVWELYWPLQEGAAVVI--AAPDgHRDPAYLARVIAEQNVTCLHFVPTMLTAFL---E 782
Cdd:cd05968 270 yfqfdlKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLydGAPD-HPKADRLWRMVEDHEITHLGLSPTLIRALKprgD 348
|
....*...
gi 503164607 783 APSAKRTL 790
Cdd:cd05968 349 APVNAHDL 356
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
485-1056 |
3.22e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 77.38 E-value: 3.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 485 HPIEYKT--LLQRFQDALTRYPNEPALYACAPDedgtlspqspqayefsqvLTYHELDARARALAKAMLEAGVCPGTAVG 562
Cdd:PRK06710 17 STISYDIqpLHKYVEQMASRYPEKKALHFLGKD------------------ITFSVFHDKVKRFANYLQKLGVEKGDRVA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 563 LRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPiaeaelKPANTQSLCGLQQLEFTSL 642
Cdd:PRK06710 79 IMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFP------RVTNVQSATKIEHVIVTRI 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 643 TDPVGEPLNL-------------VDVPEAKTF-------PGIGTALD-------DTAYILFTSGSTGRPKGVAISHRS-I 694
Cdd:PRK06710 153 ADFLPFPKNLlypfvqkkqsnlvVKVSESETIhlwnsveKEVNTGVEvpcdpenDLALLQYTGGTTGFPKGVMLTHKNlV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 695 DNRL---RWQQSQIpvgastqdRAGDRILHKTPIsfdVHVWELywplqeGAAVVIAAPDGHR-------DPAYLARVIAE 764
Cdd:PRK06710 233 SNTLmgvQWLYNCK--------EGEEVVLGVLPF---FHVYGM------TAVMNLSIMQGYKmvlipkfDMKMVFEAIKK 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 765 QNVTCLHFVPTMLTAFLEAPsakrTLAEAGFGSgeqqrhVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAvDVT 844
Cdd:PRK06710 296 HKVTLFPGAPTIYIALLNSP----LLKEYDISS------IRACISGSAPLPVEVQEKFETVTGGKLVEGYGLTESS-PVT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 845 ----FWDSSqnpecstVP--IGQPVWNTQTRILD-QALQPIPPGFVGELYLSGAQLAAGYQNNPEATAqAFILDNatger 917
Cdd:PRK06710 365 hsnfLWEKR-------VPgsIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIMKGYWNKPEETA-AVLQDG----- 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 918 LYRTGDLAewnltatnqepgtlAKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLlytKTPEP---- 993
Cdd:PRK06710 432 WLHTGDVG--------------YMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTI---GVPDPyrge 494
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503164607 994 ---ALTAFLEIGDVSETERNRIvaqARQHcentLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIE 1056
Cdd:PRK06710 495 tvkAFVVLKEGTECSEEELNQF---ARKY----LAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
514-907 |
3.96e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 76.97 E-value: 3.96e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 514 PDEDGTLSPQSPQAY--EFSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPD 591
Cdd:PRK13390 3 PGTHAQIAPDRPAVIvaETGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 592 LPAERVSSMMEDAQCSALVYGSGLSPIAEAELKPANTqslcglqQLEFTSLTDPVGEplnlvdvpEAKTFPGIGTALDDT 671
Cdd:PRK13390 83 LTAPEADYIVGDSGARVLVASAALDGLAAKVGADLPL-------RLSFGGEIDGFGS--------FEAALAGAGPRLTEQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 672 ---AYILFTSGSTGRPKGVA--ISHRSIDnrlrwqQSQIPV--------GASTQD--RAGDRILHKTPISFDVHVWELyw 736
Cdd:PRK13390 148 pcgAVMLYSSGTTGFPKGIQpdLPGRDVD------APGDPIvaiarafyDISESDiyYSSAPIYHAAPLRWCSMVHAL-- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 737 plqeGAAVVIAApdgHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRTLAEAGfgsgeqqrHVRYLICSGEALQK 816
Cdd:PRK13390 220 ----GGTVVLAK---RFDAQATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVS--------SLRAVIHAAAPCPV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 817 DQILSAHNIMGVYPLNLYGPTEA----AVDVTFWDSSQNpecstvPIGQPVWNTqTRILDQALQPIPPGFVGELYLSGAQ 892
Cdd:PRK13390 285 DVKHAMIDWLGPIVYEYYSSTEAhgmtFIDSPDWLAHPG------SVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDR 357
|
410
....*....|....*
gi 503164607 893 LAAGYQNNPEATAQA 907
Cdd:PRK13390 358 LPFRYLNDPEKTAAA 372
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
526-928 |
4.27e-14 |
|
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: 76.87 E-value: 4.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 526 QAYEFsqvLTYHELDARARALAKAMLEAGVCPGTA--VGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMED 603
Cdd:cd05927 1 GPYEW---ISYKEVAERADNIGSALRSLGGKPAPAsfVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNH 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 604 AQCSALVYGSGLspiaeaelkpantqslcglqqlEFTSLTD--PVGEpLNLVDVPEAKtfpgigtaLDDTAYILFTSGST 681
Cdd:cd05927 78 AEISIVFCDAGV----------------------KVYSLEEfeKLGK-KNKVPPPPPK--------PEDLATICYTSGTT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 682 GRPKGVAISHRSIdnrlrwqQSQIpVGASTQDRAGDRILHktpisFDVHVweLYWPLQ-------EGAAVVIAAPDG--H 752
Cdd:cd05927 127 GNPKGVMLTHGNI-------VSNV-AGVFKILEILNKINP-----TDVYI--SYLPLAhifervvEALFLYHGAKIGfyS 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 753 RDPAYLARVIAEQNVTCLHFVPTMLTAFLEA--------PSAKRTLA-------EAGFGSGEQQRH-------------- 803
Cdd:cd05927 192 GDIRLLLDDIKALKPTVFPGVPRVLNRIYDKifnkvqakGPLKRKLFnfalnykLAELRSGVVRASpfwdklvfnkikqa 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 804 ----VRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTFwdssQNPECSTV-PIGQPVWNTQTRILD------ 872
Cdd:cd05927 272 lggnVRLMLTGSAPLSPEVLEFLRVALGCPVLEGYGQTECTAGATL----TLPGDTSVgHVGGPLPCAEVKLVDvpemny 347
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 503164607 873 QALQPIPPgfvGELYLSGAQLAAGYQNNPEATAQAFILDNatgerLYRTGDLAEWN 928
Cdd:cd05927 348 DAKDPNPR---GEVCIRGPNVFSGYYKDPEKTAEALDEDG-----WLHTGDIGEWL 395
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
534-1054 |
4.51e-14 |
|
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: 76.23 E-value: 4.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQcsalvygs 613
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 glspiaeaelkpantqslcglqqleftsltdpvgeplnlvdvpeaktfpgigTALDDTAYILFTSGSTGRPKGVAISHRS 693
Cdd:cd05912 74 ----------------------------------------------------VKLDDIATIMYTSGTTGKPKGVQQTFGN 101
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IDNRLRwqQSQIPVGASTQDR----------AGDRILHKTPIsfdvhvwelywplqEGAAVVIAApdgHRDPAYLARVIA 763
Cdd:cd05912 102 HWWSAI--GSALNLGLTEDDNwlcalplfhiSGLSILMRSVI--------------YGMTVYLVD---KFDAEQVLHLIN 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 764 EQNVTCLHFVPTMLTAFLEApsakrtlaeagFGSGEQQrHVRYLICSGEALQKDQILSA--HNImGVYplNLYGPTEAAV 841
Cdd:cd05912 163 SGKVTIISVVPTMLQRLLEI-----------LGEGYPN-NLRCILLGGGPAPKPLLEQCkeKGI-PVY--QSYGMTETCS 227
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 842 D-VTFwdssqNPECSTVPI---GQPVWNTQTRILDQAlqpIPPGFVGELYLSGAQLAAGYQNNPEATAQAFildnATGer 917
Cdd:cd05912 228 QiVTL-----SPEDALNKIgsaGKPLFPVELKIEDDG---QPPYEVGEILLKGPNVTKGYLNRPDATEESF----ENG-- 293
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 918 LYRTGDLAEWNltatnqEPGTL-AKNPRGVILYRGrtdhqvklhGQRLELGDIETTLSHVEGVHSAVVllyTKTPE---- 992
Cdd:cd05912 294 WFKTGDIGYLD------EEGFLyVLDRRSDLIISG---------GENIYPAEIEEVLLSHPAIKEAGV---VGIPDdkwg 355
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503164607 993 --PALTAFLEiGDVSEternrivAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQ 1054
Cdd:cd05912 356 qvPVAFVVSE-RPISE-------EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHELKQ 411
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
670-1046 |
7.39e-14 |
|
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: 74.46 E-value: 7.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 670 DTAYILFTSGSTGRPKGVAISHR-SIDNRLRWqqsqipvGASTQDRAGDRILHKTPIsFDVHVWELYW--PLQEGAAVVi 746
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRqTLRAAAAW-------ADCADLTEDDRYLIINPF-FHTFGYKAGIvaCLLTGATVV- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 747 aaPDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKR-TLAEAGFG-SGEQQRHVRYLICSGEALQKDQILSAhn 824
Cdd:cd17638 72 --PVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKfDLSSLRAAvTGAATVPVELVRRMRSELGFETVLTA-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 825 imgvyplnlYGPTEAAVdVTFWDSSQNPECSTVPIGQPVWNTQTRILDQalqpippgfvGELYLSGAQLAAGYQNNPEAT 904
Cdd:cd17638 148 ---------YGLTEAGV-ATMCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEAT 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 905 AQAFildNATGerLYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVV 984
Cdd:cd17638 208 AEAI---DADG--WLHTGDVGEL--------------DERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAV 268
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503164607 985 LlytKTPEPAL----TAFLEIGDVSETERNRIVAQARQHcentLPDYMVPRLWHTTAQFPVSPSGK 1046
Cdd:cd17638 269 I---GVPDERMgevgKAFVVARPGVTLTEEDVIAWCRER----LANYKVPRFVRFLDELPRNASGK 327
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
669-1000 |
1.50e-13 |
|
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: 74.94 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGASTQDRagdrILHKTPISfdvHVWE-------LYWplqeG 741
Cdd:cd17639 88 DDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLGPDDR----YLAYLPLA---HIFElaaenvcLYR----G 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 742 AAVviaapdGHRDPAYLARVI-AEQNVTCLHFVPTMLTA--------------------------FLEAPSAKRTLAEAG 794
Cdd:cd17639 157 GTI------GYGSPRTLTDKSkRGCKGDLTEFKPTLMVGvpaiwdtirkgvlaklnpmgglkrtlFWTAYQSKLKALKEG 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 795 FGSGEQQR------------HVRYLICSGEALQKDqilsAH---NIMGVYPLNLYGPTEAAVDVTFwdssQNPEC-STVP 858
Cdd:cd17639 231 PGTPLLDElvfkkvraalggRLRYMLSGGAPLSAD----TQeflNIVLCPVIQGYGLTETCAGGTV----QDPGDlETGR 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 859 IGQPVWNTQTRILD------QALQPIPPGfvgELYLSGAQLAAGYQNNPEATAQAFildnaTGERLYRTGDLAEWnltat 932
Cdd:cd17639 303 VGPPLPCCEIKLVDweeggySTDKPPPRG---EILIRGPNVFKGYYKNPEKTKEAF-----DGDGWFHTGDIGEF----- 369
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503164607 933 nqepgtlakNPRGVILYRGRTDHQVKL-HGQRLELGDIETTLS----------HVEGVHSAVVLLYTkTPEPALTAFLE 1000
Cdd:cd17639 370 ---------HPDGTLKIIDRKKDLVKLqNGEYIALEKLESIYRsnplvnnicvYADPDKSYPVAIVV-PNEKHLTKLAE 438
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
522-1061 |
2.03e-13 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 74.79 E-value: 2.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 522 PQSPQAYEFSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEqYIALYAAL-YAGFVYVPILPDLPAERVSSM 600
Cdd:PRK06155 35 PDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIE-FLDVFLGCaWLGAIAVPINTALRGPQLEHI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 601 MEDAQCSALVygsglspiAEAELKPANTQSLCGLQQLEFTSLTDpvGEPLNLVDVP-EAKTFPGIGTALD-------DTA 672
Cdd:PRK06155 114 LRNSGARLLV--------VEAALLAALEAADPGDLPLPAVWLLD--APASVSVPAGwSTAPLPPLDAPAPaaavqpgDTA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 673 YILFTSGSTGRPKGVAISHrsidNRLRWQqsQIPVGASTQDRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIaapdGH 752
Cdd:PRK06155 184 AILYTSGTTGPSKGVCCPH----AQFYWW--GRNSAEDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVL----EP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 753 RDPA--YLARViAEQNVTCLHFVPTMLTAFLEAPSakrtlaeagfGSGEQQRHVRYLICSGEALQKDQILSAHniMGVYP 830
Cdd:PRK06155 254 RFSAsgFWPAV-RRHGATVTYLLGAMVSILLSQPA----------RESDRAHRVRVALGPGVPAALHAAFRER--FGVDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 831 LNLYGPTEAAVDVTFWDSSQNPECstvpIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQ---LAAGYQNNPEATAQA 907
Cdd:PRK06155 321 LDGYGSTETNFVIAVTHGSQRPGS----MGRLAPGFEARVVDEHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 908 FI-LDNATGERLYRTGDlaewnltatnqepgtlaknprGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLl 986
Cdd:PRK06155 397 WRnLWFHTGDRVVRDAD---------------------GWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVF- 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 987 ytktPEPAltaflEIGD--------VSETERNRIVAQARqHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIEFT 1058
Cdd:PRK06155 455 ----PVPS-----ELGEdevmaavvLRDGTALEPVALVR-HCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVT 524
|
...
