|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
11-2072 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1780.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 11 ALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPD 90
Cdd:PRK12467 516 QLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPE 595
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 91 TPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGI---IVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQ 167
Cdd:PRK12467 596 YPQDRLAYMLDDSGVRLLLTQSHLLAQLPVPAGLrslCLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVA 675
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 168 IEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTP 247
Cdd:PRK12467 676 ISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVP 755
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 248 SLFHTIVNTASFAKDanfESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDLyEPDAFAKRPtI 327
Cdd:PRK12467 756 SHLQALLQASRVALP---RPQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSD-EERDFGNVP-I 830
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 328 GRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSP-GSLMYKTGDVVRRLSDGTLAFIG 406
Cdd:PRK12467 831 GQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYRADGVIEYLG 910
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 407 RADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYTSDQDIEKA-------ELRYQLSLTLPSHMIP 479
Cdd:PRK12467 911 RMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVADGAehqatrdELKAQLRQVLPDYMVP 990
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 480 AFFVQVDAIPLTANGKTDRNALPKPNAAQSGgKALAAPETALEESLCRIWQKTLGIEAIGIDDNFFDLGGHSLKGMMLIA 559
Cdd:PRK12467 991 AHLLLLDSLPLTPNGKLDRKALPKPDASAVQ-ATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVIS 1069
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 560 NIQAELEKSVPLKALFEQPTVRQLAAYMEASAVsGGHQVLKPADKQDMYPLSSAQKRMYVLNQLDRQTISYNMPSVLLME 639
Cdd:PRK12467 1070 RVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQ-GAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLK 1148
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 640 GELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRI-------IEKAEVDLhvfeakEDEADQKIKEFI-----RPFDL 707
Cdd:PRK12467 1149 GPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIhpvgsltLEEPLLLA------ADKDEAQLKVYVeaearQPFDL 1222
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 708 NDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKGE------QLPEPTLHYKDFAVWQN---EAEQKE 778
Cdd:PRK12467 1223 EQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYsqgqslQLPALPIQYADYAVWQRqwmDAGERA 1302
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 779 RmkeHEAYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLLAETGTTLHMVLHAVFHVFLSKISGQ 858
Cdd:PRK12467 1303 R---QLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQ 1379
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 859 RDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSALEHQEYPFEDLVNQLDLPRDMSRNPL 938
Cdd:PRK12467 1380 DDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPL 1459
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 939 FNVMVTTENPDKE-QLTLQNLSISPYEAHQGTSKFDLTLGGFTDENGIGLQLEYATDLFAKETAEKWSEYVLRLLKAVAD 1017
Cdd:PRK12467 1460 FQVMFNHQRDDHQaQAQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVA 1539
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1018 NPNQPLSSLLLVTETEKQALLEAWKGKALPVPTDKTVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDC 1097
Cdd:PRK12467 1540 DPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIAL 1619
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1098 GISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKQEGISvpdsytGDVILLDGSRT 1177
Cdd:PRK12467 1620 GVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQ------ARLPLPDGLRS 1693
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1178 ILSLP----LDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDAS 1253
Cdd:PRK12467 1694 LVLDQeddwLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVS 1773
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1254 IWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVT-ITFLPTQLaEQFMEL-----ENTSLRVLLTGGDKLKRAVKK 1327
Cdd:PRK12467 1774 VWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTtLHFVPSML-QQLLQMdeqveHPLSLRRVVCGGEALEVEALR 1852
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1328 PY-------TLVNNYGPTENTVVAT--SAEIHPEEGSLS--IGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGY 1396
Cdd:PRK12467 1853 PWlerlpdtGLFNLYGPTETAVDVThwTCRRKDLEGRDSvpIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGY 1932
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1397 LNREDETAKRFVADPF-VPGERMYRTGDLVKWVNGG-IEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKD 1474
Cdd:PRK12467 1933 LNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGvIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQDG 2012
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1475 KGGnTAIAAYVTPETADI-----------EALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPDIEAGSGEY 1543
Cdd:PRK12467 2013 ANG-KQLVAYVVPTDPGLvdddeaqvalrAILKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQAY 2091
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1544 KAPTTDMEELLAGIWQDVLGMSEVGVTDNFFSLGGDSIKGIQMASRLNQHGWKLEMKDLFQHPTIEELTQYVERAEGK-Q 1622
Cdd:PRK12467 2092 VAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTvS 2171
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1623 ADQGPVEGEVILTPIQRWFFEKNFTNKHHWNQSVMLHAKKGFDPERVEKTLQALIEHHDALRMVYREENGDIVQVYKPIG 1702
Cdd:PRK12467 2172 IDQGPVTGDLPLLPIQQMFFADDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGWSAMHRAPE 2251
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1703 ESKVSFeivdLYG---SDEEMLRSqiklLANKLQSSLDLRNGPLLKAEQYR-TEAGDHLLIAVHHLVVDGVSWRILLEDF 1778
Cdd:PRK12467 2252 QERRPL----LWQvvvADKEELEA----LCEQAQRSLDLEEGPLLRAVLATlPDGSQRLLLVIHHLVVDGVSWRILLEDL 2323
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1779 ASGYMQAEKEESLVFPQKTNSFKDWAEELAAFSQSAHLLQQAEYWSQIAAEQVSPLPKDCETEQRIVKDTSSVLCELTAE 1858
Cdd:PRK12467 2324 QTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGASTELPCDHPQGGLQRRHAASVTTHLDSE 2403
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1859 DTKHLLTDVHQPYGTEINDILLSALGLTMKEWTKGAKIGINLEGHGREDIIPNVNISRTVGWFTAQYPVVLdISDADASA 1938
Cdd:PRK12467 2404 WTRRLLQEAPAAYRTQVNDLLLTALARVIARWTGQASTLIQLEGHGREDLFDEIDLTRTVGWFTSLYPVKL-SPTASLAT 2482
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1939 VIKTVKENLRRIPDKGVGYGILRYFTETAETKGFT----PEISFNYLGQFDSEVKTD---FFEPSAFDMGRQVSGESEAL 2011
Cdd:PRK12467 2483 SIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTLQalpvPRITFNYLGQFDGSFDAEkqaLFVPSGEFSGAEQSEEAPLG 2562
|
2090 2100 2110 2120 2130 2140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 2012 YALSFSGMIRNGRFVLSCSYNEKEFERATVEEQMERFKENLLMLIRHCTEKEDKEFTPSDF 2072
Cdd:PRK12467 2563 NWLSINGQVYGGELNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVTPSDF 2623
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
10-2078 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1615.02 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 10 AALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDP 89
Cdd:PRK12316 2006 HQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDP 2085
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 90 DTPEERIRYSLEDSGAKFaVVNERNMTAIGQYEGIIVSLD---DGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGV 166
Cdd:PRK12316 2086 NYPAERLAYMLEDSGAAL-LLTQRHLLERLPLPAGVARLPldrDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGV 2164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 167 QIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELhIVQKETYTAPDEIAHYIKEHGITYIKLT 246
Cdd:PRK12316 2165 AVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTILDFP 2243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 247 PSLFHTIVNTAsfAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDLYEPDAFAKRPt 326
Cdd:PRK12316 2244 PVYLQQLAEHA--ERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVP- 2320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 327 IGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS-PGSLMYKTGDVVRRLSDGTLAFI 405
Cdd:PRK12316 2321 IGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSaSGERLYRTGDLARYRADGVVEYL 2400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 406 GRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYTSD--QDIEKAELRYQLSLTLPSHMIPAFFV 483
Cdd:PRK12316 2401 GRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDdaAEDLLAELRAWLAARLPAYMVPAHWV 2480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 484 QVDAIPLTANGKTDRNALPKPNAAQSGgKALAAPETALEESLCRIWQKTLGIEAIGIDDNFFDLGGHSLKGMMLIANIQA 563
Cdd:PRK12316 2481 VLERLPLNPNGKLDRKALPKPDVSQLR-QAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQ 2559
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 564 ELEKSVPLKALFEQPTVRQLAAYMEASAVSGGhQVLKPADKQDMYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELD 643
Cdd:PRK12316 2560 DLGLEVPLRILFERPTLAAFAASLESGQTSRA-PVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLD 2638
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 644 ISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKAEVDLHVFEAkEDEADQKIK-----EFIRPFDLNDAPLIRAALL 718
Cdd:PRK12316 2639 QAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDC-AGVADAAIRqrvaeEIQRPFDLARGPLLRVRLL 2717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 719 RIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKGE------QLPEPTLHYKDFAVWQNEAEQKERMKEHEAYWMSVLS 792
Cdd:PRK12316 2718 ALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGArrgeqpTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLG 2797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 793 GELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLLAETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTN 872
Cdd:PRK12316 2798 GEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNR 2877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 873 ADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSALEHQEYPFEDLVNQLDLPRDMSRNPLFNVMVTTENPDKEQ 952
Cdd:PRK12316 2878 AETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAA 2957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 953 LTLQNLSISPYEAHQGTSKFDLTLGGFTDENGIGLQLEYATDLFAKETAEKWSEYVLRLLKAVADNPNQPLSSLLLVTET 1032
Cdd:PRK12316 2958 AQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAE 3037
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1033 EKQALLEAWKGKALPVPTDKTVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPS 1112
Cdd:PRK12316 3038 ERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERS 3117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1113 LEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKQEGISVPDSYTGDVILLDgsrtilslPLDEN-DEGNP 1191
Cdd:PRK12316 3118 LEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLD--------RGDENyAEANP 3189
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1192 ETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVID 1271
Cdd:PRK12316 3190 AIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAG 3269
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1272 EAIRLDIVRLNDYFETNGV-TITFLPTQLAEQFMEL---ENTSLRVLLTGGDKLK----RAVKKPYTLVNNYGPTENTVV 1343
Cdd:PRK12316 3270 PEDWRDPALLVELINSEGVdVLHAYPSMLQAFLEEEdahRCTSLKRIVCGGEALPadlqQQVFAGLPLYNLYGPTEATIT 3349
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1344 ATSAEIHPE-EGSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTG 1422
Cdd:PRK12316 3350 VTHWQCVEEgKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTG 3429
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1423 DLVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKggntAIAAYVTP---ETADIEALKST 1498
Cdd:PRK12316 3430 DLARYrADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGR----QLVAYVVPedeAGDLREALKAH 3505
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1499 LKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPDIEAGSGEYKAPTTDMEELLAGIWQDVLGMSEVGVTDNFFSLGG 1578
Cdd:PRK12316 3506 LKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGG 3585
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1579 DSIKGIQMASRLNQHGWKLEMKDLFQHPTIEELTQYVERAEGKQADQGPVEGEVILTPIQRWFFEKNFTNKHHWNQSVML 1658
Cdd:PRK12316 3586 DSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGGVAVDQGPVSGETLLLPIQQQFFEEPVPERHHWNQSLLL 3665
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1659 HAKKGFDPERVEKTLQALIEHHDALRMVYREENGDIVQVYKPIGESKVSFEIVDLygSDEEMLRSqiklLANKLQSSLDL 1738
Cdd:PRK12316 3666 KPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRAEL--DDAEELER----LGEEAQRSLDL 3739
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1739 RNGPLLKAEQYRTEAGDH-LLIAVHHLVVDGVSWRILLEDFASGYMQAEKEESLVFPQKTNSFKDWAEELAAFSQSAHLL 1817
Cdd:PRK12316 3740 ADGPLLRALLATLADGSQrLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALK 3819
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1818 QQAEYWSQIAAEQVSPLPKDCETEQRIVKDTSSVLCELTAEDTKHLLTDVHQPYGTEINDILLSALGLTMKEWTKGAKIG 1897
Cdd:PRK12316 3820 AELAYWQEQLQGVSSELPCDHPQGALQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALARVVCRWTGEASAL 3899
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1898 INLEGHGREDIIPNVNISRTVGWFTAQYPVVLDISdADASAVIKTVKENLRRIPDKGVGYGILRYF--TETAETKGFTP- 1974
Cdd:PRK12316 3900 VQLEGHGREDLFADIDLSRTVGWFTSLFPVRLSPV-EDLGASIKAIKEQLRAIPNKGIGFGLLRYLgdEESRRTLAGLPv 3978
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1975 -EISFNYLGQFDSEVKTD--FFEPSAFDMGRQVSGESEALYALSFSGMIRNGRFVLSCSYNEKEFERATVEEQMERFKEN 2051
Cdd:PRK12316 3979 pRITFNYLGQFDGSFDEEmaLFVPAGESAGAEQSPDAPLDNWLSLNGRVYGGELSLDWTFSREMFEEATIQRLADDYAAE 4058
|
2090 2100
....*....|....*....|....*..
gi 2214269206 2052 LLMLIRHCTEKEDKEFTPSDFSAEDLE 2078
Cdd:PRK12316 4059 LTALVEHCCDAERHGVTPSDFPLAGLD 4085
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
6-2077 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1486.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 6 EATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFL 85
Cdd:PRK05691 1130 QAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYV 1209
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 86 PIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGII-VSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPK 164
Cdd:PRK05691 1210 PLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEGVSaIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPK 1289
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 165 GVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIK 244
Cdd:PRK05691 1290 GVGNTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLH 1369
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 245 LTPSLFHTIVNTASFAkdaNFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDLYEpdafAKR 324
Cdd:PRK05691 1370 FVPPLLQLFIDEPLAA---ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAED----GER 1442
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 325 PTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS-PGSLMYKTGDVVRRLSDGTLA 403
Cdd:PRK05691 1443 SPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWNADGALE 1522
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 404 FIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYTSD--QDIEKAELRYQLSLTLPSHMIPAF 481
Cdd:PRK05691 1523 YLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEagQEAEAERLKAALAAELPEYMVPAQ 1602
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 482 FVQVDAIPLTANGKTDRNALPKPNAAQsggKALAAPETALEESLCRIWQKTLGIEAIGIDDNFFDLGGHSLKGMMLIANI 561
Cdd:PRK05691 1603 LIRLDQMPLGPSGKLDRRALPEPVWQQ---REHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRT 1679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 562 QAELEKSVPLKALFEQPTVRQLAAYMEASAVSG---GHQVLKPADKQDMYPLSSAQKRMYVLNQLDRQTISYNMPSVLLM 638
Cdd:PRK05691 1680 RQACDVELPLRALFEASELGAFAEQVARIQAAGernSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARL 1759
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 639 EGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKAEVDLHVFEAKEDEAD---QKIKEFI-----RPFDLNDA 710
Cdd:PRK05691 1760 SGVLDVDRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDSGLRMDWQDFSALPADarqQRLQQLAdseahQPFDLERG 1839
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 711 PLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKG--EQLPEP----TLHYKDFAVWQNE-AEQKERMKEH 783
Cdd:PRK05691 1840 PLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAflDDRESPleplPVQYLDYSVWQRQwLESGERQRQL 1919
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 784 eAYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLLAETGTTLHMVLHAVFHVFLSKISGQRDIVI 863
Cdd:PRK05691 1920 -DYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRI 1998
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 864 GSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSALEHQEYPFEDLVNQLDLPRDMSRNPLFNVMV 943
Cdd:PRK05691 1999 GAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMC 2078
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 944 TTENPDKEQL-TLQNLSISPYEAHQGTSKFDLTLGgFTDENG-IGLQLEYATDLFAKETAEKWSEYVLRLLKAVADNPNQ 1021
Cdd:PRK05691 2079 NVQRWEFQQSrQLAGMTVEYLVNDARATKFDLNLE-VTDLDGrLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQ 2157
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1022 PLSSLLLVTETEKQALLEAWKGKALPVPTDKTVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISP 1101
Cdd:PRK05691 2158 RLAELPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGP 2237
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1102 DDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKQEGI-----SVPDSyTGDVILLDGSR 1176
Cdd:PRK05691 2238 QVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALfealgELPAG-VARWCLEDDAA 2316
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1177 TILSLPLDEndegnPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWE 1256
Cdd:PRK05691 2317 ALAAYSDAP-----LPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASER 2391
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1257 MFPTWTIGAELhVIDEAIRLDIVRLNDYFETNGVTIT-FLP---TQLAeQFMELENTSL--RVLLTGGDKLK-------R 1323
Cdd:PRK05691 2392 LLVPLLCGARV-VLRAQGQWGAEEICQLIREQQVSILgFTPsygSQLA-QWLAGQGEQLpvRMCITGGEALTgehlqriR 2469
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1324 AVKKPYTLVNNYGPTEnTVVATSAEIHPE-----EGSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLN 1398
Cdd:PRK05691 2470 QAFAPQLFFNAYGPTE-TVVMPLACLAPEqleegAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHD 2548
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1399 REDETAKRFVADPFVP-GERMYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKG 1476
Cdd:PRK05691 2549 RPGLTAERFVADPFAAdGGRLYRTGDLVRLrADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPS 2628
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1477 GNTaIAAYVTPETADI---------EALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPDIEAGSGEYKAPT 1547
Cdd:PRK05691 2629 GKQ-LAGYLVSAVAGQddeaqaalrEALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPR 2707
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1548 TDMEELLAGIWQDVLGMSEVGVTDNFFSLGGDSIKGIQMASRLNQHGWKLEMKDLFQHPTIEELTQYVERAEGKQADQGP 1627
Cdd:PRK05691 2708 SELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEQGP 2787
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1628 VEGEVILTPIQRWFFEKNFTNKHHWNQSVMLHAKKGFDPERVEKTLQALIEHHDALRMVYREENGDIVQVYKPIGESKV- 1706
Cdd:PRK05691 2788 LQGASGLTPIQHWFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADGRWQAEYRAVTAQELl 2867
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1707 -SFEIVDLygsdeemlrSQIKLLANKLQSSLDLRNGPLLKAEQYRTEAGDH-LLIAVHHLVVDGVSWRILLEDFASGYMQ 1784
Cdd:PRK05691 2868 wQVTVADF---------AECAALFADAQRSLDLQQGPLLRALLVDGPQGQQrLLLAIHHLVVDGVSWRVLLEDLQALYRQ 2938
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1785 AEKEESLVFPQKTNSFKDWAEELAAFSQSAHLLQQAEYWSQIAAEQVSPLPKDCETEQRIVKDTSSVLCELTAEDTKHLL 1864
Cdd:PRK05691 2939 LSAGAEPALPAKTSAFRDWAARLQAYAGSESLREELGWWQAQLGGPRAELPCDRPQGGNLNRHAQTVSVRLDAERTRQLL 3018
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1865 TDVHQPYGTEINDILLSALGLTMKEWTKGAKIGINLEGHGREDIIPNVNISRTVGWFTAQYPVVL---DISDADASAVIK 1941
Cdd:PRK05691 3019 QQAPAAYRTQVNDLLLTALARVLCRWSGQPSVLVQLEGHGREALFDDIDLTRSVGWFTSAYPLRLtpaPGDDAARGESIK 3098
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1942 TVKENLRRIPDKGVGYGILRYFTETAETKGF----TPEISFNYLGQFDSEVKTD-FFEPSAFDMGRQVSGESEALYALSF 2016
Cdd:PRK05691 3099 AIKEQLRAVPHKGLGYGVLRYLADAAVREAMaalpQAPITFNYLGQFDQSFASDaLFRPLDEPAGPAHDPDAPLPNELSV 3178
|
2090 2100 2110 2120 2130 2140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 2017 SGMIRNGRFVLSCSYNEKEFERATVEEQMERFKENLLMLIRHCTEKEDKEFTPSDFSAEDL 2077
Cdd:PRK05691 3179 DGQVYGGELVLRWTYSAERYDEQTIAELAEAYLAELQALIAHCLADGAGGLTPSDFPLAQL 3239
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
601-2072 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1232.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 601 PADKQdmyPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGE-----PVQR 675
Cdd:PRK12316 46 SAERD---RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDslaqvPLDR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 676 IIEKAEVDL-HVFEAKEDEA--DQKIKEFIRPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLY 752
Cdd:PRK12316 123 PLEVEFEDCsGLPEAEQEARlrDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 753 KGE------QLPEPTLHYKDFAVWQN---EAEQKERMKEheaYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGS 823
Cdd:PRK12316 203 SAYatgaepGLPALPIQYADYALWQRswlEAGEQERQLE---YWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDP 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 824 ETAKAVEKLLAETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLE 903
Cdd:PRK12316 280 ALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLA 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 904 LAKQTNLSALEHQEYPFEDLVNQLDLPRDMSRNPLFNVMVTTENPDKEQ---LTLQNLSISPYEAHQGTSKFDLTLGGFT 980
Cdd:PRK12316 360 GVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLVADIealDTVAGLEFGQLEWKSRTTQFDLTLDTYE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 981 DENGIGLQLEYATDLFAKETAEKWSEYVLRLLKAVADNPNQPLSSLLLVTETEKQALLEAWKGKALPVPTDKTVHQLFEE 1060
Cdd:PRK12316 440 KGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEE 519
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1061 TVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQR 1140
Cdd:PRK12316 520 QVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAER 599
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1141 IEYILQDSGAKLLLKQE--GISVPDSYTGDVILLDGSrtilSLPLDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMV 1218
Cdd:PRK12316 600 LAYMLEDSGVQLLLSQShlGRKLPLAAGVQVLDLDRP----AAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGN 675
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1219 EHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGV-TITFLPT 1297
Cdd:PRK12316 676 RHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVdTLHFVPS 755
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1298 QLaEQFMELEN----TSLRVLLTGGDKLKRAV------KKPYT-LVNNYGPTENTVVAT-SAEIHPEEGSLSIGRAIANT 1365
Cdd:PRK12316 756 ML-QAFLQDEDvascTSLRRIVCSGEALPADAqeqvfaKLPQAgLYNLYGPTEAAIDVThWTCVEEGGDSVPIGRPIANL 834
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1366 RVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKW-VNGGIEYIGRIDQQVKV 1444
Cdd:PRK12316 835 ACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYrADGVIEYAGRIDHQVKL 914
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1445 RGYRIELSEIEVQLAQLSEVQDAAVTAVKDKggntAIAAYVTPETAD---IEALKSTLKETLPDYMIPAFWVTLNELPVT 1521
Cdd:PRK12316 915 RGLRIELGEIEARLLEHPWVREAAVLAVDGK----QLVGYVVLESEGgdwREALKAHLAASLPEYMVPAQWLALERLPLT 990
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1522 ANGKVDRKALPEPDIEAGSGEYKAPTTDMEELLAGIWQDVLGMSEVGVTDNFFSLGGDSIKGIQMASRLNQHGWKLEMKD 1601
Cdd:PRK12316 991 PNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRD 1070
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1602 LFQHPTIEELTQYVERAEGKQADQGPVEGEVILTPIQRWFFEKNFTNKHHWNQSVMLHAKKGFDPERVEKTLQALIEHHD 1681
Cdd:PRK12316 1071 LFQHQTIRSLALVAKAGQATAADQGPASGEVALAPVQRWFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHD 1150
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1682 ALRMVYREENGDIVQVYKPIGESKVsfeivdLYGSDeemLRSQIKLLA--NKLQSSLDLRNGPLLKAEQYR-TEAGDHLL 1758
Cdd:PRK12316 1151 ALRLRFREEDGGWQQAYAAPQAGEV------LWQRQ---AASEEELLAlcEEAQRSLDLEQGPLLRALLVDmADGSQRLL 1221
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1759 IAVHHLVVDGVSWRILLEDFASGYMQAEkeesLVFPQKTNSFKDWAEELAAFSQSahLLQQAEYWSQIAAEQVSPLPkdC 1838
Cdd:PRK12316 1222 LVIHHLVVDGVSWRILLEDLQRAYADLD----ADLPARTSSYQAWARRLHEHAGA--RAEELDYWQAQLEDAPHELP--C 1293
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1839 ET-----EQRIVKdtsSVLCELTAEDTKHLLTDVHQPYGTEINDILLSALGLTMKEWTKGAKIGINLEGHGREDIIPNVN 1913
Cdd:PRK12316 1294 ENpdgalENRHER---KLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDID 1370
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1914 ISRTVGWFTAQYPVVLDiSDADASAVIKTVKENLRRIPDKGVGYGILRYF--TETAETKGFTPE--ISFNYLGQFDSEV- 1988
Cdd:PRK12316 1371 LSRTVGWFTSLFPVRLT-PAADLGESIKAIKEQLRAVPDKGIGYGLLRYLagEEAAARLAALPQprITFNYLGQFDRQFd 1449
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1989 KTDFFEPSAFDMGrQVSGESEALYA-LSFSGMIRNGRFVLSCSYNEKEFERATVEEQMERFKENLLMLIRHCTEKEDKEF 2067
Cdd:PRK12316 1450 EAALFVPATESAG-AAQDPCAPLANwLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIEHCCDERNRGV 1528
|
....*
gi 2214269206 2068 TPSDF 2072
Cdd:PRK12316 1529 TPSDF 1533
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
601-1835 |
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: 1047.91 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 601 PADKQDMYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKA 680
Cdd:COG1020 11 PAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 681 EV--------DLHVFEAKEDEADQKIKEFIRPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLY 752
Cdd:COG1020 91 AAplpvvvllVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLY 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 753 ------KGEQLPEPTLHYKDFAVWQNEAEQKERMKEHEAYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETA 826
Cdd:COG1020 171 laayagAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 827 KAVEKLLAETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAK 906
Cdd:COG1020 251 AALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 907 QTNLSALEHQEYPFEDLVNQLDLPRDMSRNPLFNVMVTTENPDKEQLTLQNLSISPYEAHQGTSKFDLTLGGFTDENGIG 986
Cdd:COG1020 331 ETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDLTLTVVETGDGLR 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 987 LQLEYATDLFAKETAEKWSEYVLRLLKAVADNPNQPLSSLLLVTETEKQALLEAWKGKALPVPTDKTVHQLFEETVQRHK 1066
Cdd:COG1020 411 LTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAARTP 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:COG1020 491 DAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLE 570
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLKQEGI--SVPDsYTGDVILLDgsrtilSLPLDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALV 1224
Cdd:COG1020 571 DAGARLVLTQSALaaRLPE-LGVPVLALD------ALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALV 643
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1225 NLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTITFLPTQLAEQFM 1304
Cdd:COG1020 644 NLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALL 723
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1305 ELEN---TSLRVLLTGGDKLK-------RAVKKPYTLVNNYGPTENTVVATSAEIHPEE---GSLSIGRAIANTRVYILG 1371
Cdd:COG1020 724 DAAPealPSLRLVLVGGEALPpelvrrwRARLPGARLVNLYGPTETTVDSTYYEVTPPDadgGSVPIGRPIANTRVYVLD 803
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1372 EGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPF-VPGERMYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRI 1449
Cdd:COG1020 804 AHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWlPDGNLEFLGRADDQVKIRGFRI 883
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1450 ELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE---TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKV 1526
Cdd:COG1020 884 ELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEagaAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKL 963
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1527 DRKALPEPDiEAGSGEYKAPTTDMEELLAGIWQDVLGMSEVGVTDNFFSLGGDSIKGIQMASRLNQHGWKLEMKDLFQH- 1605
Cdd:COG1020 964 DRLALPAPA-AAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLa 1042
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1606 -PTIEELTQYVERAEGKQADQGPVEGEVILTPIQRWFFEKNFTNKHHWNQSVMLHAKKGFDPERVEKTLQALIEHHDALR 1684
Cdd:COG1020 1043 aAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALL 1122
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1685 MVYREENGDIVQVYKPIGESKVSFEIVDLYGSDEEMLRSQIKLLANKLQSSLDLRNGPLLKAEQYRTEAGDHLLIAVHHL 1764
Cdd:COG1020 1123 AALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLL 1202
|
1210 1220 1230 1240 1250 1260 1270
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 1765 VVDGVSWRILLEDFASGYMQAEKEESLVFPQKTNSfkDWAEELAAFSQSAHLLQQAEYWSQIAAEQVSPLP 1835
Cdd:COG1020 1203 LLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALL--LALLALAALLALAALAALAAALLALALALLALAL 1271
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
609-1837 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 957.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 609 PLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKAEVDLHVFE 688
Cdd:PRK12467 51 PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDD 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 689 AKE---DEADQKIKEFI-----RPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKGE----- 755
Cdd:PRK12467 131 LANeqgRARESQIEAYIneevaRPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgre 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 756 -QLPEPTLHYKDFAVWQN---EAEQKERmkeHEAYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEK 831
Cdd:PRK12467 211 pSLPALPIQYADYAIWQRswlEAGERER---QLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKA 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 832 LLAETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLS 911
Cdd:PRK12467 288 LAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 912 ALEHQEYPFEDLVNQLDLPRDMSRNPLFNVMVTTEN-----PDKEQLTLQNLSISPYEAHQGTSKFDLTLGGFTDENGIG 986
Cdd:PRK12467 368 AQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNtatggRDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLW 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 987 LQLEYATDLFAKETAEKWSEYVLRLLKAVADNPNQPLSSLLLVTETEKQALLEAWKGKALPVPTDkTVHQLFEETVQRHK 1066
Cdd:PRK12467 448 AAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPD-CVHQLIEAQARQHP 526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:PRK12467 527 ERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLD 606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLKQE----GISVPDSYTGDVILLDGSrtilslPLDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHA 1222
Cdd:PRK12467 607 DSGVRLLLTQShllaQLPVPAGLRSLCLDEPAD------LLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGA 680
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1223 LVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTITFLPTQLAEQ 1302
Cdd:PRK12467 681 LANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQA 760
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1303 FMELEN----TSLRVLLTGGDKLK-------RAVKKPYTLVNNYGPTENTVVATSAEIHPEE---GSLSIGRAIANTRVY 1368
Cdd:PRK12467 761 LLQASRvalpRPQRALVCGGEALQvdllarvRALGPGARLINHYGPTETTVGVSTYELSDEErdfGNVPIGQPLANLGLY 840
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1369 ILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVP-GERMYRTGDLVKW-VNGGIEYIGRIDQQVKVRG 1446
Cdd:PRK12467 841 ILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAdGGRLYRTGDLARYrADGVIEYLGRMDHQVKIRG 920
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1447 YRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTaIAAYVTPET--------ADIEALKSTLKETLPDYMIPAFWVTLNEL 1518
Cdd:PRK12467 921 FRIELGEIEARLLAQPGVREAVVLAQPGDAGLQ-LVAYLVPAAvadgaehqATRDELKAQLRQVLPDYMVPAHLLLLDSL 999
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1519 PVTANGKVDRKALPEPDIEAGSGEYKAPTTDMEELLAGIWQDVLGMSEVGVTDNFFSLGGDSIKGIQMASRLNQH-GWKL 1597
Cdd:PRK12467 1000 PLTPNGKLDRKALPKPDASAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRlGIQV 1079
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1598 EMKDLFQHPTIEELTQYVerAEGKQADQGPVEGEVILTPIQ-------RWFFEKNFTNKHHWNQSVMLHAKKGFDPERVE 1670
Cdd:PRK12467 1080 PLRTLFEHQTLAGFAQAV--AAQQQGAQPALPDVDRDQPLPlsyaqerQWFLWQLEPGSAAYHIPQALRLKGPLDIEALE 1157
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1671 KTLQALIEHHDALRMVYREENGDIVQVYKPIGESKVSFEIVDLYGSDEEMLRSQIKLLANKLqssLDLRNGPLLKAEQYR 1750
Cdd:PRK12467 1158 RSFDALVARHESLRTTFVQEDGRTRQVIHPVGSLTLEEPLLLAADKDEAQLKVYVEAEARQP---FDLEQGPLLRVGLLR 1234
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1751 TEAGDHLLIAV-HHLVVDGVSWRILLEDFASGYMQAEKEESLVFPQKTNSFKDWAEELAAFSQSAHLLQQAEYW-SQIAA 1828
Cdd:PRK12467 1235 LAADEHVLVLTlHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERARQLAYWkAQLGG 1314
|
1290
....*....|
gi 2214269206 1829 EQ-VSPLPKD 1837
Cdd:PRK12467 1315 EQpVLELPTD 1324
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
8-1768 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 885.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 8 TFAALFEKQAQQTPDHSAVK------AGGNLLTYRELDEQANQLAHHLRAQgAGNEDIVAIVMDRSAEVMVSILGVMKAG 81
Cdd:PRK05691 10 TLVQALQRRAAQTPDRLALRfladdpGEGVVLSYRDLDLRARTIAAALQAR-ASFGDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 82 AAFLPIDPdtPE-------ERI---------RYSLEDSGAKFAVVNERNMTAIGQYEGIIV-SLDDG---KWRnESKERP 141
Cdd:PRK05691 89 VIAVPAYP--PEsarrhhqERLlsiiadaepRLLLTVADLRDSLLQMEELAAANAPELLCVdTLDPAlaeAWQ-EPALQP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 142 SSIsgsrnlAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAF--DLGytsmfpvLLGG----- 214
Cdd:PRK05691 166 DDI------AFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLNPDDVIVSWLPLyhDMG-------LIGGllqpi 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 215 --GELHIVQKETY--TAPDEIAHYIKEHGityikltpslfHTIVNTASFA--------KDANFESL-----RLIVLGGEK 277
Cdd:PRK05691 233 fsGVPCVLMSPAYflERPLRWLEAISEYG-----------GTISGGPDFAyrlcservSESALERLdlsrwRVAYSGSEP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 278 IIPTDVIAFRKMYG-----HTEFINHYGPTEATI---------GAIAGRVDlyePDAFAK---RPTIGRPIANAGALVLN 340
Cdd:PRK05691 302 IRQDSLERFAEKFAacgfdPDSFFASYGLAEATLfvsggrrgqGIPALELD---AEALARnraEPGTGSVLMSCGRSQPG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 341 EALKLVPP--------GASGQLYITGQGLARGYLNRPQLTAERFVENPyspGSLMYKTGDVvRRLSDGTLAFIGRADDQV 412
Cdd:PRK05691 379 HAVLIVDPqslevlgdNRVGEIWASGPSIAHGYWRNPEASAKTFVEHD---GRTWLRTGDL-GFLRDGELFVTGRLKDML 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 413 KIRGYRIEPKEIETVMlslsgiqEAVVLAVSEGglqELCAYYTSDQDIE----KAELRYQLSLTLPS------------- 475
Cdd:PRK05691 455 IVRGHNLYPQDIEKTV-------EREVEVVRKG---RVAAFAVNHQGEEgigiAAEISRSVQKILPPqaliksirqavae 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 476 --HMIPAFFVQVD--AIPLTANGKTDRNA---------------LPKPNAAQSGgkALAAPETALEESLCRIWQKTLGIE 536
Cdd:PRK05691 525 acQEAPSVVLLLNpgALPKTSSGKLQRSAcrlrladgsldsyalFPALQAVEAA--QTAASGDELQARIAAIWCEQLKVE 602
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 537 AIGIDDNFFDLGGHSLKGMMLIANIQAELEKSVPLKALFEQPTVRQLAAYMEASAVSGGHQV--LKPADKQDMYPLSSAQ 614
Cdd:PRK05691 603 QVAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAQaaIARLPRGQALPQSLAQ 682
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 615 KRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKAEVDLHVF------E 688
Cdd:PRK05691 683 NRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIdlsdlpE 762
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 689 AKEDEADQKIKE--FIRPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLY------KGEQLPEP 760
Cdd:PRK05691 763 AEREARAAQIREeeARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYaaacqgQTAELAPL 842
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 761 TLHYKDFAVWQNEAEQKERMKEHEAYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLLAETGTTL 840
Cdd:PRK05691 843 PLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATL 922
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 841 HMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSALEHQEYPF 920
Cdd:PRK05691 923 FMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPF 1002
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 921 EDLVNQLDLPRDMSrnpLFNVMVTTENPDKEQL-TLQNLSISPYEAHQGTSKFDLTLGGFTDENG-IGLQLEYATDLFAK 998
Cdd:PRK05691 1003 EQLVEALPQAREQG---LFQVMFNHQQRDLSALrRLPGLLAEELPWHSREAKFDLQLHSEEDRNGrLTLSFDYAAELFDA 1079
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 999 ETAEKWSEYVLRLLKAVADNPNQPLSSLLLVTETEKQALLeAWkGKALPVPTDKTVHQLFEETVQRHKDRPAVTYNGQSW 1078
Cdd:PRK05691 1080 ATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLA-QW-GQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSL 1157
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1079 TYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKQEG 1158
Cdd:PRK05691 1158 DYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSH 1237
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1159 I--SVPDSYTGDVILLDgsrtilSLPLDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSM 1236
Cdd:PRK05691 1238 LleRLPQAEGVSAIALD------SLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYAL 1311
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1237 TAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVT-ITFLPTqLAEQFME----LENTSL 1311
Cdd:PRK05691 1312 DDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTtLHFVPP-LLQLFIDeplaAACTSL 1390
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1312 RVLLTGGDKLKRAVKK-------PYTLVNNYGPTENTVVATSAEIHPEEGSLS-IGRAIANTRVYIL-GEGNQVqPEGVA 1382
Cdd:PRK05691 1391 RRLFSGGEALPAELRNrvlqrlpQVQLHNRYGPTETAINVTHWQCQAEDGERSpIGRPLGNVLCRVLdAELNLL-PPGVA 1469
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1383 GELCVAGRGLARGYLNREDETAKRFVADPFV-PGERMYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQ 1460
Cdd:PRK05691 1470 GELCIGGAGLARGYLGRPALTAERFVPDPLGeDGARLYRTGDRARWnADGALEYLGRLDQQVKLRGFRVEPEEIQARLLA 1549
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1461 LSEVQDAAVTAVKDKGGNTAIAAYVTPETADIEA--LKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPDIEA 1538
Cdd:PRK05691 1550 QPGVAQAAVLVREGAAGAQLVGYYTGEAGQEAEAerLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQ 1629
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1539 gsGEYKAPTTDMEELLAGIWQDVLGMSEVGVTDNFFSLGGDSIKGIQMASRLNQH-GWKLEMKDLFQHPTIEELTQYVER 1617
Cdd:PRK05691 1630 --REHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQAcDVELPLRALFEASELGAFAEQVAR 1707
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1618 --AEGKQADQGPVEGEVILTPI------QR-WFFEKNFTNKHHWNQSVMLHAKKGFDPERVEKTLQALIEHHDALRMVYR 1688
Cdd:PRK05691 1708 iqAAGERNSQGAIARVDRSQPVplsysqQRmWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTFP 1787
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1689 EENGdiVQVYKPIGESKVSFEIVDLYGSDEEMLRSQIKLLAN-KLQSSLDLRNGPLLKAEQYRTEAGDH-LLIAVHHLVV 1766
Cdd:PRK05691 1788 SVDG--VPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADsEAHQPFDLERGPLLRACLVKAAEREHyFVLTLHHIVT 1865
|
..
