|
Name |
Accession |
Description |
Interval |
E-value |
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
7-1295 |
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: 907.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 7 ISPQQKHLWLQQKDNYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGMNIPFQSISDAPTYNHISLAE 86
Cdd:COG1020 22 AAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 87 YDWSRLSSQVQKAKidtlfQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACLDG 166
Cdd:COG1020 102 DLEALAEAAAEAAA-----AAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 167 EEIS--EEVMQYADVSEWLNELLESEDTETARNYWQQQDISSVLNLRIPFeiknDHQSSGEISFAPQSLCLAMNRDTVEK 244
Cdd:COG1020 177 APLPlpPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPT----DRPRPAVQSYRGARVSFRLPAELTAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 245 LEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDALKFSELMERVSES 324
Cdd:COG1020 253 LRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRET 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 325 LRFVKKWQEY--------FNWENFISTNekfaarPFFPFCFDFTQQSQSYVN-GNIAFSEYKKSANIDKFQIKLSSGYSQ 395
Cdd:COG1020 333 LLAAYAHQDLpferlveeLQPERDLSRN------PLFQVMFVLQNAPADELElPGLTLEPLELDSGTAKFDLTLTVVETG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 396 DNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLLIDFNNTKIEFPHDKCLHELFAAQV 475
Cdd:COG1020 407 DGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQA 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 476 ERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLG 555
Cdd:COG1020 487 ARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLA 566
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 556 FMLEDAQIPILLTQQRLVDKFVEHKTQIICLDRdlPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVN 635
Cdd:COG1020 567 YMLEDAGARLVLTQSALAARLPELGVPVLALDA--LALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVN 644
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 636 YLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEKE--EIEALSALLQsDQNYSLVKITPAHLEMLN 713
Cdd:COG1020 645 LLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEArrDPAALAELLA-RHRVTVLNLTPSLLRALL 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 714 QMLPnhKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSLSGAILIGRPIANTQLYL 793
Cdd:COG1020 724 DAAP--EALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVYV 801
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 794 LDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSdEPNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRG 873
Cdd:COG1020 802 LDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFG-FPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRG 880
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 874 FRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPK-EQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTH 952
Cdd:COG1020 881 FRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEaGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGN 960
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 953 GKVDRQALPQPDTSRLDTlkvEFIAPRDRLELKLANIWENLLNVHPIGIKDSFFELGGHSLLAVRLMAHINQEFGKNLAL 1032
Cdd:COG1020 961 GKLDRLALPAPAAAAAAA---AAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLL 1037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1033 ATLFQNPTIEKLANLLRQTSEISS--WSPLVEIQTGNSQYPFFCLPGGGGNVLYLHELARDLGSEQTFYGLQAPGLNGES 1110
Cdd:COG1020 1038 LLFLAAAAAAAAAAAAAAAAAAAAplAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLAL 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1111 DPLTSVEEMAAYYIQAIQSVQPEGPYFLGGHSFGGIVAYEIAQQLVKSGHEVALVAILDAPAPVASDKPIYIDVDDATRL 1190
Cdd:COG1020 1118 LLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLL 1197
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1191 TETARLIERWAGKSLNISYEILQPLELDAQLEYLKEQLIAVGLLPTGTETKQVRGLVQVFETNLQASIKYSPQEVYPHRL 1270
Cdd:COG1020 1198 LLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALA 1277
|
1290 1300
....*....|....*....|....*
gi 2129675820 1271 TLLRAREVNAEDAALLTELRQDPAW 1295
Cdd:COG1020 1278 LLLPALARARAARTARALALLLLLA 1302
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
10-1048 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 718.87 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 10 QQKHLWLQQKD-NYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGmniPFQSISDAPTynHISLAEYD 88
Cdd:PRK12467 56 QERQWFLWQLDpDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEE---GFRQVIDASL--SLTIPLDD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 89 WSRLSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACLDGEE 168
Cdd:PRK12467 131 LANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGRE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 169 IS--EEVMQYADVSEWLNELLESEDTETARNYWQQQ--DISSVLnlripfEIKNDHQSSGEISFAPQSLCLAMNRDTVEK 244
Cdd:PRK12467 211 PSlpALPIQYADYAIWQRSWLEAGERERQLAYWQEQlgGEHTVL------ELPTDRPRPAVPSYRGARLRVDLPQALSAG 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 245 LEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDALKFSELMERVSES 324
Cdd:PRK12467 285 LKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 325 LRFVKKWQ--------EYFNWENFISTNekfaarPFFPFCFDF------TQQSQSYVNGNIAFSEYKKSANIDKFQIKLS 390
Cdd:PRK12467 365 ALGAQAHQdlpfeqlvEALQPERSLSHS------PLFQVMFNHqntatgGRDREGAQLPGLTVEELSWARHTAQFDLALD 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 391 SGYSQDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLLIDFNNTKIEFPHDkCLHEL 470
Cdd:PRK12467 439 TYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPD-CVHQL 517
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 471 FAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYP 550
Cdd:PRK12467 518 IEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYP 597
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 551 QERLGFMLEDAQIPILLTQQRLVDKF-VEHKTQIICLDRDLPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIP 629
Cdd:PRK12467 598 QDRLAYMLDDSGVRLLLTQSHLLAQLpVPAGLRSLCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAIS 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 630 HRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEKE--EIEALSALLqSDQNYSLVKITPA 707
Cdd:PRK12467 678 HGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCarDAEAFAALM-ADQGVTVLKIVPS 756
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 708 HLEMLNQMlPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSLSGAILIGRPIA 787
Cdd:PRK12467 757 HLQALLQA-SRVALPRPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFGNVPIGQPLA 835
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 788 NTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSdEPNSRLYKTGDLARYLPDGNIEYLGRIDH 867
Cdd:PRK12467 836 NLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFG-ADGGRLYRTGDLARYRADGVIEYLGRMDH 914
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 868 QVKIRGFRIELEEIESLLAQHPLVNAVTVIArEDQPGDKRLVGYIVPK------EQAPTSSELRQFLQSKLPEYMIPSAF 941
Cdd:PRK12467 915 QVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLVPAavadgaEHQATRDELKAQLRQVLPDYMVPAHL 993
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 942 VMLEVIPLTTHGKVDRQALPQPDTSrldTLKVEFIAPRDRLELKLANIWENLLNVHPIGIKDSFFELGGHSLLAVRLMAH 1021
Cdd:PRK12467 994 LLLDSLPLTPNGKLDRKALPKPDAS---AVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISR 1070
|
1050 1060
....*....|....*....|....*..
gi 2129675820 1022 INQEFGKNLALATLFQNPTIEKLANLL 1048
Cdd:PRK12467 1071 VRQRLGIQVPLRTLFEHQTLAGFAQAV 1097
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
10-1050 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 706.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 10 QQKHLWLQQKD-NYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGmnipfQSISDAPTYNHISLAEYD 88
Cdd:PRK12316 56 QQRMWFLWQLEpQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGAD-----DSLAQVPLDRPLEVEFED 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 89 WSRLSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACLDGEE 168
Cdd:PRK12316 131 CSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAE 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 169 ISEEVM--QYADVSEWLNELLESEDTETARNYWQQQdissvLNLRIP-FEIKNDHQSSGEISFAPQSLCLAMNRDTVEKL 245
Cdd:PRK12316 211 PGLPALpiQYADYALWQRSWLEAGEQERQLEYWRAQ-----LGEEHPvLELPTDHPRPAVPSYRGSRYEFSIDPALAEAL 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 246 EILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDALKFSELMERVSESL 325
Cdd:PRK12316 286 RGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTV 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 326 RFVKKWQ--------EYFNWENFISTNekfaarPFFPFCFDFT-----QQSQSYVNGnIAFSEYKKSANIDKFQIKLSSG 392
Cdd:PRK12316 366 LGAQAHQdlpferlvEALKVERSLSHS------PLFQVMYNHQplvadIEALDTVAG-LEFGQLEWKSRTTQFDLTLDTY 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 393 YSQDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLLIDFNNTKIEFPHDKCLHELFA 472
Cdd:PRK12316 439 EKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFE 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 473 AQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQE 552
Cdd:PRK12316 519 EQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAE 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 553 RLGFMLEDAQIPILLTQQRLVDKF-VEHKTQIICLDRDLPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHR 631
Cdd:PRK12316 599 RLAYMLEDSGVQLLLSQSHLGRKLpLAAGVQVLDLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHR 678
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 632 GLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEKE--EIEALSALLQSDQnYSLVKITPAHL 709
Cdd:PRK12316 679 ALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhrDPAKLVELINREG-VDTLHFVPSML 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 710 EMLNQMlPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVG-CCVYEVDEQtslSGAILIGRPIAN 788
Cdd:PRK12316 758 QAFLQD-EDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDvTHWTCVEEG---GDSVPIGRPIAN 833
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 789 TQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDepNSRLYKTGDLARYLPDGNIEYLGRIDHQ 868
Cdd:PRK12316 834 LACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVA--GERMYRTGDLARYRADGVIEYAGRIDHQ 911
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 869 VKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQpgdkRLVGYIVPK-EQAPTSSELRQFLQSKLPEYMIPSAFVMLEVI 947
Cdd:PRK12316 912 VKLRGLRIELGEIEARLLEHPWVREAAVLAVDGK----QLVGYVVLEsEGGDWREALKAHLAASLPEYMVPAQWLALERL 987
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 948 PLTTHGKVDRQALPQPDTSrldTLKVEFIAPRDRLELKLANIWENLLNVHPIGIKDSFFELGGHSLLAVRLMAHINQEfG 1027
Cdd:PRK12316 988 PLTPNGKLDRKALPAPEAS---VAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-G 1063
|
1050 1060
....*....|....*....|...
gi 2129675820 1028 KNLALATLFQNPTIEKLANLLRQ 1050
Cdd:PRK12316 1064 IQLSPRDLFQHQTIRSLALVAKA 1086
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-1064 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 689.59 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 7 ISPQQKHLWL--QQKDNYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGMniPFQSISDAptynhISL 84
Cdd:PRK12467 1119 LSYAQERQWFlwQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGR--TRQVIHPV-----GSL 1191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 85 AEYDWSRLSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACL 164
Cdd:PRK12467 1192 TLEEPLLLAADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYS 1271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 165 DGE--EISEEVMQYADVSEWLNELLESEDTETARNYWQQQDISSVLNLRIPFeiknDHQSSGEISFAPQSLCLAMNRDTV 242
Cdd:PRK12467 1272 QGQslQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPT----DRPRPAVQSHRGARLAFELPPALA 1347
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 243 EKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDALKFSELMERVS 322
Cdd:PRK12467 1348 EGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVK 1427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 323 ES---------LRFvKKWQEYFNWENFISTNekfaarPFFPFCFDF--TQQSQSYVNGNIAFSEYKKSANIDKFQIKLSS 391
Cdd:PRK12467 1428 QAaleaqahqdLPF-EQLVEALQPERSLSHS------PLFQVMFNHqrDDHQAQAQLPGLSVESLSWESQTAQFDLTLDT 1500
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 392 GYSQDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLLIDFNNTKIEFPHDKCLHELF 471
Cdd:PRK12467 1501 YESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLI 1580
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 472 AAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQ 551
Cdd:PRK12467 1581 EDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPR 1660
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 552 ERLGFMLEDAQIPILLTQQRLVDKF-VEHKTQIICLDRDLPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPH 630
Cdd:PRK12467 1661 ERLAYMIEDSGIELLLTQSHLQARLpLPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRH 1740
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 631 RGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLP--EKEEIEALSALLQSDQNYSLVKiTPAH 708
Cdd:PRK12467 1741 GALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPpgAHRDPEQLIQLIERQQVTTLHF-VPSM 1819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 709 LEMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDeQTSLSGAIL--IGRPI 786
Cdd:PRK12467 1820 LQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERLPDTGLFNLYGPTETAVDVTHWTCR-RKDLEGRDSvpIGQPI 1898
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 787 ANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDePNSRLYKTGDLARYLPDGNIEYLGRID 866
Cdd:PRK12467 1899 ANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGT-VGSRLYRTGDLARYRADGVIEYLGRID 1977
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 867 HQVKIRGFRIELEEIESLLAQHPLVNAVTVIArEDQPGDKRLVGYIVPKE---------QAPTSSELRQFLQSKLPEYMI 937
Cdd:PRK12467 1978 HQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYVVPTDpglvdddeaQVALRAILKNHLKASLPEYMV 2056
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 938 PSAFVMLEVIPLTTHGKVDRQALPQPDTSRLDTlkvEFIAPRDRLELKLANIWENLLNVHPIGIKDSFFELGGHSLLAVR 1017
Cdd:PRK12467 2057 PAHLVFLARMPLTPNGKLDRKALPAPDASELQQ---AYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQ 2133
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*
gi 2129675820 1018 LMAHINQEfGKNLALATLFQNPTIEKLANLLRQT--------SEISSWSPLVEIQ 1064
Cdd:PRK12467 2134 VVSRARQA-GIRFTPKDLFQHQTVQSLAAVAQEGdgtvsidqGPVTGDLPLLPIQ 2187
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
7-1174 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 676.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 7 ISPQQK----HLWLQQKDNYqaYCTQIAINITGnLNSDILKLALANLSDRYEIFHTAFHSLPGMNIPFQSIsdaptYNHI 82
Cdd:PRK12467 2649 LSPMQQgmlfHTLYEGGAGD--YINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGELEEPLQVV-----YKQA 2720
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 83 SL--AEYDWSrlSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAY 160
Cdd:PRK12467 2721 RLpfSRLDWR--DRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRY 2798
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 161 TacldGEEISEEVMQYADVSEWLnellESEDTETARNYWQQQdissVLNLRIPFEIKNDHQSSGEISFAPQ-SLCLAMNR 239
Cdd:PRK12467 2799 F----GQPPPAREGRYRDYIAWL----QAQDAEASEAFWKEQ----LAALEEPTRLARALYPAPAEAVAGHgAHYLHLDA 2866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 240 DTVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGR--EYDELKGVFGLLTKYLPI--HSRLEdalkfs 315
Cdd:PRK12467 2867 TQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRpaQLRGAEQQLGLFINTLPViaSPRAE------ 2940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 316 elmERVSESLRFVKkwqeyfnwenfistNEKFAARPF--FPFcFDFT----QQSQSYVNGNIAFSEY------KKSANID 383
Cdd:PRK12467 2941 ---QTVSDWLQQVQ--------------AQNLALREFehTPL-ADIQrwagQGGEALFDSILVFENYpisealKQGAPSG 3002
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 384 kFQIKLSSGYSQ------------DNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLL 451
Cdd:PRK12467 3003 -LRFGAVSSREQtnypltlavglgDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVL 3081
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 452 IDFNNTKIEFPHDKCLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIG 531
Cdd:PRK12467 3082 HAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVA 3161
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 532 ILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQRLVDKF-VEHKTQIICLDRDLPEnaTLSIDNPVSNVTSENL 610
Cdd:PRK12467 3162 LLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLpAPAGDTALTLDRLDLN--GYSENNPSTRVMGENL 3239
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 611 AYIIYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLP-EKEEIEAL 689
Cdd:PRK12467 3240 AYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDnDLWDPEEL 3319
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 690 SALLQSdQNYSLVKITPAhleMLNQMLPNHKG--VTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCV 767
Cdd:PRK12467 3320 WQAIHA-HRISIACFPPA---YLQQFAEDAGGadCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTL 3395
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 768 YEVD-EQTSLSGAILIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDEpNSRLYK 846
Cdd:PRK12467 3396 WKCGgDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGS-GGRLYR 3474
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 847 TGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGdKRLVGYIVPK-EQAPTSSELR 925
Cdd:PRK12467 3475 TGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGG-KQLVAYVVPAdPQGDWRETLR 3553
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 926 QFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALPQPDTSRLDtlkvEFIAPRDRLELKLANIWENLLNVHPIGIKDSF 1005
Cdd:PRK12467 3554 DHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSR----EYVAPRSEVEQQLAAIWADVLGVEQVGVTDNF 3629
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1006 FELGGHSLLAVRLMAHINQEFGKNLALATLFQNPTIEKLANLLrQTSEISSwSPLVEIQTGNSQYP-FFCLPGGGGNVLY 1084
Cdd:PRK12467 3630 FELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS-PLGDVPV-NLLLDLNRLETGFPaLFCRHEGLGTVFD 3707
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1085 LHELARDLGSEQTFYGLQAPGLNGESDPLTSVEEMAAYYIQAIQSVQPEGPYFLGGHSFGGIVAYEIAQQLVKSGHEVAL 1164
Cdd:PRK12467 3708 YEPLAVILEGDRHVLGLTCRHLLDDGWQDTSLQAMAVQYADYILWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAF 3787
|
1210
....*....|
gi 2129675820 1165 VAILDAPAPV 1174
Cdd:PRK12467 3788 LGLFDNTLPL 3797
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-1048 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 673.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 7 ISPQQK----HLWLQQKDNYqaYCTQIAINITGnLNSDILKLALANLSDRYEIFHTAFHSLPGMNIPFQSIsdaptYNHI 82
Cdd:PRK12316 4105 LSPMQQgmlfHSLYEQEAGD--YINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGELGRPLQVV-----HKQV 4176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 83 SL--AEYDWsRLSSQVQkAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAY 160
Cdd:PRK12316 4177 SLpfAELDW-RGRADLQ-AALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERY 4254
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 161 TacldGEEISEEVMQYADVSEWLnellESEDTETARNYWQQQDISSVLNLRIPFEIKNDHQSSGEisfAPQSLCLAMNRD 240
Cdd:PRK12316 4255 S----GRPPAQPGGRYRDYIAWL----QRQDAAASEAFWREQLAALDEPTRLAQAIARADLRSAN---GYGEHVRELDAT 4323
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 241 TVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYD--ELKGVFGLLTKYLPIHSRLEDALKFSELM 318
Cdd:PRK12316 4324 ATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAElpGIEGQIGLFINTLPVIATPRAQQSVVEWL 4403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 319 ERV-SESLRFvkkwQEYFNWENF-ISTNEKFAARPFFPFCFDF-----TQQSQSYVNGNIAFSEYkksANIDK--FQIKL 389
Cdd:PRK12316 4404 QQVqRQNLAL----REHEHTPLYeIQRWAGQGGEALFDSLLVFenypvSEALQQGAPGGLRFGEV---TNHEQtnYPLTL 4476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 390 SSGYSqDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLLIDFNNTKIEFPHDKCLHE 469
Cdd:PRK12316 4477 AVGLG-ETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQ 4555
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 470 LFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTY 549
Cdd:PRK12316 4556 LVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEY 4635
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 550 PQERLGFMLEDAQIPILLTQQRLVDKF-VEHKTQIICLDRDlPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMI 628
Cdd:PRK12316 4636 PRERLAYMMEDSGAALLLTQSHLLQRLpIPDGLASLALDRD-EDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAV 4714
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 629 PHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEKEEIEALSALLQSDQNYSLVKITPAH 708
Cdd:PRK12316 4715 SHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVY 4794
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 709 LEMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEV-DEQTSLSGAILIGRPIA 787
Cdd:PRK12316 4795 LQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKArDGDACGAAYMPIGTPLG 4874
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 788 NTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsDEPNSRLYKTGDLARYLPDGNIEYLGRIDH 867
Cdd:PRK12316 4875 NRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF-GAPGGRLYRTGDLARYRADGVIDYLGRVDH 4953
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 868 QVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDqPGDKRLVGYIVPKE---------QAPTSSELRQFLQSKLPEYMIP 938
Cdd:PRK12316 4954 QVKIRGFRIELGEIEARLREHPAVREAVVIAQEG-AVGKQLVGYVVPQDpaladadeaQAELRDELKAALRERLPEYMVP 5032
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 939 SAFVMLEVIPLTTHGKVDRQALPQPDTSrldTLKVEFIAPRDRLELKLANIWENLLNVHPIGIKDSFFELGGHSLLAVRL 1018
Cdd:PRK12316 5033 AHLVFLARMPLTPNGKLDRKALPQPDAS---LLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
|
1050 1060 1070
....*....|....*....|....*....|
gi 2129675820 1019 MAHINQEFGKNLALATLFQNPTIEKLANLL 1048
Cdd:PRK12316 5110 TSRIQLELGLELPLRELFQTPTLAAFVELA 5139
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
479-960 |
0e+00 |
|
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: 644.58 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 479 PNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFML 558
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 559 EDAQIPILLTQqrlvdkfvehktqiicldrdlpenatlsidnpvsnvtSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLS 638
Cdd:cd05930 81 EDSGAKLVLTD-------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 639 WCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEKEE--IEALSALLQsDQNYSLVKITPAHLEMLNQMl 716
Cdd:cd05930 124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRkdPEALADLLA-EEGITVLHLTPSLLRLLLQE- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 717 PNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSLSGAILIGRPIANTQLYLLDD 796
Cdd:cd05930 202 LELAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 797 KQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdEPNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRI 876
Cdd:cd05930 282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPF--GPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRI 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 877 ELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKE-QAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKV 955
Cdd:cd05930 360 ELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEgGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKV 439
|
....*
gi 2129675820 956 DRQAL 960
Cdd:cd05930 440 DRKAL 444
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
10-1072 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 633.92 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 10 QQKHLWlQQKDNYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGMNI----PFQSISDAPTYNHISLA 85
Cdd:PRK12316 2611 RQWFLW-QLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRqvilPNMSLRIVLEDCAGVAD 2689
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 86 EYDWSRLSSQVQkakidtlfqdtslRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACLD 165
Cdd:PRK12316 2690 AAIRQRVAEEIQ-------------RPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARR 2756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 166 GEE--ISEEVMQYADVSEWLNELLESEDTETARNYWQQQDISSVLNLRIPFeiknDHQSSGEISFAPQSLCLAMNRDTVE 243
Cdd:PRK12316 2757 GEQptLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPL----DRPRPALQSHRGARLDVALDVALSR 2832
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 244 KLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDALKFSELMERVSE 323
Cdd:PRK12316 2833 ELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKE 2912
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 324 SLRFVKKWQE--YFNWENFISTNEKFAARPFFPFCFDF-TQQSQSYVNGNIAFSEYKKSANIDKFQIKLSSGYSQDNLVV 400
Cdd:PRK12316 2913 QALGAQAHQDlpFEQLVEALQPERSLSHSPLFQVMYNHqSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGA 2992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 401 NFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLLIDFNNTKIEFPHDKCLHELFAAQVERTPN 480
Cdd:PRK12316 2993 SLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPD 3072
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 481 NIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLED 560
Cdd:PRK12316 3073 AVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLED 3152
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 561 AQIPILLTQQRLVDKFVEhKTQIICLDRDlPENAtlSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSWC 640
Cdd:PRK12316 3153 SGAQLLLSQSHLRLPLAQ-GVQVLDLDRG-DENY--AEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWM 3228
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 641 TNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLlpEKEEIEALSALLQSDQNYSLVKITPAHLEMLNQML--PN 718
Cdd:PRK12316 3229 QQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVL--AGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLeeED 3306
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 719 HKGVTETRALIIGGEALLGKSLNFWRDNAPktrIINEYGPTETVVGCCVYEVDEQTslSGAILIGRPIANTQLYLLDDKQ 798
Cdd:PRK12316 3307 AHRCTSLKRIVCGGEALPADLQQQVFAGLP---LYNLYGPTEATITVTHWQCVEEG--KDAVPIGRPIANRACYILDGSL 3381
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 799 KLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSdePNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIEL 878
Cdd:PRK12316 3382 EPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFV--PGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIEL 3459
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 879 EEIESLLAQHPLVNAVTVIAREDQpgdkRLVGYIVPKEQAPTSSE-LRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDR 957
Cdd:PRK12316 3460 GEIEARLLEHPWVREAVVLAVDGR----QLVAYVVPEDEAGDLREaLKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDR 3535
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 958 QALPQPDTSRLDTlkvEFIAPRDRLELKLANIWENLLNVHPIGIKDSFFELGGHSLLAVRLMAHINQEfGKNLALATLFQ 1037
Cdd:PRK12316 3536 KALPRPDAALLQQ---DYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQA-GIRFTPKDLFQ 3611
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|..
gi 2129675820 1038 NPTIEKLANLLR-------QTSEISSWSPLVEIQtgnsQYPF 1072
Cdd:PRK12316 3612 HQTIQGLARVARvgggvavDQGPVSGETLLLPIQ----QQFF 3649
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
469-964 |
0e+00 |
|
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: 623.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 469 ELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPT 548
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 549 YPQERLGFMLEDAQIPILLTQQRLVDKfVEHKTQIICLDRDLPENATLSIDNPVSNvtSENLAYIIYTSGSTGKPKGTMI 628
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPP-IAFIGLIDLLDEDTIYHEESENLEPVSK--SDDLAYVIYTSGSTGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 629 PHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPeKEEIEALSALLQ--SDQNYSLVKITP 706
Cdd:cd17655 158 EHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVR-KETVLDGQALTQyiRQNRITIIDLTP 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 707 AHLEMLNQMlpNHKGVTETRALIIGGEALLGKSLNFWRDN-APKTRIINEYGPTETVVGCCVYEVDEQTSLSGAILIGRP 785
Cdd:cd17655 237 AHLKLLDAA--DDSEGLSLKHLIVGGEALSTELAKKIIELfGTNPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 786 IANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdEPNSRLYKTGDLARYLPDGNIEYLGRI 865
Cdd:cd17655 315 LGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF--VPGERMYRTGDLARWLPDGNIEFLGRI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 866 DHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTsSELRQFLQSKLPEYMIPSAFVMLE 945
Cdd:cd17655 393 DHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPV-AQLREFLARELPDYMIPSYFIKLD 471
|
490
....*....|....*....
gi 2129675820 946 VIPLTTHGKVDRQALPQPD 964
Cdd:cd17655 472 EIPLTPNGKVDRKALPEPD 490
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
8-1060 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 622.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 8 SPQQKHLWL--QQKDNYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGmnIPFQSISDAPTYNhisLA 85
Cdd:PRK05691 679 SLAQNRLWLlwQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDG--VALQRIDAQGEFA---LQ 753
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 86 EYDWSRLSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACLD 165
Cdd:PRK05691 754 RIDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQ 833
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 166 GE--EISEEVMQYADVSEWLNELLESEDTETARNYWQQQ--DISSVLNLripfeiKNDHQSSGEISFAPQSLCLAMNRDT 241
Cdd:PRK05691 834 GQtaELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQlgDEQPVLEL------ATDHPRSARQAHSAARYSLRVDASL 907
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 242 VEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDALKFSELMERV 321
Cdd:PRK05691 908 SEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQV 987
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 322 SESLRFVKKWQEYfnweNFISTNEKFA-ARPFFPFCFDFTQQSQSY-----VNGNIAfSEYKKSANIDKFQIKLSSGYS- 394
Cdd:PRK05691 988 RQATLGAQAHQDL----PFEQLVEALPqAREQGLFQVMFNHQQRDLsalrrLPGLLA-EELPWHSREAKFDLQLHSEEDr 1062
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 395 QDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLLiDFNNTKIEfPHDKCLHELFAAQ 474
Cdd:PRK05691 1063 NGRLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLA-QWGQAPCA-PAQAWLPELLNEQ 1140
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 475 VERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERL 554
Cdd:PRK05691 1141 ARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERL 1220
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 555 GFMLEDAQIPILLTQQRLVDKFVEHKTQI-ICLDrdlpenaTLSIDN-----PVSNVTSENLAYIIYTSGSTGKPKGTMI 628
Cdd:PRK05691 1221 AYMLADSGVELLLTQSHLLERLPQAEGVSaIALD-------SLHLDSwpsqaPGLHLHGDNLAYVIYTSGSTGQPKGVGN 1293
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 629 PHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLP--EKEEIEALSALLQSdQNYSLVKITP 706
Cdd:PRK05691 1294 THAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGpgEHRDPQRIAELVQQ-YGVTTLHFVP 1372
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 707 AHLEMLNQMlPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGC----CVYEVDEQTSlsgailI 782
Cdd:PRK05691 1373 PLLQLFIDE-PLAAACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVthwqCQAEDGERSP------I 1445
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 783 GRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSdEPNSRLYKTGDLARYLPDGNIEYL 862
Cdd:PRK05691 1446 GRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLG-EDGARLYRTGDRARWNADGALEYL 1524
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 863 GRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGdKRLVGYIV-PKEQAPTSSELRQFLQSKLPEYMIPSAF 941
Cdd:PRK05691 1525 GRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAG-AQLVGYYTgEAGQEAEAERLKAALAAELPEYMVPAQL 1603
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 942 VMLEVIPLTTHGKVDRQALPQPDTSRLdtlkvEFIAPRDRLELKLANIWENLLNVHPIGIKDSFFELGGHSLLAVRLMAH 1021
Cdd:PRK05691 1604 IRLDQMPLGPSGKLDRRALPEPVWQQR-----EHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSR 1678
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|..
gi 2129675820 1022 INQEFGKNLALATLFQNPTIEKLAN---LLRQTSEISSWSPL 1060
Cdd:PRK05691 1679 TRQACDVELPLRALFEASELGAFAEqvaRIQAAGERNSQGAI 1720
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
11-1331 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 610.89 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 11 QKHLWLQQK--DNYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGmnIPFQSISDAPTYNHISLAEyd 88
Cdd:PRK10252 14 QPGIWMAEKlsPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNG--EVWQWVDPALTFPLPEIID-- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 89 wsrLSSQvqkakIDTLFQDTSLRVFDFEQATNL-------HFILGKLATDQHILFISLPALYADKTTLNYL---ICEIgr 158
Cdd:PRK10252 90 ---LRTQ-----PDPHAAAQALMQADLQQDLRVdsgkplvFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAItrrIAAI-- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 159 aYTACLDGEEISEEVM-QYADVSEWLNELLESEDTETARNYWQQQ--DISSVLNL---RIPFEIKNDHqssgeisFApqS 232
Cdd:PRK10252 160 -YCAWLRGEPTPASPFtPFADVVEEYQRYRASEAWQRDAAFWAEQrrQLPPPASLspaPLPGRSASAD-------IL--R 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 233 LCLAMNRDTVEKLEILQESYHTSTEAI-LLACWqvlLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDA 311
Cdd:PRK10252 230 LKLEFTDGAFRQLAAQASGVQRPDLALaLVALW---LGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQ 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 312 LKFSELMERVSESLRFVKKWQEYFNWENFISTNEKFAARPFF-------PFCF--DFTQ-QSQSYVNGniafseykkSAN 381
Cdd:PRK10252 307 ETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDEPLFgpvlnikVFDYqlDFPGvQAQTHTLA---------TGP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 382 IDKFQIKLSsGYSQDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLLiDFNNTKIEF 461
Cdd:PRK10252 378 VNDLELALF-PDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLA-QVNATAVEI 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 462 PhDKCLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGA 541
Cdd:PRK10252 456 P-ETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAA 534
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 542 YIPFDPTYPQERLGFMLEDAQIPILLTQQRLVDKFVehktqiicldrDLPENATLSIDNP--VSNVTSENL------AYI 613
Cdd:PRK10252 535 WLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFA-----------DVPDLTSLCYNAPlaPQGAAPLQLsqphhtAYI 603
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 614 IYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEK--EEIEALSA 691
Cdd:PRK10252 604 IFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEahRDPLAMQQ 683
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 692 LLQSDqnyslvKITPAHL--EMLNQML--PNHKGVTET----RALIIGGEALLGKSLNFW--RDNAPktrIINEYGPTET 761
Cdd:PRK10252 684 FFAEY------GVTTTHFvpSMLAAFVasLTPEGARQScaslRQVFCSGEALPADLCREWqqLTGAP---LHNLYGPTEA 754
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 762 VVGCCVY--EVDEQTSLSGA-ILIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSd 838
Cdd:PRK10252 755 AVDVSWYpaFGEELAAVRGSsVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA- 833
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 839 ePNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLV-----NAVTVIAREDQPGD-KRLVGYI 912
Cdd:PRK10252 834 -PGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVeqavtHACVINQAAATGGDaRQLVGYL 912
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 913 VPKEQAPTSSE-LRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALPQPDTSRldtlKVEFIAPRDRLELKLANIWE 991
Cdd:PRK10252 913 VSQSGLPLDTSaLQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKA----QVPGRAPKTGTETIIAAAFS 988
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 992 NLLNVHPIGIKDSFFELGGHSLLAVRLMAHINQEFGKNLALATLFQNPTIEKLANLLRQTSEISS---WSPLVEIQTGNS 1068
Cdd:PRK10252 989 SLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESRrlgFGTILPLREGDG 1068
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1069 QyPFFCLPGGGGNVLYLHELARDLGSEQTFYGLQAPGLNGESDPLTSVEEMAAYYIQAIQSVQPEGPYFLGGHSFGGIVA 1148
Cdd:PRK10252 1069 P-TLFCFHPASGFAWQFSVLSRYLDPQWSIYGIQSPRPDGPMQTATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLA 1147
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1149 YEIAQQLVKSGHEVALVAILDAPAPvasdkpiyidvddatrltETarliERWAGKSLNisyeILQPLELdAQLEYLKEQL 1228
Cdd:PRK10252 1148 QGIAARLRARGEEVAFLGLLDTWPP------------------ET----QNWREKEAN----GLDPEVL-AEIDREREAF 1200
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1229 IAV--GLLPTGTetkqVRGLVQVFETNLQAsIKYSPQEVYPHRLTLLRAREVNAEDAalltelrqDPAWGWGQFsTEKVD 1306
Cdd:PRK10252 1201 LAAqqGSLSTEL----FTTIEGNYADAVRL-LTTAHSVPFDGKATLFVAERTLQEGM--------SPEQAWSPW-IAELD 1266
|
1370 1380
....*....|....*....|....*
gi 2129675820 1307 IHIVPGDHMTMMTQPHISSVAKQLR 1331
Cdd:PRK10252 1267 VYRQDCAHVDIISPEAFEKIGPILR 1291
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
466-961 |
0e+00 |
|
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: 593.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 466 CLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPF 545
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 546 DPTYPQERLGFMLEDAQIPILLTQQrlvdkfvehktqiicldrdlpenatlsidnpvsnvtsENLAYIIYTSGSTGKPKG 625
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLTQP-------------------------------------ENLAYVIYTSGSTGKPKG 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 626 TMIPHRGLVNYlswctnAYALAQGYGAPVQ------SSIGFDATITSLFSPLLVGKRVVLLPEK--EEIEALSALLQsDQ 697
Cdd:cd17644 124 VMIEHQSLVNL------SHGLIKEYGITSSdrvlqfASIAFDVAAEEIYVTLLSGATLVLRPEEmrSSLEDFVQYIQ-QW 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 698 NYSLVKITPAHLEML-NQMLPNHKGVTET-RALIIGGEALLGKSLNFWRDN-APKTRIINEYGPTETVVGCCVYEV-DEQ 773
Cdd:cd17644 197 QLTVLSLPPAYWHLLvLELLLSTIDLPSSlRLVIVGGEAVQPELVRQWQKNvGNFIQLINVYGPTEATIAATVCRLtQLT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 774 TSLSGAILIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDEPNSRLYKTGDLARY 853
Cdd:cd17644 277 ERNITSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESERLYKTGDLARY 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 854 LPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPK-EQAPTSSELRQFLQSKL 932
Cdd:cd17644 357 LPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHyEESPSTVELRQFLKAKL 436
|
490 500
....*....|....*....|....*....
gi 2129675820 933 PEYMIPSAFVMLEVIPLTTHGKVDRQALP 961
Cdd:cd17644 437 PDYMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
469-960 |
0e+00 |
|
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: 579.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 469 ELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPT 548
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 549 YPQERLGFMLEDAQIPILLTQQRLVDKFVEHKTQIICLDRDLPENAtlsiDNPVSNVTSENLAYIIYTSGSTGKPKGTMI 628
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPA----GNPAVPVSPDDLAYVMYTSGSTGRPKGVAV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 629 PHRGLVnylswctnAYALAQGYGAP-------VQSSIGFDATITSLFSPLLVGKRVVLLPEKE--EIEALSALLQSDqny 699
Cdd:cd12117 157 THRGVV--------RLVKNTNYVTLgpddrvlQTSPLAFDASTFEIWGALLNGARLVLAPKGTllDPDALGALIAEE--- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 700 slvKITPAHLE--MLNQMLPNHKGVTET-RALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSL 776
Cdd:cd12117 226 ---GVTVLWLTaaLFNQLADEDPECFAGlRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 777 SGAILIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdEPNSRLYKTGDLARYLPD 856
Cdd:cd12117 303 AGSIPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF--GPGERLYRTGDLARWLPD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 857 GNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPkEQAPTSSELRQFLQSKLPEYM 936
Cdd:cd12117 381 GRLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVA-EGALDAAELRAFLRERLPAYM 459
|
490 500
....*....|....*....|....
gi 2129675820 937 IPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd12117 460 VPAAFVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
471-961 |
0e+00 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 556.57 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 471 FAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYP 550
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 551 QERLGFMLEDAQIPILLTQQRLVDKFVEHKTQIICLDRdlPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPH 630
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQ--PGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 631 RGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEKE--EIEALSALLQSDQNYSLVKITPAH 708
Cdd:cd17651 159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVrtDPPALAAWLDEQRISRVFLPTVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 709 LEMLNQMLPNHKGVTETRALIIGGEAL-LGKSLNFWRDNAPKTRIINEYGPTETVVGCCvYEVDEQTSLSGAIL-IGRPI 786
Cdd:cd17651 239 RALAEHGRPLGVRLAALRYLLTGGEQLvLTEDLREFCAGLPGLRLHNHYGPTETHVVTA-LSLPGDPAAWPAPPpIGRPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 787 ANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSdePNSRLYKTGDLARYLPDGNIEYLGRID 866
Cdd:cd17651 318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV--PGARMYRTGDLARWLPDGELEFLGRAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 867 HQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAP-TSSELRQFLQSKLPEYMIPSAFVMLE 945
Cdd:cd17651 396 DQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPvDAAELRAALATHLPEYMVPSAFVLLD 475
|
490
....*....|....*.
gi 2129675820 946 VIPLTTHGKVDRQALP 961
Cdd:cd17651 476 ALPLTPNGKLDRRALP 491
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-1228 |
5.39e-178 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 587.69 E-value: 5.39e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 7 ISPQQK----HLWLQQKDNyqAYCTQIAINITGnLNSDILKLALANLSDRYEIFHTAFHSLPGMNIPFQSIsdaptYNHI 82
Cdd:PRK12316 1559 LSPMQQgmlfHSLYEQEAG--DYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGLEQPLQVI-----HKQV 1630
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 83 SL--AEYDWsRLSSQVQKAkIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAY 160
Cdd:PRK12316 1631 ELpfAELDW-RGREDLGQA-LDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRY 1708
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 161 TacldGEEISEEVMQYADVSEWLnellESEDTETARNYWQQQDISSVLNLRIPFEIKNDHQSSGEISFApQSLCLAMNRd 240
Cdd:PRK12316 1709 A----GQPVAAPGGRYRDYIAWL----QRQDAAASEAFWKEQLAALEEPTRLAQAARTEDGQVGYGDHQ-QLLDPAQTR- 1778
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 241 tveKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYdELKGV---FGLLTKYLPIHSRLEDALKFSEL 317
Cdd:PRK12316 1779 ---ALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPA-ELPGIeqqIGLFINTLPVIAAPRPDQSVADW 1854
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 318 MERVSE---SLRF--------VKKW-----QEYFN----WENFistnekfaarpffpfcfDFTQQSQSYVNGNIAFSEYk 377
Cdd:PRK12316 1855 LQEVQAlnlALREhehtplydIQRWagqggEALFDsllvFENY-----------------PVAEALKQGAPAGLVFGRV- 1916
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 378 ksANIDKFQIKLSSGYSQ-DNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLLIDFNN 456
Cdd:PRK12316 1917 --SNHEQTNYPLTLAVTLgETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDR 1994
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 457 TKIEFPHDKCLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGIL 536
Cdd:PRK12316 1995 TPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVL 2074
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 537 KAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQRLVDKfVEHKTQIICLDRDLPEN-ATLSIDNPVSNVTSENLAYIIY 615
Cdd:PRK12316 2075 KAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLER-LPLPAGVARLPLDRDAEwADYPDTAPAVQLAGENLAYVIY 2153
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 616 TSGSTGKPKGTMIPHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEKEEIEALSALLQS 695
Cdd:PRK12316 2154 TSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEME 2233
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 696 DQNYSLVKITPAHLEMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTS 775
Cdd:PRK12316 2234 RHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDP 2313
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 776 LSGAIL-IGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDePNSRLYKTGDLARYL 854
Cdd:PRK12316 2314 CGAAYVpIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSA-SGERLYRTGDLARYR 2392
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 855 PDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAReDQPGDKRLVGYIVPKE-QAPTSSELRQFLQSKLP 933
Cdd:PRK12316 2393 ADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDaAEDLLAELRAWLAARLP 2471
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 934 EYMIPSAFVMLEVIPLTTHGKVDRQALPQPDTSRldtLKVEFIAPRDRLELKLANIWENLLNVHPIGIKDSFFELGGHSL 1013
Cdd:PRK12316 2472 AYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQ---LRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSL 2548
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1014 LAVRLMAHINQEFGKNLALATLFQNPTIEKLANLLRQTSE--------ISSWSPLVEIQTGNSQYPFFCLPGGGG----- 1080
Cdd:PRK12316 2549 LATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTsrapvlqkVTRVQPLPLSHAQQRQWFLWQLEPESAayhlp 2628
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1081 NVLYLHELARDLGSEQTFYGLQApglngESDPL-TSVEEMAAYYIQAIQSVQPEGPYFL--GGHSFGGI---VAYEIAQQ 1154
Cdd:PRK12316 2629 SALHLRGVLDQAALEQAFDALVL-----RHETLrTRFVEVGEQTRQVILPNMSLRIVLEdcAGVADAAIrqrVAEEIQRP 2703
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1155 L--------------VKSGHEVALVAILDApapVASDKPIYIDVDDATRLTETARLIERWAGKSLNISY--------EIL 1212
Cdd:PRK12316 2704 FdlargpllrvrllaLDGQEHVLVITQHHI---VSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYadyaawqrAWM 2780
|
1290
....*....|....*.
gi 2129675820 1213 QPLELDAQLEYLKEQL 1228
Cdd:PRK12316 2781 DSGEGARQLDYWRERL 2796
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
479-961 |
5.43e-178 |
|
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: 534.14 E-value: 5.43e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 479 PNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFML 558
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 559 EDAQIPILLTQqrlvdkfvehktqiicldrdlpenatlsidnpvsnvtSENLAYIIYTSGSTGKPKGTMIPHRGLVNYls 638
Cdd:cd17652 81 ADARPALLLTT-------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANL-- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 639 wctnAYALAQGYGAPVQS------SIGFDATITSLFSPLLVGKRVVLLPEKEEI--EALSALLQsDQNYSLVKITPAHLE 710
Cdd:cd17652 122 ----AAAQIAAFDVGPGSrvlqfaSPSFDASVWELLMALLAGATLVLAPAEELLpgEPLADLLR-EHRITHVTLPPAALA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 711 MLNQmlpnhKGVTETRALIIGGEALLGKSLNFWrdnAPKTRIINEYGPTETVVGCCVYEVDEQtslSGAILIGRPIANTQ 790
Cdd:cd17652 197 ALPP-----DDLPDLRTLVVAGEACPAELVDRW---APGRRMINAYGPTETTVCATMAGPLPG---GGVPPIGRPVPGTR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 791 LYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDePNSRLYKTGDLARYLPDGNIEYLGRIDHQVK 870
Cdd:cd17652 266 VYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGA-PGSRMYRTGDLARWRADGQLEFLGRADDQVK 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 871 IRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPK-EQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPL 949
Cdd:cd17652 345 IRGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPApGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPL 424
|
490
....*....|..
gi 2129675820 950 TTHGKVDRQALP 961
Cdd:cd17652 425 TPNGKLDRRALP 436
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
5-1076 |
6.34e-176 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 581.36 E-value: 6.34e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 5 IRISPQQKHLWL--QQKDNYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGmnIPFQSISDAptyNHI 82
Cdd:PRK05691 1729 VPLSYSQQRMWFlwQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFPSVDG--VPVQQVAED---SGL 1803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 83 SLAEYDWSRLSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTA 162
Cdd:PRK05691 1804 RMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEA 1883
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 163 CLDGEEISEEVM--QYADVSEWLNELLESEDTETARNYWQQQ--DISSVLNL-----RIPFEiknDHQssGEIsfapqsL 233
Cdd:PRK05691 1884 FLDDRESPLEPLpvQYLDYSVWQRQWLESGERQRQLDYWKAQlgNEHPLLELpadrpRPPVQ---SHR--GEL------Y 1952
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 234 CLAMNRDTVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDALK 313
Cdd:PRK05691 1953 RFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMS 2032
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 314 FSELMERVSESLRFVKKWQEyFNWENFISTNE---KFAARPFFP-FC----FDFtQQSQSYVNGNIafsEY-KKSANIDK 384
Cdd:PRK05691 2033 VSELLEQVRQTVIEGQSHQD-LPFDHLVEALQpprSAAYNPLFQvMCnvqrWEF-QQSRQLAGMTV---EYlVNDARATK 2107
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 385 FQIKLSSGYSQDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLLIDFNNTKIEFPHD 464
Cdd:PRK05691 2108 FDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLD 2187
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 465 KCLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIP 544
Cdd:PRK05691 2188 QTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVP 2267
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 545 FDPTYPQERLGFMLEDAQIPILLTQQRLVDKFVEHKTQII--CLDRDLPENATLSIDNPVSNVTSENLAYIIYTSGSTGK 622
Cdd:PRK05691 2268 LDPEYPLERLHYMIEDSGIGLLLSDRALFEALGELPAGVArwCLEDDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGK 2347
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 623 PKGTMIPHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPE----KEEIEALSAllqsDQN 698
Cdd:PRK05691 2348 PKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQgqwgAEEICQLIR----EQQ 2423
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 699 YSLVKITPAHLEMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVV---GCCVYEVDEQTS 775
Cdd:PRK05691 2424 VSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTETVVmplACLAPEQLEEGA 2503
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 776 lsGAILIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDEpNSRLYKTGDLARYLP 855
Cdd:PRK05691 2504 --ASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAAD-GGRLYRTGDLVRLRA 2580
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 856 DGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAReDQPGDKRLVGYIVPK-------EQAPTSSELRQFL 928
Cdd:PRK05691 2581 DGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAvagqddeAQAALREALKAHL 2659
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 929 QSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALPQPDtsrLDTLKVEFIAPRDRLELKLANIWENLLNVHPIGIKDSFFEL 1008
Cdd:PRK05691 2660 KQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPD---PELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFEL 2736
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1009 GGHSLLAVRLMAHINQeFGKNLALATLFQNPTIEKLANLLRQTSEISSWSPLVEIQTGNS--QYPFFCLP 1076
Cdd:PRK05691 2737 GGDSILSIQVVSRARQ-LGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGPLQGASGLTpiQHWFFDSP 2805
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
467-960 |
5.11e-175 |
|
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: 526.89 E-value: 5.11e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD 546
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 547 PTYPQERLGFMLEDAQIPILLTQqrlvdkfvehktqiicldrdlpenatlsidnpvsnvtSENLAYIIYTSGSTGKPKGT 626
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLTD-------------------------------------PDDLAYVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 627 MIPHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEKEEIEALSALLQSdqnySLVKITP 706
Cdd:cd12115 124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPAAAEV----TLINTVP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 707 AHLEMLNQM--LPnhkgvTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSlsGAILIGR 784
Cdd:cd12115 200 SAAAELLRHdaLP-----ASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPPGAS--GEVSIGR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 785 PIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdEPNSRLYKTGDLARYLPDGNIEYLGR 864
Cdd:cd12115 273 PLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF--GPGARLYRTGDLVRWRPDGLLEFLGR 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 865 IDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPK-EQAPTSSELRQFLQSKLPEYMIPSAFVM 943
Cdd:cd12115 351 ADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEpGAAGLVEDLRRHLGTRLPAYMVPSRFVR 430
|
490
....*....|....*..