gi 503164607 1059 FDT 1061
Cdd:PRK06155 525 ADT 527
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
670-1049 |
8.61e-13 |
|
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: 71.52 E-value: 8.61e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 670 DTAYILFTSGSTGRPKGVAISHRSIdnrlrWQQSQIPVGASTQDRAGDRILHKTPISFDVHVWELYWPLQEGAAVVIAAp 749
Cdd:cd17635 2 DPLAVIFTSGTTGEPKAVLLANKTF-----FAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGG- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 750 dGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEApsAKRTLAEAgfgsgeqqRHVRYLICSGEALQKDQILSAHNIMGVY 829
Cdd:cd17635 76 -ENTTYKSLFKILTTNAVTTTCLVPTLLSKLVSE--LKSANATV--------PSLRLIGYGGSRAIAADVRFIEATGLTN 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 830 PLNLYGPTE--AAVDVTFWDSSQNPECstvpIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQA 907
Cdd:cd17635 145 TAQVYGLSEtgTALCLPTDDDSIEINA----VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 908 FIldnatGERLYrTGDLAEwnltatnqepgtlaKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVlly 987
Cdd:cd17635 221 LI-----DGWVN-TGDLGE--------------RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECAC--- 277
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503164607 988 TKTPEPALTAF--LEIGDVSETERNRIVAQaRQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDR 1049
Cdd:cd17635 278 YEISDEEFGELvgLAVVASAELDENAIRAL-KHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
14-443 |
1.11e-12 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs); 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 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: 380453 [Multi-domain] Cd Length: 427 Bit Score: 71.67 E-value: 1.11e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 14 IPLTKSAQGIYLAAIIDPKNPCYNTAEIMECPPETNLDYLREAFIQLYRENEGFRVQTRVQTGRPEQrvIPLDEFLTNLe 93
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQ--VVLDKTVRFR- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 94 vlpvisLQIQEETEEQNPvpaavRGWASELISEPLRTD----AGVTVRSAVTYYGGKLWV-YHSFSHVVADGFAAFNGLS 168
Cdd:cd19066 79 ------IEIIDLRNLADP-----EARLLELIDQIQQTIydleRGPLVRVALFRLADERDVlVVAIHHIIVDGGSFQILFE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 169 RVAAIYRALSAGKPL---PTVKRASLMELLRaDHAAEHAREEDLALWTSEQVEVLSQPDTSLAARSASPAPQALREV-LT 244
Cdd:cd19066 148 DISSVYDAAERQKPTlppPVGSYADYAAWLE-KQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLeFF 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 245 LPDKLQRDMLEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRifgaQVPAETRALGktsaqtgtTAVNVLP- 323
Cdd:cd19066 227 LRSEETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNR----PDEAVEDTIG--------LFLNLLPl 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 324 -VQVSGMGSIAQALDSVKNQYARNASHP----LARQEDLERLAQSNDSRLFGAQINVIPFDAalPLGAPTENAPASVgyI 398
Cdd:cd19066 295 rIDTSPDATFPELLKRTKEQSREAIEHQrvpfIELVRHLGVVPEAPKHPLFEPVFTFKNNQQ--QLGKTGGFIFTTP--V 370
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 503164607 399 HNISAGPVADMTITLRGIPGRGhtISVELDANPNLYTREHVEFHA 443
Cdd:cd19066 371 YTSSEGTVFDLDLEASEDPDGD--LLLRLEYSRGVYDERTIDRFA 413
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
534-694 |
2.22e-12 |
|
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: 71.61 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVC-PGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEdaQCSALVYG 612
Cdd:cd05905 15 LTWGKLLSRAEKIAAVLQKKVGLkPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLG--TCKVRVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 613 SglspiAEAELKPANTQSLCGLQQLEftsLTDPVGEPLNL--VDVPEAKTF------PGIGTALDDTAYILFTSGSTGRP 684
Cdd:cd05905 93 T-----VEACLKGLPKKLLKSKTAAE---IAKKKGWPKILdfVKIPKSKRSklkkwgPHPPTRDGDTAYIEYSFSSDGSL 164
|
170
....*....|
gi 503164607 685 KGVAISHRSI 694
Cdd:cd05905 165 SGVAVSHSSL 174
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
534-1049 |
2.49e-12 |
|
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: 70.62 E-value: 2.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILpdlpaervssmmedaqcsalvygS 613
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLF-----------------------T 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 GLSPiaeaelkPANTQSLcglqqleftsltDPVGEPLNLVDVPEAKTFPgigtalDDTAYILFTSGSTGRPKGVAISHRS 693
Cdd:cd05973 58 AFGP-------KAIEHRL------------RTSGARLVVTDAANRHKLD------SDPFVMMFTSGTTGLPKGVPVPLRA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 694 IDNRLRWQQSQIPVgastqdRAGDRilhktpisfdvhvwelYWPLQE-----GAAVVIAAP--DGHRDPAYLARVIAEQn 766
Cdd:cd05973 113 LAAFGAYLRDAVDL------RPEDS----------------FWNAADpgwayGLYYAITGPlaLGHPTILLEGGFSVES- 169
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 767 vTCLHFVPTMLTAFLEAPSAKRTLAEAGFGSGEQQR-HVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTF 845
Cdd:cd05973 170 -TWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLAN 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 846 WDSSQNPeCSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLA----AGYQNNPEATAQAfildnatgeRLYRT 921
Cdd:cd05973 249 HHALEHP-VHAGSAGRAMPGWRVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDTPAIDG---------GYYLT 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 922 GDLAEWNltatnqepgtlaknPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLlytKTPEPALTAFLEI 1001
Cdd:cd05973 319 GDTVEFD--------------PDGSFSFIGRADDVITMSGYRIGPFDVESALIEHPAVAEAAVI---GVPDPERTEVVKA 381
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 503164607 1002 GDV--SETERNRIVAQARQ-HCENTLPDYMVPRLWHTTAQFPVSPSGKTDR 1049
Cdd:cd05973 382 FVVlrGGHEGTPALADELQlHVKKRLSAHAYPRTIHFVDELPKTPSGKIQR 432
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
534-927 |
4.75e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 70.53 E-value: 4.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAkAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPIL-PDLP--AERVSSMMEDAQCSALV 610
Cdd:PRK07769 56 LTWSQFGARNRAVG-ARLQQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLFdPAEPghVGRLHAVLDDCTPSAIL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 611 YGSGlspIAEAELK-----PANTQSlcglQQLEFTSLTDPVGEPLNLVDVPEaktfpgigtalDDTAYILFTSGSTGRPK 685
Cdd:PRK07769 135 TTTD---SAEGVRKffrarPAKERP----RVIAVDAVPDEVGATWVPPEANE-----------DTIAYLQYTSGSTRIPA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 686 GVAISHRSI-DNRLrwqQSQIPVGASTQDRA---------------------GDRILHKTPISFdvhV-----W--ELYW 736
Cdd:PRK07769 197 GVQITHLNLpTNVL---QVIDALEGQEGDRGvswlpffhdmglitvllpallGHYITFMSPAAF---VrrpgrWirELAR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 737 PLQEGAAVVIAAP--------------DGhRDPAYLARVIAEQN----VTclhfvPTMLTAFLEAPSA---KRTLAEAGF 795
Cdd:PRK07769 271 KPGGTGGTFSAAPnfafehaaarglpkDG-EPPLDLSNVKGLLNgsepVS-----PASMRKFNEAFAPyglPPTAIKPSY 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 796 GSGEQQRHVRYLICSGEA----LQKDQiLSAHNIMGVYPlnlygPTEAAVdvtfwdssqnPECSTVPIGQPVWNTqtrIL 871
Cdd:PRK07769 345 GMAEATLFVSTTPMDEEPtviyVDRDE-LNAGRFVEVPA-----DAPNAV----------AQVSAGKVGVSEWAV---IV 405
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503164607 872 D-QALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAF--ILDNATGE----------RLYRTGDLAEW 927
Cdd:PRK07769 406 DpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnILKSRLSEshaegapddaLWVRTGDYGVY 474
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
669-1048 |
5.42e-12 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 70.51 E-value: 5.42e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAISHRSIDNRLRwqqsQIPVGASTQDRagDRILHKTPI--SFDVHVwELYWPLQEGAAVVI 746
Cdd:PRK08043 365 EDAALILFTSGSEGHPKGVVHSHKSLLANVE----QIKTIADFTPN--DRFMSALPLfhSFGLTV-GLFTPLLTGAEVFL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 747 AAPDGHrdpaYlaRVIAE----QNVTCLHFVPTMLTAFleapsakrtlaeAGFGSGEQQRHVRYLICSGEALQKDQILSA 822
Cdd:PRK08043 438 YPSPLH----Y--RIVPElvydRNCTVLFGTSTFLGNY------------ARFANPYDFARLRYVVAGAEKLQESTKQLW 499
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 823 HNIMGVYPLNLYGPTEAAVDVTFwdssqnpecsTVPIGQPVwNTQTRIL---DQALQPIpPGFV--GELYLSGAQLAAGY 897
Cdd:PRK08043 500 QDKFGLRILEGYGVTECAPVVSI----------NVPMAAKP-GTVGRILpgmDARLLSV-PGIEqgGRLQLKGPNIMNGY 567
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 898 Q--NNP---EATAQafilDNATGER---LYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQVKLHGQRLELGDI 969
Cdd:PRK08043 568 LrvEKPgvlEVPTA----ENARGEMergWYDTGDIVRF--------------DEQGFVQIQGRAKRFAKIAGEMVSLEMV 629
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 970 ETTLSHV--EGVHSAVVLLYTKTPEpALTAFLEigDvSETERNRIVAQARQHcenTLPDYMVPRLWHTTAQFPVSPSGKT 1047
Cdd:PRK08043 630 EQLALGVspDKQHATAIKSDASKGE-ALVLFTT--D-SELTREKLQQYAREH---GVPELAVPRDIRYLKQLPLLGSGKP 702
|
.