gi 2214269206 1767 DG 1768
Cdd:PRK05691 1866 EG 1867
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1055-1532 |
0e+00 |
|
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: 811.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1055 HQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDP 1134
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1135 DYPDQRIEYILQDSGAKLLLKQegisvpdsytgdvilldgsrtilslpldendegnpetavtAENLAYMIYTSGTTGQPK 1214
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTN----------------------------------------PDDLAYVIYTSGSTGLPK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1215 GVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTITF 1294
Cdd:cd17645 121 GVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1295 LPTQLAEQFMELENTSLRVLLTGGDKLKRAVKKPYTLVNNYGPTENTVVATSAEIHPEEGSLSIGRAIANTRVYILGEGN 1374
Cdd:cd17645 201 LPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERKGYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEAL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1375 QVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKWVN-GGIEYIGRIDQQVKVRGYRIELSE 1453
Cdd:cd17645 281 QLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPdGNIEFLGRLDQQVKIRGYRIEPGE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1454 IEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPET-ADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALP 1532
Cdd:cd17645 361 IEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEeIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
599-2084 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 768.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 599 LKPADKQDMYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGeLDISRLRDSLNQLVNRHESLRTSFMEANG--EPVQRI 676
Cdd:PRK12316 1548 LPAGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGleQPLQVI 1626
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 677 IEKAEVDLHVFE--AKEDEAD----QKIKEFIRPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELAL 750
Cdd:PRK12316 1627 HKQVELPFAELDwrGREDLGQaldaLAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQ 1706
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 751 LYKGEQLPEPTLHYKDFAVWQneaeQKERMKEHEAYWMSvlsgELPELDLPLDYAR----PPVQSFKGDTIRFrTGSETA 826
Cdd:PRK12316 1707 RYAGQPVAAPGGRYRDYIAWL----QRQDAAASEAFWKE----QLAALEEPTRLAQaartEDGQVGYGDHQQL-LDPAQT 1777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 827 KAVEKLLAETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTN--ADVQDMPGMFVNTLALRMEAKEQQTFAELLEL 904
Cdd:PRK12316 1778 RALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAelPGIEQQIGLFINTLPVIAAPRPDQSVADWLQE 1857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 905 AKQTNLSALEHQEYPFEDLVNQLDLPRDmsrnPLFNVMVTTEN-PDKEQL---TLQNLSISPYEAHQGTSkFDLTLGgft 980
Cdd:PRK12316 1858 VQALNLALREHEHTPLYDIQRWAGQGGE----ALFDSLLVFENyPVAEALkqgAPAGLVFGRVSNHEQTN-YPLTLA--- 1929
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 981 DENGIGLQLEYATDL--FAKETAEKWSEYVLRLLKAVADNPNQPLSSLLLVTETEKQALLEAWKGKALPVPTDKTVHQLF 1058
Cdd:PRK12316 1930 VTLGETLSLQYSYDRghFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRI 2009
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1059 EETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPD 1138
Cdd:PRK12316 2010 AEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPA 2089
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1139 QRIEYILQDSGAKLLLKQEGISVPDSYTGDVILLDGSRtilSLPLDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMV 1218
Cdd:PRK12316 2090 ERLAYMLEDSGAALLLTQRHLLERLPLPAGVARLPLDR---DAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAV 2166
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1219 EHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRlDIVRLNDYFETNGVTITFLPTQ 1298
Cdd:PRK12316 2167 SHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELW-DPEQLYDEMERHGVTILDFPPV 2245
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1299 LAEQFMELEN-----TSLRVLLTGGD--------KLKRAVKKPYtLVNNYGPTENTVVATSAEIHPEEGS----LSIGRA 1361
Cdd:PRK12316 2246 YLQQLAEHAErdgrpPAVRVYCFGGEavpaaslrLAWEALRPVY-LFNGYGPTEAVVTPLLWKCRPQDPCgaayVPIGRA 2324
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1362 IANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPF-VPGERMYRTGDLVKW-VNGGIEYIGRID 1439
Cdd:PRK12316 2325 LGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYrADGVVEYLGRID 2404
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1440 QQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGnTAIAAYVTPETA---DIEALKSTLKETLPDYMIPAFWVTLN 1516
Cdd:PRK12316 2405 HQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASG-KQLVAYVVPDDAaedLLAELRAWLAARLPAYMVPAHWVVLE 2483
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1517 ELPVTANGKVDRKALPEPDIEAGSGEYKAPTTDMEELLAGIWQDVLGMSEVGVTDNFFSLGGDSIKGIQMASRLNQH-GW 1595
Cdd:PRK12316 2484 RLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDlGL 2563
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1596 KLEMKDLFQHPTIEELTQYVERAEGKQA-DQGPVEGEVIL----TPIQRWFFEKNFTNKHHWNQSVMLHAKKGFDPERVE 1670
Cdd:PRK12316 2564 EVPLRILFERPTLAAFAASLESGQTSRApVLQKVTRVQPLplshAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALE 2643
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1671 KTLQALIEHHDALRMVYREENGDIVQVYKPIGESKVSFEivDLYGSDEEMLRSQIkllANKLQSSLDLRNGPLLKAEQYR 1750
Cdd:PRK12316 2644 QAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLE--DCAGVADAAIRQRV---AEEIQRPFDLARGPLLRVRLLA 2718
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1751 TEAGDH-LLIAVHHLVVDGVSWRILLEDFASGYMQAEKEESLVFPQKTNSFKDWAEELAAFSQSAHLLQQAEYW-SQIAA 1828
Cdd:PRK12316 2719 LDGQEHvLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQLDYWrERLGG 2798
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1829 EQ-VSPLPKDCETEQRIVKDTSSVLCELTAEDTKHLLtDVHQPYGTEINDILLSALGLTMKEWTKGAKIGINLEGHGREd 1907
Cdd:PRK12316 2799 EQpVLELPLDRPRPALQSHRGARLDVALDVALSRELL-ALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRN- 2876
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1908 iipNVNISRTVGWFTAQYPVVLDISDAdasaviKTVKENLRRIPDKGVGYGILRYFTETAETKGFTPEIS------FNYL 1981
Cdd:PRK12316 2877 ---RAETERLIGFFVNTQVLRAQVDAQ------LAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSlshsplFQVM 2947
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1982 GQFDSEVKTDFFEPSAFDMGRQVSGESEALYALSFSGMIRNGRFVlSCSYNEKEFERATVeEQMERFKENLLMLIRHCTE 2061
Cdd:PRK12316 2948 YNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGA-SLTYATDLFDARTV-ERLARHWQNLLRGMVENPQ 3025
|
1530 1540
....*....|....*....|...
gi 2214269206 2062 KEDKEFTPSDFSAEDLEMDEMGD 2084
Cdd:PRK12316 3026 RSVDELAMLDAEERGQLLEAWNA 3048
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
599-1690 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 693.44 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 599 LKPADKQDMYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGeLDISRLRDSLNQLVNRHESLRTSFMEANG--EPVQRI 676
Cdd:PRK12467 2638 VAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGEleEPLQVV 2716
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 677 IEKAEV--------DLHVFEAKED---EADQKikefiRPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFV 745
Cdd:PRK12467 2717 YKQARLpfsrldwrDRADLEQALDalaAADRQ-----QGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLL 2791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 746 KELALLYKGEQLPEPTLHYKDFAVWQneaeQKERMKEHEAYWMSVLSG-ELPELDLPLDYARPpVQSFKGDTIRFRTGSE 824
Cdd:PRK12467 2792 GEVLQRYFGQPPPAREGRYRDYIAWL----QAQDAEASEAFWKEQLAAlEEPTRLARALYPAP-AEAVAGHGAHYLHLDA 2866
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 825 TAKAVEKLLA-ETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTN--ADVQDMPGMFVNTLALRMEAKEQQTFAEL 901
Cdd:PRK12467 2867 TQTRQLIEFArRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAqlRGAEQQLGLFINTLPVIASPRAEQTVSDW 2946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 902 LELAKQTNLSALEHQEYPFEDLVNQLDLPRDmsrnPLFNVMVTTEN-PDKEQL---TLQNLSISPYEAHQGTSkFDLTLG 977
Cdd:PRK12467 2947 LQQVQAQNLALREFEHTPLADIQRWAGQGGE----ALFDSILVFENyPISEALkqgAPSGLRFGAVSSREQTN-YPLTLA 3021
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 978 GFTDENgIGLQLEYATDLFAKETAEKWSEYVLRLLKAVADNPNQPLSSLLLVTETEKQALLEAWKGKALPVPTDKTVHQL 1057
Cdd:PRK12467 3022 VGLGDT-LELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVHQL 3100
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1058 FEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYP 1137
Cdd:PRK12467 3101 IEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYP 3180
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1138 DQRIEYILQDSGAKLLLKQEGI--SVPDSYTGDVILLDGsrtilsLPLDENDEGNPETAVTAENLAYMIYTSGTTGQPKG 1215
Cdd:PRK12467 3181 RERLAYMIEDSGVKLLLTQAHLleQLPAPAGDTALTLDR------LDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKG 3254
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1216 VMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRlDIVRLNDYFETNGVTITFL 1295
Cdd:PRK12467 3255 VGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLW-DPEELWQAIHAHRISIACF 3333
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1296 PTQLAEQFMELEN----TSLRVLLTGGDKLK-------RAVKKPYTLVNNYGPTENTVV----ATSAEIHPEEGSLSIGR 1360
Cdd:PRK12467 3334 PPAYLQQFAEDAGgadcASLDIYVFGGEAVPpaafeqvKRKLKPRGLTNGYGPTEAVVTvtlwKCGGDAVCEAPYAPIGR 3413
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1361 AIANTRVYIL-GEGNQVqPEGVAGELCVAGRGLARGYLNREDETAKRFVADPF-VPGERMYRTGDLVKW-VNGGIEYIGR 1437
Cdd:PRK12467 3414 PVAGRSIYVLdGQLNPV-PVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFsGSGGRLYRTGDLARYrADGVIEYLGR 3492
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1438 IDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGnTAIAAYVTP--ETADI-EALKSTLKETLPDYMIPAFWVT 1514
Cdd:PRK12467 3493 IDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGG-KQLVAYVVPadPQGDWrETLRDHLAASLPDYMVPAQLLV 3571
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1515 LNELPVTANGKVDRKALPEPDIEaGSGEYKAPTTDMEELLAGIWQDVLGMSEVGVTDNFFSLGGDSIKGIQMASRLNQ-H 1593
Cdd:PRK12467 3572 LAAMPLGPNGKVDRKALPDPDAK-GSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQsL 3650
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1594 GWKLEMKDLFQHPTIEELTQYVEraegkqadqgpvEGEVILTPIqrwffeknftnkhhwnqsvmlhakkgFDPERVEKTL 1673
Cdd:PRK12467 3651 GLKLSLRDLMSAPTIAELAGYSP------------LGDVPVNLL--------------------------LDLNRLETGF 3692
|
1130
....*....|....*..
gi 2214269206 1674 QALIEHHDALRMVYREE 1690
Cdd:PRK12467 3693 PALFCRHEGLGTVFDYE 3709
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
5-850 |
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: 687.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 5 TEATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAF 84
Cdd:COG1020 474 ADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAY 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 85 LPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGIIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPK 164
Cdd:COG1020 554 VPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPK 633
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 165 GVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIK 244
Cdd:COG1020 634 GVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLN 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 245 LTPSLFHTIVNTASfakdANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDlyEPDAFAKR 324
Cdd:COG1020 714 LTPSLLRALLDAAP----EALPSLRLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVT--PPDADGGS 787
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 325 PTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS-PGSLMYKTGDVVRRLSDGTLA 403
Cdd:COG1020 788 VPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGfPGARLYRTGDLARWLPDGNLE 867
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 404 FIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEG-GLQELCAYYTSD--QDIEKAELRYQLSLTLPSHMIPA 480
Cdd:COG1020 868 FLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDApGDKRLVAYVVPEagAAAAAALLRLALALLLPPYMVPA 947
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 481 FFVQVDAIPLTANGKTDRNALPKPNAAQSGGKALAAPETALEESLcrIWQKTLGIEAIGIDDNFFDLGGHSLKGMMLIAN 560
Cdd:COG1020 948 AVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAA--LALLLLLVVVVGDDDFFFFGGGLGLLLLLALAR 1025
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 561 IQAELEKSVPLKALFEQPTVRQLAAyMEASAVSGGHQVLKPADKQDMYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEG 640
Cdd:COG1020 1026 AARLLLLLLLLLLLFLAAAAAAAAA-AAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLL 1104
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 641 ELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEK------AEVDLHVFEAKEDEADQKIKEFIRPFDLNDAPLIR 714
Cdd:COG1020 1105 LLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVAlaaalaLAALLALLLAAAAAAAELLAAAALLLLLALLLLAL 1184
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 715 AALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLY------KGEQLPEPTLHYKDFAVWQNEA--EQKERMKEHEAY 786
Cdd:COG1020 1185 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLllaaaaAALLALALLLALLALAALLALAalAALAAALLALAL 1264
|
810 820 830 840 850 860
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2214269206 787 WMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLLAETGTTLHMVLHAVFHV 850
Cdd:COG1020 1265 ALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
599-1624 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 679.76 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 599 LKPADKQDMYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGeLDISRLRDSLNQLVNRHESLRTSFME--ANGEPVQRI 676
Cdd:PRK12316 4094 LPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWqgELGRPLQVV 4172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 677 IEKAEVDLHVFE---------AKEDEADQkikEFIRPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKE 747
Cdd:PRK12316 4173 HKQVSLPFAELDwrgradlqaALDALAAA---ERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGE 4249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 748 LALLYKGEQLPEPTLHYKDFAVWQneaeQKERMKEHEAYWMSVLSGELPELDLPLDYARPPVQSFKG--DTIRFRTGSET 825
Cdd:PRK12316 4250 VLERYSGRPPAQPGGRYRDYIAWL----QRQDAAASEAFWREQLAALDEPTRLAQAIARADLRSANGygEHVRELDATAT 4325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 826 AkAVEKLLAETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTnAD---VQDMPGMFVNTLALRMEAKEQQTFAELL 902
Cdd:PRK12316 4326 A-RLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRP-AElpgIEGQIGLFINTLPVIATPRAQQSVVEWL 4403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 903 ELAKQTNLSALEHQEYPFEDLVNQldlpRDMSRNPLFNVMVTTEN-PDKE---QLTLQNLSISPYEAH-QGTSKFDLTLG 977
Cdd:PRK12316 4404 QQVQRQNLALREHEHTPLYEIQRW----AGQGGEALFDSLLVFENyPVSEalqQGAPGGLRFGEVTNHeQTNYPLTLAVG 4479
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 978 GftdENGIGLQLEYATDLFAKETAEKWSEYVLRLLKAVADNPNQPLSSLLLVTETEKQALLEAWKGKALPVPTDKTVHQL 1057
Cdd:PRK12316 4480 L---GETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRCVHQL 4556
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1058 FEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYP 1137
Cdd:PRK12316 4557 VAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYP 4636
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1138 DQRIEYILQDSGAKLLLKQ----EGISVPDSytgdvilldgsrtILSLPLDENDE------GNPETAVTAENLAYMIYTS 1207
Cdd:PRK12316 4637 RERLAYMMEDSGAALLLTQshllQRLPIPDG-------------LASLALDRDEDwegfpaHDPAVRLHPDNLAYVIYTS 4703
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1208 GTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRlDIVRLNDYFET 1287
Cdd:PRK12316 4704 GSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEIHE 4782
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1288 NGVTITFLPT----QLAEQFMELEN-TSLRVLLTGGDKLKRAVK-------KPYTLVNNYGPTENTVV----ATSAEIHP 1351
Cdd:PRK12316 4783 HRVTVLVFPPvylqQLAEHAERDGEpPSLRVYCFGGEAVAQASYdlawralKPVYLFNGYGPTETTVTvllwKARDGDAC 4862
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1352 EEGSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPF-VPGERMYRTGDLVKW-VN 1429
Cdd:PRK12316 4863 GAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYrAD 4942
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1430 GGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGnTAIAAYVTPETADI-----------EALKST 1498
Cdd:PRK12316 4943 GVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG-KQLVGYVVPQDPALadadeaqaelrDELKAA 5021
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1499 LKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPDIEAGSGEYKAPTTDMEELLAGIWQDVLGMSEVGVTDNFFSLGG 1578
Cdd:PRK12316 5022 LRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGG 5101
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*..
gi 2214269206 1579 DSIKGIQMASRLN-QHGWKLEMKDLFQHPTIEELTQYVERAEGKQAD 1624
Cdd:PRK12316 5102 HSLLAIQVTSRIQlELGLELPLRELFQTPTLAAFVELAAAAGSGDDE 5148
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
21-501 |
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: 626.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 21 PDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSL 100
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 101 EDSGAKFAVVNernmtaigqyegiivslddgkwrneskerpssisgSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWF 180
Cdd:cd05930 81 EDSGAKLVLTD-----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 181 SEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASfa 260
Cdd:cd05930 126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 261 kDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDlyEPDAFAKRPTIGRPIANAGALVLN 340
Cdd:cd05930 204 -LAALPSLRLVLVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVP--PDDEEDGRVPIGRPIPNTRVYVLD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 341 EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIE 420
Cdd:cd05930 281 ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 421 PKEIETVMLSLSGIQEAVVLAVSEG-GLQELCAYYTSDQ--DIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTD 497
Cdd:cd05930 361 LGEIEAALLAHPGVREAAVVAREDGdGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVD 440
|
....
gi 2214269206 498 RNAL 501
Cdd:cd05930 441 RKAL 444
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1067-1531 |
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: 607.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:cd05930 2 DAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLkqegisvpdsytgdvilldgsrtilslpldendegnpetaVTAENLAYMIYTSGTTGQPKGVMVEHHALVNL 1226
Cdd:cd05930 82 DSGAKLVL----------------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1227 CFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTITFLPTQLAEQFME- 1305
Cdd:cd05930 122 LLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQe 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1306 ---LENTSLRVLLTGGDKLK-------RAVKKPYTLVNNYGPTENTVVATSAEIHPEE---GSLSIGRAIANTRVYILGE 1372
Cdd:cd05930 202 lelAALPSLRLVLVGGEALPpdlvrrwRELLPGARLVNLYGPTEATVDATYYRVPPDDeedGRVPIGRPIPNTRVYVLDE 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1373 GNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRIEL 1451
Cdd:cd05930 282 NLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWlPDGNLEFLGRIDDQVKIRGYRIEL 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1452 SEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE---TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDR 1528
Cdd:cd05930 362 GEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDeggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDR 441
|
...
gi 2214269206 1529 KAL 1531
Cdd:cd05930 442 KAL 444
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1631-2059 |
0e+00 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. 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 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: 380457 [Multi-domain] Cd Length: 428 Bit Score: 574.20 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1631 EVILTPIQRWFFEKNFTNKHHWNQSVMLHAKKGFDPERVEKTLQALIEHHDALRMVYREENGDIVQVYKPIGESKVSFEI 1710
Cdd:cd19534 1 EVPLTPIQRWFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEELFRLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1711 VDLYGSDEEmlrSQIKLLANKLQSSLDLRNGPLLKAEQY-RTEAGDHLLIAVHHLVVDGVSWRILLEDFASGYMQAEKEE 1789
Cdd:cd19534 81 VDLSSLAQA---AAIEALAAEAQSSLDLEEGPLLAAALFdGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1790 SLVFPQKTnSFKDWAEELAAFSQSAHLLQQAEYWSQIAAEQVSPLPKDCETEQrivKDTSSVLCELTAEDTKHLLTDVHQ 1869
Cdd:cd19534 158 PIPLPSKT-SFQTWAELLAEYAQSPALLEELAYWRELPAADYWGLPKDPEQTY---GDARTVSFTLDEEETEALLQEANA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1870 PYGTEINDILLSALGLTMKEWTKGAKIGINLEGHGREDIIPNVNISRTVGWFTAQYPVVLDI-SDADASAVIKTVKENLR 1948
Cdd:cd19534 234 AYRTEINDLLLAALALAFQDWTGRAPPAIFLEGHGREEIDPGLDLSRTVGWFTSMYPVVLDLeASEDLGDTLKRVKEQLR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1949 RIPDKGVGYGILRYFTETAE---TKGFTPEISFNYLGQFDSEVKTDFFEPSAFDM-GRQVSGESEALYALSFSGMIRNGR 2024
Cdd:cd19534 314 RIPNKGIGYGILRYLTPEGTkrlAFHPQPEISFNYLGQFDQGERDDALFVSAVGGgGSDIGPDTPRFALLDINAVVEGGQ 393
|
410 420 430
....*....|....*....|....*....|....*
gi 2214269206 2025 FVLSCSYNEKEFERATVEEQMERFKENLLMLIRHC 2059
Cdd:cd19534 394 LVITVSYSRNMYHEETIQQLADSYKEALEALIEHC 428
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1056-1531 |
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: 568.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1056 QLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPD 1135
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1136 YPDQRIEYILQDSGAKLLLKQEGISVPDSYTGDVILLDGsrtilslPLDENDEGNPETAVTAENLAYMIYTSGTTGQPKG 1215
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDE-------ALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1216 VMVEHHALVNLCFwHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTITFL 1295
Cdd:cd12117 154 VAVTHRGVVRLVK-NTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1296 PT----QLAEQFMELEnTSLRVLLTGGDKLK-RAVKK------PYTLVNNYGPTENTVVATSAEIHP---EEGSLSIGRA 1361
Cdd:cd12117 233 TAalfnQLADEDPECF-AGLRELLTGGEVVSpPHVRRvlaacpGLRLVNGYGPTENTTFTTSHVVTEldeVAGSIPIGRP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1362 IANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKWV-NGGIEYIGRIDQ 1440
Cdd:cd12117 312 IANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLpDGRLEFLGRIDD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1441 QVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPETA-DIEALKSTLKETLPDYMIPAFWVTLNELP 1519
Cdd:cd12117 392 QVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGAlDAAELRAFLRERLPAYMVPAAFVVLDELP 471
|
490
....*....|..
gi 2214269206 1520 VTANGKVDRKAL 1531
Cdd:cd12117 472 LTANGKVDRRAL 483
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
12-504 |
1.32e-180 |
|
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: 557.71 E-value: 1.32e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 12 LFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDT 91
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 92 PEERIRYSLEDSGAKFaVVNERNMTAIGQYEGIIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHR 171
Cdd:cd17655 82 PEERIQYILEDSGADI-LLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 172 NLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFH 251
Cdd:cd17655 161 GVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 252 TIVntasFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHT-EFINHYGPTEATIGAIAGrvdLYEPDAFAK-RPTIGR 329
Cdd:cd17655 241 LLD----AADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNpTITNAYGPTETTVDASIY---QYEPETDQQvSVPIGK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 330 PIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRAD 409
Cdd:cd17655 314 PLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 410 DQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVS-EGGLQELCAYYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAI 488
Cdd:cd17655 394 HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKdEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEI 473
|
490
....*....|....*.
gi 2214269206 489 PLTANGKTDRNALPKP 504
Cdd:cd17655 474 PLTPNGKVDRKALPEP 489
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
609-1628 |
6.88e-177 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 575.84 E-value: 6.88e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 609 PLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRI------IEKAEV 682
Cdd:PRK10252 9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVdpaltfPLPEII 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 683 DLHVFEAKEDEADQKIK-EFIRPFDL-NDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKGEQL--P 758
Cdd:PRK10252 89 DLRTQPDPHAAAQALMQaDLQQDLRVdSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRgeP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 759 EPTLHYKDFAVWQNEAE---QKERMKEHEAYWMSVLSGeLPELdLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLLAE 835
Cdd:PRK10252 169 TPASPFTPFADVVEEYQryrASEAWQRDAAFWAEQRRQ-LPPP-ASLSPAPLPGRSASADILRLKLEFTDGAFRQLAAQA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 836 TGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELL-ELAKQTNlSALE 914
Cdd:PRK10252 247 SGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELAtRLAAQLK-KMRR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 915 HQEYPFEDLVNQLDLPRDMSR--NPLFNVMVTTENPDKE--QLTLQNLSISPYEahqgtskfDLTLGGFTDENGiGLQLE 990
Cdd:PRK10252 326 HQRYDAEQIVRDSGRAAGDEPlfGPVLNIKVFDYQLDFPgvQAQTHTLATGPVN--------DLELALFPDEHG-GLSIE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 991 YAT--DLFAKETAEKWSEYVLRLLKAVADNPNQPLSSLLLVTETEKQaLLEAWKGKALPVPtDKTVHQLFEETVQRHKDR 1068
Cdd:PRK10252 397 ILAnpQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYA-QLAQVNATAVEIP-ETTLSALVAQQAAKTPDA 474
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1069 PAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDS 1148
Cdd:PRK10252 475 PALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDA 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1149 GAKLLLKQE-------GISVPDSYTGDVILLDGSRTILSLPLdendegnPETAvtaenlAYMIYTSGTTGQPKGVMVEHH 1221
Cdd:PRK10252 555 RPSLLITTAdqlprfaDVPDLTSLCYNAPLAPQGAAPLQLSQ-------PHHT------AYIIFTSGSTGRPKGVMVGQT 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1222 ALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTIT-FLPTQLA 1300
Cdd:PRK10252 622 AIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTThFVPSMLA 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1301 EQFMELEN-------TSLRVLLTGGDKL--------KRAVKKPytLVNNYGPTENTV-----VATSAEIHPEEG-SLSIG 1359
Cdd:PRK10252 702 AFVASLTPegarqscASLRQVFCSGEALpadlcrewQQLTGAP--LHNLYGPTEAAVdvswyPAFGEELAAVRGsSVPIG 779
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1360 RAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKWV-NGGIEYIGRI 1438
Cdd:PRK10252 780 YPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLdDGAVEYLGRS 859
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1439 DQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAV------KDKGGNTAIAAYVTPE---TADIEALKSTLKETLPDYMIP 1509
Cdd:PRK10252 860 DDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaATGGDARQLVGYLVSQsglPLDTSALQAQLRERLPPHMVP 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1510 AFWVTLNELPVTANGKVDRKALPEPDIEAGSGEyKAPTTDMEELLAGIWQDVLGMSEVGVTDNFFSLGGDSIKGIQMASR 1589
Cdd:PRK10252 940 VVLLQLDQLPLSANGKLDRKALPLPELKAQVPG-RAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQ 1018
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|
gi 2214269206 1590 LNQH-GWKLEMKDLFQHPTIEELTQYVERAEGKQADQGPV 1628
Cdd:PRK10252 1019 LSRQfARQVTPGQVMVASTVAKLATLLDAEEDESRRLGFG 1058
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1056-1535 |
1.08e-175 |
|
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: 544.61 E-value: 1.08e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1056 QLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPD 1135
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1136 YPDQRIEYILQDSGAKLLLKQEGISVPDSYTGDVILLDgSRTIlslplDENDEGNPETAVTAENLAYMIYTSGTTGQPKG 1215
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLD-EDTI-----YHEESENLEPVSKSDDLAYVIYTSGSTGKPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1216 VMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTITFL 1295
Cdd:cd17655 155 VMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1296 P---TQLAEQFMELENTSLRVLLTGGDKLK-RAVKKPY-------TLVNNYGPTENTVVATSAEIHPE---EGSLSIGRA 1361
Cdd:cd17655 235 TpahLKLLDAADDSEGLSLKHLIVGGEALStELAKKIIelfgtnpTITNAYGPTETTVDASIYQYEPEtdqQVSVPIGKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1362 IANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKWV-NGGIEYIGRIDQ 1440
Cdd:cd17655 315 LGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLpDGNIEFLGRIDH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1441 QVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAY-VTPETADIEALKSTLKETLPDYMIPAFWVTLNELP 1519
Cdd:cd17655 395 QVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYiVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIP 474
|
490
....*....|....*.