gi 2129675820 944 LEVIPLTTHGKVDRQAL 960
Cdd:cd12115 431 LDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
468-960 |
1.27e-174 |
|
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: 527.23 E-value: 1.27e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 468 HELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDP 547
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 548 TYPQERLGFMLEDAQIPILLTQQRLVDKFVEHKTQIICLDRDLPENATlsiDNPVSNVTSENLAYIIYTSGSTGKPKGTM 627
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPA---TPPLVPPRPDNLAYVIYTSGSTGRPKGVM 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 628 IPHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLL-PEKE-EIEALSALLQSDQnyslvkIT 705
Cdd:cd17646 158 VTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVArPGGHrDPAYLAALIREHG------VT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 706 PAHL--EMLNQML--PNHKGVTETRALIIGGEALLGKSLNFWRDnAPKTRIINEYGPTETVVGCCVYEVDEQTSlSGAIL 781
Cdd:cd17646 232 TCHFvpSMLRVFLaePAAGSCASLRRVFCSGEALPPELAARFLA-LPGAELHNLYGPTEAAIDVTHWPVRGPAE-TPSVP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 782 IGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdEPNSRLYKTGDLARYLPDGNIEY 861
Cdd:cd17646 310 IGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF--GPGSRMYRTGDLARWRPDGALEF 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 862 LGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPK--EQAPTSSELRQFLQSKLPEYMIPS 939
Cdd:cd17646 388 LGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAagAAGPDTAALRAHLAERLPEYMVPA 467
|
490 500
....*....|....*....|.
gi 2129675820 940 AFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd17646 468 AFVVLDALPLTANGKLDRAAL 488
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
492-896 |
1.13e-171 |
|
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: 516.43 E-value: 1.13e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 492 TYAQLNAKSNQLAHHLQKL-GVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQ 570
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 571 RLVDKFVEHKTQIICLDRDLPENATLSIDNPVSNVTS--ENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYALAQ 648
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSgpDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 649 GYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEKEE--IEALSALLQSDQNYSLVKITPAHLEML-NQMLPNHKGVtet 725
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEErdDAALLAALIAEHPVTVLNLTPSLLALLaAALPPALASL--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 726 RALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQ-TSLSGAILIGRPIANTQLYLLDDKQKLVPIG 804
Cdd:TIGR01733 238 RLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDdAPRESPVPIGRPLANTRLYVLDDDLRPVPVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 805 VPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDEPNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESL 884
Cdd:TIGR01733 318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
410
....*....|..
gi 2129675820 885 LAQHPLVNAVTV 896
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
479-960 |
4.38e-165 |
|
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: 501.07 E-value: 4.38e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 479 PNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFML 558
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 559 EDAQIPILLTQqrlvdkfvehktqiicldrdlpenatlsidnpvsnvtSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLS 638
Cdd:cd17643 81 ADSGPSLLLTD-------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 639 WCTNAYalaqGYGA-PVQS---SIGFDATITSLFSPLLVGKRVVLLPEkeEI----EALSALLQsDQNYSLVKITP-AHL 709
Cdd:cd17643 124 ATQRWF----GFNEdDVWTlfhSYAFDFSVWEIWGALLHGGRLVVVPY--EVarspEDFARLLR-DEGVTVLNQTPsAFY 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 710 EMLNQMLPNHKGVTETRALIIGGEALLGKSLNFW--RDNAPKTRIINEYGPTETVVGCCVYEVDEQ-TSLSGAILIGRPI 786
Cdd:cd17643 197 QLVEAADRDGRDPLALRYVIFGGEALEAAMLRPWagRFGLDRPQLVNMYGITETTVHVTFRPLDAAdLPAAAASPIGRPL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 787 ANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsDEPNSRLYKTGDLARYLPDGNIEYLGRID 866
Cdd:cd17643 277 PGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF-GGPGSRMYRTGDLARRLPDGELEYLGRAD 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 867 HQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKE-QAPTSSELRQFLQSKLPEYMIPSAFVMLE 945
Cdd:cd17643 356 EQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDgAAADIAELRALLKELLPDYMVPARYVPLD 435
|
490
....*....|....*
gi 2129675820 946 VIPLTTHGKVDRQAL 960
Cdd:cd17643 436 ALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
479-960 |
7.03e-165 |
|
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: 501.05 E-value: 7.03e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 479 PNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFML 558
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 559 EDAQIPILLTQQRLVDKFvehktqIICLDR--DLPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVNY 636
Cdd:cd12116 81 EDAEPALVLTDDALPDRL------PAGLPVllLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 637 LSwctnayALAQ--GYGAPVQ----SSIGFDATITSLFSPLLVGKRVVLLPEK--EEIEALSALLqSDQNYSLVKITPAh 708
Cdd:cd12116 155 LH------SMRErlGLGPGDRllavTTYAFDISLLELLLPLLAGARVVIAPREtqRDPEALARLI-EAHSITVMQATPA- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 709 lemLNQML-----PNHKGVTetraLIIGGEAL---LGKSLNfwrdnAPKTRIINEYGPTETVVGCCVYEVDEQtslSGAI 780
Cdd:cd12116 227 ---TWRMLldagwQGRAGLT----ALCGGEALppdLAARLL-----SRVGSLWNLYGPTETTIWSTAARVTAA---AGPI 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 781 LIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDePNSRLYKTGDLARYLPDGNIE 860
Cdd:cd12116 292 PIGRPLANTQVYVLDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAG-PGSRLYRTGDLVRRRADGRLE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 861 YLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDqPGDKRLVGYIVPKE-QAPTSSELRQFLQSKLPEYMIPS 939
Cdd:cd12116 371 YLGRADGQVKIRGHRIELGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAgAAPDAAALRAHLRATLPAYMVPS 449
|
490 500
....*....|....*....|.
gi 2129675820 940 AFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd12116 450 AFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
479-961 |
3.53e-163 |
|
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: 496.12 E-value: 3.53e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 479 PNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFML 558
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 559 EDAQIPILLTQqrlvdkfvehktqiicldrdlpenatlsidnpvsnvTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLS 638
Cdd:cd17649 81 EDSGAGLLLTH------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 639 WCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEK--EEIEALSALLQSdQNYSLVKITPAHLEMLNQML 716
Cdd:cd17649 125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDElwASADELAEMVRE-LGVTVLDLPPAYLQQLAEEA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 717 PNH--KGVTETRALIIGGEALLGKSLNFWRDNApkTRIINEYGPTETVVGCCVYEVDEQTSLSGAIL-IGRPIANTQLYL 793
Cdd:cd17649 204 DRTgdGRPPSLRLYIFGGEALSPELLRRWLKAP--VRLFNAYGPTEATVTPLVWKCEAGAARAGASMpIGRPLGGRSAYI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 794 LDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSdEPNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRG 873
Cdd:cd17649 282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFG-APGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 874 FRIELEEIESLLAQHPLVNAVTVIAReDQPGDKRLVGYIVPK---EQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLT 950
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRaaaAQPELRAQLRTALRASLPDYMVPAHLVFLARLPLT 439
|
490
....*....|.
gi 2129675820 951 THGKVDRQALP 961
Cdd:cd17649 440 PNGKLDRKALP 450
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
479-960 |
2.42e-152 |
|
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: 467.33 E-value: 2.42e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 479 PNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFML 558
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 559 EDAQIPILLTQqrlvdkfvehktqiicldrdlpenatlsidnpvsnvtSENLAYIIYTSGSTGKPKGTMIPHRGLVN-YL 637
Cdd:cd17650 81 EDSGAKLLLTQ-------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHaAH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 638 SWcTNAYALAQGYGAPVQ-SSIGFDATITSLFSPLLVGKRVVLLPE--KEEIEALSALLQSdQNYSLVKITPAHLEMLNQ 714
Cdd:cd17650 124 AW-RREYELDSFPVRLLQmASFSFDVFAGDFARSLLNGGTLVICPDevKLDPAALYDLILK-SRITLMESTPALIRPVMA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 715 MLpNHKGVT--ETRALIIGGEALLGKSL-NFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSLSGAIL-IGRPIANTQ 790
Cdd:cd17650 202 YV-YRNGLDlsAMRLLIVGSDGCKAQDFkTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVpIGRPLPNTA 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 791 LYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdEPNSRLYKTGDLARYLPDGNIEYLGRIDHQVK 870
Cdd:cd17650 281 MYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF--APGERMYRTGDLARWRADGNVELLGRVDHQVK 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 871 IRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQaPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLT 950
Cdd:cd17650 359 IRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAAT-LNTAELRAFLAKELPSYMIPSYYVQLDALPLT 437
|
490
....*....|
gi 2129675820 951 THGKVDRQAL 960
Cdd:cd17650 438 PNGKVDRRAL 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
468-961 |
9.10e-148 |
|
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: 455.09 E-value: 9.10e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 468 HELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDP 547
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 548 TYPQERLGFMLEDAQIPILLTQqrlvdkfvehktqiicldrdlpenatlsidnpvsnvtSENLAYIIYTSGSTGKPKGTM 627
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTN-------------------------------------PDDLAYVIYTSGSTGLPKGVM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 628 IPHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPE--KEEIEALSALLQsdQNYSLVKIT 705
Cdd:cd17645 124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSerRLDLDALNDYFN--QEGITISFL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 706 PAHLEMLNQMLPNHkgvtETRALIIGGEALlgkslNFWRDNAPKtrIINEYGPTETVVGCCVYEVDEQtslSGAILIGRP 785
Cdd:cd17645 202 PTGAAEQFMQLDNQ----SLRVLLTGGDKL-----KKIERKGYK--LVNNYGPTENTVVATSFEIDKP---YANIPIGKP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 786 IANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSdePNSRLYKTGDLARYLPDGNIEYLGRI 865
Cdd:cd17645 268 IDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFV--PGERMYRTGDLAKFLPDGNIEFLGRL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 866 DHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTsSELRQFLQSKLPEYMIPSAFVMLE 945
Cdd:cd17645 346 DQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPH-EELREWLKNDLPDYMIPTYFVHLK 424
|
490
....*....|....*.
gi 2129675820 946 VIPLTTHGKVDRQALP 961
Cdd:cd17645 425 ALPLTANGKVDRKALP 440
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
478-961 |
3.42e-147 |
|
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: 455.01 E-value: 3.42e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 478 TPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFM 557
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 558 LEDAQIPILLTQQRLVDKFVEHKTQIICLDRDLPENATLSIDnpvSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYL 637
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNID---YINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 638 SWcTNAYALAQGYGAPVQ-SSIGFDATITSLFSPLLVGKRVVLLPE--KEEIEALSALLQSDQNYSLVKITpahleMLNQ 714
Cdd:cd17656 158 HF-EREKTNINFSDKVLQfATCSFDVCYQEIFSTLLSGGTLYIIREetKRDVEQLFDLVKRHNIEVVFLPV-----AFLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 715 MLPNHKGVTET-----RALIIGGEALLGKslNFWRDNAPKTRII--NEYGPTETVVgCCVYEVDEQTSLSGAILIGRPIA 787
Cdd:cd17656 232 FIFSEREFINRfptcvKHIITAGEQLVIT--NEFKEMLHEHNVHlhNHYGPSETHV-VTTYTINPEAEIPELPPIGKPIS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 788 NTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdEPNSRLYKTGDLARYLPDGNIEYLGRIDH 867
Cdd:cd17656 309 NTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF--DPNERMYRTGDLARYLPDGNIEFLGRADH 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 868 QVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPkEQAPTSSELRQFLQSKLPEYMIPSAFVMLEVI 947
Cdd:cd17656 387 QVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVM-EQELNISQLREYLAKQLPEYMIPSFFVPLDQL 465
|
490
....*....|....
gi 2129675820 948 PLTTHGKVDRQALP 961
Cdd:cd17656 466 PLTPNGKVDRKALP 479
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
467-960 |
9.36e-145 |
|
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: 448.53 E-value: 9.36e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD 546
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 547 PTYPQERLGFMLEDAQIPILLTqqrlvdkfvehktqiicldrdlpenatlsidnpvsnVTSENLAYIIYTSGSTGKPKGT 626
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLT------------------------------------SSPSDAAYVIFTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 627 MIPHRglvnylSWCTNAYALAQGYGAPVQS------SIGFDATITSLFSPLLVGKRVVLLPEKEEIEALSALLQSDQ-NY 699
Cdd:cd05918 125 VIEHR------ALSTSALAHGRALGLTSESrvlqfaSYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAGFINRLRvTW 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 700 slVKITPAHLEMLNqmlpnHKGVTETRALIIGGEALLGKSLNFWrdnAPKTRIINEYGPTETVVGCCVYEVdeqTSLSGA 779
Cdd:cd05918 199 --AFLTPSVARLLD-----PEDVPSLRTLVLGGEALTQSDVDTW---ADRVRLINAYGPAECTIAATVSPV---VPSTDP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 780 ILIGRPIANTqLYLLD--DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNP-----FSDEPNSRLYKTGDLAR 852
Cdd:cd05918 266 RNIGRPLGAT-CWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqEGSGRGRRLYRTGDLVR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 853 YLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVN---AVTVIAREDQPGDKRLVGYIVPKEQAPTS-------- 921
Cdd:cd05918 345 YNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAkevVVEVVKPKDGSSSPQLVAFVVLDGSSSGSgdgdslfl 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2129675820 922 ----------SELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05918 425 epsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
468-1336 |
1.94e-139 |
|
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: 447.61 E-value: 1.94e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 468 HELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDP 547
Cdd:COG3319 4 AAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 548 TYPQERLGFMLEDAQIPILLTQQR--LVDKFVEHKTQIICLDRDLPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKG 625
Cdd:COG3319 84 LALALAAAAAALLLAALALLLALLaaLALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 626 TMIPHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEKEEIEALSALLQSDQNYSLVKIT 705
Cdd:COG3319 164 LVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 706 PAHLEMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSLSGAILIGRP 785
Cdd:COG3319 244 LAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 786 IANTQLYLLDDKQklVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDEPNSRLYKTGDLARYLPDGNIEYLGRI 865
Cdd:COG3319 324 LLVLLVLLVLLLP--LLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRL 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 866 DHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSELRQFLQSKLPEYMIPSAFVMLE 945
Cdd:COG3319 402 RLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 946 VIPLTTHGKVDRQALPQPDtsrlDTLKVEFIAPRDRLELKLANIWENLLNVHPIGIKDSFFELGGHSLLAVRLMAHINQE 1025
Cdd:COG3319 482 LLLLLLLAALLLAAAAPAA----AAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLAL 557
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1026 FGKNLALATLFQNPTIEKLANLLRQTSEISSWSPLVEIQTGNSQYPFFCLPGGGGNVLYLHELARDLGSEQTFYGLQAPG 1105
Cdd:COG3319 558 LLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGGSGPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPG 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1106 LNGESDPLTSVEEMAAYYIQAIQSVQPEGPYFLGGHSFGGIVAYEIAQQLVKSGHEVALVAILDAPAPVASDKPiyidvD 1185
Cdd:COG3319 638 LDGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLGWSFGGLVAYEMARQLEAQGEEVALLVLLDSYAPGALARL-----D 712
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1186 DATRLTETARLIERwaGKSLNISYEILQPLELDAQLEYLKEQLIAVGlLPTGTETKQVRGLVQVFETNLQASIKYSPQeV 1265
Cdd:COG3319 713 EAELLAALLRDLAR--GVDLPLDAEELRALDPEERLARLLERLREAG-LPAGLDAERLRRLLRVFRANLRALRRYRPR-P 788
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2129675820 1266 YPHRLTLLRAREVnaedaalLTELRQDPAWGWGQFSTEKVDIHIVPGDHMTMMTQPHISSVAKQLRICIEQ 1336
Cdd:COG3319 789 YDGPVLLFRAEED-------PPGRADDPALGWRPLVAGGLEVHDVPGDHFSMLREPHVAELAAALRAALAA 852
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
88-1055 |
6.33e-137 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 466.18 E-value: 6.33e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 88 DWSRLSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACLDGE 167
Cdd:PRK05691 3339 DWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGR 3418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 168 EISEEVM-QYADVSEWLnellESEDTETARNYWQQqdissvlNLRiPFE----IKND----HQSSGEISFAPQSLCLA-M 237
Cdd:PRK05691 3419 EAQLPVPpRYRDYIGWL----QRQDLAQARQWWQD-------NLR-GFErptpIPSDrpflREHAGDSGGMVVGDCYTrL 3486
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 238 NRDTVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGR--EYDELKGVFGLLTKYLPIHSRLEDALK-- 313
Cdd:PRK05691 3487 DAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFINSIALRVQLPAAGQrc 3566
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 314 -----FSELMERVSEsLRfvkkWQEYFNWENFISTNEKFAARPFFPFCFDFTqqsqsyvNGNIafseykKSANIDKFQ-I 387
Cdd:PRK05691 3567 svrqwLQGLLDSNME-LR----EYEYLPLVAIQECSELPKGQPLFDSLFVFE-------NAPV------EVSVLDRAQsL 3628
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 388 KLSSG--------------YSQDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLLID 453
Cdd:PRK05691 3629 NASSDsgrthtnfpltavcYPGDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDG 3708
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 454 FNNTKIEFPHDKCLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGIL 533
Cdd:PRK05691 3709 CNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIV 3788
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 534 GILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQR-------LVDKFVEHKTQIICLDRDLPENATLSiDNPVSNVT 606
Cdd:PRK05691 3789 GSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAAcreqaraLLDELGCANRPRLLVWEEVQAGEVAS-HNPGIYSG 3867
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 607 SENLAYIIYTSGSTGKPKGTMIPHRGLVN-------YLSwCTNAYALAQgygapvQSSIGFDATITSLFSPLLVGKRVVL 679
Cdd:PRK05691 3868 PDNLAYVIYTSGSTGLPKGVMVEQRGMLNnqlskvpYLA-LSEADVIAQ------TASQSFDISVWQFLAAPLFGARVEI 3940
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 680 LPEK--EEIEALSALLQSdQNYSLVKITPAhleMLNQMLPN-HKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEY 756
Cdd:PRK05691 3941 VPNAiaHDPQGLLAHVQA-QGITVLESVPS---LIQGMLAEdRQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAY 4016
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 757 GPTETVVGCCVYEVDEQTSLSGAILIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPF 836
Cdd:PRK05691 4017 GPAECSDDVAFFRVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPF 4096
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 837 SdEPNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGdKRLVGYIVPKE 916
Cdd:PRK05691 4097 G-APGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNG-KHLVGYLVPHQ 4174
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 917 QAPTSSEL----RQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALPQPDTSRLDTLkvEFIAPRDRLELKLANIWEN 992
Cdd:PRK05691 4175 TVLAQGALleriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQ--AYLAPRNELEQTLATIWAD 4252
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2129675820 993 LLNVHPIGIKDSFFELGGHSLLAVRLMAHINQEFGKNLALATLFQNPTIEKLANLLR--QTSEIS 1055
Cdd:PRK05691 4253 VLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEglAGSAID 4317
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
479-961 |
2.91e-129 |
|
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: 406.40 E-value: 2.91e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 479 PNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLG-VKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFM 557
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 558 LEDAQIPILLTqqrlvdkfvehktqiicldrdlpenatlsidnpvsnvTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYL 637
Cdd:cd17648 81 LEDTGARVVIT-------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 638 SWCTNAYALA-QGYGA-PVQSSIGFDATITSLFSPLLVGKRVVLLPE--KEEIEALSALLQsDQNYSLVKITPAHLEMLN 713
Cdd:cd17648 124 TSLSERYFGRdNGDEAvLFFSNYVFDFFVEQMTLALLNGQKLVVPPDemRFDPDRFYAYIN-REKVTYLSGTPSVLQQYD 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 714 QMLPNHkgvteTRALIIGGEALLGKSLNFWRDNAPkTRIINEYGPTETVVGCCV--YEVDEQTSLSgailIGRPIANTQL 791
Cdd:cd17648 203 LARLPH-----LKRVDAAGEEFTAPVFEKLRSRFA-GLIINAYGPTETTVTNHKrfFPGDQRFDKS----LGRPVRNTKC 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 792 YLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDEP------NSRLYKTGDLARYLPDGNIEYLGRI 865
Cdd:cd17648 273 YVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrNARLYKTGDLVRWLPSGELEYLGRN 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 866 DHQVKIRGFRIELEEIESLLAQHPLVNAVTVIARED-----QPGDKRLVGYIVPKEQAPTSSELRQFLQSKLPEYMIPSA 940
Cdd:cd17648 353 DFQVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqSRIQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMVPAR 432
|
490 500
....*....|....*....|.
gi 2129675820 941 FVMLEVIPLTTHGKVDRQALP 961
Cdd:cd17648 433 LVRLEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
479-960 |
6.96e-128 |
|
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: 403.58 E-value: 6.96e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 479 PNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFML 558
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 559 EDAQIPILLTQQRLVDKFVEHktqiICLDRDLPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLS 638
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAV----FDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTIL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 639 WCTNAYALaqgyGAPVQ----SSIGFDATITSLFSPLLVGKRVVLLPEKEEIEALS-ALLQSDQNYSLVKITPAHLEMLN 713
Cdd:cd12114 157 DINRRFAV----GPDDRvlalSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHwAELIERHGVTLWNSVPALLEMLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 714 QMLPNHKGVTET-RALIIGGE----ALLGKslnfWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSLSGAILIGRPIAN 788
Cdd:cd12114 233 DVLEAAQALLPSlRLVLLSGDwiplDLPAR----LRALAPDARLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLAN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 789 TQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFipnpFSDEPNSRLYKTGDLARYLPDGNIEYLGRIDHQ 868
Cdd:cd12114 309 QRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARF----VTHPDGERLYRTGDLGRYRPDGTLEFLGRRDGQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 869 VKIRGFRIELEEIESLLAQHPLVNAVTVIAReDQPGDKRLVGYIVPKEQAPT--SSELRQFLQSKLPEYMIPSAFVMLEV 946
Cdd:cd12114 385 VKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPiaPDALRAFLAQTLPAYMIPSRVIALEA 463
|
490
....*....|....
gi 2129675820 947 IPLTTHGKVDRQAL 960
Cdd:cd12114 464 LPLTANGKVDRAAL 477
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
469-960 |
2.55e-123 |
|
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: 389.75 E-value: 2.55e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 469 ELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPT 548
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 549 YPQERLGFMLEDAQipilltqqrlvdkfvehKTQIICLDRDlpenatlsidnpvsnvtsENLAYIIYTSGSTGKPKGTMI 628
Cdd:cd17653 81 LPSARIQAILRTSG-----------------ATLLLTTDSP------------------DDLAYIIFTSGSTGIPKGVMV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 629 PHRGLVNYLSWcTNAyALAQGYGAPVQS--SIGFDATITSLFSPLLVGKRVVLlpeKEEIEALSALLQSdqnYSLVKITP 706
Cdd:cd17653 126 PHRGVLNYVSQ-PPA-RLDVGPGSRVAQvlSIAFDACIGEIFSTLCNGGTLVL---ADPSDPFAHVART---VDALMSTP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 707 AHLEMLN-QMLPNHKGVtetralIIGGEALLGKSLNFWRDNApktRIINEYGPTETVVGCCVYEV--DEQTSlsgailIG 783
Cdd:cd17653 198 SILSTLSpQDFPNLKTI------FLGGEAVPPSLLDRWSPGR---RLYNAYGPTECTISSTMTELlpGQPVT------IG 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 784 RPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdEPNSRLYKTGDLARYLPDGNIEYLG 863
Cdd:cd17653 263 KPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF--WPGSRMYRTGDYGRWTEDGGLEFLG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 864 RIDHQVKIRGFRIELEEIES-LLAQHPLVNAVTVIAREDqpgdkRLVGYIVPkEQAPTSSeLRQFLQSKLPEYMIPSAFV 942
Cdd:cd17653 341 REDNQVKVRGFRINLEEIEEvVLQSQPEVTQAAAIVVNG-----RLVAFVTP-ETVDVDG-LRSELAKHLPSYAVPDRII 413
|
490
....*....|....*...
gi 2129675820 943 MLEVIPLTTHGKVDRQAL 960
Cdd:cd17653 414 ALDSFPLTANGKVDRKAL 431
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
475-960 |
5.25e-113 |
|
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: 362.33 E-value: 5.25e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 475 VERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERL 554
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 555 GFMLEDAQIPILLtqqrlvdkfvehktqiicldrdlpenatlsidnpvsnVTSENLAYIIYTSGSTGKPKGTMIPHRGLV 634
Cdd:cd05945 81 REILDAAKPALLI-------------------------------------ADGDDNAYIIFTSGSTGRPKGVQISHDNLV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 635 NYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPeKEEIEALSALLQ--SDQNYSLVKITPAHLEML 712
Cdd:cd05945 124 SFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVP-RDATADPKQLFRflAEHGITVWVSTPSFAAMC 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 713 -------NQMLPNHKGVtetralIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVD-EQTSLSGAILIGR 784
Cdd:cd05945 203 llsptftPESLPSLRHF------LFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTpEVLDGYDRLPIGY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 785 PIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPfsdepNSRLYKTGDLARYLPDGNIEYLGR 864
Cdd:cd05945 277 AKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-----GQRAYRTGDLVRLEADGLLFYRGR 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 865 IDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKE--QAPTSSELRQFLQSKLPEYMIPSAFV 942
Cdd:cd05945 352 LDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPgaEAGLTKAIKAELAERLPPYMIPRRFV 431
|
490
....*....|....*...
gi 2129675820 943 MLEVIPLTTHGKVDRQAL 960
Cdd:cd05945 432 YLDELPLNANGKIDRKAL 449
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
258-1056 |
1.41e-111 |
|
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: 383.26 E-value: 1.41e-111
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 258 AILLACWQVLLWRLSGQSEIVIG--AAGDGREydelkgvfglltkyLPIHSRLEDALKFSELMERVSESLRFVKKwQEYF 335
Cdd:TIGR03443 50 IILLAAFAALVYRLTGDEDIVLGtsSNKSGRP--------------FVLRLNITPELSFLQLYAKVSEEEKEGAS-DIGV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 336 NWE---NFISTNEKFAARP-FFPFCFDFTQQSQSyvngniafSEYKKSANIDkfqIKLSSGYSQDNLVVNFDYDANLFSE 411
Cdd:TIGR03443 115 PFDelsEHIQAAKKLERTPpLFRLAFQDAPDNQQ--------TTYSTGSTTD---LTVFLTPSSPELELSIYYNSLLFSS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 412 DSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLL-----IDFNNTKiefphdKCLHELFAAQVER--------- 477
Cdd:TIGR03443 184 DRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKSLLPdptkdLDWSGFR------GAIHDIFADNAEKhpdrtcvve 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 478 TPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFM 557
Cdd:TIGR03443 258 TPSFLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 558 LEDAQIPILL------TQQRLVDKFVEHKTQIICL--DRDLPENATL---SIDNPVSNVTSENLAY-------------- 612
Cdd:TIGR03443 338 LSVAKPRALIviekagTLDQLVRDYIDKELELRTEipALALQDDGSLvggSLEGGETDVLAPYQALkdtptgvvvgpdsn 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 613 --IIYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVvLLPEKEEIEALS 690
Cdd:TIGR03443 418 ptLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQL-LVPTADDIGTPG 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 691 ALLQSDQNY--SLVKITPAhlemLNQMLPnhKGVTET-----RALIIGGeaLLGKslnfwRDN------APKTRIINEYG 757
Cdd:TIGR03443 497 RLAEWMAKYgaTVTHLTPA----MGQLLS--AQATTPipslhHAFFVGD--ILTK-----RDClrlqtlAENVCIVNMYG 563
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 758 PTETVVGCCVYEV----DEQT---SLSGAILIGRPIANTQLYLLD--DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQ 828
Cdd:TIGR03443 564 TTETQRAVSYFEIpsrsSDSTflkNLKDVMPAGKGMKNVQLLVVNrnDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNA 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 829 QRFIPNPFSDE--------------------PNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQH 888
Cdd:TIGR03443 644 EKFVNNWFVDPshwidldkennkperefwlgPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQH 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 889 PLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSEL---------------------------RQFLQSKLPEYMIPSAF 941
Cdd:TIGR03443 724 PLVRENVTLVRRDKDEEPTLVSYIVPQDKSDELEEFksevddeessdpvvkglikyrklikdiREYLKKKLPSYAIPTVI 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 942 VMLEVIPLTTHGKVDRQALPQPDTSRLdtlkvEFIAPRDR----------LELKLANIWENLLNVHP--IGIKDSFFELG 1009
Cdd:TIGR03443 804 VPLKKLPLNPNGKVDKPALPFPDTAQL-----AAVAKNRSasaadeefteTEREIRDLWLELLPNRPatISPDDSFFDLG 878
|
890 900 910 920 930
....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1010 GHSLLAVRLMAHINQEFGKNLALATLFQNPTIEKLAN---LLRQTSEISS 1056
Cdd:TIGR03443 879 GHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKevdRLKKGEELAD 928
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
471-872 |
1.41e-101 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 330.04 E-value: 1.41e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 471 FAAQVERTPNNIAVE-FNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTY 549
Cdd:pfam00501 1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 550 PQERLGFMLEDAQIPILLTQQRLV-------DKFVEHKTQIICLDRDLPENATLSIDN---------PVSNVTSENLAYI 613
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKleelleaLGKLEVVKLVLVLDRDPVLKEEPLPEEakpadvpppPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 614 IYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYALAQGYGA----PVQSSIGFDA-TITSLFSPLLVGKRVVLLPEKEE--I 686
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGPddrvLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFPAldP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 687 EALSALLQSdqnyslVKIT-----PAHLEMLNQMLPNHKGVTET-RALIIGGEALLGKSLNFWRDnAPKTRIINEYGPTE 760
Cdd:pfam00501 241 AALLELIER------YKVTvlygvPTLLNMLLEAGAPKRALLSSlRLVLSGGAPLPPELARRFRE-LFGGALVNGYGLTE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 761 T-VVGCCVYEVDEQTSLSGAilIGRPIANTQLYLLDDK-QKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNpfsd 838
Cdd:pfam00501 314 TtGVVTTPLPLDEDLRSLGS--VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED---- 387
|
410 420 430
....*....|....*....|....*....|....
gi 2129675820 839 epnsRLYKTGDLARYLPDGNIEYLGRIDHQVKIR 872
Cdd:pfam00501 388 ----GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
467-962 |
4.58e-101 |
|
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: 329.85 E-value: 4.58e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD 546
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 547 PTYPQERLGFMLEDAQIPILLTqqrlvdkfvehktqiicldrdlpenatlsidnpvsnvtsenlAYIIYTSGSTGKPKGT 626
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGV 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 627 MIPHRglvnylSWCTNAYALAQGYG----------APVQSSIGFdatITSLFSPLLVGKRVVLLPeKEEIEALSALLQSD 696
Cdd:COG0318 119 MLTHR------NLLANAAAIAAALGltpgdvvlvaLPLFHVFGL---TVGLLAPLLAGATLVLLP-RFDPERVLELIERE 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 697 Q--NYSLVkitPAHLEMLNQMLPNHKGVTET-RALIIGGEALLGKSLNFWRDnAPKTRIINEYGPTETVVGCCVYEVDEQ 773
Cdd:COG0318 189 RvtVLFGV---PTMLARLLRHPEFARYDLSSlRLVVSGGAPLPPELLERFEE-RFGVRIVEGYGLTETSPVVTVNPEDPG 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 774 TSLSGAIliGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPnpfsdepnsRLYKTGDLARY 853
Cdd:COG0318 265 ERRPGSV--GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRD---------GWLRTGDLGRL 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 854 LPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQA-PTSSELRQFLQSKL 932
Cdd:COG0318 334 DEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAeLDAEELRAFLRERL 413
|
490 500 510
....*....|....*....|....*....|
gi 2129675820 933 PEYMIPSAFVMLEVIPLTTHGKVDRQALPQ 962
Cdd:COG0318 414 ARYKVPRRVEFVDELPRTASGKIDRRALRE 443
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
475-960 |
1.77e-86 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 291.41 E-value: 1.77e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 475 VERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGV---KPEVLVGicvERSLDMLIGILGILKAGGAYIPFDPTYPQ 551
Cdd:PRK04813 12 AQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLpdkSPIIVFG---HMSPEMLATFLGAVKAGHAYIPVDVSSPA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 552 ERLGFMLEDAQIPILLTQQRLvdKFVEHKTQIICLD---RDLPENATLSIDNPVSNvtsENLAYIIYTSGSTGKPKGTMI 628
Cdd:PRK04813 89 ERIEMIIEVAKPSLIIATEEL--PLEILGIPVITLDelkDIFATGNPYDFDHAVKG---DDNYYIIFTSGTTGKPKGVQI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 629 PHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPeKEEIEAL----SALLQSDQNyslVKI 704
Cdd:PRK04813 164 SHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALP-KDMTANFkqlfETLPQLPIN---VWV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 705 -TPAHLEM-LnqMLP--NHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQtslsgaI 780
Cdd:PRK04813 240 sTPSFADMcL--LDPsfNEEHLPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEITDE------M 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 781 L-------IGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFipnpFSDEpNSRLYKTGDLArY 853
Cdd:PRK04813 312 LdqykrlpIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFD-GQPAYHTGDAG-Y 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 854 LPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKE-----QAPTSSELRQFL 928
Cdd:PRK04813 386 LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEedferEFELTKAIKKEL 465
|
490 500 510
....*....|....*....|....*....|..
gi 2129675820 929 QSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK04813 466 KERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
465-962 |
8.18e-83 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 280.88 E-value: 8.18e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 465 KCLHELFAAqVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGV---KPEVLVGicvERSLDMLIGILGILKAGGA 541
Cdd:TIGR01734 1 KLIEAIQAF-AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILpkkSPIIVYG---HMEPHMLVAFLGSIKSGHA 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 542 YIPFDPTYPQERLGFMLEDAQIPILLTQQRLVDKFVEhkTQIICLDRD---LPENATLSIDNPVSNvtSENLaYIIYTSG 618
Cdd:TIGR01734 77 YIPVDTSIPSERIEMIIEAAGPELVIHTAELSIDAVG--TQIITLSALeqaETSGGPVSFDHAVKG--DDNY-YIIYTSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 619 STGKPKGTMIPHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPE------KEEIEALSAL 692
Cdd:TIGR01734 152 STGNPKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKditnnfKLLFEELPKT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 693 lqsdqNYSLVKITPAHLEM------LNQmlPNHKGVTEtraLIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCC 766
Cdd:TIGR01734 232 -----GLNVWVSTPSFVDMclldpnFNQ--ENYPHLTH---FLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVT 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 767 VYEV-DEQTSLSGAILIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFipnpFSDEpNSRLY 845
Cdd:TIGR01734 302 SVKItQEILDQYPRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF----FSHE-GQPAY 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 846 KTGDLArYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLV-NAVTVIAREDQPGDKRLVGYIVPKEQA-----P 919
Cdd:TIGR01734 377 RTGDAG-TITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIeSAVVVPKYNKDHKVEYLIAAIVPETEDfekefQ 455
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2129675820 920 TSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALPQ 962
Cdd:TIGR01734 456 LTKAIKKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKALAE 498
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
488-963 |
9.06e-74 |
|
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: 255.52 E-value: 9.06e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 488 HESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQiPILL 567
Cdd:cd17647 18 TRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAK-PRGL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 568 TQQRLVDKFVehktqiicldrdlpenatlsidNPVSNVTsenlayIIYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYALA 647
Cdd:cd17647 97 IVIRAAGVVV----------------------GPDSNPT------LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 648 QGYGAPVQSSIGFDATITSLFSPLLVGKRVvLLPEKEEIEALSALLQSDQNY--SLVKITPAHLEML-----NQMLPNHk 720
Cdd:cd17647 149 ENDKFTMLSGIAHDPIQRDMFTPLFLGAQL-LVPTQDDIGTPGRLAEWMAKYgaTVTHLTPAMGQLLtaqatTPFPKLH- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 721 gvtetRALIIGgEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTS-------LSGAILIGRPIANTQLYL 793
Cdd:cd17647 227 -----HAFFVG-DILTKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVPSRSSdptflknLKDVMPAGRGMLNVQLLV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 794 LD--DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDE--------------------PNSRLYKTGDLA 851
Cdd:cd17647 301 VNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPdhwnyldkdnnepwrqfwlgPRDRLYRTGDLG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 852 RYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTS---------- 921
Cdd:cd17647 381 RYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDesfaqedvpk 460
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 922 ------------------SELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALPQP 963
Cdd:cd17647 461 evstdpivkgligyrkliKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
610-956 |
7.54e-65 |
|
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: 223.70 E-value: 7.54e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 610 LAYIIYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEKEEIEAL 689
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 690 SALlqsdQNYslvKIT-----PAHLEMLNQmLPNHKGVTET--RALIIGGEALLGKSLNFWRDnAPKTRIINEYGPTETV 762
Cdd:cd04433 82 ELI----ERE---KVTillgvPTLLARLLK-APESAGYDLSslRALVSGGAPLPPELLERFEE-APGIKLVNGYGLTETG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 763 VGCCVYEVDEQTSLSGAIliGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNpfsdepns 842
Cdd:cd04433 153 GTVATGPPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG-------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 843 rLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQA-PTS 921
Cdd:cd04433 223 -WYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGAdLDA 301
|
330 340 350
....*....|....*....|....*....|....*
gi 2129675820 922 SELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVD 956
Cdd:cd04433 302 EELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
467-960 |
1.57e-60 |
|
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: 215.50 E-value: 1.57e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD 546
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 547 PTYPQERLGFMLEDAQIPILLtqqrlVDKFVEHKTQIiclDRDLPENATlsidnpvsnVTSENLAYIIYTSGSTGKPKGT 626
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALI-----VAVSFTDLLAA---GAPLGERVA---------LTPEDVAVLQYTSGTTGVPKGA 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 627 MIPHRGLVnylswcTNAYALAQGYGAPVQSSIGFDATI---------TSLFSPLLVGKRVVLLPEKEEIEALSALLQSDq 697
Cdd:cd05936 144 MLTHRNLV------ANALQIKAWLEDLLEGDDVVLAALplfhvfgltVALLLPLALGATIVLIPRFRPIGVLKEIRKHR- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 698 nyslVKITPAHLEMLNQMLpNHKGVTET-----RALIIGGEALLGKSLNFWRDnapKT--RIINEYGPTETV-VGCC--V 767
Cdd:cd05936 217 ----VTIFPGVPTMYIALL-NAPEFKKRdfsslRLCISGGAPLPVEVAERFEE---LTgvPIVEGYGLTETSpVVAVnpL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 768 YEVDEQTSlsgailIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIpnpfsdepNSRLyKT 847
Cdd:cd05936 289 DGPRKPGS------IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFV--------DGWL-RT 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 848 GDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKE-QAPTSSELRQ 926
Cdd:cd05936 354 GDIGYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEgASLTEEEIIA 433
|
490 500 510
....*....|....*....|....*....|....
gi 2129675820 927 FLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05936 434 FCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
490-960 |
4.70e-58 |
|
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: 207.71 E-value: 4.70e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAqipilltq 569
Cdd:cd17654 16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKC-------- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 570 qrLVDKFVEHKTQIICLDRDLPENATLSIDnpvsnvTSENLAYIIYTSGSTGKPKGTMIPHRGLV-NYLSWCT------- 641
Cdd:cd17654 88 --HVSYLLQNKELDNAPLSFTPEHRHFNIR------TDECLAYVIHTSGTTGTPKIVAVPHKCILpNIQHFRSlfnitse 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 642 NAYALAqgygapvqSSIGFDATITSLFSPLLVGkrVVLLPEKEEIEALSALLQ----SDQNYSLVKITPAHLEMLNQMLP 717
Cdd:cd17654 160 DILFLT--------SPLTFDPSVVEIFLSLSSG--ATLLIVPTSVKVLPSKLAdilfKRHRITVLQATPTLFRRFGSQSI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 718 NHK---GVTETRALIIGGEALLGKSLN-FWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSlsgAILIGRPIANTQLYL 793
Cdd:cd17654 230 KSTvlsATSSLRVLALGGEPFPSLVILsSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDS---PVQLGSPLLGTVIEV 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 794 LDdkqkLVPIGVPGELYIGgaGVARGYLNRPELTQqrfipnpfsdePNSRLYKTGDLARyLPDGNIEYLGRIDHQVKIRG 873
Cdd:cd17654 307 RD----QNGSEGTGQVFLG--GLNRVCILDDEVTV-----------PKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRG 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 874 FRIELEEIESLLAQHPLVNAvTVIAREDQpgdKRLVGYIVPKE-QAPTSSELRQFLqskLPEYMIPSAFVMLEVIPLTTH 952
Cdd:cd17654 369 KRINLDLIQQVIESCLGVES-CAVTLSDQ---QRLIAFIVGESsSSRIHKELQLTL---LSSHAIPDTFVQIDKLPLTSH 441
|
....*...
gi 2129675820 953 GKVDRQAL 960
Cdd:cd17654 442 GKVDKSEL 449
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
467-960 |
2.01e-57 |
|
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an AMP-binding domain (pfam00501) associated with acyl CoA-ligases. These proteins are generally found in genomes containing the exosortase/PEP-CTERM protein expoert system, specifically the type 1 variant of this system described by the Genome Property GenProp0652. When found in this context they are invariably present next to a decarboxylase enzyme. A number of sequences from Burkholderia species also hit this model, but the genomic context is obviously different. The hypothesis of a constant substrate for this family is only strong where the exosortase context is present.
Pssm-ID: 211788 [Multi-domain] Cd Length: 517 Bit Score: 208.10 E-value: 2.01e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD 546
Cdd:TIGR03098 2 LHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 547 PTYPQERLGFMLEDAQIPILLTQQRLVDKFveHKTQIICLD----------------------RDLPENATLSIDNPVSN 604
Cdd:TIGR03098 82 PLLKAEQVAHILADCNVRLLVTSSERLDLL--HPALPGCHDlrtliivgdpahaseghpgeepASWPKLLALGDADPPHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 605 VTSENLAYIIYTSGSTGKPKGTMIPHRGLV-------NYLSWCTNAYALAqgyGAPvqssIGFDATITSLFSPLLVGKRV 677
Cdd:TIGR03098 160 VIDSDMAAILYTSGSTGRPKGVVLSHRNLVagaqsvaTYLENRPDDRLLA---VLP----LSFDYGFNQLTTAFYVGATV 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 678 V----LLP-------EKEEIEALSAllqsdqnyslvkITPAHLEMLNQMLPNHKGVTeTRALIIGGEALLGKSLNFWRDN 746
Cdd:TIGR03098 233 VlhdyLLPrdvlkalEKHGITGLAA------------VPPLWAQLAQLDWPESAAPS-LRYLTNSGGAMPRATLSRLRSF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 747 APKTRIINEYGPTETVVGCCV--YEVDEQ-TSlsgailIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNR 823
Cdd:TIGR03098 300 LPNARLFLMYGLTEAFRSTYLppEEVDRRpDS------IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWND 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 824 PELTQQRFIPNP-FSDEPnsRLYKT----GDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLV-NAVTVI 897
Cdd:TIGR03098 374 PEKTAERFRPLPpFPGEL--HLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVaEAVAFG 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129675820 898 AREDQPGDkRLVGYIVPKEQAPTS-SELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:TIGR03098 452 VPDPTLGQ-AIVLVVTPPGGEELDrAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
490-935 |
3.63e-56 |
|
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: 203.60 E-value: 3.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQ 569
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 570 QRLVD------KFVEHKTQIICLdrDLPENATLSIDNPVSNVTSEN--------------LAYIIYTSGSTGKPKGTMIP 629
Cdd:cd05911 90 PDGLEkvkeaaKELGPKDKIIVL--DDKPDGVLSIEDLLSPTLGEEdedlppplkdgkddTAAILYSSGTTGLPKGVCLS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 630 HRGLVNYLSWCTNAYALAQGYGAPVQSSI------GFDATITSlfspLLVGKRVVLLPEKEEIEALSALlqsdQNY--SL 701
Cdd:cd05911 168 HRNLIANLSQVQTFLYGNDGSNDVILGFLplyhiyGLFTTLAS----LLNGATVIIMPKFDSELFLDLI----EKYkiTF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 702 VKITPAHLEMLNqmlpNHKGVTET-----RALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCV--YEVDEQT 774
Cdd:cd05911 240 LYLVPPIAAALA----KSPLLDKYdlsslRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVnpDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 775 SlsgailIGRPIANTQLYLLD-DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARY 853
Cdd:cd05911 316 S------VGRLLPNVEAKIVDdDGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW--------LHTGDIGYF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 854 LPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAP-TSSELRQFLQSKL 932
Cdd:cd05911 382 DEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKlTEKEVKDYVAKKV 461
|
...
gi 2129675820 933 PEY 935
Cdd:cd05911 462 ASY 464
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
479-960 |
5.95e-51 |
|
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: 188.73 E-value: 5.95e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 479 PNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFML 558
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 559 EDAQIPILLTQQRLVDKF-------VEHKTQIICLDRDLPEN---------ATLSIDNPVSNVTSENLAYIIYTSGSTGK 622
Cdd:cd05959 98 EDSRARVVVVSGELAPVLaaaltksEHTLVVLIVSGGAGPEAgalllaelvAAEAEQLKPAATHADDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 623 PKGTMIPHRGLVnylsWCTNAYalAQGYGAPVQSSIGFDATI--------TSLFSPLLVGKRVVLLPEKEEIEALSALLQ 694
Cdd:cd05959 178 PKGVVHLHADIY----WTAELY--ARNVLGIREDDVCFSAAKlffayglgNSLTFPLSVGATTVLMPERPTPAAVFKRIR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 695 SDQNYSLVKITPAHLEMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTrIINEYGPTETVVGCCvyevdeqT 774
Cdd:cd05959 252 RYRPTVFFGVPTLYAAMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARFGLD-ILDGIGSTEMLHIFL-------S 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 775 SLSGAI---LIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIpnpfsdepnSRLYKTGDLA 851
Cdd:cd05959 324 NRPGRVrygTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ---------GEWTRTGDKY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 852 RYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPK----EQAPTSSELRQF 927
Cdd:cd05959 395 VRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRpgyeDSEALEEELKEF 474
|
490 500 510
....*....|....*....|....*....|...
gi 2129675820 928 LQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05959 475 VKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
468-969 |
3.70e-50 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 187.63 E-value: 3.70e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 468 HELFAAQVERTPNNIAVEF-----NHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAY 542
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWegedgEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 543 IPFDPTYPQERLGFMLEDAQIPILLT--QQRLVDKFVEHK-------------TQIICLDR--------------DLPEN 593
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITadGGLRGGKVIDLKekvdealeelpslEHVIVVGRtgadvpmegdldwdELLAA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 594 ATLSIDnPVSnVTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLS---------------WCTnayalaqgygapvqSSI 658
Cdd:COG0365 172 ASAEFE-PEP-TDADDPLFILYTSGTTGKPKGVVHTHGGYLVHAAttakyvldlkpgdvfWCT--------------ADI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 659 GFdATITS--LFSPLLVGKRVVLLPEK----------EEIE------------ALSALLQSD----QNYSLVKItpahle 710
Cdd:COG0365 236 GW-ATGHSyiVYGPLLNGATVVLYEGRpdfpdpgrlwELIEkygvtvfftaptAIRALMKAGdeplKKYDLSSL------ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 711 mlnqmlpnhkgvtetRALIIGGEALLGKSLNFWRDNApKTRIINEYGPTETvvGCCVyevdeqtsLSGAIL-------IG 783
Cdd:COG0365 309 ---------------RLLGSAGEPLNPEVWEWWYEAV-GVPIVDGWGQTET--GGIF--------ISNLPGlpvkpgsMG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 784 RPIANTQLYLLDDKQKLVPIGVPGELYIGGA--GVARGYLNRPELTQQRFipnpFSDEPNsrLYKTGDLARYLPDGNIEY 861
Cdd:COG0365 363 KPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPERYRETY----FGRFPG--WYRTGDGARRDEDGYFWI 436
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 862 LGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTS----SELRQFLQSKLPEYMI 937
Cdd:COG0365 437 LGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEPSdelaKELQAHVREELGPYAY 516
|
570 580 590
....*....|....*....|....*....|....*....