gi 503164607 1048 D 1048
Cdd:PRK08043 703 D 703
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
486-1052 |
5.54e-12 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 70.05 E-value: 5.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 486 PIEYKTLLQRFQDALTRYPNEPAlYACapdedgtlspqspqayeFSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRF 565
Cdd:PRK07059 19 ASQYPSLADLLEESFRQYADRPA-FIC-----------------MGKAITYGELDELSRALAAWLQSRGLAKGARVAIMM 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 566 HRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIAEAELkpANTQslcgLQQLEFTSLTDP 645
Cdd:PRK07059 81 PNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIVVLENFATTVQQVL--AKTA----VKHVVVASMGDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 646 VGEPLNLVD---------VP-----------------EAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSI-DNRL 698
Cdd:PRK07059 155 LGFKGHIVNfvvrrvkkmVPawslpghvrfndalaegARQTFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIvANVL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 699 R---WQQSQIpvgastqdRAGDRILHKTPIS-------FDVHVWELYWPLQEGAAVVIAAPdghRDPAYLARVIAEQNVT 768
Cdd:PRK07059 235 QmeaWLQPAF--------EKKPRPDQLNFVCalplyhiFALTVCGLLGMRTGGRNILIPNP---RDIPGFIKELKKYQVH 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 769 CLHFVPTMLTAFLEAPS------AKRTLAEAGfgsgeqqrhvrylicsGEALQKDQILSAHNIMGVYPLNLYGPTEAAVD 842
Cdd:PRK07059 304 IFPAVNTLYNALLNNPDfdkldfSKLIVANGG----------------GMAVQRPVAERWLEMTGCPITEGYGLSETSPV 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 843 VTfwdssQNPECSTV---PIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNatgerLY 919
Cdd:PRK07059 368 AT-----CNPVDATEfsgTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADG-----FF 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 920 RTGDLaewnltatnqepGTLakNPRG----------VIL------YRGRTDHQVKLHGQRLELGDIettlsHVEGVHSA- 982
Cdd:PRK07059 438 RTGDV------------GVM--DERGytkivdrkkdMILvsgfnvYPNEIEEVVASHPGVLEVAAV-----GVPDEHSGe 498
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 983 VVLLYTKTPEPALTAfleigdvseternrivAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:PRK07059 499 AVKLFVVKKDPALTE----------------EDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
531-1054 |
6.32e-12 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 69.73 E-value: 6.32e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 531 SQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALV 610
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 611 -YGSGLSPIAEAelKPANTQSLCGLQQLEFTS--------LTDPVGEplnlVDVPE--AKTFPGIGTALDDTAYILFTSG 679
Cdd:PRK12406 89 aHADLLHGLASA--LPAGVTVLSVPTPPEIAAayrispalLTPPAGA----IDWEGwlAQQEPYDGPPVPQPQSMIYTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 680 STGRPKGVAISHRSIDNRLRWQQSQIPVGASTQdraGDRIL------HKTPISFDVHVWELywplqegAAVVIAAPdgHR 753
Cdd:PRK12406 163 TTGHPKGVRRAAPTPEQAAAAEQMRALIYGLKP---GIRALltgplyHSAPNAYGLRAGRL-------GGVLVLQP--RF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 754 DPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRtlaeAGFGSgEQQRHVRYLICSGEALQKDQILsahNIMGVYPLNL 833
Cdd:PRK12406 231 DPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVR----AKYDV-SSLRHVIHAAAPCPADVKRAMI---EWWGPVIYEY 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 834 YGPTEAAVdVTFWDSSQ---NPecSTVpiGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAA-GYQNNPEATAQAfi 909
Cdd:PRK12406 303 YGSTESGA-VTFATSEDalsHP--GTV--GKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEI-- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 910 ldnatgER--LYRTGDLaewnltatnqepGTLAKNPRGVILYRGRTdhQVKLHGQRLELGDIETTLSHVEGVHSAVVLly 987
Cdd:PRK12406 376 ------DRggFITSGDV------------GYLDADGYLFLCDRKRD--MVISGGVNIYPAEIEAVLHAVPGVHDCAVF-- 433
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503164607 988 tKTPEP----ALTAFLEIGDVSETErnriVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQ 1054
Cdd:PRK12406 434 -GIPDAefgeALMAVVEPQPGATLD----EADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
491-1053 |
1.10e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 69.27 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 491 TLLQRFQDALTRYPNEPALYACapdeDGTlspqspqayefsQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLE 570
Cdd:PRK05857 15 TVLDRVFEQARQQPEAIALRRC----DGT------------SALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 571 QYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSpiAEAELKPANTQSLCGLQqlefTSLTDPVGEPL 650
Cdd:PRK05857 79 TYLSVLACAKLGAIAVMADGNLPIAAIERFCQITDPAAALVAPGSK--MASSAVPEALHSIPVIA----VDIAAVTRESE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 651 NLVDVPEAKTFPGIGTalDDTAYILFTSGSTGRPKGVAISHRSI--------DNRLRWqqSQIPVGASTQdragdrilhk 722
Cdd:PRK05857 153 HSLDAASLAGNADQGS--EDPLAMIFTSGTTGEPKAVLLANRTFfavpdilqKEGLNW--VTWVVGETTY---------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 723 TPISfDVHVWELYW---PLQEGAAVVIAAPDGhrdpAYLARVIA--EQNVTCLhfVPTMLTafleapsakRTLAEAGFGs 797
Cdd:PRK05857 219 SPLP-ATHIGGLWWiltCLMHGGLCVTGGENT----TSLLEILTtnAVATTCL--VPTLLS---------KLVSELKSA- 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 798 GEQQRHVRYLICSG-EALQKD-QILSAhniMGVYPLNLYGPTEAAVDVTFW--DSSQNPECSTVPIGQPVWNTQTRILDQ 873
Cdd:PRK05857 282 NATVPSLRLVGYGGsRAIAADvRFIEA---TGVRTAQVYGLSETGCTALCLptDDGSIVKIEAGAVGRPYPGVDVYLAAT 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 874 ------ALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFIldnatgERLYRTGDLAEwnltatnqepgtlaKNPRGVI 947
Cdd:PRK05857 359 dgigptAPGAGPSASFGTLWIKSPANMLGYWNNPERTAEVLI------DGWVNTGDLLE--------------RREDGFF 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 948 LYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLlytKTPEPALTAFLEIGDVSETE---------RNRIVAQARQ 1018
Cdd:PRK05857 419 YIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACY---EIPDEEFGALVGLAVVASAEldesaaralKHTIAARFRR 495
|
570 580 590
....*....|....*....|....*....|....*.
gi 503164607 1019 HCENTL-PDYMVprlwhTTAQFPVSPSGKTDRKNLA 1053
Cdd:PRK05857 496 ESEPMArPSTIV-----IVTDIPRTQSGKVMRASLA 526
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
670-1048 |
1.57e-11 |
|
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: 67.79 E-value: 1.57e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 670 DTAYILFTSGSTGRPKGVAishrsidnrlrWQQSQIPVGA------STQDRAGDRILHKTPISFDVHVWELYWPLQEGAA 743
Cdd:cd05924 4 DDLYILYTGGTTGMPKGVM-----------WRQEDIFRMLmggadfGTGEFTPSEDAHKAAAAAAGTVMFPAPPLMHGTG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 744 V-----------VIAAPDGHRDPAYLARVIAEQNVTCLHFV-PTMLTAFLEAPSAKRTLAEAGFgsgeqqrhvrYLICSG 811
Cdd:cd05924 73 SwtafggllggqTVVLPDDRFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDAGPYDLSSL----------FAISSG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 812 EAL----QKDQILSA-HNIMgvyPLNLYGPTEAAVDVTFWDSSQNPECSTVPIGQPvwntQTRILDQALQPIPPG--FVG 884
Cdd:cd05924 143 GALlspeVKQGLLELvPNIT---LVDAFGSSETGFTGSGHSAGSGPETGPFTRANP----DTVVLDDDGRVVPPGsgGVG 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 885 ELYLSGaQLAAGYQNNPEATAQAFIldNATGERLYRTGDLAEWNltatnqEPGTlaknprgVILYrGRTDHQVKLHGQRL 964
Cdd:cd05924 216 WIARRG-HIPLGYYGDEAKTAETFP--EVDGVRYAVPGDRATVE------ADGT-------VTLL-GRGSVCINTGGEKV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 965 ELGDIETTLSHVEGVHSAVVLlytKTPEP-------ALTAFLEIGDVSEternrivAQARQHCENTLPDYMVPRLWHTTA 1037
Cdd:cd05924 279 FPEEVEEALKSHPAVYDVLVV---GRPDErwgqevvAVVQLREGAGVDL-------EELREHCRTRIARYKLPKQVVFVD 348
|
410
....*....|.
gi 503164607 1038 QFPVSPSGKTD 1048
Cdd:cd05924 349 EIERSPAGKAD 359
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
669-1055 |
1.88e-11 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 68.33 E-value: 1.88e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAISHR----SIDNRLRWQQSQIPVGASTqdragDRILHKTPIsFDVHVWELYWP--LQEGA 742
Cdd:PLN02574 198 DDVAAIMYSSGTTGASKGVVLTHRnliaMVELFVRFEASQYEYPGSD-----NVYLAALPM-FHIYGLSLFVVglLSLGS 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 743 AVVIAApdgHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEapSAKRTLAEAgFGSGEQqrhvrylICSGEALQKDQILsa 822
Cdd:PLN02574 272 TIVVMR---RFDASDMVKVIDRFKVTHFPVVPPILMALTK--KAKGVCGEV-LKSLKQ-------VSCGAAPLSGKFI-- 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 823 HNIMGVYP----LNLYGPTE-AAVDVTFWDSSQNPECSTVPIGQPvwNTQTRILDQALQP-IPPGFVGELYLSGAQLAAG 896
Cdd:PLN02574 337 QDFVQTLPhvdfIQGYGMTEsTAVGTRGFNTEKLSKYSSVGLLAP--NMQAKVVDWSTGClLPPGNCGELWIQGPGVMKG 414
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 897 YQNNPEATAQAFILDNatgerLYRTGDLAEWNLTatnqepgtlaknprGVILYRGRTDHQVKLHGQRLELGDIETTL-SH 975
Cdd:PLN02574 415 YLNNPKATQSTIDKDG-----WLRTGDIAYFDED--------------GYLYIVDRLKEIIKYKGFQIAPADLEAVLiSH 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 976 VEGVHSAVVLLYTKTPEPALTAFLeigdVSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQI 1055
Cdd:PLN02574 476 PEIIDAAVTAVPDKECGEIPVAFV----VRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
498-1049 |
1.98e-11 |
|
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: 68.29 E-value: 1.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 498 DALTR-YPNEPALYACapDEDGTlspqspqayefSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALY 576
Cdd:cd05970 24 DAMAKeYPDKLALVWC--DDAGE-----------ERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 577 AALYAGFVYVPILPDLPAERVSSMMEDAQCSALVY--GSGLSPIAEAELKPANTQSL---CGLQQLE-FTSLTDPVGEPL 650
Cdd:cd05970 91 ALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAiaEDNIPEEIEKAAPECPSKPKlvwVGDPVPEgWIDFRKLIKNAS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 651 NLVDVPEAKTFPGIgtalDDTAYILFTSGSTGRPKGVAISHrsidnrlRWQQSQIPVGASTQD-RAGDRILHKTPISFDV 729
Cdd:cd05970 171 PDFERPTANSYPCG----EDILLVYFSSGTTGMPKMVEHDF-------TYPLGHIVTAKYWQNvREGGLHLTVADTGWGK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 730 HVW-ELYWPLQEGAAVVIAapDGHR-DPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRTLAEagfgsgeqqrhVRYL 807
Cdd:cd05970 240 AVWgKIYGQWIAGAAVFVY--DYDKfDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSS-----------LRYC 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 808 ICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDV-TFwdssqnPECSTVP--IGQPVWNTQTRILDQALQPIPPGFVG 884
Cdd:cd05970 307 TTAGEALNPEVFNTFKEKTGIKLMEGFGQTETTLTIaTF------PWMEPKPgsMGKPAPGYEIDLIDREGRSCEAGEEG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 885 ELYLSGAQ-----LAAGYQNNPEATAQAFildnatGERLYRTGDLAeWnltatnqepgtlaKNPRGVILYRGRTDHQVKL 959
Cdd:cd05970 381 EIVIRTSKgkpvgLFGGYYKDAEKTAEVW------HDGYYHTGDAA-W-------------MDEDGYLWFVGRTDDLIKS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 960 HGQRLELGDIETTL-SHVEGVHSAVvllyTKTPEP----------ALTAFLEIGDVSETErnrivaqARQHCENTLPDYM 1028
Cdd:cd05970 441 SGYRIGPFEVESALiQHPAVLECAV----TGVPDPirgqvvkatiVLAKGYEPSEELKKE-------LQDHVKKVTAPYK 509
|
570 580
....*....|....*....|.