gi 2214269206 1520 VTANGKVDRKALPEPD 1535
Cdd:cd17655 475 LTPNGKVDRKALPEPD 490
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
608-1019 |
4.48e-175 |
|
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: 540.02 E-value: 4.48e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 608 YPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKAEVDLHV- 686
Cdd:cd19531 2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPVv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 687 ------FEAKEDEADQKIKEFI-RPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKGE---- 755
Cdd:cd19531 82 dlsglpEAEREAEAQRLAREEArRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFlagr 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 756 --QLPEPTLHYKDFAVWQNEAEQKERMKEHEAYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLL 833
Cdd:cd19531 162 psPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALRALA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 834 AETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSAL 913
Cdd:cd19531 242 RREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETALEAY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 914 EHQEYPFEDLVNQLDLPRDMSRNPLFNVMVTTENPDKEQLTLQNLSISPYEAHQGTSKFDLTLGGFTDENGIGLQLEYAT 993
Cdd:cd19531 322 AHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLEYNT 401
|
410 420
....*....|....*....|....*.
gi 2214269206 994 DLFAKETAEKWSEYVLRLLKAVADNP 1019
Cdd:cd19531 402 DLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1058-1532 |
2.02e-174 |
|
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: 541.16 E-value: 2.02e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1058 FEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYP 1137
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1138 DQRIEYILQDSGAKLLLKQEGisvpDSYTGDVILLDGSRTiLSLPLDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVM 1217
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPA----LAGELAVELVAVTLL-DQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1218 VEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTITFLPT 1297
Cdd:cd17651 156 MPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1298 QLAEQFMEL------ENTSLRVLLTGGDKLKRAVKKPY--------TLVNNYGPTENTVVatSAEIHPEEGS-----LSI 1358
Cdd:cd17651 236 VALRALAEHgrplgvRLAALRYLLTGGEQLVLTEDLREfcaglpglRLHNHYGPTETHVV--TALSLPGDPAawpapPPI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1359 GRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKWV-NGGIEYIGR 1437
Cdd:cd17651 314 GRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLpDGELEFLGR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1438 IDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE---TADIEALKSTLKETLPDYMIPAFWVT 1514
Cdd:cd17651 394 ADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDpeaPVDAAELRAALATHLPEYMVPSAFVL 473
|
490
....*....|....*...
gi 2214269206 1515 LNELPVTANGKVDRKALP 1532
Cdd:cd17651 474 LDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
11-501 |
1.11e-173 |
|
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: 538.71 E-value: 1.11e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 11 ALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPD 90
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 91 TPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGIIVSLDDgkWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEH 170
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEA--LDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 171 RNLTNYV--SWFseeAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPS 248
Cdd:cd12117 159 RGVVRLVknTNY---VTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 249 LFHTIVNTASFAkdanFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDlyEPDAFAKRPTIG 328
Cdd:cd12117 236 LFNQLADEDPEC----FAGLRELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVT--ELDEVAGSIPIG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 329 RPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRA 408
Cdd:cd12117 310 RPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 409 DDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV-SEGGLQELCAYYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDA 487
Cdd:cd12117 390 DDQVKIRGFRIELGEIEAALRAHPGVREAVVVVReDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDE 469
|
490
....*....|....
gi 2214269206 488 IPLTANGKTDRNAL 501
Cdd:cd12117 470 LPLTANGKVDRRAL 483
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
604-1038 |
1.30e-172 |
|
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: 534.61 E-value: 1.30e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 604 KQDMYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFM-EANGEPVQRIIEKAEV 682
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVILEERPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 683 DLHVFEAK---EDEADQKIKEFIR-----PFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLY-- 752
Cdd:pfam00668 81 ELEIIDISdlsESEEEEAIEAFIQrdlqsPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYqq 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 753 --KGEQLPEPTLH-YKDFAVWQNEAEQKERMKEHEAYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAV 829
Cdd:pfam00668 161 llKGEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 830 EKLLAETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTN 909
Cdd:pfam00668 241 RKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 910 LSALEHQEYPFEDLVNQLDLPRDMSRNPLFNVMVTTEN-------PDKEQLTLQNLSISPYEAHQgtSKFDLTLGGFTDE 982
Cdd:pfam00668 321 LSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNylgqdsqEEEFQLSELDLSVSSVIEEE--AKYDLSLTASERG 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 983 NGIGLQLEYATDLFAKETAEKWSEYVLRLLKAVADNPNQPLSSLLLVTETEKQALL 1038
Cdd:pfam00668 399 GGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
5-835 |
1.81e-166 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 571.52 E-value: 1.81e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 5 TEATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAF 84
Cdd:PRK12316 509 LQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAY 588
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 85 LPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGI-IVSLDD-GKW-RNESKERPSSISGSRNLAYVIYTSGTTG 161
Cdd:PRK12316 589 VPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVqVLDLDRpAAWlEGYSEENPGTELNPENLAYVIYTSGSTG 668
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 162 KPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGIT 241
Cdd:PRK12316 669 KPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVD 748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 242 YIKLTPSLFHTIVNtasFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAI-AGRVDlyepdA 320
Cdd:PRK12316 749 TLHFVPSMLQAFLQ---DEDVASCTSLRRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVThWTCVE-----E 820
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 321 FAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDG 400
Cdd:PRK12316 821 GGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADG 900
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 401 TLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVseGGLQeLCAYY--TSDQDIEKAELRYQLSLTLPSHMI 478
Cdd:PRK12316 901 VIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV--DGKQ-LVGYVvlESEGGDWREALKAHLAASLPEYMV 977
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 479 PAFFVQVDAIPLTANGKTDRNALPKPNAAQSgGKALAAPETALEESLCRIWQKTLGIEAIGIDDNFFDLGGHSLKGMMLI 558
Cdd:PRK12316 978 PAQWLALERLPLTPNGKLDRKALPAPEASVA-QQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVV 1056
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 559 ANI-QAELEKSvPlKALFEQPTVRQLAAYMEASAVSGGHQvlKPADKQdmYPLSSAQKRMYVLNQLDRQtiSYNMpSVLL 637
Cdd:PRK12316 1057 SRArQAGIQLS-P-RDLFQHQTIRSLALVAKAGQATAADQ--GPASGE--VALAPVQRWFFEQAIPQRQ--HWNQ-SLLL 1127
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 638 MEGE-LDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKAEVDLHVFEAKEDEADQK--IKEFIRPFDLNDAPLIR 714
Cdd:PRK12316 1128 QARQpLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQAASEEELLalCEEAQRSLDLEQGPLLR 1207
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 715 AALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKGEQ--LPEPTLHYKDFAVWQNEAEQKErmKEHEAYWMSVLs 792
Cdd:PRK12316 1208 ALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDadLPARTSSYQAWARRLHEHAGAR--AEELDYWQAQL- 1284
|
810 820 830 840
....*....|....*....|....*....|....*....|...
gi 2214269206 793 GELPElDLPLDYARPPVQSFKGDTIRFRTGSETAKaveKLLAE 835
Cdd:PRK12316 1285 EDAPH-ELPCENPDGALENRHERKLELRLDAERTR---QLLQE 1323
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
13-502 |
4.08e-161 |
|
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: 504.57 E-value: 4.08e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 13 FEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTP 92
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 93 EERIRYSLEDSGAKFAVVNERNMTAIGQYEGIIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRN 172
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 173 LTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHT 252
Cdd:cd17651 161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 253 IVNtASFAKDANFESLRLIVLGGEKIIPTDVIA--FRKMyGHTEFINHYGPTEATIgAIAGRVDLyEPDAFAKRPTIGRP 330
Cdd:cd17651 241 LAE-HGRPLGVRLAALRYLLTGGEQLVLTEDLRefCAGL-PGLRLHNHYGPTETHV-VTALSLPG-DPAAWPAPPPIGRP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 331 IANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADD 410
Cdd:cd17651 317 IDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 411 QVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEG-GLQELCAYYTSDQDIEK--AELRYQLSLTLPSHMIPAFFVQVDA 487
Cdd:cd17651 397 QVKIRGFRIELGEIEAALARHPGVREAVVLAREDRpGEKRLVAYVVGDPEAPVdaAELRAALATHLPEYMVPSAFVLLDA 476
|
490
....*....|....*
gi 2214269206 488 IPLTANGKTDRNALP 502
Cdd:cd17651 477 LPLTPNGKLDRRALP 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
34-439 |
8.27e-160 |
|
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: 497.56 E-value: 8.27e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLRAQ-GAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNE 112
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 RNMTAIGQY--EGIIVSLDDGK--WRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTE 188
Cdd:TIGR01733 81 ALASRLAGLvlPVILLDPLELAalDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 189 NDKTVLLSSYAFDLGYTSMFPVLLGGGEL-HIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNtasfAKDANFES 267
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLvVPPEDEERDDAALLAALIAEHPVTVLNLTPSLLALLAA----ALPPALAS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 268 LRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDlYEPDAFAKRPTIGRPIANAGALVLNEALKLVP 347
Cdd:TIGR01733 237 LRLVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVD-PDDAPRESPVPIGRPLANTRLYVLDDDLRPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 348 PGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSL--MYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIE 425
Cdd:TIGR01733 316 VGVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGarLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIE 395
|
410
....*....|....
gi 2214269206 426 TVMLSLSGIQEAVV 439
Cdd:TIGR01733 396 AALLRHPGVREAVV 409
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
11-501 |
2.54e-158 |
|
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: 496.80 E-value: 2.54e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 11 ALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPD 90
Cdd:cd17646 2 ALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 91 TPEERIRYSLEDSGAKFaVVNERNMTAIGQYEGIIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEH 170
Cdd:cd17646 82 YPADRLAYMLADAGPAV-VLTTADLAARLPAGGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 171 RNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLF 250
Cdd:cd17646 161 AGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSML 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 251 HTIVNTASFAKDAnfeSLRLIVLGGEKIiPTDVIA-FRKMyGHTEFINHYGPTEATIGAIAGRVDlyePDAFAKRPTIGR 329
Cdd:cd17646 241 RVFLAEPAAGSCA---SLRRVFCSGEAL-PPELAArFLAL-PGAELHNLYGPTEAAIDVTHWPVR---GPAETPSVPIGR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 330 PIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRAD 409
Cdd:cd17646 313 PVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 410 DQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEG-GLQELCAYYTSD---QDIEKAELRYQLSLTLPSHMIPAFFVQV 485
Cdd:cd17646 393 DQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPaGAARLVGYVVPAagaAGPDTAALRAHLAERLPEYMVPAAFVVL 472
|
490
....*....|....*.
gi 2214269206 486 DAIPLTANGKTDRNAL 501
Cdd:cd17646 473 DALPLTANGKLDRAAL 488
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1055-1531 |
8.83e-156 |
|
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: 489.86 E-value: 8.83e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1055 HQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDP 1134
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1135 DYPDQRIEYILQDSGAKLLLKQEGISVPDSYTGDVILLDGSRtilslpLDENDEGNPETAVTAENLAYMIYTSGTTGQPK 1214
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA------LAAPPATPPLVPPRPDNLAYVIYTSGSTGRPK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1215 GVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTIT- 1293
Cdd:cd17646 155 GVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCh 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1294 FLPTQLaEQFMEL----ENTSLRVLLTGGDKL-----KRAVKKPY-TLVNNYGPTENTVVATSAEIHP--EEGSLSIGRA 1361
Cdd:cd17646 235 FVPSML-RVFLAEpaagSCASLRRVFCSGEALppelaARFLALPGaELHNLYGPTEAAIDVTHWPVRGpaETPSVPIGRP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1362 IANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKWV-NGGIEYIGRIDQ 1440
Cdd:cd17646 314 VPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRpDGALEFLGRSDD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1441 QVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP----ETADIEALKSTLKETLPDYMIPAFWVTLN 1516
Cdd:cd17646 394 QVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPaagaAGPDTAALRAHLAERLPEYMVPAAFVVLD 473
|
490
....*....|....*
gi 2214269206 1517 ELPVTANGKVDRKAL 1531
Cdd:cd17646 474 ALPLTANGKLDRAAL 488
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
21-502 |
1.15e-151 |
|
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: 476.36 E-value: 1.15e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 21 PDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSL 100
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 101 EDSGAkfavvnernmtaigqyeGIIVSLDDgkwrneskerpssisgsrNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWF 180
Cdd:cd17652 81 ADARP-----------------ALLLTTPD------------------NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 181 SEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIvntasfa 260
Cdd:cd17652 126 IAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAAL------- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 261 KDANFESLRLIVLGGEKIIPTDViafRKMYGHTEFINHYGPTEATIGAIagrvdLYEPDAFAKRPTIGRPIANAGALVLN 340
Cdd:cd17652 199 PPDDLPDLRTLVVAGEACPAELV---DRWAPGRRMINAYGPTETTVCAT-----MAGPLPGGGVPPIGRPVPGTRVYVLD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 341 EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS-PGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRI 419
Cdd:cd17652 271 ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGaPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 420 EPKEIETVMLSLSGIQEAVVLAVSEG-GLQELCAYYTSDQD--IEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKT 496
Cdd:cd17652 351 ELGEVEAALTEHPGVAEAVVVVRDDRpGDKRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKL 430
|
....*.
gi 2214269206 497 DRNALP 502
Cdd:cd17652 431 DRRALP 436
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1067-1532 |
3.39e-150 |
|
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: 472.12 E-value: 3.39e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:cd17652 2 DAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLKQegisvpdsytgdvilldgsrtilslpldendegnpetavtAENLAYMIYTSGTTGQPKGVMVEHHALVNL 1226
Cdd:cd17652 82 DARPALLLTT----------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1227 CFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTITFLPTQLAEQFMEL 1306
Cdd:cd17652 122 AAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1307 ENTSLRVLLTGGDKLKRAVKKPY----TLVNNYGPTENTVVATSAEIHPEEGSLSIGRAIANTRVYILGEGNQVQPEGVA 1382
Cdd:cd17652 202 DLPDLRTLVVAGEACPAELVDRWapgrRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVP 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1383 GELCVAGRGLARGYLNREDETAKRFVADPF-VPGERMYRTGDLVKWVNGG-IEYIGRIDQQVKVRGYRIELSEIEVQLAQ 1460
Cdd:cd17652 282 GELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGqLEFLGRADDQVKIRGFRIELGEVEAALTE 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 1461 LSEVQDAAVTAVKDKGGNTAIAAYVTP---ETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALP 1532
Cdd:cd17652 362 HPGVAEAVVVVRDDRPGDKRLVAYVVPapgAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1067-1532 |
1.36e-149 |
|
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: 471.08 E-value: 1.36e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:cd17649 2 DAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLKQEGisvpdsytgdvilldgsrtilslpldendegnpetavtaENLAYMIYTSGTTGQPKGVMVEHHALVNL 1226
Cdd:cd17649 82 DSGAGLLLTHHP---------------------------------------RQLAYVIYTSGSTGTPKGVAVSHGPLAAH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1227 CFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTITFLPT----QLAEQ 1302
Cdd:cd17649 123 CQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPaylqQLAEE 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1303 FMELENT---SLRVLLTGGDK-----LKRAVKKPYTLVNNYGPTENTVVATSAEIHPEEG----SLSIGRAIANTRVYIL 1370
Cdd:cd17649 203 ADRTGDGrppSLRLYIFGGEAlspelLRRWLKAPVRLFNAYGPTEATVTPLVWKCEAGAAragaSMPIGRPLGGRSAYIL 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1371 GEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPF-VPGERMYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYR 1448
Cdd:cd17649 283 DADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWrDDGVIEYLGRVDHQVKIRGFR 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1449 IELSEIEVQLAQLSEVQDAAVTAVKDKGGnTAIAAYVTPE-----TADIEALKSTLKETLPDYMIPAFWVTLNELPVTAN 1523
Cdd:cd17649 363 IELGEIEAALLEHPGVREAAVVALDGAGG-KQLVAYVVLRaaaaqPELRAQLRTALRASLPDYMVPAHLVFLARLPLTPN 441
|
....*....
gi 2214269206 1524 GKVDRKALP 1532
Cdd:cd17649 442 GKLDRKALP 450
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
4-798 |
1.13e-148 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 516.25 E-value: 1.13e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 4 ITEATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAA 83
Cdd:PRK12467 3092 PSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGA 3171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 84 FLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGI-IVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGK 162
Cdd:PRK12467 3172 YVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPAPAGDtALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGK 3251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 163 PKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTaPDEIAHYIKEHGITY 242
Cdd:PRK12467 3252 PKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWD-PEELWQAIHAHRISI 3330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 243 IKLTPSLFHTIvntASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDLYEPDAFA 322
Cdd:PRK12467 3331 ACFPPAYLQQF---AEDAGGADCASLDIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVCEAP 3407
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 323 KRPtIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS-PGSLMYKTGDVVRRLSDGT 401
Cdd:PRK12467 3408 YAP-IGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGV 3486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 402 LAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYTSDQDIE--KAELRYQLSLTLPSHMIP 479
Cdd:PRK12467 3487 IEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGdwRETLRDHLAASLPDYMVP 3566
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 480 AFFVQVDAIPLTANGKTDRNALPKPNAAQSGgkALAAPETALEESLCRIWQKTLGIEAIGIDDNFFDLGGHSLKGMMLIA 559
Cdd:PRK12467 3567 AQLLVLAAMPLGPNGKVDRKALPDPDAKGSR--EYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLS 3644
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 560 NIQAELEKSVPLKALFEQPTVRQLAAYMEASAVSgghqvLKPAdkqdmyplssaqkrmyvlnqldrqtisynmpsvllme 639
Cdd:PRK12467 3645 RIRQSLGLKLSLRDLMSAPTIAELAGYSPLGDVP-----VNLL------------------------------------- 3682
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 640 geLDISRLRDSLNQLVNRHESLRTSFmeaNGEPVQRIiekaevdlhvfeakedeadqkikefirpfdlndapliraallr 719
Cdd:PRK12467 3683 --LDLNRLETGFPALFCRHEGLGTVF---DYEPLAVI------------------------------------------- 3714
|
730 740 750 760 770 780 790
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 720 IEAKKHLLLLDMHHIIADGvsrgifvkelallYKGEQLPEPTLHYKDFAVWqneaeQKERMKEHEAYWMsvLSGELPEL 798
Cdd:PRK12467 3715 LEGDRHVLGLTCRHLLDDG-------------WQDTSLQAMAVQYADYILW-----QQAKGPYGLLGWS--LGGTLARL 3773
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
21-501 |
4.27e-148 |
|
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: 467.92 E-value: 4.27e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 21 PDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSL 100
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 101 EDSGAKFAVVNERNMTAigqYEGIIVSLDDGKWRNE-SKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSW 179
Cdd:cd12116 81 EDAEPALVLTDDALPDR---LPAGLPVLLLALAAAAaAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 180 FSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASF 259
Cdd:cd12116 158 MRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGWQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 260 AKdanfESLRLIVlGGEKIIPTdvIAFRKMYGHTEFINHYGPTEATIGAIAGRVdlyepDAFAKRPTIGRPIANAGALVL 339
Cdd:cd12116 238 GR----AGLTALC-GGEALPPD--LAARLLSRVGSLWNLYGPTETTIWSTAARV-----TAAAGPIPIGRPLANTQVYVL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 340 NEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS-PGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYR 418
Cdd:cd12116 306 DAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 419 IEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYTSDQD--IEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKT 496
Cdd:cd12116 386 IELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGaaPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
....*
gi 2214269206 497 DRNAL 501
Cdd:cd12116 466 DRKAL 470
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1067-1531 |
1.53e-147 |
|
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: 466.38 E-value: 1.53e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:cd12116 2 DATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLKQEGIsvPDSYTGdvillDGSRTILSLPLDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNL 1226
Cdd:cd12116 82 DAEPALVLTDDAL--PDRLPA-----GLPVLLLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1227 CFWHHDAFSMTAEDRSAKYAGFGFDASIWEMF-PTWTiGAELHVIDEAIRLDIVRLNDYFETNGVTI---TflPT--QLA 1300
Cdd:cd12116 155 LHSMRERLGLGPGDRLLAVTTYAFDISLLELLlPLLA-GARVVIAPRETQRDPEALARLIEAHSITVmqaT--PAtwRML 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1301 EQFMELENTSLRvLLTGGDKL-----KRAVKKPYTLVNNYGPTENTVVATSAEIHPEEGSLSIGRAIANTRVYILGEGNQ 1375
Cdd:cd12116 232 LDAGWQGRAGLT-ALCGGEALppdlaARLLSRVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1376 VQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFV-PGERMYRTGDLVKWVNGG-IEYIGRIDQQVKVRGYRIELSE 1453
Cdd:cd12116 311 PVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAgPGSRLYRTGDLVRRRADGrLEYLGRADGQVKIRGHRIELGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1454 IEVQLAQLSEVQDAAVTaVKDKGGNTAIAAYVTP---ETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKA 1530
Cdd:cd12116 391 IEAALAAHPGVAQAAVV-VREDGGDRRLVAYVVLkagAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKA 469
|
.
gi 2214269206 1531 L 1531
Cdd:cd12116 470 L 470
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
601-1629 |
1.97e-147 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 512.41 E-value: 1.97e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 601 PADKQDMYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEK- 679
Cdd:PRK05691 3251 AAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKp 3330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 680 --AEVDLHVFEA-KEDEADQKIKEFIRP-----FDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALL 751
Cdd:PRK05691 3331 grTPIDYLDWRGlPEDGQEQRLQALHKQereagFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEI 3410
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 752 YK--GE----QLPEPTlHYKDFAVWQneaeQKERMKEHEAYWMSVLSGELPELDLPLDyaRPPVQSFKGDTIRFRTG--- 822
Cdd:PRK05691 3411 YTalGEgreaQLPVPP-RYRDYIGWL----QRQDLAQARQWWQDNLRGFERPTPIPSD--RPFLREHAGDSGGMVVGdcy 3483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 823 ---SETAKAVEKLLAETGT-TLHMVLHAVFHVFLSKISGQRDIVIGSVTAGR--TNADVQDMPGMFVNTLALRM---EAK 893
Cdd:PRK05691 3484 trlDAADGARLRELAQAHQlTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFINSIALRVqlpAAG 3563
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 894 EQQTFAELLELAKQTNLSALEHQEYPFEDLVNQLDLPRDmsrNPLFNVMVTTENPDKEQLTL---QNLSISPYEAHQGTS 970
Cdd:PRK05691 3564 QRCSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKG---QPLFDSLFVFENAPVEVSVLdraQSLNASSDSGRTHTN 3640
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 971 kFDLTLGGFTDENgIGLQLEYATDLFAKETAEKWSEYVLRLLKAVADNPNQPLSSLLLVTETEKQALLEAWKGKALPVPT 1050
Cdd:PRK05691 3641 -FPLTAVCYPGDD-LGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYPL 3718
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1051 DKTVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFV 1130
Cdd:PRK05691 3719 EQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYL 3798
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1131 PIDPDYPDQRIEYILQDSGAKLLL-----KQEGISVPDSYTGdvilldGSRTIL----SLPLDENDEGNPETAVTAENLA 1201
Cdd:PRK05691 3799 PLDPGLPAQRLQRIIELSRTPVLVcsaacREQARALLDELGC------ANRPRLlvweEVQAGEVASHNPGIYSGPDNLA 3872
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1202 YMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRL 1281
Cdd:PRK05691 3873 YVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGL 3952
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1282 NDYFETNGVTI-----TFLPTQLAEQFMELEntSLRVLLTGGD----KLKRAVKKPYT---LVNNYGPTE--NTVVATSA 1347
Cdd:PRK05691 3953 LAHVQAQGITVlesvpSLIQGMLAEDRQALD--GLRWMLPTGEamppELARQWLQRYPqigLVNAYGPAEcsDDVAFFRV 4030
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1348 EIHPEEGS-LSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPF-VPGERMYRTGDLV 1425
Cdd:PRK05691 4031 DLASTRGSyLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLA 4110
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1426 KW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVtAVKDKGGNTAIAAYVTP------ETADIEALKST 1498
Cdd:PRK05691 4111 RRrSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNGKHLVGYLVPhqtvlaQGALLERIKQR 4189
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1499 LKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPDI-EAGSGEYKAPTTDMEELLAGIWQDVLGMSEVGVTDNFFSLG 1577
Cdd:PRK05691 4190 LRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIgQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELG 4269
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 1578 GDSIKGIQMASRLNQHGWK-LEMKDLFQHPTIEELTQYVERAEGKQADQGPVE 1629
Cdd:PRK05691 4270 GHSLLATQIASRVQKALQRnVPLRAMFECSTVEELAEYIEGLAGSAIDEQKVD 4322
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
3-590 |
4.67e-147 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 492.25 E-value: 4.67e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 3 QITEATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGA 82
Cdd:PRK10252 454 EIPETTLSALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGA 533
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 83 AFLPIDPDTPEERIRYSLEDSGAKFAVvnernmTAIGQYE-----GIIVSLDDGKWRNESKERPSSISGSRNLAYVIYTS 157
Cdd:PRK10252 534 AWLPLDTGYPDDRLKMMLEDARPSLLI------TTADQLPrfadvPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTS 607
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 158 GTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKE 237
Cdd:PRK10252 608 GSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAE 687
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 238 HGITYIKLTPSLFHTIVNT-ASFAKDANFESLRLIVLGGEKIiPTDVIafRKMYGHT--EFINHYGPTEAtigaiAGRVD 314
Cdd:PRK10252 688 YGVTTTHFVPSMLAAFVASlTPEGARQSCASLRQVFCSGEAL-PADLC--REWQQLTgaPLHNLYGPTEA-----AVDVS 759
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 315 LY--EPDAFAKRPT----IGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMY 388
Cdd:PRK10252 760 WYpaFGEELAAVRGssvpIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMY 839
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 389 KTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV-------SEGGLQELCAYYTSDQD-- 459
Cdd:PRK10252 840 RTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaaTGGDARQLVGYLVSQSGlp 919
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 460 IEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALPKPN-AAQSGGKalaAPETALEESLCRIWQKTLGIEAI 538
Cdd:PRK10252 920 LDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPElKAQVPGR---APKTGTETIIAAAFSSLLGCDVV 996
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 539 GIDDNFFDLGGHSLKGMMLIANIQAELEKSVPLKALFEQPTVRQLAAYMEAS 590
Cdd:PRK10252 997 DADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAE 1048
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
21-501 |
1.72e-145 |
|
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: 459.85 E-value: 1.72e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 21 PDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSL 100
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 101 EDSGAKFAVVnernmtaigqyegiivslddgkwrneskeRPSsisgsrNLAYVIYTSGTTGKPKGVQIEHRNLTNYVS-- 178
Cdd:cd17643 81 ADSGPSLLLT-----------------------------DPD------DLAYVIYTSGSTGRPKGVVVSHANVLALFAat 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 179 --WFseeaGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNT 256
Cdd:cd17643 126 qrWF----GFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 257 ASFAKDANfESLRLIVLGGEKIIPTDVIAFRKMYGH--TEFINHYGPTEATIGAIAGRVDLYEPDAFAKRPtIGRPIANA 334
Cdd:cd17643 202 ADRDGRDP-LALRYVIFGGEALEAAMLRPWAGRFGLdrPQLVNMYGITETTVHVTFRPLDAADLPAAAASP-IGRPLPGL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 335 GALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS-PGSLMYKTGDVVRRLSDGTLAFIGRADDQVK 413
Cdd:cd17643 280 RVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLPDGELEYLGRADEQVK 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 414 IRGYRIEPKEIETVMLSLSGIQEAVVLA-VSEGGLQELCAYYTSD--QDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPL 490
Cdd:cd17643 360 IRGFRIELGEIEAALATHPSVRDAAVIVrEDEPGDTRLVAYVVADdgAAADIAELRALLKELLPDYMVPARYVPLDALPL 439
|
490
....*....|.
gi 2214269206 491 TANGKTDRNAL 501
Cdd:cd17643 440 TVNGKLDRAAL 450
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1067-1531 |
8.92e-145 |
|
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: 457.54 E-value: 8.92e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:cd17643 2 EAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLkqegisvpdsytgdvilldgsrtilslpldendegnpetaVTAENLAYMIYTSGTTGQPKGVMVEHHALVNL 1226
Cdd:cd17643 82 DSGPSLLL----------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANVLAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1227 cFWHHD-AFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTI------TFLPTQL 1299
Cdd:cd17643 122 -FAATQrWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVlnqtpsAFYQLVE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1300 AEQFMELENTSLRVLLTGGDKLKRAVKKPY---------TLVNNYGPTENTVVAT-----SAEIHPEEGSLsIGRAIANT 1365
Cdd:cd17643 201 AADRDGRDPLALRYVIFGGEALEAAMLRPWagrfgldrpQLVNMYGITETTVHVTfrpldAADLPAAAASP-IGRPLPGL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1366 RVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFV-PGERMYRTGDLVKWV-NGGIEYIGRIDQQVK 1443
Cdd:cd17643 280 RVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGgPGSRMYRTGDLARRLpDGELEYLGRADEQVK 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1444 VRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE---TADIEALKSTLKETLPDYMIPAFWVTLNELPV 1520
Cdd:cd17643 360 IRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADdgaAADIAELRALLKELLPDYMVPARYVPLDALPL 439
|
490
....*....|.
gi 2214269206 1521 TANGKVDRKAL 1531
Cdd:cd17643 440 TVNGKLDRAAL 450
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1079-1469 |
9.83e-145 |
|
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: 455.96 E-value: 9.83e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1079 TYGELNAKANRLARILMD-CGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKQE 1157
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1158 GISVPDSYTGDVILLDGSRTILSLPlDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMT 1237
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALD-DAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1238 AEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYF-ETNGVTITFLPTQLAEQFMELENT---SLRV 1313
Cdd:TIGR01733 160 PDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLAAALPPalaSLRL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1314 LLTGGDKLK-------RAVKKPYTLVNNYGPTENTVVATSAEIHP----EEGSLSIGRAIANTRVYILGEGNQVQPEGVA 1382
Cdd:TIGR01733 240 VILGGEALTpalvdrwRARGPGARLINLYGPTETTVWSTATLVDPddapRESPVPIGRPLANTRLYVLDDDLRPVPVGVV 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1383 GELCVAGRGLARGYLNREDETAKRFVADPFVP--GERMYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLA 1459
Cdd:TIGR01733 320 GELYIGGPGVARGYLNRPELTAERFVPDPFAGgdGARLYRTGDLVRYlPDGNLEFLGRIDDQVKIRGYRIELGEIEAALL 399
|
410
....*....|
gi 2214269206 1460 QLSEVQDAAV 1469
Cdd:TIGR01733 400 RHPGVREAVV 409
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
12-502 |
1.28e-144 |
|
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: 458.05 E-value: 1.28e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 12 LFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDT 91
Cdd:cd17644 5 LFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 92 PEERIRYSLEDSGAKFAVVNERNmtaigqyegiivslddgkwrneskerpssisgsrnLAYVIYTSGTTGKPKGVQIEHR 171
Cdd:cd17644 85 PQERLTYILEDAQISVLLTQPEN-----------------------------------LAYVIYTSGSTGKPKGVMIEHQ 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 172 NLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFH 251
Cdd:cd17644 130 SLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWH 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 252 TIVNTASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGH-TEFINHYGPTEATIGAIAGRVDLYEpDAFAKRPTIGRP 330
Cdd:cd17644 210 LLVLELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVGNfIQLINVYGPTEATIAATVCRLTQLT-ERNITSVPIGRP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 331 IANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPY--SPGSLMYKTGDVVRRLSDGTLAFIGRA 408
Cdd:cd17644 289 IANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnsSESERLYKTGDLARYLPDGNIEYLGRI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 409 DDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLA-VSEGGLQELCAYYT--SDQDIEKAELRYQLSLTLPSHMIPAFFVQV 485
Cdd:cd17644 369 DNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVrEDQPGNKRLVAYIVphYEESPSTVELRQFLKAKLPDYMIPSAFVVL 448
|
490
....*....|....*..