gi 2129675820 938 PSAFVMLEVIPLTTHGKVDRQAL-------PQPDTSRLD 969
Cdd:COG0365 517 PREIEFVDELPKTRSGKIMRRLLrkiaegrPLGDTSTLE 555
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
477-957 |
4.91e-50 |
|
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: 183.97 E-value: 4.91e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 477 RTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPfdptypqerLGF 556
Cdd:cd17631 7 RHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVP---------LNF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 557 MLEDAQIPILLTQQRlvdkfvehktqiicldrdlpenATLSIDNPvsnvtsenlAYIIYTSGSTGKPKGTMIPHRGLVNY 636
Cdd:cd17631 78 RLTPPEVAYILADSG----------------------AKVLFDDL---------ALLMYTSGTTGRPKGAMLTHRNLLWN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 637 LSWCTNAYALAQG----YGAPVqssigFDATITSLFSP--LLVGKRVVLLPeKEEIEALSALLQSDQ--NYSLVkitPAh 708
Cdd:cd17631 127 AVNALAALDLGPDdvllVVAPL-----FHIGGLGVFTLptLLRGGTVVILR-KFDPETVLDLIERHRvtSFFLV---PT- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 709 leMLNQMLpNHKGVTET-----RALIIGGEALLGKSLNFWRDNAPKtrIINEYGPTETVVGCCVYEVDEQTSLSGAIliG 783
Cdd:cd17631 197 --MIQALL-QHPRFATTdlsslRAVIYGGAPMPERLLRALQARGVK--FVQGYGMTETSPGVTFLSPEDHRRKLGSA--G 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 784 RPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTqqrfiPNPFSDEpnsrLYKTGDLARYLPDGNIEYLG 863
Cdd:cd17631 270 RPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEAT-----AAAFRDG----WFHTGDLGRLDEDGYLYIVD 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 864 RIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAP-TSSELRQFLQSKLPEYMIPSAFV 942
Cdd:cd17631 341 RKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAElDEDELIAHCRERLARYKIPKSVE 420
|
490
....*....|....*
gi 2129675820 943 MLEVIPLTTHGKVDR 957
Cdd:cd17631 421 FVDALPRNATGKILK 435
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
8-451 |
8.38e-50 |
|
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: 183.69 E-value: 8.38e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 8 SPQQKHLWLQQK--DNYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFhSLPGMNIPFQSISDaptYNHISLA 85
Cdd:pfam00668 8 SPAQKRMWFLEKlePHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVF-IRQENGEPVQVILE---ERPFELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 86 EYDWSRLSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACLD 165
Cdd:pfam00668 84 IIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 166 GEEISE-EVMQYADVSEWLNELLESEDTETARNYWQQQDISSVLNLRIPfeikNDHQSSGEISFAPQSLCLAMNRDTVEK 244
Cdd:pfam00668 164 GEPLPLpPKTPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLP----KDYARPADRSFKGDRLSFTLDEDTEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 245 LEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDALKFSELMERVSES 324
Cdd:pfam00668 240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 325 LRFVKKWQEY-FNWENFISTNEKFAAR-PFFP--FCFDFTQQSQSYVNGNIaFSEYKKSANIDKFQIK---LSSGYSQDN 397
Cdd:pfam00668 320 LLSAEPHQGYpFGDLVNDLRLPRDLSRhPLFDpmFSFQNYLGQDSQEEEFQ-LSELDLSVSSVIEEEAkydLSLTASERG 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2129675820 398 --LVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNPEAAIIDLNMISESDRQKLL 451
Cdd:pfam00668 399 ggLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
469-960 |
4.72e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 180.10 E-value: 4.72e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 469 ELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPT 548
Cdd:PRK07656 9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 549 YPQERLGFMLEDAQIPILLTQQRLVDKF---------VEHKtqIICLDRDLPENA--TLSIDNPVSN---------VTSE 608
Cdd:PRK07656 89 YTADEAAYILARGDAKALFVLGLFLGVDysattrlpaLEHV--VICETEEDDPHTekMKTFTDFLAAgdpaerapeVDPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 609 NLAYIIYTSGSTGKPKGTMIPHRGLV-NYLSWCTNAyALAQG--YGA--PVQSSIGFDAtitSLFSPLLVGKRVVLLPeK 683
Cdd:PRK07656 167 DVADILFTSGTTGRPKGAMLTHRQLLsNAADWAEYL-GLTEGdrYLAanPFFHVFGYKA---GVNAPLMRGATILPLP-V 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 684 EEIEALSALLQSDQnyslVKITPAHLEMLNQMLpNHKGVTET-----RALIIGGEALLGKSLNFWRDNAPKTRIINEYGP 758
Cdd:PRK07656 242 FDPDEVFRLIETER----ITVLPGPPTMYNSLL-QHPDRSAEdlsslRLAVTGAASMPVALLERFESELGVDIVLTGYGL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 759 TETV-VGCCVYEVDEQTSLSGAilIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFipnpfs 837
Cdd:PRK07656 317 SEASgVTTFNRLDDDRKTVAGT--IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAI------ 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 838 dEPNSRLYkTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQpgdkRL--VG--YIV 913
Cdd:PRK07656 389 -DADGWLH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDE----RLgeVGkaYVV 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2129675820 914 PKEQAP-TSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK07656 463 LKPGAElTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
482-960 |
1.18e-47 |
|
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: 177.10 E-value: 1.18e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 482 IAVEFNHESLTYAQLNAKSNQLAHHLQ-KLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLED 560
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 561 AQIPILLtqqrlvdkfvehktqiicldrdlpenatlsidnpvsnvtseNLAYIIYTSGSTGKPKGTMIPHRGLVNYLSWC 640
Cdd:cd05941 83 SEPSLVL-----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 641 TNAYALAQG----YGAPVQSSIGfdaTITSLFSPLLVGKRVVLLPEKEEIEALSALLQSDQN--------YSlvKITPAH 708
Cdd:cd05941 122 VDAWRWTEDdvllHVLPLHHVHG---LVNALLCPLFAGASVEFLPKFDPKEVAISRLMPSITvfmgvptiYT--RLLQYY 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 709 LEMLNQMLPNHKGVTET-RALIIGGEALLGKSLNFWRDnapKT--RIINEYGPTETVVgccvyevdeqtSLSGAI----- 780
Cdd:cd05941 197 EAHFTDPQFARAAAAERlRLMVSGSAALPVPTLEEWEA---ITghTLLERYGMTEIGM-----------ALSNPLdgerr 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 781 --LIGRPIANTQLYLLDDK-QKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARYLPDG 857
Cdd:cd05941 263 pgTVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW--------FKTGDLGVVDEDG 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 858 NIEYLGRI-DHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSS--ELRQFLQSKLPE 934
Cdd:cd05941 335 YYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSleELKEWAKQRLAP 414
|
490 500
....*....|....*....|....*.
gi 2129675820 935 YMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05941 415 YKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
490-960 |
5.37e-46 |
|
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: 172.26 E-value: 5.37e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQ 569
Cdd:cd05919 10 SVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 570 QrlvdkfvehktqiicldrdlpenatlsidnpvsnvtsENLAYIIYTSGSTGKPKGTMIPHRGLVNYL-SWCTNAYALAQ 648
Cdd:cd05919 90 A-------------------------------------DDIAYLLYSSGTTGPPKGVMHAHRDPLLFAdAMAREALGLTP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 649 GYGAPVQSSIGFD-ATITSLFSPLLVGKRVVLLPEKEEIEALSALLQSDQNYSLVKITPAHLEMLNQMLPNHKGVTETRA 727
Cdd:cd05919 133 GDRVFSSAKMFFGyGLGNSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDALRSLRL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 728 LIIGGEALLGKSLNFWRDnAPKTRIINEYGPTETVvgccvyevdeQTSLS---GAILI---GRPIANTQLYLLDDKQKLV 801
Cdd:cd05919 213 CVSAGEALPRGLGERWME-HFGGPILDGIGATEVG----------HIFLSnrpGAWRLgstGRPVPGYEIRLVDEEGHTI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 802 PIGVPGELYIGGAGVARGYLNRPELTQQRFipnpfsdepNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEI 881
Cdd:cd05919 282 PPGEEGDLLVRGPSAAVGYWNNPEKSRATF---------NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 882 ESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPK-EQAPT---SSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDR 957
Cdd:cd05919 353 ESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKsPAAPQeslARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQR 432
|
...
gi 2129675820 958 QAL 960
Cdd:cd05919 433 FKL 435
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
467-960 |
8.62e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 167.67 E-value: 8.62e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD 546
Cdd:PRK06187 8 IGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPIN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 547 PTYPQERLGFMLEDAQIPILLTQQRLVD---------KFVEHKtqIICLDRDLPENATLSI----------DNPVSNVTS 607
Cdd:PRK06187 88 IRLKPEEIAYILNDAEDRVVLVDSEFVPllaailpqlPTVRTV--IVEGDGPAAPLAPEVGeyeellaaasDTFDFPDID 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 608 EN-LAYIIYTSGSTGKPKGTMIPHRglvnylswctNAYALAQGygapVQSSIGFDAT-----ITSLF---------SPLL 672
Cdd:PRK06187 166 ENdAAAMLYTSGTTGHPKGVVLSHR----------NLFLHSLA----VCAWLKLSRDdvylvIVPMFhvhawglpyLALM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 673 VGKRVVLLPEKEEIEALSALLQSdqnyslvKITPAHL--EMLnQMLPNHKGVTET-----RALIIGGEALLGKSLNFWRD 745
Cdd:PRK06187 232 AGAKQVIPRRFDPENLLDLIETE-------RVTFFFAvpTIW-QMLLKAPRAYFVdfsslRLVIYGGAALPPALLREFKE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 746 NApKTRIINEYGPTET--VVGCCVYEVDEQTSLSGAILIGRPIANTQLYLLDDKQKLVP--IGVPGELYIGGAGVARGYL 821
Cdd:PRK06187 304 KF-GIDLVQGYGMTETspVVSVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYW 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 822 NRPELTQqRFIPNPFsdepnsrlYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIARED 901
Cdd:PRK06187 383 NRPEATA-ETIDGGW--------LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPD 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 902 QPGDKRLVGYIVPKE-QAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK06187 454 EKWGERPVAVVVLKPgATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
464-968 |
2.10e-42 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 164.15 E-value: 2.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 464 DKCLHELFAAQVERTPNNIAVEFNH-ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAY 542
Cdd:PRK06087 22 DASLADYWQQTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 543 IPFDPTYPQERLGFMLEDAQ-----IPILLTQQRLVDKF------VEHKTQIICLDRDLPENATLSIDN------PVS-- 603
Cdd:PRK06087 102 VPLLPSWREAELVWVLNKCQakmffAPTLFKQTRPVDLIlplqnqLPQLQQIVGVDKLAPATSSLSLSQiiadyePLTta 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 604 -NVTSENLAYIIYTSGSTGKPKGTMIPHrglvNYLSWCTNAYALAQGYG--------APVQSSIGFDATITslfSPLLVG 674
Cdd:PRK06087 182 iTTHGDELAAVLFTSGTEGLPKGVMLTH----NNILASERAYCARLNLTwqdvfmmpAPLGHATGFLHGVT---APFLIG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 675 KRVVLLPEKEEIEALSALLQSDQNYSLvKITPAHLEMLNQMLPNHKGVTETRALIIGGEALLGKSL-NFWRDNapkTRII 753
Cdd:PRK06087 255 ARSVLLDIFTPDACLALLEQQRCTCML-GATPFIYDLLNLLEKQPADLSALRFFLCGGTTIPKKVArECQQRG---IKLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 754 NEYGPTETVVGCCVyEVDEQTSLSGAiLIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFip 833
Cdd:PRK06087 331 SVYGSTESSPHAVV-NLDDPLSRFMH-TDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARAL-- 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 834 npfsDEPNsrLYKTGDLARYLPDGNIEYLGRiDHQVKIRGFR-IELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYI 912
Cdd:PRK06087 407 ----DEEG--WYYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2129675820 913 VPK--EQAPTSSELRQFLQSK-LPEYMIPSAFVMLEVIPLTTHGKVDRQALPQPDTSRL 968
Cdd:PRK06087 480 VLKapHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMRRL 538
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
500-960 |
5.10e-42 |
|
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: 161.07 E-value: 5.10e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 500 SNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGA----YIPFDPTYPQERLGFMLEDAQIPILLTQQRLVDK 575
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAADR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 576 FveHKTQIICLDRDL---PENATLSIDN-PVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVnylswcTNAYALAQGYG 651
Cdd:cd05922 83 L--RDALPASPDPGTvldADGIRAARASaPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLL------ANARSIAEYLG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 652 ------APVQSSIGFDATITSLFSPLLVGKRVVLLPEKEEIEALSALLQsDQNYSLVKITPAHLEMLNQM------LPNH 719
Cdd:cd05922 155 itaddrALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDLR-EHGATGLAGVPSTYAMLTRLgfdpakLPSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 720 KGVTETraliigGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSLSGAIliGRPIANTQLYLLDDKQK 799
Cdd:cd05922 234 RYLTQA------GGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYLPPERILEKPGSI--GLAIPGGEFEILDDDGT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 800 LVPIGVPGELYIGGAGVARGYLNRPEltqqrFIPNPfsDEPNSRLYkTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELE 879
Cdd:cd05922 306 PTPPGEPGEIVHRGPNVMKGYWNDPP-----YRRKE--GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 880 EIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPtsSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQA 959
Cdd:cd05922 378 EIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKIDP--KDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAA 455
|
.
gi 2129675820 960 L 960
Cdd:cd05922 456 L 456
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
489-960 |
8.92e-42 |
|
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: 159.91 E-value: 8.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 489 ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLT 568
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 569 qqrlvdkfvehktqiicldrDLpenatlsidnpvsnvtSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYALAQ 648
Cdd:cd05971 85 --------------------DG----------------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 649 G-----YGAPVQSSIG--FDATITSLFSPL-LVGKRvvllPEKEEIEALSALLqSDQNYSLVKITPAHLEMLNQMLP--N 718
Cdd:cd05971 129 RdgdlyWTPADWAWIGglLDVLLPSLYFGVpVLAHR----MTKFDPKAALDLM-SRYGVTTAFLPPTALKMMRQQGEqlK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 719 HKGVtETRALIIGGEALLGKSLNFWRDNAPKTriINE-YGPTET--VVGCC--VYEVDEQTslsgailIGRPIANTQLYL 793
Cdd:cd05971 204 HAQV-KLRAIATGGESLGEELLGWAREQFGVE--VNEfYGQTECnlVIGNCsaLFPIKPGS-------MGKPIPGHRVAI 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 794 LDDKQKLVPIGVPGELyiggaGVAR-------GYLNRPELTQQRFipnpfsdepNSRLYKTGDLARYLPDGNIEYLGRID 866
Cdd:cd05971 274 VDDNGTPLPPGEVGEI-----AVELpdpvaflGYWNNPSATEKKM---------AGDWLLTGDLGRKDSDGYFWYVGRDD 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 867 HQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTS----SELRQFLQSKLPEYMIPSAFV 942
Cdd:cd05971 340 DVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSdalaREIQELVKTRLAAHEYPREIE 419
|
490
....*....|....*...
gi 2129675820 943 MLEVIPLTTHGKVDRQAL 960
Cdd:cd05971 420 FVNELPRTATGKIRRREL 437
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
482-960 |
3.13e-40 |
|
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: 156.70 E-value: 3.13e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 482 IAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDA 561
Cdd:cd05926 6 LVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 562 QIPILLTQQ---------------RLVDKFVEHKTQIICLD-RDLP-ENATLSIDNPVSNVTSENLAYIIYTSGSTGKPK 624
Cdd:cd05926 86 GSKLVLTPKgelgpasraasklglAILELALDVGVLIRAPSaESLSnLLADKKNAKSEGVPLPDDLALILHTSGTTGRPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 625 GTMIPHRGLVNYLSWCTNAYALAQGygapvqssigfDAT------------ITSLFSPLLVGKRVVLLPekeeieALSAL 692
Cdd:cd05926 166 GVPLTHRNLAASATNITNTYKLTPD-----------DRTlvvmplfhvhglVASLLSTLAAGGSVVLPP------RFSAS 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 693 L---QSDQN----YSLVkitPAhleMLNQMLPNHKGVTETR----------------ALIIGGEALLGkslnfwrdnAPk 749
Cdd:cd05926 229 TfwpDVRDYnatwYTAV---PT---IHQILLNRPEPNPESPppklrfirscsaslppAVLEALEATFG---------AP- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 750 trIINEYGPTETV--VGCCVYEVDEQTSLSgailIGRPiANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELT 827
Cdd:cd05926 293 --VLEAYGMTEAAhqMTSNPLPPGPRKPGS----VGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEAN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 828 QQRFIPNPFsdepnsrlYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKR 907
Cdd:cd05926 366 AEAAFKDGW--------FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEE 437
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2129675820 908 LVGYIVPKEQAP-TSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05926 438 VAAAVVLREGASvTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
467-960 |
5.76e-40 |
|
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: 155.74 E-value: 5.76e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHEL--FAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIP 544
Cdd:cd05923 3 VFEMlrRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 545 FDPTYPQERLGFMLEDAQI------PILLTQQRLVDKFVEHKTQIICLDRDLPENATLSIDNPVSNVtsENLAYIIYTSG 618
Cdd:cd05923 83 INPRLKAAELAELIERGEMtaaviaVDAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDPPREP--EQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 619 STGKPKGTMIPHRGLVNYLSWCTNAYALAQGYG------APVQSSIGFDATitsLFSPLLVGKRVVLLPEKEEIEALsAL 692
Cdd:cd05923 161 TTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHnvvlglMPLYHVIGFFAV---LVAALALDGTYVVVEEFDPADAL-KL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 693 LQSDQNYSLVkITPAHLE-MLNQMLPNHKGVTETRALIIGGEAL---LGKSLNfwrdNAPKTRIINEYGPTETVVGCCVY 768
Cdd:cd05923 237 IEQERVTSLF-ATPTHLDaLAAAAEFAGLKLSSLRHVTFAGATMpdaVLERVN----QHLPGEKVNIYGTTEAMNSLYMR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 769 EVDEQTSLsgailigRPIANTQLY---LLDDKQKLVPIGVPGELYIGGAGVA--RGYLNRPELTQQRFipnpfsdepNSR 843
Cdd:cd05923 312 DARTGTEM-------RPGFFSEVRivrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKL---------QDG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 844 LYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSE 923
Cdd:cd05923 376 WYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADE 455
|
490 500 510
....*....|....*....|....*....|....*...
gi 2129675820 924 LRQF-LQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05923 456 LDQFcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
460-960 |
8.39e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 156.74 E-value: 8.39e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 460 EFPH-DKCLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKA 538
Cdd:PRK06178 27 EYPHgERPLTEYLRAWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 539 GGAYIPFDPTYPQERLGFMLEDAQIPILLTQQRLVDKFVEHKTQ-------IICLDRDLPENATL----SIDNP------ 601
Cdd:PRK06178 107 GAVHVPVSPLFREHELSYELNDAGAEVLLALDQLAPVVEQVRAEtslrhviVTSLADVLPAEPTLplpdSLRAPrlaaag 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 602 -------VSNVTSE---------NLAYIIYTSGSTGKPKGTMIPHRGLVnYLswCTNAYALAQGYGAPvQSSIGFDATI- 664
Cdd:PRK06178 187 aidllpaLRACTAPvplpppaldALAALNYTGGTTGMPKGCEHTQRDMV-YT--AAAAYAVAVVGGED-SVFLSFLPEFw 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 665 -----TSLFSPLLVGKRVVLLPEKEEIEALSALlqsdQNYSlVKITPAHLEMLNQMLpNHKGVTET--RALIIGGEALLG 737
Cdd:PRK06178 263 iagenFGLLFPLFSGATLVLLARWDAVAFMAAV----ERYR-VTRTVMLVDNAVELM-DHPRFAEYdlSSLRQVRVVSFV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 738 KSLNF-----WRDNAPKTRIINEYGPTET------VVGccvYEVDEQTSLSGAILIGRPIANTQLYLLD-DKQKLVPIGV 805
Cdd:PRK06178 337 KKLNPdyrqrWRALTGSVLAEAAWGMTEThtcdtfTAG---FQDDDFDLLSQPVFVGLPVPGTEFKICDfETGELLPLGA 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 806 PGELYIGGAGVARGYLNRPELTQQRFIPNpfsdepnsrLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLL 885
Cdd:PRK06178 414 EGEIVVRTPSLLKGYWNKPEATAEALRDG---------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALL 484
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2129675820 886 AQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSE-LRQFLQSKLPEYMIPSAFVmLEVIPLTTHGKVDRQAL 960
Cdd:PRK06178 485 GQHPAVLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAaLQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
492-960 |
1.09e-39 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 153.76 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 492 TYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQr 571
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 572 lvdKFVEHKTQIICLDR-DLPENATLSIDnpvSNVTSENLAYIIYTSGSTGKPKGTMIPHRglvnylswctNAYALAQGy 650
Cdd:TIGR01923 80 ---LLEEKDFQADSLDRiEAAGRYETSLS---ASFNMDQIATLMFTSGTTGKPKAVPHTFR----------NHYASAVG- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 651 gapVQSSIGFDAT--------------ITSLFSPLLVGKRVVLlpekeeIEALSALLQSDQNYslvKITPAHL--EMLNQ 714
Cdd:TIGR01923 143 ---SKENLGFTEDdnwllslplyhisgLSILFRWLIEGATLRI------VDKFNQLLEMIANE---RVTHISLvpTQLNR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 715 MLPNHKGVTETRALIIGGEA----LLGKSLNFwrdNAPktrIINEYGPTETVVGCCVYEVDeqtSLSGAILIGRPIANTQ 790
Cdd:TIGR01923 211 LLDEGGHNENLRKILLGGSAipapLIEEAQQY---GLP---IYLSYGMTETCSQVTTATPE---MLHARPDVGRPLAGRE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 791 LYLLDDKQKLVpigvpGELYIGGAGVARGYLNRPELTQQRFipnpfsdepNSRLYKTGDLARYLPDGNIEYLGRIDHQVK 870
Cdd:TIGR01923 282 IKIKVDNKEGH-----GEIMVKGANLMKGYLYQGELTPAFE---------QQGWFNTGDIGELDGEGFLYVLGRRDDLII 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 871 IRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVpKEQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLT 950
Cdd:TIGR01923 348 SGGENIYPEEIETVLYQHPGIQEAVVVPKPDAEWGQVPVAYIV-SESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYN 426
|
490
....*....|
gi 2129675820 951 THGKVDRQAL 960
Cdd:TIGR01923 427 ASGKILRNQL 436
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
492-961 |
2.15e-39 |
|
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: 152.45 E-value: 2.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 492 TYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTqqr 571
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 572 lvdkfvehktqiicldrdlpenatlsidnpvsnvtseNLAYIIYTSGSTGKPKGTMIPHRglvNYLSWctnAYALAQGYG 651
Cdd:cd05934 82 -------------------------------------DPASILYTSGTTGPPKGVVITHA---NLTFA---GYYSARRFG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 652 APVQSSIG-----F--DATITSLFSPLLVGKRVVLLPEKeeieALSALLQSDQNY--SLVKITPAHLEMLNQMLPNHKGV 722
Cdd:cd05934 119 LGEDDVYLtvlplFhiNAQAVSVLAALSVGATLVLLPRF----SASRFWSDVRRYgaTVTNYLGAMLSYLLAQPPSPDDR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 723 TETRALIIGGEALLGkslnFWRD--NAPKTRIINEYGPTETVVgCCVYEVDEQTslsGAILIGRPIANTQLYLLDDKQKL 800
Cdd:cd05934 195 AHRLRAAYGAPNPPE----LHEEfeERFGVRLLEGYGMTETIV-GVIGPRDEPR---RPGSIGRPAPGYEVRIVDDDGQE 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 801 VPIGVPGELYI---GGAGVARGYLNRPELTQQRFiPNPFsdepnsrlYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIE 877
Cdd:cd05934 267 LPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM-RNGW--------FHTGDLGYRDADGFFYFVDRKKDMIRRRGENIS 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 878 LEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTS-SELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVD 956
Cdd:cd05934 338 SAEVERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVA 417
|
....*
gi 2129675820 957 RQALP 961
Cdd:cd05934 418 KAQLR 422
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
464-960 |
4.27e-39 |
|
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: 152.87 E-value: 4.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 464 DKCLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKP--EVLVGI--CVErsldMLIGILGILKAG 539
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPgdRVVVQLpnVAE----FVVLFFALLRLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 540 GAYIPFDPTYPQERLGFMLEDAQiPILLTQQRLVDKFvEHKTQIICLDRDLPEnatlsidnpvsnvtsenLAYIIYTSGS 619
Cdd:cd05920 90 AVPVLALPSHRRSELSAFCAHAE-AVAYIVPDRHAGF-DHRALARELAESIPE-----------------VALFLLSGGT 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 620 TGKPKgtMIP--HRGLVNYLSWCTNAYALAQG--YGAPVQSSIGFDATITSLFSPLLVGKRVVLLPEKEEIEALsALLQS 695
Cdd:cd05920 151 TGTPK--LIPrtHNDYAYNVRASAEVCGLDQDtvYLAVLPAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAF-PLIER 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 696 DQnYSLVKITPAHLEM-LNQMLPNHKGVTETRALIIGGEALlgkslnfwrDNAPKTRIINEYGPT-ETVVG-----CCVY 768
Cdd:cd05920 228 EG-VTVTALVPALVSLwLDAAASRRADLSSLRLLQVGGARL---------SPALARRVPPVLGCTlQQVFGmaeglLNYT 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 769 EVDEqtslSGAILI---GRPI-ANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrl 844
Cdd:cd05920 298 RLDD----PDEVIIhtqGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------- 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 845 YKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSEL 924
Cdd:cd05920 366 YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAAQL 445
|
490 500 510
....*....|....*....|....*....|....*..
gi 2129675820 925 RQFL-QSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05920 446 RRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
474-962 |
7.07e-39 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 152.42 E-value: 7.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 474 QVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGiLKAGGAYIPFDPT-YPQE 552
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHA-LQQLGAVAVLLNTrLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 553 RLGFMLEDAQIPILLTQQRLVDKFVEHKTQIIcldRDLPENATLSIDnPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRg 632
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKLIPGISVKF---AELMNGPKEEAE-IQEEFDLDEVATIMYTSGTTGKPKGVIQTYG- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 633 lvNYLsWCTNAYALAQGYGA--------PVQSSIGFDAtitsLFSPLLVGKRVVLLpEKEEIEALSALLQSDQnYSLVKI 704
Cdd:PRK03640 165 --NHW-WSAVGSALNLGLTEddcwlaavPIFHISGLSI----LMRSVIYGMRVVLV-EKFDAEKINKLLQTGG-VTIISV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 705 TPAHLEMLNQMLPNHKGVTETRALIIGG----EALLGKSLnfwRDNAPktrIINEYGPTETVVGCCVYEVDE-QTSLSGA 779
Cdd:PRK03640 236 VSTMLQRLLERLGEGTYPSSFRCMLLGGgpapKPLLEQCK---EKGIP---VYQSYGMTETASQIVTLSPEDaLTKLGSA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 780 iliGRPIANTQLYLLDDKQKLVPiGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlyKTGDLArYL-PDGN 858
Cdd:PRK03640 310 ---GKPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQDGWF---------KTGDIG-YLdEEGF 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 859 IEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVpKEQAPTSSELRQFLQSKLPEYMIP 938
Cdd:PRK03640 376 LYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV-KSGEVTEEELRHFCEEKLAKYKVP 454
|
490 500
....*....|....*....|....
gi 2129675820 939 SAFVMLEVIPLTTHGKVDRQALPQ 962
Cdd:PRK03640 455 KRFYFVEELPRNASGKLLRHELKQ 478
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
491-960 |
2.15e-38 |
|
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: 149.79 E-value: 2.15e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 491 LTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTqq 570
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 571 rlvdkfvehktqiicldrdlpenatlsidnpvsnvTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLS------------ 638
Cdd:cd05972 79 -----------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPtaaywlglrpdd 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 639 --WCTNAYALAQGygapvqssigfdaTITSLFSPLLVGKRVVLLpEKEEIEALSAL-LQSDQNYSLVKITPAHLEMLNQM 715
Cdd:cd05972 124 ihWNIADPGWAKG-------------AWSSFFGPWLLGATVFVY-EGPRFDAERILeLLERYGVTSFCGPPTAYRMLIKQ 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 716 LPNHKGVTETRALIIGGEALLGKSLNFWRDnAPKTRIINEYGPTETVVGCCVYEVDEQTSLSgailIGRPIANTQLYLLD 795
Cdd:cd05972 190 DLSSYKFSHLRLVVSAGEPLNPEVIEWWRA-ATGLPIRDGYGQTETGLTVGNFPDMPVKPGS----MGRPTPGYDVAIID 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 796 DKQKLVPIGVPGELYI--GGAGVARGYLNRPELTQQRFIPNpfsdepnsrLYKTGDLARYLPDGNIEYLGRIDHQVKIRG 873
Cdd:cd05972 265 DDGRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD---------YYLTGDRAYRDEDGYFWFVGRADDIIKSSG 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 874 FRIELEEIESLLAQHPLVNAVTVIAREDqPGDKRLV-GYIVPKEQAPTS----SELRQFLQSKLPEYMIPSAFVMLEVIP 948
Cdd:cd05972 336 YRIGPFEVESALLEHPAVAEAAVVGSPD-PVRGEVVkAFVVLTSGYEPSeelaEELQGHVKKVLAPYKYPREIEFVEELP 414
|
490
....*....|..
gi 2129675820 949 LTTHGKVDRQAL 960
Cdd:cd05972 415 KTISGKIRRVEL 426
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
464-960 |
2.74e-38 |
|
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: 151.45 E-value: 2.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 464 DKCLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPE--VLV--GICVErsldMLIGILGILKAG 539
Cdd:COG1021 24 GETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGdrVVVqlPNVAE----FVIVFFALFRAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 540 G------------------------AYIpfdptYPQERLGF----MLED--AQIPILltQQRLV----DKFVEhktqiic 585
Cdd:COG1021 100 AipvfalpahrraeishfaeqseavAYI-----IPDRHRGFdyraLARElqAEVPSL--RHVLVvgdaGEFTS------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 586 LDRDLPENATLSIDNPvsnvTSENLAYIIYTSGSTGKPKgtMIP--HRGLVnYLSWCTNAY-----------ALAQGYGA 652
Cdd:COG1021 166 LDALLAAPADLSEPRP----DPDDVAFFQLSGGTTGLPK--LIPrtHDDYL-YSVRASAEIcgldadtvylaALPAAHNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 653 PVqSSIGFdatitslFSPLLVGKRVVLLP-----------EKEEIEALSallqsdqnysLVkitPAHLEMLNQMLPNHKG 721
Cdd:COG1021 239 PL-SSPGV-------LGVLYAGGTVVLAPdpspdtafpliERERVTVTA----------LV---PPLALLWLDAAERSRY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 722 VTET-RALIIGG-----------EALLGKSL-----------NFwrdnapkTRIineYGPTETVVGCCvyevdeqtslsg 778
Cdd:COG1021 298 DLSSlRVLQVGGaklspelarrvRPALGCTLqqvfgmaeglvNY-------TRL---DDPEEVILTTQ------------ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 779 ailiGRPI-ANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARYLPDG 857
Cdd:COG1021 356 ----GRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF--------YRTGDLVRRTPDG 423
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 858 NIEYLGRIDHQVkIR-GFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSELRQFLQSK-LPEY 935
Cdd:COG1021 424 YLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSCAFVVPRGEPLTLAELRRFLRERgLAAF 502
|
570 580
....*....|....*....|....*
gi 2129675820 936 MIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:COG1021 503 KLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
490-955 |
2.10e-37 |
|
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: 146.76 E-value: 2.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQ 569
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 570 QRlvdkFVEHKTQiicldrDLPENatlsidnpvsnvtsenLAYIIYTSGSTGKPKGTMIPHRGLVnylswcTNAYALAQG 649
Cdd:cd05903 81 ER----FRQFDPA------AMPDA----------------VALLLFTSGTTGEPKGVMHSHNTLS------ASIRQYAER 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 650 YG----------APVQSSIGFdatITSLFSPLLVGKRVVLLPEKEEIEALsALLQSDQNYSLVKITPAHLEMLNQMLPNH 719
Cdd:cd05903 129 LGlgpgdvflvaSPMAHQTGF---VYGFTLPLLLGAPVVLQDIWDPDKAL-ALMREHGVTFMMGATPFLTDLLNAVEEAG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 720 KGVTETRALIIGGeALLGKSLNFWRDNAPKTRIINEYGPTEtvvgCCVYEVDEQTSLSGAILI--GRPIANTQLYLLDDK 797
Cdd:cd05903 205 EPLSRLRTFVCGG-ATVPRSLARRAAELLGAKVCSAYGSTE----CPGAVTSITPAPEDRRLYtdGRPLPGVEIKVVDDT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 798 QKLVPIGVPGELYIGGAGVARGYLNRPELTqqrfipnpfSDEPNSRLYKTGDLARYLPDGNIEYLGRiDHQVKIR-GFRI 876
Cdd:cd05903 280 GATLAPGVEGELLSRGPSVFLGYLDRPDLT---------ADAAPEGWFRTGDLARLDEDGYLRITGR-SKDIIIRgGENI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 877 ELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQA-PTSSELRQFLQSK-LPEYMIPSAFVMLEVIPLTTHGK 954
Cdd:cd05903 350 PVLEVEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGAlLTFDELVAYLDRQgVAKQYWPERLVHVDDLPRTPSGK 429
|
.
gi 2129675820 955 V 955
Cdd:cd05903 430 V 430
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
610-960 |
6.40e-37 |
|
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: 142.47 E-value: 6.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 610 LAYIIYTSGSTGKPKGTMIPHRglvnylswctNAYALAQGygapVQSSIGFDATITSLFS-PL-------------LVGK 675
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAA----------NLLASAAG----LHSRLGFGGGDSWLLSlPLyhvgglailvrslLAGA 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 676 RVVLlPEKEEIEALSALLQSDQNYSLVkitPAHLEMLnqmLPNHKG---VTETRALIIGGEALlgkslnfWRD--NAPKT 750
Cdd:cd17630 68 ELVL-LERNQALAEDLAPPGVTHVSLV---PTQLQRL---LDSGQGpaaLKSLRAVLLGGAPI-------PPEllERAAD 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 751 RIIN---EYGPTETVVGCCVYEVDEqtslSGAILIGRPIANTQLYLLDDkqklvpigvpGELYIGGAGVARGYLNRPelt 827
Cdd:cd17630 134 RGIPlytTYGMTETASQVATKRPDG----FGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ--- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 828 qqrfIPNPFSDEPnsrLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKR 907
Cdd:cd17630 197 ----LVPEFNEDG---WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQR 269
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2129675820 908 LVGYIVPKEQAPTsSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd17630 270 PVAVIVGRGPADP-AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
491-960 |
6.72e-36 |
|
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: 142.64 E-value: 6.72e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 491 LTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQ 570
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 571 RLVDKfvehktqiicldrdlpenatlsidnpvsnVTSENLAYIIYTSGSTGKPKGTMIPHRGLVNY-------------- 636
Cdd:cd05969 81 ELYER-----------------------------TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYyftgkyvldlhpdd 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 637 LSWCTNAYALAQGygapvqssigfdaTITSLFSPLLVGKRVVLLPEKEEIEALSALLQsDQNYSLVKITPAHLEML---- 712
Cdd:cd05969 132 IYWCTADPGWVTG-------------TVYGIWAPWLNGVTNVVYEGRFDAESWYGIIE-RVKVTVWYTAPTAIRMLmkeg 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 713 NQMLPNHKgVTETRALIIGGEALLGKSLNfWRDNAPKTRIINEYGPTETvvgccvyevdeqtslsGAILI---------- 782
Cdd:cd05969 198 DELARKYD-LSSLRFIHSVGEPLNPEAIR-WGMEVFGVPIHDTWWQTET----------------GSIMIanypcmpikp 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 783 ---GRPIANTQLYLLDDKQKLVPIGVPGELYI--GGAGVARGYLNRPELTQQRFIpnpfsdepnSRLYKTGDLARYLPDG 857
Cdd:cd05969 260 gsmGKPLPGVKAAVVDENGNELPPGTKGILALkpGWPSMFRGIWNDEERYKNSFI---------DGWYLTGDLAYRDEDG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 858 NIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSELRQ----FLQSKLP 933
Cdd:cd05969 331 YFWFVGRADDIIKTSGHRVGPFEVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELKEeiinFVRQKLG 410
|
490 500
....*....|....*....|....*..
gi 2129675820 934 EYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05969 411 AHVAPREIEFVDNLPKTRSGKIMRRVL 437
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
492-960 |
1.16e-35 |
|
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: 143.54 E-value: 1.16e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 492 TYAQLNAKSNQLAHHLQKLGVKPEVLVG-ICVE--RSLDMLIGILGIlkaGGAYIPFDPTYPQERLGFMLEDAQIPILLT 568
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVAtLAWNthRHLELYYAVPGM---GAVLHTINPRLFPEQIAYIINHAEDRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 569 Q---QRLVDKFVEHKTQI---ICLDRDLPENAT-----------LSIDNPVSNVTS--ENLAYII-YTSGSTGKPKGTMI 628
Cdd:cd12119 104 DrdfLPLLEAIAPRLPTVehvVVMTDDAAMPEPagvgvlayeelLAAESPEYDWPDfdENTAAAIcYTSGTTGNPKGVVY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 629 PHRGLVnylswcTNAYALAQGYGAPVQSSigfDAT--ITSLF---------SPLLVGKRVVLLPEKEEIEALSALLQSDq 697
Cdd:cd12119 184 SHRSLV------LHAMAALLTDGLGLSES---DVVlpVVPMFhvnawglpyAAAMVGAKLVLPGPYLDPASLAELIERE- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 698 nyslvKITPAH------LEMLNQMLPNHKGVTETRALIIGGEALlGKSL-NFWRDNApkTRIINEYGPTETV-VGCCVYE 769
Cdd:cd12119 254 -----GVTFAAgvptvwQGLLDHLEANGRDLSSLRRVVIGGSAV-PRSLiEAFEERG--VRVIHAWGMTETSpLGTVARP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 770 VDEQTSLSGA------ILIGRPIANTQLYLLDDKQKLVPI-GVP-GELYIGGAGVARGYLNRPELTQQRFiPNPFsdepn 841
Cdd:cd12119 326 PSEHSNLSEDeqlalrAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEALT-EDGW----- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 842 srlYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKE-QAPT 920
Cdd:cd12119 400 ---LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEgATVT 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 2129675820 921 SSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd12119 477 AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
1071-1330 |
9.75e-35 |
|
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: 132.90 E-value: 9.75e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1071 PFFCLPGGGGNVLYLHELARDLGSEQTFYGLQAPGLNGESDPLTSVEEMAAYYIQAIQSVQPEGPYFLGGHSFGGIVAYE 1150
Cdd:pfam00975 2 PLFCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAFE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1151 IAQQLVKSGHEVALVAILDAPAPvasdkpiYIDVDDATRLTETARLIErwagkslnisyEILQPLELDAQLEYLKEQLIa 1230
Cdd:pfam00975 82 VARRLERQGEAVRSLFLSDASAP-------HTVRYEASRAPDDDEVVA-----------EFTDEGGTPEELLEDEELLS- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1231 vGLLPTgtetkqVRGLVQVFETnlqasikyspqevYPHRLTLLRAREVNAEDAALLTELRQDPAWGWgQFSTEKVDIHIV 1310
Cdd:pfam00975 143 -MLLPA------LRADYRALES-------------YSCPPLDAQSATLFYGSDDPLHDADDLAEWVR-DHTPGEFDVHVF 201
|
250 260
....*....|....*....|..
gi 2129675820 1311 PGDHMTMMTQP--HISSVAKQL 1330
Cdd:pfam00975 202 DGDHFYLIEHLeaVLEIIEAKL 223
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
473-967 |
7.06e-34 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 137.68 E-value: 7.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 473 AQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQ-KLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQ 551
Cdd:PRK06839 10 KRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 552 ERLGFMLEDAQIPILLTQQRLVDKfVEHKTQIICLDR-----DLPENATLSIDNPVSNvtSENLAYII-YTSGSTGKPKG 625
Cdd:PRK06839 90 NELIFQLKDSGTTVLFVEKTFQNM-ALSMQKVSYVQRvisitSLKEIEDRKIDNFVEK--NESASFIIcYTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 626 TMIPHRGLvnYLSWCTNAYALaqgygapvqSSIGFDATITSL------------FSPLLVGKRVVLlPEKEEIEALSALL 693
Cdd:PRK06839 167 AVLTQENM--FWNALNNTFAI---------DLTMHDRSIVLLplfhiggiglfaFPTLFAGGVIIV-PRKFEPTKALSMI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 694 QSDQNYSLVKITPAHLEMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNApkTRIINEYGPTETvvGCCVYEVDEQ 773
Cdd:PRK06839 235 EKHKVTVVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRG--FLFGQGFGMTET--SPTVFMLSEE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 774 TSLSGAILIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFipnpfsdePNSRLYkTGDLARY 853
Cdd:PRK06839 311 DARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI--------QDGWLC-TGDLARV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 854 LPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAP-TSSELRQFLQSKL 932
Cdd:PRK06839 382 DEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVlIEKDVIEHCRLFL 461
|
490 500 510
....*....|....*....|....*....|....*
gi 2129675820 933 PEYMIPSAFVMLEVIPLTTHGKVDRQALPQPDTSR 967
Cdd:PRK06839 462 AKYKIPKEIVFLKELPKNATGKIQKAQLVNQLKSR 496
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
467-931 |
1.42e-33 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 138.31 E-value: 1.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNH----ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAY 542
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 543 IPFDPTYPQERLGFMLEDAQIPILLTQ-QRLVDKFVEHKTQ------IICLD----RDLPENATLS-------------- 597
Cdd:COG1022 93 VPIYPTSSAEEVAYILNDSGAKVLFVEdQEQLDKLLEVRDElpslrhIVVLDprglRDDPRLLSLDellalgrevadpae 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 598 IDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLV----------------NYLSW---------CTNAYALAQGYga 652
Cdd:COG1022 173 LEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLsnarallerlplgpgdRTLSFlplahvferTVSYYALAAGA-- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 653 pvqsSIGFDATITSL------FSP--LLVGKRVVllpEK------EEIEALSALLQS--------DQNYSLVKIT----P 706
Cdd:COG1022 251 ----TVAFAESPDTLaedlreVKPtfMLAVPRVW---EKvyagiqAKAEEAGGLKRKlfrwalavGRRYARARLAgkspS 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 707 AHLEMLNQMLpnHKGV---------TETRALIIGGEAlLGKSLNFWRDNA--PktrIINEYGPTETVVGCCVYEVDEQ-- 773
Cdd:COG1022 324 LLLRLKHALA--DKLVfsklrealgGRLRFAVSGGAA-LGPELARFFRALgiP---VLEGYGLTETSPVITVNRPGDNri 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 774 -TslsgailIGRPIANTQlyllddkqklVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLAR 852
Cdd:COG1022 398 gT-------VGPPLPGVE----------VKIAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW--------LHTGDIGE 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 853 YLPDGNIEYLGRIDHQVKIR-GFRIELEEIESLLAQHPLVNAVTVIaredqpGDKR--LVGYIVPKEQAptsseLRQFLQ 929
Cdd:COG1022 453 LDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV------GDGRpfLAALIVPDFEA-----LGEWAE 521
|
..
gi 2129675820 930 SK 931
Cdd:COG1022 522 EN 523
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
8-432 |
1.67e-33 |
|
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar domains including the C-domain of SgcC5, a free-standing NRPS with both ester- and amide- bond forming activity; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as 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. Streptomyces globisporus 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. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380454 [Multi-domain] Cd Length: 427 Bit Score: 135.18 E-value: 1.67e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 8 SPQQKHLW-LQQ--KDNYqAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGmnIPFQSISDAPTynhISL 84
Cdd:cd19531 5 SFAQQRLWfLDQlePGSA-AYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDG--EPVQVILPPLP---LPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 85 AEYDWSRLSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACL 164
Cdd:cd19531 79 PVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 165 DGEEIS--EEVMQYADVSEWLNELLESEDTETARNYWQQQ--DISSVLNLriPFeiknDHQSSGEISFAPQSLCLAMNRD 240
Cdd:cd19531 159 AGRPSPlpPLPIQYADYAVWQREWLQGEVLERQLAYWREQlaGAPPVLEL--PT----DRPRPAVQSFRGARVRFTLPAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 241 TVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLL--TkyLPIHSRLEDALKFSELM 318
Cdd:cd19531 233 LTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFvnT--LVLRTDLSGDPTFRELL 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 319 ERVSESLR----------------------------FvkkwQEYFNWENFISTNEKFaarpffpfcfdftqqsqsyvnGN 370
Cdd:cd19531 311 ARVRETALeayahqdlpfeklvealqperdlsrsplF----QVMFVLQNAPAAALEL---------------------PG 365
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2129675820 371 IAFSEYKKSANIDKFQIKLSSGYSQDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNP 432
Cdd:cd19531 366 LTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
490-960 |
3.79e-33 |
|
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: 134.14 E-value: 3.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQ 569
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 570 QRLvdkfvehktqiicldrdlpenatlsidnpvsnvtsENLAYIIYTSGSTGKPKGTMIPHRGLVnylswcTNAYALAQG 649
Cdd:cd05935 81 SEL-----------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAA------ANALQSAVW 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 650 YGA----------PVQSSIGFdatITSLFSPLLVGKRVVLLPEKEEiEALSALLQSDQNYSLVKITPAHLEMLNQMLPNH 719
Cdd:cd05935 120 TGLtpsdvilaclPLFHVTGF---VGSLNTAVYVGGTYVLMARWDR-ETALELIEKYKVTFWTNIPTMLVDLLATPEFKT 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 720 KGVTETRALIIGGEAL---LGKSLnfwRDNApKTRIINEYGPTETvvgCCVYEVDEQTSLSGAILiGRPIANTQLYLLD- 795
Cdd:cd05935 196 RDLSSLKVLTGGGAPMppaVAEKL---LKLT-GLRFVEGYGLTET---MSQTHTNPPLRPKLQCL-GIP*FGVDARVIDi 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 796 DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIpnpfsDEPNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFR 875
Cdd:cd05935 268 ETGRELPPNEVGEIVVRGPQIFKGYWNRPEETEESFI-----EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 876 IELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAP---TSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTH 952
Cdd:cd05935 343 VWPAEVEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRgkvTEEDIIEWAREQMAAYKYPREVEFVDELPRSAS 422
|
....*...