gi 503164607 1029 VPRLWHTTAQFPVSPSGKTDR 1049
Cdd:cd05970 510 YPRIVEFVDELPKTISGKIRR 530
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
535-1056 |
2.06e-11 |
|
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: 68.26 E-value: 2.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 535 TYHELDARARALAKAMLEA-GVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGS 613
Cdd:cd05928 43 SFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 GLSPIAEA---ELKPANTQSLCGLQQ----LEFTSLTDPVGEPLNLVDvpeaktfpgigTALDDTAYILFTSGSTGRPKG 686
Cdd:cd05928 123 ELAPEVDSvasECPSLKTKLLVSEKSrdgwLNFKELLNEASTEHHCVE-----------TGSQEPMAIYFTSGTTGSPKM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 687 VAISHRSID-----NRLRWqqsqipVGASTQD---RAGDRILHKTPIsfdvhvWELYWPLQEGAAVVIaapdgHRDPAYL 758
Cdd:cd05928 192 AEHSHSSLGlglkvNGRYW------LDLTASDimwNTSDTGWIKSAW------SSLFEPWIQGACVFV-----HHLPRFD 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 759 ARVIAEqnvTCLHFvPtmLTAFLEAPSAKRTLAEAGFGSgEQQRHVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTE 838
Cdd:cd05928 255 PLVILK---TLSSY-P--ITTFCGAPTVYRMLVQQDLSS-YKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 839 AAVDV-TFWDSSQNPECstvpIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQ-----LAAGYQNNPEATAQAFILDn 912
Cdd:cd05928 328 TGLICaNFKGMKIKPGS----MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKPirpfgLFSGYVDNPEKTAATIRGD- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 913 atgerLYRTGDLAewnltatnqepgtlAKNPRGVILYRGRTDHQVKLHGQRLELGDIETTL-SHVEGVHSAVVllytKTP 991
Cdd:cd05928 403 -----FYLTGDRG--------------IMDEDGYFWFMGRADDVINSSGYRIGPFEVESALiEHPAVVESAVV----SSP 459
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 992 EP----ALTAFLEIG-DVSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIE 1056
Cdd:cd05928 460 DPirgeVVKAFVVLApQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRDKE 529
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
535-923 |
2.47e-11 |
|
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: 68.23 E-value: 2.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 535 TYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILP-------DLpaERVSSMMEDAQcS 607
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPayslmsqDL--AKLKHLFELLK-P 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 608 ALVYGSGLSPIAEA--ELKPANTQSL------CGLQQLEFTSL--TDPVGeplnlvDVPEAktFPGIGTalDDTAYILFT 677
Cdd:cd05921 104 GLVFAQDAAPFARAlaAIFPLGTPLVvsrnavAGRGAISFAELaaTPPTA------AVDAA--FAAVGP--DTVAKFLFT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 678 SGSTGRPKGVAISHRSIDNrlrwQQSQIpvgASTQDRAGDRIlhktPISFDvhvWeLYWPLQEGAAVVIAA--------- 748
Cdd:cd05921 174 SGSTGLPKAVINTQRMLCA----NQAML---EQTYPFFGEEP----PVLVD---W-LPWNHTFGGNHNFNLvlynggtly 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 749 -PDGHRDPAYLARVIA---EQNVTCLHFVPTMLTAFLEAPSAKRTLAEAGFgsgeqqRHVRYLICSGEALQK------DQ 818
Cdd:cd05921 239 iDDGKPMPGGFEETLRnlrEISPTVYFNVPAGWEMLVAALEKDEALRRRFF------KRLKLMFYAGAGLSQdvwdrlQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 819 ILSAHNIMGVYPLNLYGPTEAAVDVTFwdsSQNPECSTVPIGQPVWNTQTRIldqalqpIPPGFVGELYLSGAQLAAGYQ 898
Cdd:cd05921 313 LAVATVGERIPMMAGLGATETAPTATF---THWPTERSGLIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYW 382
|
410 420
....*....|....*....|....*
gi 503164607 899 NNPEATAQAFilDNatgERLYRTGD 923
Cdd:cd05921 383 RQPELTAQAF--DE---EGFYCLGD 402
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
666-993 |
3.19e-11 |
|
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: 67.21 E-value: 3.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 666 TALDDTAYILFTSGSTGRPKGVAISHRSidnrlrwqqsqIPVG-ASTQD----RAGDRILHKTPISFDVHVWE-LYWPLQ 739
Cdd:cd05974 82 THADDPMLLYFTSGTTSKPKLVEHTHRS-----------YPVGhLSTMYwiglKPGDVHWNISSPGWAKHAWScFFAPWN 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 740 EGAAVViAAPDGHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRTLAeagfgsgeqqrhVRYLICSGEALQKDQI 819
Cdd:cd05974 151 AGATVF-LFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFDVK------------LREVVGAGEPLNPEVI 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 820 LSAHNIMGVYPLNLYGPTEAAVDVTfwdSSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGeLYLSGAQ---LAAG 896
Cdd:cd05974 218 EQVRRAWGLTIRDGYGQTETTALVG---NSPGQPVKAGSMGRPLPGYRVALLDPDGAPATEGEVA-LDLGDTRpvgLMKG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 897 YQNNPEATAQAFildnatGERLYRTGDLAewnltatnqepgtlAKNPRGVILYRGRTDHQVKLHGQRLELGDIETTLSHV 976
Cdd:cd05974 294 YAGDPDKTAHAM------RGGYYRTGDIA--------------MRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEH 353
|
330
....*....|....*..
gi 503164607 977 EGVHSAVVLlytKTPEP 993
Cdd:cd05974 354 PAVAEAAVV---PSPDP 367
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
525-1031 |
4.13e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 67.56 E-value: 4.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 525 PQAYEFSQvlTYHeldaRARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDA 604
Cdd:PLN02479 43 SVRYTWAQ--TYQ----RCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLLEHS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 605 QCSALVYGSGLSPIAEAELKPANTQSLCGLQQLEFTSLTDPVGEPLNLVD-----VPEAKTFPGIGtaldDTAY------ 673
Cdd:PLN02479 117 KSEVVMVDQEFFTLAEEALKILAEKKKSSFKPPLLIVIGDPTCDPKSLQYalgkgAIEYEKFLETG----DPEFawkppa 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 674 -------ILFTSGSTGRPKGVAISHR-----SIDNRLRWQqsqIPVGAStqdragdrILHKTPIsFDVHVWELYWPLQEG 741
Cdd:PLN02479 193 dewqsiaLGYTSGTTASPKGVVLHHRgaylmALSNALIWG---MNEGAV--------YLWTLPM-FHCNGWCFTWTLAAL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 742 AAVVIAAPDGHRDPAYLArvIAEQNVTclHF--VPTMLTAFLEAPSAKRTLAEAgfgsgeqqrHVRYLICSGEAlQKDQI 819
Cdd:PLN02479 261 CGTNICLRQVTAKAIYSA--IANYGVT--HFcaAPVVLNTIVNAPKSETILPLP---------RVVHVMTAGAA-PPPSV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 820 LSAHNIMG-----VYPLN-LYGPTEAAVDVTFWDSSQNPECSTVPIGQPVWNTQTRILD----QALQPIPP--GFVGELY 887
Cdd:PLN02479 327 LFAMSEKGfrvthTYGLSeTYGPSTVCAWKPEWDSLPPEEQARLNARQGVRYIGLEGLDvvdtKTMKPVPAdgKTMGEIV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 888 LSGAQLAAGYQNNPEATAQAFildnATGerLYRTGDLAewnltatnqepgtlAKNPRGVILYRGRTDHQVKLHGQRLELG 967
Cdd:PLN02479 407 MRGNMVMKGYLKNPKANEEAF----ANG--WFHSGDLG--------------VKHPDGYIEIKDRSKDIIISGGENISSL 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 968 DIETTLSHVEGVHSAVVLL-----YTKTPepalTAFLEI-GDVSETERNRIVAQARQHCENTLPDYMVPR 1031
Cdd:PLN02479 467 EVENVVYTHPAVLEASVVArpderWGESP----CAFVTLkPGVDKSDEAALAEDIMKFCRERLPAYWVPK 532
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
676-1055 |
4.79e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 67.35 E-value: 4.79e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 676 FTSGSTGRPKGVAISHR-----SIDNRLRWQQSQIPVgastqdragdrILHKTPIsFDVHVWELYWPL--QEGAAVVI-- 746
Cdd:PLN03102 193 YTSGTTADPKGVVISHRgaylsTLSAIIGWEMGTCPV-----------YLWTLPM-FHCNGWTFTWGTaaRGGTSVCMrh 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 747 -AAPDGHRDpaylarvIAEQNVTCLHFVPTMLTAFLEAPSAKRTLAeagfgSGEQQrhvrylICSGEALQKDQILSAHNI 825
Cdd:PLN03102 261 vTAPEIYKN-------IEMHNVTHMCCVPTVFNILLKGNSLDLSPR-----SGPVH------VLTGGSPPPAALVKKVQR 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 826 MGVYPLNLYGPTEAAVDVTF--WDSSQN--PECSTVPIGQ------------PVWNTQTrildQALQPIPPGFVGELYLS 889
Cdd:PLN03102 323 LGFQVMHAYGLTEATGPVLFceWQDEWNrlPENQQMELKArqgvsilgladvDVKNKET----QESVPRDGKTMGEIVIK 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 890 GAQLAAGYQNNPEATAQAFildnatGERLYRTGDLaewnltatnqepGTLakNPRGVILYRGRTDHQVKLHGQRLELGDI 969
Cdd:PLN03102 399 GSSIMKGYLKNPKATSEAF------KHGWLNTGDV------------GVI--HPDGHVEIKDRSKDIIISGGENISSVEV 458
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 970 ETTL-SHVEGVHSAVVL----LYTKTPepalTAF--LEIGDVSETER-NRIVAQAR---QHCENTLPDYMVPRLWHTTAQ 1038
Cdd:PLN03102 459 ENVLyKYPKVLETAVVAmphpTWGETP----CAFvvLEKGETTKEDRvDKLVTRERdliEYCRENLPHFMCPRKVVFLQE 534
|
410
....*....|....*..
gi 503164607 1039 FPVSPSGKTDRKNLAQI 1055
Cdd:PLN03102 535 LPKNGNGKILKPKLRDI 551
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
534-694 |
5.89e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 67.07 E-value: 5.89e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAkAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPIL-PDLP--AERVSSMMEDAQCSALv 610
Cdd:PRK12476 69 LTWTQLGVRLRAVG-ARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFaPELPghAERLDTALRDAEPTVV- 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 611 ygsgLSPIAEAElkpANTQSLCGLQQLEftsltdpvgEPLNLV--DVPE--AKTFPGIGTALDDTAYILFTSGSTGRPKG 686
Cdd:PRK12476 147 ----LTTTAAAE---AVEGFLRNLPRLR---------RPRVIAidAIPDsaGESFVPVELDTDDVSHLQYTSGSTRPPVG 210
|
....*...
gi 503164607 687 VAISHRSI 694
Cdd:PRK12476 211 VEITHRAV 218
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
488-1055 |
8.07e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 66.38 E-value: 8.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 488 EYKTLLQRFQDALTRYPNEPAlyacapdedgtlspqspqayeFSQV---LTYHELDARARALAkAMLEA--GVCPGTAVG 562
Cdd:PRK12492 22 AYKSVVEVFERSCKKFADRPA---------------------FSNLgvtLSYAELERHSAAFA-AYLQQhtDLVPGDRIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 563 LRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIAEAELKPANTQSLCGLQQLEF--- 639
Cdd:PRK12492 80 VQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALVYLNMFGKLVQEVLPDTGIEYLIEAKMGDLlpa 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 640 ------TSLTDPVGEPLNLVDVPEAKTFP-----GIGTA-------LDDTAYILFTSGSTGRPKGVAISHRS-IDN--RL 698
Cdd:PRK12492 160 akgwlvNTVVDKVKKMVPAYHLPQAVPFKqalrqGRGLSlkpvpvgLDDIAVLQYTGGTTGLAKGAMLTHGNlVANmlQV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 699 RWQQSQIPVGASTQDRAGDRILhKTPISFdVHVWE-----LYWPLQEGAAVVIAAPdghRDPAYLARVIAEQNVTCLHFV 773
Cdd:PRK12492 240 RACLSQLGPDGQPLMKEGQEVM-IAPLPL-YHIYAftancMCMMVSGNHNVLITNP---RDIPGFIKELGKWRFSALLGL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 774 PTMLTAFLEAPSAKRTLAEA--GFGSGeqqrhvrylicsGEALQKDQILSAHNIMGVYPLNLYGPTEAAvdvtfwdssqn 851
Cdd:PRK12492 315 NTLFVALMDHPGFKDLDFSAlkLTNSG------------GTALVKATAERWEQLTGCTIVEGYGLTETS----------- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 852 PECSTVPIGQ---------PVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAfiLDnatGERLYRTG 922
Cdd:PRK12492 372 PVASTNPYGElarlgtvgiPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEA--LD---AEGWFKTG 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 923 DLAewnltatnqepgtlAKNPRGVILYRGRTDHQVKLHGQRLELGDIE-TTLSHVEGVHSAVVLLYTKTPEPALTAFlei 1001
Cdd:PRK12492 447 DIA--------------VIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEdVVMAHPKVANCAAIGVPDERSGEAVKLF--- 509
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....