gi 2214269206 486 DAIPLTANGKTDRNALP 502
Cdd:cd17644 449 EELPLTPNGKIDRRALP 465
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
12-595 |
1.76e-144 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 503.34 E-value: 1.76e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 12 LFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDT 91
Cdd:PRK12316 4556 LVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEY 4635
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 92 PEERIRYSLEDSGAKFAVVNERNMTAIGQYEGI-IVSLD-DGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIE 169
Cdd:PRK12316 4636 PRERLAYMMEDSGAALLLTQSHLLQRLPIPDGLaSLALDrDEDWEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVS 4715
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 170 HRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIvQKETYTAPDEIAHYIKEHGITYIKLTPSL 249
Cdd:PRK12316 4716 HGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVI-RDDSLWDPERLYAEIHEHRVTVLVFPPVY 4794
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 250 FHTIVNTAsfAKDANFESLRLIVLGGEKIIPTDV-IAFRKMYgHTEFINHYGPTEATIGAIAGRVDLYEPDAFAKRPtIG 328
Cdd:PRK12316 4795 LQQLAEHA--ERDGEPPSLRVYCFGGEAVAQASYdLAWRALK-PVYLFNGYGPTETTVTVLLWKARDGDACGAAYMP-IG 4870
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 329 RPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPY-SPGSLMYKTGDVVRRLSDGTLAFIGR 407
Cdd:PRK12316 4871 TPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGR 4950
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 408 ADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYT------SDQDIEKAELRYQ----LSLTLPSHM 477
Cdd:PRK12316 4951 VDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVpqdpalADADEAQAELRDElkaaLRERLPEYM 5030
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 478 IPAFFVQVDAIPLTANGKTDRNALPKPNAAQSgGKALAAPETALEESLCRIWQKTLGIEAIGIDDNFFDLGGHSLKGMML 557
Cdd:PRK12316 5031 VPAHLVFLARMPLTPNGKLDRKALPQPDASLL-QQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQV 5109
|
570 580 590
....*....|....*....|....*....|....*...
gi 2214269206 558 IANIQAELEKSVPLKALFEQPTvrqLAAYMEASAVSGG 595
Cdd:PRK12316 5110 TSRIQLELGLELPLRELFQTPT---LAAFVELAAAAGS 5144
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
20-502 |
1.74e-142 |
|
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: 452.31 E-value: 1.74e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 20 TPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYS 99
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 100 LEDSGAKFaVVNERNMTAIGQYEGIIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSW 179
Cdd:cd17656 81 MLDSGVRV-VLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 180 FSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASF 259
Cdd:cd17656 160 EREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 260 AKDAnFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIgAIAGRVDlyEPDAFAKRPTIGRPIANAGALVL 339
Cdd:cd17656 240 INRF-PTCVKHIITAGEQLVITNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTIN--PEAEIPELPPIGKPISNTWIYIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 340 NEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRI 419
Cdd:cd17656 316 DQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 420 EPKEIETVMLSLSGIQEAVVLAVSE-GGLQELCAYYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDR 498
Cdd:cd17656 396 ELGEIEAQLLNHPGVSEAVVLDKADdKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDR 475
|
....
gi 2214269206 499 NALP 502
Cdd:cd17656 476 KALP 479
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
12-502 |
2.19e-142 |
|
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: 450.47 E-value: 2.19e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 12 LFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDT 91
Cdd:cd17645 3 LFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 92 PEERIRYSLEDSGAKFAvvnernmtaigqyegiivslddgkwrneskerpssISGSRNLAYVIYTSGTTGKPKGVQIEHR 171
Cdd:cd17645 83 PGERIAYMLADSSAKIL-----------------------------------LTNPDDLAYVIYTSGSTGLPKGVMIEHH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 172 NLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITyIKLTPS--- 248
Cdd:cd17645 128 NLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT-ISFLPTgaa 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 249 -LFHTIVNTasfakdanfeSLRLIVLGGEKIiptdVIAFRKMYghtEFINHYGPTEATIGAIAGRVDLYEPDAfakrpTI 327
Cdd:cd17645 207 eQFMQLDNQ----------SLRVLLTGGDKL----KKIERKGY---KLVNNYGPTENTVVATSFEIDKPYANI-----PI 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 328 GRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGR 407
Cdd:cd17645 265 GKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 408 ADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSE-GGLQELCAYYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVD 486
Cdd:cd17645 345 LDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDaDGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLK 424
|
490
....*....|....*.
gi 2214269206 487 AIPLTANGKTDRNALP 502
Cdd:cd17645 425 ALPLTANGKVDRKALP 440
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
21-502 |
4.26e-142 |
|
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: 450.28 E-value: 4.26e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 21 PDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSL 100
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 101 EDSGAKfavvnernmTAIGQyegiivslddgkwrneskerpssisGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWF 180
Cdd:cd17649 81 EDSGAG---------LLLTH-------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 181 SEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFA 260
Cdd:cd17649 127 AERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 261 KDANFESLRLIVLGGEKIIPTDVIAFRKmyGHTEFINHYGPTEATIGAIAGRVDLYEPDAFAKRPtIGRPIANAGALVLN 340
Cdd:cd17649 207 GDGRPPSLRLYIFGGEALSPELLRRWLK--APVRLFNAYGPTEATVTPLVWKCEAGAARAGASMP-IGRPLGGRSAYILD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 341 EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYS-PGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRI 419
Cdd:cd17649 284 ADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGaPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 420 EPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYTSDQDIE----KAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:cd17649 364 ELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAqpelRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGK 443
|
....*..
gi 2214269206 496 TDRNALP 502
Cdd:cd17649 444 LDRKALP 450
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1628-2077 |
7.36e-141 |
|
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: 446.78 E-value: 7.36e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1628 VEGEVILTPIQ--RWFFEKNFTNKHHWNQSVMLHAKKGFDPERVEKTLQALIEHHDALRMVY-REENGDIVQVYKPigES 1704
Cdd:pfam00668 1 VQDEYPLSPAQkrMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFiRQENGEPVQVILE--ER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1705 KVSFEIVDLYGSDEEMLRSQIKLLANK-LQSSLDLRNGPLLKAEQYR-TEAGDHLLIAVHHLVVDGVSWRILLEDFASGY 1782
Cdd:pfam00668 79 PFELEIIDISDLSESEEEEAIEAFIQRdLQSPFDLEKGPLFRAGLFRiAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1783 MQAEKEESLVFPQKTnSFKDWAEELAAFSQSAHLLQQAEYWSQIAA--EQVSPLPKD-CETEQRIVK-DTSSVLCEltaE 1858
Cdd:pfam00668 159 QQLLKGEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEgeLPVLQLPKDyARPADRSFKgDRLSFTLD---E 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1859 DTKHLLTDVHQPYGTEINDILLSALGLTMKEWTKGAKIGINLEGHGRediiPNVNISRTVGWFTAQYPVVLDISDADA-S 1937
Cdd:pfam00668 235 DTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR----PSPDIERMVGMFVNTLPLRIDPKGGKTfS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1938 AVIKTVKENLRRI-PDKGVGYGILRYFTETAETKG----FTPEISF-NYLGQfdsEVKTDFFEPSAFDMGRQVSGESEAL 2011
Cdd:pfam00668 311 ELIKRVQEDLLSAePHQGYPFGDLVNDLRLPRDLSrhplFDPMFSFqNYLGQ---DSQEEEFQLSELDLSVSSVIEEEAK 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 2012 YALSFSGMIRNGRFVLSCSYNEKEFERATVEEQMERFKENLLMLIRHCTEKEDKEFTPSDFSAEDL 2077
Cdd:pfam00668 388 YDLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKL 453
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1067-1532 |
9.09e-141 |
|
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: 447.69 E-value: 9.09e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:cd17656 3 DAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLKQEGISVPDSYTGDVILLDGSRtilslpLDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNL 1226
Cdd:cd17656 83 DSGVRVVLTQRHLKSKLSFNKSTILLEDPS------ISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1227 CFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTITFLPTQLAEQFMEL 1306
Cdd:cd17656 157 LHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSE 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1307 EN------TSLRVLLTGGDKL-------KRAVKKPYTLVNNYGPTENTVVaTSAEIHPE-EGSL--SIGRAIANTRVYIL 1370
Cdd:cd17656 237 REfinrfpTCVKHIITAGEQLvitnefkEMLHEHNVHLHNHYGPSETHVV-TTYTINPEaEIPElpPIGKPISNTWIYIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1371 GEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKWV-NGGIEYIGRIDQQVKVRGYRI 1449
Cdd:cd17656 316 DQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLpDGNIEFLGRADHQVKIRGYRI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1450 ELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE-TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDR 1528
Cdd:cd17656 396 ELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEqELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDR 475
|
....
gi 2214269206 1529 KALP 1532
Cdd:cd17656 476 KALP 479
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1053-1532 |
2.55e-138 |
|
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: 440.33 E-value: 2.55e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1053 TVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPI 1132
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1133 DPDYPDQRIEYILQDSGAKLLLKQEgisvpdsytgdvilldgsrtilslpldendegnpetavtaENLAYMIYTSGTTGQ 1212
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLTQP----------------------------------------ENLAYVIYTSGSTGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1213 PKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTI 1292
Cdd:cd17644 121 PKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1293 -TFLPTQLAEQFMELENT------SLRVLLTGGDK--------LKRAVKKPYTLVNNYGPTENTVVATSAEI----HPEE 1353
Cdd:cd17644 201 lSLPPAYWHLLVLELLLStidlpsSLRLVIVGGEAvqpelvrqWQKNVGNFIQLINVYGPTEATIAATVCRLtqltERNI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1354 GSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFV--PGERMYRTGDLVKWV-NG 1430
Cdd:cd17644 281 TSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLpDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1431 GIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE---TADIEALKSTLKETLPDYM 1507
Cdd:cd17644 361 NIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHyeeSPSTVELRQFLKAKLPDYM 440
|
490 500
....*....|....*....|....*
gi 2214269206 1508 IPAFWVTLNELPVTANGKVDRKALP 1532
Cdd:cd17644 441 IPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1054-1531 |
1.15e-133 |
|
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: 427.73 E-value: 1.15e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1054 VHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPID 1133
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1134 PDYPDQRIEYILQDSGAKLLLkqegISVPDsytgdvilldgsrtilslpldendegnpetavtaeNLAYMIYTSGTTGQP 1213
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVL----TSSPS-----------------------------------DAAYVIFTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1214 KGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDivRLNDYFETNGVTIT 1293
Cdd:cd05918 122 KGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWA 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1294 FLPTQLAEQFMELENTSLRVLLTGGDKLKRAVKKPY----TLVNNYGPTENTVVATSAEIHPEEGSLSIGRAIAnTRVYI 1369
Cdd:cd05918 200 FLTPSVARLLDPEDVPSLRTLVLGGEALTQSDVDTWadrvRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLG-ATCWV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1370 LGEGNQVQ--PEGVAGELCVAGRGLARGYLNREDETAKRFVADP-------FVPGERMYRTGDLVKW-VNGGIEYIGRID 1439
Cdd:cd05918 279 VDPDNHDRlvPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYnPDGSLEYVGRKD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1440 QQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAV---KDKGGNTAIAAYVTPETAD--------------------IEALK 1496
Cdd:cd05918 359 TQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkpKDGSSSPQLVAFVVLDGSSsgsgdgdslflepsdefralVAELR 438
|
490 500 510
....*....|....*....|....*....|....*
gi 2214269206 1497 STLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05918 439 SKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
12-501 |
3.31e-132 |
|
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: 422.11 E-value: 3.31e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 12 LFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDT 91
Cdd:cd12115 4 LVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 92 PEERIRYSLEDSGAKFAVVnernmtaigqyegiivslddgkwrneskerpssisGSRNLAYVIYTSGTTGKPKGVQIEHR 171
Cdd:cd12115 84 PPERLRFILEDAQARLVLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVAIEHR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 172 NLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQkETYTAPDEIAHyikeHGITYIKLTPSlfh 251
Cdd:cd12115 129 NAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD-NVLALPDLPAA----AEVTLINTVPS--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 252 tiVNTASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVdlyePDAFAKRPTIGRPI 331
Cdd:cd12115 201 --AAAELLRHDALPASVRVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPV----PPGASGEVSIGRPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 332 ANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQ 411
Cdd:cd12115 275 ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 412 VKIRGYRIEPKEIETVMLSLSGIQEAVVLA-VSEGGLQELCAYYTSDQD--IEKAELRYQLSLTLPSHMIPAFFVQVDAI 488
Cdd:cd12115 355 VKVRGFRIELGEIEAALRSIPGVREAVVVAiGDAAGERRLVAYIVAEPGaaGLVEDLRRHLGTRLPAYMVPSRFVRLDAL 434
|
490
....*....|...
gi 2214269206 489 PLTANGKTDRNAL 501
Cdd:cd12115 435 PLTPNGKIDRSAL 447
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1054-1531 |
6.83e-132 |
|
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: 421.34 E-value: 6.83e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1054 VHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPID 1133
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1134 PDYPDQRIEYILQDSGAKLLLkqegisvpdsytgdvilldgsrtilslpldendegnpetaVTAENLAYMIYTSGTTGQP 1213
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVL----------------------------------------TDPDDLAYVIYTSGSTGRP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1214 KGVMVEHHALVNLCFWHHDAFSmtAEDRSAKYAG--FGFDASIWEMFPTWTIGAELHVIDEAIRLDivrlnDYFETNGVT 1291
Cdd:cd12115 121 KGVAIEHRNAAAFLQWAAAAFS--AEELAGVLAStsICFDLSVFELFGPLATGGKVVLADNVLALP-----DLPAAAEVT 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1292 -ITFLPTqLAEQFMELEN--TSLRVLLTGGDKLKRA-VKKPYT------LVNNYGPTENTVVATSAEIHPE-EGSLSIGR 1360
Cdd:cd12115 194 lINTVPS-AAAELLRHDAlpASVRVVNLAGEPLPRDlVQRLYArlqverVVNLYGPSEDTTYSTVAPVPPGaSGEVSIGR 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1361 AIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKWV-NGGIEYIGRID 1439
Cdd:cd12115 273 PLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRpDGLLEFLGRAD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1440 QQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPETA---DIEALKSTLKETLPDYMIPAFWVTLN 1516
Cdd:cd12115 353 NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGaagLVEDLRRHLGTRLPAYMVPSRFVRLD 432
|
490
....*....|....*
gi 2214269206 1517 ELPVTANGKVDRKAL 1531
Cdd:cd12115 433 ALPLTPNGKIDRSAL 447
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
21-501 |
1.92e-129 |
|
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: 414.56 E-value: 1.92e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 21 PDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSL 100
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 101 EDSGAKFAVVNernmtaigqyegiivslddgkwrneskerPSsisgsrNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWF 180
Cdd:cd17650 81 EDSGAKLLLTQ-----------------------------PE------DLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 181 SEEAGLTENDKTVL-LSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASF 259
Cdd:cd17650 126 RREYELDSFPVRLLqMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 260 AKdANFESLRLIVLGGEKIIPTD-VIAFRKMYGHTEFINHYGPTEATIGAIAGRVDLYEPDAFAKRPtIGRPIANAGALV 338
Cdd:cd17650 206 NG-LDLSAMRLLIVGSDGCKAQDfKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVP-IGRPLPNTAMYV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 339 LNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYR 418
Cdd:cd17650 284 LDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFR 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 419 IEPKEIETVMLSLSGIQEAVVlAVSE--GGLQELCAYYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKT 496
Cdd:cd17650 364 IELGEIESQLARHPAIDEAVV-AVREdkGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKV 442
|
....*
gi 2214269206 497 DRNAL 501
Cdd:cd17650 443 DRRAL 447
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1056-1531 |
1.06e-128 |
|
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: 411.70 E-value: 1.06e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1056 QLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPD 1135
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1136 YPDQRIEYILQDSGAKLLLkqegisvpdsytgdvilldgsrtilslpldendegnpeTAVTAENLAYMIYTSGTTGQPKG 1215
Cdd:cd17653 81 LPSARIQAILRTSGATLLL--------------------------------------TTDSPDDLAYIIFTSGSTGIPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1216 VMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEairldivrlNDYFETNGVTITFL 1295
Cdd:cd17653 123 VMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADP---------SDPFAHVARTVDAL 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1296 ---PTQLAEqfmeLENT---SLRVLLTGGD----KLKRAVKKPYTLVNNYGPTENTVVATSAEIHPEEgSLSIGRAIANT 1365
Cdd:cd17653 194 mstPSILST----LSPQdfpNLKTIFLGGEavppSLLDRWSPGRRLYNAYGPTECTISSTMTELLPGQ-PVTIGKPIPNS 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1366 RVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKWV-NGGIEYIGRIDQQVKV 1444
Cdd:cd17653 269 TCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTeDGGLEFLGREDNQVKV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1445 RGYRIELSEIE-VQLAQLSEVQDAAVTAVKDkggntAIAAYVTPETADIEALKSTLKETLPDYMIPAFWVTLNELPVTAN 1523
Cdd:cd17653 349 RGFRINLEEIEeVVLQSQPEVTQAAAIVVNG-----RLVAFVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTAN 423
|
....*...
gi 2214269206 1524 GKVDRKAL 1531
Cdd:cd17653 424 GKVDRKAL 431
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
21-502 |
3.55e-128 |
|
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: 411.02 E-value: 3.55e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 21 PDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGN-EDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYS 99
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 100 LEDSGAKfaVVnernmtaigqyegiivslddgkwrneskerpssISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSW 179
Cdd:cd17648 81 LEDTGAR--VV---------------------------------ITNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 180 FSEEAGLTENDKTVLL--SSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIvnta 257
Cdd:cd17648 126 LSERYFGRDNGDEAVLffSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY---- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 258 SFAKdanFESLRLIVLGGEKIIPTdviAFRKMYGhtEF----INHYGPTEATIGAIagrVDLYEPDAfAKRPTIGRPIAN 333
Cdd:cd17648 202 DLAR---LPHLKRVDAAGEEFTAP---VFEKLRS--RFagliINAYGPTETTVTNH---KRFFPGDQ-RFDKSLGRPVRN 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 334 AGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPY--------SPGSLMYKTGDVVRRLSDGTLAFI 405
Cdd:cd17648 270 TKCYVLNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqteqerarGRNARLYKTGDLVRWLPSGELEYL 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 406 GRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLA------VSEGGLQELCAYYTSDQD-IEKAELRYQLSLTLPSHMI 478
Cdd:cd17648 350 GRNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVAkedasqAQSRIQKYLVGYYLPEPGhVPESDLLSFLRAKLPRYMV 429
|
490 500
....*....|....*....|....
gi 2214269206 479 PAFFVQVDAIPLTANGKTDRNALP 502
Cdd:cd17648 430 PARLVRLEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
12-501 |
5.23e-127 |
|
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: 408.85 E-value: 5.23e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 12 LFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDT 91
Cdd:cd05918 4 LIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSH 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 92 PEERIRYSLEDSGAKFAVVnernmtaigqyegiivslddgkwrneskerpSSISgsrNLAYVIYTSGTTGKPKGVQIEHR 171
Cdd:cd05918 84 PLQRLQEILQDTGAKVVLT-------------------------------SSPS---DAAYVIFTSGSTGKPKGVVIEHR 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 172 NLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIvqketytAPDE-----IAHYIKEHGITYIKLT 246
Cdd:cd05918 130 ALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI-------PSEEdrlndLAGFINRLRVTWAFLT 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 247 PSLFHTIvntasfaKDANFESLRLIVLGGEKIIPTDViafRKMYGHTEFINHYGPTEATIGAIAGrvdlyEPDAFAKRPT 326
Cdd:cd05918 203 PSVARLL-------DPEDVPSLRTLVLGGEALTQSDV---DTWADRVRLINAYGPAECTIAATVS-----PVVPSTDPRN 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 327 IGRPIAnAGALVLNEA--LKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPY-------SPGSLMYKTGDVVRRL 397
Cdd:cd05918 268 IGRPLG-ATCWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegsGRGRRLYRTGDLVRYN 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 398 SDGTLAFIGRADDQVKIRGYRIEPKEIE-TVMLSLSGIQEAVVLAVSEGGLQE---LCAYYTSDQDIEK----------- 462
Cdd:cd05918 347 PDGSLEYVGRKDTQVKIRGQRVELGEIEhHLRQSLPGAKEVVVEVVKPKDGSSspqLVAFVVLDGSSSGsgdgdslflep 426
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2214269206 463 --------AELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd05918 427 sdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1067-1531 |
3.59e-125 |
|
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: 402.23 E-value: 3.59e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:cd17650 2 DAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLKQegisvpdsytgdvilldgsrtilslpldendegnpetavtAENLAYMIYTSGTTGQPKGVMVEHHALVNL 1226
Cdd:cd17650 82 DSGAKLLLTQ----------------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1227 CF-----WHHDAFSMtaedRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTI-TFLPTqLA 1300
Cdd:cd17650 122 AHawrreYELDSFPV----RLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLmESTPA-LI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1301 EQFME------LENTSLRVLLTGGDKLKRAVKKPYT--------LVNNYGPTENTVVAT----SAEIHPEEGSLSIGRAI 1362
Cdd:cd17650 197 RPVMAyvyrngLDLSAMRLLIVGSDGCKAQDFKTLAarfgqgmrIINSYGVTEATIDSTyyeeGRDPLGDSANVPIGRPL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1363 ANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKWV-NGGIEYIGRIDQQ 1441
Cdd:cd17650 277 PNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRaDGNVELLGRVDHQ 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1442 VKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP-ETADIEALKSTLKETLPDYMIPAFWVTLNELPV 1520
Cdd:cd17650 357 VKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAaATLNTAELRAFLAKELPSYMIPSYYVQLDALPL 436
|
490
....*....|.
gi 2214269206 1521 TANGKVDRKAL 1531
Cdd:cd17650 437 TPNGKVDRRAL 447
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
609-1019 |
7.03e-124 |
|
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: 397.95 E-value: 7.03e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 609 PLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRII--EKAEVDLHV 686
Cdd:cd19540 3 PLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLpaAEARPDLTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 687 FEAKEDEADQKIKEFI-RPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLY----KGE--QLPE 759
Cdd:cd19540 83 VDVTEDELAARLAEAArRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAGRapDWAP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 760 PTLHYKDFAVWQ-----NEAEQKERMKEHEAYWMSVLSGeLPE-LDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLL 833
Cdd:cd19540 163 LPVQYADYALWQrellgDEDDPDSLAARQLAYWRETLAG-LPEeLELPTDRPRPAVASYRGGTVEFTIDAELHARLAALA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 834 AETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSAL 913
Cdd:cd19540 242 REHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAF 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 914 EHQEYPFEDLVNQLDLPRDMSRNPLFNVMVTTENPDKEQLTLQNLSISPYEAHQGTSKFDLTL------GGFTDENGIGL 987
Cdd:cd19540 322 AHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFtlterrDADGAPAGLTG 401
|
410 420 430
....*....|....*....|....*....|..
gi 2214269206 988 QLEYATDLFAKETAEKWSEYVLRLLKAVADNP 1019
Cdd:cd19540 402 ELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
21-501 |
8.50e-122 |
|
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: 393.95 E-value: 8.50e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 21 PDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSL 100
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 101 EDSGAKFAVVNErnMTAIGQYEGIIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWF 180
Cdd:cd12114 81 ADAGARLVLTDG--PDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 181 SEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFA 260
Cdd:cd12114 159 NRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 261 KDANfESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDLYEPDafakRPTI--GRPIANAGALV 338
Cdd:cd12114 239 QALL-PSLRLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIWSIYHPIDEVPPD----WRSIpyGRPLANQRYRV 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 339 LNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPysPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYR 418
Cdd:cd12114 314 LDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYR 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 419 IEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYTSDQD---IEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:cd12114 392 IELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDgtpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGK 471
|
....*.
gi 2214269206 496 TDRNAL 501
Cdd:cd12114 472 VDRAAL 477
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1067-1531 |
1.07e-120 |
|
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: 390.48 E-value: 1.07e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:cd12114 2 DATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLKQEGISVPDSYTGDVILLDGSRTILSLPldendegNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNL 1226
Cdd:cd12114 82 DAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAP-------PPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1227 CFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTI-TFLPTQL------ 1299
Cdd:cd12114 155 ILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLwNSVPALLemlldv 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1300 AEQFMELeNTSLRVLLTGGD--------KLKRAVKKPyTLVNNYGPTENTVVATSAEIHPEEGSL-SI--GRAIANTRVY 1368
Cdd:cd12114 235 LEAAQAL-LPSLRLVLLSGDwipldlpaRLRALAPDA-RLISLGGATEASIWSIYHPIDEVPPDWrSIpyGRPLANQRYR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1369 ILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPfvPGERMYRTGDLVK-WVNGGIEYIGRIDQQVKVRGY 1447
Cdd:cd12114 313 VLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRyRPDGTLEFLGRRDGQVKVRGY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1448 RIELSEIEVQLAQLSEVQDAAVTAVKDKGGnTAIAAYVTPE----TADIEALKSTLKETLPDYMIPAFWVTLNELPVTAN 1523
Cdd:cd12114 391 RIELGEIEAALQAHPGVARAVVVVLGDPGG-KRLAAFVVPDndgtPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTAN 469
|
....*...
gi 2214269206 1524 GKVDRKAL 1531
Cdd:cd12114 470 GKVDRAAL 477
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
12-501 |
2.23e-118 |
|
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: 382.43 E-value: 2.23e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 12 LFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDT 91
Cdd:cd17653 2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 92 PEERIRYSLEDSGAKFAVVNernmtaigqyegiivslddgkwrneskerpssiSGSRNLAYVIYTSGTTGKPKGVQIEHR 171
Cdd:cd17653 82 PSARIQAILRTSGATLLLTT---------------------------------DSPDDLAYIIFTSGSTGIPKGVMVPHR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 172 NLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVqketyTAPDEIAHYIKEhgITYIKLTPSLFH 251
Cdd:cd17653 129 GVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLA-----DPSDPFAHVART--VDALMSTPSILS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 252 TIvntasfaKDANFESLRLIVLGGEKIIPTDViafRKMYGHTEFINHYGPTEATIGAIAGRVdlyEPDafaKRPTIGRPI 331
Cdd:cd17653 202 TL-------SPQDFPNLKTIFLGGEAVPPSLL---DRWSPGRRLYNAYGPTECTISSTMTEL---LPG---QPVTIGKPI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 332 ANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQ 411
Cdd:cd17653 266 PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 412 VKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGglqELCAYYTSdQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLT 491
Cdd:cd17653 346 VKVRGFRINLEEIEEVVLQSQPEVTQAAAIVVNG---RLVAFVTP-ETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLT 421
|
490
....*....|
gi 2214269206 492 ANGKTDRNAL 501
Cdd:cd17653 422 ANGKVDRKAL 431
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
13-415 |
2.64e-116 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 375.50 E-value: 2.64e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 13 FEKQAQQTPDHSAV-KAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDT 91
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 92 PEERIRYSLEDSGAKFAVVNERNM-------TAIGQYEGIIVSLDDGKWRNE-----------SKERPSSISGSRNLAYV 153
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKleelleaLGKLEVVKLVLVLDRDPVLKEeplpeeakpadVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 154 IYTSGTTGKPKGVQIEHRNLTNYVSWFSEEA----GLTENDKTVLLSSYAFDLGYTS-MFPVLLGGGELHIVQKETYTAP 228
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 229 DEIAHYIKEHGITYIKLTPSLFHTIVNtASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHtEFINHYGPTEATIGA 308
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLE-AGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG-ALVNGYGLTETTGVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 309 IagrVDLYEPDAFAKRPTIGRPIANAGALVLNEA-LKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPyspgslM 387
Cdd:pfam00501 319 T---TPLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDG------W 389
|
410 420
....*....|....*....|....*...
gi 2214269206 388 YKTGDVVRRLSDGTLAFIGRADDQVKIR 415
Cdd:pfam00501 390 YRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1062-1531 |
1.55e-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: 368.88 E-value: 1.55e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1062 VQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRI 1141
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1142 EYILQDSGAKLLlkqegISVPDSytgdvilldgsrtilslpldendegnpetavtaenLAYMIYTSGTTGQPKGVMVEHH 1221
Cdd:cd05945 81 REILDAAKPALL-----IADGDD-----------------------------------NAYIIFTSGSTGRPKGVQISHD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1222 ALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTI-----TFLP 1296
Cdd:cd05945 121 NLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVwvstpSFAA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1297 TQLAEQ-FMELENTSLR-VLLTGGDKLKRAVKK------PYTLVNNYGPTENTVVATSAEIHPE----EGSLSIGRAIAN 1364
Cdd:cd05945 201 MCLLSPtFTPESLPSLRhFLFCGEVLPHKTARAlqqrfpDARIYNTYGPTEATVAVTYIEVTPEvldgYDRLPIGYAKPG 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1365 TRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADpfvPGERMYRTGDLVKWVNGG-IEYIGRIDQQVK 1443
Cdd:cd05945 281 AKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPD---EGQRAYRTGDLVRLEADGlLFYRGRLDFQVK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1444 VRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPETADIE----ALKSTLKETLPDYMIPAFWVTLNELP 1519
Cdd:cd05945 358 LNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAgltkAIKAELAERLPPYMIPRRFVYLDELP 437
|
490
....*....|..
gi 2214269206 1520 VTANGKVDRKAL 1531
Cdd:cd05945 438 LNANGKIDRKAL 449
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1067-1532 |
1.15e-112 |
|
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: 366.73 E-value: 1.15e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCG-ISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYIL 1145
Cdd:cd17648 2 DRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1146 QDSGAKLLLkqegisvpdsytgdvilldgsrtilslpldendegnpetaVTAENLAYMIYTSGTTGQPKGVMVEHHALVN 1225
Cdd:cd17648 82 EDTGARVVI----------------------------------------TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVN 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1226 LCFWHHDAFSMTAEDRSA--KYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVT-ITFLPTQLaeQ 1302
Cdd:cd17648 122 LRTSLSERYFGRDNGDEAvlFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTyLSGTPSVL--Q 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1303 FMELEN-TSLRVLLTGG--------DKLKRAVKKPytLVNNYGPTENTVVATsaeIHPEEGS----LSIGRAIANTRVYI 1369
Cdd:cd17648 200 QYDLARlPHLKRVDAAGeeftapvfEKLRSRFAGL--IINAYGPTETTVTNH---KRFFPGDqrfdKSLGRPVRNTKCYV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1370 LGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPF-VPGE-------RMYRTGDLVKWV-NGGIEYIGRIDQ 1440
Cdd:cd17648 275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFqTEQErargrnaRLYKTGDLVRWLpSGELEYLGRNDF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1441 QVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTA-----IAAYVTPETADIEA--LKSTLKETLPDYMIPAFWV 1513
Cdd:cd17648 355 QVKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEPGHVPEsdLLSFLRAKLPRYMVPARLV 434
|
490
....*....|....*....
gi 2214269206 1514 TLNELPVTANGKVDRKALP 1532
Cdd:cd17648 435 RLEGIPVTINGKLDVRALP 453
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
609-1019 |
8.17e-112 |
|
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: 363.51 E-value: 8.17e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 609 PLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIE--KAEVDLHV 686
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEedEATPKLEI 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 687 FEAKEDEADQKIKEFIR-PFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYK---GEQLPEPT- 761
Cdd:cd19538 83 KEVDEEELESEINEAVRyPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRarcKGEAPELAp 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 762 --LHYKDFAVWQ-----NEAEQKERMKEHEAYWMSVLSGeLP-ELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLL 833
Cdd:cd19538 163 lpVQYADYALWQqellgDESDPDSLIARQLAYWKKQLAG-LPdEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 834 AETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSAL 913
Cdd:cd19538 242 KDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 914 EHQEYPFEDLVNQLDLPRDMSRNPLFNVMVTTENPDKEQLTLQNLSISPYEAHQGTSKFDLTLG---GFTDE--NGIGLQ 988
Cdd:cd19538 322 EHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFElreQYNDGtpNGIEGF 401
|
410 420 430
....*....|....*....|....*....|.
gi 2214269206 989 LEYATDLFAKETAEKWSEYVLRLLKAVADNP 1019
Cdd:cd19538 402 IEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1058-1445 |
1.32e-110 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 359.32 E-value: 1.32e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1058 FEETVQRHKDRPAV-TYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDY 1136
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1137 PDQRIEYILQDSGAKLLLKQEGISVP--------DSYTGDVILLDGSRTILSLPLDENDEGN-----PETAVTAENLAYM 1203
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEellealgkLEVVKLVLVLDRDPVLKEEPLPEEAKPAdvpppPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1204 IYTSGTTGQPKGVMVEHHALVNLCFWH----HDAFSMTAEDRSAKYAGFGFDAS-IWEMFPTWTIGAELHVIDEAIRLDI 1278
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1279 VRLNDYFETNGVTITFLPTQLAEQFMELEN------TSLRVLLTGGDKLKRAVKKPY------TLVNNYGPTENTVVATS 1346
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGApkrallSSLRLVLSGGAPLPPELARRFrelfggALVNGYGLTETTGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1347 AEIHPEEGSL--SIGRAIANTRVYILG-EGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADpfvpgeRMYRTGD 1423
Cdd:pfam00501 321 PLPLDEDLRSlgSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED------GWYRTGD 394
|
410 420
....*....|....*....|...