gi 2129675820 953 GKVDRQAL 960
Cdd:cd05935 423 GKILWRLL 430
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
490-918 |
9.80e-33 |
|
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: 133.49 E-value: 9.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILltq 569
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKAL--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 570 qrlvdkFVEhktqiicldrdlpenatlsidnpvsnvTSENLAYIIYTSGSTGKPKGTMIPHRglvnylSWCTNAYALAQG 649
Cdd:cd05907 82 ------FVE---------------------------DPDDLATIIYTSGTTGRPKGVMLSHR------NILSNALALAER 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 650 YGA-PVQSSIGF------DATITSLFSPLLVGKRVVLLPEkeeIEALSALLQSdqnyslVKIT-----PAHLEMLnQMLP 717
Cdd:cd05907 123 LPAtEGDRHLSFlplahvFERRAGLYVPLLAGARIYFASS---AETLLDDLSE------VRPTvflavPRVWEKV-YAAI 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 718 NHKGVTE-------------TRALIIGGEALLGKSLNFWR-DNAPktrIINEYGPTETVVGCCVYEVDEQTSLSgailIG 783
Cdd:cd05907 193 KVKAVPGlkrklfdlavggrLRFAASGGAPLPAELLHFFRaLGIP---VYEGYGLTETSAVVTLNPPGDNRIGT----VG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 784 RPIANTQLYLLDDkqklvpigvpGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARYLPDGNIEYLG 863
Cdd:cd05907 266 KPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW--------LHTGDLGEIDEDGFLHITG 327
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2129675820 864 RI-DHQVKIRGFRIELEEIESLLAQHPLVNAVTVIaredqpGDKR--LVGYIVPKEQA 918
Cdd:cd05907 328 RKkDLIITSGGKNISPEPIENALKASPLISQAVVI------GDGRpfLVALIVPDPEA 379
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
463-960 |
1.11e-32 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 134.80 E-value: 1.11e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 463 HDKCLHELFAAQVERTPNNIAV-EFNHES-----LTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGIL 536
Cdd:PRK13295 22 HDRTINDDLDACVASCPDKTAVtAVRLGTgaprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACS 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 537 KAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQRLVDkfVEHKTQIICLDRDLPE------------------------ 592
Cdd:PRK13295 102 RIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRG--FDHAAMARRLRPELPAlrhvvvvggdgadsfeallitpaw 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 593 ------NATLSIDNPVSNvtseNLAYIIYTSGSTGKPKGTMIPHRGLV-NYLswctnAYALAQGYGA--------PVQSS 657
Cdd:PRK13295 180 eqepdaPAILARLRPGPD----DVTQLIYTSGTTGEPKGVMHTANTLMaNIV-----PYAERLGLGAddvilmasPMAHQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 658 IGFdatITSLFSPLLVGKRVVLLPEKEEIEALsALLQSDQ-NYSLVKiTPAHLEMLNQMLPNHKGVTETRALIIGGEALL 736
Cdd:PRK13295 251 TGF---MYGLMMPVMLGATAVLQDIWDPARAA-ELIRTEGvTFTMAS-TPFLTDLTRAVKESGRPVSSLRTFLCAGAPIP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 737 GkSLNFWRDNAPKTRIINEYGPTET--VVGCCVYEVDEQTSLSGailiGRPIANTQLYLLDDKQKLVPIGVPGELYIGGA 814
Cdd:PRK13295 326 G-ALVERARAALGAKIVSAWGMTENgaVTLTKLDDPDERASTTD----GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 815 GVARGYLNRPELTqqrfipnpfSDEPNSrLYKTGDLARYLPDGNIEYLGRiDHQVKIRGFR-IELEEIESLLAQHPLVNA 893
Cdd:PRK13295 401 SNFGGYLKRPQLN---------GTDADG-WFDTGDLARIDADGYIRISGR-SKDVIIRGGEnIPVVEIEALLYRHPAIAQ 469
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2129675820 894 VTVIAREDQPGDKRLVGYIVPKE-QAPTSSELRQFLQS-KLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK13295 470 VAIVAYPDERLGERACAFVVPRPgQSLDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
488-960 |
1.16e-32 |
|
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: 132.99 E-value: 1.16e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 488 HESLTYAQLNAKSNQLAHHLQ-KLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPIL 566
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 567 LTQQRLVdkfvehktqiicldrdlpenatlsidnpvsnvTSENLAYIIYTSGSTGKPKGTMIPHRGLVnylswctnayAL 646
Cdd:cd05958 88 LCAHALT--------------------------------ASDDICILAFTSGTTGAPKATMHFHRDPL----------AS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 647 AQGYG---------------APVQSSIGFDATitsLFSPLLVGKRVVLLPEKEEIEALSALLQSDQNYsLVKITPAHLEM 711
Cdd:cd05958 126 ADRYAvnvlrlreddrfvgsPPLAFTFGLGGV---LLFPFGVGASGVLLEEATPDLLLSAIARYKPTV-LFTAPTAYRAM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 712 LNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDnAPKTRIINEYGPTEtvvgccVYEV----DEQTSLSGAIliGRPIA 787
Cdd:cd05958 202 LAHPDAAGPDLSSLRKCVSAGEALPAALHRAWKE-ATGIPIIDGIGSTE------MFHIfisaRPGDARPGAT--GKPVP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 788 NTQLYLLDDKQKLVPIGVPGELYIGGAGVARgYLNRPeltQQRfipNPFSDEPNSrlykTGDLARYLPDGNIEYLGRIDH 867
Cdd:cd05958 273 GYEAKVVDDEGNPVPDGTIGRLAVRGPTGCR-YLADK---RQR---TYVQGGWNI----TGDTYSRDPDGYFRHQGRSDD 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 868 QVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPK-EQAPTS---SELRQFLQSKLPEYMIPSAFVM 943
Cdd:cd05958 342 MIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpGVIPGPvlaRELQDHAKAHIAPYKYPRAIEF 421
|
490
....*....|....*..
gi 2129675820 944 LEVIPLTTHGKVDRQAL 960
Cdd:cd05958 422 VTELPRTATGKLQRFAL 438
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
490-956 |
1.32e-32 |
|
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: 133.61 E-value: 1.32e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKlGVKPEVLVGICVERSLDMLIGILGILKAGgaYIPFDPTYPQ--ERLGFMLEDAQIPILL 567
Cdd:cd05909 7 SLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAglRELRACIKLAGIKTVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 568 TQQRLVDKFVEHKT-------QIICLDrDLPENATLS-----------------IDNPVSNVTSENLAYIIYTSGSTGKP 623
Cdd:cd05909 84 TSKQFIEKLKLHHLfdveydaRIVYLE-DLRAKISKAdkckaflagkfppkwllRIFGVAPVQPDDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 624 KGTMIPHRGLVnylswcTNAYALAQGYGA----------PVQSSIGFDATitsLFSPLLVGKRVVLLPEKEEIEALSALL 693
Cdd:cd05909 163 KGVVLSHKNLL------ANVEQITAIFDPnpedvvfgalPFFHSFGLTGC---LWLPLLSGIKVVFHPNPLDYKKIPELI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 694 QsDQNYSLVKITPAhleMLNQMLPN-HKGVTET-RALIIGGEALLGKSLNFWRDNAPKtRIINEYGPTET--VVGCCVYE 769
Cdd:cd05909 234 Y-DKKATILLGTPT---FLRGYARAaHPEDFSSlRLVVAGAEKLKDTLRQEFQEKFGI-RILEGYGTTECspVISVNTPQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 770 VDEQTSlsgaiLIGRPIANTQLYLLD-DKQKLVPIGVPGELYIGGAGVARGYLNRPELTqqrfipnpfSDEPNSRLYKTG 848
Cdd:cd05909 309 SPNKEG-----TVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELT---------SFAFGDGWYDTG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 849 DLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQH-PLVNAVTVIARED-QPGDKRLVGYIvpkEQAPTSSELRQ 926
Cdd:cd05909 375 DIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEIlPEDNEVAVVSVPDgRKGEKIVLLTT---TTDTDPSSLND 451
|
490 500 510
....*....|....*....|....*....|.
gi 2129675820 927 FLQ-SKLPEYMIPSAFVMLEVIPLTTHGKVD 956
Cdd:cd05909 452 ILKnAGISNLAKPSYIHQVEEIPLLGTGKPD 482
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
470-956 |
7.46e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 132.32 E-value: 7.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 470 LFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTY 549
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 550 PQERLGFMLEDAQIPILLTQQRLVDKFVEhktqiiCLDRdLPENATL-SIDNPVSN------VTSENLA----------- 611
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYEREFAPRVAE------VLPR-LPKLRTLvVVEDGSGNdllpgaVDYEDALaagsperdfge 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 612 ------YIIYTSGSTGKPKGTMIPH----RGLVNYLSWCT-----NAYALAQGyGAPVQSSIGFD-------ATITSLFS 669
Cdd:PRK07798 161 rspddlYLLYTGGTTGMPKGVMWRQedifRVLLGGRDFATgepieDEEELAKR-AAAGPGMRRFPapplmhgAGQWAAFA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 670 PLLVGKRVVLLPeKEEIEALSALLQSDQN-YSLVKIT------PahleMLNQMLPNHKGVTETRALIIGGEALLGKSL-N 741
Cdd:PRK07798 240 ALFSGQTVVLLP-DVRFDADEVWRTIEREkVNVITIVgdamarP----LLDALEARGPYDLSSLFAIASGGALFSPSVkE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 742 FWRDNAPKTRIINEYGPTETVVGCCVyevdeqTSLSGAILIGRP---IANTQLYLLDDKQKLVP-IGVPGELYIGGAgVA 817
Cdd:PRK07798 315 ALLELLPNVVLTDSIGSSETGFGGSG------TVAKGAVHTGGPrftIGPRTVVLDEDGNPVEPgSGEIGWIARRGH-IP 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 818 RGYLNRPELTQQRFIpnpfsdEPNSRLYK-TGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTV 896
Cdd:PRK07798 388 LGYYKDPEKTAETFP------TIDGVRYAiPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALV 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2129675820 897 IAREDQPGDKRLVGYIVPKEQA-PTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVD 956
Cdd:PRK07798 462 VGVPDERWGQEVVAVVQLREGArPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
475-959 |
9.54e-32 |
|
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: 131.98 E-value: 9.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 475 VERTPNNIAVEFNH------ESLTYAQLNAKSNQLAHHLQKLGVKPEVlVGICVERSLDMLIGILGILKAGGAYIP-FDP 547
Cdd:cd05931 3 AAARPDRPAYTFLDdeggreETLTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAIAVPlPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 548 TYP--QERLGFMLEDAQIPILLTQQRLVDKFVEHKT------QIICLDRDLPENATLSiDNPVSNVTSENLAYIIYTSGS 619
Cdd:cd05931 82 TPGrhAERLAAILADAGPRVVLTTAAALAAVRAFAAsrpaagTPRLLVVDLLPDTSAA-DWPPPSPDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 620 TGKPKGTMIPHRGLVnylswcTNAYALAQGYGAPVQSSIGF------D-ATITSLFSPLLVGKRVVLL--------PEK- 683
Cdd:cd05931 161 TGTPKGVVVTHRNLL------ANVRQIRRAYGLDPGDVVVSwlplyhDmGLIGGLLTPLYSGGPSVLMspaaflrrPLRw 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 684 -EEIEALSALLQSDQN--YSLV--KITPAHLEMLNqmLPNhkgvteTRALIIGGEALLGKSLN-----FWRDNAPKTRII 753
Cdd:cd05931 235 lRLISRYRATISAAPNfaYDLCvrRVRDEDLEGLD--LSS------WRVALNGAEPVRPATLRrfaeaFAPFGFRPEAFR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 754 NEYGPTETVV---------GCCVYEVDEQTSLSGAILI-------------GRPIANTQLYLLD-DKQKLVPIGVPGELY 810
Cdd:cd05931 307 PSYGLAEATLfvsggppgtGPVVLRVDRDALAGRAVAVaaddpaarelvscGRPLPDQEVRIVDpETGRELPDGEVGEIW 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 811 IGGAGVARGYLNRPELTQQRFipNPFSDEPNSRLYKTGDLArYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPL 890
Cdd:cd05931 387 VRGPSVASGYWGRPEATAETF--GALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 891 V---NAVTVIAREDQPGDKRLV-----GYIVPKEQAPTSSELRQFLQSklpEY-MIPSAFVMLE--VIPLTTHGKVDRQA 959
Cdd:cd05931 464 AlrpGCVAAFSVPDDGEERLVVvaeveRGADPADLAAIAAAIRAAVAR---EHgVAPADVVLVRpgSIPRTSSGKIQRRA 540
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
476-962 |
1.10e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 131.05 E-value: 1.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 476 ERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVlVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLG 555
Cdd:PRK07638 12 SLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 556 FMLEDAQIPILLTQQRLVDKFVEHKTQIICLDRdlpENATLSIDNPV-SNVTSENLA--YIIYTSGSTGKPKGTMIPHRg 632
Cdd:PRK07638 91 ERLAISNADMIVTERYKLNDLPDEEGRVIEIDE---WKRMIEKYLPTyAPIENVQNApfYMGFTSGSTGKPKAFLRAQQ- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 633 lvnylSWCTNAYALAQGYGAPVQSSIGFDATI-TSLF-----SPLLVGKRVVLLPEKEEIEALSALLQsdQNYSLVKITP 706
Cdd:PRK07638 167 -----SWLHSFDCNVHDFHMKREDSVLIAGTLvHSLFlygaiSTLYVGQTVHLMRKFIPNQVLDKLET--ENISVMYTVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 707 AHLEMLNQMlpnhKGVTETRALIIGGEALLGK-SLNFWRDNAPKTRIINEYGPTEtvVGCCVYEVDEQtSLSGAILIGRP 785
Cdd:PRK07638 240 TMLESLYKE----NRVIENKMKIISSGAKWEAeAKEKIKNIFPYAKLYEFYGASE--LSFVTALVDEE-SERRPNSVGRP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 786 IANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQqrfipnpfsdEPNSRLYKT-GDLARYLPDGNIEYLGR 864
Cdd:PRK07638 313 FHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLAR----------ELNADGWMTvRDVGYEDEEGFIYIVGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 865 IDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIvpkEQAPTSSELRQFLQSKLPEYMIPSAFVML 944
Cdd:PRK07638 383 EKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII---KGSATKQQLKSFCLQRLSSFKIPKEWHFV 459
|
490
....*....|....*...
gi 2129675820 945 EVIPLTTHGKVDRQALPQ 962
Cdd:PRK07638 460 DEIPYTNSGKIARMEAKS 477
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
491-960 |
3.10e-31 |
|
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: 128.40 E-value: 3.10e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 491 LTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIP----FDPTYPQERLGfmLEDAQIPIL 566
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPlftaFGPKAIEHRLR--TSGARLVVT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 567 LTQQRlvdkfveHKtqiicLDRDLpenatlsidnpvsnvtsenlAYIIYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYAL 646
Cdd:cd05973 79 DAANR-------HK-----LDSDP--------------------FVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 647 AQG----YGAPVQSSIGFDATITSlfsPLLVGKRVVLLPEKEEIE---------ALSALLQSDQNYSLVKITPAHLEmln 713
Cdd:cd05973 127 RPEdsfwNAADPGWAYGLYYAITG---PLALGHPTILLEGGFSVEstwrvierlGVTNLAGSPTAYRLLMAAGAEVP--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 714 qmlPNHKGvtETRALIIGGEALlGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSLSGAIliGRPIANTQLYL 793
Cdd:cd05973 201 ---ARPKG--RLRRVSSAGEPL-TPEVIRWFDAALGVPIHDHYGQTELGMVLANHHALEHPVHAGSA--GRAMPGWRVAV 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 794 LDDKQKLVPIGVPGELYIGGAGVA----RGYLNRPELTqqrfipnpfsdePNSRLYKTGDLARYLPDGNIEYLGRIDHQV 869
Cdd:cd05973 273 LDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDTPA------------IDGGYYLTGDTVEFDPDGSFSFIGRADDVI 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 870 KIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTS----SELRQFLQSKLPEYMIPSAFVMLE 945
Cdd:cd05973 341 TMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpalaDELQLHVKKRLSAHAYPRTIHFVD 420
|
490
....*....|....*
gi 2129675820 946 VIPLTTHGKVDRQAL 960
Cdd:cd05973 421 ELPKTPSGKIQRFLL 435
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
475-955 |
3.49e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 130.05 E-value: 3.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 475 VERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERL 554
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 555 GFMLEDAQIPILLTQQRLVDKfVEHKTQIICLDR---------DLPENATLSIDN---------PVSNVTSENLAYIIYT 616
Cdd:PRK08316 101 AYILDHSGARAFLVDPALAPT-AEAALALLPVDTlilslvlggREAPGGWLDFADwaeagsvaePDVELADDDLAQILYT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 617 SGSTGKPKGTMIPHRGLV-NYLSwCTnayaLAQGYGA--------PVQSSIGFDAtitsLFSP-LLVGKRVVLLP----- 681
Cdd:PRK08316 180 SGTESLPKGAMLTHRALIaEYVS-CI----VAGDMSAddiplhalPLYHCAQLDV----FLGPyLYVGATNVILDapdpe 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 682 ------EKEEIEALSA-------LLQS---DQN--YSLVK------ITPAhlEMLNQMlpnhkgvtetraliiggeallg 737
Cdd:PRK08316 251 lilrtiEAERITSFFApptvwisLLRHpdfDTRdlSSLRKgyygasIMPV--EVLKEL---------------------- 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 738 kslnfwRDNAPKTRIINEYGPTE-----TVVGccvyeVDEQTSLSGAIliGRPIANTQLYLLDDKQKLVPIGVPGELYIG 812
Cdd:PRK08316 307 ------RERLPGLRFYNCYGQTEiaplaTVLG-----PEEHLRRPGSA--GRPVLNVETRVVDDDGNDVAPGEVGEIVHR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 813 GAGVARGYLNRPELTQQRFIPNPFsdepnsrlyKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVN 892
Cdd:PRK08316 374 SPQLMLGYWDDPEKTAEAFRGGWF---------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVA 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129675820 893 AVTVIAREDQPGDKRLVGYIVPK-EQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKV 955
Cdd:PRK08316 445 EVAVIGLPDPKWIEAVTAVVVPKaGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
472-960 |
3.27e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 126.46 E-value: 3.27e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 472 AAQVERTPNNIA-VEF-NHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTY 549
Cdd:PRK09088 2 AFHARLQPQRLAaVDLaLGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 550 PQERLGFMLEDAQIPILLTQQRLVDKfvehKTQIICLDrDLPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIP 629
Cdd:PRK09088 82 SASELDALLQDAEPRLLLGDDAVAAG----RTDVEDLA-AFIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 630 HRglvnylswctNAYALAQGYG--------------APVQSSIGFdatITSLFSPLLVGKRVVLLPEKEEIEALSALlqS 695
Cdd:PRK09088 157 ER----------NLQQTAHNFGvlgrvdahssflcdAPMFHIIGL---ITSVRPVLAVGGSILVSNGFEPKRTLGRL--G 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 696 DQNyslVKITpaH---LEMLNQMLPNHKGVTETR-----ALIIGGEALLGKSLNFWRDNApkTRIINEYGPTE--TVVGC 765
Cdd:PRK09088 222 DPA---LGIT--HyfcVPQMAQAFRAQPGFDAAAlrhltALFTGGAPHAAEDILGWLDDG--IPMVDGFGMSEagTVFGM 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 766 CVyEVDEQTSLSGAIliGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlY 845
Cdd:PRK09088 295 SV-DCDVIRAKAGAA--GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW--------F 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 846 KTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIARED-QPGDkrlVGY--IVPKEQAPTSS 922
Cdd:PRK09088 364 RTGDIARRDADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADaQWGE---VGYlaIVPADGAPLDL 440
|
490 500 510
....*....|....*....|....*....|....*....
gi 2129675820 923 E-LRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK09088 441 ErIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
487-962 |
1.05e-29 |
|
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: 125.72 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 487 NHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPIL 566
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIV 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 567 LTQQRLVDKFVEHKTQ------IICLD----------------RDLPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPK 624
Cdd:cd17642 121 FCSKKGLQKVLNVQKKlkiiktIIILDskedykgyqclytfitQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 625 GTMIPHRGLVNYLSWCTN-AYALAQGYGAPVQSSIGFDAT--ITSLFSPLLVGKRVVLLPEKEEiealSALLQSDQNYsl 701
Cdd:cd17642 201 GVQLTHKNIVARFSHARDpIFGNQIIPDTAILTVIPFHHGfgMFTTLGYLICGFRVVLMYKFEE----ELFLRSLQDY-- 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 702 vKITPAHL-EMLNQMLPNHKGVTE----TRALIIGGEALLGKSLNFW---RDNAPKTRiiNEYGPTETVVGCCVY-EVDE 772
Cdd:cd17642 275 -KVQSALLvPTLFAFFAKSTLVDKydlsNLHEIASGGAPLSKEVGEAvakRFKLPGIR--QGYGLTETTSAILITpEGDD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 773 QTSLSGAILIGRPIANTQLylldDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLAR 852
Cdd:cd17642 352 KPGAVGKVVPFFYAKVVDL----DTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGW--------LHSGDIAY 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 853 YLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQ-PGDKRLVGYIVPKEQAPTSSELRQFLQSK 931
Cdd:cd17642 420 YDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEdAGELPAAVVVLEAGKTMTEKEVMDYVASQ 499
|
490 500 510
....*....|....*....|....*....|..
gi 2129675820 932 L-PEYMIPSAFVMLEVIPLTTHGKVDRQALPQ 962
Cdd:cd17642 500 VsTAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
459-957 |
1.06e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 126.27 E-value: 1.06e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 459 IEFPhDKCLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKA 538
Cdd:PRK05605 27 LDYG-DTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 539 GGAYIPFDPTYPQERLGFMLED--AQIPILLtqqrlvDKFVEHKTQiicLDRDLPENATLSID----------------- 599
Cdd:PRK05605 106 GAVVVEHNPLYTAHELEHPFEDhgARVAIVW------DKVAPTVER---LRRTTPLETIVSVNmiaampllqrlalrlpi 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 600 -----------NPVSN-----------------------VTSENLAYIIYTSGSTGKPKGTMIPHRGLvnylswCTNAya 645
Cdd:PRK05605 177 palrkaraaltGPAPGtvpwetlvdaaiggdgsdvshprPTPDDVALILYTSGTTGKPKGAQLTHRNL------FANA-- 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 646 lAQG--------------YGA-PVQSSIGFdaTITSLFSPLlVGKRVVLLPEKEEIEALSALLQSDQNYsLVKITPAHLE 710
Cdd:PRK05605 249 -AQGkawvpglgdgpervLAAlPMFHAYGL--TLCLTLAVS-IGGELVLLPAPDIDLILDAMKKHPPTW-LPGVPPLYEK 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 711 MLNQMLPNHKGVTETRALIIGGEALLGKSLNFWrDNAPKTRIINEYGPTET---VVGCCVYEVDEQTSlsgailIGRPIA 787
Cdd:PRK05605 324 IAEAAEERGVDLSGVRNAFSGAMALPVSTVELW-EKLTGGLLVEGYGLTETspiIVGNPMSDDRRPGY------VGVPFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 788 NTQLYLLD--DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNpfsdepnsrLYKTGDLARYLPDGNIEYLGRI 865
Cdd:PRK05605 397 DTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG---------WFRTGDVVVMEEDGFIRIVDRI 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 866 DHQVKIRGFRIELEEIESLLAQHPLVNAVTV--IAREDqpGDKRLVGYIVPKEQAPTSSE-LRQFLQSKLPEYMIPSAFV 942
Cdd:PRK05605 468 KELIITGGFNVYPAEVEEVLREHPGVEDAAVvgLPRED--GSEEVVAAVVLEPGAALDPEgLRAYCREHLTRYKVPRRFY 545
|
570
....*....|....*
gi 2129675820 943 MLEVIPLTTHGKVDR 957
Cdd:PRK05605 546 HVDELPRDQLGKVRR 560
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
7-432 |
1.36e-29 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs), similar to Bacillus subtilis PksJ; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily have the typical C-domain HHxxxD motif. PksJ is involved in some intermediate steps for the synthesis of the antibiotic polyketide bacillaene which is important in secondary metabolism. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380472 [Multi-domain] Cd Length: 430 Bit Score: 123.58 E-value: 1.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 7 ISPQQKHLWLQQK--DNYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGMniPFQSISDAptyNHISL 84
Cdd:cd20484 4 LSEGQKGLWMLQKmsPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGV--PFQKIEPS---KPLSF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 85 AEYDWSRL-SSQV-----QKAKID-TLFQDTSLRVFDFEQATNLHFILgklATDQHILFISLPALYADKTTLNyliceig 157
Cdd:cd20484 79 QEEDISSLkESEIiaylrEKAKEPfVLENGPLMRVHLFSRSEQEHFVL---ITIHHIIFDGSSSLTLIHSLLD------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 158 rAYTACLDGEE--ISEEVMQYADVSEWLNELLESEDTETARNYWQQQDISSVLNLRIPfeikNDHQSSGEISFAPQSLCL 235
Cdd:cd20484 149 -AYQALLQGKQptLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELP----ADRPRSSAPSFEGQTYTR 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 236 AMNRDTVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDALKFS 315
Cdd:cd20484 224 RLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 316 ELMER------------------------VSESLRFVKKWQEYFNWENFISTN--EKFAA--RPFFPFCF-DFTQQSQSY 366
Cdd:cd20484 304 DFIRKlqltvldgldhaaypfpamvrdlnIPRSQANSPVFQVAFFYQNFLQSTslQQFLAeyQDVLSIEFvEGIHQEGEY 383
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2129675820 367 vngNIAFSEYKKsanidkfqiklssgysQDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNP 432
Cdd:cd20484 384 ---ELVLEVYEQ----------------EDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
490-960 |
2.51e-29 |
|
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: 123.88 E-value: 2.51e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQ 569
Cdd:cd05904 32 ALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTT 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 570 QRLVDKFVEHKTQIICLDR--------DLPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVnylswct 641
Cdd:cd05904 112 AELAEKLASLALPVVLLDSaefdslsfSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLI------- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 642 nayALAQGYGAPVQSSIGFDAT------------ITSLF-SPLLVGKRVVLLPEKEEIEALSALlqsdQNYslvKIT--- 705
Cdd:cd05904 185 ---AMVAQFVAGEGSNSDSEDVflcvlpmfhiygLSSFAlGLLRLGATVVVMPRFDLEELLAAI----ERY---KVThlp 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 706 ---PAHLEMLNQMLPNHKGVTETRALIIGGeALLGKSL-NFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSL-SGAI 780
Cdd:cd05904 255 vvpPIVLALVKSPIVDKYDLSSLRQIMSGA-APLGKELiEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAkYGSV 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 781 liGRPIANTQLYLLD-DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARYLPDGNI 859
Cdd:cd05904 334 --GRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW--------LHTGDLCYIDEDGYL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 860 EYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTS-SELRQFLQSKLPEYMIP 938
Cdd:cd05904 404 FIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTeDEIMDFVAKQVAPYKKV 483
|
490 500
....*....|....*....|..
gi 2129675820 939 SAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05904 484 RKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
469-960 |
2.64e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 124.33 E-value: 2.64e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 469 ELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPT 548
Cdd:PRK06188 16 HLLVSALKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 549 YPQERLGFMLEDAQIPILLtqqrlVD--KFVEHK----------TQIICLD-----RDLPENATLSIDNP-VSNVTSENL 610
Cdd:PRK06188 96 GSLDDHAYVLEDAGISTLI-----VDpaPFVERAlallarvpslKHVLTLGpvpdgVDLLAAAAKFGPAPlVAAALPPDI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 611 AYIIYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYALAQG----YGAPVQSSIGfdatitSLFSP-LLVGKRVVLLP---- 681
Cdd:PRK06188 171 AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADprflMCTPLSHAGG------AFFLPtLLRGGTVIVLAkfdp 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 682 -------EKEEIEAlsALLQSDQNYSLVKITPAH------LEML----NQMLPnhkgvteTRaLIIGGEAL---LGKSln 741
Cdd:PRK06188 245 aevlraiEEQRITA--TFLVPTMIYALLDHPDLRtrdlssLETVyygaSPMSP-------VR-LAEAIERFgpiFAQY-- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 742 fwrdnapktriineYGPTETVVGCCVYEVDEQTSLSGAILI--GRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARG 819
Cdd:PRK06188 313 --------------YGQTEAPMVITYLRKRDHDPDDPKRLTscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 820 YLNRPELTQQRFipnpfsdePNSRLYkTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAR 899
Cdd:PRK06188 379 YWNRPEETAEAF--------RDGWLH-TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGV 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2129675820 900 EDQPGDKRLVGYIVPK-EQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK06188 450 PDEKWGEAVTAVVVLRpGAAVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
490-962 |
1.84e-28 |
|
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: 119.76 E-value: 1.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQipilltq 569
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 570 qrlvdkfvehktqiicldrdlpenatlsidnpvsnVTSENLAYIIYTSGSTGKPKGTMIPHRglvnylswctNAYALAQG 649
Cdd:cd05912 74 -----------------------------------VKLDDIATIMYTSGTTGKPKGVQQTFG----------NHWWSAIG 108
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 650 ygapVQSSIGFDAT--------------ITSLFSPLLVGKRVVLLpEKEEIEALSALLQSdQNYSLVKITPAHLEMLNQM 715
Cdd:cd05912 109 ----SALNLGLTEDdnwlcalplfhisgLSILMRSVIYGMTVYLV-DKFDAEQVLHLINS-GKVTIISVVPTMLQRLLEI 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 716 LPNHKGVTeTRALIIGGEAllgkslnfwrdnAPKTR----------IINEYGPTETVVGCCVYEVDEQTSLSGAIliGRP 785
Cdd:cd05912 183 LGEGYPNN-LRCILLGGGP------------APKPLleqckekgipVYQSYGMTETCSQIVTLSPEDALNKIGSA--GKP 247
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 786 IANTQLYLLDDKQklvPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlyKTGDLArYL-PDGNIEYLGR 864
Cdd:cd05912 248 LFPVELKIEDDGQ---PPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF---------KTGDIG-YLdEEGFLYVLDR 314
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 865 IDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVpKEQAPTSSELRQFLQSKLPEYMIPSAFVML 944
Cdd:cd05912 315 RSDLIISGGENIYPAEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVV-SERPISEEELIAYCSEKLAKYKVPKKIYFV 393
|
490
....*....|....*...
gi 2129675820 945 EVIPLTTHGKVDRQALPQ 962
Cdd:cd05912 394 DELPRTASGKLLRHELKQ 411
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
460-960 |
3.28e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 121.29 E-value: 3.28e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 460 EFPHD-----KCLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILG 534
Cdd:PRK06710 14 EIPSTisydiQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYG 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 535 ILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQ-------------------------------QRLVDKFVEHK--- 580
Cdd:PRK06710 94 TLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLdlvfprvtnvqsatkiehvivtriadflpfpKNLLYPFVQKKqsn 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 581 -------TQIICLDRDLPENATLSIDNPVSnvTSENLAYIIYTSGSTGKPKGTMIPHRGLVN-------YLSWCTNAYAL 646
Cdd:PRK06710 174 lvvkvseSETIHLWNSVEKEVNTGVEVPCD--PENDLALLQYTGGTTGFPKGVMLTHKNLVSntlmgvqWLYNCKEGEEV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 647 AQGYgAPVQSSIGFDATITslfSPLLVGKRVVLLPEKEEIEALSALlqSDQNYSLVKITPA-HLEMLNQMLPNHKGVTET 725
Cdd:PRK06710 252 VLGV-LPFFHVYGMTAVMN---LSIMQGYKMVLIPKFDMKMVFEAI--KKHKVTLFPGAPTiYIALLNSPLLKEYDISSI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 726 RAlIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQtSLSGAILIGRPIANTQLYLLDDKQKLVPiGV 805
Cdd:PRK06710 326 RA-CISGSAPLPVEVQEKFETVTGGKLVEGYGLTESSPVTHSNFLWEK-RVPGSIGVPWPDTEAMIMSLETGEALPP-GE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 806 PGELYIGGAGVARGYLNRPELTQQRFipnpfsdepNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLL 885
Cdd:PRK06710 403 IGEIVVKGPQIMKGYWNKPEETAAVL---------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVL 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2129675820 886 AQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTS-SELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK06710 474 YEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSeEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
4-432 |
4.50e-28 |
|
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: 119.05 E-value: 4.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 4 LIRISPQQKHLWLQQK--DNYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFhsLPGMNIPFQSISDAPTYNH 81
Cdd:cd19066 1 KIPLSPMQRGMWFLKKlaTDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRF--CEEAGRYEQVVLDKTVRFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 82 ISlaEYDWSRLSSQvqKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAY- 160
Cdd:cd19066 79 IE--IIDLRNLADP--EARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYd 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 161 TACLDGEEISEEVMQYADVSEWLNELLESEDTETARNYW--QQQDISSVLNLRIPFEIK-NDHQSSGEISFAPQSlclam 237
Cdd:cd19066 155 AAERQKPTLPPPVGSYADYAAWLEKQLESEAAQADLAYWtsYLHGLPPPLPLPKAKRPSqVASYEVLTLEFFLRS----- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 238 nrDTVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDALKFSEL 317
Cdd:cd19066 230 --EETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 318 MERVSESLRFVKKWQEYFNWENFISTN--EKFAARPFFPFCFDF-TQQSQSYVNGNIAFSEYK-KSANIDKFQIKLS-SG 392
Cdd:cd19066 308 LKRTKEQSREAIEHQRVPFIELVRHLGvvPEAPKHPLFEPVFTFkNNQQQLGKTGGFIFTTPVyTSSEGTVFDLDLEaSE 387
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2129675820 393 YSQDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNP 432
Cdd:cd19066 388 DPDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
24-432 |
6.40e-28 |
|
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: 118.46 E-value: 6.40e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 24 AYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLpGMNIPFQSI-SDAPtynhISLAEYDWSRLSSQVQKAKID 102
Cdd:cd19543 23 AYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWE-GLGEPLQVVlKDRK----LPWRELDLSHLSEAEQEAELE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 103 TLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACLDGEEIS-EEVMQYADVSE 181
Cdd:cd19543 98 ALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGEGQPPSlPPVRPYRDYIA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 182 WlnelLESEDTETARNYWQQQdissvL-NLRIPFEIKNDHQSSGEISFAPQSLCLAMNRDTVEKLEILQESYHTSTEAIL 260
Cdd:cd19543 178 W----LQRQDKEAAEAYWREY-----LaGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTLNTVV 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 261 LACWQVLLWRLSGQSEIVIGAAGDGREYDeLKGV---FGLLTKYLPIHSRLEDALKFSELMERVseslrfvkkwQEYFNw 337
Cdd:cd19543 249 QGAWALLLSRYSGRDDVVFGTTVSGRPAE-LPGIetmVGLFINTLPVRVRLDPDQTVLELLKDL----------QAQQL- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 338 enfistnekfAARP--FFPFcFDFtqQSQSYVNGN-----IAFSEY------KKSANIDKFQIKLSSGYSQDN------- 397
Cdd:cd19543 317 ----------ELREheYVPL-YEI--QAWSEGKQAlfdhlLVFENYpvdeslEEEQDEDGLRITDVSAEEQTNypltvva 383
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2129675820 398 -----LVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNP 432
Cdd:cd19543 384 ipgeeLTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
467-960 |
1.09e-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: 119.31 E-value: 1.09e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHES----LTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAY 542
Cdd:cd05906 12 LLELLLRAAERGPTKGITYIDADGseefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 543 IPFD--PTYPQ--------ERLGFMLEDaqiPILLTQQRLVDKFVEHKTqiiclDRDLPENATLSIDN--------PVSN 604
Cdd:cd05906 92 APLTvpPTYDEpnarlrklRHIWQLLGS---PVVLTDAELVAEFAGLET-----LSGLPGIRVLSIEElldtaadhDLPQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 605 VTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSwctnayALAQGYGAPVQSSI----GFDATITSLFSPLlvgkRVVLL 680
Cdd:cd05906 164 SRPDDLALLMLTSGSTGFPKAVPLTHRNILARSA------GKIQHNGLTPQDVFlnwvPLDHVGGLVELHL----RAVYL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 681 pEKEEIEALSALLQSD--------QNYSlVKITPA---HLEMLNQMLPNHKGVT----ETRALIIGGEALLGKSLNFW-- 743
Cdd:cd05906 234 -GCQQVHVPTEEILADplrwldliDRYR-VTITWApnfAFALLNDLLEEIEDGTwdlsSLRYLVNAGEAVVAKTIRRLlr 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 744 ---RDNAPKTRIINEYGPTETVVGCCVYEVDEQTSLSGAIL---IGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVA 817
Cdd:cd05906 312 llePYGLPPDAIRPAFGMTETCSGVIYSRSFPTYDHSQALEfvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVT 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 818 RGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLArYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVN---AV 894
Cdd:cd05906 392 KGYYNNPEANAEAFTEDGW--------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEpsfTA 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129675820 895 TVIAREDQPGDKRLVGYIVP-KEQAPTSSELRQFLQSKL-------PEYMIPsafVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05906 463 AFAVRDPGAETEELAIFFVPeYDLQDALSETLRAIRSVVsrevgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
490-960 |
1.43e-27 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 119.54 E-value: 1.43e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQK-LGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPIL-- 566
Cdd:PRK12492 49 TLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALvy 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 567 ------LTQQRLVDKFVE---------------------------------HKTQIICLDRDLPENATLSIdNPVSnVTS 607
Cdd:PRK12492 129 lnmfgkLVQEVLPDTGIEylieakmgdllpaakgwlvntvvdkvkkmvpayHLPQAVPFKQALRQGRGLSL-KPVP-VGL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 608 ENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSwctNAYALAQGYGAPVQSSI--GFDATITSLfsPL-------------- 671
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLVANML---QVRACLSQLGPDGQPLMkeGQEVMIAPL--PLyhiyaftancmcmm 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 672 LVGKRVVLLPEKEEIEALSALLQSDQNYSLVKITPAHLEMLNQmlPNHKGVTETRALII--GGEALLGKSLNFWRDnAPK 749
Cdd:PRK12492 282 VSGNHNVLITNPRDIPGFIKELGKWRFSALLGLNTLFVALMDH--PGFKDLDFSALKLTnsGGTALVKATAERWEQ-LTG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 750 TRIINEYGPTETVVGCCVYEVDEQTSLSgaiLIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQ 829
Cdd:PRK12492 359 CTIVEGYGLTETSPVASTNPYGELARLG---TVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 830 RFipnpfsDEPNsrLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLV 909
Cdd:PRK12492 436 AL------DAEG--WFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVK 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2129675820 910 GYIVPKEQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK12492 508 LFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
8-255 |
1.90e-27 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 112.44 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 8 SPQQKHLWLQQKDNyQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGmnIPFQSISDAPTynhISLAEY 87
Cdd:COG4908 2 SPAQKRFLFLEPGS-NAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDG--EPVQRIDPDAD---LPLEVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 88 DWSRLSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACLDGE 167
Cdd:COG4908 76 DLSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 168 EISEEVM--QYADVSEWLNELLESEDTETARNYWQQQDISSVLNLRIPFeiknDHQSSGEISFAPQSLCLAMNRDTVEKL 245
Cdd:COG4908 156 PPPLPELpiQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPT----DRPRPAVQTFRGATLSFTLPAELTEAL 231
|
250
....*....|
gi 2129675820 246 EILQESYHTS 255
Cdd:COG4908 232 KALAKAHGAT 241
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
467-960 |
4.18e-27 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 117.85 E-value: 4.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQ-KLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPF 545
Cdd:PRK08974 25 LVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 546 DPTYPQERLGFMLEDA---QIPILLTQQRLVDKFVEhKTQI--ICLDR---------------------------DLPEn 593
Cdd:PRK08974 105 NPLYTPRELEHQLNDSgakAIVIVSNFAHTLEKVVF-KTPVkhVILTRmgdqlstakgtlvnfvvkyikrlvpkyHLPD- 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 594 aTLSIDNPVSN----------VTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYAlaqgygaPVQSSiGFDAT 663
Cdd:PRK08974 183 -AISFRSALHKgrrmqyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYG-------PLLHP-GKELV 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 664 ITSLfsPLL--------------VGKRVVLLPEKEEIEALSALLQsdqNYSLVKITPAHlEMLNQMLPN---HKGVTETR 726
Cdd:PRK08974 254 VTAL--PLYhifaltvncllfieLGGQNLLITNPRDIPGFVKELK---KYPFTAITGVN-TLFNALLNNeefQELDFSSL 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 727 ALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTET--VVGCCVYEVDEQtslSGAIliGRPIANTQLYLLDDKQKLVPIG 804
Cdd:PRK08974 328 KLSVGGGMAVQQAVAERWVKLTGQYLLEGYGLTECspLVSVNPYDLDYY---SGSI--GLPVPSTEIKLVDDDGNEVPPG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 805 VPGELYIGGAGVARGYLNRPELTQQrFIPNPFsdepnsrlYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESL 884
Cdd:PRK08974 403 EPGELWVKGPQVMLGYWQRPEATDE-VIKDGW--------LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDV 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2129675820 885 LAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK08974 474 VMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
467-955 |
6.50e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 116.98 E-value: 6.50e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQ-KLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPF 545
Cdd:PRK08314 12 LFHNLEVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 546 DPTYPQERLGFMLEDAQIPILLTQQRLVDKF----------------------------------VEHKTQIICLDRDLP 591
Cdd:PRK08314 92 NPMNREEELAHYVTDSGARVAIVGSELAPKVapavgnlrlrhvivaqysdylpaepeiavpawlrAEPPLQALAPGGVVA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 592 ENATLS--IDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLvnylsWCTNAYALAQGYGAPvqSSIG------FDAT 663
Cdd:PRK08314 172 WKEALAagLAPPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTV-----MANAVGSVLWSNSTP--ESVVlavlplFHVT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 664 --ITSLFSPLLVGKRVVLLP--EKEeieaLSALLQSDQNYSLVKITPAhleMLNQMLPNhKGVTE----TRALIIGGEAL 735
Cdd:PRK08314 245 gmVHSMNAPIYAGATVVLMPrwDRE----AAARLIERYRVTHWTNIPT---MVVDFLAS-PGLAErdlsSLRYIGGGGAA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 736 LGKS----------LNFwrdnapktriINEYGPTETVVG-----------CCvyevdeqtslsgailIGRPIANTQLYLL 794
Cdd:PRK08314 317 MPEAvaerlkeltgLDY----------VEGYGLTETMAQthsnppdrpklQC---------------LGIPTFGVDARVI 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 795 D-DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIpnpfsdEPN-SRLYKTGDLARYLPDGNIEYLGRIDHQVKIR 872
Cdd:PRK08314 372 DpETLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFI------EIDgKRFFRTGDLGRMDEEGYFFITDRLKRMINAS 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 873 GFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQA---PTSSELRQFLQSKLPEYMIPSAFVMLEVIPL 949
Cdd:PRK08314 446 GFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVVLRPEArgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPK 525
|
....*.
gi 2129675820 950 TTHGKV 955
Cdd:PRK08314 526 SGSGKI 531
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
491-918 |
7.51e-27 |
|
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: 115.92 E-value: 7.51e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 491 LTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAqipilltqq 570
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHS--------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 571 rlvdkfvehktqiicldrdlpENATLSIDNpvsnvTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSwctNAYALAQG- 649
Cdd:cd17640 77 ---------------------ESVALVVEN-----DSDDLATIIYTSGTTGNPKGVMLTHANLLHQIR---SLSDIVPPq 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 650 YGAPVQS---------------------SIGFdATITSLFSPLLVGKRVVLLPEKEEIEALSALLQsDQnyslVKITPAH 708
Cdd:cd17640 128 PGDRFLSilpiwhsyersaeyfifacgcSQAY-TSIRTLKDDLKRVKPHYIVSVPRLWESLYSGIQ-KQ----VSKSSPI 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 709 LEMLNQMLpnhKGVTETRALIIGGEALLGKSLNFWrdNAPKTRIINEYGPTETVVGCCVYEVDEQTSLSgailIGRPIAN 788
Cdd:cd17640 202 KQFLFLFF---LSGGIFKFGISGGGALPPHVDTFF--EAIGIEVLNGYGLTETSPVVSARRLKCNVRGS----VGRPLPG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 789 TQLYLLD-DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDepnsrlykTGDLARYLPDGNIEYLGRI-D 866
Cdd:cd17640 273 TEIKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFN--------TGDLGWLTCGGELVLTGRAkD 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 2129675820 867 HQVKIRGFRIELEEIESLLAQHPLVNAVTVIArEDQpgdKRLVGYIVP-KEQA 918
Cdd:cd17640 345 TIVLSNGENVEPQPIEEALMRSPFIEQIMVVG-QDQ---KRLGALIVPnFEEL 393
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
588-960 |
2.18e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 112.45 E-value: 2.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 588 RDLPENATLS--------IDNPVSNVTSenlayiiyTSGSTGKPKGTMIPHRGLVnylswcTNAYALAQGYGAPVQ---- 655
Cdd:PRK07824 15 QDERRAALLRdalrvgepIDDDVALVVA--------TSGTTGTPKGAMLTAAALT------ASADATHDRLGGPGQwlla 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 656 ---SSIgfdATITSLFSPLLVGKR--VVLLPEKEEIEALS---ALLQSDQNY-SLVKI-------TPAHLEMLnqmlpnh 719
Cdd:PRK07824 81 lpaHHI---AGLQVLVRSVIAGSEpvELDVSAGFDPTALPravAELGGGRRYtSLVPMqlakaldDPAATAAL------- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 720 kgvTETRALIIGGEALLGKSLNfwRDNAPKTRIINEYGPTETvVGCCVYEvdeqtslsgailiGRPIANTQLYLLDdkqk 799
Cdd:PRK07824 151 ---AELDAVLVGGGPAPAPVLD--AAAAAGINVVRTYGMSET-SGGCVYD-------------GVPLDGVRVRVED---- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 800 lvpigvpGELYIGGAGVARGYLNRPEltqqrfiPNPFSdEPNsrLYKTGDLARyLPDGNIEYLGRIDHQVKIRGFRIELE 879
Cdd:PRK07824 208 -------GRIALGGPTLAKGYRNPVD-------PDPFA-EPG--WFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 880 EIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQ-APTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQ 958
Cdd:PRK07824 270 VVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGpAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRR 349
|
..