gi 503164607 1002 gdVSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQI 1055
Cdd:PRK12492 510 --VVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
534-925 |
9.15e-11 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 66.46 E-value: 9.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGS 613
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 614 GLspiaeAELKPANTqslcgLQQLEFTSLTD-PVGEPLNLVDVPEA-----KTFPGIGTALDDTAYILFTSGSTGRPKGV 687
Cdd:PRK04319 154 AL-----LERKPADD-----LPSLKHVLLVGeDVEEGPGTLDFNALmeqasDEFDIEWTDREDGAILHYTSGSTGKPKGV 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 688 AISHrsidnrlrwqqsqipvGASTQDRA-GDRILhktpisfDVHVWELYW-----------------PLQEGAAVVIaap 749
Cdd:PRK04319 224 LHVH----------------NAMLQHYQtGKYVL-------DLHEDDVYWctadpgwvtgtsygifaPWLNGATNVI--- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 750 DGHR-DPAYLARVIAEQNVtclhfvptmlTAFLEAPSAKRTLAEAGFGSGEQQR--HVRYLICSGEALQKDQILSAHNIM 826
Cdd:PRK04319 278 DGGRfSPERWYRILEDYKV----------TVWYTAPTAIRMLMGAGDDLVKKYDlsSLRHILSVGEPLNPEVVRWGMKVF 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 827 GVYPLNLYGPTE---------AAVDVTfwdssqnpecstvP--IGQPVWNTQTRILDQALQPIPPGFVGELYLSGA--QL 893
Cdd:PRK04319 348 GLPIHDNWWMTEtggimianyPAMDIK-------------PgsMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGwpSM 414
|
410 420 430
....*....|....*....|....*....|..
gi 503164607 894 AAGYQNNPEATAQAFILDnatgerLYRTGDLA 925
Cdd:PRK04319 415 MRGIWNNPEKYESYFAGD------WYVSGDSA 440
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
535-979 |
1.07e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 66.17 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 535 TYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGfVYVPILP------DLPA-----ERVSSMMED 603
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRG-ASLTMLHqptprtDLAVwaedtLRVIGMIGA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 604 aqcSALVYGS---GLSPIAEAElkpantqslcGLQQLEFTSLTDpvGEPLNLVDVPEaktfpgigtalDDTAYILFTSGS 680
Cdd:PRK07768 110 ---KAVVVGEpflAAAPVLEEK----------GIRVLTVADLLA--ADPIDPVETGE-----------DDLALMQLTSGS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 681 TGRPKGVAISHRSIdnrlrWQQSQIPVGASTQDRAGDRILHKTPISFDV-HVWELYWPLQEGAAVVIAAP-DGHRDPAYL 758
Cdd:PRK07768 164 TGSPKAVQITHGNL-----YANAEAMFVAAEFDVETDVMVSWLPLFHDMgMVGFLTVPMYFGAELVKVTPmDFLRDPLLW 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 759 ARVIAeqnvtclHFVPTMLTA--FLEAPSAKRTLAEAGFGSGEQQRhVRYLICSGEALQKDQI---LSAHNIMGVYPLNL 833
Cdd:PRK07768 239 AELIS-------KYRGTMTAApnFAYALLARRLRRQAKPGAFDLSS-LRFALNGAEPIDPADVedlLDAGARFGLRPEAI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 834 ---YGPTEAAVDVTFWDSSQNPECSTV-----------------------PIGQPVWNTQTRILDQALQPIPPGFVGELY 887
Cdd:PRK07768 311 lpaYGMAEATLAVSFSPCGAGLVVDEVdadllaalrravpatkgntrrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 888 LSGAQLAAGYqnnpeATAQAFI-LDNATGerLYRTGDLaewnltatnqepGTLAKNPRGVILyrGRTDHQVKLHGQRLEL 966
Cdd:PRK07768 391 LRGESVTPGY-----LTMDGFIpAQDADG--WLDTGDL------------GYLTEEGEVVVC--GRVKDVIIMAGRNIYP 449
|
490
....*....|...
gi 503164607 967 GDIETTLSHVEGV 979
Cdd:PRK07768 450 TDIERAAARVEGV 462
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
485-928 |
1.49e-10 |
|
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: 65.63 E-value: 1.49e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 485 HPIEYKTLLQRFQDALTRYpnepalyACAPDEDGTLSPQSPQAYEFSQvltYHELDARaraLAKAMLEAGVCPGTAVGLR 564
Cdd:cd17642 9 YPLEDGTAGEQLHKAMKRY-------ASVPGTIAFTDAHTGVNYSYAE---YLEMSVR---LAEALKKYGLKQNDRIAVC 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 565 FHRGLEQYIALYAALYAGFVYVPiLPDLPAER--VSSMMEDAQCSALVYGSGLSPIAEAELKPANTQS---------LCG 633
Cdd:cd17642 76 SENSLQFFLPVIAGLFIGVGVAP-TNDIYNERelDHSLNISKPTIVFCSKKGLQKVLNVQKKLKIIKTiiildskedYKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 634 LQQLE-FTSLTDPVGeplnlvdVPEAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGASTQ 712
Cdd:cd17642 155 YQCLYtFITQNLPPG-------FNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFSHARDPIFGNQIIP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 713 DRAgdrILHKTPISFDVHVWELYWPLQEGAAVVIAapdgHR-DPAYLARVIAEQNVTCLHFVPTmLTAFLeapsAKRTLA 791
Cdd:cd17642 228 DTA---ILTVIPFHHGFGMFTTLGYLICGFRVVLM----YKfEEELFLRSLQDYKVQSALLVPT-LFAFF----AKSTLV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 792 EAGFGSgeqqrHVRYLICSGEALQK---DQILSAHNIMGVYplNLYGPTE--AAVDVTfwdssqnPECSTVP--IGQPVW 864
Cdd:cd17642 296 DKYDLS-----NLHEIASGGAPLSKevgEAVAKRFKLPGIR--QGYGLTEttSAILIT-------PEGDDKPgaVGKVVP 361
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503164607 865 NTQTRILD-QALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFILDNatgerLYRTGDLAEWN 928
Cdd:cd17642 362 FFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDG-----WLHSGDIAYYD 421
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
669-926 |
1.70e-10 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 64.42 E-value: 1.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAISHRSidnrlrwQQSQIPVGASTQD-RAGDRILHKTPIsFDVH--VWELYWPLQEGAAVV 745
Cdd:cd05944 2 DDVAAYFHTGGTTGTPKLAQHTHSN-------EVYNAWMLALNSLfDPDDVLLCGLPL-FHVNgsVVTLLTPLASGAHVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 746 IAAPDGHRDPAY---LARVIAEQNVTCLHFVPTMLTAFLEAPsakrtlAEAGFGSgeqqrhVRYLICSGEALQKDQILSA 822
Cdd:cd05944 74 LAGPAGYRNPGLfdnFWKLVERYRITSLSTVPTVYAALLQVP------VNADISS------LRFAMSGAAPLPVELRARF 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 823 HNIMGVYPLNLYGPTEA--AVDVTFWDSSQNPECstvpIGQPVWNTQTRIL-----DQALQPIPPGFVGELYLSGAQLAA 895
Cdd:cd05944 142 EDATGLPVVEGYGLTEAtcLVAVNPPDGPKRPGS----VGLRLPYARVRIKvldgvGRLLRDCAPDEVGEICVAGPGVFG 217
|
250 260 270
....*....|....*....|....*....|.
gi 503164607 896 GYQNNpEATAQAFIldnatGERLYRTGDLAE 926
Cdd:cd05944 218 GYLYT-EGNKNAFV-----ADGWLNTGDLGR 242
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
674-924 |
1.84e-10 |
|
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: 64.21 E-value: 1.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 674 ILFTSGSTGRPKGVAISHRSIdnrlrwQQSQIPVGASTQDRAGDRILHKTPIsFdvHVWELYWPL---QEGAAVVIAApd 750
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNL------IAANLQLIHAMGLTEADVYLNMLPL-F--HIAGLNLALatfHAGGANVVME-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 751 gHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEApsakrtlAEAGFGSGEQQRHVRYLicsgEALQKDQILSAHNIMGVYp 830
Cdd:cd17637 74 -KFDPAEALELIEEEKVTLMGSFPPILSNLLDA-------AEKSGVDLSSLRHVLGL----DAPETIQRFEETTGATFW- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 831 lNLYGPTEAAVDVTFWDSSQNPECStvpiGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFil 910
Cdd:cd17637 141 -SLYGQTETSGLVTLSPYRERPGSA----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-- 213
|
250
....*....|....
gi 503164607 911 DNAtgerLYRTGDL 924
Cdd:cd17637 214 RNG----WHHTGDL 223
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
16-264 |
2.08e-10 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 62.75 E-value: 2.08e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 16 LTKSAQGIYLAaiiDPKNPCYNTAEIMECPPETNLDYLREAFIQLYRENEGFRVQTRVQTGRPEQRVIPLDEFltnleVL 95
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADL-----PL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 96 PVISLQIQEETEEQnpvpAAVRGWASELISEPLRTDAGVTVRSAVTYYGGK----LWVYHsfsHVVADGFAAFNGLSRVA 171
Cdd:COG4908 73 EVVDLSALPEPERE----AELEELVAEEASRPFDLARGPLLRAALIRLGEDehvlLLTIH---HIISDGWSLGILLRELA 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 172 AIYRALSAGKPLP----TVKRASLMELLRAdHAAEHAREEDLALWT---SEQVEVLSQPdtSLAARSASPAPQALREVLT 244
Cdd:COG4908 146 ALYAALLEGEPPPlpelPIQYADYAAWQRA-WLQSEALEKQLEYWRqqlAGAPPVLELP--TDRPRPAVQTFRGATLSFT 222
|
250 260
....*....|....*....|
gi 503164607 245 LPDKLQRDMLEIGKMYGTSW 264
Cdd:COG4908 223 LPAELTEALKALAKAHGATV 242
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
532-1001 |
5.24e-10 |
|
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: 63.98 E-value: 5.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVY 611
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 GS-----GLSPIAEAelkpantqslcgLQQLEFTSLTDPVG-----EPlNLVDVPE--------AKTFPGIGTAL----- 668
Cdd:cd17641 90 EDeeqvdKLLEIADR------------IPSVRYVIYCDPRGmrkydDP-RLISFEDvvalgralDRRDPGLYEREvaagk 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 -DDTAYILFTSGSTGRPKGVAISHRSI----------DNRLR-----------WQQSQI-PVGASTQDRagdrilhktpi 725
Cdd:cd17641 157 gEDVAVLCTTSGTTGKPKLAMLSHGNFlghcaaylaaDPLGPgdeyvsvlplpWIGEQMySVGQALVCG----------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 726 sFDVHVWELYWPLQE-----GAAVVIAAPdghrdpaylaRVIAEQnvtcLHFVPTMLtafLEAPSAKRTLAEAGFGSGEQ 800
Cdd:cd17641 226 -FIVNFPEEPETMMEdlreiGPTFVLLPP----------RVWEGI----AADVRARM---MDATPFKRFMFELGMKLGLR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 801 Q-----------------------------------RHVRYLICSGEALQKDqILSAHNIMGVYPLNLYGPTEAAVDVTF 845
Cdd:cd17641 288 AldrgkrgrpvslwlrlaswladallfrplrdrlgfSRLRSAATGGAALGPD-TFRFFHAIGVPLKQLYGQTELAGAYTV 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 846 WDSSQNPEcSTVpiGQPVWNTQTRILDqalqpippgfVGELYLSGAQLAAGYQNNPEATAQAFILDNatgerLYRTGDla 925
Cdd:cd17641 367 HRDGDVDP-DTV--GVPFPGTEVRIDE----------VGEILVRSPGVFVGYYKNPEATAEDFDEDG-----WLHTGD-- 426
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503164607 926 ewnltatnqePGTLAKNPRGVILYRGRtDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKtpePALTAFLEI 1001
Cdd:cd17641 427 ----------AGYFKENGHLVVIDRAK-DVGTTSDGTRFSPQFIENKLKFSPYIAEAVVLGAGR---PYLTAFICI 488
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1073-1131 |
9.71e-10 |
|
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: 55.65 E-value: 9.71e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503164607 1073 QQISEIIAGVLGRS--QFGVTEDFLAAGGNSLAALSVIAKIEENLGKMLSIGALFANPTVK 1131
Cdd:pfam00550 1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
532-692 |
1.05e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 62.97 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILP-------DLpaERVSSMMEDA 604
Cdd:PRK08180 68 RRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPayslvsqDF--GKLRHVLELL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 605 QcSALVYGSGLSPIAEA--ELKPANTQSLC------GLQQLEFTSLTDPVGEPlnlvDVPEAktFPGIGtaLDDTAYILF 676
Cdd:PRK08180 146 T-PGLVFADDGAAFARAlaAVVPADVEVVAvrgavpGRAATPFAALLATPPTA----AVDAA--HAAVG--PDTIAKFLF 216
|
170
....*....|....*.