gi 2214269206 1424 LVKWV-NGGIEYIGRIDQQVKVR 1445
Cdd:pfam00501 395 LGRRDeDGYLEIVGRKKDQIKLG 417
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
17-501 |
3.31e-110 |
|
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: 359.25 E-value: 3.31e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 17 AQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERI 96
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 97 RYSLEDSGAKfavvnernmtaigqyeGIIVSLDDgkwrneskerpssisgsrnLAYVIYTSGTTGKPKGVQIEHRNLTNY 176
Cdd:cd05945 81 REILDAAKPA----------------LLIADGDD-------------------NAYIIFTSGSTGRPKGVQISHDNLVSF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 177 VSWFSEEAGLTENDktVLLS--SYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIV 254
Cdd:cd05945 126 TNWMLSDFPLGPGD--VFLNqaPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMCL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 255 NTASFAKdANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDlYEPDAFAKRPTIGRPIANA 334
Cdd:cd05945 204 LSPTFTP-ESLPSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVT-PEVLDGYDRLPIGYAKPGA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 335 GALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPyspGSLMYKTGDVVRRLSDGTLAFIGRADDQVKI 414
Cdd:cd05945 282 KLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQVKL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 415 RGYRIEPKEIETVMLSLSGIQEAVVLAVSEG-GLQELCAYYTSDQDIEKA---ELRYQLSLTLPSHMIPAFFVQVDAIPL 490
Cdd:cd05945 359 NGYRIELEEIEAALRQVPGVKEAVVVPKYKGeKVTELIAFVVPKPGAEAGltkAIKAELAERLPPYMIPRRFVYLDELPL 438
|
490
....*....|.
gi 2214269206 491 TANGKTDRNAL 501
Cdd:cd05945 439 NANGKIDRKAL 449
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
9-501 |
2.24e-109 |
|
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: 357.20 E-value: 2.24e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 9 FAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPID 88
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 89 PDTPEERIRYSLEDSGAKFAVVnernmtaigqyegiivslddgkwrneskerpssisgsrnlAYVIYTSGTTGKPKGVQI 168
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVML 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 169 EHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYT-SMFPVLLGGGELHIVQKetyTAPDEIAHYIKEHGITYIKLTP 247
Cdd:COG0318 121 THRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTvGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 248 SLFHTIVNTASFAKdANFESLRLIVLGGEKIIPTDVIAFRKMYGHtEFINHYGPTEATIGAIAGRVDLYEpdafAKRPTI 327
Cdd:COG0318 198 TMLARLLRHPEFAR-YDLSSLRLVVSGGAPLPPELLERFEERFGV-RIVEGYGLTETSPVVTVNPEDPGE----RRPGSV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 328 GRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpyspgslMYKTGDVVRRLSDGTLAFIGR 407
Cdd:COG0318 272 GRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG-------WLRTGDLGRLDEDGYLYIVGR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 408 ADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV-SEGGLQELCAYYT--SDQDIEKAELRYQLSLTLPSHMIPAFFVQ 484
Cdd:COG0318 345 KKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVpDEKWGERVVAFVVlrPGAELDAEELRAFLRERLARYKVPRRVEF 424
|
490
....*....|....*..
gi 2214269206 485 VDAIPLTANGKTDRNAL 501
Cdd:COG0318 425 VDELPRTASGKIDRRAL 441
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1054-1533 |
5.43e-108 |
|
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: 353.35 E-value: 5.43e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1054 VHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPID 1133
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1134 PDYPDQRIEYILQDSGAKLLLkqegisvpdsytgdvilldgsrtilslpldendegnpetavtaenLAYMIYTSGTTGQP 1213
Cdd:COG0318 81 PRLTAEELAYILEDSGARALV---------------------------------------------TALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1214 KGVMVEHHALVNLCFWHHDAFSMTAEDRSAK----YAGFGFdasIWEMFPTWTIGAELHVIDeaiRLDIVRLNDYFETNG 1289
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAALGLTPGDVVLValplFHVFGL---TVGLLAPLLAGATLVLLP---RFDPERVLELIERER 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1290 VTITFL-PTQL-----AEQFMELENTSLRVLLTGGDKLKRAVKKPY------TLVNNYGPTENTVVAT-SAEIHPEEGSL 1356
Cdd:COG0318 190 VTVLFGvPTMLarllrHPEFARYDLSSLRLVVSGGAPLPPELLERFeerfgvRIVEGYGLTETSPVVTvNPEDPGERRPG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1357 SIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFvADPFvpgermYRTGDLVKWVNGG-IEYI 1435
Cdd:COG0318 270 SVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW------LRTGDLGRLDEDGyLYIV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1436 GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP---ETADIEALKSTLKETLPDYMIPAFW 1512
Cdd:COG0318 343 GRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLrpgAELDAEELRAFLRERLARYKVPRRV 422
|
490 500
....*....|....*....|.
gi 2214269206 1513 VTLNELPVTANGKVDRKALPE 1533
Cdd:COG0318 423 EFVDELPRTASGKIDRRALRE 443
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
6-593 |
4.65e-106 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 381.05 E-value: 4.65e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 6 EATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFL 85
Cdd:PRK05691 3719 EQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYL 3798
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 86 PIDPDTPEERIRYSLEDSGAKFAVVN----ERNMTAIGQYEGI----IVSLDDGKWRNESKERPSSISGSRNLAYVIYTS 157
Cdd:PRK05691 3799 PLDPGLPAQRLQRIIELSRTPVLVCSaacrEQARALLDELGCAnrprLLVWEEVQAGEVASHNPGIYSGPDNLAYVIYTS 3878
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 158 GTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVqketytaPDEIAH---- 233
Cdd:PRK05691 3879 GSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIV-------PNAIAHdpqg 3951
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 234 ---YIKEHGITYIKLTPSLFhtivnTASFAKD-ANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAI 309
Cdd:PRK05691 3952 llaHVQAQGITVLESVPSLI-----QGMLAEDrQALDGLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVA 4026
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 310 AGRVDL------YEPdafakrptIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPY-S 382
Cdd:PRK05691 4027 FFRVDLastrgsYLP--------IGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgA 4098
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 383 PGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVlAVSEGGL-QELCAYYT-SDQDI 460
Cdd:PRK05691 4099 PGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV-AVQEGVNgKHLVGYLVpHQTVL 4177
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 461 EKAELRYQ----LSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALPKPNAAQSGGKALAAPETALEESLCRIWQKTLGIE 536
Cdd:PRK05691 4178 AQGALLERikqrLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVE 4257
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 537 AIGIDDNFFDLGGHSLKGMMLIANIQAELEKSVPLKALFEQPTVRQLAAYME---ASAVS 593
Cdd:PRK05691 4258 RVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEglaGSAID 4317
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1058-1531 |
3.57e-90 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 303.74 E-value: 3.57e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1058 FEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYP 1137
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1138 DQRIEYILQDSGAKLLLKQEGISVPDSYTgDVILLDGSRTILSLPLDENdegnPETAVTAENLAYMIYTSGTTGQPKGVM 1217
Cdd:PRK04813 88 AERIEMIIEVAKPSLIIATEELPLEILGI-PVITLDELKDIFATGNPYD----FDHAVKGDDNYYIIFTSGTTGKPKGVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1218 VEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNGVTI-TFLP 1296
Cdd:PRK04813 163 ISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPINVwVSTP 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1297 T-----QLAEQFMELENTSLRVLLTGGDKL-KRAVKKPY------TLVNNYGPTENTVVATSAEIHPE----EGSLSIGR 1360
Cdd:PRK04813 243 SfadmcLLDPSFNEEHLPNLTHFLFCGEELpHKTAKKLLerfpsaTIYNTYGPTEATVAVTSIEITDEmldqYKRLPIGY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1361 AIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVadpFVPGERMYRTGDLVKWVNGGIEYIGRIDQ 1440
Cdd:PRK04813 323 AKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQPAYHTGDAGYLEDGLLFYQGRIDF 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1441 QVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPETADIE-------ALKSTLKETLPDYMIPAFWV 1513
Cdd:PRK04813 400 QIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFErefeltkAIKKELKERLMEYMIPRKFI 479
|
490
....*....|....*...
gi 2214269206 1514 TLNELPVTANGKVDRKAL 1531
Cdd:PRK04813 480 YRDSLPLTPNGKIDRKAL 497
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
1052-1533 |
7.32e-90 |
|
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: 302.83 E-value: 7.32e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1052 KTVHQLFEeTVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVP 1131
Cdd:TIGR01734 1 KLIEAIQA-FAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1132 IDPDYPDQRIEYILQDSGAKLLLKQEGISVpDSYTGDVIlldgsrTILSLPLDENDEGNP--ETAVTAENLAYMIYTSGT 1209
Cdd:TIGR01734 80 VDTSIPSERIEMIIEAAGPELVIHTAELSI-DAVGTQII------TLSALEQAETSGGPVsfDHAVKGDDNYYIIYTSGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1210 TGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLNDYFETNG 1289
Cdd:TIGR01734 153 TGNPKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1290 VTI-TFLPT-----QLAEQFMELENTSLRVLLTGGDKL-KRAVKK------PYTLVNNYGPTENTVVATSAEIHPE---- 1352
Cdd:TIGR01734 233 LNVwVSTPSfvdmcLLDPNFNQENYPHLTHFLFCGEELpVKTAKAllerfpKATIYNTYGPTEATVAVTSVKITQEildq 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1353 EGSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVadpFVPGERMYRTGDLVKWVNGGI 1432
Cdd:TIGR01734 313 YPRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFF---SHEGQPAYRTGDAGTITDGQL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1433 EYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGN-TAIAAYVTPETADIE-------ALKSTLKETLP 1504
Cdd:TIGR01734 390 FYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAIVPETEDFEkefqltkAIKKELKKSLP 469
|
490 500
....*....|....*....|....*....
gi 2214269206 1505 DYMIPAFWVTLNELPVTANGKVDRKALPE 1533
Cdd:TIGR01734 470 AYMIPRKFIYRDQLPLTANGKIDRKALAE 498
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
609-1019 |
4.24e-89 |
|
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: 297.75 E-value: 4.24e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 609 PLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFM-EANGEPVQRIIEKAEVDLHVF 687
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVrDDGGVPRQEILPPGPAPLEVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 688 EAKEDEAD--QKIKEFIR-----PFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKGEQ---- 756
Cdd:cd19539 83 DLSDPDSDreRRLEELLReresrGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkgpa 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 757 --LPEPTLHYKDFAVWQNEAEQKERMKEHEAYWMSVLSGeLPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLLA 834
Cdd:cd19539 163 apLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAK 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 835 ETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSALE 914
Cdd:cd19539 242 RARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQR 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 915 HQEYPFEDLVNQLDLPRDMSRNPLF-NVMVTTENPDKEQLTLQNLSISPYEAHQGTSKFDLTLGGFTDENGIGLQLEYAT 993
Cdd:cd19539 322 HQELPFQQLVAELPVDRDAGRHPLVqIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYAT 401
|
410 420
....*....|....*....|....*.
gi 2214269206 994 DLFAKETAEKWSEYVLRLLKAVADNP 1019
Cdd:cd19539 402 SLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
609-1019 |
1.14e-79 |
|
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: 270.10 E-value: 1.14e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 609 PLSSAQKRMYVLNQ-LDRQTiSYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFM--EANGEPVQRIIEKAEVDL- 684
Cdd:cd19532 3 PMSFGQSRFWFLQQyLEDPT-TFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFtdPEDGEPMQGVLASSPLRLe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 685 HVFEAKEDEADQKIKEF-IRPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKGEQLPEPTLH 763
Cdd:cd19532 82 HVQISDEAEVEEEFERLkNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 764 YKDFAVWQNEAEQKERMKEHEAYWMSVLSGELPELDLpLDYA----RPPVQSFKGDTIRFRTGSETAKAVEKLLAETGTT 839
Cdd:cd19532 162 YLDFAARQRQDYESGALDEDLAYWKSEFSTLPEPLPL-LPFAkvksRPPLTRYDTHTAERRLDAALAARIKEASRKLRVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 840 ---LHMvlhAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSALEHQ 916
Cdd:cd19532 241 pfhFYL---AALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 917 EYPFEDLVNQLDLPRDMSRNPLFNVMVtteN---PDKEQLTLQNLSISPYEAHQGTSKFDLTLgGFTD--ENGIGLQLEY 991
Cdd:cd19532 318 RVPFDVLLDELGVPRSATHSPLFQVFI---NyrqGVAESRPFGDCELEGEEFEDARTPYDLSL-DIIDnpDGDCLLTLKV 393
|
410 420
....*....|....*....|....*....
gi 2214269206 992 ATDLFAKETAEKWSE-YVlRLLKAVADNP 1019
Cdd:cd19532 394 QSSLYSEEDAELLLDsYV-NLLEAFARDP 421
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
607-1019 |
4.23e-78 |
|
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: 265.99 E-value: 4.23e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 607 MYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFM-EANGEPVQRIIEKAEVDLH 685
Cdd:cd19543 1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVwEGLGEPLQVVLKDRKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 686 VF---EAKEDEADQKIKEF-----IRPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLY----K 753
Cdd:cd19543 81 ELdlsHLSEAEQEAELEALaeedrERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYaalgE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 754 GEQLP-EPTLHYKDFAVWQneaeQKERMKEHEAYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKL 832
Cdd:cd19543 161 GQPPSlPPVRPYRDYIAWL----QRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 833 LAETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRtNAD---VQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTN 909
Cdd:cd19543 237 ARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGR-PAElpgIETMVGLFINTLPVRVRLDPDQTVLELLKDLQAQQ 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 910 LSALEHQEYPFEDLVNQLDLPRdmsrnPLFNVMVTTEN-PDKEQLTLQN----LSISPYEAHQGTSkFDLTLGGFTDEnG 984
Cdd:cd19543 316 LELREHEYVPLYEIQAWSEGKQ-----ALFDHLLVFENyPVDESLEEEQdedgLRITDVSAEEQTN-YPLTVVAIPGE-E 388
|
410 420 430
....*....|....*....|....*....|....*
gi 2214269206 985 IGLQLEYATDLFAKETAEKWSEYVLRLLKAVADNP 1019
Cdd:cd19543 389 LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
17-501 |
3.52e-75 |
|
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: 260.08 E-value: 3.52e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 17 AQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERI 96
Cdd:TIGR01734 10 AETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVDTSIPSERI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 97 RYSLEDSGAKFAV-VNERNMTAIGQYEGIIVSLDDGKWRNESKERPSSISGSRNLaYVIYTSGTTGKPKGVQIEHRNLTN 175
Cdd:TIGR01734 90 EMIIEAAGPELVIhTAELSIDAVGTQIITLSALEQAETSGGPVSFDHAVKGDDNY-YIIYTSGSTGNPKGVQISHDNLVS 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 176 YVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVN 255
Cdd:TIGR01734 169 FTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVWVSTPSFVDMCLL 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 256 TASFAKDaNFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDLYEPDAFAKRPtIGRPIANAG 335
Cdd:TIGR01734 249 DPNFNQE-NYPHLTHFLFCGEELPVKTAKALLERFPKATIYNTYGPTEATVAVTSVKITQEILDQYPRLP-IGFAKPDMN 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 336 ALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGslmYKTGDVVRrLSDGTLAFIGRADDQVKIR 415
Cdd:TIGR01734 327 LFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSHEGQPA---YRTGDAGT-ITDGQLFYQGRLDFQIKLH 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 416 GYRIEPKEIETVMLSLSGIQEAVVLAV--SEGGLQELCAYY-TSDQDIEKA-----ELRYQLSLTLPSHMIPAFFVQVDA 487
Cdd:TIGR01734 403 GYRIELEDIEFNLRQSSYIESAVVVPKynKDHKVEYLIAAIvPETEDFEKEfqltkAIKKELKKSLPAYMIPRKFIYRDQ 482
|
490
....*....|....
gi 2214269206 488 IPLTANGKTDRNAL 501
Cdd:TIGR01734 483 LPLTANGKIDRKAL 496
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
787-1636 |
7.69e-75 |
|
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: 276.18 E-value: 7.69e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 787 WMSVLSGeLPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVekllaeTGTTLHMVLHAVFHVFLSKISGQRDIVIGSv 866
Cdd:TIGR03443 2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSAEVTAG------GGSTPFIILLAAFAALVYRLTGDEDIVLGT- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 867 tagRTNADVqdmpgmfvNTLALRMEAKEQQTFAELLELAKQTNLSALEHQEYPFEDLVNQLDLPRDMSRNPLFNVMVTTE 946
Cdd:TIGR03443 74 ---SSNKSG--------RPFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPLFRLAFQD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 947 NPDKEQLTLQNLSISpyeahqgtskfDLTLGGFTDENGIGLQLEYATDLFAKETAEKWSEYVLRLLKAVADNPNQPLSSL 1026
Cdd:TIGR03443 143 APDNQQTTYSTGSTT-----------DLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKV 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1027 LLVTETEKQALleawkgkalPVPTDK--------TVHQLFEETVQRHKDRPAVT-----YNGQS----WTYGELNAKANR 1089
Cdd:TIGR03443 212 SLITPSQKSLL---------PDPTKDldwsgfrgAIHDIFADNAEKHPDRTCVVetpsfLDPSSktrsFTYKQINEASNI 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1090 LARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKQEGISVPDSYTGDV 1169
Cdd:TIGR03443 283 LAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIVIEKAGTLDQLVRDY 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1170 I---------------LLDGSRTILSLPLDENDEGNPETAVTAENLAYMI---------YTSGTTGQPKGVMVEHHALVN 1225
Cdd:TIGR03443 363 IdkelelrteipalalQDDGSLVGGSLEGGETDVLAPYQALKDTPTGVVVgpdsnptlsFTSGSEGIPKGVLGRHFSLAY 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1226 LCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVideAIRLDI---VRLNDYFETNGVTIT--------F 1294
Cdd:TIGR03443 443 YFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLV---PTADDIgtpGRLAEWMAKYGATVThltpamgqL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1295 LPTQLAEQFMELENtSLRVlltgGDKL-KRAVKKPYTL------VNNYGPTENTVVATSAEIHPEEGSLSI--------- 1358
Cdd:TIGR03443 520 LSAQATTPIPSLHH-AFFV----GDILtKRDCLRLQTLaenvciVNMYGTTETQRAVSYFEIPSRSSDSTFlknlkdvmp 594
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1359 -GRAIANTRVYILGEGNQVQPEGVA--GELCVAGRGLARGYLNREDETAKRFVADPFV---------------------- 1413
Cdd:TIGR03443 595 aGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVdpshwidldkennkperefwlg 674
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1414 PGERMYRTGDLVKWV-NGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDaAVTAV-KDKGGNTAIAAYVTP--ET 1489
Cdd:TIGR03443 675 PRDRLYRTGDLGRYLpDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRE-NVTLVrRDKDEEPTLVSYIVPqdKS 753
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1490 ADIEALKST---------------------------LKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPDIE--AGS 1540
Cdd:TIGR03443 754 DELEEFKSEvddeessdpvvkglikyrklikdireyLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAqlAAV 833
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1541 GEYKAPTTDMEEL------LAGIWQDVL--GMSEVGVTDNFFSLGGDSIKGIQMASRLNQHgWKLE--MKDLFQHPTIEE 1610
Cdd:TIGR03443 834 AKNRSASAADEEFtetereIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKK-LNVElpLGLIFKSPTIKG 912
|
970 980
....*....|....*....|....*...
gi 2214269206 1611 LTQYVER--AEGKQADQGPVEGEVILTP 1636
Cdd:TIGR03443 913 FAKEVDRlkKGEELADEGDSEIEEEETV 940
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
607-1019 |
8.55e-75 |
|
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: 256.57 E-value: 8.55e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 607 MYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKAE-VDLH 685
Cdd:cd19066 1 KIPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVrFRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 686 VFEAKE-DEADQKIKEFI-----RPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKG----- 754
Cdd:cd19066 81 IIDLRNlADPEARLLELIdqiqqTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaerqk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 755 EQLPEPTLHYKDFAVWQNEAEQKERMKEHEAYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLLA 834
Cdd:cd19066 161 PTLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVAR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 835 ETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSALE 914
Cdd:cd19066 241 ESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 915 HQEYPFEDLVNQLDLPRDMSRNPLFNVMVTTENPDKEQLTLQNLS-ISPYEAHQGTSKFDLTLGGFTDENG-IGLQLEYA 992
Cdd:cd19066 321 HQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIfTTPVYTSSEGTVFDLDLEASEDPDGdLLLRLEYS 400
|
410 420
....*....|....*....|....*..
gi 2214269206 993 TDLFAKETAEKWSEYVLRLLKAVADNP 1019
Cdd:cd19066 401 RGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
610-840 |
1.34e-74 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 248.80 E-value: 1.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 610 LSSAQKRMYVLnqlDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKAEVDLHVF-- 687
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVdl 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 688 -----EAKEDEADQKIKEFI-RPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLY------KGE 755
Cdd:COG4908 78 salpePEREAELEELVAEEAsRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYaallegEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 756 QLPEPTLHYKDFAVWQNEAEQKERMKEHEAYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLLAE 835
Cdd:COG4908 158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237
|
....*
gi 2214269206 836 TGTTL 840
Cdd:COG4908 238 HGATV 242
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
13-501 |
3.03e-74 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 257.52 E-value: 3.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 13 FEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTP 92
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 93 EERIRYSLEDSGAKFAVVNERNMTAIGQYEGIIVS-LDDGKWRNESKERPSSISGSRNlAYVIYTSGTTGKPKGVQIEHR 171
Cdd:PRK04813 88 AERIEMIIEVAKPSLIIATEELPLEILGIPVITLDeLKDIFATGNPYDFDHAVKGDDN-YYIIFTSGTTGKPKGVQISHD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 172 NLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITyikltpslfh 251
Cdd:PRK04813 167 NLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPIN---------- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 252 TIVNTASFAK----DANFE-----SLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDlyePDAFA 322
Cdd:PRK04813 237 VWVSTPSFADmcllDPSFNeehlpNLTHFLFCGEELPHKTAKKLLERFPSATIYNTYGPTEATVAVTSIEIT---DEMLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 323 KRPT--IGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVEnpySPGSLMYKTGDVVRrLSDG 400
Cdd:PRK04813 314 QYKRlpIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY-LEDG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 401 TLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGG-LQELCAY-------YTSDQDIEKAeLRYQLSLT 472
Cdd:PRK04813 390 LLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHkVQYLIAYvvpkeedFEREFELTKA-IKKELKER 468
|
490 500
....*....|....*....|....*....
gi 2214269206 473 LPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK04813 469 LMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
19-588 |
6.27e-74 |
|
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: 273.48 E-value: 6.27e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 19 QTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRY 98
Cdd:TIGR03443 257 ETPSFLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTI 336
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 99 SLEDSGAKFAVVNErnmtAIGQYEGIIVS-----------------LDDGKWRNeskerpSSISGSRN--LA-YVIY--- 155
Cdd:TIGR03443 337 YLSVAKPRALIVIE----KAGTLDQLVRDyidkelelrteipalalQDDGSLVG------GSLEGGETdvLApYQALkdt 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 156 ----------------TSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHI 219
Cdd:TIGR03443 407 ptgvvvgpdsnptlsfTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLV 486
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 220 VQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASfakdANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHY 299
Cdd:TIGR03443 487 PTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAQAT----TPIPSLHHAFFVGDILTKRDCLRLQTLAENVCIVNMY 562
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 300 GPTEaTIGAiagrVDLYEPDAFAKRPTI----------GRPIANAGALVLN--EALKLVPPGASGQLYITGQGLARGYLN 367
Cdd:TIGR03443 563 GTTE-TQRA----VSYFEIPSRSSDSTFlknlkdvmpaGKGMKNVQLLVVNrnDRTQTCGVGEVGEIYVRAGGLAEGYLG 637
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 368 RPQLTAERFVENPY----------------------SPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIE 425
Cdd:TIGR03443 638 LPELNAEKFVNNWFvdpshwidldkennkperefwlGPRDRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEID 717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 426 TVMLSLSGIQEAVVLA--------------VSEGGLQELCAYYTSDQDIEKAE---------------LRYQLSLTLPSH 476
Cdd:TIGR03443 718 THLSQHPLVRENVTLVrrdkdeeptlvsyiVPQDKSDELEEFKSEVDDEESSDpvvkglikyrklikdIREYLKKKLPSY 797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 477 MIPAFFVQVDAIPLTANGKTDRNALPKPNAAQ-----SGGKALAAPE--TALEESLCRIWQKTL--GIEAIGIDDNFFDL 547
Cdd:TIGR03443 798 AIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQlaavaKNRSASAADEefTETEREIRDLWLELLpnRPATISPDDSFFDL 877
|
650 660 670 680
....*....|....*....|....*....|....*....|.
gi 2214269206 548 GGHSLKGMMLIANIQAELEKSVPLKALFEQPTVRQLAAYME 588
Cdd:TIGR03443 878 GGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFAKEVD 918
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
8-503 |
8.45e-72 |
|
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: 250.85 E-value: 8.45e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 8 TFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPI 87
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 88 DPDTPEERIRYSLEDSGAKFAVVNE----------------RNMTAIGQYEGIIVSLDDGK---WRnESKERPSSISGSR 148
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSerldllhpalpgchdlRTLIIVGDPAHASEGHPGEEpasWP-KLLALGDADPPHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 149 ----NLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQket 224
Cdd:TIGR03098 160 vidsDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD--- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 225 YTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTAsfAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEA 304
Cdd:TIGR03098 237 YLLPRDVLKALEKHGITGLAAVPPLWAQLAQLD--WPESAAPSLRYLTNSGGAMPRATLSRLRSFLPNARLFLMYGLTEA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 305 TigaiagRVDLYEPDAFAKRPT-IGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSP 383
Cdd:TIGR03098 315 F------RSTYLPPEEVDRRPDsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 384 GSLMYK-----TGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQE---LCAYYT 455
Cdd:TIGR03098 389 GELHLPelavwSGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQaivLVVTPP 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2214269206 456 SDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALPK 503
Cdd:TIGR03098 469 GGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
150-497 |
5.46e-69 |
|
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: 236.41 E-value: 5.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 150 LAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETytaPD 229
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFD---PE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 230 EIAHYIKEHGITYIKLTPSLFHTIVNTASFAkDANFESLRLIVLGGEKIIPTDVIAFRKMYGhTEFINHYGPTEATIGAI 309
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESA-GYDLSSLRALVSGGAPLPPELLERFEEAPG-IKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 310 AGRVDLYEpdafAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpyspgslMYK 389
Cdd:cd04433 157 TGPPDDDA----RKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDEDG-------WYR 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 390 TGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV-SEGGLQELCAY--YTSDQDIEKAELR 466
Cdd:cd04433 226 TGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVpDPEWGERVVAVvvLRPGADLDAEELR 305
|
330 340 350
....*....|....*....|....*....|.
gi 2214269206 467 YQLSLTLPSHMIPAFFVQVDAIPLTANGKTD 497
Cdd:cd04433 306 AHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1634-2059 |
6.20e-69 |
|
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: 239.62 E-value: 6.20e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1634 LTPIQRWFFEKNFTN--KHHWNQSVMLHAKKGFDPERVEKTLQALIEHHDALRMVYREENGDIVQVYKPIGEsKVSFEIV 1711
Cdd:cd19066 4 LSPMQRGMWFLKKLAtdPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTV-RFRIEII 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1712 DLYGSDEEMLRSQiKLLANKLQSSLDLRNGPLLKAEQYRT-EAGDHLLIAVHHLVVDGVSWRILLEDFASGYMQAEKEES 1790
Cdd:cd19066 83 DLRNLADPEARLL-ELIDQIQQTIYDLERGPLVRVALFRLaDERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQKP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1791 lVFPQKTNSFKDWAEELAAFSQSAHLLQQAEYWSQIAAE--QVSPLPKDCETEQRIVKDTSSVLCELTAEDTKHlLTDVH 1868
Cdd:cd19066 162 -TLPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGlpPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKR-LREVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1869 QPYGTEINDILLSALGLTMKEWTKGAKIGINLEGHGRediiPNVNISRTVGWFTAQYPVVLDIS-DADASAVIKTVKENL 1947
Cdd:cd19066 240 RESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNR----PDEAVEDTIGLFLNLLPLRIDTSpDATFPELLKRTKEQS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1948 RRIPDKGVGYGILR----YFTETAEtKGFTPEISFNYLGQFDSEVKTDFFEpsafDMGRQVSGESEALYALSFSGMI-RN 2022
Cdd:cd19066 316 REAIEHQRVPFIELvrhlGVVPEAP-KHPLFEPVFTFKNNQQQLGKTGGFI----FTTPVYTSSEGTVFDLDLEASEdPD 390
|
410 420 430
....*....|....*....|....*....|....*..
gi 2214269206 2023 GRFVLSCSYNEKEFERATVEEQMERFKENLLMLIRHC 2059
Cdd:cd19066 391 GDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| NRPS-para261 |
TIGR01720 |
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ... |
1935-2085 |
9.10e-69 |
|
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.