gi 2129675820 959 AL 960
Cdd:PRK07824 350 AL 351
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
444-955 |
2.68e-26 |
|
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: 115.75 E-value: 2.68e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 444 ESDRQKLLIDFNNTKIEFPHDKCL---HELFAAQVERTPNNIAVEFNHE------SLTYAQLNAKSNQLAHHLQKLGVKP 514
Cdd:cd17634 29 YQKVKNTSFAPGAPSIKWFEDATLnlaANALDRHLRENGDRTAIIYEGDdtsqsrTISYRELHREVCRFAGTLLDLGVKK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 515 EVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQ------RLVD--KFVEHKTQ---- 582
Cdd:cd17634 109 GDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragRSVPlkKNVDDALNpnvt 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 583 ----IICLDR-----DLPENATLSIDNPVSN---------VTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSWcTNAY 644
Cdd:cd17634 189 svehVIVLKRtgsdiDWQEGRDLWWRDLIAKaspehqpeaMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAAT-TMKY 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 645 ALAQGYGAPVQ--SSIGFdATITS--LFSPLLVGKRVVLLPEKEEIEALSALLQ--SDQNYSLVKITPAHLEMLNQMLPN 718
Cdd:cd17634 268 VFDYGPGDIYWctADVGW-VTGHSylLYGPLACGATTLLYEGVPNWPTPARMWQvvDKHGVNILYTAPTAIRALMAAGDD 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 719 HKGVTETRALIIGGEAllGKSLN------FWRD-NAPKTRIINEYGPTETVVGCCvyevdeqTSLSGAILIG-----RPI 786
Cdd:cd17634 347 AIEGTDRSSLRILGSV--GEPINpeayewYWKKiGKEKCPVVDTWWQTETGGFMI-------TPLPGAIELKagsatRPV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 787 ANTQLYLLDDKQKLVPIGVPGELYIGGA--GVARGYLNRPEltqqRFIPNPFSDEPNsrLYKTGDLARYLPDGNIEYLGR 864
Cdd:cd17634 418 FGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKG--MYFSGDGARRDEDGYYWITGR 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 865 IDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPK---EQAPT-SSELRQFLQSKLPEYMIPSA 940
Cdd:cd17634 492 SDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNhgvEPSPElYAELRNWVRKEIGPLATPDV 571
|
570
....*....|....*
gi 2129675820 941 FVMLEVIPLTTHGKV 955
Cdd:cd17634 572 VHWVDSLPKTRSGKI 586
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
467-962 |
1.21e-25 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 113.06 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHE--SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIP 544
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 545 FDPTYP-------QERLG--FMLEDAQIPillTQQRLVDKFVEHKTQIICLDRDlPENATLSID-------NPVSNvTSE 608
Cdd:PRK05852 98 LDPALPiaeqrvrSQAAGarVVLIDADGP---HDRAEPTTRWWPLTVNVGGDSG-PSGGTLSVHldaatepTPATS-TPE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 609 NL----AYIIYTSGSTGKPKgtMIP--HRGLVNYLSWCTNAYALAQGygapvqssigfDAT------------ITSLFSP 670
Cdd:PRK05852 173 GLrpddAMIMFTGGTTGLPK--MVPwtHANIASSVRAIITGYRLSPR-----------DATvavmplyhghglIAALLAT 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 671 LLVGKrVVLLPEK---------EEIEALSALLqsdqnYSLVkitPAHLEMLNQmLPNHKGVTETRAliiggeallgkSLN 741
Cdd:PRK05852 240 LASGG-AVLLPARgrfsahtfwDDIKAVGATW-----YTAV---PTIHQILLE-RAATEPSGRKPA-----------ALR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 742 FWRD-NAPKTR-------------IINEYGPTETV--VGCCVYEVDEQTSLSGAI--LIGRPIANTQLYLLDDKQKLVPi 803
Cdd:PRK05852 299 FIRScSAPLTAetaqalqtefaapVVCAFGMTEAThqVTTTQIEGIGQTENPVVStgLVGRSTGAQIRIVGSDGLPLPA- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 804 GVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlyKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIES 883
Cdd:PRK05852 378 GAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL---------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 884 LLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQA-PTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALPQ 962
Cdd:PRK05852 449 VLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESApPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
467-969 |
2.68e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 112.14 E-value: 2.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD 546
Cdd:PRK06164 12 LASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 547 PTYPQERLGFMLEDAQIPILLTQQRL--VDKF-----VEHKT-----QIICLDR-----------------DLPENATLS 597
Cdd:PRK06164 92 TRYRSHEVAHILGRGRARWLVVWPGFkgIDFAailaaVPPDAlpplrAIAVVDDaadatpapapgarvqlfALPDPAPPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 598 IDNPVSNVtsENLAYIIYT-SGSTGKPKGTMIPHRGLVNYLSWCTNAYALAQGY----GAPVQSSIGFdatiTSLFSPLL 672
Cdd:PRK06164 172 AAGERAAD--PDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAvllaALPFCGVFGF----STLLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 673 VGKRVVLLPEKEEIEALSALLQSDqnyslVKITPAHLEMLNQMlpnHKGVTETRAL----IIGGEALLGKslnfWRDNAP 748
Cdd:PRK06164 246 GGAPLVCEPVFDAARTARALRRHR-----VTHTFGNDEMLRRI---LDTAGERADFpsarLFGFASFAPA----LGELAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 749 KTR-----IINEYGPTE--TVVGCCVYEVDEQTSLSGAILIGRPIANTQLYLLDDKQkLVPIGVPGELYIGGAGVARGYL 821
Cdd:PRK06164 314 LARargvpLTGLYGSSEvqALVALQPATDPVSVRIEGGGRPASPEARVRARDPQDGA-LLPDGESGEIEIRAPSLMRGYL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 822 NRPELTQQRFIPNPFsdepnsrlYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIARED 901
Cdd:PRK06164 393 DNPDATARALTDDGY--------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATR 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2129675820 902 QpGDKRLVGYIVPKEQAPT-SSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHG---KVDRQALPQPDTSRLD 969
Cdd:PRK06164 465 D-GKTVPVAFVIPTDGASPdEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLREMAQARLA 535
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
476-962 |
4.46e-25 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 110.35 E-value: 4.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 476 ERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLG 555
Cdd:PRK09029 14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 556 FMLEDAQIPILLtqqrlvdkFVEHKTQIICLDrdlpeNATLSIDNPVSNVT--SENLAYIIYTSGSTGKPKGTMIPHRgl 633
Cdd:PRK09029 94 ELLPSLTLDFAL--------VLEGENTFSALT-----SLHLQLVEGAHAVAwqPQRLATMTLTSGSTGLPKAAVHTAQ-- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 634 vNYLswctnayALAQGygapVQSSIGFDATITSLFS-P-------------LLVGKRVVlLPEKEEieaLSALLQSDQNY 699
Cdd:PRK09029 159 -AHL-------ASAEG----VLSLMPFTAQDSWLLSlPlfhvsgqgivwrwLYAGATLV-VRDKQP---LEQALAGCTHA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 700 SLVkitPAHLEMLnqmLPNHKGVTETRALIIGGeALLGKSLNfwrDNAPKTRIinE----YGPTE---TVvgcCVYEVDe 772
Cdd:PRK09029 223 SLV---PTQLWRL---LDNRSEPLSLKAVLLGG-AAIPVELT---EQAEQQGI--RcwcgYGLTEmasTV---CAKRAD- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 773 qtSLSGAiliGRPIANTQLYLLDDkqklvpigvpgELYIGGAGVARGYLNRPELTqqrfipnPFSDEPNsrLYKTGDLAR 852
Cdd:PRK09029 287 --GLAGV---GSPLPGREVKLVDG-----------EIWLRGASLALGYWRQGQLV-------PLVNDEG--WFATRDRGE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 853 yLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGyIVPKEQAPTSSELRQFLQSKL 932
Cdd:PRK09029 342 -WQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVA-VVESDSEAAVVNLAEWLQDKL 419
|
490 500 510
....*....|....*....|....*....|
gi 2129675820 933 PEYMIPSAFVMLEVIPLTTHGKVDRQALPQ 962
Cdd:PRK09029 420 ARFQQPVAYYLLPPELKNGGIKISRQALKE 449
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
483-963 |
6.58e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 110.08 E-value: 6.58e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 483 AVEFNHESLTYAQLNAKSNQLAHHLQKLGvkpevLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQ 562
Cdd:PRK07787 18 AVRIGGRVLSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 563 IPILLTQQRLVDKFVEHktqiicLDRDLPENATLSIDNPvsnvTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSwctn 642
Cdd:PRK07787 93 AQAWLGPAPDDPAGLPH------VPVRLHARSWHRYPEP----DPDAPALIVYTSGTTGPPKGVVLSRRAIAADLD---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 643 ayALAQGY----------GAPVQSSIGFdatITSLFSPLLVGKRVVLLPeKEEIEALSALLQSDQN--------YSLVKI 704
Cdd:PRK07787 159 --ALAEAWqwtaddvlvhGLPLFHVHGL---VLGVLGPLRIGNRFVHTG-RPTPEAYAQALSEGGTlyfgvptvWSRIAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 705 TPAHLEMLnqmlpnhkgvTETRALIIGGEALlgkSLNFWRDNAPKT--RIINEYGPTETVVGCCVYEVDEQTslsgAILI 782
Cdd:PRK07787 233 DPEAARAL----------RGARLLVSGSAAL---PVPVFDRLAALTghRPVERYGMTETLITLSTRADGERR----PGWV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 783 GRPIANTQLYLLDDKQKLVPIGVP--GELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARYLPDGNIE 860
Cdd:PRK07787 296 GLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW--------FRTGDVAVVDPDGMHR 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 861 YLGR--IDhQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEqAPTSSELRQFLQSKLPEYMIP 938
Cdd:PRK07787 368 IVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGAD-DVAADELIDFVAQQLSVHKRP 445
|
490 500
....*....|....*....|....*
gi 2129675820 939 SAFVMLEVIPLTTHGKVDRQALPQP 963
Cdd:PRK07787 446 REVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
491-932 |
9.49e-25 |
|
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: 110.00 E-value: 9.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 491 LTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGgayIPFDPTYpqERLGfmlEDAqipilltqq 570
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVY--ATLG---EDA--------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 571 rLVDKFVE-HKTQIICldrdlpenatlsidnpvsNVTSENLAYIIYTSGSTGKPKGTMIPHRGLV--------------- 634
Cdd:cd17639 69 -LIHSLNEtECSAIFT------------------DGKPDDLACIMYTSGSTGNPKGVMLTHGNLVagiaglgdrvpellg 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 635 ---NYLSW----------CTN---AYALAQGYGAPvqssigfdATIT-----------SLFSP-LLVG--------KRVV 678
Cdd:cd17639 130 pddRYLAYlplahifelaAENvclYRGGTIGYGSP--------RTLTdkskrgckgdlTEFKPtLMVGvpaiwdtiRKGV 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 679 LlpekEEIEALSALLQS--DQNYSL-------VKITPAHLEM----LNQMLPNHkgvteTRALIIGGEALLGKSLNFWrd 745
Cdd:cd17639 202 L----AKLNPMGGLKRTlfWTAYQSklkalkeGPGTPLLDELvfkkVRAALGGR-----LRYMLSGGAPLSADTQEFL-- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 746 NAPKTRIINEYGPTETVVGCCVYEVDEQTSLSgailIGRPIANTQLYLLD-DKQKLVPIGVP--GELYIGGAGVARGYLN 822
Cdd:cd17639 271 NIVLCPVIQGYGLTETCAGGTVQDPGDLETGR----VGPPLPCCEIKLVDwEEGGYSTDKPPprGEILIRGPNVFKGYYK 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 823 RPELTQQRFIPNpfsdepnsRLYKTGDLARYLPDGNIEYLGRIDHQVKIR-GFRIELEEIESLLAQHPLVNAVTVIARED 901
Cdd:cd17639 347 NPEKTKEAFDGD--------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPD 418
|
490 500 510
....*....|....*....|....*....|.
gi 2129675820 902 QPgdkRLVGYIVPKEQAptsseLRQFLQSKL 932
Cdd:cd17639 419 KS---YPVAIVVPNEKH-----LTKLAEKHG 441
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
464-962 |
9.64e-25 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 110.46 E-value: 9.64e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 464 DKCLHELFAAQVErtPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPE----VLVGICVErsldMLIGILGILKAG 539
Cdd:PRK10946 24 DLPLTDILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGdtalVQLGNVAE----FYITFFALLKLG 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 540 GAyiPFDPTYPQERLGFMLEDAQI-PILLTQQR---------LVDKFVEHKT--QIICLDRDLPENATLS-IDNPVSNVT 606
Cdd:PRK10946 98 VA--PVNALFSHQRSELNAYASQIePALLIADRqhalfsdddFLNTLVAEHSslRVVLLLNDDGEHSLDDaINHPAEDFT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 607 -----SENLAYIIYTSGSTGKPKgtMIP--H-------RGLVN---------YLswCtnayALAQGYGAPVQS--SIGFd 661
Cdd:PRK10946 176 atpspADEVAFFQLSGGSTGTPK--LIPrtHndyyysvRRSVEicgftpqtrYL--C----ALPAAHNYPMSSpgALGV- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 662 atitslfspLLVGKRVVLLPEKEEIEALSALLQSDQNY-SLVKitPAHLEMLNQM-LPNHKGVTETRALIIGGEALLGKS 739
Cdd:PRK10946 247 ---------FLAGGTVVLAPDPSATLCFPLIEKHQVNVtALVP--PAVSLWLQAIaEGGSRAQLASLKLLQVGGARLSET 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 740 LnfwrdnapKTRIineygPTEtvVGCCVYEV----------------DEQTSLSGailiGRPIA-NTQLYLLDDKQKLVP 802
Cdd:PRK10946 316 L--------ARRI-----PAE--LGCQLQQVfgmaeglvnytrlddsDERIFTTQ----GRPMSpDDEVWVADADGNPLP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 803 IGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIE 882
Cdd:PRK10946 377 QGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF--------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIE 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 883 SLLAQHPLVNAVTVIARED-QPGDKRlVGYIVPKEqAPTSSELRQFLQSK-LPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK10946 449 NLLLRHPAVIHAALVSMEDeLMGEKS-CAFLVVKE-PLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
..
gi 2129675820 961 PQ 962
Cdd:PRK10946 527 RQ 528
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
460-960 |
1.64e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 109.85 E-value: 1.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 460 EFPHdkcLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKL-GVKPEVLVGICVERSLDMLIGILGILKA 538
Cdd:PRK05677 22 EYPN---IQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 539 GGAYIPFDPTYPQERLGFMLEDAQIPILL---------------TQQR-----------------LVDKFVEHKTQII-- 584
Cdd:PRK05677 99 GLIVVNTNPLYTAREMEHQFNDSGAKALVclanmahlaekvlpkTGVKhvivtevadmlpplkrlLINAVVKHVKKMVpa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 585 -CLDRDLPENATLSI--DNPVSNVT--SENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYALAQGYG-----APV 654
Cdd:PRK05677 179 yHLPQAVKFNDALAKgaGQPVTEANpqADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGceiliAPL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 655 QSSIGFDATITSLFSpLLVGKRVVLLPEKEEIEALSALLQSDQNYSLVKITPAHLEMLNQMLPNHKGVTETRALIIGGEA 734
Cdd:PRK05677 259 PLYHIYAFTFHCMAM-MLIGNHNILISNPRDLPAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMA 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 735 LLGKSLNFWRDnAPKTRIINEYGPTETVVGCCVYEVDeqtslsgAI---LIGRPIANTQLYLLDDKQKLVPIGVPGELYI 811
Cdd:PRK05677 338 LQLATAERWKE-VTGCAICEGYGMTETSPVVSVNPSQ-------AIqvgTIGIPVPSTLCKVIDDDGNELPLGEVGELCV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 812 GGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLV 891
Cdd:PRK05677 410 KGPQVMKGYWQRPEATDEILDSDGW--------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGV 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 892 NAVTVIAREDQPGDKRLVGYIVPKEQAP-TSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK05677 482 LQCAAIGVPDEKSGEAIKVFVVVKPGETlTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
782-1056 |
2.23e-24 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 105.22 E-value: 2.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 782 IGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFSDEPNSRLYKTGDLARYLPDGNIEY 861
Cdd:COG3433 20 IPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 862 LGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPkEQAPTSSELRQFLQSKLPEYMIPSAF 941
Cdd:COG3433 100 ERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAA-LDGLAAAAALAALDKVPPDVVAASAV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 942 VMLEVIPLTTHGKVDRQALPQPDTSRLDTLKVEFIAPRDRLELK-LANIWENLLNVHP--IGIKDSFFELGGHSLLAVRL 1018
Cdd:COG3433 179 VALDALLLLALKVVARAAPALAAAEALLAAASPAPALETALTEEeLRADVAELLGVDPeeIDPDDNLFDLGLDSIRLMQL 258
|
250 260 270
....*....|....*....|....*....|....*...
gi 2129675820 1019 MAHINQEfGKNLALATLFQNPTIEKLANLLRQTSEISS 1056
Cdd:COG3433 259 VERWRKA-GLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
462-960 |
3.00e-24 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 108.69 E-value: 3.00e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 462 PHDKCLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGA 541
Cdd:PRK06155 18 PSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 542 YIPFDPTYPQERLGFMLEDAQIPILLTQQRLVDKfVEHktqiiCLDRDLPENATLSIDNPVSNVTSENLAY--------- 612
Cdd:PRK06155 98 AVPINTALRGPQLEHILRNSGARLLVVEAALLAA-LEA-----ADPGDLPLPAVWLLDAPASVSVPAGWSTaplppldap 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 613 -------------IIYTSGSTGKPKGTMIPHrglVNYLSWCTN-AYALAQGYGAPVQSSIGFDAT--ITSLFSPLLVGKR 676
Cdd:PRK06155 172 apaaavqpgdtaaILYTSGTTGPSKGVCCPH---AQFYWWGRNsAEDLEIGADDVLYTTLPLFHTnaLNAFFQALLAGAT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 677 VVLLPEkeeieaLSAllqSDQNYSLVK--ITPAHL--EMLNQML-----PNHKGVTETRALIIGGEALLGKSLnFWRDNA 747
Cdd:PRK06155 249 YVLEPR------FSA---SGFWPAVRRhgATVTYLlgAMVSILLsqparESDRAHRVRVALGPGVPAALHAAF-RERFGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 748 PktrIINEYGPTETVVGCCVyEVDEQTSLSgailIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGA---GVARGYLNRP 824
Cdd:PRK06155 319 D---LLDGYGSTETNFVIAV-THGSQRPGS----MGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 825 ELTQQRFipnpfsdepNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPG 904
Cdd:PRK06155 391 EKTVEAW---------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELG 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2129675820 905 DKRLVGYIVPKE-QAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK06155 462 EDEVMAAVVLRDgTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
613-957 |
3.08e-24 |
|
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: 105.82 E-value: 3.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 613 IIYTSGSTGKPKGTMIPHRGLVNylswctNAY--ALAQGYGA------PVQ------SSIGFDATIT---------SLFS 669
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVN------NGYfiGERLGLTEqdrlciPVPlfhcfgSVLGVLACLThgatmvfpsPSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 670 PLLVGKRVvllpEKEEIEALSAllqsdqnyslvkiTPA-HLEMLNQMLPNHKGVTETRALIIGG----EALLGKSLNfwR 744
Cdd:cd05917 81 PLAVLEAI----EKEKCTALHG-------------VPTmFIAELEHPDFDKFDLSSLRTGIMAGapcpPELMKRVIE--V 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 745 DNAPKTRIIneYGPTETVVGCCVYEVDEqTSLSGAILIGRPIANTQLYLLD-DKQKLVPIGVPGELYIGGAGVARGYLNR 823
Cdd:cd05917 142 MNMKDVTIA--YGMTETSPVSTQTRTDD-SIEKRVNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWND 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 824 PELTQQrfipnpfsDEPNSRLYKTGDLARYLPDGNIEYLGRIDHQVkIRGFR-IELEEIESLLAQHPLVNAVTVIAREDQ 902
Cdd:cd05917 219 PEKTAE--------AIDGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDE 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2129675820 903 PGDKRLVGYIVPKEQA-PTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDR 957
Cdd:cd05917 290 RYGEEVCAWIRLKEGAeLTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
467-960 |
3.53e-24 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 108.95 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD 546
Cdd:PRK07059 25 LADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 547 PTYPQERLGFMLED--AQIPILL-----TQQRLVDK-----------------------FVEHKTQIICLDRDLP----- 591
Cdd:PRK07059 105 PLYTPRELEHQLKDsgAEAIVVLenfatTVQQVLAKtavkhvvvasmgdllgfkghivnFVVRRVKKMVPAWSLPghvrf 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 592 -----ENATLSIDNPvsNVTSENLAYIIYTSGSTGKPKGTMIPHRGLV-NYL---SWCTNAYALaqgYGAPVQSSIG--- 659
Cdd:PRK07059 185 ndalaEGARQTFKPV--KLGPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLqmeAWLQPAFEK---KPRPDQLNFVcal 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 660 -----FDATITSLFSpLLVGKRVVLLPEKEEIEALSALLQSDQnyslVKITPAHLEMLNQMLpNHKGVTET--RALII-- 730
Cdd:PRK07059 260 plyhiFALTVCGLLG-MRTGGRNILIPNPRDIPGFIKELKKYQ----VHIFPAVNTLYNALL-NNPDFDKLdfSKLIVan 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 731 -GGEALLGKSLNFWRDNApKTRIINEYGPTET--VVGCCVYEVDEqtsLSGAIliGRPIANTQLYLLDDKQKLVPIGVPG 807
Cdd:PRK07059 334 gGGMAVQRPVAERWLEMT-GCPITEGYGLSETspVATCNPVDATE---FSGTI--GLPLPSTEVSIRDDDGNDLPLGEPG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 808 ELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQ 887
Cdd:PRK07059 408 EICIRGPQVMAGYWNRPDETAKVMTADGF--------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVAS 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2129675820 888 HPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK07059 480 HPGVLEVAAVGVPDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
488-970 |
4.57e-24 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 108.44 E-value: 4.57e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 488 HESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIP----FDPTYPQERlgfmLEDAQI 563
Cdd:PRK04319 71 KEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPlfeaFMEEAVRDR----LEDSEA 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 564 PILLTQQRL-----VDKFVEHKTQIICLDRDLPENATLSIDN---------PVSNVTSENLAYIIYTSGSTGKPKGTMIP 629
Cdd:PRK04319 147 KVLITTPALlerkpADDLPSLKHVLLVGEDVEEGPGTLDFNAlmeqasdefDIEWTDREDGAILHYTSGSTGKPKGVLHV 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 630 HRGLV-NYLS-------------WCTNAYALAQG--YGapvqssigfdatitsLFSPLLVGKRVVLLPEKEEIEALSALL 693
Cdd:PRK04319 227 HNAMLqHYQTgkyvldlheddvyWCTADPGWVTGtsYG---------------IFAPWLNGATNVIDGGRFSPERWYRIL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 694 QsDQNYSLVKITPAHLEMLnqMlpnhKGVTETRA--------LIiggeALLGKSLN----FWRDNAPKTRIINEYGPTET 761
Cdd:PRK04319 292 E-DYKVTVWYTAPTAIRML--M----GAGDDLVKkydlsslrHI----LSVGEPLNpevvRWGMKVFGLPIHDNWWMTET 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 762 vvgccvyevdeqtslsGAILI-------------GRPIANTQLYLLDDKQKLVPIGVPGELYI--GGAGVARGYLNRPEL 826
Cdd:PRK04319 361 ----------------GGIMIanypamdikpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEK 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 827 TQQRFIPNpfsdepnsrLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQpgdk 906
Cdd:PRK04319 425 YESYFAGD---------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDP---- 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 907 rLVGYIV-----------PKEQapTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQ-------ALPQPDTSRL 968
Cdd:PRK04319 492 -VRGEIIkafvalrpgyePSEE--LKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRvlkawelGLPEGDLSTM 568
|
..
gi 2129675820 969 DT 970
Cdd:PRK04319 569 ED 570
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
474-955 |
6.19e-24 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 107.94 E-value: 6.19e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 474 QVER----TPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIP--FDP 547
Cdd:PRK07786 22 QLARhalmQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPvnFRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 548 TYPQerLGFMLEDAQIPILLTQQRLVD-----KFVEHKTQIICLDRDLPENATLSIDN---------PVSNVTSENLAYI 613
Cdd:PRK07786 102 TPPE--IAFLVSDCGAHVVVTEAALAPvatavRDIVPLLSTVVVAGGSSDDSVLGYEDllaeagpahAPVDIPNDSPALI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 614 IYTSGSTGKPKGTMIPHRGLVnylswcTNAYALAQGYGAPVQSSIGF-------DATITSLFSPLLVGKRVVLLPEK--E 684
Cdd:PRK07786 180 MYTSGTTGRPKGAVLTHANLT------GQAMTCLRTNGADINSDVGFvgvplfhIAGIGSMLPGLLLGAPTVIYPLGafD 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 685 EIEALSALLQsdQNYSLVKITPAHLEMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVG 764
Cdd:PRK07786 254 PGQLLDVLEA--EKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 765 CCVYEVDEQTSLSGAIliGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrl 844
Cdd:PRK07786 332 TCMLLGEDAIRKLGSV--GKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF-------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 845 yKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAP--TSS 922
Cdd:PRK07786 402 -HSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAalTLE 480
|
490 500 510
....*....|....*....|....*....|...
gi 2129675820 923 ELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKV 955
Cdd:PRK07786 481 DLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
464-957 |
1.28e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 107.17 E-value: 1.28e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 464 DKCLHELFAAQVERTPNNIAVEFNHESL--TYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGA 541
Cdd:PRK12583 17 TQTIGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 542 YIPFDPTYPQERLGFMLE----------------------DAQIPILLTQQR--LVDKFVEHKTQIICLDRDLPE----- 592
Cdd:PRK12583 97 LVNINPAYRASELEYALGqsgvrwvicadafktsdyhamlQELLPGLAEGQPgaLACERLPELRGVVSLAPAPPPgflaw 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 593 ------------------NATLSIDNPVSnvtsenlayIIYTSGSTGKPKGTMIPHRGLVNylswctNAYALAQGYG--- 651
Cdd:PRK12583 177 helqargetvsrealaerQASLDRDDPIN---------IQYTSGTTGFPKGATLSHHNILN------NGYFVAESLGlte 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 652 -----APVQSSIGFDATITSL---------------FSPLLVGKRVvllpEKEEIEALsallqsdqnYSLVKITPAHLEM 711
Cdd:PRK12583 242 hdrlcVPVPLYHCFGMVLANLgcmtvgaclvypneaFDPLATLQAV----EEERCTAL---------YGVPTMFIAELDH 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 712 lnqmlPNHKG--VTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVvgccvyEVDEQTSLSGAI-----LIGR 784
Cdd:PRK12583 309 -----PQRGNfdLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETS------PVSLQTTAADDLerrveTVGR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 785 PIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQrfipnpfSDEPNSRLYkTGDLARYLPDGNIEYLGR 864
Cdd:PRK12583 378 TQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAE-------SIDEDGWMH-TGDLATMDEQGYVRIVGR 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 865 IDHQVkIRGFR-IELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIV--PKEQApTSSELRQFLQSKLPEYMIPSAF 941
Cdd:PRK12583 450 SKDMI-IRGGEnIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRlhPGHAA-SEEELREFCKARIAHFKVPRYF 527
|
570
....*....|....*.
gi 2129675820 942 VMLEVIPLTTHGKVDR 957
Cdd:PRK12583 528 RFVDEFPMTVTGKVQK 543
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
472-955 |
1.85e-23 |
|
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: 105.84 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 472 AAQVErtPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQ 551
Cdd:cd12118 13 AAAVY--PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 552 ERLGFMLEDAQIPILLtqqrlVDKFVEHKTQIICLDRDLPENATLSIDNPVSnvtsenlayIIYTSGSTGKPKGTMIPHR 631
Cdd:cd12118 91 EEIAFILRHSEAKVLF-----VDREFEYEDLLAEGDPDFEWIPPADEWDPIA---------LNYTSGTTGRPKGVVYHHR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 632 GLvnYLswctNAYALAQGYGAPvQSSI-------------GFDATITSlfspllVGKRVVLLPEKEEIEALSALLQSdqn 698
Cdd:cd12118 157 GA--YL----NALANILEWEMK-QHPVylwtlpmfhcngwCFPWTVAA------VGGTNVCLRKVDAKAIYDLIEKH--- 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 699 yslvKIT-----PAHLEML-NQMLPNHKGVTETRALIIGG----EALLGK--SLNFwrdnapktRIINEYGPTET--VVG 764
Cdd:cd12118 221 ----KVThfcgaPTVLNMLaNAPPSDARPLPHRVHVMTAGapppAAVLAKmeELGF--------DVTHVYGLTETygPAT 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 765 CCVYEvDEQTSLSG---AILIGRP-IANTQLYLLD--DKQKLVPigVP------GELYIGGAGVARGYLNRPELTQQRFi 832
Cdd:cd12118 289 VCAWK-PEWDELPTeerARLKARQgVRYVGLEEVDvlDPETMKP--VPrdgktiGEIVFRGNIVMKGYLKNPEATAEAF- 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 833 pnpfsdepNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYI 912
Cdd:cd12118 365 --------RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFV 436
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2129675820 913 VPKE-QAPTSSELRQFLQSKLPEYMIPSAFVMLEvIPLTTHGKV 955
Cdd:cd12118 437 ELKEgAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGKI 479
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
467-956 |
2.09e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 108.09 E-value: 2.09e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAV-EFNHESLTYAQLNAKSNQLAHHLQKLgVKPEVLVGICVERSLDMLIGILGILKAGGAYIPF 545
Cdd:PRK08633 617 LAEAWIDTAKRNWSRLAVaDSTGGELSYGKALTGALALARLLKRE-LKDEENVGILLPPSVAGALANLALLLAGKVPVNL 695
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 546 DPTYPQERLGFMLEDAQIPILLTQQRLVDK-----------------FVE------HKTQIIC---LDRDLPENATLSID 599
Cdd:PRK08633 696 NYTASEAALKSAIEQAQIKTVITSRKFLEKlknkgfdlelpenvkviYLEdlkakiSKVDKLTallAARLLPARLLKRLY 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 600 NPvsNVTSENLAYIIYTSGSTGKPKGTMIPHRglvNYLSwctNAYALAQGYGA----------PVQSSIGFDATitsLFS 669
Cdd:PRK08633 776 GP--TFKPDDTATIIFSSGSEGEPKGVMLSHH---NILS---NIEQISDVFNLrnddvilsslPFFHSFGLTVT---LWL 844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 670 PLLVGKRVVLLPEKEEIEALSALLqSDQNYSLVKITP-----------AHLEMLNQMlpnhkgvtetRALIIGGEALLGK 738
Cdd:PRK08633 845 PLLEGIKVVYHPDPTDALGIAKLV-AKHRATILLGTPtflrlylrnkkLHPLMFASL----------RLVVAGAEKLKPE 913
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 739 SLNFWRDNApKTRIINEYGPTET--VVGCCV-----YEVDEQT-SLSGAIliGRPIANTQLYLLD-DKQKLVPIGVPGEL 809
Cdd:PRK08633 914 VADAFEEKF-GIRILEGYGATETspVASVNLpdvlaADFKRQTgSKEGSV--GMPLPGVAVRIVDpETFEELPPGEDGLI 990
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 810 YIGGAGVARGYLNRPELTQQrfipnPFSDEPNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIEL----EEIESLL 885
Cdd:PRK08633 991 LIGGPQVMKGYLGDPEKTAE-----VIKDIDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLgaveEELAKAL 1065
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2129675820 886 AQHPLVNAVTVIarEDQPGDKRLVGYIVPKEQAPtsSELRQFL-QSKLPEYMIPSAFVMLEVIPLTTHGKVD 956
Cdd:PRK08633 1066 GGEEVVFAVTAV--PDEKKGEKLVVLHTCGAEDV--EELKRAIkESGLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
491-960 |
3.92e-23 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 104.96 E-value: 3.92e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 491 LTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQiPILL--- 567
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAE-PALVvcd 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 568 -TQQRLVDKFVEHK--TQIICLDRD----LPENA-TLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRglvNYLSw 639
Cdd:PRK07514 108 pANFAWLSKIAAAAgaPHVETLDADgtgsLLEAAaAAPDDFETVPRGADDLAAILYTSGTTGRSKGAMLSHG---NLLS- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 640 ctNAYALAQ--GYGA--------PVQSSIG-FDATITSLFSpllvGKRVVLLPEKEEIEALSALLQSD------------ 696
Cdd:PRK07514 184 --NALTLVDywRFTPddvlihalPIFHTHGlFVATNVALLA----GASMIFLPKFDPDAVLALMPRATvmmgvptfytrl 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 697 -QNYSLVKITPAHLEmlnqmlpnhkgvtetraLIIGGEA-LLGKSLNFWRDnapKT--RIINEYGPTETVVgccvyevde 772
Cdd:PRK07514 258 lQEPRLTREAAAHMR-----------------LFISGSApLLAETHREFQE---RTghAILERYGMTETNM--------- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 773 QTS-------LSGAIliGRPIANTQLYLLD-DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrl 844
Cdd:PRK07514 309 NTSnpydgerRAGTV--GFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF-------- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 845 YKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLV--NAVTVIAREDQpGDKrLVGYIVPKEQA-PTS 921
Cdd:PRK07514 379 FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVveSAVIGVPHPDF-GEG-VTAVVVPKPGAaLDE 456
|
490 500 510
....*....|....*....|....*....|....*....
gi 2129675820 922 SELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK07514 457 AAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
608-957 |
6.37e-23 |
|
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: 101.95 E-value: 6.37e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 608 ENLAYIIYTSGSTGKPKGTMIPHRGLV--------NYLSWCTNAYALAQgygAPVQSSIGFDATITSLFSpllvGKRVVL 679
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFavpdilqkEGLNWVVGDVTYLP---LPATHIGGLWWILTCLIH----GGLCVT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 680 LPEKEEIEALSALLQSDQNYSLVkITPAHLEMLNQMLPN-HKGVTETRALIIGGEALLGKSLNFWRDNaPKTRIINEYGP 758
Cdd:cd17635 74 GGENTTYKSLFKILTTNAVTTTC-LVPTLLSKLVSELKSaNATVPSLRLIGYGGSRAIAADVRFIEAT-GLTNTAQVYGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 759 TETVVGCCvyeVDEQTSLSGAILIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsd 838
Cdd:cd17635 152 SETGTALC---LPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 839 epnsrlyKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQA 918
Cdd:cd17635 227 -------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAEL 299
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2129675820 919 PTS--SELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDR 957
Cdd:cd17635 300 DENaiRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
460-1045 |
1.18e-22 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 106.02 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 460 EFPHDkcLHELFAAQVERTPNNIAVEFNHES------LTYAQLNAKSNQLAHHLQKLGVKPEVLVgICVERSLDMLIGIL 533
Cdd:PRK05691 6 ELPLT--LVQALQRRAAQTPDRLALRFLADDpgegvvLSYRDLDLRARTIAAALQARASFGDRAV-LLFPSGPDYVAAFF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 534 GILKAGGAYIPfdpTYP--------QERLGFMLEDAQIPILLTQQRLVDKFVE-------HKTQIICLDRDLPENATlSI 598
Cdd:PRK05691 83 GCLYAGVIAVP---AYPpesarrhhQERLLSIIADAEPRLLLTVADLRDSLLQmeelaaaNAPELLCVDTLDPALAE-AW 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 599 DNPvsNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVnylswcTNAYALAQGYGAPVqssiGFDATITSLfspllvgkrvv 678
Cdd:PRK05691 159 QEP--ALQPDDIAFLQYTSGSTALPKGVQVSHGNLV------ANEQLIRHGFGIDL----NPDDVIVSW----------- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 679 lLPEKEEIEALSALLQSDqnYS---LVKITPAHLemLNQMLPNHKGVTETRALIIGG--------------EALLGKSLN 741
Cdd:PRK05691 216 -LPLYHDMGLIGGLLQPI--FSgvpCVLMSPAYF--LERPLRWLEAISEYGGTISGGpdfayrlcservseSALERLDLS 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 742 FWRDNAPKTRIINE-----------------------YGPTETVV---------GCCVYEVDEQtSLS--------GAIL 781
Cdd:PRK05691 291 RWRVAYSGSEPIRQdslerfaekfaacgfdpdsffasYGLAEATLfvsggrrgqGIPALELDAE-ALArnraepgtGSVL 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 782 I--GRPIANTQLYLLDDKQKLV-PIGVPGELYIGGAGVARGYLNRPELTQQRFIpnpfsdEPNSRLY-KTGDLArYLPDG 857
Cdd:PRK05691 370 MscGRSQPGHAVLIVDPQSLEVlGDNRVGEIWASGPSIAHGYWRNPEASAKTFV------EHDGRTWlRTGDLG-FLRDG 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 858 NIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLV---NAVTVIAREDQPGD--------KRLVGYIVPKEQAPTSseLRQ 926
Cdd:PRK05691 443 ELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVvrkGRVAAFAVNHQGEEgigiaaeiSRSVQKILPPQALIKS--IRQ 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 927 FLQSKLPEymIPSAFVMLE--VIPLTTHGKVDRQA--LPQPDTSrLD----------TLKVEFIAPRDRLELKLANIWEN 992
Cdd:PRK05691 521 AVAEACQE--APSVVLLLNpgALPKTSSGKLQRSAcrLRLADGS-LDsyalfpalqaVEAAQTAASGDELQARIAAIWCE 597
|
650 660 670 680 690
....*....|....*....|....*....|....*....|....*....|...
gi 2129675820 993 LLNVHPIGIKDSFFELGGHSLLAVRLMAHINQEFGKNLALATLFQNPTIEKLA 1045
Cdd:PRK05691 598 QLKVEQVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFS 650
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
489-960 |
1.33e-22 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 103.77 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 489 ESLTYAQLNAKSNQLAHHL-QKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILL 567
Cdd:PLN02574 65 FSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAF 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 568 TQQRLVDKFVEHKTQIICL------DRDLPENAT----LSIDN---PVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLV 634
Cdd:PLN02574 145 TSPENVEKLSPLGVPVIGVpenydfDSKRIEFPKfyelIKEDFdfvPKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLI 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 635 NYL-------------SWCTNAYALAqgygAPVQSSIGFDATITSLFSpllVGKRVVLLPEKEEIEALSALLQSDQNYSL 701
Cdd:PLN02574 225 AMVelfvrfeasqyeyPGSDNVYLAA----LPMFHIYGLSLFVVGLLS---LGSTIVVMRRFDASDMVKVIDRFKVTHFP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 702 VkITPAHLEMLNQMLPNHKGVTETRALIIGGEA-LLGKSLNFWRDNAPKTRIINEYGPTE-TVVGCCVYEVDEQTSLSGa 779
Cdd:PLN02574 298 V-VPPILMALTKKAKGVCGEVLKSLKQVSCGAApLSGKFIQDFVQTLPHVDFIQGYGMTEsTAVGTRGFNTEKLSKYSS- 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 780 ilIGRPIANTQLYLLD-DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIpnpfsdepNSRLYKTGDLARYLPDGN 858
Cdd:PLN02574 376 --VGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTID--------KDGWLRTGDIAYFDEDGY 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 859 IEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSE-LRQFLQSKLPEYMI 937
Cdd:PLN02574 446 LYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEaVINYVAKQVAPYKK 525
|
490 500
....*....|....*....|...
gi 2129675820 938 PSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PLN02574 526 VRKVVFVQSIPKSPAGKILRREL 548
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
471-961 |
1.49e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 103.47 E-value: 1.49e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 471 FAAQV----ERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD 546
Cdd:PRK07788 51 FAGLVahaaRRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLN 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 547 PTY--PQ-------ERLGFMLEDAQIPILLTQqrLVDKFVEHKTQIICLDRDLPENATL-SIDNPVSNVTSENL------ 610
Cdd:PRK07788 131 TGFsgPQlaevaarEGVKALVYDDEFTDLLSA--LPPDLGRLRAWGGNPDDDEPSGSTDeTLDDLIAGSSTAPLpkppkp 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 611 -AYIIYTSGSTGKPKGTMIPH-------RGLVNYLSWCTN-AYALAqgygAPVQSSIGFDATITSLFspllVGKRVVLlP 681
Cdd:PRK07788 209 gGIVILTSGTTGTPKGAPRPEpsplaplAGLLSRVPFRAGeTTLLP----APMFHATGWAHLTLAMA----LGSTVVL-R 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 682 EKEEIEALSALLQSDQNYSLVkITPAhleMLNQML---PNHKGVTETRAL---IIGGEALlGKSLNfwrdnapkTRIINE 755
Cdd:PRK07788 280 RRFDPEATLEDIAKHKATALV-VVPV---MLSRILdlgPEVLAKYDTSSLkiiFVSGSAL-SPELA--------TRALEA 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 756 YGPtetvVGCCVY---EVDEQTSLSGAIL------IGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPel 826
Cdd:PRK07788 347 FGP----VLYNLYgstEVAFATIATPEDLaeapgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGR-- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 827 TQQRFipnpfsDEpnsrLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDK 906
Cdd:PRK07788 421 DKQII------DG----LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQ 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2129675820 907 RLVGYIVPKE-QAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALP 961
Cdd:PRK07788 491 RLRAFVVKAPgAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
467-960 |
2.44e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 102.66 E-value: 2.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD 546
Cdd:PRK06145 4 LSASIAFHARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPIN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 547 PTYPQERLGFMLEDAQIPILLTQQRLvDKFVEHKTQIICLDRDLPENATLSIDN-----PVSNVTSENLAYIIYTSGSTG 621
Cdd:PRK06145 84 YRLAADEVAYILGDAGAKLLLVDEEF-DAIVALETPKIVIDAAAQADSRRLAQGgleipPQAAVAPTDLVRLMYTSGTTD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 622 KPKGTMIPHrglvNYLSWCTNAYALAQGYGA--------PVQSSIGFDATITSLfspLLVGKRVVLLPEKEEIEALSALL 693
Cdd:PRK06145 163 RPKGVMHSY----GNLHWKSIDHVIALGLTAserllvvgPLYHVGAFDLPGIAV---LWVGGTLRIHREFDPEAVLAAIE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 694 QSdqnyslvKITPAHLE--MLNQML----PNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCV 767
Cdd:PRK06145 236 RH-------RLTCAWMApvMLSRVLtvpdRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 768 YEVDEQTSLSGAIliGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlyKT 847
Cdd:PRK06145 309 MEAGREIEKIGST--GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF---------RS 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 848 GDLArYLPDGNIEYL-GRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKE-QAPTSSELR 925
Cdd:PRK06145 378 GDVG-YLDEEGFLYLtDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPgATLTLEALD 456
|
490 500 510
....*....|....*....|....*....|....*
gi 2129675820 926 QFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK06145 457 RHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
613-956 |
2.93e-22 |
|
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: 99.68 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 613 IIYTSGSTGKPKGTMIPHRGLVnylswctnAYALAQGYGAPVQSSIGF--------DATITSLFSPLLVGKRVVLLPEKE 684
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALL--------AQALVLAVLQAIDEGTVFlnsgplfhIGTLMFTLATFHAGGTNVFVRRVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 685 EiEALSALLQSDqnyslvKITPAHL--EMLNQMlpnHKGVTETRALIIGGEALLGKSLnfWR-----DNAPKTRIINEYG 757
Cdd:cd17636 77 A-EEVLELIEAE------RCTHAFLlpPTIDQI---VELNADGLYDLSSLRSSPAAPE--WNdmatvDTSPWGRKPGGYG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 758 PTEtVVGCCVYEVDEQTSLSGAiliGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFipnpfs 837
Cdd:cd17636 145 QTE-VMGLATFAALGGGAIGGA---GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT------ 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 838 depNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKE- 916
Cdd:cd17636 215 ---RGGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPg 291
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 2129675820 917 QAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVD 956
Cdd:cd17636 292 ASVTEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
457-960 |
6.18e-22 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 101.88 E-value: 6.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 457 TKIEFPHDKCLHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHL-QKLGVKPEVLVGICVERSLDMLIGILGI 535
Cdd:PRK08751 17 AEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLlGELQLKKGDRVALMMPNCLQYPIATFGV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 536 LKAGGAYIPFDPTYPQERLGFMLEDAQIPILLT--------QQRLVDKFVEHKTQIICLDR-DLPENATLS--------- 597
Cdd:PRK08751 97 LRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVidnfgttvQQVIADTPVKQVITTGLGDMlGFPKAALVNfvvkyvkkl 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 598 -----IDN----------------PVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVnylswcTNAYALAQGYGAPVQS 656
Cdd:PRK08751 177 vpeyrINGairfrealalgrkhsmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLV------ANMQQAHQWLAGTGKL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 657 SIGFDATITSLfsPL-----LVGKRVVLLpekeEIEALSALLQSDQNY-SLVK---------ITPAHlEMLNQMLpNHKG 721
Cdd:PRK08751 251 EEGCEVVITAL--PLyhifaLTANGLVFM----KIGGCNHLISNPRDMpGFVKelkktrftaFTGVN-TLFNGLL-NTPG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 722 VTE----TRALIIGGEALLGKSL-NFWRDNAPKTrIINEYGPTETVVGCCVYEVDEQtSLSGAIliGRPIANTQLYLLDD 796
Cdd:PRK08751 323 FDQidfsSLKMTLGGGMAVQRSVaERWKQVTGLT-LVEAYGLTETSPAACINPLTLK-EYNGSI--GLPIPSTDACIKDD 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 797 KQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRI 876
Cdd:PRK08751 399 AGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW--------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 877 ELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVD 956
Cdd:PRK08751 471 YPNEIEDVIAMMPGVLEVAAVGVPDEKSGEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKIL 550
|
....
gi 2129675820 957 RQAL 960
Cdd:PRK08751 551 RREL 554
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
468-960 |
1.62e-21 |
|
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: 100.64 E-value: 1.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 468 HELFAAQVERTPNNIAVEFNHE-----SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAY 542
Cdd:cd05968 64 EQLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIV 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 543 IPFDPTYPQERLGFMLEDAQIPILLTQQ------RLV------DKFVEHKTQI--ICLDRDLPENATLSIDNPVS----- 603
Cdd:cd05968 144 VPIFSGFGKEAAATRLQDAEAKALITADgftrrgREVnlkeeaDKACAQCPTVekVVVVRHLGNDFTPAKGRDLSydeek 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 604 --------NVTSENLAYIIYTSGSTGKPKGTMIPHRGLVnyLSWCTNAY---ALAQGYGAPVQSSIGFDATITSLFSPLL 672
Cdd:cd05968 224 etagdgaeRTESEDPLMIIYTSGTTGKPKGTVHVHAGFP--LKAAQDMYfqfDLKPGDLLTWFTDLGWMMGPWLIFGGLI 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 673 VGKRVVL---LPEKEEIEALSallqsdqnyslvkitpahlEMLNQMLPNHKGVTET--RALIIGGEA-----------LL 736
Cdd:cd05968 302 LGATMVLydgAPDHPKADRLW-------------------RMVEDHEITHLGLSPTliRALKPRGDApvnahdlsslrVL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 737 GKSLNFW-------------RDNAPktrIINEYGPTET---VVGCCVYEVDEQTSLSGailigrPIANTQLYLLDDKQKL 800
Cdd:cd05968 363 GSTGEPWnpepwnwlfetvgKGRNP---IINYSGGTEIsggILGNVLIKPIKPSSFNG------PVPGMKADVLDESGKP 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 801 VPIGVpGELYIGGA--GVARGYLNRPEltqqRFIPNPFSDEPNsrLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIEL 878
Cdd:cd05968 434 ARPEV-GELVLLAPwpGMTRGFWRDED----RYLETYWSRFDN--VWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGP 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 879 EEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQ-APT---SSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGK 954
Cdd:cd05968 507 AEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVLKPGvTPTealAEELMERVADELGKPLSPERILFVKDLPKTRNAK 586
|
....*.
gi 2129675820 955 VDRQAL 960
Cdd:cd05968 587 VMRRVI 592
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
459-960 |
1.36e-20 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 97.36 E-value: 1.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 459 IEFPHDKCLHE-LF--AAQVERTPNNIAVEfNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGI 535
Cdd:PLN02246 17 IYIPNHLPLHDyCFerLSEFSDRPCLIDGA-TGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 536 LKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQRLVDKF----VEHKTQIICLDRDlPEN----ATLSIDN----PVS 603
Cdd:PLN02246 96 SRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYVDKLkglaEDDGVTVVTIDDP-PEGclhfSELTQADenelPEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 604 NVTSENLAYIIYTSGSTGKPKGTMIPHRGLVnylswcTNAYALAQGyGAPvqsSIGFDAT-----------ITSLFSPLL 672
Cdd:PLN02246 175 EISPDDVVALPYSSGTTGLPKGVMLTHKGLV------TSVAQQVDG-ENP---NLYFHSDdvilcvlpmfhIYSLNSVLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 673 VGKRV---VLLPEKEEIealSALLQSDQNYslvKIT------PAHLEML-NQMLPNHKgVTETRaLIIGGEALLGKSL-N 741
Cdd:PLN02246 245 CGLRVgaaILIMPKFEI---GALLELIQRH---KVTiapfvpPIVLAIAkSPVVEKYD-LSSIR-MVLSGAAPLGKELeD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 742 FWRDNAPKTRIINEYGPTE--TVVGCCVYEVDEQTSL-SGAilIGRPIANTQLYLLD-DKQKLVPIGVPGELYIGGAGVA 817
Cdd:PLN02246 317 AFRAKLPNAVLGQGYGMTEagPVLAMCLAFAKEPFPVkSGS--CGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 818 RGYLNRPELTqQRFIpnpfsDEpNSRLYkTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVI 897
Cdd:PLN02246 395 KGYLNDPEAT-ANTI-----DK-DGWLH-TGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVV 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129675820 898 AREDQPGDKRLVGYIV-PKEQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PLN02246 467 PMKDEVAGEVPVAFVVrSNGSEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
489-926 |
3.38e-19 |
|
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: 92.51 E-value: 3.38e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 489 ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLT 568
Cdd:cd05914 6 EPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 569 QqrlvdkfvehktqiicldrdlpenatlsiDNpvsnvtsENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSWCtNAYALAq 648
Cdd:cd05914 86 S-----------------------------DE-------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGV-KEVVLL- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 649 GYGAPVQSSIGFDAT---ITSLFSPLLVGKRVVLL----------PEKEEIE---ALSALLQSDQNYSLVKITPAHLEML 712
Cdd:cd05914 128 GKGDKILSILPLHHIyplTFTLLLPLLNGAHVVFLdkipsakiiaLAFAQVTptlGVPVPLVIEKIFKMDIIPKLTLKKF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 713 NQML---PNH--------KGVTET-----RALIIGGEALLGKSLNFWRD-NAPktrIINEYGPTETVVGCCvYEVDEQTS 775
Cdd:cd05914 208 KFKLakkINNrkirklafKKVHEAfggniKEFVIGGAKINPDVEEFLRTiGFP---YTIGYGMTETAPIIS-YSPPNRIR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 776 LSGAiliGRPIANTQLYLLDDKqklvPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARYLP 855
Cdd:cd05914 284 LGSA---GKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW--------FHTGDLGKIDA 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2129675820 856 DGNIEYLGRIDHQ-VKIRGFRIELEEIESLLAQHPLVNAVTVIAREdqpgdKRLVGYIVPKEQAPTSSELRQ 926
Cdd:cd05914 349 EGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQE-----KKLVALAYIDPDFLDVKALKQ 415
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
6-323 |
3.71e-19 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHxxxD motif, a few such as Monascus pilosus lovastatin nonaketide synthase MokA have a non-canonical HRxxxD motif in the C-domain and are unable to catalyze amide-bond formation. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380455 [Multi-domain] Cd Length: 421 Bit Score: 91.75 E-value: 3.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 6 RISPQQKHLWLQQK--DNYQAY-CTqIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGMNIPFQSISDAPTY--N 80
Cdd:cd19532 3 PMSFGQSRFWFLQQylEDPTTFnVT-FSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDGEPMQGVLASSPLrlE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 81 HISLAEydwsrlSSQVQKAkidtlFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAY 160
Cdd:cd19532 82 HVQISD------EAEVEEE-----FERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 161 taclDGEEISEEVMQYADVSEWLNELLESEDTETARNYWQQQ--DISSVLNL--------RIPFEIKNDHQSSGEISfap 230
Cdd:cd19532 151 ----NGQPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEfsTLPEPLPLlpfakvksRPPLTRYDTHTAERRLD--- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 231 qslclamnRDTVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLED 310
Cdd:cd19532 224 --------AALAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDP 295
|
330
....*....|...