gi 503164607 677 TSGSTGRPKGVAISHR 692
Cdd:PRK08180 217 TSGSTGLPKAVINTHR 232
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
530-924 |
1.09e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 62.65 E-value: 1.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 530 FSQVLTYHELDARARALAKAMLEAGVcPGTAVGLRFHRGLEQYIALYAALYAGFVYVPiLPdLPA-----ERVSSMMEDA 604
Cdd:PRK05850 32 VAETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAGLIAVP-LS-VPQggahdERVSAVLRDT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 605 QCSALVygsGLSPIAEAELKPANTQSLcglqqleftSLTDPVGEpLNLVDVPEAKTFPGIGTALDDTAYILFTSGSTGRP 684
Cdd:PRK05850 109 SPSVVL---TTSAVVDDVTEYVAPQPG---------QSAPPVIE-VDLLDLDSPRGSDARPRDLPSTAYLQYTSGSTRTP 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 685 KGVAISHRSIDNRLRwqqsQIpVGASTQDRAGDRILHKTPISfdvhvwelyW-PLQE--GAAVVIAAPDGHRDPAYLARV 761
Cdd:PRK05850 176 AGVMVSHRNVIANFE----QL-MSDYFGDTGGVPPPDTTVVS---------WlPFYHdmGLVLGVCAPILGGCPAVLTSP 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 762 IA--EQNVTCLHFVPTMLTAFLEAP------SAKRTLAE--AGFGSGeqqrHVRYLICSGEALQKDQI------LSAHNI 825
Cdd:PRK05850 242 VAflQRPARWMQLLASNPHAFSAAPnfafelAVRKTSDDdmAGLDLG----GVLGIISGSERVHPATLkrfadrFAPFNL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 826 M--GVYPLnlYGPTEAAVDVTFWDSSQNPE----------------CST------VPIGQPvWNTQTRILD-QALQPIPP 880
Cdd:PRK05850 318 RetAIRPS--YGLAEATVYVATREPGQPPEsvrfdyeklsaghakrCETgggtplVSYGSP-RSPTVRIVDpDTCIECPA 394
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 503164607 881 GFVGELYLSGAQLAAGYQNNPEATAQAF---ILDNATGER---LYRTGDL 924
Cdd:PRK05850 395 GTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPGTPegpWLRTGDL 444
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1071-1139 |
2.93e-09 |
|
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: 54.86 E-value: 2.93e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503164607 1071 LEQQISEIIAGVLG--RSQFGVTEDFLAA-GGNSLAALSVIAKIEENLGKMLSIGALFANPTVKGIAAALNE 1139
Cdd:COG0236 6 LEERLAEIIAEVLGvdPEEITPDDSFFEDlGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
1168-1406 |
3.12e-09 |
|
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: 58.94 E-value: 3.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1168 PLFILPPAGGLGWCYAAYLPHIPGHPSVYALQHEAFTNPNAgYAQSLRELAEGYLARIRETLEERqlPsqFSLMGWSVGG 1247
Cdd:pfam00975 2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEP-PLNSIEALADEYAEALRQIQPEG--P--YALFGHSMGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1248 TAAVEVAALAETAGYDVQQVTLLDAY-PVEQWQGIPEPDEQESFRALL-RMGGLPEVSAQTVLDLPQTLERLRDAGSAMG 1325
Cdd:pfam00975 77 MLAFEVARRLERQGEAVRSLFLSDASaPHTVRYEASRAPDDDEVVAEFtDEGGTPEELLEDEELLSMLLPALRADYRALE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1326 YLPedklevCLESMRASAALMRGsnhlnfggkvvligvSHD---DQPYLDAHGWELHVGSFRTVTLkNGTHPDLV-NPER 1401
Cdd:pfam00975 157 SYS------CPPLDAQSATLFYG---------------SDDplhDADDLAEWVRDHTPGEFDVHVF-DGDHFYLIeHLEA 214
|
....*
gi 503164607 1402 IPEII 1406
Cdd:pfam00975 215 VLEII 219
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
535-925 |
6.68e-09 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 60.15 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 535 TYHELDARARALAKAMLEAGVCPGTAVGL---RFHRGLEqyiALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVY 611
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATiawNTWRHLE---AWYGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 GSGLSPIAEAeLKPAntqslcgLQQLE-FTSLTDPVGEPLNlvDVPEAKTFPGI----------GTALDDTAYIL-FTSG 679
Cdd:PRK06018 118 DLTFVPILEK-IADK-------LPSVErYVVLTDAAHMPQT--TLKNAVAYEEWiaeadgdfawKTFDENTAAGMcYTSG 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 680 STGRPKGVAISHRSidNRLRWQQSQIP--VGAStqdrAGDRILHKTPIsFDVHVWELYW--PLQeGAAVVIaaPDGHRDP 755
Cdd:PRK06018 188 TTGDPKGVLYSHRS--NVLHALMANNGdaLGTS----AADTMLPVVPL-FHANSWGIAFsaPSM-GTKLVM--PGAKLDG 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 756 AYLARVIAEQNVTCLHFVPT---MLTAFLEAPSAKRTlaeagfgsgeqqrHVRYLICSGEALQKdQILSAHNIMGVYPLN 832
Cdd:PRK06018 258 ASVYELLDTEKVTFTAGVPTvwlMLLQYMEKEGLKLP-------------HLKMVVCGGSAMPR-SMIKAFEDMGVEVRH 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 833 LYGPTEAAVDVTFwdSSQNPECSTVPI----------GQPVWNTQTRILDQALQPIP---PGFvGELYLSGAQLAAGYQN 899
Cdd:PRK06018 324 AWGMTEMSPLGTL--AALKPPFSKLPGdarldvlqkqGYPPFGVEMKITDDAGKELPwdgKTF-GRLKVRGPAVAAAYYR 400
|
410 420
....*....|....*....|....*.
gi 503164607 900 npeatAQAFILDNatgERLYRTGDLA 925
Cdd:PRK06018 401 -----VDGEILDD---DGFFDTGDVA 418
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
619-1009 |
1.27e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 59.01 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 619 AEAELKPANTQSLCGLQQLEFTSLTD-PVGEPLNLVDVPeaktfpgigtaLDDTAYILFTSGSTGRPKGVAISHRSIDN- 696
Cdd:COG1541 43 DEAGVDPDDIKSLEDLAKLPFTTKEDlRDNYPFGLFAVP-----------LEEIVRIHASSGTTGKPTVVGYTRKDLDRw 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 697 RLRWQQSQIPVGAstqdRAGDRILhktpISFDVHVWELYWPLQEGA----AVVIAApdGHRDPAYLARVIAEQNVTCLHF 772
Cdd:COG1541 112 AELFARSLRAAGV----RPGDRVQ----NAFGYGLFTGGLGLHYGAerlgATVIPA--GGGNTERQLRLMQDFGPTVLVG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 773 VPTMLTAFLEapsakrTLAEAGFGSGEQqrHVRYLICSGEAL---QKDQILSAHNIMgVYplNLYGPTEAAVDVTFwdss 849
Cdd:COG1541 182 TPSYLLYLAE------VAEEEGIDPRDL--SLKKGIFGGEPWseeMRKEIEERWGIK-AY--DIYGLTEVGPGVAY---- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 850 qnpECSTVPiGQPVWNTQ--TRILD-QALQPIPPGFVGELYLSGaqLaagyqnnpeaTAQAF--IldnatgeRlYRTGDL 924
Cdd:COG1541 247 ---ECEAQD-GLHIWEDHflVEIIDpETGEPVPEGEEGELVVTT--L----------TKEAMplI-------R-YRTGDL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 925 AEWNltatnqePGTLA---KNPR--GVIlyrGRTDHQVKLHGQRLELGDIETTLSHVEGVHS-AVVLLYTKTPEPALTAF 998
Cdd:COG1541 303 TRLL-------PEPCPcgrTHPRigRIL---GRADDMLIIRGVNVFPSQIEEVLLRIPEVGPeYQIVVDREGGLDELTVR 372
|
410
....*....|.
gi 503164607 999 LEIGDVSETER 1009
Cdd:COG1541 373 VELAPGASLEA 383
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
532-792 |
2.68e-08 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 58.26 E-value: 2.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAKAML-EAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLP----------------- 593
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMndqivhiinhaedeviv 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 594 -----AERVSSMMEDAQCSALVYGSGLSPIAEAElkpanTQSLCGLQQLEFTSLTDPVGEPLNLVDVPEaktfpgigtal 668
Cdd:PRK05620 117 adprlAEQLGEILKECPCVRAVVFIGPSDADSAA-----AHMPEGIKVYSYEALLDGRSTVYDWPELDE----------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAISHRSIdnrlrWQQSQIPVGA-STQDRAGDRILHKTPIsfdVHVweLYW--PL---QEGA 742
Cdd:PRK05620 181 TTAAAICYSTGTTGAPKGVVYSHRSL-----YLQSLSLRTTdSLAVTHGESFLCCVPI---YHV--LSWgvPLaafMSGT 250
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 503164607 743 AVVIAAPDghRDPAYLARVIAEQNVTCLHFVPT----MLTAFLEAPSAKRTLAE 792
Cdd:PRK05620 251 PLVFPGPD--LSAPTLAKIIATAMPRVAHGVPTlwiqLMVHYLKNPPERMSLQE 302
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
535-775 |
7.09e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 57.02 E-value: 7.09e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 535 TYHELDARARALAKAMLEAGVCPGTAVG-LRF--HRGLEQYialYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVY 611
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGtLAWngYRHLEAY---YGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 612 GSGLSPIAEAeLKPAntqslCGLQQlEFTSLTD----PVGE-PL----NLVDV-PEAKTFPgigtALDD--TAYILFTSG 679
Cdd:PRK07008 118 DLTFLPLVDA-LAPQ-----CPNVK-GWVAMTDaahlPAGStPLlcyeTLVGAqDGDYDWP----RFDEnqASSLCYTSG 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 680 STGRPKGVAISHRSidNRLRWQQSQIP--VGAStqdrAGDRILHKTPIsFDVHVWELYW--PLQeGAAVVIAAPDghRDP 755
Cdd:PRK07008 187 TTGNPKGALYSHRS--TVLHAYGAALPdaMGLS----ARDAVLPVVPM-FHVNAWGLPYsaPLT-GAKLVLPGPD--LDG 256
|
250 260
....*....|....*....|
gi 503164607 756 AYLARVIAEQNVTCLHFVPT 775
Cdd:PRK07008 257 KSLYELIEAERVTFSAGVPT 276
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
534-1055 |
8.85e-08 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 56.54 E-value: 8.85e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 534 LTYHELDARARALAKAMLEAGVCPG-TAVgLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYG 612
Cdd:PRK10946 49 FSYRELNQASDNLACSLRRQGIKPGdTAL-VQLGNVAEFYITFFALLKLGVAPVNALFSHQRSELNAYASQIEPALLIAD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 613 SGLSPIAEAELKPANTQSLCGLQQLEFtsLTDPVGEPLNLVDVPEAKTFPGIGTALDDTAYILFTSGSTGRPKGVAISHR 692
Cdd:PRK10946 128 RQHALFSDDDFLNTLVAEHSSLRVVLL--LNDDGEHSLDDAINHPAEDFTATPSPADEVAFFQLSGGSTGTPKLIPRTHN 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 693 SIDNRLRWQQSQIPVGASTqdragdRILHKTPISfdvHVWELYWP-----LQEGAAVVIAApdghrDPAYLA--RVIAEQ 765
Cdd:PRK10946 206 DYYYSVRRSVEICGFTPQT------RYLCALPAA---HNYPMSSPgalgvFLAGGTVVLAP-----DPSATLcfPLIEKH 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 766 NVTCLHFVPTMLTAFLEAPSAKrtlaeagfGSGEQQRHVRYLICSG----EALQKdQILSahnIMGVYPLNLYGPTEAAV 841
Cdd:PRK10946 272 QVNVTALVPPAVSLWLQAIAEG--------GSRAQLASLKLLQVGGarlsETLAR-RIPA---ELGCQLQQVFGMAEGLV 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 842 DVTFWDSSQnpecstvpigQPVWNTQTR---------ILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQAFildN 912
Cdd:PRK10946 340 NYTRLDDSD----------ERIFTTQGRpmspddevwVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAF---D 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 913 ATGerLYRTGDLAewnltatnqepgtlAKNPRGVILYRGRTDHQVKLHGQRLELGDIET-TLSHVEGVHSAVVLLytktP 991