Pssm-ID: 273774 [Multi-domain] Cd Length: 153 Bit Score: 228.31 E-value: 9.10e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1935 DASAVIKTVKENLRRIPDKGVGYGILRYFTETAETKGF--TPEISFNYLGQFDSEVKTDFFEPSAFDMGRQVSGESEALY 2012
Cdd:TIGR01720 1 ELGRLIKAVKEQLRRIPNKGVGYGVLRYLTEPEEKLAAspQPEISFNYLGQFDADSNDELFQPSSYSPGEAISPESPRPY 80
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 2013 ALSFSGMIRNGRFVLSCSYNEKEFERATVEEQMERFKENLLMLIRHCTEKEDKEFTPSDFSAEDLEMDEMGDI 2085
Cdd:TIGR01720 81 ALEINAMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
608-1019 |
1.16e-67 |
|
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: 235.34 E-value: 1.16e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 608 YPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKAEVDLHVF 687
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 688 -----EAKEDEADQKIKEFIR-PFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLY----KGEQL 757
Cdd:cd19533 82 dlsgdPDPEGAAQQWMQEDLRkPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtallKGRPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 758 PEPTLHYKDFAVwqnEAEQK----ERMKEHEAYWMSVLSGeLPELDLPLDYARPPVQSFKGDTIRFRtgSETAKAVEKLL 833
Cdd:cd19533 162 PPAPFGSFLDLV---EEEQAyrqsERFERDRAFWTEQFED-LPEPVSLARRAPGRSLAFLRRTAELP--PELTRTLLEAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 834 AETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSAL 913
Cdd:cd19533 236 EAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 914 EHQEYPFEDLVNqlDLPRDMSRNPLFNVMVTTENPDKEQL------TLQNLSISPyeahqgTSKFDLTLGGFTDENGIGL 987
Cdd:cd19533 316 RHQRYRYEDLRR--DLGLTGELHPLFGPTVNYMPFDYGLDfggvvgLTHNLSSGP------TNDLSIFVYDRDDESGLRI 387
|
410 420 430
....*....|....*....|....*....|..
gi 2214269206 988 QLEYATDLFAKETAEKWSEYVLRLLKAVADNP 1019
Cdd:cd19533 388 DFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
13-498 |
4.63e-67 |
|
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: 234.43 E-value: 4.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 13 FEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPD-T 91
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRlT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 92 PEErIRYSLEDSGAKfavvnernmtaigqyegiiVSLDDgkwrneskerpssisgsrnLAYVIYTSGTTGKPKGVQIEHR 171
Cdd:cd17631 81 PPE-VAYILADSGAK-------------------VLFDD-------------------LALLMYTSGTTGRPKGAMLTHR 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 172 NLT-NYVSWFSEeAGLTENDKTvLLSSYAFDLGYTSMF--PVLLGGGELHIVQKETytaPDEIAHYIKEHGITYIKLTPS 248
Cdd:cd17631 122 NLLwNAVNALAA-LDLGPDDVL-LVVAPLFHIGGLGVFtlPTLLRGGTVVILRKFD---PETVLDLIERHRVTSFFLVPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 249 LFHTIVNTASFAkDANFESLRLIVLGGEKIiPTDVIAFRKMYGhTEFINHYGPTEATIGAIAgrvdLYEPDAFAKRPTIG 328
Cdd:cd17631 197 MIQALLQHPRFA-TTDLSSLRAVIYGGAPM-PERLLRALQARG-VKFVQGYGMTETSPGVTF----LSPEDHRRKLGSAG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 329 RPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpyspgslMYKTGDVVRRLSDGTLAFIGRA 408
Cdd:cd17631 270 RPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG-------WFHTGDLGRLDEDGYLYIVDRK 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 409 DDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQEL-CAYY--TSDQDIEKAELRYQLSLTLPSHMIPAFFVQV 485
Cdd:cd17631 343 KDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAvVAVVvpRPGAELDEDELIAHCRERLARYKIPKSVEFV 422
|
490
....*....|...
gi 2214269206 486 DAIPLTANGKTDR 498
Cdd:cd17631 423 DALPRNATGKILK 435
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
608-1019 |
4.96e-66 |
|
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: 231.05 E-value: 4.96e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 608 YPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIiekaEVDLHVF 687
Cdd:cd20484 2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKI----EPSKPLS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 688 EAKEDEAD---QKIKEFIR-----PFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKEL----ALLYKGE 755
Cdd:cd20484 78 FQEEDISSlkeSEIIAYLRekakePFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLldayQALLQGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 756 Q--LPEPTLHYKDFAVWQNEAEQKERMKEHEAYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLL 833
Cdd:cd20484 158 QptLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 834 AETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSAL 913
Cdd:cd20484 238 RSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 914 EHQEYPFEDLVNQLDLPRDMSRNPLFNVMVTTENpdkeqlTLQNLS----ISPY----------EAHQgTSKFDLTLGGF 979
Cdd:cd20484 318 DHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQN------FLQSTSlqqfLAEYqdvlsiefveGIHQ-EGEYELVLEVY 390
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 2214269206 980 TDENGIGLQLEYATDLFAKETAEKWSEYVLRLLKAVADNP 1019
Cdd:cd20484 391 EQEDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
31-501 |
1.01e-65 |
|
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: 230.82 E-value: 1.01e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 31 NLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVV 110
Cdd:cd17654 15 TTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 111 NERNMTAigqyegiivslddgKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTEND 190
Cdd:cd17654 95 NKELDNA--------------PLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 191 KTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYI-KEHGITYIKLTPSLFHTIvnTASFAKDANF---E 266
Cdd:cd17654 161 ILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKRHRITVLQATPTLFRRF--GSQSIKSTVLsatS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 267 SLRLIVLGGEKiIPTDVI--AFRKMYGHTEFINHYGPTEATIGAIAGRVdlyePDAFAKRPtIGRPIANagalVLNEALK 344
Cdd:cd17654 239 SLRVLALGGEP-FPSLVIlsSWRGKGNRTRIFNIYGITEVSCWALAYKV----PEEDSPVQ-LGSPLLG----TVIEVRD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 345 LVPPGASGQLYItgQGLARGYLNRPQLTaerfvenpySPGSLMYKTGDVVRRlSDGTLAFIGRADDQVKIRGYRIEPKEI 424
Cdd:cd17654 309 QNGSEGTGQVFL--GGLNRVCILDDEVT---------VPKGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLI 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 425 ETVMLSLSGIQEAVVLAVSeggLQELCAYYTSDQdiEKAELRYQLSLT-LPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd17654 377 QQVIESCLGVESCAVTLSD---QQRLIAFIVGES--SSSRIHKELQLTlLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
609-999 |
1.17e-65 |
|
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: 230.22 E-value: 1.17e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 609 PLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKAEVDLHVFE 688
Cdd:cd20483 3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 689 AKED-EADQKIKEFIR-----PFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKG-------E 755
Cdd:cd20483 83 LSEAaDPEAALDQLVRnlrrqELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDAlragrdlA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 756 QLPEPTLHYKDFAVWQNEAEQKERMKEHEAYWMSVLSGeLPELD--LPLDYA-RPPVQSFKGDTIRFRTGSETAKAVEKL 832
Cdd:cd20483 163 TVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEG-IPDASklLPFAKAeRPPVKDYERSTVEATLDKELLARMKRI 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 833 LAETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSA 912
Cdd:cd20483 242 CAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEA 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 913 LEHQEYPFEDLVNQLDLPRDMSRNPLFNVMVTTENPDK-EQLTLQNLSISPYEAHQGTSKFDLTLGGFTD-ENGIGLQLE 990
Cdd:cd20483 322 YEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQVHGKfPEYDTGDFKFTDYDHYDIPTACDIALEAEEDpDGGLDLRLE 401
|
....*....
gi 2214269206 991 YATDLFAKE 999
Cdd:cd20483 402 FSTTLYDSA 410
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
9-501 |
1.81e-65 |
|
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: 230.91 E-value: 1.81e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 9 FAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPID 88
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 89 PDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEG----IIVSLDDgkwrneskerpssisgsrnLAYVIYTSGTTGKPK 164
Cdd:cd05936 81 PLYTPRELEHILNDSGAKALIVAVSFTDLLAAGAPlgerVALTPED-------------------VAVLQYTSGTTGVPK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 165 GVQIEHRNLT-N-YVSWFSEEAGLTENDK--TVLLSSYAFDLGYTSMFPVLLGGgelHIVQKETYTAPDEIAHyIKEHGI 240
Cdd:cd05936 142 GAMLTHRNLVaNaLQIKAWLEDLLEGDDVvlAALPLFHVFGLTVALLLPLALGA---TIVLIPRFRPIGVLKE-IRKHRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 241 TYIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGEKiIPTDVI-AFRKMYGhTEFINHYGPTEATIGAIAGRVDlyepd 319
Cdd:cd05936 218 TIFPGVPTMYIALLNAPEFKK-RDFSSLRLCISGGAP-LPVEVAeRFEELTG-VPIVEGYGLTETSPVVAVNPLD----- 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 320 aFAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVEnpyspGSLmyKTGDVVRRLS 398
Cdd:cd05936 290 -GPRKPgSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVD-----GWL--RTGDIGYMDE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 399 DGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV--SEGGlQELCAYYT--SDQDIEKAELRYQLSLTLP 474
Cdd:cd05936 362 DGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVpdPYSG-EAVKAFVVlkEGASLTEEEIIAFCREQLA 440
|
490 500
....*....|....*....|....*..
gi 2214269206 475 SHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd05936 441 GYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1058-1528 |
3.25e-65 |
|
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: 229.03 E-value: 3.25e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1058 FEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYP 1137
Cdd:cd17631 1 LRRRARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1138 DQRIEYILQDSGAKLLLkqegisvpdsytgdvilldgsrtilslpldendegnpetavtaENLAYMIYTSGTTGQPKGVM 1217
Cdd:cd17631 81 PPEVAYILADSGAKVLF-------------------------------------------DDLALLMYTSGTTGRPKGAM 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1218 VEHHALVNLCFWHHDAFSMTAEDRSAKYAG-FGFDASIWEMFPTWTIGAELHVIDeaiRLDIVRLNDYFETNGVTITFL- 1295
Cdd:cd17631 118 LTHRNLLWNAVNALAALDLGPDDVLLVVAPlFHIGGLGVFTLPTLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLv 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1296 PTQL-----AEQFMELENTSLRVLLTGGDKLKRAVKKPYT-----LVNNYGPTENTVVAT--SAEIHpEEGSLSIGRAIA 1363
Cdd:cd17631 195 PTMIqallqHPRFATTDLSSLRAVIYGGAPMPERLLRALQargvkFVQGYGMTETSPGVTflSPEDH-RRKLGSAGRPVF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1364 NTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermyRTGDLVKWVNGGIEYI-GRIDQQV 1442
Cdd:cd17631 274 FVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIvDRKKDMI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1443 KVRGYRIELSEIEVQLAQLSEVQDAAVTAVKD-KGGNTAIAAYVTPE--TADIEALKSTLKETLPDYMIPAFWVTLNELP 1519
Cdd:cd17631 347 ISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDeKWGEAVVAVVVPRPgaELDEDELIAHCRERLARYKIPKSVEFVDALP 426
|
....*....
gi 2214269206 1520 VTANGKVDR 1528
Cdd:cd17631 427 RNATGKILK 435
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
1053-1531 |
3.30e-64 |
|
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: 228.51 E-value: 3.30e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1053 TVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPI 1132
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1133 DPDYPDQRIEYILQDSGAKLL--------LKQEGISVPDSYTGDVILLDGSRTILSLPLDENDE-------GNPETAVTA 1197
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLvtsserldLLHPALPGCHDLRTLIIVGDPAHASEGHPGEEPASwpkllalGDADPPHPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1198 --ENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIR 1275
Cdd:TIGR03098 161 idSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1276 LDIVRLndyFETNGVT-ITFLP---TQLAE-QFMELENTSLRVLLTGGDKLKRAV----------KKPYTLvnnYGPTEn 1340
Cdd:TIGR03098 241 RDVLKA---LEKHGITgLAAVPplwAQLAQlDWPESAAPSLRYLTNSGGAMPRATlsrlrsflpnARLFLM---YGLTE- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1341 tvVATSAEIHPEEGSL---SIGRAIANTRVYILGE-GNQVQPeGVAGELCVAGRGLARGYLNREDETAKRFVADPFVPG- 1415
Cdd:TIGR03098 314 --AFRSTYLPPEEVDRrpdSIGKAIPNAEVLVLREdGSECAP-GEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGe 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1416 ----ERMYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP--- 1487
Cdd:TIGR03098 391 lhlpELAVWSGDTVRRdEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPpgg 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2214269206 1488 ETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:TIGR03098 471 EELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1053-1534 |
6.33e-64 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 227.76 E-value: 6.33e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1053 TVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPI 1132
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1133 DPDYPDQRIEYILQDSGAKLLL-KQEGISVPDSYTGD------VILLDGSRTILSLP--------LDENDEGNPETAVTA 1197
Cdd:PRK06187 87 NIRLKPEEIAYILNDAEDRVVLvDSEFVPLLAAILPQlptvrtVIVEGDGPAAPLAPevgeyeelLAAASDTFDFPDIDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1198 ENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYA-GFGFDASIWEMFPTWTiGAELHVIDeaiRL 1276
Cdd:PRK06187 167 NDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVpMFHVHAWGLPYLALMA-GAKQVIPR---RF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1277 DIVRLNDYFETNGVTITFL-PT-------QLAEQFMELenTSLRVLLTGG-----DKLKRAVKKPY-TLVNNYGPTENTV 1342
Cdd:PRK06187 243 DPENLLDLIETERVTFFFAvPTiwqmllkAPRAYFVDF--SSLRLVIYGGaalppALLREFKEKFGiDLVQGYGMTETSP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1343 VATSAeiHPEEG-------SLSIGRAIANTRVYILG-EGNQVQPEGVA-GELCVAGRGLARGYLNREDETAKRFVADpfv 1413
Cdd:PRK06187 321 VVSVL--PPEDQlpgqwtkRRSAGRPLPGVEARIVDdDGDELPPDGGEvGEIIVRGPWLMQGYWNRPEATAETIDGG--- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1414 pgerMYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP---ET 1489
Cdd:PRK06187 396 ----WLHTGDVGYIDEDGYLYItDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLkpgAT 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2214269206 1490 ADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEP 1534
Cdd:PRK06187 472 LDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQ 516
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
33-523 |
1.25e-63 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 228.46 E-value: 1.25e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPD-TPEErIRYSLEDSGAKFAVVN 111
Cdd:COG0365 40 LTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGfGAEA-LADRIEDAEAKVLITA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 112 E---RNMTAIG---------------------QYEGIIVSLDDGKW-----RNESKERPSSISGSRNLAYVIYTSGTTGK 162
Cdd:COG0365 119 DgglRGGKVIDlkekvdealeelpslehvivvGRTGADVPMEGDLDwdellAAASAEFEPEPTDADDPLFILYTSGTTGK 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 163 PKGVQIEHRNLTNYVSWFSEEA-GLTENDktVLLSS----YAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKE 237
Cdd:COG0365 199 PKGVVHTHGGYLVHAATTAKYVlDLKPGD--VFWCTadigWATGHSYIVYGPLLNGATVVLYEGRPDFPDPGRLWELIEK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 238 HGITYIKLTPSLFHTIVNTA-SFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTeFINHYGPTEaTIGAIAGrvdlY 316
Cdd:COG0365 277 YGVTVFFTAPTAIRALMKAGdEPLKKYDLSSLRLLGSAGEPLNPEVWEWWYEAVGVP-IVDGWGQTE-TGGIFIS----N 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 317 EPDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQ--GLARGYLNRPQLTAERFVEnpYSPGslMYKTGDVV 394
Cdd:COG0365 351 LPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWNDPERYRETYFG--RFPG--WYRTGDGA 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 395 RRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVS-EGGLQELCAY------YTSDQDIEKaELRY 467
Cdd:COG0365 427 RRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPdEIRGQVVKAFvvlkpgVEPSDELAK-ELQA 505
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 468 QLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALPKPNAAQSGGK--ALAAPEtALEE 523
Cdd:COG0365 506 HVREELGPYAYPREIEFVDELPKTRSGKIMRRLLRKIAEGRPLGDtsTLEDPE-ALDE 562
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1200-1527 |
8.82e-62 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 215.61 E-value: 8.82e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1200 LAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDeaiRLDIV 1279
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLP---KFDPE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1280 RLNDYFETNGVTITFLPTQLAEQFMELENT------SLRVLLTGG-----DKLKRAVKKPY-TLVNNYGPTENTVVATSA 1347
Cdd:cd04433 79 AALELIEREKVTILLGVPTLLARLLKAPESagydlsSLRALVSGGaplppELLERFEEAPGiKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1348 EIHPEEGSL-SIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFvadpfvpGERMYRTGDLVK 1426
Cdd:cd04433 159 PPDDDARKPgSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGDLGR 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1427 W-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP---ETADIEALKSTLKET 1502
Cdd:cd04433 232 LdEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLrpgADLDAEELRAHVRER 311
|
330 340
....*....|....*....|....*
gi 2214269206 1503 LPDYMIPAFWVTLNELPVTANGKVD 1527
Cdd:cd04433 312 LAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1056-1531 |
4.18e-61 |
|
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: 218.20 E-value: 4.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1056 QLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPD 1135
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1136 YPDQRIEYILQDSGAKLLLkqegisVPDSYTGdviLLDGSRTILSLPldendegnpetAVTAENLAYMIYTSGTTGQPKG 1215
Cdd:cd05936 83 YTPRELEHILNDSGAKALI------VAVSFTD---LLAAGAPLGERV-----------ALTPEDVAVLQYTSGTTGVPKG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1216 VMVEHHALV-NL--CfWHHDAFSMTAEDRSAK----YAGFGFDASiweMFPTWTIGAELHVIDeaiRLDIVRLNDYFETN 1288
Cdd:cd05936 143 AMLTHRNLVaNAlqI-KAWLEDLLEGDDVVLAalplFHVFGLTVA---LLLPLALGATIVLIP---RFRPIGVLKEIRKH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1289 GVTI-TFLPTQL-----AEQFMELENTSLRVLLTGGDKLKRAVKKPY------TLVNNYGPTENTVVATSAEIHPEEGSL 1356
Cdd:cd05936 216 RVTIfPGVPTMYiallnAPEFKKRDFSSLRLCISGGAPLPVEVAERFeeltgvPIVEGYGLTETSPVVAVNPLDGPRKPG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1357 SIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermyRTGDLVKWVNGGIEYI- 1435
Cdd:cd05936 296 SIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYMDEDGYFFIv 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1436 GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP---ETADIEALKSTLKETLPDYMIPAFW 1512
Cdd:cd05936 369 DRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLkegASLTEEEIIAFCREQLAGYKVPRQV 448
|
490
....*....|....*....
gi 2214269206 1513 VTLNELPVTANGKVDRKAL 1531
Cdd:cd05936 449 EFRDELPKSAVGKILRREL 467
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
34-504 |
7.77e-61 |
|
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: 218.93 E-value: 7.77e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLedsgakfAVVNER 113
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYL-------GVAKPR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 114 NMTAIgQYEGIIVSLDdgkwrneskERPSsisgsrnlayVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTV 193
Cdd:cd17647 95 GLIVI-RAAGVVVGPD---------SNPT----------LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 194 LLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTAsfakDANFESLRLIVL 273
Cdd:cd17647 155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQA----TTPFPKLHHAFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 274 GGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGaiagrVDLYEPDAFAKRPTI----------GRPIANAGALVLN--E 341
Cdd:cd17647 231 VGDILTKRDCLRLQTLAENVRIVNMYGTTETQRA-----VSYFEVPSRSSDPTFlknlkdvmpaGRGMLNVQLLVVNrnD 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 342 ALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVEN-----------------PYSPGSL-----MYKTGDVVRRLSD 399
Cdd:cd17647 306 RTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnePWRQFWLgprdrLYRTGDLGRYLPN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 400 GTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLA--------------VSEGGLQELCAYYTSDQDIEKAE- 464
Cdd:cd17647 386 GDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVrrdkdeeptlvsyiVPRFDKPDDESFAQEDVPKEVSTd 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 465 ---------------LRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALPKP 504
Cdd:cd17647 466 pivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1634-1876 |
4.78e-60 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 206.81 E-value: 4.78e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1634 LTPIQRWFFEkNFTNKHHWNQSVMLHAKKGFDPERVEKTLQALIEHHDALRMVYREENGDIVQVYKPigESKVSFEIVDL 1713
Cdd:COG4908 1 LSPAQKRFLF-LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDP--DADLPLEVVDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1714 YG-SDEEMLRSQIKLLANKLQSSLDLRNGPLLKAEQYRTEAGDH-LLIAVHHLVVDGVSWRILLEDFASGYMQAEKEESL 1791
Cdd:COG4908 78 SAlPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHvLLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1792 VFPQKTNSFKDWAEELAAFSQSAHLLQQAEYWSQIAAE--QVSPLPKDCETEQRIVKDTSSVLCELTAEDTKHLLTDVHQ 1869
Cdd:COG4908 158 PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGapPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKA 237
|
....*..
gi 2214269206 1870 pYGTEIN 1876
Cdd:COG4908 238 -HGATVN 243
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
609-1019 |
3.57e-59 |
|
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: 211.57 E-value: 3.57e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 609 PLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRII--EKAEVDLHV 686
Cdd:cd19546 6 PATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILdaDAARPELPV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 687 FEAKEDEADQKIKEFI-RPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKG-------EQLP 758
Cdd:cd19546 86 VPATEEELPALLADRAaHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGArregrapERAP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 759 EPtLHYKDFAVWQ-----NEAEQKERMKEHEAYWMSVLSGELPELDLPLDYARPPVQSFKGDTIRFRTGSETAKAVEKLL 833
Cdd:cd19546 166 LP-LQFADYALWErellaGEDDRDSLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLMEAA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 834 AETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTN-ADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSA 912
Cdd:cd19546 245 ESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEeGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 913 LEHQEYPFEDLVNQLDLPRDMSRNPLFNVM--VTTENPDKEQL-TLQNLSISPYEAHQGTSKFDLTL------GGFTDEN 983
Cdd:cd19546 325 RRHQDVPFERLAELLALPPSADRHPVFQVAldVRDDDNDPWDApELPGLRTSPVPLGTEAMELDLSLalterrNDDGDPD 404
|
410 420 430
....*....|....*....|....*....|....*.
gi 2214269206 984 GIGLQLEYATDLFAKETAEKWSEYVLRLLKAVADNP 1019
Cdd:cd19546 405 GLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
42-501 |
6.20e-59 |
|
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: 211.53 E-value: 6.20e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 42 ANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAA----FLPIDPDTPEERIRYSLEDSGAKFAVVNERNMT- 116
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAADr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 117 ---AIGQYEGIIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTV 193
Cdd:cd05922 83 lrdALPASPDPGTVLDADGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRAL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 194 LLSSYAFDLGYTSMFPVLLGGGELhiVQKETYTAPDEIAHYIKEHGITYIKLTPSLFhTIVNTASFAkDANFESLRLIVL 273
Cdd:cd05922 163 TVLPLSYDYGLSVLNTHLLRGATL--VLTNDGVLDDAFWEDLREHGATGLAGVPSTY-AMLTRLGFD-PAKLPSLRYLTQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 274 GGEKIIPTDVIAFRKMYGHTEFINHYGPTEATigaiaGRVDLYEPDAFAKRPT-IGRPIANAGALVLNEALKLVPPGASG 352
Cdd:cd05922 239 AGGRLPQETIARLRELLPGAQVYVMYGQTEAT-----RRMTYLPPERILEKPGsIGLAIPGGEFEILDDDGTPTPPGEPG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 353 QLYITGQGLARGYLNRPQLTAErfvenPYSPGSLMYkTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLS 432
Cdd:cd05922 314 EIVHRGPNVMKGYWNDPPYRRK-----EGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSIG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 433 GIQEAVVLAVSEGGLQELCAYYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd05922 388 LIIEAAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1053-1531 |
7.72e-59 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 214.21 E-value: 7.72e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1053 TVHQLFEETVQRHKDRPAVTYNG-----QSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGA 1127
Cdd:COG0365 10 IAYNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1128 AFVPIDPDYPDQRIEYILQDSGAKLLlkqegISVPDSYTGD---------------------VILLDGSRTILSLPLD-- 1184
Cdd:COG0365 90 VHSPVFPGFGAEALADRIEDAEAKVL-----ITADGGLRGGkvidlkekvdealeelpslehVIVVGRTGADVPMEGDld 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1185 -----ENDEGNPETAVT-AENLAYMIYTSGTTGQPKGVMVEHHA-LVNLCFWHHDAFSMTAEDR---SAKyAGFGFDASI 1254
Cdd:COG0365 165 wdellAAASAEFEPEPTdADDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVfwcTAD-IGWATGHSY 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1255 WeMFPTWTIGAELhVIDEA--IRLDIVRLNDYFETNGVTITFL-PTQLAeQFMELEN--------TSLRVLLTGG----- 1318
Cdd:COG0365 244 I-VYGPLLNGATV-VLYEGrpDFPDPGRLWELIEKYGVTVFFTaPTAIR-ALMKAGDeplkkydlSSLRLLGSAGeplnp 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1319 ---DKLKRAVKKPytLVNNYGPTENTVVATSA----EIHPeeGslSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGR- 1390
Cdd:COG0365 321 evwEWWYEAVGVP--IVDGWGQTETGGIFISNlpglPVKP--G--SMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPw 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1391 -GLARGYLNREDETAKRFVADpfVPGerMYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAA 1468
Cdd:COG0365 395 pGMFRGYWNDPERYRETYFGR--FPG--WYRTGDGARRdEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAA 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 1469 VTAVKDKGGNTAIAAYV------TPETADIEALKSTLKETLPDYMIPA--FWVTlnELPVTANGKVDRKAL 1531
Cdd:COG0365 471 VVGVPDEIRGQVVKAFVvlkpgvEPSDELAKELQAHVREELGPYAYPReiEFVD--ELPKTRSGKIMRRLL 539
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
33-501 |
1.07e-58 |
|
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: 210.01 E-value: 1.07e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFavvne 112
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARL----- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 rnmtaigqyegIIVSLDDgkwrneskerpssisgsrnLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEA-GLTENDK 191
Cdd:cd05919 86 -----------VVTSADD-------------------IAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREAlGLTPGDR 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 192 TVLLSS--YAFDLGYTSMFPVLLGGGelhIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAKDAnFESLR 269
Cdd:cd05919 136 VFSSAKmfFGYGLGNSLWFPLAVGAS---AVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLLDSCAGSPDA-LRSLR 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 270 LIVLGGEKIiPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDLYEPDafakrpTIGRPIANAGALVLNEALKLVPPG 349
Cdd:cd05919 212 LCVSAGEAL-PRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRLG------STGRPVPGYEIRLVDEEGHTIPPG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 350 ASGQLYITGQGLARGYLNRPQLTAERFVENpyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVML 429
Cdd:cd05919 285 EEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLII 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 430 SLSGIQEAVVLAVSEG-GLQELCAYYT--SDQDIEKA---ELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd05919 358 QHPAVAEAAVVAVPEStGLSRLTAFVVlkSPAAPQESlarDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1075-1532 |
2.57e-58 |
|
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: 208.30 E-value: 2.57e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1075 GQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLl 1154
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLV- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1155 kqegisvpdsytgdvilldgsrtilslpldendegnpetaVTAenLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAF 1234
Cdd:cd05934 80 ----------------------------------------VVD--PASILYTSGTTGPPKGVVITHANLTFAGYYSARRF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1235 SMTAEDRSAKYAG-FGFDASIWEMFPTWTIGAELHVIDeaiRLDIVRLNDYFETNGVTIT----FLPTQLAEQFMELENT 1309
Cdd:cd05934 118 GLGEDDVYLTVLPlFHINAQAVSVLAALSVGATLVLLP---RFSASRFWSDVRRYGATVTnylgAMLSYLLAQPPSPDDR 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1310 SLRVLLTGG----DKLKRAVKKPY--TLVNNYGPTEnTVVATSAEIHPEEGSLSIGRAIANTRVYILGEGNQVQPEGVAG 1383
Cdd:cd05934 195 AHRLRAAYGapnpPELHEEFEERFgvRLLEGYGMTE-TIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1384 ELCV---AGRGLARGYLNREDETAKRFvadpfvpGERMYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLA 1459
Cdd:cd05934 274 ELVIrglRGWGFFKGYYNMPEATAEAM-------RNGWFHTGDLGYRdADGFFYFVDRKKDMIRRRGENISSAEVERAIL 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 1460 QLSEVQDAAVTAVKDKGGNTAIAAYVT---PETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALP 1532
Cdd:cd05934 347 RHPAVREAAVVAVPDEVGEDEVKAVVVlrpGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
34-501 |
4.03e-57 |
|
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: 205.38 E-value: 4.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKF----AV 109
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLlltdSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 110 VNERNMTAIgqyegiivSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTEN 189
Cdd:TIGR01923 81 LEEKDFQAD--------SLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTED 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 190 DKTvLLSSYAFDL-GYTSMFPVLLGGGELHIVQKETytapdEIAHYIKEHGITYIKLTPSLFHTIVNtasfaKDANFESL 268
Cdd:TIGR01923 153 DNW-LLSLPLYHIsGLSILFRWLIEGATLRIVDKFN-----QLLEMIANERVTHISLVPTQLNRLLD-----EGGHNENL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 269 RLIVLGGEKIiPTDVIAFRKMYGHTEFiNHYGPTEAtigaiAGRVDLYEPDAFAKRPTIGRPIANAGALVLNEALKLVpp 348
Cdd:TIGR01923 222 RKILLGGSAI-PAPLIEEAQQYGLPIY-LSYGMTET-----CSQVTTATPEMLHARPDVGRPLAGREIKIKVDNKEGH-- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 349 gasGQLYITGQGLARGYLNRPQLTaERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVM 428
Cdd:TIGR01923 293 ---GEIMVKGANLMKGYLYQGELT-PAFEQQGW------FNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVL 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 429 LSLSGIQEAVVLAV--SEGGlQELCAYYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:TIGR01923 363 YQHPGIQEAVVVPKpdAEWG-QVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
33-501 |
3.77e-56 |
|
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: 204.91 E-value: 3.77e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNE 112
Cdd:cd05959 30 LTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 RNMTAIGQ--------YEGIIVSLDDGK----------WRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLT 174
Cdd:cd05959 110 ELAPVLAAaltksehtLVVLIVSGGAGPeagalllaelVAAEAEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHADIY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 175 nyvsWFSEEA-----GLTENDktVLLSS----YAFDLGYTSMFPVLLGGGELHIVQKETytaPDEIAHYIKEHGITYIKL 245
Cdd:cd05959 190 ----WTAELYarnvlGIREDD--VCFSAaklfFAYGLGNSLTFPLSVGATTVLMPERPT---PAAVFKRIRRYRPTVFFG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 246 TPSLFHTIVNtASFAKDANFESLRLIVLGGEkIIPTDVI-AFRKMYGHtEFINHYGPTEATIGAIAGRVDlyepdafAKR 324
Cdd:cd05959 261 VPTLYAAMLA-APNLPSRDLSSLRLCVSAGE-ALPAEVGeRWKARFGL-DILDGIGSTEMLHIFLSNRPG-------RVR 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 325 P-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVenpyspGSlMYKTGDVVRRLSDGTLA 403
Cdd:cd05959 331 YgTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGDKYVRDDDGFYT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 404 FIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVS-EGGLQELCAYY-----TSDQDIEKAELRYQLSLTLPSHM 477
Cdd:cd05959 404 YAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEdEDGLTKPKAFVvlrpgYEDSEALEEELKEFVKDRLAPYK 483
|
490 500
....*....|....*....|....
gi 2214269206 478 IPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd05959 484 YPRWIVFVDELPKTATGKIQRFKL 507
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1066-1531 |
6.24e-56 |
|
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: 202.32 E-value: 6.24e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1066 KDRPAVTYNGQ----SWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRI 1141
Cdd:cd17654 1 PDRPALIIDQTtsdtTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1142 EYILQDSGAKLLLKqegisvpdsytgdvilldgSRTILSLPLDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHH 1221
Cdd:cd17654 81 LTVMKKCHVSYLLQ-------------------NKELDNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1222 ALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLND-YFETNGVTITFLPTQLA 1300
Cdd:cd17654 142 CILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1301 EQF----MELEN----TSLRVLLTGGDKL-------KRAVKKPYTLV-NNYGPTENTVVATSAEIHPEEGSLSIGRAIAN 1364
Cdd:cd17654 222 RRFgsqsIKSTVlsatSSLRVLALGGEPFpslvilsSWRGKGNRTRIfNIYGITEVSCWALAYKVPEEDSPVQLGSPLLG 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1365 TRVYIlgegnqVQPEGVAGELCVAGRGLARGYLNREDETakrfvadpfVPGERMYRTGDLVKWVNGGIEYIGRIDQQVKV 1444
Cdd:cd17654 302 TVIEV------RDQNGSEGTGQVFLGGLNRVCILDDEVT---------VPKGTMRATGDFVTVKDGELFFLGRKDSQIKR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1445 RGYRIELSEIEVQLAQLSEVQDAAVTAVKDKggnTAIAAYVTPETADIEAlKSTLKETLPDYMIPAFWVTLNELPVTANG 1524
Cdd:cd17654 367 RGKRINLDLIQQVIESCLGVESCAVTLSDQQ---RLIAFIVGESSSSRIH-KELQLTLLSSHAIPDTFVQIDKLPLTSHG 442
|
....*..
gi 2214269206 1525 KVDRKAL 1531
Cdd:cd17654 443 KVDKSEL 449
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
608-1019 |
2.57e-55 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 199.07 E-value: 2.57e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 608 YPLSSAQKrMYVLNQLdRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEP--VQRIIEKAEVDLH 685
Cdd:cd19542 2 YPCTPMQE-GMLLSQL-RSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGtfLQVVLKSLDPPIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 686 VFEAKEDEADQKIKEFIRPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKGeQLPEPTLHYK 765
Cdd:cd19542 80 EVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG-QLLPPAPPFS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 766 DFAVWQNEAEQkermKEHEAYWMSVLSGELPeldlpldYARPPVQSFKGDTIRFRTGSETAKAVEKLLAETGTTLHMVLH 845
Cdd:cd19542 159 DYISYLQSQSQ----EESLQYWRKYLQGASP-------CAFPSLSPKRPAERSLSSTRRSLAKLEAFCASLGVTLASLFQ 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 846 AVFHVFLSKISGQRDIVIGSVTAGRTNA--DVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSALEHQEYPFEDL 923
Cdd:cd19542 228 AAWALVLARYTGSRDVVFGYVVSGRDLPvpGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 924 VNQLDLPRdmsRNPLFNVMVTTENPDKEQLTLQNLSISPYEAH-QGTSKFDLTLGGFTDENGIGLQLEYATDLFAKETAE 1002
Cdd:cd19542 308 QRALGLWP---SGTLFNTLVSYQNFEASPESELSGSSVFELSAaEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQAE 384
|
410
....*....|....*..
gi 2214269206 1003 KWSEYVLRLLKAVADNP 1019
Cdd:cd19542 385 ELLEQFDDILEALLANP 401
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1067-1531 |
3.71e-54 |
|
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: 197.13 E-value: 3.71e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLA-RILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYIL 1145
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLAnRLLALGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1146 QDSGAKLLLkqegisvpdsytgdvilldgsrtilslpldendegnpetavtaeNLAYMIYTSGTTGQPKGVMVEHHALVN 1225
Cdd:cd05941 81 TDSEPSLVL--------------------------------------------DPALILYTSGTTGRPKGVVLTHANLAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1226 LCFWHHDAFSMTAEDR------------------SAKYAG------FGFDASIWE---------MF---PT-WTigaelh 1268
Cdd:cd05941 117 NVRALVDAWRWTEDDVllhvlplhhvhglvnallCPLFAGasveflPKFDPKEVAisrlmpsitVFmgvPTiYT------ 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1269 videairldivRLNDYFETNGVTITFLPTQLAEQfmelentsLRVLLTGGDKLKRAVKKPY------TLVNNYGPTEnTV 1342
Cdd:cd05941 191 -----------RLLQYYEAHFTDPQFARAAAAER--------LRLMVSGSAALPVPTLEEWeaitghTLLERYGMTE-IG 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1343 VATSAEIHPEEGSLSIGRAIANTRVYIL-GEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermYRT 1421
Cdd:cd05941 251 MALSNPLDGERRPGTVGMPLPGVQARIVdEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1422 GDLVKWVNGGIEYI-GRI-DQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE----TADIEAL 1495
Cdd:cd05941 325 GDLGVVDEDGYYWIlGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRagaaALSLEEL 404
|
490 500 510
....*....|....*....|....*....|....*.