gi 2129675820 311 ALKFSELMERVSE 323
Cdd:cd19532 296 SQTFADVLKETRD 308
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
609-957 |
5.22e-19 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 89.77 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 609 NLAYIIYTSGSTGKPKGTMIPHRglvnylSW-----CTNAYALAQGYGA-----PVQSSIGFDATITSLFSpllvGKRVV 678
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSER------SWiesfvCNEDLFNISGEDAilapgPLSHSLFLYGAISALYL----GGTFI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 679 LLPEKEEIEALSALLQsdQNYSLVKITPAhleMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGP 758
Cdd:cd17633 71 GQRKFNPKSWIRKINQ--YNATVIYLVPT---MLQALARTLEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 759 TETvvGCCVYEVDEQTSLSGAilIGRPIANTQLYLLDDKQklvpiGVPGELYIGGAGVARGYLNRPELTQqrfipnpfsD 838
Cdd:cd17633 146 SEL--SFITYNFNQESRPPNS--VGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNP---------D 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 839 EPnsrlYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVgYIVPKEQA 918
Cdd:cd17633 208 GW----MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAV-ALYSGDKL 282
|
330 340 350
....*....|....*....|....*....|....*....
gi 2129675820 919 pTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDR 957
Cdd:cd17633 283 -TYKQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
462-960 |
8.10e-19 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 91.96 E-value: 8.10e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 462 PHDKCLHELFAAQVERTPNNIA-VE-FNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAG 539
Cdd:PLN02330 25 PDKLTLPDFVLQDAELYADKVAfVEaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 540 GAYIPFDPTYPQERLGFMLEDAQIPILLTQQRLVDKFVEHKTQIICLD----------RDLPENATLSIDNPVSNVTSE- 608
Cdd:PLN02330 105 GVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLGLPVIVLGeekiegavnwKELLEAADRAGDTSDNEEILQt 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 609 NLAYIIYTSGSTGKPKGTMIPHRGLVNYLswCTNAYALAQgygapvqSSIGFDAT-----------ITSLFSPLLVGK-R 676
Cdd:PLN02330 185 DLCALPFSSGTTGISKGVMLTHRNLVANL--CSSLFSVGP-------EMIGQVVTlglipffhiygITGICCATLRNKgK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 677 VVLLPEKEEIEALSALLQSDQNYSLVkITPAHLEMLNQMLPNHKGVTET--RALIIGGEALLGKSLNFWRDNAPKTRIIN 754
Cdd:PLN02330 256 VVVMSRFELRTFLNALITQEVSFAPI-VPPIILNLVKNPIVEEFDLSKLklQAIMTAAAPLAPELLTAFEAKFPGVQVQE 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 755 EYGPTE-TVVGCCVYEVDEQTSLSGAILIGRPIANTQLYLLD-DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFi 832
Cdd:PLN02330 335 AYGLTEhSCITLTHGDPEKGHGIAKKNSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTI- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 833 pnpfsdEPNSRLYkTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYI 912
Cdd:PLN02330 414 ------DEDGWLH-TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACV 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2129675820 913 VPKEQAPTSSE-LRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PLN02330 487 VINPKAKESEEdILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
474-960 |
9.00e-19 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 91.93 E-value: 9.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 474 QVERTPNNIAVEFNHES------LTYAQLNAKSNQLAHHLQKLGVKPEVLVGI----CVERSLDML----IGILGILKAG 539
Cdd:TIGR02188 66 HLEARPDKVAIIWEGDEpgevrkITYRELHREVCRFANVLKSLGVKKGDRVAIympmIPEAAIAMLacarIGAIHSVVFG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 540 GayipFDPTYPQERLgfmlEDAQIPILLTQ------------QRLVDKFVEHKTQII--CL--------------DRDLP 591
Cdd:TIGR02188 146 G----FSAEALADRI----NDAGAKLVITAdeglrggkviplKAIVDEALEKCPVSVehVLvvrrtgnpvvpwveGRDVW 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 592 EN---ATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTM-----------IPHRGLVNY----LSWCTnayalaqgygap 653
Cdd:TIGR02188 218 WHdlmAKASAYCEPEPMDSEDPLFILYTSGSTGKPKGVLhttggyllyaaMTMKYVFDIkdgdIFWCT------------ 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 654 vqSSIGFdatITS----LFSPLLVGKRVVLLpekeeiEALSALLQSDQNYSLV---KIT-----PAHLEMLNQMLPNHKG 721
Cdd:TIGR02188 286 --ADVGW---ITGhsyiVYGPLANGATTVMF------EGVPTYPDPGRFWEIIekhKVTifytaPTAIRALMRLGDEWVK 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 722 VTETRAL-IIG--GEALLGKSLNFWRDNAPKTR--IINEYGPTETvvGCCVYevdeqTSLSGAILI-----GRPIANTQL 791
Cdd:TIGR02188 355 KHDLSSLrLLGsvGEPINPEAWMWYYKVVGKERcpIVDTWWQTET--GGIMI-----TPLPGATPTkpgsaTLPFFGIEP 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 792 YLLDDKQKLVPI-GVPGELYIGGA--GVARGYLNRPEltqqRFIPNPFSDEPNsrLYKTGDLARYLPDGNIEYLGRIDHQ 868
Cdd:TIGR02188 428 AVVDEEGNPVEGpGEGGYLVIKQPwpGMLRTIYGDHE----RFVDTYFSPFPG--YYFTGDGARRDKDGYIWITGRVDDV 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 869 VKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSS----ELRQFLQSKLPEYMIPSAFVML 944
Cdd:TIGR02188 502 INVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDelrkELRKHVRKEIGPIAKPDKIRFV 581
|
570
....*....|....*.
gi 2129675820 945 EVIPLTTHGKVDRQAL 960
Cdd:TIGR02188 582 PGLPKTRSGKIMRRLL 597
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
4-432 |
1.16e-18 |
|
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: 90.52 E-value: 1.16e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 4 LIRISPQQKHLWL--QQKDNYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGmNIPFQSI--SDAPTY 79
Cdd:cd19539 1 RIPLSFAQERLWFidQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDG-GVPRQEIlpPGPAPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 80 NHISLaeydwSRLSSQVQKAkIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRA 159
Cdd:cd19539 80 EVRDL-----SDPDSDRERR-LEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 160 YTACLDGE--EISEEVMQYADVSEWLNELLESEDTETARNYWQQQdissvLNLRIPFEIKNDHQSSGEISFAPQSLCLAM 237
Cdd:cd19539 154 YAARRKGPaaPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRR-----LRGAEPTALPTDRPRPAGFPYPGADLRFEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 238 NRDTVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDALKFSEL 317
Cdd:cd19539 229 DAELVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 318 MERVSESL------------RFVKKWQEyfnwenfistnEKFAAR-PFFPFCFDFTQQSQSY--VNGNIAFSEYKKSANI 382
Cdd:cd19539 309 IARVRKALvdaqrhqelpfqQLVAELPV-----------DRDAGRhPLVQIVFQVTNAPAGEleLAGGLSYTEGSDIPDG 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 2129675820 383 DKFQIKLSSGYSQDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNP 432
Cdd:cd19539 378 AKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
503-971 |
1.37e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 91.40 E-value: 1.37e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 503 LAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQRLVDKFVEHKTQ 582
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSWYEELQND 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 583 II------------CLDRDLPENATLSID------------NPVSnvTSENLAYIIYTSGSTGKPKGTMIPHRGLVnyls 638
Cdd:PLN02860 125 RLpslmwqvflespSSSVFIFLNSFLTTEmlkqralgttelDYAW--APDDAVLICFTSGTTGRPKGVTISHSALI---- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 639 wctnAYALAQ----GYG--------APVqSSIGfdaTITSLFSPLLVGKRVVLLPEKEEIEALSALLQsdQNYSLVKITP 706
Cdd:PLN02860 199 ----VQSLAKiaivGYGeddvylhtAPL-CHIG---GLSSALAMLMVGACHVLLPKFDAKAALQAIKQ--HNVTSMITVP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 707 AHLEML---NQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTET---------------VVGCCVY 768
Cdd:PLN02860 269 AMMADLislTRKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcssltfmtlhdptleSPKQTLQ 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 769 EVDEQTSLS----GAILIGRPIANTQLYLLDDKQKLVpigvpGELYIGGAGVARGYLNRPELTQqrfipnpfSDEPNSRL 844
Cdd:PLN02860 349 TVNQTKSSSvhqpQGVCVGKPAPHVELKIGLDESSRV-----GRILTRGPHVMLGYWGQNSETA--------SVLSNDGW 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 845 YKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQpgdkRLVGYIVP---------- 914
Cdd:PLN02860 416 LDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDS----RLTEMVVAcvrlrdgwiw 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2129675820 915 ---------KEQAPTSSELRQFLQSK-LPEYMIPSAFVMLE-VIPLTTHGKVDRQALPQPDTSRLDTL 971
Cdd:PLN02860 492 sdnekenakKNLTLSSETLRHHCREKnLSRFKIPKLFVQWRkPFPLTTTGKIRRDEVRREVLSHLQSL 559
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
476-959 |
1.57e-18 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 91.34 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 476 ERTPNNIAVEfnhesLTYAQLNAKSNQLAHHLQKLgVKPEVLVGICVERSLDMLIGILGILKAGGAYIP-FDPTYP--QE 552
Cdd:PRK12476 59 SHSAAGCAVE-----LTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPlFAPELPghAE 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 553 RLGFMLEDAQIPILLTQQ---RLVDKFVE-----HKTQIICLDrDLPENATLSIDnPVsNVTSENLAYIIYTSGSTGKPK 624
Cdd:PRK12476 133 RLDTALRDAEPTVVLTTTaaaEAVEGFLRnlprlRRPRVIAID-AIPDSAGESFV-PV-ELDTDDVSHLQYTSGSTRPPV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 625 GTMIPHRGL----------VNYLSWCTNAYALAQGYGAPVQSSIGFDATI---TSLFSPLLVGKRvvllPEKeEIEALSA 691
Cdd:PRK12476 210 GVEITHRAVgtnlvqmilsIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYgghSTLMSPTAFVRR----PQR-WIKALSE 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 692 llQSDQNYSLVKITPAHLEMLNQM-LPNHKGVTETR--ALIIGGEALLGKSLN-----FWRDNAPKTRIINEYGPTETVV 763
Cdd:PRK12476 285 --GSRTGRVVTAAPNFAYEWAAQRgLPAEGDDIDLSnvVLIIGSEPVSIDAVTtfnkaFAPYGLPRTAFKPSYGIAEATL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 764 ----------GCCVYEVDEQTSLSGAILI-------------GRPIANTQLYLLD-DKQKLVPIGVPGELYIGGAGVARG 819
Cdd:PRK12476 363 fvatiapdaePSVVYLDREQLGAGRAVRVaadapnavahvscGQVARSQWAVIVDpDTGAELPDGEVGEIWLHGDNIGRG 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 820 YLNRPELTQQRF---IPNPFSD-------EPNSRLYKTGDLARYLpDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQ-H 888
Cdd:PRK12476 443 YWGRPEETERTFgakLQSRLAEgshadgaADDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEaS 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2129675820 889 PLVNAVTVIAREdQPGDKRLVGYIVPKEQAPTSSELRQFLQSKL-----PEYMIPSA---FVMLEVIPLTTHGKVDRQA 959
Cdd:PRK12476 522 PMVRRGYVTAFT-VPAEDNERLVIVAERAAGTSRADPAPAIDAIraavsRRHGLAVAdvrLVPAGAIPRTTSGKLARRA 599
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
479-959 |
1.79e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 90.77 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 479 PNNIAVEFN---------HESLTYAQLNAKSNQLAHHLQKLGVKPEVLVgICVERSLDMLIGILGILKAGGAYIPFDPty 549
Cdd:PRK05850 15 PDDAAFTFIdyeqdpagvAETLTWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQAGLIAVPLSV-- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 550 PQ-----ERLGFMLEDAQIPILLTQQRLVDKFVEHKTQ--------IICLDR-DLPENATLSIDNpvsnVTSENLAYIIY 615
Cdd:PRK05850 92 PQggahdERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPqpgqsappVIEVDLlDLDSPRGSDARP----RDLPSTAYLQY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 616 TSGSTGKPKGTMIPHRGL-VNYLSWCTNAYAlAQGYGAPVqssigfDATITS-------------LFSPLLVGKRVVLL- 680
Cdd:PRK05850 168 TSGSTRTPAGVMVSHRNViANFEQLMSDYFG-DTGGVPPP------DTTVVSwlpfyhdmglvlgVCAPILGGCPAVLTs 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 681 PEkeeiealsALLQSdqnyslvkitPAHLeMlnQMLPNHKG-------------VTET-------------RALIIGGEA 734
Cdd:PRK05850 241 PV--------AFLQR----------PARW-M--QLLASNPHafsaapnfafelaVRKTsdddmagldlggvLGIISGSER 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 735 LLGKSLN-----FWRDNAPKTRIINEYGPTETVVGCCVYEVDEQ-------------------TSLSGAILIGRPIANTQ 790
Cdd:PRK05850 300 VHPATLKrfadrFAPFNLRETAIRPSYGLAEATVYVATREPGQPpesvrfdyeklsaghakrcETGGGTPLVSYGSPRSP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 791 LYLLDDKQKLV--PIGVPGELYIGGAGVARGYLNRPELTQQRF---IPNPFSDEPNSRLYKTGDLArYLPDGNIEYLGRI 865
Cdd:PRK05850 380 TVRIVDPDTCIecPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPGTPEGPWLRTGDLG-FISEGELFIVGRI 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 866 DHQVKIRGFRIELEEIESLLAQ--HPLVNAVTViaredqPGD--KRLVGYIVPKEQAPTSSELRQFLQSKLPEymIPSA- 940
Cdd:PRK05850 459 KDLLIVDGRNHYPDDIEATIQEitGGRVAAISV------PDDgtEKLVAIIELKKRGDSDEEAMDRLRTVKRE--VTSAi 530
|
570 580 590
....*....|....*....|....*....|.
gi 2129675820 941 ----------FVMLE--VIPLTTHGKVDRQA 959
Cdd:PRK05850 531 skshglsvadLVLVApgSIPITTSGKIRRAA 561
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
470-963 |
2.07e-18 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 90.59 E-value: 2.07e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 470 LFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTY 549
Cdd:PRK13382 48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 550 PQERLGFMLEDAQIPILLTQQRLVDkfvehktqiiCLDRDLPE--NATLSIDNP--VSNVTSENLA-------------- 611
Cdd:PRK13382 128 AGPALAEVVTREGVDTVIYDEEFSA----------TVDRALADcpQATRIVAWTdeDHDLTVEVLIaahagqrpeptgrk 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 612 --YIIYTSGSTGKPKGTMIPHRGLVNYLS-------W-CTNAYALAqgygAPVQSSIGF-DATITSLFSPLLVGKRvvll 680
Cdd:PRK13382 198 grVILLTSGTTGTPKGARRSGPGGIGTLKaildrtpWrAEEPTVIV----APMFHAWGFsQLVLAASLACTIVTRR---- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 681 peKEEIEALSALLQSDQNYSLVkITPAhleMLNQMLpnhKGVTETRAliiggeALLGKSLNFWRDNAPKTR--------- 751
Cdd:PRK13382 270 --RFDPEATLDLIDRHRATGLA-VVPV---MFDRIM---DLPAEVRN------RYSGRSLRFAAASGSRMRpdvviafmd 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 752 -----IINEYGPTETVVGCCVYEVDEQTSLSGAiliGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYlnrpel 826
Cdd:PRK13382 335 qfgdvIYNNYNATEAGMIATATPADLRAAPDTA---GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY------ 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 827 tqqrfipNPFSD-EPNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGD 905
Cdd:PRK13382 406 -------TSGSTkDFHDGFMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYG 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2129675820 906 KRLVGYIVPKEQAP-TSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALPQP 963
Cdd:PRK13382 479 QRLAAFVVLKPGASaTPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
486-960 |
4.50e-18 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 90.09 E-value: 4.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 486 FNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPI 565
Cdd:PRK06060 26 YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPAL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 566 LLTQQRLVDKFvehKTQIICLDRDLPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYL-SWCTNAY 644
Cdd:PRK06060 106 VVTSDALRDRF---QPSRVAEAAELMSEAARVAPGGYEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVdAMCRKAL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 645 ALAQGYGAPVQSSIGFDATI-TSLFSPLLVGKRVVL--LPEKEEIEA-LSALLQSDQNYSLvkitPAHL-EMLNQMLPNh 719
Cdd:PRK06060 183 RLTPEDTGLCSARMYFAYGLgNSVWFPLATGGSAVInsAPVTPEAAAiLSARFGPSVLYGV----PNFFaRVIDSCSPD- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 720 kGVTETRALIIGGEALlgkslnfwrDNAPKTRIINEYGPTETVVGCCVYEVDeQTSLSGAI------LIGRPIANTQLYL 793
Cdd:PRK06060 258 -SFRSLRCVVSAGEAL---------ELGLAERLMEFFGGIPILDGIGSTEVG-QTFVSNRVdewrlgTLGRVLPPYEIRV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 794 LDDKQKLVPIGVPGELYIGGAGVARGYLNRPE--LTQQRFIpnpfsdepNSRlyktgDLARYLPDGNIEYLGRIDHQVKI 871
Cdd:PRK06060 327 VAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWL--------DTR-----DRVCIDSDGWVTYRCRADDTEVI 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 872 RGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQA----PTSSELRQFLQSKLPEYMIPSAFVMLEVI 947
Cdd:PRK06060 394 GGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGAtidgSVMRDLHRGLLNRLSAFKVPHRFAVVDRL 473
|
490
....*....|...
gi 2129675820 948 PLTTHGKVDRQAL 960
Cdd:PRK06060 474 PRTPNGKLVRGAL 486
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
492-960 |
5.91e-18 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 89.04 E-value: 5.91e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 492 TYAQLNAKSNQLAHHLQKLGVKPEVLVGIC---VERSLDMLIGILGIlkaGGAYIPFDPTYPQERLGFMLEDAQ------ 562
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIINHAEdrvvit 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 563 ----IPILltqQRLVDKFVEHKTQIICLDRD-LPENatlSIDNPVS--------------NVTSENLAY-IIYTSGSTGK 622
Cdd:PRK06018 118 dltfVPIL---EKIADKLPSVERYVVLTDAAhMPQT---TLKNAVAyeewiaeadgdfawKTFDENTAAgMCYTSGTTGD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 623 PKGTMIPHRGLVNYLSWCTNAYALaqGYGA-----PVQSSigFDATITSL-FSPLLVGKRVVLLPEKEEIEALSALLQSD 696
Cdd:PRK06018 192 PKGVLYSHRSNVLHALMANNGDAL--GTSAadtmlPVVPL--FHANSWGIaFSAPSMGTKLVMPGAKLDGASVYELLDTE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 697 QnyslVKITPA----------HLEMLNQMLPNHKGVtetralIIGGEALLGKSLNFWRDNAPKTRiiNEYGPTETV-VGC 765
Cdd:PRK06018 268 K----VTFTAGvptvwlmllqYMEKEGLKLPHLKMV------VCGGSAMPRSMIKAFEDMGVEVR--HAWGMTEMSpLGT 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 766 CVYEVDEQTSLSGAILI------GRPIANTQLYLLDDKQKLVPIG--VPGELYIGGAGVARGYLnrpeltqqRFIPNPFS 837
Cdd:PRK06018 336 LAALKPPFSKLPGDARLdvlqkqGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYY--------RVDGEILD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 838 DEPnsrLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKE- 916
Cdd:PRK06018 408 DDG---FFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPg 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2129675820 917 QAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK06018 485 ETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
491-919 |
6.23e-18 |
|
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: 88.29 E-value: 6.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 491 LTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGayipfdptypqerlgfmledaqIPILltqq 570
Cdd:cd05910 3 LSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGA----------------------VPVL---- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 571 rlVDKFVEHKTQIICLDRDLPEnATLSI---DNPvsnvtsenlAYIIYTSGSTGKPKGTMIPHRGLVNYLSwctnayALA 647
Cdd:cd05910 57 --IDPGMGRKNLKQCLQEAEPD-AFIGIpkaDEP---------AAILFTSGSTGTPKGVVYRHGTFAAQID------ALR 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 648 QGYGaPVQSSI---GFdaTITSLFSPLLVGKRVV-----LLPEKEEIEALSALLQSDQ------NYSLVKITPAHLEMLN 713
Cdd:cd05910 119 QLYG-IRPGEVdlaTF--PLFALFGPALGLTSVIpdmdpTRPARADPQKLVGAIRQYGvsivfgSPALLERVARYCAQHG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 714 QMLPNHKGVTETRA-LIIGGEALLGKSLNfwrdnaPKTRIINEYGPTETVVGCCV------YEVDEQTSLSGAILIGRPI 786
Cdd:cd05910 196 ITLPSLRRVLSAGApVPIALAARLRKMLS------DEAEILTPYGATEALPVSSIgsrellATTTAATSGGAGTCVGRPI 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 787 ANTQLYLLD---------DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPnpfsDEPNSRLYKTGDLARYLPDG 857
Cdd:cd05910 270 PGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKID----DNSEGFWHRMGDLGYLDDEG 345
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129675820 858 NIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVnavtviaredqpgdKR--LVGYIVPKEQAP 919
Cdd:cd05910 346 RLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGV--------------RRsaLVGVGKPGCQLP 395
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
613-957 |
8.39e-18 |
|
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: 86.17 E-value: 8.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 613 IIYTSGSTGKPKGTMIPHRGLVnylswctnaYALAQgygapVQSSIGFDAT-----------ITSLFSPLLV----GKRV 677
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLI---------AANLQ-----LIHAMGLTEAdvylnmlplfhIAGLNLALATfhagGANV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 678 VLlpEKEEIEALSALLQSDQNYSLVKITPahleMLNQMLPNH----------KGVT--ETRALIIGGEALLGKslNFWrd 745
Cdd:cd17637 71 VM--EKFDPAEALELIEEEKVTLMGSFPP----ILSNLLDAAeksgvdlsslRHVLglDAPETIQRFEETTGA--TFW-- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 746 napktriiNEYGPTETVVGCCVYEVDEQtslSGAIliGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPE 825
Cdd:cd17637 141 --------SLYGQTETSGLVTLSPYRER---PGSA--GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 826 LTQQRFipnpfsdepnsR--LYKTGDLARYLPDGNIEYLGRIDHQ--VKIRGFRIELEEIESLLAQHPLVNAVTVIARED 901
Cdd:cd17637 208 LTAYTF-----------RngWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPD 276
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2129675820 902 QP---GDKRLVgyIVPKEQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDR 957
Cdd:cd17637 277 PKwgeGIKAVC--VLKPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
612-956 |
8.60e-18 |
|
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: 86.67 E-value: 8.60e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 612 YIIYTSGSTGKPKGTMIPHRGlvnylSWCTNAYALAQGYGAPVQSSIGFDATIT-------------------SLFSPLL 672
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQED-----IFRMLMGGADFGTGEFTPSEDAHKAAAAaagtvmfpapplmhgtgswTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 673 VGKRVVLLPEKEEIEALSALLQSDQNYSLVKITPAHLEMLNQML--PNHKGVTETRALIIGGeALLGKSL-NFWRDNAPK 749
Cdd:cd05924 82 GGQTVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMARPLIDALrdAGPYDLSSLFAISSGG-ALLSPEVkQGLLELVPN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 750 TRIINEYGPTETVVGCCVYeVDEQTSLSGAiligRPIANTQLYLLDDKQKLVPIGVPGELYIGGAG-VARGYLNRPELTQ 828
Cdd:cd05924 161 ITLVDAFGSSETGFTGSGH-SAGSGPETGP----FTRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 829 QRFipnPFSDepNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRL 908
Cdd:cd05924 236 ETF---PEVD--GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEV 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2129675820 909 VGYIVPKEQA-PTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVD 956
Cdd:cd05924 311 VAVVQLREGAgVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
1073-1321 |
8.73e-18 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 84.13 E-value: 8.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1073 FCLPGGGGNVLYLHELARDLGSEQTFYGLQAPG---LNGEsDPLTSVEEMAAYYIQAIQSvQPEGPYFLGGHSFGGIVAY 1149
Cdd:COG3208 10 FCFPYAGGSASAYRPWAAALPPDIEVLAVQLPGrgdRLGE-PPLTSLEELADDLAEELAP-LLDRPFALFGHSMGALLAF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1150 EIAQQLVKSGHE--VALVAI-LDAPAPVASDKPIYiDVDDATRLTEtarlIERWAGkslnISYEILQPLELdaqLEYlke 1226
Cdd:COG3208 88 ELARRLERRGRPlpAHLFVSgRRAPHLPRRRRPLH-DLSDAELLAE----LRRLGG----TPEEVLADPEL---LEL--- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1227 qliavgLLPTgtetkqVRGLVQVFETnlqasikYSPQEVYPHR--LTLLRARE---VNAEDAAlltelrqdpawGWGQFS 1301
Cdd:COG3208 153 ------FLPI------LRADFRLLET-------YRYTPGPPLDcpITALGGDDdplVSPEELA-----------AWREHT 202
|
250 260
....*....|....*....|
gi 2129675820 1302 TEKVDIHIVPGDHMTMMTQP 1321
Cdd:COG3208 203 TGPFRLRVFPGGHFFLRDHP 222
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
464-955 |
1.07e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 88.33 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 464 DKCLHELFAAQVERTPNNIAVEFNHESL--TYAQLNAKSNQLAHHLQKLGVKPEVLVGI----CVERSLDMLigilGILK 537
Cdd:PRK08315 15 EQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIwapnVPEWVLTQF----ATAK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 538 AGGAYIPFDPTYPQERL----------------GF-------MLEDAqIPILLTQQR--LVDKFVEHKTQIICLDRDLPE 592
Cdd:PRK08315 91 IGAILVTINPAYRLSELeyalnqsgckaliaadGFkdsdyvaMLYEL-APELATCEPgqLQSARLPELRRVIFLGDEKHP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 593 N-----------------------ATLSIDNPVSnvtsenlayIIYTSGSTGKPKGTMIPHRGLVNylswctNAY--ALA 647
Cdd:PRK08315 170 GmlnfdellalgravddaelaarqATLDPDDPIN---------IQYTSGTTGFPKGATLTHRNILN------NGYfiGEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 648 QGYGA------PVQ------SSIGFDATITS---------LFSPLLVGKRVvllpEKEEIEALsallqsdqnYSLvkitP 706
Cdd:PRK08315 235 MKLTEedrlciPVPlyhcfgMVLGNLACVTHgatmvypgeGFDPLATLAAV----EEERCTAL---------YGV----P 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 707 AhleMLNQMLpNHKGVTET-----RALIIGGeallgkslnfwrdnAP------KtRIINE---------YGPTETVVGCC 766
Cdd:PRK08315 298 T---MFIAEL-DHPDFARFdlsslRTGIMAG--------------SPcpievmK-RVIDKmhmsevtiaYGMTETSPVST 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 767 vyevdeQTSLSGAI-----LIGRPIANTQLYLLD-DKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQrfipnpfSDEP 840
Cdd:PRK08315 359 ------QTRTDDPLekrvtTVGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAE-------AIDA 425
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 841 NSRLYkTGDLARYLPDGNIEYLGRIDHQVkIRGFR-IELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKE-QA 918
Cdd:PRK08315 426 DGWMH-TGDLAVMDEEGYVNIVGRIKDMI-IRGGEnIYPREIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPgAT 503
|
570 580 590
....*....|....*....|....*....|....*..
gi 2129675820 919 PTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKV 955
Cdd:PRK08315 504 LTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
607-960 |
2.27e-17 |
|
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: 85.61 E-value: 2.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 607 SENLAYIIYTSGSTGKPKGTMIPHRGLVnYLSWCTNAYALAQG-----YGAPVqssIGFDATITSLFSPLLVGKRVVL-- 679
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNEV-YNAWMLALNSLFDPddvllCGLPL---FHVNGSVVTLLTPLASGAHVVLag 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 680 ---------------LPEKEEIEALSALlqsdqnyslvkitPAHLEMLNQMlPNHKGVTETRALIIGGEALLGKSLNFWR 744
Cdd:cd05944 77 pagyrnpglfdnfwkLVERYRITSLSTV-------------PTVYAALLQV-PVNADISSLRFAMSGAAPLPVELRARFE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 745 DnAPKTRIINEYGPTETVVGCCVYEVDEQTSLsGAILIGRPIANTQLYLLD-DKQKLVPIGVP--GELYIGGAGVARGYL 821
Cdd:cd05944 143 D-ATGLPVVEGYGLTEATCLVAVNPPDGPKRP-GSVGLRLPYARVRIKVLDgVGRLLRDCAPDevGEICVAGPGVFGGYL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 822 NRpELTQQRFIpnpfsdepNSRLYKTGDLARYLPDGNIEYLGRIDHQVkIRG-FRIELEEIESLLAQHPLVNAVTVIARE 900
Cdd:cd05944 221 YT-EGNKNAFV--------ADGWLNTGDLGRLDADGYLFITGRAKDLI-IRGgHNIDPALIEEALLRHPAVAFAGAVGQP 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2129675820 901 DQPGDKRLVGYIVPKEQAP-TSSELRQFLQSKLPEY-MIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05944 291 DAHAGELPVAYVQLKPGAVvEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
489-960 |
2.92e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 86.67 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 489 ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLT 568
Cdd:PRK13391 23 EVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALIT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 569 QQRLVDKFVEHKTQI----ICLDRDLP---------ENATLSIdnPVSNVTSENL-AYIIYTSGSTGKPKGTM--IPHRG 632
Cdd:PRK13391 103 SAAKLDVARALLKQCpgvrHRLVLDGDgelegfvgyAEAVAGL--PATPIADESLgTDMLYSSGTTGRPKGIKrpLPEQP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 633 LV---NYLSWCTNAYALAQG---------YGAPVQSSIGfdaTITSLfspllvGKRVVLLpEKEEIEALSALLQSdqnys 700
Cdd:PRK13391 181 PDtplPLTAFLQRLWGFRSDmvylspaplYHSAPQRAVM---LVIRL------GGTVIVM-EHFDAEQYLALIEE----- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 701 lVKITPAHL--EMLNQMLpnhKGVTETRA--------LIIGGEA-----LLGKSLNFWrdnAPktrIINE-YGPTETVvG 764
Cdd:PRK13391 246 -YGVTHTQLvpTMFSRML---KLPEEVRDkydlssleVAIHAAApcppqVKEQMIDWW---GP---IIHEyYAATEGL-G 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 765 CCVyeVDEQTSLSGAILIGRPIANTqLYLLDDKQKLVPIGVPGELYIGGaGVARGYLNRPELTQQrfipnpfSDEPNSRL 844
Cdd:PRK13391 315 FTA--CDSEEWLAHPGTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAE-------ARHPDGTW 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 845 YKTGDLArYLPDGNIEYL-GRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSS- 922
Cdd:PRK13391 384 STVGDIG-YVDEDGYLYLtDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPVDGVDPGPa 462
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2129675820 923 ---ELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK13391 463 laaELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
467-960 |
4.69e-17 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 86.55 E-value: 4.69e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNH--------ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILG---- 534
Cdd:PRK07529 27 TYELLSRAAARHPDAPALSFLLdadpldrpETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGgeaa 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 535 -----------------ILKAGGAYI-----PFDPTYPQERLGFMLedAQIPILLT------------QQRLVDKFVEHK 580
Cdd:PRK07529 107 gianpinpllepeqiaeLLRAAGAKVlvtlgPFPGTDIWQKVAEVL--AALPELRTvvevdlarylpgPKRLAVPLIRRK 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 581 TQIICLDRD-----LPENATLSIDNPVSNVTSenlAYIiYTSGSTGKPKGTMIPHRGLVnylswcTNAYALAQGYGAPVQ 655
Cdd:PRK07529 185 AHARILDFDaelarQPGDRLFSGRPIGPDDVA---AYF-HTGGTTGMPKLAQHTHGNEV------ANAWLGALLLGLGPG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 656 SSIGFD-------ATITSLFSPLLVGKRVVLLP-----------------EKEEIEALSALlqsdqnyslvkitPAHLEM 711
Cdd:PRK07529 255 DTVFCGlplfhvnALLVTGLAPLARGAHVVLATpqgyrgpgvianfwkivERYRINFLSGV-------------PTVYAA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 712 LNQMLPNHKGVTETRALIIGGEALlgkSLNFWRDNAPKT--RIINEYGPTETVVGCCVYEVDEQTSLsGAILIGRPIANT 789
Cdd:PRK07529 322 LLQVPVDGHDISSLRYALCGAAPL---PVEVFRRFEAATgvRIVEGYGLTEATCVSSVNPPDGERRI-GSVGLRLPYQRV 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 790 QLYLLDDKQKLV---PIGVPGELYIGGAGVARGYLNrpeltqqrfipnpfsDEPNSRLY------KTGDLARYLPDGNIE 860
Cdd:PRK07529 398 RVVILDDAGRYLrdcAVDEVGVLCIAGPNVFSGYLE---------------AAHNKGLWledgwlNTGDLGRIDADGYFW 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 861 YLGRidhqVK---IR-GFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYI--VPKEQApTSSELRQFLQSKLPE 934
Cdd:PRK07529 463 LTGR----AKdliIRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVqlKPGASA-TEAELLAFARDHIAE 537
|
570 580
....*....|....*....|....*..
gi 2129675820 935 -YMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK07529 538 rAAVPKHVRILDALPKTAVGKIFKPAL 564
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
466-920 |
5.49e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 86.11 E-value: 5.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 466 CLHELFAAQveRTPNNIAV----------EFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGI 535
Cdd:PRK09274 9 ARHLPRAAQ--ERPDQLAVavpggrgadgKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 536 LKAGGAYIPFDPTYPQERLGFMLEDAQ------IPILLTQQRLVDKFVEHKTQIICLD-RDLPENATLS--------IDN 600
Cdd:PRK09274 87 FKAGAVPVLVDPGMGIKNLKQCLAEAQpdafigIPKAHLARRLFGWGKPSVRRLVTVGgRLLWGGTTLAtllrdgaaAPF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 601 PVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSWCTNAYALAQGygapvqssiGFD-AT--ITSLFSPLLvGKRV 677
Cdd:PRK09274 167 PMADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPG---------EIDlPTfpLFALFGPAL-GMTS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 678 VLlPEKEEIEALSA----LLQSDQNYslvKIT-----PAHLEML-------NQMLPNHKGVTE-----TRALIIGGEALL 736
Cdd:PRK09274 237 VI-PDMDPTRPATVdpakLFAAIERY---GVTnlfgsPALLERLgrygeanGIKLPSLRRVISagapvPIAVIERFRAML 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 737 gkslnfwrdnAPKTRIINEYGPTEtVVGCCVYEVDEQ-------TSLSGAILIGRPIANTQLYLLD---------DKQKL 800
Cdd:PRK09274 313 ----------PPDAEILTPYGATE-ALPISSIESREIlfatraaTDNGAGICVGRPVDGVEVRIIAisdapipewDDALR 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 801 VPIGVPGELYIGGAGVARGYLNRPELTQQRFIPNPfsdEPNSRlYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEE 880
Cdd:PRK09274 382 LATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDG---QGDVW-HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIP 457
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2129675820 881 IESLLAQHPLVnavtviaredqpgdKR--LVGYIVPKEQAPT 920
Cdd:PRK09274 458 CERIFNTHPGV--------------KRsaLVGVGVPGAQRPV 485
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
609-955 |
6.06e-17 |
|
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: 83.70 E-value: 6.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 609 NLAYIIYTSGSTGKPKGTMIPHRGLVN-YLSWCTNA-------YALAQgygaPVQSSIGFDATItslFSPLLVGKRVVll 680
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRaAAAWADCAdlteddrYLIIN----PFFHTFGYKAGI---VACLLTGATVV-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 681 PEKE-EIEALSALLQSDQnyslVKITPAHLEMLNQML--PNHKG--VTETRALIIGGEALLGKSLNFWRDNAPKTRIINE 755
Cdd:cd17638 72 PVAVfDVDAILEAIERER----ITVLPGPPTLFQSLLdhPGRKKfdLSSLRAAVTGAATVPVELVRRMRSELGFETVLTA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 756 YGPTETVVGCCVYEVDEQTSLsgAILIGRPIANTQLYLLDDkqklvpigvpGELYIGGAGVARGYLNRPELTQQRFipnp 835
Cdd:cd17638 148 YGLTEAGVATMCRPGDDAETV--ATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI---- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 836 fsdEPNSRLYkTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQpgdkRL--VG--Y 911
Cdd:cd17638 212 ---DADGWLH-TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDE----RMgeVGkaF 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 2129675820 912 IVPKE-QAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKV 955
Cdd:cd17638 284 VVARPgVTLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
488-918 |
6.45e-17 |
|
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: 85.73 E-value: 6.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 488 HESLTYAQLNAKSNQLAHHLQKLGVK--PEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPI 565
Cdd:cd05927 3 YEWISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 566 LltqqrlvdkFVEHKTQIICLDrdlpENATLSIDNPVSNV--TSENLAYIIYTSGSTGKPKGTMIPHRGLVN-------- 635
Cdd:cd05927 83 V---------FCDAGVKVYSLE----EFEKLGKKNKVPPPppKPEDLATICYTSGTTGNPKGVMLTHGNIVSnvagvfki 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 636 ------------YLSW---------CTNAYALAQGygapvqSSIGF-DATITSLFspllvgkrvvllpekEEIEALS--- 690
Cdd:cd05927 150 leilnkinptdvYISYlplahiferVVEALFLYHG------AKIGFySGDIRLLL---------------DDIKALKptv 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 691 -------------ALLQSDQNYSLVKitpahlEMLNQMLPNHK------GVTET--------------------RALIIG 731
Cdd:cd05927 209 fpgvprvlnriydKIFNKVQAKGPLK------RKLFNFALNYKlaelrsGVVRAspfwdklvfnkikqalggnvRLMLTG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 732 GEALLGKSLNFWRdNAPKTRIINEYGPTETVVGCCVYEVDEQTSLSgailIGRPIANTQLYLLD--DKQKLVPIGVP-GE 808
Cdd:cd05927 283 SAPLSPEVLEFLR-VALGCPVLEGYGQTECTAGATLTLPGDTSVGH----VGGPLPCAEVKLVDvpEMNYDAKDPNPrGE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 809 LYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARYLPDGNIEYLGRIDHQVKI-RGFRIELEEIESLLAQ 887
Cdd:cd05927 358 VCIRGPNVFSGYYKDPEKTAEALDEDGW--------LHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYAR 429
|
490 500 510
....*....|....*....|....*....|....
gi 2129675820 888 HPLVNAVTVIaredqpGDKR---LVGYIVPKEQA 918
Cdd:cd05927 430 SPFVAQIFVY------GDSLksfLVAIVVPDPDV 457
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
490-960 |
1.07e-16 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 85.12 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQ 569
Cdd:PRK08008 37 RYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 570 -------QRLVDKFVEHKTQIICLDRDLPEN--------------ATLSIDNPVSnvtSENLAYIIYTSGSTGKPKGTMI 628
Cdd:PRK08008 117 aqfypmyRQIQQEDATPLRHICLTRVALPADdgvssftqlkaqqpATLCYAPPLS---TDDTAEILFTSGTTSRPKGVVI 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 629 PHRGLV---NYLSWCTnayAL-AQGYGAPVQSSIGFDATITSLFSPLLVGKRVVLLpEKeeiealsallqsdqnYSLVKi 704
Cdd:PRK08008 194 THYNLRfagYYSAWQC---ALrDDDVYLTVMPAFHIDCQCTAAMAAFSAGATFVLL-EK---------------YSARA- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 705 tpahleMLNQMLPNHKGVTETRALIIggEALLGKSLNFWRDNAP----------------------KTRIINEYGPTETV 762
Cdd:PRK08008 254 ------FWGQVCKYRATITECIPMMI--RTLMVQPPSANDRQHClrevmfylnlsdqekdafeerfGVRLLTSYGMTETI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 763 VGCCV-YEVDEQTSLSgailIGRPIANTQLYLLDDKQKLVPIGVPGELYIGG-AG--VARGYLNRPELTQQRFipnpfsd 838
Cdd:PRK08008 326 VGIIGdRPGDKRRWPS----IGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvPGktIFKEYYLDPKATAKVL------- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 839 EPNSRLYkTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQA 918
Cdd:PRK08008 395 EADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVLNEGE 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2129675820 919 PTSSE-LRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK08008 474 TLSEEeFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
467-961 |
1.44e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 84.66 E-value: 1.44e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 467 LHELFAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD 546
Cdd:PRK13383 37 PYTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPIS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 547 PTYPQERLGFMLEDAQIPILLTQQRLVDKFVEHKTQIICLDrdlPENATLSiDNPVSNVTSENLAYIIYTSGSTGKPKGt 626
Cdd:PRK13383 117 TEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVID---PATAGAE-ESGGRPAVAAPGRIVLLTSGTTGKPKG- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 627 mIPHrglvnylswctnayalaqgygAP-VQSSIGFDATI---------------TSLFSPLLVGKRVVLLP------EKE 684
Cdd:PRK13383 192 -VPR---------------------APqLRSAVGVWVTIldrtrlrtgsrisvaMPMFHGLGLGMLMLTIAlggtvlTHR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 685 EIEALSALLQSD----QNYSLVKITPAHLEMLNQMLPNHKGVTETRALIIGGEAL---LGKSLNfwrdNAPKTRIINEYG 757
Cdd:PRK13383 250 HFDAEAALAQASlhraDAFTAVPVVLARILELPPRVRARNPLPQLRVVMSSGDRLdptLGQRFM----DTYGDILYNGYG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 758 PTETVVGCCVYEVDEQTSLSgaiLIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGagvargylnrpELTQQRFipnpfS 837
Cdd:PRK13383 326 STEVGIGALATPADLRDAPE---TVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGG-----------ELAGTRY-----T 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 838 DEPNSR----LYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIV 913
Cdd:PRK13383 387 DGGGKAvvdgMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVV 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2129675820 914 PKEQAPT-SSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALP 961
Cdd:PRK13383 467 LHPGSGVdAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
489-960 |
2.53e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 83.80 E-value: 2.53e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 489 ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLT 568
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 569 QQRLVDkfvehktQIICLDRDLPENAT--LSIDNPVSNVTS-ENL---------------AYIIYTSGSTGKPKGTMIPH 630
Cdd:PRK08276 90 SAALAD-------TAAELAAELPAGVPllLVVAGPVPGFRSyEEAlaaqpdtpiadetagADMLYSSGTTGRPKGIKRPL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 631 RGLvnylswcTNAYALAQGYGAPVQSSIGFDATITSLFSPL-------------LVGKRVVLLPEKEEIEALSALlqsdQ 697
Cdd:PRK08276 163 PGL-------DPDEAPGMMLALLGFGMYGGPDSVYLSPAPLyhtaplrfgmsalALGGTVVVMEKFDAEEALALI----E 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 698 NYslvKITPAHL------EMLNqmLP----NHKGVTETRALIIGGeallgkslnfwrdnAP-----KTRIINEYGPtetv 762
Cdd:PRK08276 232 RY---RVTHSQLvptmfvRMLK--LPeevrARYDVSSLRVAIHAA--------------APcpvevKRAMIDWWGP---- 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 763 vgcCVYEVDEQTSLSGAILI------------GRPIAnTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQR 830
Cdd:PRK08276 289 ---IIHEYYASSEGGGVTVItsedwlahpgsvGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 831 FIPNPFSdepnsrlyKTGDLArYL-PDGnieYL---GRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDK 906
Cdd:PRK08276 365 RNPHGWV--------TVGDVG-YLdEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGE 432
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2129675820 907 RLVGYIVPKEQAPTS----SELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK08276 433 RVKAVVQPADGADAGdalaAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
605-960 |
3.98e-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: 83.52 E-value: 3.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 605 VTSENLAYIIYTSGSTGKPKGTMIPHRGLVNYLSWC-TNAYALAQG---YGApvqSSIGFDATIT-SLFSPLLVGKRVVL 679
Cdd:cd05967 227 VAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWSmRNIYGIKPGdvwWAA---SDVGWVVGHSyIVYGPLLHGATTVL 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 680 LPEKEE-----------IE------------ALSALLQSDQNYSLVKITPahlemlnqmlpnhkgVTETRALIIGGEALL 736
Cdd:cd05967 304 YEGKPVgtpdpgafwrvIEkyqvnalftaptAIRAIRKEDPDGKYIKKYD---------------LSSLRTLFLAGERLD 368
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 737 GKSLNfWRDNAPKTRIINEYGPTET---VVGCCVYEVDEQTSLSGAiliGRPIANTQLYLLDDKQKLVPIGVPGELYIGG 813
Cdd:cd05967 369 PPTLE-WAENTLGVPVIDHWWQTETgwpITANPVGLEPLPIKAGSP---GKPVPGYQVQVLDEDGEPVGPNELGNIVIKL 444
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 814 AgVARGYLNRPELTQQRFIPNPFSDEPNsrLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNA 893
Cdd:cd05967 445 P-LPPGCLLTLWKNDERFKKLYLSKFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAE 521
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2129675820 894 VTVIAREDQPGDKRLVGYIVPKEQAPT-----SSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05967 522 CAVVGVRDELKGQVPLGLVVLKEGVKItaeelEKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTL 593
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
5-324 |
4.77e-16 |
|
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as 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. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380461 [Multi-domain] Cd Length: 432 Bit Score: 82.31 E-value: 4.77e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 5 IRISPQQKHLW-LQQKDNYQA-YCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGMniPFQSIsdaptynhI 82
Cdd:cd19538 2 IPLSFAQRRLWfLHQLEGPSAtYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGV--PYQLI--------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 83 SLAEYDWSRLSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTA 162
Cdd:cd19538 72 EEDEATPKLEIKEVDEEELESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 163 CLDGEEISEEVM--QYADVSEWLNELLESEDTETAR-----NYWQQQdissvLNlRIPFEIK--NDHQSSGEISFAPQSL 233
Cdd:cd19538 152 RCKGEAPELAPLpvQYADYALWQQELLGDESDPDSLiarqlAYWKKQ-----LA-GLPDEIElpTDYPRPAESSYEGGTL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 234 CLAMNRDTVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLPIHSRLEDALK 313
Cdd:cd19538 226 TFEIDSELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPS 305
|
330
....*....|.
gi 2129675820 314 FSELMERVSES 324
Cdd:cd19538 306 FRELLERVKET 316
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
492-954 |
1.70e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 81.29 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 492 TYAQLNAKSNQLAHHLQKLGVKPEVLVGICV---ERSLDMLIGILGilkAGGAYIPFDPTYPQERLGFMLEDAQIPIL-- 566
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAYYGVSG---SGAVCHTINPRLFPEQIAYIVNHAEDRYVlf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 567 -LTQQRLVDKFVEH----KTQIICLDRD-LPENAT--LSIDNPVSNVTS--------ENLA-YIIYTSGSTGKPKGTMIP 629
Cdd:PRK07008 118 dLTFLPLVDALAPQcpnvKGWVAMTDAAhLPAGSTplLCYETLVGAQDGdydwprfdENQAsSLCYTSGTTGNPKGALYS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 630 HRGLVnylswctnayalAQGYGAPVQSSIGFDATITSL--------------FSPLLVGKRVVLLPEKEEIEALSALLQS 695
Cdd:PRK07008 198 HRSTV------------LHAYGAALPDAMGLSARDAVLpvvpmfhvnawglpYSAPLTGAKLVLPGPDLDGKSLYELIEA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 696 DQNYSLVKITPAHLEMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNApKTRIINEYGPTE-TVVGCCVYEVDEQT 774
Cdd:PRK07008 266 ERVTFSAGVPTVWLGLLNHMREAGLRFSTLRRTVIGGSACPPAMIRTFEDEY-GVEVIHAWGMTEmSPLGTLCKLKWKHS 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 775 SLSG----AILI--GRPIANTQLYLLDDKQKLVPI-GVP-GELYIGGAGVARGYLNRPEltqqrfipNPFSDepnsRLYK 846
Cdd:PRK07008 345 QLPLdeqrKLLEkqGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRGDA--------SPLVD----GWFP 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 847 TGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAP-TSSELR 925
Cdd:PRK07008 413 TGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEvTREELL 492
|
490 500
....*....|....*....|....*....