Cdd:PRK10946 407 ANG--FYCSGDLV--------------SIDPDGYITVVGREKDQINRGGEKIAAEEIENlLLRHPAVIHAALVSM----E 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503164607 992 EPAL----TAFLeigdVSeTERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQI 1055
Cdd:PRK10946 467 DELMgeksCAFL----VV-KEPLKAVQLRRFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQW 529
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
495-719 |
1.16e-07 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 56.42 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 495 RFQDALTRYPNEPALYacapDEDgtlspqspqayefsQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIA 574
Cdd:PRK08279 42 VFEEAAARHPDRPALL----FED--------------QSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 575 LYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIAE---AELKPANTQSLCGLQQLeftslTDPVGEpLN 651
Cdd:PRK08279 104 WLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEearADLARPPRLWVAGGDTL-----DDPEGY-ED 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503164607 652 LVDvpEAKTFPGI------GTALDDTAYILFTSGSTGRPKGVAISHRsidnrlRWQQSQIPVGASTQDRAGDRI 719
Cdd:PRK08279 178 LAA--AAAGAPTTnpasrsGVTAKDTAFYIYTSGTTGLPKAAVMSHM------RWLKAMGGFGGLLRLTPDDVL 243
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
669-986 |
1.61e-07 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 55.89 E-value: 1.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPvGASTqdraGDRILHKTPISfdvHVWELYWP---LQEGAAVV 745
Cdd:PLN02387 250 NDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVP-KLGK----NDVYLAYLPLA---HILELAAEsvmAAVGAAIG 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 746 IAAPDGHRDPAYLARVIAEQNVTCLhfVPTMLTA-----------FLEAPSAKRTLAEAGFGSGEQQR------------ 802
Cdd:PLN02387 322 YGSPLTLTDTSNKIKKGTKGDASAL--KPTLMTAvpaildrvrdgVRKKVDAKGGLAKKLFDIAYKRRlaaiegswfgaw 399
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 803 ---------------------HVRYLICSGEALQKDQILSAHNIMGVYPLNLYGPTEAAVDVTF--WDSSqnpecSTVPI 859
Cdd:PLN02387 400 glekllwdalvfkkiravlggRIRFMLSGGAPLSGDTQRFINICLGAPIGQGYGLTETCAGATFseWDDT-----SVGRV 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 860 GQPVWNTQTRILD-------QALQPIPPgfvGELYLSGAQLAAGYQNNPEATAQAFILDNaTGERLYRTGDLAEWnltat 932
Cdd:PLN02387 475 GPPLPCCYVKLVSweeggylISDKPMPR---GEIVIGGPSVTLGYFKNQEKTDEVYKVDE-RGMRWFYTGDIGQF----- 545
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503164607 933 nqepgtlakNPRGVILYRGRTDHQVKL-HGQRLELGDIETTLS----------HVEGVHSAVVLL 986
Cdd:PLN02387 546 ---------HPDGCLEIIDRKKDIVKLqHGEYVSLGKVEAALSvspyvdnimvHADPFHSYCVAL 601
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
855-1145 |
2.40e-07 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 53.99 E-value: 2.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 855 STVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNP---EATAQAFILDNATGERLYRTGDLAEWNLta 931
Cdd:COG3433 12 TPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIrllAAAARAPFIPVPYPAQPGRQADDLRLLL-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 932 tnqepgtlaknpRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLLYTKTPEPALTAfLEIGDVSETERNR 1011
Cdd:COG3433 90 ------------RRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGL-LLIVGAVAALDGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1012 IVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLAQIEF----TFDTNTADGPHGLLEQQISEIIAGVLGRS- 1086
Cdd:COG3433 157 AAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAeallAAASPAPALETALTEEELRADVAELLGVDp 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 1087 -QFGVTEDFLAAGGNSLAALSVIAKIEENlGKMLSIGALFANPTVKGIAAALNEDSPDIE 1145
Cdd:COG3433 237 eEIDPDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
520-1052 |
2.54e-07 |
|
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: 55.08 E-value: 2.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 520 LSPQSPQAYEFSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHrglEQYIALYAALYAGFVYvpilpDLPAeRVSS 599
Cdd:cd05929 4 RDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLI---NSILTVFAAAAAWKCG-----ACPA-YKSS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 600 MMEDAqcsalvygsglspIAEAELKPANTQSLCGLqqleftsltDPVGEPLN-LVDVPEAKTFPGIgTALDDTA---YIL 675
Cdd:cd05929 75 RAPRA-------------EACAIIEIKAAALVCGL---------FTGGGALDgLEDYEAAEGGSPE-TPIEDEAagwKML 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 676 FTSGSTGRPKGV--AISHRSIDNRLR--WQQSQIPVGASTQDRAGDrILHKTPISFDVHVwelywpLQEGAAVVIAApdg 751
Cdd:cd05929 132 YSGGTTGRPKGIkrGLPGGPPDNDTLmaAALGFGPGADSVYLSPAP-LYHAAPFRWSMTA------LFMGGTLVLME--- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 752 HRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRtlAEAGFGSGEQQRHVRyLICSgeALQKDQILsahNIMGVYPL 831
Cdd:cd05929 202 KFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVR--NAYDLSSLKRVIHAA-APCP--PWVKEQWI---DWGGPIIW 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 832 NLYGPTEaAVDVTFWDSSqnpECSTVP--IGQPVwNTQTRILDQALQPIPPGFVGELYLSGAQlAAGYQNNPEATAQAFi 909
Cdd:cd05929 274 EYYGGTE-GQGLTIINGE---EWLTHPgsVGRAV-LGKVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAAR- 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 910 ldNATGerlYRT-GDLaewnltatnqepGTLAKNprGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLlyt 988
Cdd:cd05929 347 --NEGG---WSTlGDV------------GYLDED--GYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVV--- 404
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503164607 989 KTPEP----ALTAFLEIGDvsETERNRIVAQA-RQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:cd05929 405 GVPDEelgqRVHAVVQPAP--GADAGTALAEElIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
532-984 |
7.35e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 53.53 E-value: 7.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 532 QVLTYHELDARARALAkAMLEAGVCPGTA--VGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSAL 609
Cdd:PRK07867 27 SFTSWREHIRGSAARA-AALRARLDPTRPphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIAHADCQLV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 610 VYGSGLSPIA---EAELKPANTQSLcglqqlEFTSLTDPvgeplnlvdvpEAKTFPGIGTAL-DDTAYILFTSGSTGRPK 685
Cdd:PRK07867 106 LTESAHAELLdglDPGVRVINVDSP------AWADELAA-----------HRDAEPPFRVADpDDLFMLIFTSGTSGDPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 686 GVAISHRSIdnrlrwqqsQIPvGASTQDRAGDRilhktpiSFDVHVweLYWPLQEGAAVVIA---APDGHRDPAYLARVI 762
Cdd:PRK07867 169 AVRCTHRKV---------ASA-GVMLAQRFGLG-------PDDVCY--VSMPLFHSNAVMAGwavALAAGASIALRRKFS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 763 AEQ--------NVTCLHFVPTMLTAFLEAP----SAKRTLaEAGFGSGEQQRHVRYLICSgealqkdqilsahniMGVYP 830
Cdd:PRK07867 230 ASGflpdvrryGATYANYVGKPLSYVLATPerpdDADNPL-RIVYGNEGAPGDIARFARR---------------FGCVV 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 831 LNLYGPTEAAVDVTfwdssQNPECSTVPIGQPVWNTQtrILD-QALQPIPPG------------FVGELY-LSGAQLAAG 896
Cdd:PRK07867 294 VDGFGSTEGGVAIT-----RTPDTPPGALGPLPPGVA--IVDpDTGTECPPAedadgrllnadeAIGELVnTAGPGGFEG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 897 YQNNPEATAqafildnatgERL----YRTGDLAewnltatnqepgtlAKNPRGVILYRGRTDHQVKLHGQRLELGDIETT 972
Cdd:PRK07867 367 YYNDPEADA----------ERMrggvYWSGDLA--------------YRDADGYAYFAGRLGDWMRVDGENLGTAPIERI 422
|
490
....*....|..
gi 503164607 973 LSHVEGVHSAVV 984
Cdd:PRK07867 423 LLRYPDATEVAV 434
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
531-694 |
9.41e-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: 53.45 E-value: 9.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 531 SQVLTYHELDARARALAKAML-EAGVCPGTAVGLrFHRGLEQYIALYAALYAGFVYVPILPdlPAERVSSMMEDAQCSAl 609
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLaHAGLRPGDTVAL-LLGNEPAFLWIWLGLAKLGCPVAFLN--TNIRSKSLLHCFRCCG- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 610 vyGSGLspIAEAELKPANTQSLCGLQQ-------LEFTSLTDPVGEPLNLVDVPEAKTFPG---IGTALDDTAYILFTSG 679
Cdd:cd05938 79 --AKVL--VVAPELQEAVEEVLPALRAdgvsvwyLSHTSNTEGVISLLDKVDAASDEPVPAslrAHVTIKSPALYIYTSG 154
|
170
....*....|....*
gi 503164607 680 STGRPKGVAISHRSI 694
Cdd:cd05938 155 TTGLPKAARISHLRV 169
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
658-1048 |
4.24e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 51.50 E-value: 4.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 658 AKTFPGIGTAL---DDTAYILFTSGSTGRPKGVAISHRSIDNRLRWQQSQIPVGAStqdragDRILHKTPI--SFDVHVW 732
Cdd:PRK06814 779 AGRFPLVYFCNrdpDDPAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPE------DKVFNALPVfhSFGLTGG 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 733 ELYwPLQEGAAVVIAAPDGHrdpaYlaRVIAE----QNVTCLHFVPTMLTAFleapsaKRTLAEAGFgsgeqqRHVRYLI 808
Cdd:PRK06814 853 LVL-PLLSGVKVFLYPSPLH----Y--RIIPEliydTNATILFGTDTFLNGY------ARYAHPYDF------RSLRYVF 913
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 809 CSGEALQKDQILSAHNIMGVYPLNLYGPTEAAvdvtfwdssqnP--ECSTvpigqPVWN---TQTRIL---DQALQPIP- 879
Cdd:PRK06814 914 AGAEKVKEETRQTWMEKFGIRILEGYGVTETA-----------PviALNT-----PMHNkagTVGRLLpgiEYRLEPVPg 977
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 880 --PGfvGELYLSGAQLAAGYQnnpEATAQAFILDNATGErlYRTGDLAEWnltatnqepgtlakNPRGVILYRGRTDHQV 957
Cdd:PRK06814 978 idEG--GRLFVRGPNVMLGYL---RAENPGVLEPPADGW--YDTGDIVTI--------------DEEGFITIKGRAKRFA 1036
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 958 KLHGQRLELGDIETTLSHV-EGVHSAVVLLYTKTPEPALTAFLEIGDVSeteRNRIVAQARQhceNTLPDYMVPRLWHTT 1036
Cdd:PRK06814 1037 KIAGEMISLAAVEELAAELwPDALHAAVSIPDARKGERIILLTTASDAT---RAAFLAHAKA---AGASELMVPAEIITI 1110
|
410
....*....|..