gi 2214269206 1496 KSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05941 405 KEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
8-501 |
4.12e-53 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 195.89 E-value: 4.12e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 8 TFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPI 87
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 88 DPD-TPEErIRYSLEDSGAK-------FAVVNERNMTAIGQYEGIIVSLDD---------GKW-----RNESKERPSSIS 145
Cdd:PRK07656 86 NTRyTADE-AAYILARGDAKalfvlglFLGVDYSATTRLPALEHVVICETEeddphtekmKTFtdflaAGDPAERAPEVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 146 GSrNLAYVIYTSGTTGKPKGVQIEHRNLT-NYVSWfSEEAGLTENDKTVLLSSYAFDLGYT-SMFPVLLGGGELHIVQKe 223
Cdd:PRK07656 165 PD-DVADILFTSGTTGRPKGAMLTHRQLLsNAADW-AEYLGLTEGDRYLAANPFFHVFGYKaGVNAPLMRGATILPLPV- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 224 tyTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTE 303
Cdd:PRK07656 242 --FDPDEVFRLIETERITVLPGPPTMYNSLLQHPD-RSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 304 ATIGAIAGRVDlyepDAFAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpys 382
Cdd:PRK07656 319 ASGVTTFNRLD----DDRKTVAgTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDAD--- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 383 pGSLmyKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQEL-CAYYT--SDQD 459
Cdd:PRK07656 392 -GWL--HTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVgKAYVVlkPGAE 468
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2214269206 460 IEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK07656 469 LTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
8-501 |
1.20e-52 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 194.64 E-value: 1.20e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 8 TFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPI 87
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 88 DPDTPEERIRYSLEDSGAKFAVVNErnmTAIGQYEGI---------IVSLDDGK-------------WRN-ESKERPSSI 144
Cdd:PRK06187 87 NIRLKPEEIAYILNDAEDRVVLVDS---EFVPLLAAIlpqlptvrtVIVEGDGPaaplapevgeyeeLLAaASDTFDFPD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 145 SGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYV----SWFseeaGLTENDktVLLS------SYAFDLGYtsmFPVLLGG 214
Cdd:PRK06187 164 IDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSlavcAWL----KLSRDD--VYLVivpmfhVHAWGLPY---LALMAGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 215 GelHIVQKEtYtAPDEIAHYIKEHGITYIKLTPSLFHTIVNtASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGhTE 294
Cdd:PRK06187 235 K--QVIPRR-F-DPENLLDLIETERVTFFFAVPTIWQMLLK-APRAYFVDFSSLRLVIYGGAALPPALLREFKEKFG-ID 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 295 FINHYGPTEAT-IGAIAgRVDLYEPDAFAKRPTIGRPIANAGALVLNEALKLVPP--GASGQLYITGQGLARGYLNRPQL 371
Cdd:PRK06187 309 LVQGYGMTETSpVVSVL-PPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 372 TAERFVeNPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQE-L 450
Cdd:PRK06187 388 TAETID-GGW------LHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGErP 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 451 CAYYT--SDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK06187 461 VAVVVlkPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1074-1526 |
3.02e-52 |
|
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: 192.81 E-value: 3.02e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1074 NGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLL 1153
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1154 lkqegISVPDSYT------------GDVILLDGSR-------TILSLPLDENDEGNPETAVTAEN-LAYMIYTSGTTGQP 1213
Cdd:cd05911 87 -----FTDPDGLEkvkeaakelgpkDKIIVLDDKPdgvlsieDLLSPTLGEEDEDLPPPLKDGKDdTAAILYSSGTTGLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1214 KGVMVEHHalvNLCFWHHDAFSMTAEDRSAKYAGFGFdASIWEMFPTWTI------GAELHVIDeaiRLDIVRLNDYFET 1287
Cdd:cd05911 162 KGVCLSHR---NLIANLSQVQTFLYGNDGSNDVILGF-LPLYHIYGLFTTlasllnGATVIIMP---KFDSELFLDLIEK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1288 NGVTITFLPTQLAEQFMELENT------SLRVLLTGGD----KLKRAVKKPY---TLVNNYGPTENTVVATSAEIHPEEG 1354
Cdd:cd05911 235 YKITFLYLVPPIAAALAKSPLLdkydlsSLRVILSGGAplskELQELLAKRFpnaTIKQGYGMTETGGILTVNPDGDDKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1355 SlSIGRAIANTRVYILGE-GNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermYRTGDLVKWVNGGIE 1433
Cdd:cd05911 315 G-SVGRLLPNVEAKIVDDdGKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1434 YI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP---ETADIEALKSTLKETLPDY--- 1506
Cdd:cd05911 388 YIvDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRkpgEKLTEKEVKDYVAKKVASYkql 467
|
490 500
....*....|....*....|....*
gi 2214269206 1507 -----MIPafwvtlnELPVTANGKV 1526
Cdd:cd05911 468 rggvvFVD-------EIPKSASGKI 485
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
33-495 |
3.79e-51 |
|
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: 189.35 E-value: 3.79e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNE 112
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 RN-------------------MTAIGQYEGIIVSLDDGKWRNESKERP-SSISGSRNLAYVIYTSGTTGKPKGVQIEHRN 172
Cdd:cd05911 91 DGlekvkeaakelgpkdkiivLDDKPDGVLSIEDLLSPTLGEEDEDLPpPLKDGKDDTAAILYSSGTTGLPKGVCLSHRN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 173 LTN--YVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKetyTAPDEIAHYIKEHGITYIKLTPSLF 250
Cdd:cd05911 171 LIAnlSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATVIIMPK---FDSELFLDLIEKYKITFLYLVPPIA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 251 HTIVNTASFAKdANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIagrvdlYEPDAFAKRPTIGRP 330
Cdd:cd05911 248 AALAKSPLLDK-YDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILT------VNPDGDDKPGSVGRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 331 IANAGALVLNEALK-LVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRAD 409
Cdd:cd05911 321 LPNVEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYLYIVDRKK 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 410 DQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYY---TSDQDIEKAELRYQLSLTLPSHM-----IpaF 481
Cdd:cd05911 395 ELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYvvrKPGEKLTEKEVKDYVAKKVASYKqlrggV--V 472
|
490
....*....|....
gi 2214269206 482 FvqVDAIPLTANGK 495
Cdd:cd05911 473 F--VDEIPKSASGK 484
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
607-1019 |
5.64e-51 |
|
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: 186.89 E-value: 5.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 607 MYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEAN-GEPVQRIIEKAEVDLH 685
Cdd:cd19536 1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 686 VFE-AKEDEADQKIKEFI-----RPFDLNDAPLIRAALLRIEAKKHLLL-LDMHHIIADGVSRGIFVKELALLYKG---- 754
Cdd:cd19536 81 ELDlTPLEEQLDPLRAYKeetkiRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQlley 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 755 --EQLPePTLHYKDFAVWQNEAEQKErmkEHEAYWMSVLSGelpeldlpLDYARPPVQSFK--GDTIR---FRTGSETAK 827
Cdd:cd19536 161 kpLSLP-PAQPYRDFVAHERASIQQA---ASERYWREYLAG--------ATLATLPALSEAvgGGPEQdseLLVSVPLPV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 828 AVEKLLAETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRT--NADVQDMPGMFVNTLALRMEAKEqQTFAELLELA 905
Cdd:cd19536 229 RSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSeeTTGAERLLGLFLNTLPLRVTLSE-ETVEDLLKRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 906 KQTNLSALEHQEYPFEdlvnqlDLPRDMSRNPLFNVMVTTENPDkEQLTLQNLSISPYEAH---QGTSKFDLTLGGFTDE 982
Cdd:cd19536 308 QEQELESLSHEQVPLA------DIQRCSEGEPLFDSIVNFRHFD-LDFGLPEWGSDEGMRRgllFSEFKSNYDVNLSVLP 380
|
410 420 430
....*....|....*....|....*....|....*....
gi 2214269206 983 NGIGL--QLEYATDLFAKETAEKWSEYVLRLLKAVADNP 1019
Cdd:cd19536 381 KQDRLelKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
30-495 |
1.88e-49 |
|
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: 182.49 E-value: 1.88e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 30 GNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAV 109
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 110 VNernmtaigqyegiivslddgkwrneskerpssisgsrnLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTEN 189
Cdd:cd05934 81 VD--------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGED 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 190 DktVLLSSY-AFDLG--YTSMFPVLLGGGELHIVqkETYTAPDEIAHyIKEHGITYIKLTPSLFHTIVNTASFAKDANfE 266
Cdd:cd05934 123 D--VYLTVLpLFHINaqAVSVLAALSVGATLVLL--PRFSASRFWSD-VRRYGATVTNYLGAMLSYLLAQPPSPDDRA-H 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 267 SLRLIvlGGEKIIPTDVIAFRKMYGhTEFINHYGPTEATIGAIAgrvdlyEPDAFAKRPTIGRPIANAGALVLNEALKLV 346
Cdd:cd05934 197 RLRAA--YGAPNPPELHEEFEERFG-VRLLEGYGMTETIVGVIG------PRDEPRRPGSIGRPAPGYEVRIVDDDGQEL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 347 PPGASGQLYIT---GQGLARGYLNRPQLTAERFvENpyspgsLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKE 423
Cdd:cd05934 268 PAGEPGELVIRglrGWGFFKGYYNMPEATAEAM-RN------GWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAE 340
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 424 IETVMLSLSGIQEAVVLAV-SEGGLQELCAYY--TSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:cd05934 341 VERAILRHPAVREAAVVAVpDEVGEDEVKAVVvlRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEK 415
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1079-1837 |
2.51e-49 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 195.00 E-value: 2.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1079 TYGELNAKANRLARILMDCGiSPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDP-----DYPDQRIEYILQDSGAKLL 1153
Cdd:PRK05691 42 SYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAGVIAVPAYPpesarRHHQERLLSIIADAEPRLL 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1154 LKQEGISvpDSYTG-DVILLDGSRTILSL-PLD-ENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALV-NLCFW 1229
Cdd:PRK05691 121 LTVADLR--DSLLQmEELAAANAPELLCVdTLDpALAEAWQEPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVaNEQLI 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1230 HHdafsmtaedrsakyaGFGFDASIWEMFPTWT--------IGAELHVIDEAIRLdIVRLNDYFETN-----------GV 1290
Cdd:PRK05691 199 RH---------------GFGIDLNPDDVIVSWLplyhdmglIGGLLQPIFSGVPC-VLMSPAYFLERplrwleaiseyGG 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1291 TITFLP--------TQLAEQFME-LENTSLRVLLTGG-----DKLKRAVKK-------PYTLVNNYGPTENTVVATSAE- 1348
Cdd:PRK05691 263 TISGGPdfayrlcsERVSESALErLDLSRWRVAYSGSepirqDSLERFAEKfaacgfdPDSFFASYGLAEATLFVSGGRr 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1349 ------IHPEEGSLSIGRAIANTRVYILGEGN---------------QVQPEGVAGELCVAGRGLARGYLNREDETAKRF 1407
Cdd:PRK05691 343 gqgipaLELDAEALARNRAEPGTGSVLMSCGRsqpghavlivdpqslEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTF 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1408 VAdpfVPGERMYRTGDLVKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEV---QDAAVTAVKDKGGN-TAIAA 1483
Cdd:PRK05691 423 VE---HDGRTWLRTGDLGFLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVvrkGRVAAFAVNHQGEEgIGIAA 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1484 YVTPETADI---EALKSTLKETLPD--YMIPAFWVTLN--ELPVTANGKVDRKA---------------LPEPD-IEAGS 1540
Cdd:PRK05691 500 EISRSVQKIlppQALIKSIRQAVAEacQEAPSVVLLLNpgALPKTSSGKLQRSAcrlrladgsldsyalFPALQaVEAAQ 579
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1541 GEykAPTTDMEELLAGIWQDVLGMSEVGVTDNFFSLGGDSIKGIQMASRLNQH-GWKLEMKDLFQHPTIEELTQYVERae 1619
Cdd:PRK05691 580 TA--ASGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLRDElGIDLNLRQLFEAPTLAAFSAAVAR-- 655
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1620 gKQADQGPVEGEVILTPIQR-----------WFFEKNFTNKHHWNQSVMLHAKKGFDPERVEKTLQALIEHHDALRMVYR 1688
Cdd:PRK05691 656 -QLAGGGAAQAAIARLPRGQalpqslaqnrlWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFY 734
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1689 EENGDIVQVYKPIGESKVSF-EIVDLYGSDEEMLRSQIKllANKLQSSLDLRNGPLLKAEQYRTEAGDH-LLIAVHHLVV 1766
Cdd:PRK05691 735 ERDGVALQRIDAQGEFALQRiDLSDLPEAEREARAAQIR--EEEARQPFDLEKGPLLRVTLVRLDDEEHqLLVTLHHIVA 812
|
810 820 830 840 850 860 870
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 1767 DGVSWRILLEDFASGYMQAEKEESLVFPQKTNSFKDWAEELAAFSQSAHLLQQAEYW-SQIAAEQ-VSPLPKD 1837
Cdd:PRK05691 813 DGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWkAQLGDEQpVLELATD 885
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1087-1531 |
7.93e-49 |
|
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: 181.87 E-value: 7.93e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1087 ANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAA----FVPIDPDYPDQRIEYILQDSGAKLLLKQEG---- 1158
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGaadr 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1159 --ISVPDSYTGD-VILLDGSRtilslpldenDEGNPETA--VTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDA 1233
Cdd:cd05922 83 lrDALPASPDPGtVLDADGIR----------AARASAPAheVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1234 FSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELhVIDEAIRLDIVRLNDYFETNGVTITFLPTqLAEQFMEL-----EN 1308
Cdd:cd05922 153 LGITADDRALTVLPLSYDYGLSVLNTHLLRGATL-VLTNDGVLDDAFWEDLREHGATGLAGVPS-TYAMLTRLgfdpaKL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1309 TSLRVLLTGGDKLKRAV------KKPYT-LVNNYGPTENTvvATSAEIHPE---EGSLSIGRAIANTRVYILGEGNQVQP 1378
Cdd:cd05922 231 PSLRYLTQAGGRLPQETiarlreLLPGAqVYVMYGQTEAT--RRMTYLPPErilEKPGSIGLAIPGGEFEILDDDGTPTP 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1379 EGVAGELCVAGRGLARGYLNREdetakRFVADPFVPGERMYrTGDL-VKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQ 1457
Cdd:cd05922 309 PGEPGEIVHRGPNVMKGYWNDP-----PYRRKEGRGGGVLH-TGDLaRRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAA 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2214269206 1458 LAQLSEVQDAAVTAVKDKGGNTAIAAYVTPETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05922 383 ARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1078-1531 |
3.76e-48 |
|
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: 179.17 E-value: 3.76e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1078 WTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKlllkqe 1157
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS------ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1158 gisvpdsytgdVILLDGSrtilslpldendegnpetavtaENLAYMIYTSGTTGQPKGVMVEHHAL------VNLCfwhH 1231
Cdd:cd05971 81 -----------ALVTDGS----------------------DDPALIIYTSGTTGPPKGALHAHRVLlghlpgVQFP---F 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1232 DAFSMTAED--RSAKYAGFG--FDAsiweMFPTWTIGAELhVIDEAIRLDIVRLNDYFETNGVTITFLP-TQL---AEQF 1303
Cdd:cd05971 125 NLFPRDGDLywTPADWAWIGglLDV----LLPSLYFGVPV-LAHRMTKFDPKAALDLMSRYGVTTAFLPpTALkmmRQQG 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1304 MELENT--SLRVLLTGGDKL--------KRAVKKPytlVNN-YGPTE-NTVVATSAEIHPEEGSlSIGRAIANTRVYILG 1371
Cdd:cd05971 200 EQLKHAqvKLRAIATGGESLgeellgwaREQFGVE---VNEfYGQTEcNLVIGNCSALFPIKPG-SMGKPIPGHRVAIVD 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1372 EGNQVQPEGVAGELCV----AGRGLarGYLNREDETAKRFVADPFvpgermyRTGDLVKWVNGG-IEYIGRIDQQVKVRG 1446
Cdd:cd05971 276 DNGTPLPPGEVGEIAVelpdPVAFL--GYWNNPSATEKKMAGDWL-------LTGDLGRKDSDGyFWYVGRDDDVITSSG 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1447 YRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVT--PETADIEALKSTLKE----TLPDYMIPAFWVTLNELPV 1520
Cdd:cd05971 347 YRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnPGETPSDALAREIQElvktRLAAHEYPREIEFVNELPR 426
|
490
....*....|.
gi 2214269206 1521 TANGKVDRKAL 1531
Cdd:cd05971 427 TATGKIRRREL 437
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1076-1534 |
5.42e-48 |
|
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: 181.18 E-value: 5.42e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1076 QSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLL-- 1153
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLiv 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1154 LKQEGISV-PDSytgdvilldgsrtilslpldendegNPETAvtaenlaymiYTSGTTGQPKGVMVEHHALVNLCFWHHD 1232
Cdd:cd17647 99 IRAAGVVVgPDS-------------------------NPTLS----------FTSGSEGIPKGVLGRHFSLAYYFPWMAK 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1233 AFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVideAIRLDIV---RLNDYFETNGVTIT--------FLPTQLAE 1301
Cdd:cd17647 144 RFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLV---PTQDDIGtpgRLAEWMAKYGATVThltpamgqLLTAQATT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1302 QFMELentsLRVLLTGGDKLKRAVKKPYTLVNN------YGPTENTVVATSAEIhPEEGS-----------LSIGRAIAN 1364
Cdd:cd17647 221 PFPKL----HHAFFVGDILTKRDCLRLQTLAENvrivnmYGTTETQRAVSYFEV-PSRSSdptflknlkdvMPAGRGMLN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1365 TRVYILGEGNQVQPEGVA--GELCVAGRGLARGYLNREDETAKRFVADPFV----------------------PGERMYR 1420
Cdd:cd17647 296 VQLLVVNRNDRTQICGIGevGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVepdhwnyldkdnnepwrqfwlgPRDRLYR 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1421 TGDLVKWV-NGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPETADIEA----- 1494
Cdd:cd17647 376 TGDLGRYLpNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDesfaq 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 1495 -------------------------LKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEP 1534
Cdd:cd17647 456 edvpkevstdpivkgligyrklikdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
22-501 |
1.07e-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: 178.25 E-value: 1.07e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 22 DHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNE-DIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSL 100
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDLRgDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 101 EDSGAKFAVvnernmtaigqyegiivslddgkwrneskerpssisgsrNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWF 180
Cdd:cd05941 81 TDSEPSLVL---------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 181 SEEAGLTENDktVLLssYAFDLGYT-SMFPVLLG----GGELHIVQKETytaPDEIAHYIKEHGIT--------YIKLTP 247
Cdd:cd05941 122 VDAWRWTEDD--VLL--HVLPLHHVhGLVNALLCplfaGASVEFLPKFD---PKEVAISRLMPSITvfmgvptiYTRLLQ 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 248 SLFHTIVNTASFAKDAnFESLRLIVlGGEKIIPTDVIA-FRKMYGHTeFINHYGPTEatIGaiagrVDLYEPDAFAKRP- 325
Cdd:cd05941 195 YYEAHFTDPQFARAAA-AERLRLMV-SGSAALPVPTLEeWEAITGHT-LLERYGMTE--IG-----MALSNPLDGERRPg 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 326 TIGRPIANAGA-LVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAF 404
Cdd:cd05941 265 TVGMPLPGVQArIVDEETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDEDGYYWI 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 405 IGR-ADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGL-QELCAYYT---SDQDIEKAELRYQLSLTLPSHMIP 479
Cdd:cd05941 339 LGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWgERVVAVVVlraGAAALSLEELKEWAKQRLAPYKRP 418
|
490 500
....*....|....*....|..
gi 2214269206 480 AFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd05941 419 RRLILVDELPRNAMGKVNKKEL 440
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1068-1531 |
1.53e-47 |
|
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: 177.27 E-value: 1.53e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1068 RPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQD 1147
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1148 SGAKLLLkqegisvpdsytgdvilldgsrtilslpldendegnpetaVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLC 1227
Cdd:cd05919 81 CEARLVV----------------------------------------TSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1228 -FWHHDAFSMTAEDR---SAK-YAGFGFDASIWemFPtWTIGAELHVID-----EAIRLDIVRLndyfetnGVTITF-LP 1296
Cdd:cd05919 121 dAMAREALGLTPGDRvfsSAKmFFGYGLGNSLW--FP-LAVGASAVLNPgwptaERVLATLARF-------RPTVLYgVP 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1297 TQLAE-----QFMELENTSLRVLLTGGDKLKRAVKKPYT------LVNNYGPTENTVVATSAEihPEEGSL-SIGRAIAN 1364
Cdd:cd05919 191 TFYANlldscAGSPDALRSLRLCVSAGEALPRGLGERWMehfggpILDGIGATEVGHIFLSNR--PGAWRLgSTGRPVPG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1365 TRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVadpfvpgERMYRTGDLVKW-VNGGIEYIGRIDQQVK 1443
Cdd:cd05919 269 YEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFN-------GGWYRTGDKFCRdADGWYTHAGRADDMLK 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1444 VRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPET------ADIEALKSTLKETLPDYMIPAFWVTLNE 1517
Cdd:cd05919 342 VGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSpaapqeSLARDIHRHLLERLSAHKVPRRIAFVDE 421
|
490
....*....|....
gi 2214269206 1518 LPVTANGKVDRKAL 1531
Cdd:cd05919 422 LPRTATGKLQRFKL 435
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1053-1533 |
1.73e-47 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 179.33 E-value: 1.73e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1053 TVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPI 1132
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1133 DPDYPDQRIEYILQDSGAKLLLKQEGIsVPDSYTGDVILLDgSRTILSLPLDENDEGNPET-----------------AV 1195
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLGLF-LGVDYSATTRLPA-LEHVVICETEEDDPHTEKMktftdflaagdpaerapEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1196 TAENLAYMIYTSGTTGQPKGVMVEHHALVnlcfwhhDAFSMTAEdrsakYAGfgfdasiwemfptwtigaelhvIDEAIR 1275
Cdd:PRK07656 164 DPDDVADILFTSGTTGRPKGAMLTHRQLL-------SNAADWAE-----YLG----------------------LTEGDR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1276 LDIVrlNDYFET------------NGVTITFLPTQLAEQFMEL-EN---------------------------TSLRVLL 1315
Cdd:PRK07656 210 YLAA--NPFFHVfgykagvnaplmRGATILPLPVFDPDEVFRLiETeritvlpgpptmynsllqhpdrsaedlSSLRLAV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1316 TGGD----KLKRAVKKPY---TLVNNYGPTENTVVATSAEIH--PEEGSLSIGRAIANTRVYILGEGNQVQPEGVAGELC 1386
Cdd:PRK07656 288 TGAAsmpvALLERFESELgvdIVLTGYGLSEASGVTTFNRLDddRKTVAGTIGTAIAGVENKIVNELGEEVPVGEVGELL 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1387 VAGRGLARGYLNREDETAKRFVADPFVpgermyRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQ 1465
Cdd:PRK07656 368 VRGPNVMKGYYDDPEATAAAIDADGWL------HTGDLGRLDEEGYLYIvDRKKDMFIVGGFNVYPAEVEEVLYEHPAVA 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 1466 DAAVTAVKDKGGNTAIAAYVTP---ETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPE 1533
Cdd:PRK07656 442 EAAVIGVPDERLGEVGKAYVVLkpgAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1067-1533 |
2.20e-47 |
|
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: 178.66 E-value: 2.20e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPA--VTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYI 1144
Cdd:cd05926 2 DAPAlvVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1145 LQDSGAKLLLKQEGISVPDS--------YTGDVILLDGSRTI------LSLPLDENDEGNPETAVTAENLAYMIYTSGTT 1210
Cdd:cd05926 82 LADLGSKLVLTPKGELGPASraasklglAILELALDVGVLIRapsaesLSNLLADKKNAKSEGVPLPDDLALILHTSGTT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1211 GQPKGVMVEHHalvNLCFWHHD---AFSMTAEDR------------------SAKYAG------FGFDAS-IWEMF---- 1258
Cdd:cd05926 162 GRPKGVPLTHR---NLAASATNitnTYKLTPDDRtlvvmplfhvhglvasllSTLAAGgsvvlpPRFSAStFWPDVrdyn 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1259 PTWtigaeLHVIDEAIRLDIVRLNDYFETNGVTITFLPT---QLAEQFMElentslrvlltggdKLKRAVKKPytLVNNY 1335
Cdd:cd05926 239 ATW-----YTAVPTIHQILLNRPEPNPESPPPKLRFIRScsaSLPPAVLE--------------ALEATFGAP--VLEAY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1336 GPTENTVVATSAEIHPEEGSL-SIGRAiANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvp 1414
Cdd:cd05926 298 GMTEAAHQMTSNPLPPGPRKPgSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1415 germYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE---TA 1490
Cdd:cd05926 375 ----FRTGDLGYLDADGYLFLtGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLRegaSV 450
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 2214269206 1491 DIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPE 1533
Cdd:cd05926 451 TEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1067-1531 |
1.27e-45 |
|
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: 173.71 E-value: 1.27e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:cd05959 19 DKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLKQE----------GISVPDSYTgdVILLDGSRTILSLPLDEND----EGNPETAVT-AENLAYMIYTSGTTG 1211
Cdd:cd05959 99 DSRARVVVVSGelapvlaaalTKSEHTLVV--LIVSGGAGPEAGALLLAELvaaeAEQLKPAAThADDPAFWLYSSGSTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1212 QPKGVMVEHHALVNLC-FWHHDAFSMTAEDR---SAK-YAGFGFDASIweMFPTWtIGAElhVIDEAIRLDIVRLNDYFE 1286
Cdd:cd05959 177 RPKGVVHLHADIYWTAeLYARNVLGIREDDVcfsAAKlFFAYGLGNSL--TFPLS-VGAT--TVLMPERPTPAAVFKRIR 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1287 TNGVTITF-LPTQLA-----EQFMELENTSLRVLLTGGDKLKRAV----KKPY--TLVNNYGPTENTVVATS---AEIHP 1351
Cdd:cd05959 252 RYRPTVFFgVPTLYAamlaaPNLPSRDLSSLRLCVSAGEALPAEVgerwKARFglDILDGIGSTEMLHIFLSnrpGRVRY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1352 EegslSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVadpfvpGErMYRTGDlvKWV--- 1428
Cdd:cd05959 332 G----TTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------GE-WTRTGD--KYVrdd 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1429 NGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP------ETADIEALKSTLKET 1502
Cdd:cd05959 399 DGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLrpgyedSEALEEELKEFVKDR 478
|
490 500
....*....|....*....|....*....
gi 2214269206 1503 LPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05959 479 LAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
33-501 |
3.52e-45 |
|
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: 172.11 E-value: 3.52e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVV-N 111
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTpK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 112 ERNMTAI--------------GQYEGIIVSLDDGKWRNESKERPSSISGSRNL----AYVIYTSGTTGKPKGVQIEHRNL 173
Cdd:cd05926 95 GELGPASraasklglailelaLDVGVLIRAPSAESLSNLLADKKNAKSEGVPLpddlALILHTSGTTGRPKGVPLTHRNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 174 TNYVSWFSEEAGLTENDKTVLLssyafdlgyTSMF----------PVLLGGGELHIvqketytAPDEIAH----YIKEHG 239
Cdd:cd05926 175 AASATNITNTYKLTPDDRTLVV---------MPLFhvhglvasllSTLAAGGSVVL-------PPRFSAStfwpDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 240 ITYIKLTPSLFHTIVNTASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGhTEFINHYGPTEATIGAIAGRVdlyePD 319
Cdd:cd05926 239 ATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATFG-APVLEAYGMTEAAHQMTSNPL----PP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 320 AFAKRPTIGRPiANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSD 399
Cdd:cd05926 314 GPRKPGSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLDAD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 400 GTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGL-QELCAYYT--SDQDIEKAELRYQLSLTLPSH 476
Cdd:cd05926 387 GYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYgEEVAAAVVlrEGASVTEEELRAFCRKHLAAF 466
|
490 500
....*....|....*....|....*
gi 2214269206 477 MIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd05926 467 KVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
609-1018 |
1.18e-44 |
|
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: 167.75 E-value: 1.18e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 609 PLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKA-------E 681
Cdd:cd19537 3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPprvqrvdT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 682 VDLHvfeakedeadqkiKEFIRPFDLNDAPLIRAALlrieAKKHLLLLdMHHIIADGVSRGIFVKELALLYKGEQLPEPT 761
Cdd:cd19537 83 LDVW-------------KEINRPFDLEREDPIRVFI----SPDTLLVV-MSHIICDLTTLQLLLREVSAAYNGKLLPPVR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 762 LHYKDFAVWQNEAEQkermkEHEAYWMSVLSGeLPELDLPldyARPPVQSFKGDTIRFRTGSETAKAVEKLLAETGTTLH 841
Cdd:cd19537 145 REYLDSTAWSRPASP-----EDLDFWSEYLSG-LPLLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLH 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 842 -MVLHAVFHVfLSKISGQRDIVIGSVTAGRTNADVQDMPGMFVNTLALR--MEAKEQQTFAELLELAKQTNLSALEHQeY 918
Cdd:cd19537 216 qLALAAVALA-LQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRirFPSSSDASAADFLRAVRRSSQAALAHA-I 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 919 PFEDLVNQLDLPRDMSRNPLFNVMVTTENPDKEQLTLQNLSISPYEAHQGTSKFDLtLGGFT--DENGIGLQLEYATDLF 996
Cdd:cd19537 294 PWHQLLEHLGLPPDSPNHPLFDVMVTFHDDRGVSLALPIPGVEPLYTWAEGAKFPL-MFEFTalSDDSLLLRLEYDTDCF 372
|
410 420
....*....|....*....|..
gi 2214269206 997 AKETAEKWSEYVLRLLKAVADN 1018
Cdd:cd19537 373 SEEEIDRIESLILAALELLVEG 394
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
33-501 |
1.28e-44 |
|
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: 168.29 E-value: 1.28e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGakfavvne 112
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 rnmtaigqyegiiVSLDDgkwrneskerpssisgsrnLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKT 192
Cdd:cd05912 74 -------------VKLDD-------------------IATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNW 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 193 vLLSSYAFDL-GYTSMFPVLLGGGELHIVQKetyTAPDEIAHYIKEHGITYIKLTPSLFHTIVntasfAKDANF--ESLR 269
Cdd:cd05912 122 -LCALPLFHIsGLSILMRSVIYGMTVYLVDK---FDAEQVLHLINSGKVTIISVVPTMLQRLL-----EILGEGypNNLR 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 270 LIVLGGEKiIPTDVIAFRKMYGhTEFINHYGPTEATIGAIAgrvdLYEPDAFAKRPTIGRPIANAGALVLNEalkLVPPG 349
Cdd:cd05912 193 CILLGGGP-APKPLLEQCKEKG-IPVYQSYGMTETCSQIVT----LSPEDALNKIGSAGKPLFPVELKIEDD---GQPPY 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 350 ASGQLYITGQGLARGYLNRPQLTAERFvENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVML 429
Cdd:cd05912 264 EVGEILLKGPNVTKGYLNRPDATEESF-ENGW------FKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLL 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2214269206 430 SLSGIQEAVVLAV--SEGGlQELCAYYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd05912 337 SHPAIKEAGVVGIpdDKWG-QVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1078-1531 |
3.64e-44 |
|
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: 167.13 E-value: 3.64e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1078 WTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLkqe 1157
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1158 gisvpdsytgdvilldgsrtilslpldendegnpetaVTAENLAYMIYTSGTTGQPKGVMVEHHA----LVNLCFWH--- 1230
Cdd:cd05972 78 -------------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYplghIPTAAYWLglr 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1231 -HDAFSMTAEDRSAKYAGFGFdasiweMFPtWTIGAELhVIDEAIRLDIVRLNDYFETNGVTITFLPTQLAEQFMELENT 1309
Cdd:cd05972 121 pDDIHWNIADPGWAKGAWSSF------FGP-WLLGATV-FVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLS 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1310 S-----LRVLLTGGDKLKRAVKKPY------TLVNNYGPTENT-VVATSAEIHPEEGslSIGRAIANTRVYILGEGNQVQ 1377
Cdd:cd05972 193 SykfshLRLVVSAGEPLNPEVIEWWraatglPIRDGYGQTETGlTVGNFPDMPVKPG--SMGRPTPGYDVAIIDDDGREL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1378 PEGVAGELCV--AGRGLARGYLNREDETAKRFVADPFVPGERMYRTGDlvkwvnGGIEYIGRIDQQVKVRGYRIELSEIE 1455
Cdd:cd05972 271 PPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGDYYLTGDRAYRDED------GYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1456 VQLAQLSEVQDAAVTAVKDKGGNTAIAAYV------TPETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRK 1529
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVvltsgyEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRV 424
|
..