gi 2129675820 926 QFLQSKLPEYMIPSAFVMLEVIPLTTHGK 954
Cdd:PRK07008 493 AFYEGKVAKWWIPDDVVFVDAIPHTATGK 521
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
487-962 |
2.27e-15 |
|
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: 80.61 E-value: 2.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 487 NHESLTYAQLNAKSNQLAHHLQKLGVKP--EVLVGICVERS-LDMLIGILGilkagGAYIPfdptypqerlgfmledaqI 563
Cdd:cd05908 12 KEKFVSYRHLREEALGYLGALQELGIKPgqEVVFQITHNNKfLYLFWACLL-----GGMIA------------------V 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 564 PILltqqrlVDKFVEHKTQIICLDRDLpENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVN-------- 635
Cdd:cd05908 69 PVS------IGSNEEHKLKLNKVWNTL-KNPYLITEEEVLCELADELAFIQFSSGSTGDPKGVMLTHENLVHnmfailns 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 636 --------YLSW--CTNAYALAQGYGAPVQSSIGFDATITSLF--SPLLVGKRVvllpEKEEIEALSAllqSDQNYSLVk 703
Cdd:cd05908 142 tewktkdrILSWmpLTHDMGLIAFHLAPLIAGMNQYLMPTRLFirRPILWLKKA----SEHKATIVSS---PNFGYKYF- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 704 itpahLEMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRD-----NAPKTRIINEYGPTETVVGCC------------ 766
Cdd:cd05908 214 -----LKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDhmskyGLKRNAILPVYGLAEASVGASlpkaqspfktit 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 767 -----------VYEVDEQTSLSGAIL-IGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFIPN 834
Cdd:cd05908 289 lgrrhvthgepEPEVDKKDSECLTFVeVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDD 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 835 PFsdepnsrlYKTGDLArYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIA---REDQPGDKRLVGY 911
Cdd:cd05908 369 GW--------LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVAcgvNNSNTRNEEIFCF 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2129675820 912 IVPKEQAPTSSELRQFLQSKLPE---YMIpSAFVMLEVIPLTTHGKVDRQALPQ 962
Cdd:cd05908 440 IEHRKSEDDFYPLGKKIKKHLNKrggWQI-NEVLPIRRIPKTTSGKVKRYELAQ 492
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
492-964 |
2.84e-15 |
|
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: 80.62 E-value: 2.84e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 492 TYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIP-ILLTQQ 570
Cdd:cd05970 49 TFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKmIVAIAE 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 571 RLVDKFVE-------HKTQIICLDRDLPE----------NATLSIDNPVSNVTS--ENLAYIIYTSGSTGKPKgtMIPHR 631
Cdd:cd05970 129 DNIPEEIEkaapecpSKPKLVWVGDPVPEgwidfrklikNASPDFERPTANSYPcgEDILLVYFSSGTTGMPK--MVEHD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 632 -----GLVNYLSWCTNA------YALAQ-GYGAPVQSSIgfdatitslFSPLLVGKRVVLLPEKEEIEAlsALLQSDQNY 699
Cdd:cd05970 207 ftyplGHIVTAKYWQNVregglhLTVADtGWGKAVWGKI---------YGQWIAGAAVFVYDYDKFDPK--ALLEKLSKY 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 700 SLVKIT--PAHLEMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDnAPKTRIINEYGPTETVVGCCVYEVDEQTSLS 777
Cdd:cd05970 276 GVTTFCapPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKE-KTGIKLMEGFGQTETTLTIATFPWMEPKPGS 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 778 gailIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGA-----GVARGYLNRPELTQQRFipnpfsdepNSRLYKTGDLAR 852
Cdd:cd05970 355 ----MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW---------HDGYYHTGDAAW 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 853 YLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSELRQFLQSKL 932
Cdd:cd05970 422 MDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKGYEPSEELKKELQDHV 501
|
490 500 510
....*....|....*....|....*....|....*.
gi 2129675820 933 PE----YMIPSAFVMLEVIPLTTHGKVDRQALPQPD 964
Cdd:cd05970 502 KKvtapYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
977-1050 |
3.76e-15 |
|
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: 71.81 E-value: 3.76e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2129675820 977 APRDRLELKLANIWENLLNVHP--IGIKDSFF-ELGGHSLLAVRLMAHINQEFGKNLALATLFQNPTIEKLANLLRQ 1050
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDPeeITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
474-928 |
5.38e-15 |
|
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: 79.91 E-value: 5.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 474 QVERTPNNIAVEF------NHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGI----CVERSLDML----IG-ILGILKA 538
Cdd:cd05966 62 HLKERGDKVAIIWegdepdQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIympmIPELVIAMLacarIGaVHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 539 GgayipFDPTYPQERLgfmlEDAQIPILLTQ------------QRLVDKFVEHKTQII-CL-------------DRDLP- 591
Cdd:cd05966 142 G-----FSAESLADRI----NDAQCKLVITAdggyrggkviplKEIVDEALEKCPSVEkVLvvkrtggevpmteGRDLWw 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 592 --ENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGlvnYLS------------------WCTnayalaqgyg 651
Cdd:cd05966 213 hdLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVVHTTGG---YLLyaattfkyvfdyhpddiyWCT---------- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 652 apvqSSIGFdatIT----SLFSPLLVGKRVVLLpekeeiEALSALLQSDQNYSLV---KIT-----PAHLEMLNQMLPNH 719
Cdd:cd05966 280 ----ADIGW---ITghsyIVYGPLANGATTVMF------EGTPTYPDPGRYWDIVekhKVTifytaPTAIRALMKFGDEW 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 720 KGVTETRAL-IIG--GEALLGKSLNFWRDNAPKTR--IINEYGPTETVvGCCVyevdeqTSLSGAILI-----GRPIANT 789
Cdd:cd05966 347 VKKHDLSSLrVLGsvGEPINPEAWMWYYEVIGKERcpIVDTWWQTETG-GIMI------TPLPGATPLkpgsaTRPFFGI 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 790 QLYLLDDKQKLVPIGVPGELYIGGA--GVARGYLNRPEltqqRFIPNPFSDEPNsrLYKTGDLARYLPDGNIEYLGRIDH 867
Cdd:cd05966 420 EPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPG--YYFTGDGARRDEDGYYWITGRVDD 493
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2129675820 868 QVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSELRQFL 928
Cdd:cd05966 494 VINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDELRKEL 554
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
7-324 |
6.70e-15 |
|
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS/NRPSs); Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Hybrid PKS/NRPS create polymers containing both polyketide and amide linkages. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Most members of this subfamily have the typical C-domain HHXXXD motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380471 [Multi-domain] Cd Length: 430 Bit Score: 78.84 E-value: 6.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 7 ISPQQKHLWLQQK--DNYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSlpGMNIPFQSISDAPTYNhisL 84
Cdd:cd20483 4 MSTFQRRLWFLHNflEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFE--GDDFGEQQVLDDPSFH---L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 85 AEYDWSrlSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACL 164
Cdd:cd20483 79 IVIDLS--EAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 165 DGE---EISEEVMQYADVSEWLNELLESEDTETARNYWQQ--QDISSVLNLrIPF------EIKNDHQSSGEISFAPqSL 233
Cdd:cd20483 157 AGRdlaTVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEklEGIPDASKL-LPFakaerpPVKDYERSTVEATLDK-EL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 234 CLAMNRdtvekleILQESYHTSTEaILLACWQVLLWRLSGQSEIVIGAAgDG-REYDELKGVFGLLTKYLPIHSRLEDAL 312
Cdd:cd20483 235 LARMKR-------ICAQHAVTPFM-FLLAAFRAFLYRYTEDEDLTIGMV-DGdRPHPDFDDLVGFFVNMLPIRCRMDCDM 305
|
330
....*....|..
gi 2129675820 313 KFSELMERVSES 324
Cdd:cd20483 306 SFDDLLESTKTT 317
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
471-639 |
7.83e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 79.53 E-value: 7.83e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 471 FAAQVERTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGG--AYIPFDPT 548
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAvvALLNTQQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 549 ypQERLGFMLEDAQIPILLTQQRLVDKFVEHK------------TQIICLDRDLPEN-----ATLSIDNPVS--NVTSEN 609
Cdd:PRK08279 123 --GAVLAHSLNLVDAKHLIVGEELVEAFEEARadlarpprlwvaGGDTLDDPEGYEDlaaaaAGAPTTNPASrsGVTAKD 200
|
170 180 190
....*....|....*....|....*....|
gi 2129675820 610 LAYIIYTSGSTGKPKGTMIPHRGLVNYLSW 639
Cdd:PRK08279 201 TAFYIYTSGTTGLPKAAVMSHMRWLKAMGG 230
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
24-432 |
1.01e-14 |
|
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: 77.87 E-value: 1.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 24 AYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHsLPGMNIPFQ---SISDAPtynhisLAEYDWSRLSSQVQKak 100
Cdd:cd19536 23 VYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFI-EDGLGQPVQvvhRQAQVP------VTELDLTPLEEQLDP-- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 101 IDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILF-ISLPALYADKTTLNYLICEIGRAYTACLDGEEISE-EVMQYAD 178
Cdd:cd19536 94 LRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQLLEYKPLSLpPAQPYRD 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 179 VSEWLnelLESEDTETARNYWQQ--QDISSVlNLRIPFEIKNDHQSSGEISFAPQSLClamnrdtvEKLEILQESYHTST 256
Cdd:cd19536 174 FVAHE---RASIQQAASERYWREylAGATLA-TLPALSEAVGGGPEQDSELLVSVPLP--------VRSRSLAKRSGIPL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 257 EAILLACWQVLLWRLSGQSEIVIGAAGDGR--EYDELKGVFGLLTKYLPIHSRLEDAlKFSELMERVSESLRFVKKWQEY 334
Cdd:cd19536 242 STLLLAAWALVLSRHSGSDDVVFGTVVHGRseETTGAERLLGLFLNTLPLRVTLSEE-TVEDLLKRAQEQELESLSHEQV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 335 FNWENFISTnekfAARPFFPFCFDFtqQSQSYVNGNIAFSEYKKSANIDKF-------QIKLSSGYSQDNLVVNFDYDAN 407
Cdd:cd19536 321 PLADIQRCS----EGEPLFDSIVNF--RHFDLDFGLPEWGSDEGMRRGLLFsefksnyDVNLSVLPKQDRLELKLAYNSQ 394
|
410 420
....*....|....*....|....*
gi 2129675820 408 LFSEDSIKILAEQYLTLIASVTYNP 432
Cdd:cd19536 395 VLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
751-960 |
2.44e-14 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 77.58 E-value: 2.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 751 RIINEYGPTETV--VGCCVY--EVDEQTSLSGAILIGRP-IANTQLYLLD--DKQKLVPigVP------GELYIGGAGVA 817
Cdd:PLN02479 336 RVTHTYGLSETYgpSTVCAWkpEWDSLPPEEQARLNARQgVRYIGLEGLDvvDTKTMKP--VPadgktmGEIVMRGNMVM 413
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 818 RGYLNRPELTQQRFipnpfsdepNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVI 897
Cdd:PLN02479 414 KGYLKNPKANEEAF---------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVV 484
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2129675820 898 AREDQPGDKRLVGYIVPKEQAPTSSELR------QFLQSKLPEYMIPSAfVMLEVIPLTTHGKVDRQAL 960
Cdd:PLN02479 485 ARPDERWGESPCAFVTLKPGVDKSDEAAlaedimKFCRERLPAYWVPKS-VVFGPLPKTATGKIQKHVL 552
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
491-960 |
2.54e-14 |
|
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: 76.84 E-value: 2.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 491 LTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPfdptypqerlgfmledaqIPILLTQQ 570
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTPD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 571 RLVDKFVEHKTQIICLDRdlpenaTLSIDNPVsnvtsenLAYiiYTSGSTGKPKGTMIPHR----GLVNYLSWCtnayAL 646
Cdd:cd05974 63 DLRDRVDRGGAVYAAVDE------NTHADDPM-------LLY--FTSGTTSKPKLVEHTHRsypvGHLSTMYWI----GL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 647 AQGYGAPVQSSIGF-DATITSLFSPLLVGKRVVLLPEKE-EIEALSALLQSdQNYSLVKITPAHLEMLNQMlPNHKGVTE 724
Cdd:cd05974 124 KPGDVHWNISSPGWaKHAWSCFFAPWNAGATVFLFNYARfDAKRVLAALVR-YGVTTLCAPPTVWRMLIQQ-DLASFDVK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 725 TRALIIGGEALLGKSLNFWRdNAPKTRIINEYGPTETVvgCCVYEVDEQTSLSGAIliGRPIANTQLYLLDdkqklvPIG 804
Cdd:cd05974 202 LREVVGAGEPLNPEVIEQVR-RAWGLTIRDGYGQTETT--ALVGNSPGQPVKAGSM--GRPLPGYRVALLD------PDG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 805 VP---GE--LYIGG---AGVARGYLNRPELTqqrfipnpfSDEPNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRI 876
Cdd:cd05974 271 APateGEvaLDLGDtrpVGLMKGYAGDPDKT---------AHAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRI 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 877 ELEEIESLLAQHPLVNAVTVIAredQPGDKRLVgyiVPK---------EQAP-TSSELRQFLQSKLPEYMIPSAFVMLEv 946
Cdd:cd05974 342 SPFELESVLIEHPAVAEAAVVP---SPDPVRLS---VPKafivlragyEPSPeTALEIFRFSRERLAPYKRIRRLEFAE- 414
|
490
....*....|....
gi 2129675820 947 IPLTTHGKVDRQAL 960
Cdd:cd05974 415 LPKTISGKIRRVEL 428
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
880-954 |
7.63e-14 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 67.95 E-value: 7.63e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2129675820 880 EIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKE-QAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGK 954
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPgVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
456-873 |
1.34e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 75.54 E-value: 1.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 456 NTKIEFPHDKCLHELFAAQVERTPNNIA---VEFNHES------LTYAQLNAKSNQLAHHLQKLGvKPEVLVGICVERSL 526
Cdd:PRK07769 12 NGKIRFPPNTNLVRHVERWAKVRGDKLAyrfLDFSTERdgvardLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 527 DMLIGILGILKAGGAYIP-FDPTYP--QERLGFMLEDAQIPILLTQQRL---VDKFVEH-----KTQIICLDRdLPENAT 595
Cdd:PRK07769 91 DYLIAFFGALYAGRIAVPlFDPAEPghVGRLHAVLDDCTPSAILTTTDSaegVRKFFRArpakeRPRVIAVDA-VPDEVG 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 596 LSIDNPVsnVTSENLAYIIYTSGSTGKPKGTMIPHRGLvnylswCTNAYALAQGYGA----------PVQSSIGFdatIT 665
Cdd:PRK07769 170 ATWVPPE--ANEDTIAYLQYTSGSTRIPAGVQITHLNL------PTNVLQVIDALEGqegdrgvswlPFFHDMGL---IT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 666 SLFSPLLvGKRVVL----------------LPEKEE--IEALSALLQSDQNYSLVKITPAHLEM-LNqmLPNHKGvtetr 726
Cdd:PRK07769 239 VLLPALL-GHYITFmspaafvrrpgrwireLARKPGgtGGTFSAAPNFAFEHAAARGLPKDGEPpLD--LSNVKG----- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 727 aLIIGGEALLGKSL-NFWRDNAP----KTRIINEYGPTETVVGCCVYEVDEQTSLsgaILIGRPIANTQLYLL--DDKQK 799
Cdd:PRK07769 311 -LLNGSEPVSPASMrKFNEAFAPyglpPTAIKPSYGMAEATLFVSTTPMDEEPTV---IYVDRDELNAGRFVEvpADAPN 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 800 LVP------IGVP-------------------GELYIGGAGVARGYLNRPELTQQRF-------IPNPFSD--EPNSRLY 845
Cdd:PRK07769 387 AVAqvsagkVGVSewavivdpetaselpdgqiGEIWLHGNNIGTGYWGKPEETAATFqnilksrLSESHAEgaPDDALWV 466
|
490 500
....*....|....*....|....*...
gi 2129675820 846 KTGDLARYLpDGNIEYLGRIDHQVKIRG 873
Cdd:PRK07769 467 RTGDYGVYF-DGELYITGRVKDLVIIDG 493
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
489-865 |
1.53e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 75.47 E-value: 1.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 489 ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYpqerlGFMLED-AQIPIL- 566
Cdd:PRK12582 79 RKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAY-----SLMSHDhAKLKHLf 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 567 -LTQQRLVdkFVEH--------------KTQIICLDRDLPENATLSIDN----PVSN--------VTSENLAYIIYTSGS 619
Cdd:PRK12582 154 dLVKPRVV--FAQSgapfaralaaldllDVTVVHVTGPGEGIASIAFADlaatPPTAavaaaiaaITPDTVAKYLFTSGS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 620 TGKPKGTMIPHRGLvnylswCTNAYALAQ------GYGAPVQ--------SSIGfdatiTSLFSPLLVGKRVVLL----P 681
Cdd:PRK12582 232 TGMPKAVINTQRMM------CANIAMQEQlrprepDPPPPVSldwmpwnhTMGG-----NANFNGLLWGGGTLYIddgkP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 682 EKEEIEALSALLQ--SDQNYSLVkitPAHLEMLNQMLPNHKGVTET-----RALIIGGEALlgkSLNFW-RDNAPKTRII 753
Cdd:PRK12582 301 LPGMFEETIRNLReiSPTVYGNV---PAGYAMLAEAMEKDDALRRSffknlRLMAYGGATL---SDDLYeRMQALAVRTT 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 754 NE-------YGPTETV-VGCCVYEVDEQTSLsgailIGRPIANTQLyllddkqKLVPIGVPGELYIGGAGVARGYLNRPE 825
Cdd:PRK12582 375 GHripfytgYGATETApTTTGTHWDTERVGL-----IGLPLPGVEL-------KLAPVGDKYEVRVKGPNVTPGYHKDPE 442
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 2129675820 826 LTQQRFipnpfsDEPNsrLYKTGDLARYL----PDGNIEYLGRI 865
Cdd:PRK12582 443 LTAAAF------DEEG--FYRLGDAARFVdpddPEKGLIFDGRV 478
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
613-960 |
6.10e-13 |
|
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: 73.27 E-value: 6.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 613 IIYTSGSTGKPKgtMIPHrglvnylSWCT--NAYALAQGYGAPVQSSIGF---------DATITSLFSPLLVGKRVV--L 679
Cdd:cd05928 179 IYFTSGTTGSPK--MAEH-------SHSSlgLGLKVNGRYWLDLTASDIMwntsdtgwiKSAWSSLFEPWIQGACVFvhH 249
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 680 LPEKEEIEALSALLQSDQNySLVKITPAHLEMLNQMLPNHKgVTETRALIIGGEALLGKSLNFWRdNAPKTRIINEYGPT 759
Cdd:cd05928 250 LPRFDPLVILKTLSSYPIT-TFCGAPTVYRMLVQQDLSSYK-FPSLQHCVTGGEPLNPEVLEKWK-AQTGLDIYEGYGQT 326
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 760 ETVVGCCVYEVDEQTSLSgailIGRPIANTQLYLLDDKQKLVPIGVPGELYIggagvaRGYLNRPELTQQRFIPNPFSDE 839
Cdd:cd05928 327 ETGLICANFKGMKIKPGS----MGKASPPYDVQIIDDNGNVLPPGTEGDIGI------RVKPIRPFGLFSGYVDNPEKTA 396
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 840 PNSR--LYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIV---- 913
Cdd:cd05928 397 ATIRgdFYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVVlapq 476
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 2129675820 914 --PKEQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05928 477 flSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
489-938 |
9.23e-13 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 72.00 E-value: 9.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 489 ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGayipfdptypqerlgfmledaqIPILL- 567
Cdd:cd05940 2 EALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA----------------------VAALIn 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 568 TQQRLvdKFVEHktqiiCLDrdlpenatlsIDNPVSNVTseNLAYIIYTSGSTGKPKGTMIPHRGLVNYlswctnaYALA 647
Cdd:cd05940 60 YNLRG--ESLAH-----CLN----------VSSAKHLVV--DAALYIYTSGTTGLPKAAIISHRRAWRG-------GAFF 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 648 QGYGAPVQSSIGFD--------ATITSLFSPLLVGKRVVLlpeKEEIEAlSALLQSDQNYSlVKITPAHLEMLNQMLpNH 719
Cdd:cd05940 114 AGSGGALPSDVLYTclplyhstALIVGWSACLASGATLVI---RKKFSA-SNFWDDIRKYQ-ATIFQYIGELCRYLL-NQ 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 720 KGVTETRALIIggEALLGKSL--NFWRD-----NAPktRIINEYGPTETVVGccVYEVDEQTSLSGAI-LIGRPIANTQL 791
Cdd:cd05940 188 PPKPTERKHKV--RMIFGNGLrpDIWEEfkerfGVP--RIAEFYAATEGNSG--FINFFGKPGAIGRNpSLLRKVAPLAL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 792 YLLD-DKQKL----------VPIGVPGEL--YIGGAGVARGYLNrPELTQQRFIPNPFSDepNSRLYKTGDLARYLPDGN 858
Cdd:cd05940 262 VKYDlESGEPirdaegrcikVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFKK--GDAWFNTGDLMRLDGEGF 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 859 IEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTV--IAREDQPGDKRLVGYIVPKEQAPTSSELRQFLQSKLPEYM 936
Cdd:cd05940 339 WYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIVLQPNEEFDLSALAAHLEKNLPGYA 418
|
..
gi 2129675820 937 IP 938
Cdd:cd05940 419 RP 420
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
492-865 |
1.77e-12 |
|
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: 71.69 E-value: 1.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 492 TYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYP----------------QERLG 555
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSlmsqdlaklkhlfellKPGLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 556 F-----MLEDAQIPILLTQQRLVDKF--VEHKTQIIcLDRDLPENATLSIDNPVSNVTSENLAYIIYTSGSTGKPKGTMI 628
Cdd:cd05921 107 FaqdaaPFARALAAIFPLGTPLVVSRnaVAGRGAIS-FAELAATPPTAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVIN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 629 PHRGLvnylswCTNAYALAQGYG------------APVQSSIGFDATitslFSPLLVGKRVVLLPEKEEIEALSAllQSD 696
Cdd:cd05921 186 TQRML------CANQAMLEQTYPffgeeppvlvdwLPWNHTFGGNHN----FNLVLYNGGTLYIDDGKPMPGGFE--ETL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 697 QNYSLVKIT-----PAHLEMLNQMLPNHKGVTET-----RALIIGGEALlgkSLNFW---RDNAPKT-----RIINEYGP 758
Cdd:cd05921 254 RNLREISPTvyfnvPAGWEMLVAALEKDEALRRRffkrlKLMFYAGAGL---SQDVWdrlQALAVATvgeriPMMAGLGA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 759 TETVVGCCVyeVDEQTSLSGaiLIGRPIANTQLyllddkqKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFipnpfsD 838
Cdd:cd05921 331 TETAPTATF--THWPTERSG--LIGLPAPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAF------D 393
|
410 420 430
....*....|....*....|....*....|.
gi 2129675820 839 EPNsrLYKTGDLARYL----PDGNIEYLGRI 865
Cdd:cd05921 394 EEG--FYCLGDAAKLAdpddPAKGLVFDGRV 422
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
985-1042 |
3.91e-12 |
|
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: 62.58 E-value: 3.91e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 985 KLANIWENLLNV--HPIGIKDSFFELGGHSLLAVRLMAHINQEFGKNLALATLFQNPTIE 1042
Cdd:pfam00550 2 RLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
477-955 |
3.95e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 70.46 E-value: 3.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 477 RTPNNIAVEFNHESLTYAQLNAKSNQLAHHLQKLGVKP--EVLVGI--CVErsldMLIGILGILKAGGAYIP--FDPTyP 550
Cdd:PRK07470 19 RFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKgdRILVHSrnCNQ----MFESMFAAFRLGAVWVPtnFRQT-P 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 551 QE--------RLGFMLEDAQIPILLTQQRLVDKFVEHKTQI----------ICLDRDL---PENATLSIDNPvsnvtsen 609
Cdd:PRK07470 94 DEvaylaeasGARAMICHADFPEHAAAVRAASPDLTHVVAIggaragldyeALVARHLgarVANAAVDHDDP-------- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 610 lAYIIYTSGSTGKPKGTMIPH----------------------RGLVNY-LSWCTNAYALAQ---GYGAPVQSSIGFDAT 663
Cdd:PRK07470 166 -CWFFFTSGTTGRPKAAVLTHgqmafvitnhladlmpgtteqdASLVVApLSHGAGIHQLCQvarGAATVLLPSERFDPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 664 ----------ITSLFS-PLLVgKRVVLLPEKEE---------IEALSALLQSDQNYSLVKITPahlemlnqMLPNHKGVT 723
Cdd:PRK07470 245 evwalverhrVTNLFTvPTIL-KMLVEHPAVDRydhsslryvIYAGAPMYRADQKRALAKLGK--------VLVQYFGLG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 724 EtralIIGGEALLGKSLNFwRDNAPKTRIineygptetvvGCCvyevdeqtslsgailiGRPIANTQLYLLDDKQKLVPI 803
Cdd:PRK07470 316 E----VTGNITVLPPALHD-AEDGPDARI-----------GTC----------------GFERTGMEVQIQDDEGRELPP 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 804 GVPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlyKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIES 883
Cdd:PRK07470 364 GETGEICVIGPAVFAGYYNNPEANAKAFRDGWF---------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEE 434
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2129675820 884 LLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAP-TSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKV 955
Cdd:PRK07470 435 KLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPvDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
8-323 |
6.83e-12 |
|
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; LCL-type Condensation (C) domains catalyze peptide bond formation between two L-amino acids, ((L)C(L)). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). In addition to the LCL-type, there are various subtypes of C-domains such as 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. An HHxx[SAG]DGxSx(6)[ED] motif is characteristic of LCL-type C-domains.
Pssm-ID: 380463 [Multi-domain] Cd Length: 433 Bit Score: 69.37 E-value: 6.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 8 SPQQKHLW-LQQKDNYQA-YCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGmnIPFQSISDA----PTYNH 81
Cdd:cd19540 5 SFAQQRLWfLNRLDGPSAaYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDG--GPYQVVLPAaearPDLTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 82 ISLAEydwsrlssqvqkAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFI----------SLPALYADKTTlny 151
Cdd:cd19540 83 VDVTE------------DELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLvvhhiaadgwSMAPLARDLAT--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 152 liceigrAYTACLDGEEIS---EEVmQYADVSEWLNELLESEDTETAR-----NYWQQQ--DISSVLNLriPFeiknDHQ 221
Cdd:cd19540 148 -------AYAARRAGRAPDwapLPV-QYADYALWQRELLGDEDDPDSLaarqlAYWRETlaGLPEELEL--PT----DRP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 222 SSGEISFAPQSLCLAMNRDTVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKY 301
Cdd:cd19540 214 RPAVASYRGGTVEFTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNT 293
|
330 340
....*....|....*....|..
gi 2129675820 302 LPIHSRLEDALKFSELMERVSE 323
Cdd:cd19540 294 LVLRTDVSGDPTFAELLARVRE 315
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
490-960 |
7.23e-12 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 69.84 E-value: 7.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKLgvkPEVLVGICVERSLDMLIGILGILKAGGayIPFDPTYPQ--ERLGFMLEDAQIPILL 567
Cdd:PRK06334 45 KLSYNQVRKAVIALATKVSKY---PDQHIGIMMPASAGAYIAYFATLLSGK--IPVMINWSQglREVTACANLVGVTHVL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 568 TQQRLVDKF-------VEHKTQIICLDR-----------------DLPENATLSIDNpVSNVTSENLAYIIYTSGSTGKP 623
Cdd:PRK06334 120 TSKQLMQHLaqthgedAEYPFSLIYMEEvrkelsfwekcrigiymSIPFEWLMRWFG-VSDKDPEDVAVILFTSGTEKLP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 624 KGTMIPHRGLVNYLSWCTNAYAlaqgygaPVQSSI-----------GFDATitSLFsPLLVGKRVVL----LPEKEEIEa 688
Cdd:PRK06334 199 KGVPLTHANLLANQRACLKFFS-------PKEDDVmmsflppfhayGFNSC--TLF-PLLSGVPVVFaynpLYPKKIVE- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 689 lsalLQSDQNYSLVKITPAHLE-MLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTEtvvgCC- 766
Cdd:PRK06334 268 ----MIDEAKVTFLGSTPVFFDyILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTTE----CSp 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 767 VYEVDEQTSLSGAILIGRPIANTQLYLLDDKQKL-VPIGVPGELYIGGAGVARGYLNRPEltQQRFIpnpfsDEPNSRLY 845
Cdd:PRK06334 340 VITINTVNSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLGEDF--GQGFV-----ELGGETWY 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 846 KTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHplvnavtvIAREDQPGDKRLVGYIVPKEQA------- 918
Cdd:PRK06334 413 VTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEG--------FGQNAADHAGPLVVCGLPGEKVrlclftt 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2129675820 919 -PTS-SELRQFLQ-SKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK06334 485 fPTSiSEVNDILKnSKTSSILKISYHHQVESIPMLGTGKPDYCSL 529
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
584-962 |
8.73e-12 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 68.87 E-value: 8.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 584 ICLDRDLPENATLSIDNPVSNVTSENLAYI-IYTSGSTGKPKGTMipH---------RGLVNYLSW-CTNAYALAqgyga 652
Cdd:PRK07445 95 QIWGLDQLKLSHPPPLPSQGILPNLETGWImIPTGGSSGQIRFAI--HtwetltasvQGFQRYFQLqQVNSFCVL----- 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 653 PVQSSIGFDATITSLfsplLVGKRVVLLPEKE-EIEALSALLQSDQNYSLVkitPAHLEMLNQMLPNHkgVTETRALIIG 731
Cdd:PRK07445 168 PLYHVSGLMQFMRSF----LTGGKLVILPYKRlKSGQELPPNPSDFFLSLV---PTQLQRLLQLRPQW--LAQFRTILLG 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 732 G----EALLGKSLNFwrdnapKTRIINEYGPTETVVGCCVYEVDEqtSLSGAILIGRPIANTQLYLLDDKQklvpigvpG 807
Cdd:PRK07445 239 GapawPSLLEQARQL------QLRLAPTYGMTETASQIATLKPDD--FLAGNNSSGQVLPHAQITIPANQT--------G 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 808 ELYIGGAGVARGYLnrPELtqqrfipnpfsdEPNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQ 887
Cdd:PRK07445 303 NITIQAQSLALGYY--PQI------------LDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA 368
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2129675820 888 HPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALPQ 962
Cdd:PRK07445 369 TGLVQDVCVLGLPDPHWGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
587-960 |
1.20e-11 |
|
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: 68.56 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 587 DRDLPENATLSIDNPVSNVTSENlaYIIYTSGSTGKPKG-------------------TMIPHRGLVNYLSwctnayala 647
Cdd:cd05929 106 LEDYEAAEGGSPETPIEDEAAGW--KMLYSGGTTGRPKGikrglpggppdndtlmaaaLGFGPGADSVYLS--------- 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 648 qgyGAPVQSSIGFDATITSLFspllVGKRVVLLPEKEEIEALSALlqsdQNYslvKITPAHL--EMLNQMLP------NH 719
Cdd:cd05929 175 ---PAPLYHAAPFRWSMTALF----MGGTLVLMEKFDPEEFLRLI----ERY---RVTFAQFvpTMFVRLLKlpeavrNA 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 720 KGVTETRALIIGGE----ALLGKSLNFWrdnAPKtrIINEYGPTETVvGCCVYEVDEQTSLSGAIliGRPIANtQLYLLD 795
Cdd:cd05929 241 YDLSSLKRVIHAAApcppWVKEQWIDWG---GPI--IWEYYGGTEGQ-GLTIINGEEWLTHPGSV--GRAVLG-KVHILD 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 796 DKQKLVPIGVPGELYIGGAGvARGYLNRPELTQQrfipnpfsdEPNSRLYKT-GDLARYLPDGNIEYLGRIDHQVKIRGF 874
Cdd:cd05929 312 EDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAA---------ARNEGGWSTlGDVGYLDEDGYLYLTDRRSDMIISGGV 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 875 RIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPT----SSELRQFLQSKLPEYMIPSAFVMLEVIPLT 950
Cdd:cd05929 382 NIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAgtalAEELIAFLRDRLSRYKCPRSIEFVAELPRD 461
|
410
....*....|
gi 2129675820 951 THGKVDRQAL 960
Cdd:cd05929 462 DTGKLYRRLL 471
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
11-326 |
1.61e-11 |
|
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to the non-ribosomal peptide synthetase (NRPS); The X-domain is a catalytically inactive member of the Condensation (C) domain family of non-ribosomal peptide synthetase (NRPS). It has been shown to recruit oxygenases to the NRPS to perform side-chain crosslinking in the production of glycopeptide antibiotics. 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 this X-domain, 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, and dual E/C (epimerization and condensation) domains. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity; members of this X-domain subfamily lack the second H of this motif.
Pssm-ID: 380468 [Multi-domain] Cd Length: 440 Bit Score: 68.28 E-value: 1.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 11 QKHLWLQQK--DNYQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFhslPGmnipfqsiSDAPTYNHISLAEYD 88
Cdd:cd19546 11 QLRTWLLARldEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTF---PG--------DGGDVHQRILDADAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 89 WSRLS-SQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACLDGE 167
Cdd:cd19546 80 RPELPvVPATEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGARREGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 168 --EISEEVMQYADVSEWLNELLESEDT-ETARN----YWQQQDISSVLNLRIPFeiknDHQSSGEISFAPQSLCLAMNRD 240
Cdd:cd19546 160 apERAPLPLQFADYALWERELLAGEDDrDSLIGdqiaYWRDALAGAPDELELPT----DRPRPVLPSRRAGAVPLRLDAE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 241 TVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYD-ELKGVFGLLTKYLPIHSRLEDALKFSELME 319
Cdd:cd19546 236 VHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTFRELLG 315
|
....*..
gi 2129675820 320 RVSESLR 326
Cdd:cd19546 316 RVREAVR 322
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
488-918 |
2.17e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 68.60 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 488 HESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILL 567
Cdd:PLN02387 104 YEWITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVI 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 568 TQQRLVDKFVEHKTQ------IICLDRDLPENATLSIDN------PVSNV--------------TSENLAYIIYTSGSTG 621
Cdd:PLN02387 184 CDSKQLKKLIDISSQletvkrVIYMDDEGVDSDSSLSGSsnwtvsSFSEVeklgkenpvdpdlpSPNDIAVIMYTSGSTG 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 622 KPKGTMIPHRGLVN-----------------YLSWCTNAYAL---AQGYGAPVQSSIGFDA--TITSLFSPLLVGKR--- 676
Cdd:PLN02387 264 LPKGVMMTHGNIVAtvagvmtvvpklgkndvYLAYLPLAHILelaAESVMAAVGAAIGYGSplTLTDTSNKIKKGTKgda 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 677 VVLLPEKeeIEALSALL---------QSDQNYSLVK----ITPAHLEM-----------LNQMLPNHKGVTETRA----- 727
Cdd:PLN02387 344 SALKPTL--MTAVPAILdrvrdgvrkKVDAKGGLAKklfdIAYKRRLAaiegswfgawgLEKLLWDALVFKKIRAvlggr 421
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 728 ---LIIGGEALLGKSLNFWrdN----APktrIINEYGPTETVVGCCVYEVDEQTslsgailIGR-----PIANTQL---- 791
Cdd:PLN02387 422 irfMLSGGAPLSGDTQRFI--NiclgAP---IGQGYGLTETCAGATFSEWDDTS-------VGRvgpplPCCYVKLvswe 489
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 792 ---YLLDDKqklvPIgvP-GELYIGGAGVARGYLNRPELTQQRFIpnpfSDEPNSRLYKTGDLARYLPDGNIEYLGRIDH 867
Cdd:PLN02387 490 eggYLISDK----PM--PrGEIVIGGPSVTLGYFKNQEKTDEVYK----VDERGMRWFYTGDIGQFHPDGCLEIIDRKKD 559
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2129675820 868 QVKIR-GFRIELEEIESLLAQHPLVNAVTVIAredQPGDKRLVGYIVPKEQA 918
Cdd:PLN02387 560 IVKLQhGEYVSLGKVEAALSVSPYVDNIMVHA---DPFHSYCVALVVPSQQA 608
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
469-960 |
2.61e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 67.73 E-value: 2.61e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 469 ELFAAQVERTPNNIAVEFNH--ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD 546
Cdd:PRK05857 18 DRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMAD 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 547 PTYPQERLGFMLEDAQ-IPILLTQQRLVD--KFVEHKTQIICLDRDLPENATLSIDNPVSNVTSENLAY-------IIYT 616
Cdd:PRK05857 98 GNLPIAAIERFCQITDpAAALVAPGSKMAssAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQgsedplaMIFT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 617 SGSTGKPKGTMIPHRGL-----------VNYLSWCTNAYAlaqgYGAPVQSSIGfdaTITSLFSPLLVGKrvVLLPEKEE 685
Cdd:PRK05857 178 SGTTGEPKAVLLANRTFfavpdilqkegLNWVTWVVGETT----YSPLPATHIG---GLWWILTCLMHGG--LCVTGGEN 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 686 IEALSALLQSDQnYSLVKITPAHLEMLNQMLPNHKGVTET-RALIIGGEALLGKSLNFWRdnAPKTRIINEYGPTETvvG 764
Cdd:PRK05857 249 TTSLLEILTTNA-VATTCLVPTLLSKLVSELKSANATVPSlRLVGYGGSRAIAADVRFIE--ATGVRTAQVYGLSET--G 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 765 C---CVYEVDEQTSLSGAILIGRPIANTQLYLLDDK--QKLVPIGVP----GELYIGGAGVARGYLNRPELTQQRFIPNp 835
Cdd:PRK05857 324 CtalCLPTDDGSIVKIEAGAVGRPYPGVDVYLAATDgiGPTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVLIDG- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 836 fsdepnsrLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDqPGDKRLVGY-IVP 914
Cdd:PRK05857 403 --------WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD-EEFGALVGLaVVA 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2129675820 915 KEQ--APTSSELRQFLQSKL---PEYMI-PSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK05857 474 SAEldESAARALKHTIAARFrreSEPMArPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
7-432 |
3.46e-11 |
|
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: 67.01 E-value: 3.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 7 ISPQQKHLWLQQK---DNyQAYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGMniPFQSISDAPTY--NH 81
Cdd:cd19533 4 LTSAQRGVWFAEQldpEG-SIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGE--PYQWIDPYTPVpiRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 82 ISL--------AEYDWSRlsSQVQKAkidtlfqdtslrvFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLI 153
Cdd:cd19533 81 IDLsgdpdpegAAQQWMQ--EDLRKP-------------LPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFG 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 154 CEIGRAYTACLDGEEISE-EVMQYADVSEWLNELLESEDTETARNYWQQQdissvlnLRIPFEIkndhqssgeISFAPQ- 231
Cdd:cd19533 146 QRVAEIYTALLKGRPAPPaPFGSFLDLVEEEQAYRQSERFERDRAFWTEQ-------FEDLPEP---------VSLARRa 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 232 -SLCLAMNRDT-------VEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLP 303
Cdd:cd19533 210 pGRSLAFLRRTaelppelTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLP 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 304 IHSRLEDALKFSELMERVSESLRFVKKWQEY-----FNWENFISTNEKFaARPFF---PFCFDFTQQSQSYVNGNIAfse 375
Cdd:cd19533 290 LRLTVDPQQTFAELVAQVSRELRSLLRHQRYryedlRRDLGLTGELHPL-FGPTVnymPFDYGLDFGGVVGLTHNLS--- 365
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 2129675820 376 ykkSANIDKFQIKLSSGYSQDNLVVNFDYDANLFSEDSIKILAEQYLTLIASVTYNP 432
Cdd:cd19533 366 ---SGPTNDLSIFVYDRDDESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
468-956 |
8.74e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 66.91 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 468 HELFAAQVE----RTPNNIAVE-FNHESLTYAQLNAKSNQLAHHLQKLGVKPEVlVGICVERSLDMLIGILGILKAGgaY 542
Cdd:PRK06814 631 RTLFEALIEaakiHGFKKLAVEdPVNGPLTYRKLLTGAFVLGRKLKKNTPPGEN-VGVMLPNANGAAVTFFALQSAG--R 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 543 IPFdptypqerlgfML-------------EDAQIPILLTQQRLVDKF--------VEHKTQIICLDrDLPENATLSID-- 599
Cdd:PRK06814 708 VPA-----------MInfsagianilsacKAAQVKTVLTSRAFIEKArlgplieaLEFGIRIIYLE-DVRAQIGLADKik 775
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 600 ---------NPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGLVnylswcTNAYALAQ--GYGA--------PVQSSIGF 660
Cdd:PRK06814 776 gllagrfplVYFCNRDPDDPAVILFTSGSEGTPKGVVLSHRNLL------ANRAQVAAriDFSPedkvfnalPVFHSFGL 849
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 661 DAtitSLFSPLLVGKRVVLLPekeeiealSALlqsdqNYSLVkitPahlEMLNQMLPNHKGVTET--------------- 725
Cdd:PRK06814 850 TG---GLVLPLLSGVKVFLYP--------SPL-----HYRII---P---ELIYDTNATILFGTDTflngyaryahpydfr 907
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 726 --RALIIGGEALLGKSLNFWRDNApKTRIINEYGPTETvvgccvyevdeqtslSGAILIGRPIAN---TQLYLLDD-KQK 799
Cdd:PRK06814 908 slRYVFAGAEKVKEETRQTWMEKF-GIRILEGYGVTET---------------APVIALNTPMHNkagTVGRLLPGiEYR 971
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 800 LVPI-GVP--GELYIGGAGVARGYLnRPEltqqrfipNPFSDEPNSR-LYKTGDLARYLPDGNIEYLGRIDHQVKIRGFR 875
Cdd:PRK06814 972 LEPVpGIDegGRLFVRGPNVMLGYL-RAE--------NPGVLEPPADgWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEM 1042
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 876 IELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVgYIVPKEQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKV 955
Cdd:PRK06814 1043 ISLAAVEELAAELWPDALHAAVSIPDARKGERII-LLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKI 1121
|
.