gi 503164607 1037 AQFPVSPSGKTD 1048
Cdd:PRK06814 1111 DEIPLLGTGKID 1122
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
559-1052 |
5.13e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 50.42 E-value: 5.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 559 TAVGLRF---HRGLEQYIALYAALY-AGFVYVPILPDLPAERVSSMMEDAQCSALVYGSGLSPIAEAELKPANTQSLcgL 634
Cdd:PRK08308 29 EAAGNRFavcLKDPFDIITLVFFLKeKGASVLPIHPDTPKEAAIRMAKRAGCHGLLYGESDFTKLEAVNYLAEEPSL--L 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 635 QqleftsltdpvgeplnlvdvpeaktfpgigtalddtayilFTSGSTGRPKGVAISHRSIDN-------RLRWQQSQIPV 707
Cdd:PRK08308 107 Q----------------------------------------YSSGTTGEPKLIRRSWTEIDReieayneALNCEQDETPI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 708 GAStqdragdrilhktPISfdvHVWEL----YWPLQEGAAVVIAapdGHRDPAYLARVIAEQNVTCLHFVPTMLTAFlea 783
Cdd:PRK08308 147 VAC-------------PVT---HSYGLicgvLAALTRGSKPVII---TNKNPKFALNILRNTPQHILYAVPLMLHIL--- 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 784 psakrtlaeAGFGSGEQQRHVryLICSGeALQKDQILSAHNIMGVYPLNLYGPTEAAVdvtfwdSSQNPECST-VPIGQP 862
Cdd:PRK08308 205 ---------GRLLPGTFQFHA--VMTSG-TPLPEAWFYKLRERTTYMMQQYGCSEAGC------VSICPDMKShLDLGNP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 863 vwntqtrildqalqpippgfvgelyLSGAQLAAGyqNNPEATAQAFIldnATGERLYRTGDLAEWNltatnqepgtlakn 942
Cdd:PRK08308 267 -------------------------LPHVSVSAG--SDENAPEEIVV---KMGDKEIFTKDLGYKS-------------- 302
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 943 PRGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHSAVVLlytKTPEPALTAFLEIGDVSETERNriVAQARQHCEN 1022
Cdd:PRK08308 303 ERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVY---RGKDPVAGERVKAKVISHEEID--PVQLREWCIQ 377
|
490 500 510
....*....|....*....|....*....|
gi 503164607 1023 TLPDYMVPRLWHTTAQFPVSPSGKTDRKNL 1052
Cdd:PRK08308 378 HLAPYQVPHEIESVTEIPKNANGKVSRKLL 407
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
485-694 |
6.94e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 50.48 E-value: 6.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 485 HPiEYKTLLQRFQDALTRYPNEPALyACAPDEDGTlspqsPQAYEFsqvLTYHELDARARALAKAMLEAGVCPGTAVGLR 564
Cdd:PLN02736 40 HP-EIGTLHDNFVYAVETFRDYKYL-GTRIRVDGT-----VGEYKW---MTYGEAGTARTAIGSGLVQHGIPKGACVGLY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 565 FHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQ-----CSALVYGSGLSPIAE--------------AELKP 625
Cdd:PLN02736 110 FINRPEWLIVDHACSAYSYVSVPLYDTLGPDAVKFIVNHAEvaaifCVPQTLNTLLSCLSEipsvrlivvvggadEPLPS 189
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503164607 626 ANTQSLCGL---QQLEFTSLTDPVgeplnlvdvpeaktfPGIGTALDDTAYILFTSGSTGRPKGVAISHRSI 694
Cdd:PLN02736 190 LPSGTGVEIvtySKLLAQGRSSPQ---------------PFRPPKPEDVATICYTSGTTGTPKGVVLTHGNL 246
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
15-400 |
2.59e-05 |
|
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: 48.21 E-value: 2.59e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 15 PLTKSAQGIYLAAIIDPKNPCYNTAEIMECPPETNLDYLREAFIQLYRENEGFRVQTRVQ-TGRPEQRVipldefLTNLE 93
Cdd:cd19536 3 PLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDgLGQPVQVV------HRQAQ 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 94 VlPVISLQIQEETEEQnpvpAAVRGWASELISEPLRTDAGVTVRSAVTYYGGK---LWVYhSFSHVVADGFAAFNGLSRV 170
Cdd:cd19536 77 V-PVTELDLTPLEEQL----DPLRAYKEETKIRRFDLGRAPLVRAALVRKDERerfLLVI-SDHHSILDGWSLYLLVKEI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 171 AAIYRALSAGKPLPTVKRASLMELLRadHAAEHA-REEDLALWTSEQVEVLSQpdTSLAARSASPAPQALREVLTLPDKL 249
Cdd:cd19536 151 LAVYNQLLEYKPLSLPPAQPYRDFVA--HERASIqQAASERYWREYLAGATLA--TLPALSEAVGGGPEQDSELLVSVPL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 250 QRDMLEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGVPQMNRifgaqvPAET----RALGKTsaqtgttaVNVLPVQ 325
Cdd:cd19536 227 PVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGR------SEETtgaeRLLGLF--------LNTLPLR 292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 503164607 326 VS-GMGSIAQALDSVKNQYARNASHplaRQEDLERLAQSNDSR-LFGAQINVIPFDAALPLGAPTENAPASVGYIHN 400
Cdd:cd19536 293 VTlSEETVEDLLKRAQEQELESLSH---EQVPLADIQRCSEGEpLFDSIVNFRHFDLDFGLPEWGSDEGMRRGLLFS 366
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
520-692 |
2.67e-05 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 48.33 E-value: 2.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 520 LSPQSPQAYEFSQVLTYHELDARARALAKAMLEAGVCPGTAVGLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVss 599
Cdd:PRK09029 15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL-- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 600 mmedaqcsalvygsglspiaeAELKPANtqslcglqQLEFTSLTDPVGEPLNLVDVPEAKTFPGIGTALDDT--AYILFT 677
Cdd:PRK09029 93 ---------------------EELLPSL--------TLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQrlATMTLT 143
|
170
....*....|....*
gi 503164607 678 SGSTGRPKGVAISHR 692
Cdd:PRK09029 144 SGSTGLPKAAVHTAQ 158
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
670-924 |
6.72e-05 |
|
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: 46.91 E-value: 6.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 670 DTAYILFTSGSTGRPKGVAISHRSidnrLRWQQSQipVGASTQDRAGDRILHKTPIsfdVHVWELYWPL---QEGAAVVI 746
Cdd:cd17636 1 DPVLAIYTAAFSGRPNGALLSHQA----LLAQALV--LAVLQAIDEGTVFLNSGPL---FHIGTLMFTLatfHAGGTNVF 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 747 AApdgHRDPAYLARVIAEQNVTCLHFVPTMLTAFLEAPSAKRtlaeagfgsgeqqRHVRYLICSGEALQKDQILSAHNIM 826
Cdd:cd17636 72 VR---RVDAEEVLELIEAERCTHAFLLPPTIDQIVELNADGL-------------YDLSSLRSSPAAPEWNDMATVDTSP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 827 GVYPLNLYGPTEAAVDVTFwdsSQNPECSTVPIGQPVWNTQTRILDQALQPIPPGFVGELYLSGAQLAAGYQNNPEATAQ 906
Cdd:cd17636 136 WGRKPGGYGQTEVMGLATF---AALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNAR 212
|
250
....*....|....*...
gi 503164607 907 AFildnATGerLYRTGDL 924
Cdd:cd17636 213 RT----RGG--WHHTNDL 224
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
491-694 |
1.25e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 46.51 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 491 TLLQRFQDALTRYPNEPAL-Y--------ACAPDEDGTLSPQSPQAYEFSQVLTYHELDARARALAKAMLEAGVCPGTAV 561
Cdd:PTZ00216 70 NFLQRLERICKERGDRRALaYrpvervekEVVKDADGKERTMEVTHFNETRYITYAELWERIVNFGRGLAELGLTKGSNV 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 562 GLRFHRGLEQYIALYAALYAGFVYVPILPDLPAERVSSMMEDAQCSALVYGSG-----LSPIAEAELK----------PA 626
Cdd:PTZ00216 150 AIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKnvpnlLRLMKSGGMPnttiiyldslPA 229
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503164607 627 NTQSLcGLQQLEFTSLTDpVGEPlnlvdvpEAKTFPG-IGTALDDTAYILFTSGSTGRPKGVAISHRSI 694
Cdd:PTZ00216 230 SVDTE-GCRLVAWTDVVA-KGHS-------AGSHHPLnIPENNDDLALIMYTSGTTGDPKGVMHTHGSL 289
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1063-1137 |
2.56e-04 |
|
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: 41.08 E-value: 2.56e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503164607 1063 TADGPHGLLEQQISEIIAGVLGRS---QFGVTEDFLAAGGNSLAALSVIAKIEENLGKMLSIGALFANPTVKGIAAAL 1137
Cdd:smart00823 5 PPAERRRLLLDLVREQVAAVLGHAaaeAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHL 82
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
147-451 |
4.69e-04 |
|
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: 44.50 E-value: 4.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 147 LWVYHsfsHVVADGFAAFNGLSRVAAIYRALSAGKP--LPTVKRASlmellraDHAA---EHAREEDLALWtSEQVEVLS 221
Cdd:cd19543 131 VWSFH---HILLDGWSLPILLKELFAIYAALGEGQPpsLPPVRPYR-------DYIAwlqRQDKEAAEAYW-REYLAGFE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 222 QPDTSLAARSASPAPQALRE--VLTLPDKLQRDMLEIGKMYGTSWPVTVTGAVGSYLARIGVHRSAAFGV-----Pqmnr 294
Cdd:cd19543 200 EPTPLPKELPADADGSYEPGevSFELSAELTARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTtvsgrP---- 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 295 ifgAQVPAETRALGktsaqtgtTAVNVLP--VQVSGMGSIAQALDSVKNQYARNASH---PLARqedlerlAQSNDSRlf 369
Cdd:cd19543 276 ---AELPGIETMVG--------LFINTLPvrVRLDPDQTVLELLKDLQAQQLELREHeyvPLYE-------IQAWSEG-- 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 370 GAQInvipFDAAL-----PLGAPTENAPASVGY-IHNISAGPVADMTITLRGIPgrGHTISVELDANPNLYTREHVEFHA 443
Cdd:cd19543 336 KQAL----FDHLLvfenyPVDESLEEEQDEDGLrITDVSAEEQTNYPLTVVAIP--GEELTIKLSYDAEVFDEATIERLL 409
|
....*...
gi 503164607 444 RHLQNWLE 451
Cdd:cd19543 410 GHLRRVLE 417
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
669-1053 |
5.58e-04 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 43.88 E-value: 5.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 669 DDTAYILFTSGSTGRPKGVAISHRSIdnrlrwqqsqIPVGASTQDRAGD--RILHKTPISFDVHVWELYWPLQEGAA-VV 745
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAAL----------TASADATHDRLGGpgQWLLALPAHHIAGLQVLVRSVIAGSEpVE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 746 IAAPDGHrDPAYLARVIAE----QNVTCLhfVPTMLTAFLEAPSAKRTLAEagFGSgeqqrhvrylICSGEALQKDQILS 821
Cdd:PRK07824 105 LDVSAGF-DPTALPRAVAElgggRRYTSL--VPMQLAKALDDPAATAALAE--LDA----------VLVGGGPAPAPVLD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 822 AHNIMGVYPLNLYGPTEAAvdvtfwdssqnPECstVPIGQPVWNTQTRILDqalqpippgfvGELYLSGAQLAAGYQNNP 901
Cdd:PRK07824 170 AAAAAGINVVRTYGMSETS-----------GGC--VYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 902 EATAQAfildnatGERLYRTGDLaewnltatnqepGTLAKnprGVILYRGRTDHQVKLHGQRLELGDIETTLSHVEGVHS 981
Cdd:PRK07824 226 DPDPFA-------EPGWFRTDDL------------GALDD---GVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVAD 283
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503164607 982 AVVLlytKTPEPALTAFLEIGDVSETERNRIVAQARQHCENTLPDYMVPRLWHTTAQFPVSPSGKTDRKNLA 1053
Cdd:PRK07824 284 CAVF---GLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALV 352
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
670-791 |
1.17e-03 |
|
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: 43.32 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 670 DTAYILFTSGSTGRPKGVAisHRsidnrlrwqQSQIPVGASTQdragdrilHKTpiSFDVHVWELYW------------- 736
Cdd:cd05966 232 DPLFILYTSGSTGKPKGVV--HT---------TGGYLLYAATT--------FKY--VFDYHPDDIYWctadigwitghsy 290
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503164607 737 ----PLQEGAAVVI--AAPDgHRDPAYLARVIAEQNVTCLHFVPT---MLTAFLEAPSAKRTLA 791
Cdd:cd05966 291 ivygPLANGATTVMfeGTPT-YPDPGRYWDIVEKHKVTIFYTAPTairALMKFGDEWVKKHDLS 353
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
14-205 |
3.16e-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: 41.60 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 14 IPLTKSAQGIYLAAIIDPKNPCYNTAEIMECPPETNLDYLREAFIQLYRENEGFR-VQTRVQTGRPEQRVIPLDEFLTNL 92
Cdd:cd19539 2 IPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRtLLVRDDGGVPRQEILPPGPAPLEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503164607 93 EVLPVISLQIQEETEEQnpvpaavrgwASELISEPLRTDAGVTVRSAV-TYYGGKLWVYHSFSHVVADGFAAFNGLSRVA 171
Cdd:cd19539 82 RDLSDPDSDRERRLEEL----------LRERESRGFDLDEEPPIRAVLgRFDPDDHVLVLVAHHTAFDAWSLDVFARDLA 151
|
170 180 190
....*....|....*....|....*....|....*.
gi 503164607 172 AIYRALSAGKPlptvkrASLMELLR--ADHAAEHAR 205
Cdd:cd19539 152 ALYAARRKGPA------APLPELRQqyKEYAAWQRE 181
|
|
| |