gi 2129675820 956 D 956
Cdd:PRK06814 1122 D 1122
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
491-903 |
1.15e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 66.15 E-value: 1.15e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 491 LTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGI----LKAGGAYipfdPTYPQERLGFMLEDAQ---- 562
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIwsqsMVAATVY----ANLGEDALAYALRETEckai 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 563 ------IPILLtqqRLVDKFVEHKTQIICLDrDLPEN----------------------ATLSIDNPVSNvtsENLAYII 614
Cdd:PTZ00216 198 vcngknVPNLL---RLMKSGGMPNTTIIYLD-SLPASvdtegcrlvawtdvvakghsagSHHPLNIPENN---DDLALIM 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 615 YTSGSTGKPKGTMIPHRGLVN---------------------YLSW----------CTNAYaLAQGygapvqSSIGFDA- 662
Cdd:PTZ00216 271 YTSGTTGDPKGVMHTHGSLTAgilaledrlndligppeedetYCSYlplahimefgVTNIF-LARG------ALIGFGSp 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 663 -TITSL----------FSP-LLVG--------KRVV--LLPE----KEEI------EALSALLQS-DQNYSLVKITPAHL 709
Cdd:PTZ00216 344 rTLTDTfarphgdlteFRPvFLIGvprifdtiKKAVeaKLPPvgslKRRVfdhayqSRLRALKEGkDTPYWNEKVFSAPR 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 710 EMLNQMLpnhkgvtetRALIIGGEALLGKSLNFWrdNAPKTRIINEYGPTETVvgCCvyevdeqtslsGAI--------- 780
Cdd:PTZ00216 424 AVLGGRV---------RAMLSGGGPLSAATQEFV--NVVFGMVIQGWGLTETV--CC-----------GGIqrtgdlepn 479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 781 LIGRPIANTQLYLLD-DKQKLVPIGVP-GELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlYKTGDLARYLPDGN 858
Cdd:PTZ00216 480 AVGQLLKGVEMKLLDtEEYKHTDTPEPrGEILLRGPFLFKGYYKQEELTREVLDEDGW--------FHTGDVGSIAANGT 551
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2129675820 859 IEYLGRIDHQVK-IRGFRIELEEIESLLAQHPLV--NAVTVIAREDQP 903
Cdd:PTZ00216 552 LRIIGRVKALAKnCLGEYIALEALEALYGQNELVvpNGVCVLVHPARS 599
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
486-959 |
4.34e-10 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 63.61 E-value: 4.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 486 FNHESLTYAQLNAKSNQLAHHLQK-LGVKPEVLVGICVERSLDMLIGILGILKAGGAyipfdptypqerlgfmledaqiP 564
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA----------------------P 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 565 ILLTQQRLVDKFVeHKTQIicldrdlpENATLSIdnpvsnVTSENLAYIIYTSGSTGKPKGTMIPHRGL---VNYLS-WC 640
Cdd:cd05937 59 AFINYNLSGDPLI-HCLKL--------SGSRFVI------VDPDDPAILIYTSGTTGLPKAAAISWRRTlvtSNLLShDL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 641 TNAYALAQGYGAPV-QSSIGFDATITSLFSpllvGKRVVLLPE-------KEEIEALSALLQ----------------SD 696
Cdd:cd05937 124 NLKNGDRTYTCMPLyHGTAAFLGACNCLMS----GGTLALSRKfsasqfwKDVRDSGATIIQyvgelcryllstppspYD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 697 QNYSLVKITPahlemlNQMLPN-------HKGVTETRALIIGGEALlGKSLNFWRdNAPKTRIINEYGPTEtvvgccvye 769
Cdd:cd05937 200 RDHKVRVAWG------NGLRPDiwerfreRFNVPEIGEFYAATEGV-FALTNHNV-GDFGAGAIGHHGLIR--------- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 770 vdeQTSLSGAILIGRPIANTQLYLLDDKQ---KLVPIGVPGE----LYIGGAGVARGYLNRPELTQQRFIPNPFsdEPNS 842
Cdd:cd05937 263 ---RWKFENQVVLVKMDPETDDPIRDPKTgfcVRAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVF--RKGD 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 843 RLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHP-----LVNAVTVIAREDQPGdkRLVGYIVPKEQ 917
Cdd:cd05937 338 IYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPdiaeaNVYGVKVPGHDGRAG--CAAITLEESSA 415
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2129675820 918 APTS---SELRQFLQSKLPEYMIPsafVMLEVIPLTTHGKVDRQA 959
Cdd:cd05937 416 VPTEftkSLLASLARKNLPSYAVP---LFLRLTEEVATTDNHKQQ 457
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
605-960 |
6.57e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 63.61 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 605 VTSENLAYIIYTSGSTGKPKGTMI---PHRGLVNYLSWCTNAYALAQGYGApvQSSIGFDATITSLFSPLLVGKRVVLL- 680
Cdd:PTZ00237 251 VESSHPLYILYTSGTTGNSKAVVRsngPHLVGLKYYWRSIIEKDIPTVVFS--HSSIGWVSFHGFLYGSLSLGNTFVMFe 328
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 681 -----PEKEEIEALSALLQSDQNYSLVkiTPAHLEMLNQMLPNHKGV------TETRALIIGGEaLLGKSLNFWRDNAPK 749
Cdd:PTZ00237 329 ggiikNKHIEDDLWNTIEKHKVTHTLT--LPKTIRYLIKTDPEATIIrskydlSNLKEIWCGGE-VIEESIPEYIENKLK 405
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 750 TRIINEYGPTETvvGCC-VYEVDEQTSLSGAIliGRPIANTQLYLLDDKQKLVPIGVPGELYIG---GAGVARGYLNRPE 825
Cdd:PTZ00237 406 IKSSRGYGQTEI--GITyLYCYGHINIPYNAT--GVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDE 481
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 826 LTQQRFIPNPfsdepnsRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGD 905
Cdd:PTZ00237 482 KFKQLFSKFP-------GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCY 554
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2129675820 906 KRLVGYIVPKEQAPTSS--------ELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PTZ00237 555 NVPIGLLVLKQDQSNQSidlnklknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQII 617
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
490-963 |
7.40e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.18 E-value: 7.40e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQ 569
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 570 QRL---VDKFVEHKTQIICL---------------DRDLPENAT-----LSIDNPVSNVTSENLAYIIYTSGSTGKPKGT 626
Cdd:PRK12406 91 ADLlhgLASALPAGVTVLSVptppeiaaayrispaLLTPPAGAIdwegwLAQQEPYDGPPVPQPQSMIYTSGTTGHPKGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 627 M----IPHRGLVnYLSWCTNAYALAQG----------YGAPvqSSIGFDAtitslfspLLVGKRVVLLPeKEEIEALSAL 692
Cdd:PRK12406 171 RraapTPEQAAA-AEQMRALIYGLKPGiralltgplyHSAP--NAYGLRA--------GRLGGVLVLQP-RFDPEELLQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 693 LQSDqnyslvKITpaHLEMLNQM------LP----NHKGVTETRALIIGG--------EALLgkslNFWrdnAPktrIIN 754
Cdd:PRK12406 239 IERH------RIT--HMHMVPTMfirllkLPeevrAKYDVSSLRHVIHAAapcpadvkRAMI----EWW---GP---VIY 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 755 E-YGPTET--VVGCcvyevDEQTSLSGAILIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVAR-GYLNRPE----L 826
Cdd:PRK12406 301 EyYGSTESgaVTFA-----TSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEkraeI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 827 TQQRFIpnpfsdepnsrlyKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDK 906
Cdd:PRK12406 376 DRGGFI-------------TSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGE 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2129675820 907 RLVGYIVPKEQA-PTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALPQP 963
Cdd:PRK12406 443 ALMAVVEPQPGAtLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
489-955 |
7.73e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 63.10 E-value: 7.73e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 489 ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLT 568
Cdd:PRK13390 23 EQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 569 QQRL--------------------VDKFVEHKTQIICLDRDLPENatlsidnPVSnvtsenlAYIIYTSGSTGKPKGTM- 627
Cdd:PRK13390 103 SAALdglaakvgadlplrlsfggeIDGFGSFEAALAGAGPRLTEQ-------PCG-------AVMLYSSGTTGFPKGIQp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 628 -IPHRGLVnylSWCTNAYALAQGYGAPVQSSIGFDATITSLFSPL-------LVGKRVVLlpeKEEIEALSALLQSDQ-N 698
Cdd:PRK13390 169 dLPGRDVD---APGDPIVAIARAFYDISESDIYYSSAPIYHAAPLrwcsmvhALGGTVVL---AKRFDAQATLGHVERyR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 699 YSLVKITPA---HLEMLNQMLPNHKGVTETRALIIGGEAL---LGKSLNFWRdnAPktrIINEYGPTETVVGCCVYEVDE 772
Cdd:PRK13390 243 ITVTQMVPTmfvRLLKLDADVRTRYDVSSLRAVIHAAAPCpvdVKHAMIDWL--GP---IVYEYYSSTEAHGMTFIDSPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 773 QTSLSGAIliGRPIANTqLYLLDDKQKLVPIGVPGELYIGGAGVARGYLNRPELTQQrfipnpfSDEPNSRLYKT-GDLA 851
Cdd:PRK13390 318 WLAHPGSV--GRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA-------AQHPAHPFWTTvGDLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 852 RYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIARED-QPGDK-----RLVGYIVPKEQapTSSELR 925
Cdd:PRK13390 388 SVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDpEMGEQvkaviQLVEGIRGSDE--LARELI 465
|
490 500 510
....*....|....*....|....*....|
gi 2129675820 926 QFLQSKLPEYMIPSAFVMLEVIPLTTHGKV 955
Cdd:PRK13390 466 DYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
24-325 |
9.55e-10 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 62.33 E-value: 9.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 24 AYCTQIAINITGNLNSDILKLALANLSDRYEIFHTAFhSLPGMNIPFQSISD--APTYnhislAEYDWSRLSSQVQKAKI 101
Cdd:cd19547 23 AYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGF-TWRDRAEPLQYVRDdlAPPW-----ALLDWSGEDPDRRAELL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 102 DTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACLDGEEIS-EEVMQYADVS 180
Cdd:cd19547 97 ERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAHGREPQlSPCRPYRDYV 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 181 EWLNEllESEDTETARNYWQQ--QDISSVlnlriPF-EIKNDHQssGEISFAPQSLCLAMNRDTVEKleilQESYHTSTE 257
Cdd:cd19547 177 RWIRA--RTAQSEESERFWREylRDLTPS-----PFsTAPADRE--GEFDTVVHEFPEQLTRLVNEA----ARGYGVTTN 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2129675820 258 AILLACWQVLLWRLSGQSEIVIGAAGDGREyDELKG---VFGLLTKYLPIHSRLEDALKFSELMERVSESL 325
Cdd:cd19547 244 AISQAAWSMLLALQTGARDVVHGLTIAGRP-PELEGsehMVGIFINTIPLRIRLDPDQTVTGLLETIHRDL 313
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
491-926 |
1.03e-09 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 62.85 E-value: 1.03e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 491 LTYAQLNAKSNQLAHHLQKLGVKPEVLVGI----CVERSLDML----IG-ILGILKAGgayipFDPTYPQERLgfmlEDA 561
Cdd:PRK00174 99 ITYRELHREVCRFANALKSLGVKKGDRVAIympmIPEAAVAMLacarIGaVHSVVFGG-----FSAEALADRI----IDA 169
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 562 QIPILLT---QQR---------LVDK------FVEHktqIICLDR----------------DLPENAtlSIDNPVSNVTS 607
Cdd:PRK00174 170 GAKLVITadeGVRggkpiplkaNVDEalancpSVEK---VIVVRRtggdvdwvegrdlwwhELVAGA--SDECEPEPMDA 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 608 ENLAYIIYTSGSTGKPKG-----------TMIPHRGLVNY----LSWCTnayalaqgygapvqSSIGFdatIT----SLF 668
Cdd:PRK00174 245 EDPLFILYTSGSTGKPKGvlhttggylvyAAMTMKYVFDYkdgdVYWCT--------------ADVGW---VTghsyIVY 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 669 SPLLVGKRVVLL---PekeeiealsallqsdqNYSlvkiTPA-HLEMLNQmlpnHKgV-------TETRALIIGGEALLG 737
Cdd:PRK00174 308 GPLANGATTLMFegvP----------------NYP----DPGrFWEVIDK----HK-VtifytapTAIRALMKEGDEHPK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 738 K----SLnfwrdnapktRIINEYGptE-----------TVVG---CCVyeVDE--QTSlSGAILI--------------G 783
Cdd:PRK00174 363 KydlsSL----------RLLGSVG--EpinpeawewyyKVVGgerCPI--VDTwwQTE-TGGIMItplpgatplkpgsaT 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 784 RPIANTQLYLLDDKQKLVPIGVPGELYIGGA--GVARGYLNRPEltqqRFIPNPFSDEPNsrLYKTGDLARYLPDGNIEY 861
Cdd:PRK00174 428 RPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDHE----RFVKTYFSTFKG--MYFTGDGARRDEDGYYWI 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2129675820 862 LGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSELRQ 926
Cdd:PRK00174 502 TGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDIKGQGIYAFVTLKGGEEPSDELRK 566
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
489-932 |
4.36e-09 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 60.56 E-value: 4.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 489 ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLt 568
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALF- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 569 qqrlVDKFVEHKTQ--------IICLD------------RDLPENATLSIDNPVSNvtSENLAYIIYTSGSTGKPKGTMi 628
Cdd:cd05932 84 ----VGKLDDWKAMapgvpeglISISLpppsaancqyqwDDLIAQHPPLEERPTRF--PEQLATLIYTSGTTGQPKGVM- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 629 phrglvnyLSWCTNAYALAQGYgapvqSSIGFDATiTSLFS--PLL-VGKRV----------VLLPEKEEIEALSALLQS 695
Cdd:cd05932 157 --------LTFGSFAWAAQAGI-----EHIGTEEN-DRMLSylPLAhVTERVfveggslyggVLVAFAESLDTFVEDVQR 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 696 D---------------QNYSLVKITPAHLEMLNQM-----LPNHK-----GVTETRaLIIGGEALLGKSLNFWRDNApKT 750
Cdd:cd05932 223 ArptlffsvprlwtkfQQGVQDKIPQQKLNLLLKIpvvnsLVKRKvlkglGLDQCR-LAGCGSAPVPPALLEWYRSL-GL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 751 RIINEYGPTET-VVGCCVYEVDEQTSlsgaiLIGRPIANTQLYLLDDkqklvpigvpGELYIGGAGVARGYLNRPELTQQ 829
Cdd:cd05932 301 NILEAYGMTENfAYSHLNYPGRDKIG-----TVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAE 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 830 RFIPNPFsdepnsrlYKTGDLARYLPDGNIEYLGRIDHQVKI-RGFRIELEEIESLLAQHPLVNAVTVIArEDQPGDKRL 908
Cdd:cd05932 366 AFTADGF--------LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIG-SGLPAPLAL 436
|
490 500
....*....|....*....|....*..
gi 2129675820 909 V---GYIVPKEQAPTSSELRQFLQSKL 932
Cdd:cd05932 437 VvlsEEARLRADAFARAELEASLRAHL 463
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
571-950 |
6.37e-09 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 60.16 E-value: 6.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 571 RLVDKF--VEHKTQIICLDRDLPENATLSIDnpvsnVTSENLAYIIYTSGSTGKPKGTMIPHRgLVnylswcTNAYALAQ 648
Cdd:cd17632 189 RLAAVGipVTTLTLIAVRGRDLPPAPLFRPE-----PDDDPLALLIYTSGSTGTPKGAMYTER-LV------ATFWLKVS 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 649 GYGAPVQSsigfdATITSLFSPLL-VGKRVVLlpekeeIEALSA------LLQSD-----QNYSLVKIT-----PAHLEM 711
Cdd:cd17632 257 SIQDIRPP-----ASITLNFMPMShIAGRISL------YGTLARggtayfAAASDmstlfDDLALVRPTelflvPRVCDM 325
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 712 LNQML------PNHKGV----------TETRALIIGGE--------ALLGKSLNFWRDNAPKTRIINEYGPTETvvgccv 767
Cdd:cd17632 326 LFQRYqaeldrRSVAGAdaetlaervkAELRERVLGGRllaavcgsAPLSAEMKAFMESLLDLDLHDGYGSTEA------ 399
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 768 yevdeqtslsGAILI-GR----PIANTQL-------YLLDDKqklvpigvP---GELYIGGAGVARGYLNRPELTQQRFI 832
Cdd:cd17632 400 ----------GAVILdGVivrpPVLDYKLvdvpelgYFRTDR--------PhprGELLVKTDTLFPGYYKRPEVTAEVFD 461
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 833 PNPFsdepnsrlYKTGD-LARYLPDgNIEYLGRIDHQVKI-RGFRIELEEIESLLAQHPLVNAVTVIAREDQpgdKRLVG 910
Cdd:cd17632 462 EDGF--------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYGNSER---AYLLA 529
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 2129675820 911 YIVPKEQAP-------TSSELRQFLQ-----SKLPEYMIPSAFVmLEVIPLT 950
Cdd:cd17632 530 VVVPTQDALagedtarLRAALAESLQriareAGLQSYEIPRDFL-IETEPFT 580
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
520-961 |
7.50e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 59.66 E-value: 7.50e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 520 ICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQrlVDKFVEHktqiicldrdlpenatlsid 599
Cdd:PRK08308 37 VCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLLYGE--SDFTKLE-------------------- 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 600 npVSNVTSENLAYIIYTSGSTGKPK-----GTMIpHRGLVNYLSWCTNAYALAQGYGAPVQSSIGFdatITSLFSPLLVG 674
Cdd:PRK08308 95 --AVNYLAEEPSLLQYSSGTTGEPKlirrsWTEI-DREIEAYNEALNCEQDETPIVACPVTHSYGL---ICGVLAALTRG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 675 KRVVLLPEKEEIEALSALLQSDQNysLVKITPAHLEMLNQMLPnhKGVTETRALIIGgeALLGKSLnFWRDNAPKTRIIN 754
Cdd:PRK08308 169 SKPVIITNKNPKFALNILRNTPQH--ILYAVPLMLHILGRLLP--GTFQFHAVMTSG--TPLPEAW-FYKLRERTTYMMQ 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 755 EYGPTETvvGCCVYEVDEQTSLSgailIGRPIANTQLYLLDDKQKlvpigvPGELYIggagvargylnrpeltqqrfipn 834
Cdd:PRK08308 242 QYGCSEA--GCVSICPDMKSHLD----LGNPLPHVSVSAGSDENA------PEEIVV----------------------- 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 835 pfsdEPNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRlVGYIVP 914
Cdd:PRK08308 287 ----KMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGER-VKAKVI 361
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2129675820 915 KEQAPTSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALP 961
Cdd:PRK08308 362 SHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
11-422 |
2.12e-08 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 59.20 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 11 QKHLWLQQkdnyqayctqIAINITGNLNSDILKLALANLSDRYEIFHTAFHSLPGmnipfqsisdAPTYNHISLAEYDWS 90
Cdd:PRK12316 3655 ERHHWNQS----------LLLKPREALDAAALEAALQALVEHHDALRLRFVEDAG----------GWTAEHLPVELGGAL 3714
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 91 RLSSQVQKAKIDTLFQDTSLRVFDFEQATNLHFILGKLATDQHILFISLPALYADKTTLNYLICEIGRAYTACLDGE--E 168
Cdd:PRK12316 3715 LWRAELDDAEELERLGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEapR 3794
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 169 ISEEVMQYADVSEWLNELLESEDTETARNYWQQQ--DISSvlnlripfEIKNDHQSSGEISFAPQSLCLAMNRDTVEKLe 246
Cdd:PRK12316 3795 LPAKTSSFKAWAERLQEHARGEALKAELAYWQEQlqGVSS--------ELPCDHPQGALQNRHAASVQTRLDRELTRRL- 3865
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 247 iLQES---YHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGRE--YDE--LKGVFGLLTKYLPIhsRLEDALKFSELME 319
Cdd:PRK12316 3866 -LQQApaaYRTQVNDLLLTALARVVCRWTGEASALVQLEGHGREdlFADidLSRTVGWFTSLFPV--RLSPVEDLGASIK 3942
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 320 RVSESLRFVKKWQEYFNWENFI---STNEKFAARPFFPFCFDFTQQSQSYVN---------GNIAFSEYKKSANIDKFqI 387
Cdd:PRK12316 3943 AIKEQLRAIPNKGIGFGLLRYLgdeESRRTLAGLPVPRITFNYLGQFDGSFDeemalfvpaGESAGAEQSPDAPLDNW-L 4021
|
410 420 430
....*....|....*....|....*....|....*
gi 2129675820 388 KLSSGYSQDNLVVNFDYDANLFSEDSIKILAEQYL 422
Cdd:PRK12316 4022 SLNGRVYGGELSLDWTFSREMFEEATIQRLADDYA 4056
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
518-960 |
5.50e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 57.34 E-value: 5.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 518 VGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQrlvdkfvEHKTQIICLDrdLPENATLS 597
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLNTTRRGAALAADIRRADCQLLVTDA-------EHRPLLDGLD--LPGVRVLD 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 598 ID--------------NPVSNVTSENLAYIIYTSGSTGKPKGTMIPHrGLVNYLswctnAYALAQGYGApVQSSIGFDA- 662
Cdd:PRK13388 126 VDtpayaelvaaagalTPHREVDAMDPFMLIFTSGTTGAPKAVRCSH-GRLAFA-----GRALTERFGL-TRDDVCYVSm 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 663 ------TITSLFSPLLVGKRVVLLPEKeeieaLSA--LLQSDQNY------------SLVKITPAHlemlnqmlPNHKGV 722
Cdd:PRK13388 199 plfhsnAVMAGWAPAVASGAAVALPAK-----FSAsgFLDDVRRYgatyfnyvgkplAYILATPER--------PDDADN 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 723 TETRALiiGGEALLGKSLNFWRDNApkTRIINEYGPTETVVGCcvyeVDEQTSLSGAIliGRPIANTQLYlldDKQKLVP 802
Cdd:PRK13388 266 PLRVAF--GNEASPRDIAEFSRRFG--CQVEDGYGSSEGAVIV----VREPGTPPGSI--GRGAPGVAIY---NPETLTE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 803 IGVP---------------GELY-IGGAGVARGYLNRPELTQQRFipnpfsdepnsR--LYKTGDLARYLPDGNIEYLGR 864
Cdd:PRK13388 333 CAVArfdahgallnadeaiGELVnTAGAGFFEGYYNNPEATAERM-----------RhgMYWSGDLAYRDADGWIYFAGR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 865 IDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQ-PGDKRLVGYIVPKEQAPTSSELRQFL--QSKLPEYMIPSAF 941
Cdd:PRK13388 402 TADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDErVGDQVMAALVLRDGATFDPDAFAAFLaaQPDLGTKAWPRYV 481
|
490
....*....|....*....
gi 2129675820 942 VMLEVIPLTTHGKVDRQAL 960
Cdd:PRK13388 482 RIAADLPSTATNKVLKREL 500
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
999-1050 |
9.12e-08 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 50.71 E-value: 9.12e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2129675820 999 IGIKDSFFELGGHSLLAVRLMAHINQEFGKNLALATLFQNPTIEKLANLLRQ 1050
Cdd:smart00823 33 IDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
480-701 |
1.26e-07 |
|
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: 56.20 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 480 NNIAVEFNheSLTYAQLNAKSNQLAHHLQ-KLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFML 558
Cdd:cd05905 6 DSKGKEAT--TLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 559 EDAQIPILLTQqrlvdkFVEHKTQIICLDRDLPenATLSIDN---PVSNVTS---------------------ENLAYII 614
Cdd:cd05905 84 GTCKVRVALTV------EACLKGLPKKLLKSKT--AAEIAKKkgwPKILDFVkipkskrsklkkwgphpptrdGDTAYIE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 615 YTSGSTGKPKGTMIPHRGLvnyLSWCTNAYALAQGY-------GAPVQSSIGFDATI-TSLFSpllvGKRVVLLPEKEEI 686
Cdd:cd05905 156 YSFSSDGSLSGVAVSHSSL---LAHCRALKEACELYesrplvtVLDFKSGLGLWHGClLSVYS----GHHTILIPPELMK 228
|
250
....*....|....*
gi 2129675820 687 EALSALLQSDQNYSL 701
Cdd:cd05905 229 TNPLLWLQTLSQYKV 243
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
615-960 |
1.45e-07 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 55.80 E-value: 1.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 615 YTSGSTGKPKGTMIPHRGLvnYLS-----------------WC-----TNAYALAQGYGAPVQSSIGFD----------- 661
Cdd:PLN03102 193 YTSGTTADPKGVVISHRGA--YLStlsaiigwemgtcpvylWTlpmfhCNGWTFTWGTAARGGTSVCMRhvtapeiykni 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 662 --------ATITSLFSPLLVGKRVVLLPEKEEIEALSAllQSDQNYSLVKitpaHLEMLNQMLPNHKGVTETRALIIGGE 733
Cdd:PLN03102 271 emhnvthmCCVPTVFNILLKGNSLDLSPRSGPVHVLTG--GSPPPAALVK----KVQRLGFQVMHAYGLTEATGPVLFCE 344
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 734 allgkslnfWRDNAPKTriineygPTETVVgccvyEVDEQTSLSGAILIGRPIANTQlyllddKQKLVPIG--VPGELYI 811
Cdd:PLN03102 345 ---------WQDEWNRL-------PENQQM-----ELKARQGVSILGLADVDVKNKE------TQESVPRDgkTMGEIVI 397
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 812 GGAGVARGYLNRPELTQQRFipnpfsdepNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLV 891
Cdd:PLN03102 398 KGSSIMKGYLKNPKATSEAF---------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKV 468
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 892 NAVTVIA----------------REDQPGDKRLVGYIVPKEQaptssELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKV 955
Cdd:PLN03102 469 LETAVVAmphptwgetpcafvvlEKGETTKEDRVDKLVTRER-----DLIEYCRENLPHFMCPRKVVFLQELPKNGNGKI 543
|
....*
gi 2129675820 956 DRQAL 960
Cdd:PLN03102 544 LKPKL 548
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
490-971 |
1.81e-07 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 55.67 E-value: 1.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 490 SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQ 569
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDCKPKVVITC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 570 QRlvdkfVEHKTQIICL----DRDLPENAT--------LSIDN------------------------------PVSNVTS 607
Cdd:PLN02654 200 NA-----VKRGPKTINLkdivDAALDESAKngvsvgicLTYENqlamkredtkwqegrdvwwqdvvpnyptkcEVEWVDA 274
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 608 ENLAYIIYTSGSTGKPKGTMIPHRGLVNYLS---------------WCTNAYALAQGYgapvqssigfdATITslFSPLL 672
Cdd:PLN02654 275 EDPLFLLYTSGSTGKPKGVLHTTGGYMVYTAttfkyafdykptdvyWCTADCGWITGH-----------SYVT--YGPML 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 673 VGKRVVLLpekeeiEALSALLQSDQNYSLV---KITPAHlemlnqmlpnhKGVTETRALIIGGEALLGkslnfwRDNAPK 749
Cdd:PLN02654 342 NGATVLVF------EGAPNYPDSGRCWDIVdkyKVTIFY-----------TAPTLVRSLMRDGDEYVT------RHSRKS 398
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 750 TRIINEYG----PTE-----TVVG---CCVYEVDEQTSLSGAILIGRPIA-------------NTQLYLLDDKQKLVPIG 804
Cdd:PLN02654 399 LRVLGSVGepinPSAwrwffNVVGdsrCPISDTWWQTETGGFMITPLPGAwpqkpgsatfpffGVQPVIVDEKGKEIEGE 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 805 VPGELYIGGA--GVAR---GYLNRPELTQQRfipnPFSDepnsrLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELE 879
Cdd:PLN02654 479 CSGYLCVKKSwpGAFRtlyGDHERYETTYFK----PFAG-----YYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTA 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 880 EIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSELRQFL----QSKLPEYMIPSAFVMLEVIPLTTHGKV 955
Cdd:PLN02654 550 EVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSEELRKSLiltvRNQIGAFAAPDKIHWAPGLPKTRSGKI 629
|
570
....*....|....*.
gi 2129675820 956 DRQALPQPDTSRLDTL 971
Cdd:PLN02654 630 MRRILRKIASRQLDEL 645
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
807-960 |
2.56e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 55.07 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 807 GELY-IGGAGVARGYLNRPELTQQRFipnpfsdepNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLL 885
Cdd:PRK07867 353 GELVnTAGPGGFEGYYNDPEADAERM---------RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERIL 423
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2129675820 886 AQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAP-TSSELRQFL--QSKLPEYMIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:PRK07867 424 LRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKfDPDAFAEFLaaQPDLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
807-960 |
9.68e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 53.03 E-value: 9.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 807 GELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlyKTGDLARYLPDGNIeylgridhQVKIR--------GFRIEL 878
Cdd:PRK08162 389 GEIMFRGNIVMKGYLKNPKATEEAFAGGWF---------HTGDLAVLHPDGYI--------KIKDRskdiiisgGENISS 451
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 879 EEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAP-TSSELRQFLQSKLPEYMIPSAFVMLEvIPLTTHGKVDR 957
Cdd:PRK08162 452 IEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASaTEEEIIAHCREHLAGFKVPKAVVFGE-LPKTSTGKIQK 530
|
...
gi 2129675820 958 QAL 960
Cdd:PRK08162 531 FVL 533
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
489-957 |
1.19e-06 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 53.09 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 489 ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFD-PT-------YpQERLGFMLED 560
Cdd:PRK09192 48 EALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMgfggresY-IAQLRGMLAS 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 561 AQIPILLTQQRLVDkFVEHKTQIICL-------DRDLPENAtlsiDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGL 633
Cdd:PRK09192 127 AQPAAIITPDELLP-WVNEATHGNPLlhvlshaWFKALPEA----DVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 634 VnylswcTNAYALAQgYGAPVQSS---------------IGFdatitsLFSPLLVGKRVVLLPEKE-EIEALSALLQSDQ 697
Cdd:PRK09192 202 M------ANLRAISH-DGLKVRPGdrcvswlpfyhdmglVGF------LLTPVATQLSVDYLPTRDfARRPLQWLDLISR 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 698 NYSLVKITPAHLEMLNQMLPNHKGVTET-----RALIIGGEALLGKSL-NF--------WRDNApktrIINEYGPTETVV 763
Cdd:PRK09192 269 NRGTISYSPPFGYELCARRVNSKDLAELdlscwRVAGIGADMIRPDVLhQFaeafapagFDDKA----FMPSYGLAEATL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 764 ---------GCCVYEVDEQTsLSGA----------------ILIGRPIANTQLYLLDDKQKLVPIGVPGELYIGGAGVAR 818
Cdd:PRK09192 345 avsfsplgsGIVVEEVDRDR-LEYQgkavapgaetrrvrtfVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMS 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 819 GYLNRPElTQQRFIPNPFSDepnsrlykTGDLArYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNA--VTV 896
Cdd:PRK09192 424 GYFRDEE-SQDVLAADGWLD--------TGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSgdAAA 493
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 897 IAREDQPGDKrlvgyIVPKEQAPTSS-ELRQFLQSKLPEyMIPSAF---VMLEV-----IPLTTHGKVDR 957
Cdd:PRK09192 494 FSIAQENGEK-----IVLLVQCRISDeERRGQLIHALAA-LVRSEFgveAAVELvpphsLPRTSSGKLSR 557
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
845-960 |
1.29e-06 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 52.82 E-value: 1.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 845 YKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSEL 924
Cdd:cd05915 391 FRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPRGEKPTPEEL 470
|
90 100 110
....*....|....*....|....*....|....*..
gi 2129675820 925 RQFLQSKLPEY-MIPSAFVMLEVIPLTTHGKVDRQAL 960
Cdd:cd05915 471 NEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
1073-1331 |
2.89e-06 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 49.53 E-value: 2.89e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1073 FCLPG---GGGNVLYLHeLARDLGSEQTFYGLQAPGLnGESDPLT-SVEEMAAYYIQAIQSVQPEGPYFLGGHSFGGIVA 1148
Cdd:smart00824 1 ICFPStaaPSGPHEYAR-LAAALRGRRDVSALPLPGF-GPGEPLPaSADALVEAQAEAVLRAAGGRPFVLVGHSSGGLLA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1149 YEIAQQLVKSGHEVALVAILDAPAP----VASDKP-----IYIDVDDATRLTET--------ARLIERWagkslnisyei 1211
Cdd:smart00824 79 HAVAARLEARGIPPAAVVLLDTYPPgdpaPEGWLPellrgVFEREDSFVPMDDArltamgayLRLFGGW----------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1212 lQPLELDAqleylkeqliavgllPTgtetkqvrglvqvfetnlqasikyspqevyphrlTLLRAREVNAEDAALLTELRQ 1291
Cdd:smart00824 148 -TPGPVAA---------------PT----------------------------------LLVRASEPLAEWPDEDPDGWR 177
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 2129675820 1292 dPAWGwgqFSTEKVDihiVPGDHMTMMTQpHISSVAKQLR 1331
Cdd:smart00824 178 -AHWP---LPHTVVD---VPGDHFTMMEE-HAAATARAVH 209
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
1064-1201 |
3.02e-06 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 49.61 E-value: 3.02e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1064 QTGNSQYPFFCLPGGGGNVLYLHELARDLGSEQTFYGLQAPGLnGESDPLT---SVEEMAAYYIQAIQSVQPEgPYFLGG 1140
Cdd:COG0596 18 EAGPDGPPVVLLHGLPGSSYEWRPLIPALAAGYRVIAPDLRGH-GRSDKPAggyTLDDLADDLAALLDALGLE-RVVLVG 95
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2129675820 1141 HSFGGIVAYEIAQQ---LVKsghevALVAILDAPAPVAsdKPIYIDVDDATRLTETARLIERWA 1201
Cdd:COG0596 96 HSMGGMVALELAARhpeRVA-----GLVLVDEVLAALA--EPLRRPGLAPEALAALLRALARTD 152
|
|
| PldB |
COG2267 |
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism]; |
1075-1175 |
3.37e-06 |
|
Lysophospholipase, alpha-beta hydrolase superfamily [Lipid transport and metabolism];
Pssm-ID: 441868 [Multi-domain] Cd Length: 221 Bit Score: 49.62 E-value: 3.37e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1075 LPGGGGNVLYLHELARDLGSEQ-TFYGLQAPGlNGESDPLTSVEEMAAYYIQAIQSV------QPEGPYFLGGHSFGGIV 1147
Cdd:COG2267 34 VHGLGEHSGRYAELAEALAAAGyAVLAFDLRG-HGRSDGPRGHVDSFDDYVDDLRAAldalraRPGLPVVLLGHSMGGLI 112
|
90 100
....*....|....*....|....*...
gi 2129675820 1148 AYEIAQQLvksGHEVALVaILDAPAPVA 1175
Cdd:COG2267 113 ALLYAARY---PDRVAGL-VLLAPAYRA 136
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
848-954 |
4.10e-06 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 51.12 E-value: 4.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 848 GDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSSELRQF 927
Cdd:cd05943 489 GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDELRKR 568
|
90 100 110
....*....|....*....|....*....|.
gi 2129675820 928 LQSKLPEYM----IPSAFVMLEVIPLTTHGK 954
Cdd:cd05943 569 IRSTIRSALsprhVPAKIIAVPDIPRTLSGK 599
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
756-892 |
1.13e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 49.72 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 756 YGPTETVVGCCVYEVDEQTSLSgailIGRPIANTQLYLLDDKQKLVPIGVP--GELYIGGAGVARGYLNRPELTQQRFIP 833
Cdd:PTZ00342 493 YGLTETTGPIFVQHADDNNTES----IGGPISPNTKYKVRTWETYKATDTLpkGELLIKSDSIFSGYFLEKEQTKNAFTE 568
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 834 NPFsdepnsrlYKTGDLARYLPDGNIEYLGRIDHQVKI-RGFRIELEEIESLLAQHPLVN 892
Cdd:PTZ00342 569 DGY--------FKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIETDMLNNLYSQISFIN 620
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
726-917 |
1.54e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 49.43 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 726 RALIIGGEALLGKSLNFWRDNAPkTRIINEYGPTETVVGCCVYEVDEQtSLSGAIliGRPIANTQLYLLD-DKQKLVPIG 804
Cdd:PLN02430 386 RLLISGGAPLSTEIEEFLRVTSC-AFVVQGYGLTETLGPTTLGFPDEM-CMLGTV--GAPAVYNELRLEEvPEMGYDPLG 461
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 805 VP--GELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlyKTGDLARYLPDGNIEYLGRIDHQVKI-RGFRIELEEI 881
Cdd:PLN02430 462 EPprGEICVRGKCLFSGYYKNPELTEEVMKDGWF---------HTGDIGEILPNGVLKIIDRKKNLIKLsQGEYVALEYL 532
|
170 180 190
....*....|....*....|....*....|....*.
gi 2129675820 882 ESLLAQHPLVNAVTVIAREDQPgdkRLVGYIVPKEQ 917
Cdd:PLN02430 533 ENVYGQNPIVEDIWVYGDSFKS---MLVAVVVPNEE 565
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
464-896 |
3.37e-05 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 48.48 E-value: 3.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 464 DKCLhELFAAQVERTPNNIAVEFNHES---------LTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILG 534
Cdd:PLN02614 45 DSCW-DVFRMSVEKYPNNPMLGRREIVdgkpgkyvwQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 535 ILKAGGAYIPFDPTYPQERLGFMLEDAQIPILLTQQRLVDKFV---------------------EHKTQ-------IICL 586
Cdd:PLN02614 124 CNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISELFktcpnsteymktvvsfggvsrEQKEEaetfglvIYAW 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 587 DRDLPENATLSIDNPVSNvtSENLAYIIYTSGSTGKPKGTMIPHRGLVN---------------------YLSWCTNAYA 645
Cdd:PLN02614 204 DEFLKLGEGKQYDLPIKK--KSDICTIMYTSGTTGDPKGVMISNESIVTliagvirllksanaaltvkdvYLSYLPLAHI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 646 LAQGYGA---PVQSSIGF-DATITSLFSPLLVGKRVVLLPEKEEIEALSALLQS-------------DQNYSL----VKI 704
Cdd:PLN02614 282 FDRVIEEcfiQHGAAIGFwRGDVKLLIEDLGELKPTIFCAVPRVLDRVYSGLQKklsdggflkkfvfDSAFSYkfgnMKK 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 705 TPAHLE---MLNQMLPNH--KGVTETRALIIGGEALLGKSLNFWRDNAPKTRIINEYGPTETVVGCCVYEVDEQTSLSga 779
Cdd:PLN02614 362 GQSHVEaspLCDKLVFNKvkQGLGGNVRIILSGAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLG-- 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 780 iLIGRPIANTQLYL--LDDKQKLVPIGVP-GELYIGGAGVARGYLNRPELTQQRFIPNpfsdepnsrLYKTGDLARYLPD 856
Cdd:PLN02614 440 -TVGPPVPNVDIRLesVPEMEYDALASTPrGEICIRGKTLFSGYYKREDLTKEVLIDG---------WLHTGDVGEWQPN 509
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2129675820 857 GNIEYLGRIDHQVKI-RGFRIELEEIESLLAQHPLVNAVTV 896
Cdd:PLN02614 510 GSMKIIDRKKNIFKLsQGEYVAVENIENIYGEVQAVDSVWV 550
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
482-960 |
3.53e-05 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 48.02 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 482 IAVEFNHE-SLTYAQLNAKSNQLAHHLQKLGVKP--EVLV--GICVERSLDML----IGILGILKAGGayipfdptYPQE 552
Cdd:PRK10524 75 VSTETDEErTYTFRQLHDEVNRMAAMLRSLGVQRgdRVLIymPMIAEAAFAMLacarIGAIHSVVFGG--------FASH 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 553 RLGFMLEDAQiPILLTQ-------------QRLVDKFV---EHKTQ-IICLDRDLPEN----------ATL---SIDN-- 600
Cdd:PRK10524 147 SLAARIDDAK-PVLIVSadagsrggkvvpyKPLLDEAIalaQHKPRhVLLVDRGLAPMarvagrdvdyATLraqHLGArv 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 601 PVSNVTSENLAYIIYTSGSTGKPKGTmipHRGLVNYlswctnAYALAQGY-----GAPVQ-----SSIGF---DATItsL 667
Cdd:PRK10524 226 PVEWLESNEPSYILYTSGTTGKPKGV---QRDTGGY------AVALATSMdtifgGKAGEtffcaSDIGWvvgHSYI--V 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 668 FSPLLVGKRVVL---LPekeeiealsalLQSDQN--YSLV---KIT-----PAHLEMLNQ----MLPNHKgVTETRALII 730
Cdd:PRK10524 295 YAPLLAGMATIMyegLP-----------TRPDAGiwWRIVekyKVNrmfsaPTAIRVLKKqdpaLLRKHD-LSSLRALFL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 731 GGEALlGKSLNFWRDNAPKTRIINEYGPTET-------VVGccvyeVDEQTSLSGAIliGRPIANTQLYLLDDK-QKLVP 802
Cdd:PRK10524 363 AGEPL-DEPTASWISEALGVPVIDNYWQTETgwpilaiARG-----VEDRPTRLGSP--GVPMYGYNVKLLNEVtGEPCG 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 803 IGVPGELYIGGAgVARGYLNRPELTQQRFIPNPFSDEpNSRLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIE 882
Cdd:PRK10524 435 PNEKGVLVIEGP-LPPGCMQTVWGDDDRFVKTYWSLF-GRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIE 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 883 SLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAPTSS---------ELRQFLQSKLPEYMIPSAFVMLEVIPLTTHG 953
Cdd:PRK10524 513 ESISSHPAVAEVAVVGVKDALKGQVAVAFVVPKDSDSLADrearlalekEIMALVDSQLGAVARPARVWFVSALPKTRSG 592
|
....*..
gi 2129675820 954 KVDRQAL 960
Cdd:PRK10524 593 KLLRRAI 599
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
462-865 |
3.70e-05 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 47.95 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 462 PHDKCLHELFAAQVERTPNNIAV---EFNHE--SLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGIL 536
Cdd:PRK08180 36 DYPRRLTDRLVHWAQEAPDRVFLaerGADGGwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAM 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 537 KAGGAYIPFDPTYPQ-----ERLGFMLEdaqipiLLTQ-----------QRLVDKFVEHKTQIICLDRDLPENATLS--- 597
Cdd:PRK08180 116 YAGVPYAPVSPAYSLvsqdfGKLRHVLE------LLTPglvfaddgaafARALAAVVPADVEVVAVRGAVPGRAATPfaa 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 598 ---------IDNPVSNVTSENLAYIIYTSGSTGKPKGTMIPHRGL---------------------VNYLSWC----TNA 643
Cdd:PRK08180 190 llatpptaaVDAAHAAVGPDTIAKFLFTSGSTGLPKAVINTHRMLcanqqmlaqtfpflaeeppvlVDWLPWNhtfgGNH 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 644 ---YALAQG---Y---GAPVQSsiGFDATITSL--FSPLL---VGKRV-VLLPEKEEIEALSALLqsdqnYSLVKIT--- 705
Cdd:PRK08180 270 nlgIVLYNGgtlYiddGKPTPG--GFDETLRNLreISPTVyfnVPKGWeMLVPALERDAALRRRF-----FSRLKLLfya 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 706 ----PAHL-EMLNQMlpnhkgvtetraliigGEALLGKslnfwrdnapKTRIINEYGPTETVvGCCVYeVDEQTSLSGai 780
Cdd:PRK08180 343 gaalSQDVwDRLDRV----------------AEATCGE----------RIRMMTGLGMTETA-PSATF-TTGPLSRAG-- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 781 LIGRPIANTQLyllddkqKLVPIGVPGELYIGGAGVARGYLNRPELTQQRFipnpfsDEPNsrLYKTGDLARYL----PD 856
Cdd:PRK08180 393 NIGLPAPGCEV-------KLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAF------DEEG--YYRSGDAVRFVdpadPE 457
|
....*....
gi 2129675820 857 GNIEYLGRI 865
Cdd:PRK08180 458 RGLMFDGRI 466
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
489-962 |
5.72e-05 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 47.47 E-value: 5.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 489 ESLTYAQLNAKSNQLAHHLQ-KLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILL 567
Cdd:PRK05620 37 EQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 568 TQQRLVDKFVEHKTQIICLD--------------RDLPENATL----------SIDNPVSNVTSENLAYIIYTSGSTGKP 623
Cdd:PRK05620 117 ADPRLAEQLGEILKECPCVRavvfigpsdadsaaAHMPEGIKVysyealldgrSTVYDWPELDETTAAAICYSTGTTGAP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 624 KGTMIPHRGLvnYLS----WCTNAYALAQGY----GAPVQSSIGFDATITSLFS--PLLVGKRVVLLPEKEEIEAlSALL 693
Cdd:PRK05620 197 KGVVYSHRSL--YLQslslRTTDSLAVTHGEsflcCVPIYHVLSWGVPLAAFMSgtPLVFPGPDLSAPTLAKIIA-TAMP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 694 QSDQNYSLVKItpahlEMLNQMLPNHKGVTETRALIIGGEALLGKSLNFWRDNApKTRIINEYGPTETV-VGCCVYE--- 769
Cdd:PRK05620 274 RVAHGVPTLWI-----QLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERY-GVDVVHVWGMTETSpVGTVARPpsg 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 770 VDEQTSLSGAILIGRPIANTQLYLLDDKQKLVPIGV-PGELYIGGAGVARGYLNRPELTQ----QRFIPNPFSDEPNS-- 842
Cdd:PRK05620 348 VSGEARWAYRVSQGRFPASLEYRIVNDGQVMESTDRnEGEIQVRGNWVTASYYHSPTEEGggaaSTFRGEDVEDANDRft 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 843 --RLYKTGDLARYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRLVGYIVPKEQAP- 919
Cdd:PRK05620 428 adGWLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEp 507
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2129675820 920 ---TSSELRQFLQSKLPEYMIPSAFVMLEVIPLTTHGKVDRQALPQ 962
Cdd:PRK05620 508 treTAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
613-918 |
9.61e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 46.76 E-value: 9.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 613 IIYTSGSTGKPKGTMIPHRGLV---------------------NYLSWCTNAYALAQ---GYGAPVQSSIGF-DATITSL 667
Cdd:PLN02861 225 IMYTSGTTGEPKGVILTNRAIIaevlstdhllkvtdrvateedSYFSYLPLAHVYDQvieTYCISKGASIGFwQGDIRYL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 668 FSPLLVGKRVVL--LPEKEE------IEALSA-------LLQSDQNYSLVKitpahlemLNQMLPNHKGVTETRALIIGG 732
Cdd:PLN02861 305 MEDVQALKPTIFcgVPRVYDriytgiMQKISSggmlrkkLFDFAYNYKLGN--------LRKGLKQEEASPRLDRLVFDK 376
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 733 --EALLGKSLNFWRDNAPKTRIINE-------------YGPTETVVGCCVYEVDEqTSLSGAIliGRPIANTQLYLLD-- 795
Cdd:PLN02861 377 ikEGLGGRVRLLLSGAAPLPRHVEEflrvtscsvlsqgYGLTESCGGCFTSIANV-FSMVGTV--GVPMTTIEARLESvp 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 796 ----DKQKLVPigvPGELYIGGAGVARGYLNRPELTQQRFIPNPFsdepnsrlyKTGDLARYLPDGNIEYLGRIDHQVKI 871
Cdd:PLN02861 454 emgyDALSDVP---RGEICLRGNTLFSGYHKRQDLTEEVLIDGWF---------HTGDIGEWQPNGAMKIIDRKKNIFKL 521
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 2129675820 872 -RGFRIELEEIESLLAQHPLVNAVTVIAREdqpGDKRLVGYIVPKEQA 918
Cdd:PLN02861 522 sQGEYVAVENLENTYSRCPLIASIWVYGNS---FESFLVAVVVPDRQA 566
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
1072-1183 |
1.53e-04 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 44.39 E-value: 1.53e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1072 FFCLPGGGGNVLYLHELARDLGseqTFYGLQAPGLNGESDPLTSVEEMAAYyIQAIQSVQPEGPYFLGGHSFGGIVAYEI 1151
Cdd:pfam12697 1 VVLVHGAGLSAAPLAALLAAGV---AVLAPDLPGHGSSSPPPLDLADLADL-AALLDELGAARPVVLVGHSLGGAVALAA 76
|
90 100 110
....*....|....*....|....*....|..
gi 2129675820 1152 AQQLVKSGhevALVAILDAPAPVASDKPIYID 1183
Cdd:pfam12697 77 AAAALVVG---VLVAPLAAPPGLLAALLALLA 105
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
770-957 |
1.89e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 45.53 E-value: 1.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 770 VDEQTSLSG------AILiGRPIANTQLYLL--DDKQKLVPIGVpGELYIGGAGVARGYLNRPELTQQRFIPnpfsdepn 841
Cdd:PRK05851 330 VDEVTTDDGsgarrhAVL-GNPIPGMEVRISpgDGAAGVAGREI-GEIEIRGASMMSGYLGQAPIDPDDWFP-------- 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 842 srlykTGDLArYLPDGNIEYLGRIDHQVKIRGFRIELEEIESLLAQHPLVNAVTVIAREDQPGDKRlVGYIVPKE----- 916
Cdd:PRK05851 400 -----TGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSAR-PGLVIAAEfrgpd 472
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 2129675820 917 QAPTSSELRQFLQSKLPeyMIPSAFVMLE--VIPLTTHGKVDR 957
Cdd:PRK05851 473 EAGARSEVVQRVASECG--VVPSDVVFVApgSLPRTSSGKLRR 513
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
489-630 |
2.14e-04 |
|
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very long-chain fatty acid CoA synthetase is named bubblegum because Drosophila melanogaster mutant bubblegum (BGM) has elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene of this family. The human homolog (hsBG) 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. VL-FACS is involved in the first reaction step of very long chain fatty acid degradation. It 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: 341256 [Multi-domain] Cd Length: 596 Bit Score: 45.81 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 489 ESLTYAQLNAKSNQLAHHLQKLGVKPEVLVGICVERSLDMLIGILGILKAGGAYIPFDPTYPQERLGFMLEDAQIPILL- 567
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 568 -TQQRL-----VDKFVEHKTQIICLDRDLPE------------NATLSI-----DNPVSNVTSENLAYIIYTSGSTGKPK 624
Cdd:cd05933 87 eNQKQLqkilqIQDKLPHLKAIIQYKEPLKEkepnlyswdefmELGRSIpdeqlDAIISSQKPNQCCTLIYTSGTTGMPK 166
|
....*.
gi 2129675820 625 GTMIPH 630
Cdd:cd05933 167 GVMLSH 172
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
6-304 |
4.46e-04 |
|
Condensation family domain with an atypical active site motif; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. Members of this subfamily typically have a non-canonical conserved SHXXXDX(14)Y motif. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380460 [Multi-domain] Cd Length: 395 Bit Score: 44.10 E-value: 4.46e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 6 RISPQQKHLWLQqkdnYQAYCTQIAINI------TGNLNSDILKLALANLSDRYEIFHTAFHSLPGmnIPFQSISDAPty 79
Cdd:cd19537 3 ALSPIEREWWHK----YQLSTGTSSFNVsfacrlSGDVDRDRLASAWNTVLARHRILRSRYVPRDG--GLRRSYSSSP-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 80 nhislaeydwsrlsSQVQKakidtlfqdtsLRVFDFEQATNLHFilgKLATDQ----------------HILfislpaly 143
Cdd:cd19537 75 --------------PRVQR-----------VDTLDVWKEINRPF---DLEREDpirvfispdtllvvmsHII-------- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 144 ADKTTLNYLICEIGRAYtaclDGEEISEEVMQYADVSEWlnellESEDTETARNYWQQqdissvlNLRIPfEIKNDHQSS 223
Cdd:cd19537 119 CDLTTLQLLLREVSAAY----NGKLLPPVRREYLDSTAW-----SRPASPEDLDFWSE-------YLSGL-PLLNLPRRT 181
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 224 GEISFAPQSLCLAMNRDTVEKLEILQESYHTSTEAILLACWQVLLWRLSGQSEIVIGAAGDGREYDELKGVFGLLTKYLP 303
Cdd:cd19537 182 SSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLP 261
|
.
gi 2129675820 304 I 304
Cdd:cd19537 262 I 262
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
1070-1200 |
6.20e-04 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 42.88 E-value: 6.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1070 YPFFCLPGGGGNVLYLHELARDLG-SEQTFYGLQAPGlNGESDPLTSVEEMA----AYYIQAIQSVQPEGPYFLGGHSFG 1144
Cdd:pfam00561 1 PPVLLLHGLPGSSDLWRKLAPALArDGFRVIALDLRG-FGKSSRPKAQDDYRtddlAEDLEYILEALGLEKVNLVGHSMG 79
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 2129675820 1145 GIVA---YEIAQQLVKSgheVALVAILDaPAPVASDKPIYIDVDDATRLTETARLIERW 1200
Cdd:pfam00561 80 GLIAlayAAKYPDRVKA---LVLLGALD-PPHELDEADRFILALFPGFFDGFVADFAPN 134
|
|
| YpfH |
COG0400 |
Predicted esterase [General function prediction only]; |
1065-1228 |
6.62e-04 |
|
Predicted esterase [General function prediction only];
Pssm-ID: 440169 [Multi-domain] Cd Length: 200 Bit Score: 42.59 E-value: 6.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1065 TGNSQYPFFCLPGGGGNVLYLHELARDLGSEQT-FYGLQAP--------------GLNGESDPlTSVEEMAAYYIQAIQS 1129
Cdd:COG0400 1 GGPAAPLVVLLHGYGGDEEDLLPLAPELALPGAaVLAPRAPvpegpggrawfdlsFLEGREDE-EGLAAAAEALAAFIDE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2129675820 1130 VQ-----PEGPYFLGGHSFGGIVAYEIA---QQLVK-----SGHeVALVAILDAPAPVASDKPIYI---DVDDATRLTET 1193
Cdd:COG0400 80 LEarygiDPERIVLAGFSQGAAMALSLAlrrPELLAgvvalSGY-LPGEEALPAPEAALAGTPVFLahgTQDPVIPVERA 158
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2129675820 1194 ARLIERWAGKSLNISYEI------LQPLELDAQLEYLKEQL 1228
Cdd:COG0400 159 REAAEALEAAGADVTYREypggheISPEELADARAWLAERL 199
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
608-634 |
8.71e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 43.55 E-value: 8.71e-04
10 20
....*....|....*....|....*..
gi 2129675820 608 ENLAYIIYTSGSTGKPKGTMIPHRGLV 634
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLI 247
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
845-901 |
1.96e-03 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 42.44 E-value: 1.96e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2129675820 845 YKTGDLARYLPDGN--------IEY-LGRIDHQVKIRGFRIELEEIESLLAQHPLV--NAVTVIARED 901
Cdd:COG1541 297 YRTGDLTRLLPEPCpcgrthprIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVgpEYQIVVDREG 364
|
|
| |