gi 2214269206 1530 AL 1531
Cdd:cd05972 425 EL 426
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
21-501 |
1.43e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 167.86 E-value: 1.43e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 21 PDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSL 100
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 101 EDSGAKFAVVN-----ERNMTAIGQYEGI--IVSLDDGKW--------RNESKERPSSISGSRNLAYVIYTSGTTGKPKG 165
Cdd:PRK06188 106 EDAGISTLIVDpapfvERALALLARVPSLkhVLTLGPVPDgvdllaaaAKFGPAPLVAAALPPDIAGLAYTGGTTGKPKG 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 166 VQIEHRNLTNYVSWFSEEAGLTENDKTVLLS--SYAfdlGYTSMFPVLLGGGELHIVQKetyTAPDEIAHYIKEHGITYI 243
Cdd:PRK06188 186 VMGTHRSIATMAQIQLAEWEWPADPRFLMCTplSHA---GGAFFLPTLLRGGTVIVLAK---FDPAEVLRAIEEQRITAT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 244 KLTPSLFHTIVNTASFAkDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTeFINHYGPTEATIGAIAGRVDLYEPDAFAK 323
Cdd:PRK06188 260 FLVPTMIYALLDHPDLR-TRDLSSLETVYYGASPMSPVRLAEAIERFGPI-FAQYYGQTEAPMVITYLRKRDHDPDDPKR 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 324 RPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVEnpyspGSLmyKTGDVVRRLSDGTLA 403
Cdd:PRK06188 338 LTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRD-----GWL--HTGDVAREDEDGFYY 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 404 FIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQEL---CAYYTSDQDIEKAELRYQLSLTLPSHMIPA 480
Cdd:PRK06188 411 IVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAvtaVVVLRPGAAVDAAELQAHVKERKGSVHAPK 490
|
490 500
....*....|....*....|.
gi 2214269206 481 FFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK06188 491 QVDFVDSLPLTALGKPDKKAL 511
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
33-495 |
4.16e-43 |
|
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: 164.48 E-value: 4.16e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNE 112
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 RnmtaigqyegiivslddgkWRnesKERPSSISGSrnLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKT 192
Cdd:cd05903 82 R-------------------FR---QFDPAAMPDA--VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 193 VLLSSYAFDLG--YTSMFPVLLGGGelhIVQKETYTaPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAkDANFESLRL 270
Cdd:cd05903 138 LVASPMAHQTGfvYGFTLPLLLGAP---VVLQDIWD-PDKALALMREHGVTFMMGATPFLTDLLNAVEEA-GEPLSRLRT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 271 IVLGGEKiIPTDVIAFRKMYGHTEFINHYGPTEATigAIAGRVDLYEPDAFAKrpTIGRPIANAGALVLNEALKLVPPGA 350
Cdd:cd05903 213 FVCGGAT-VPRSLARRAAELLGAKVCSAYGSTECP--GAVTSITPAPEDRRLY--TDGRPLPGVEIKVVDDTGATLAPGV 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 351 SGQLYITGQGLARGYLNRPQLTAERFVEnpyspgsLMYKTGDVVRRLSDGTLAFIGRADDqVKIR-GYRIEPKEIETVML 429
Cdd:cd05903 288 EGELLSRGPSVFLGYLDRPDLTADAAPE-------GWFRTGDLARLDEDGYLRITGRSKD-IIIRgGENIPVLEVEDLLL 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 430 SLSGIQEAVVLAVSEGGLQE-LCAYYT--SDQDIEKAELR-YQLSLTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:cd05903 360 GHPGVIEAAVVALPDERLGErACAVVVtkSGALLTFDELVaYLDRQGVAKQYWPERLVHVDDLPRTPSGK 429
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
33-501 |
3.24e-42 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 161.74 E-value: 3.24e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKfavvne 112
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAK------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 rnmtaigqyeGIIVSLDDgkwrneskerpssisgsrnLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDK- 191
Cdd:cd05972 75 ----------AIVTDAED-------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIh 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 192 -TVLLSSYAFDLGYTSMFPVLLGggeLHIVqkeTYTA----PDEIAHYIKEHGITYIKLTPSLFHTI--VNTASFakdaN 264
Cdd:cd05972 126 wNIADPGWAKGAWSSFFGPWLLG---ATVF---VYEGprfdAERILELLERYGVTSFCGPPTAYRMLikQDLSSY----K 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 265 FESLRLIVLGGEKIIPTDVIAFRKMYGHTeFINHYGPTE--ATIGAIagrvdlyePDAFAKRPTIGRPIANAGALVLNEA 342
Cdd:cd05972 196 FSHLRLVVSAGEPLNPEVIEWWRAATGLP-IRDGYGQTEtgLTVGNF--------PDMPVKPGSMGRPTPGYDVAIIDDD 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 343 LKLVPPGASGQLYI--TGQGLARGYLNRPQLTAERFVENpyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIE 420
Cdd:cd05972 267 GRELPPGEEGDIAIklPPPGLFLGYVGDPEKTEASIRGD-------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIG 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 421 PKEIETVMLSLSGIQEAVVLAVSEGGLQELC--------AYYTSDQDIEkaELRYQLSLTLPSHMIPAFFVQVDAIPLTA 492
Cdd:cd05972 340 PFEVESALLEHPAVAEAAVVGSPDPVRGEVVkafvvltsGYEPSEELAE--ELQGHVKKVLAPYKYPREIEFVEELPKTI 417
|
....*....
gi 2214269206 493 NGKTDRNAL 501
Cdd:cd05972 418 SGKIRRVEL 426
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
15-501 |
3.67e-42 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 162.82 E-value: 3.67e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 15 KQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEE 94
Cdd:PRK03640 10 QRAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSRE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 95 RIRYSLEDSGAKFAVVNERNMTAIgqYEGIIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNlt 174
Cdd:PRK03640 90 ELLWQLDDAEVKCLITDDDFEAKL--IPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGN-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 175 nyvSWFS-----EEAGLTENDKTvLLSSYAFDL-GYTSMFPVLLGGGELHIVQKetYTApDEIAHYIKEHGITYIKLTPS 248
Cdd:PRK03640 166 ---HWWSavgsaLNLGLTEDDCW-LAAVPIFHIsGLSILMRSVIYGMRVVLVEK--FDA-EKINKLLQTGGVTIISVVST 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 249 LFHTIVntASFAKDANFESLRLIVLGG------------EKIIPtdVIafrKMYGHTEfinhygpTEATIgaiagrVDLY 316
Cdd:PRK03640 239 MLQRLL--ERLGEGTYPSSFRCMLLGGgpapkplleqckEKGIP--VY---QSYGMTE-------TASQI------VTLS 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 317 EPDAFAKRPTIGRPIANAGaLVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpyspgslMYKTGDVVRR 396
Cdd:PRK03640 299 PEDALTKLGSAGKPLFPCE-LKIEKDGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDG-------WFKTGDIGYL 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 397 LSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEG--GlQELCAYYTSDQDIEKAELRYQLSLTLP 474
Cdd:PRK03640 371 DEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDkwG-QVPVAFVVKSGEVTEEELRHFCEEKLA 449
|
490 500
....*....|....*....|....*..
gi 2214269206 475 SHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK03640 450 KYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1048-1533 |
9.98e-42 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 163.01 E-value: 9.98e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1048 VPTDKTVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGA 1127
Cdd:PRK06155 17 PPSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1128 AFVPIDPDYPDQRIEYILQDSGAKLLLKQ-------EGISVPDSYTGDVILLDGS------RTILSLPLDENDEGNPETA 1194
Cdd:PRK06155 97 IAVPINTALRGPQLEHILRNSGARLLVVEaallaalEAADPGDLPLPAVWLLDAPasvsvpAGWSTAPLPPLDAPAPAAA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1195 VTAENLAYMIYTSGTTGQPKGVMVEHHALvnlcFW--HHDAFSMTAEDRSAKYAGFG-FDASIWEMF-PTWTIGAELHVI 1270
Cdd:PRK06155 177 VQPGDTAAILYTSGTTGPSKGVCCPHAQF----YWwgRNSAEDLEIGADDVLYTTLPlFHTNALNAFfQALLAGATYVLE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1271 DeaiRLDIVRLNDYFETNGVTITFL-----PTQLAEQFMELENTS-LRVLLTGGdkLKRAVKKPY------TLVNNYGPT 1338
Cdd:PRK06155 253 P---RFSASGFWPAVRRHGATVTYLlgamvSILLSQPARESDRAHrVRVALGPG--VPAALHAAFrerfgvDLLDGYGST 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1339 E-NTVVATSaeiHPEEGSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGR---GLARGYLNREDETAKRFVADPFVP 1414
Cdd:PRK06155 328 EtNFVIAVT---HGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEAWRNLWFHT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1415 GERMYRTGDlvkwvnGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE---TAD 1491
Cdd:PRK06155 405 GDRVVRDAD------GWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRdgtALE 478
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2214269206 1492 IEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPE 1533
Cdd:PRK06155 479 PVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
17-501 |
2.95e-41 |
|
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: 160.37 E-value: 2.95e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 17 AQQTPDHSAV--KAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEE 94
Cdd:cd05923 11 ASRAPDACAIadPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 95 RIRYSLEDSGAKFAV--VNERNMTAIGQYEGIIVSLDD----GKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQI 168
Cdd:cd05923 91 ELAELIERGEMTAAViaVDAQVMDAIFQSGVRVLALSDlvglGEPESAGPLIEDPPREPEQPAFVFYTSGTTGLPKGAVI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 169 EHRNLTNYVSWFSEEAGLTENDKTVLLSSYAF--DLGYTSMFPVLLGGGELHIVQkeTYTAPDEIAHYIKEHGITYIKLT 246
Cdd:cd05923 171 PQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLyhVIGFFAVLVAALALDGTYVVV--EEFDPADALKLIEQERVTSLFAT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 247 PSLFHTIVNTASFAKdANFESLRLIVLGGEKIipTDVIaFRKMYGH--TEFINHYGPTEATigaiagrVDLYEPDAfaKR 324
Cdd:cd05923 249 PTHLDALAAAAEFAG-LKLSSLRHVTFAGATM--PDAV-LERVNQHlpGEKVNIYGTTEAM-------NSLYMRDA--RT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 325 PTIGRPIANAG---ALVLNEALKLVPPGASGQLYITGQGLA--RGYLNRPQLTAERFVENpyspgslMYKTGDVVRRLSD 399
Cdd:cd05923 316 GTEMRPGFFSEvriVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQDG-------WYRTGDVGYVDPS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 400 GTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVS-EGGLQELCAYYTSDQDIEKAELRYQLSLT--LPSH 476
Cdd:cd05923 389 GDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVAdERWGQSVTACVVPREGTLSADELDQFCRAseLADF 468
|
490 500
....*....|....*....|....*
gi 2214269206 477 MIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd05923 469 KRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
33-501 |
3.60e-41 |
|
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: 158.82 E-value: 3.60e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNE 112
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 RnmtaigqyegiivslddgKWRNESKERPssisgsrnlAYVIYTSGTTGKPKGVQIEHRNLTNYvsWFSEEA--GLTEND 190
Cdd:cd05969 81 E------------------LYERTDPEDP---------TLLHYTSGTTGTPKGVLHVHDAMIFY--YFTGKYvlDLHPDD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 191 KTVLLSSYAFDLGYT-SMFPVLLGGgeLHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNT-ASFAKDANFESL 268
Cdd:cd05969 132 IYWCTADPGWVTGTVyGIWAPWLNG--VTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgDELARKYDLSSL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 269 RLIVLGGEKIIPTDVIAFRKMYGhTEFINHYGPTEATIGAIAGRvdlyePDAFAKRPTIGRPIANAGALVLNEALKLVPP 348
Cdd:cd05969 210 RFIHSVGEPLNPEAIRWGMEVFG-VPIHDTWWQTETGSIMIANY-----PCMPIKPGSMGKPLPGVKAAVVDENGNELPP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 349 GASGQLYITGQ--GLARGYLNRPQLTAERFVENpyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIET 426
Cdd:cd05969 284 GTKGILALKPGwpSMFRGIWNDEERYKNSFIDG-------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVES 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 427 VMLSLSGIQEAVVLAVSEGGLQELC-AYYTSDQDIE-----KAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNA 500
Cdd:cd05969 357 ALMEHPAVAEAGVIGKPDPLRGEIIkAFISLKEGFEpsdelKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRV 436
|
.
gi 2214269206 501 L 501
Cdd:cd05969 437 L 437
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
33-503 |
5.20e-41 |
|
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: 158.45 E-value: 5.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNE 112
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 RNMTaigqyegiivSLDDGkwrneskerpssisgsrnLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKT 192
Cdd:cd05973 81 ANRH----------KLDSD------------------PFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 193 VLLSS--YAFDLGYTSMFPVLLGGGELHIvqkETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAKDANFESLRL 270
Cdd:cd05973 133 WNAADpgWAYGLYYAITGPLALGHPTILL---EGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEVPARPKGRLRR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 271 IVLGGEKIIPTDVIAFRKMYGhTEFINHYGPTEATIgAIAGRVDLYEPdafAKRPTIGRPIANAGALVLNEALKLVPPGA 350
Cdd:cd05973 210 VSSAGEPLTPEVIRWFDAALG-VPIHDHYGQTELGM-VLANHHALEHP---VHAGSAGRAMPGWRVAVLDDDGDELGPGE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 351 SGQLYITGQGLA----RGYLNRPQLTaerfvenpysPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIET 426
Cdd:cd05973 285 PGRLAIDIANSPlmwfRGYQLPDTPA----------IDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 427 VMLSLSGIQEAVVLAVSEGGLQE-------LCAYYTSDQDIEKaELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRN 499
Cdd:cd05973 355 ALIEHPAVAEAAVIGVPDPERTEvvkafvvLRGGHEGTPALAD-ELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRF 433
|
....
gi 2214269206 500 ALPK 503
Cdd:cd05973 434 LLRR 437
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
8-501 |
5.45e-41 |
|
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: 159.42 E-value: 5.45e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 8 TFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPI 87
Cdd:cd05920 16 PLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 88 DPDTPEERIRYSLEDSGAKFAVVNERNmtaigqyegiivSLDDGkwRNESKERPSSIsgsRNLAYVIYTSGTTGKPKGVQ 167
Cdd:cd05920 96 LPSHRRSELSAFCAHAEAVAYIVPDRH------------AGFDH--RALARELAESI---PEVALFLLSGGTTGTPKLIP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 168 IEHRNLTNYVSWFSEEAGLTENDK--TVLLSSYAFDLGYTSMFPVLLGGGELHIVQKetyTAPDEIAHYIKEHGITYIKL 245
Cdd:cd05920 159 RTHNDYAYNVRASAEVCGLDQDTVylAVLPAAHNFPLACPGVLGTLLAGGRVVLAPD---PSPDAAFPLIEREGVTVTAL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 246 TPSLFHTIVNTASFAKDAnFESLRLIVLGGEKIIPTDVIAFRKMYGHTeFINHYGPTEATIGAIagRVDlyEPDAfAKRP 325
Cdd:cd05920 236 VPALVSLWLDAAASRRAD-LSSLRLLQVGGARLSPALARRVPPVLGCT-LQQVFGMAEGLLNYT--RLD--DPDE-VIIH 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 326 TIGRPI-ANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAF 404
Cdd:cd05920 309 TQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 405 IGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQE-LCAYYT-SDQDIEKAELRYQL-SLTLPSHMIPAF 481
Cdd:cd05920 383 EGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGErSCAFVVlRDPPPSAAQLRRFLrERGLAAYKLPDR 462
|
490 500
....*....|....*....|
gi 2214269206 482 FVQVDAIPLTANGKTDRNAL 501
Cdd:cd05920 463 IEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1053-1526 |
6.71e-41 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 160.10 E-value: 6.71e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1053 TVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPI 1132
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1133 DPDYPDQRIEYILQDSGAKLLLKQEGISVPDSYTGDVILLDGSRTILSLPLDENDEG--------------NPETAVTAE 1198
Cdd:PRK08316 92 NFMLTGEELAYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGwldfadwaeagsvaEPDVELADD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1199 NLAYMIYTSGTTGQPKGVMVEHHALVnlcfwhHD------AFSMTAEDR---------SAKYAGFgfdasiweMFPTWTI 1263
Cdd:PRK08316 172 DLAQILYTSGTESLPKGAMLTHRALI------AEyvscivAGDMSADDIplhalplyhCAQLDVF--------LGPYLYV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1264 GAELHVIDEAirlDIVRLNDYFETNGVTITFLPTQL------AEQFMELENTSLR------------VLLTGGDKLKRAv 1325
Cdd:PRK08316 238 GATNVILDAP---DPELILRTIEAERITSFFAPPTVwisllrHPDFDTRDLSSLRkgyygasimpveVLKELRERLPGL- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1326 kkpyTLVNNYGPTENTVVAT--SAEIHPEEGSlSIGRAIAN--TRVyILGEGNQVqPEGVAGELCVAGRGLARGYLNRED 1401
Cdd:PRK08316 314 ----RFYNCYGQTEIAPLATvlGPEEHLRRPG-SAGRPVLNveTRV-VDDDGNDV-APGEVGEIVHRSPQLMLGYWDDPE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1402 ETAKRFVADPFvpgermyRTGDL-VKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTA 1480
Cdd:PRK08316 387 KTAEAFRGGWF-------HSGDLgVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEA 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2214269206 1481 IAAYVTP---ETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKV 1526
Cdd:PRK08316 460 VTAVVVPkagATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
14-501 |
7.39e-41 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 159.26 E-value: 7.39e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 14 EKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQ-GAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTP 92
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 93 EERIRYSLEDSGAKFAVVNERNMTAIGQYEGII-----VSLDDGKwRNESKERPSSISGSRNLAYVI-YTSGTTGKPKGV 166
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNMALSMQKVSyvqrvISITSLK-EIEDRKIDNFVEKNESASFIIcYTSGTTGKPKGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 167 QIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYaFDLGYTSMF--PVLLGGGELHIVQKetyTAPDEIAHYIKEHGITYIK 244
Cdd:PRK06839 168 VLTQENMFWNALNNTFAIDLTMHDRSIVLLPL-FHIGGIGLFafPTLFAGGVIIVPRK---FEPTKALSMIEKHKVTVVM 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 245 LTPSLFHTIVNTASFAKdANFESLRLIVLGGEKIiPTDVIA--------FRKMYGHTEfinhygpTEATIGAIAgrvdly 316
Cdd:PRK06839 244 GVPTIHQALINCSKFET-TNLQSVRWFYNGGAPC-PEELMRefidrgflFGQGFGMTE-------TSPTVFMLS------ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 317 EPDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERfVENPYspgslmYKTGDVVRR 396
Cdd:PRK06839 309 EEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW------LCTGDLARV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 397 LSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYT---SDQDIEKAELRYQLSLTL 473
Cdd:PRK06839 382 DEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIvkkSSSVLIEKDVIEHCRLFL 461
|
490 500
....*....|....*....|....*...
gi 2214269206 474 PSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK06839 462 AKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
34-501 |
7.33e-40 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 154.90 E-value: 7.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKfAVVNEr 113
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS-ALVTD- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 114 nmtaigqyegiivslddgkwrneskerpssisGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTV 193
Cdd:cd05971 86 --------------------------------GSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 194 LLSSYafDLGYTS-----MFPVLLGGGELhIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAKDANFEsL 268
Cdd:cd05971 134 YWTPA--DWAWIGglldvLLPSLYFGVPV-LAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVK-L 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 269 RLIVLGGEKIIPTDVIAFRKMYGHT--EFinhYGPTEATigAIAGRVdlyePDAFAKRP-TIGRPIANAGALVLNEALKL 345
Cdd:cd05971 210 RAIATGGESLGEELLGWAREQFGVEvnEF---YGQTECN--LVIGNC----SALFPIKPgSMGKPIPGHRVAIVDDNGTP 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 346 VPPGASGQLyitgqGLAR-------GYLNRPQLTAERFVenpyspGSLMyKTGDVVRRLSDGTLAFIGRADDQVKIRGYR 418
Cdd:cd05971 281 LPPGEVGEI-----AVELpdpvaflGYWNNPSATEKKMA------GDWL-LTGDLGRKDSDGYFWYVGRDDDVITSSGYR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 419 IEPKEIETVMLSLSGIQEA-----------------VVLAVSEGGLQELcayytsdqdieKAELRYQLSLTLPSHMIPAF 481
Cdd:cd05971 349 IGPAEIEECLLKHPAVLMAavvgipdpirgeivkafVVLNPGETPSDAL-----------AREIQELVKTRLAAHEYPRE 417
|
490 500
....*....|....*....|
gi 2214269206 482 FVQVDAIPLTANGKTDRNAL 501
Cdd:cd05971 418 IEFVNELPRTATGKIRRREL 437
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1064-1531 |
7.74e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 156.68 E-value: 7.74e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1064 RHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLE----MSAAVLgvlkAGAAFVPIDP--DYP 1137
Cdd:PRK06188 24 RYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEvlmaIGAAQL----AGLRRTALHPlgSLD 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1138 DQRieYILQDSGAKLLlkqegISVPDSYTGDVILL----DGSRTILSLP--------LDENDEGNPETAVTAE---NLAY 1202
Cdd:PRK06188 100 DHA--YVLEDAGISTL-----IVDPAPFVERALALlarvPSLKHVLTLGpvpdgvdlLAAAAKFGPAPLVAAAlppDIAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1203 MIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDR-----SAKYAGFGFdasiweMFPTWTIGAELHVIDeaiRLD 1277
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRflmctPLSHAGGAF------FLPTLLRGGTVIVLA---KFD 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1278 IVRLNDYFETNGVTITFL-PTQLaeqFMELEN--------TSLRVLLTGG-----DKLKRAVKK--PyTLVNNYGPTENT 1341
Cdd:PRK06188 244 PAEVLRAIEEQRITATFLvPTMI---YALLDHpdlrtrdlSSLETVYYGAspmspVRLAEAIERfgP-IFAQYYGQTEAP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1342 VVAT--SAEIHP---EEGSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFvADPFVpge 1416
Cdd:PRK06188 320 MVITylRKRDHDpddPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF-RDGWL--- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1417 rmyRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP---ETADI 1492
Cdd:PRK06188 396 ---HTGDVAREDEDGFYYIvDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLrpgAAVDA 472
|
490 500 510
....*....|....*....|....*....|....*....
gi 2214269206 1493 EALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK06188 473 AELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1063-1531 |
7.93e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 156.20 E-value: 7.93e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1063 QRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIE 1142
Cdd:PRK06145 13 RRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1143 YILQDSGAKLLLKQEGISVPDSYTGDVILLDGSRTILSLPLDENDEGNPETAVTAE-NLAYMIYTSGTTGQPKGVMVEHH 1221
Cdd:PRK06145 93 YILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADSRRLAQGGLEIPPQAAVAPtDLVRLMYTSGTTDRPKGVMHSYG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1222 ALVNLCFWHHDAFSMTAEDR----SAKYAGFGFD----ASIWEmfptwtiGAELHV--------IDEAIRLDivRLNDYF 1285
Cdd:PRK06145 173 NLHWKSIDHVIALGLTASERllvvGPLYHVGAFDlpgiAVLWV-------GGTLRIhrefdpeaVLAAIERH--RLTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1286 ETNGVTITFLPTQLAEQFmelENTSLRVLLTGGDKLK----RAVKKPYT---LVNNYGPTE----NTVVATSAEIhpeEG 1354
Cdd:PRK06145 244 MAPVMLSRVLTVPDRDRF---DLDSLAWCIGGGEKTPesriRDFTRVFTrarYIDAYGLTEtcsgDTLMEAGREI---EK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1355 SLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermyRTGDLVKWVNGGIEY 1434
Cdd:PRK06145 318 IGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1435 I-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKD-KGGN--TAIAAYVTPETADIEALKSTLKETLPDYMIPA 1510
Cdd:PRK06145 391 LtDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDdRWGEriTAVVVLNPGATLTLEALDRHCRQRLASFKVPR 470
|
490 500
....*....|....*....|.
gi 2214269206 1511 FWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK06145 471 QLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
9-504 |
8.35e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 155.53 E-value: 8.35e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 9 FAALFEKQAQQTPDHS-AVKAGGNLLTYRELDEQANQLAHHLRaqGAGNediVAIVMDRSAEVMVSILGVMKAGAAFLPI 87
Cdd:PRK07787 1 LASLNPAAVAAAADIAdAVRIGGRVLSRSDLAGAATAVAERVA--GARR---VAVLATPTLATVLAVVGALIAGVPVVPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 88 DPDTPEERIRYSLEDSGAKfAVVNERNMTAIGqYEGIIVSLDDGKWRNESKERPSSIsgsrnlAYVIYTSGTTGKPKGVQ 167
Cdd:PRK07787 76 PPDSGVAERRHILADSGAQ-AWLGPAPDDPAG-LPHVPVRLHARSWHRYPEPDPDAP------ALIVYTSGTTGPPKGVV 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 168 IEHRNLTNYVSWFSEEAGLTENDKTV----LLSSYAFDLGytsmfpvLLG----GGELHIVQKETytaPDEIAHYIKEHG 239
Cdd:PRK07787 148 LSRRAIAADLDALAEAWQWTADDVLVhglpLFHVHGLVLG-------VLGplriGNRFVHTGRPT---PEAYAQALSEGG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 240 ITYIKLtPSLFHTIVNTASFAKdaNFESLRLIVLGGEKIIPTDVIAFRKMYGHtEFINHYGPTEaTIGAIAGRVDlyepd 319
Cdd:PRK07787 218 TLYFGV-PTVWSRIAADPEAAR--ALRGARLLVSGSAALPVPVFDRLAALTGH-RPVERYGMTE-TLITLSTRAD----- 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 320 aFAKRP-TIGRPIANAGALVLNEALKLVPP-GAS-GQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRR 396
Cdd:PRK07787 288 -GERRPgWVGLPLAGVETRLVDEDGGPVPHdGETvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVV 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 397 LSDGTLAFIGR-ADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGL-QELCAYYTSDQDIEKAELRYQLSLTLP 474
Cdd:PRK07787 361 DPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLgQRIVAYVVGADDVAADELIDFVAQQLS 440
|
490 500 510
....*....|....*....|....*....|
gi 2214269206 475 SHMIPAFFVQVDAIPLTANGKTDRNALPKP 504
Cdd:PRK07787 441 VHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
33-501 |
1.07e-39 |
|
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: 154.17 E-value: 1.07e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNE 112
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 rnmtaigqyegiivSLDDgkwrneskerpssisgsrnLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKT 192
Cdd:cd05935 82 --------------ELDD-------------------LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 193 VLLSSYAFDLGYT-SMFPVLLGGGELHIVQK-ETYTAPDEIahyiKEHGITYIKLTPSLFHTIVNTASFaKDANFESLRl 270
Cdd:cd05935 129 LACLPLFHVTGFVgSLNTAVYVGGTYVLMARwDRETALELI----EKYKVTFWTNIPTMLVDLLATPEF-KTRDLSSLK- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 271 IVLGGEKIIPTDVIafRKMYGHT--EFINHYGPTEATIGAIAgrvdlyEPDAFAKRPTIGRPIANAGALVLN-EALKLVP 347
Cdd:cd05935 203 VLTGGGAPMPPAVA--EKLLKLTglRFVEGYGLTETMSQTHT------NPPLRPKLQCLGIP*FGVDARVIDiETGRELP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 348 PGASGQLYITGQGLARGYLNRPQLTAERFVENPyspGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETV 427
Cdd:cd05935 275 PNEVGEIVVRGPQIFKGYWNRPEETEESFIEIK---GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAK 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 428 MLSLSGIQEAVVLAV-SEGGLQELCAYY---------TSDQDIEKAeLRYQLSltlpSHMIPAFFVQVDAIPLTANGKTD 497
Cdd:cd05935 352 LYKHPAI*EVCVISVpDERVGEEVKAFIvlrpeyrgkVTEEDIIEW-AREQMA----AYKYPREVEFVDELPRSASGKIL 426
|
....
gi 2214269206 498 RNAL 501
Cdd:cd05935 427 WRLL 430
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
8-501 |
1.28e-39 |
|
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: 156.46 E-value: 1.28e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 8 TFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAafLPI 87
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 88 DPdTPEER---IRYSLEDSGAKfAVVnernmtAIGQYEG-------------------IIV--------SLDDgkWRNES 137
Cdd:COG1021 104 FA-LPAHRraeISHFAEQSEAV-AYI------IPDRHRGfdyralarelqaevpslrhVLVvgdageftSLDA--LLAAP 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 138 KERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKT--VL-------LSSYAFdLGytsmf 208
Cdd:COG1021 174 ADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVYlaALpaahnfpLSSPGV-LG----- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 209 pVLLGGGelHIVQkETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAkDANFESLRLIVLGGEKIIPTDVIAFRK 288
Cdd:COG1021 248 -VLYAGG--TVVL-APDPSPDTAFPLIERERVTVTALVPPLALLWLDAAERS-RYDLSSLRVLQVGGAKLSPELARRVRP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 289 MYGHTeFINHYG-------------PTEATIGaiagrvdlyepdafakrpTIGRPIANAG-ALVLNEALKLVPPGASGQL 354
Cdd:COG1021 323 ALGCT-LQQVFGmaeglvnytrlddPEEVILT------------------TQGRPISPDDeVRIVDEDGNPVPPGEVGEL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 355 YITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVkIR-GYRIEPKEIETVMLSLSG 433
Cdd:COG1021 384 LTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLLAHPA 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 434 IQEAVVLAVSEGGLQE-LCAYY-TSDQDIEKAELR-YQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:COG1021 457 VHDAAVVAMPDEYLGErSCAFVvPRGEPLTLAELRrFLRERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1079-1526 |
5.70e-39 |
|
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: 152.15 E-value: 5.70e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1079 TYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLkqeg 1158
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFV---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1159 isVPDSYtgdvilldGSRTILSLPLDendegnpetavtaenLAYMIYTSGTTGQPKGVMVEHHALV--------NLCFWH 1230
Cdd:cd05903 79 --VPERF--------RQFDPAAMPDA---------------VALLLFTSGTTGEPKGVMHSHNTLSasirqyaeRLGLGP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1231 HDAFSMTAEdrSAKYAGFGFDAsiweMFPTwTIGAELHVIDEAIRLDIVRLndyFETNGVTITFLPTQLAEQFMELEN-- 1308
Cdd:cd05903 134 GDVFLVASP--MAHQTGFVYGF----TLPL-LLGAPVVLQDIWDPDKALAL---MREHGVTFMMGATPFLTDLLNAVEea 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1309 ----TSLRVLLTGGDKLKRAVKKP------YTLVNNYGPTENTVVATSAEIHPEEGSL-SIGRAIANTRVYILGEGNQVQ 1377
Cdd:cd05903 204 geplSRLRTFVCGGATVPRSLARRaaellgAKVCSAYGSTECPGAVTSITPAPEDRRLyTDGRPLPGVEIKVVDDTGATL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1378 PEGVAGELCVAGRGLARGYLNREDETakrFVADPfvpgERMYRTGDLVKWVNGGieYIgRIDQQVK---VR-GYRIELSE 1453
Cdd:cd05903 284 APGVEGELLSRGPSVFLGYLDRPDLT---ADAAP----EGWFRTGDLARLDEDG--YL-RITGRSKdiiIRgGENIPVLE 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214269206 1454 IEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPETA---DIEALKSTL-KETLPDYMIPAFWVTLNELPVTANGKV 1526
Cdd:cd05903 354 VEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGallTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1050-1531 |
6.05e-39 |
|
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: 154.53 E-value: 6.05e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1050 TDKTVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVgVLTKP-SLEMSAAVLGVLKAGAa 1128
Cdd:COG1021 23 RGETLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRV-VVQLPnVAEFVIVFFALFRAGA- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1129 fVPIDPdYPDQR---IEYILQDSGAKLLLkqegisVPDSYTG------------------DVILLDGSRTILSL-PLDEN 1186
Cdd:COG1021 101 -IPVFA-LPAHRraeISHFAEQSEAVAYI------IPDRHRGfdyralarelqaevpslrHVLVVGDAGEFTSLdALLAA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1187 DEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHH-------ALVNLCfwhhdafSMTAEDRsakY-----AGFGFDASI 1254
Cdd:COG1021 173 PADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDdylysvrASAEIC-------GLDADTV---YlaalpAAHNFPLSS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1255 WEMFPTWTIGAELhVI------DEAIRLdIVRlndyfetNGVTITFL-PT--QLAEQFMELEN---TSLRVLLTGGDKLK 1322
Cdd:COG1021 243 PGVLGVLYAGGTV-VLapdpspDTAFPL-IER-------ERVTVTALvPPlaLLWLDAAERSRydlSSLRVLQVGGAKLS 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1323 RAVKK------PYTLVNNYGPTENTVVATSAEiHPEEGSL-SIGRAIAN---TRVyILGEGNQVqPEGVAGELCVAGRGL 1392
Cdd:COG1021 314 PELARrvrpalGCTLQQVFGMAEGLVNYTRLD-DPEEVILtTQGRPISPddeVRI-VDEDGNPV-PPGEVGELLTRGPYT 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1393 ARGYLNREDETAKRFVADPFvpgermYRTGDLVKWVNGG-IEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTA 1471
Cdd:COG1021 391 IRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGyLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVA 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 1472 VKD-----KggntaIAAYVTP--ETADIEALKSTLKET-LPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:COG1021 465 MPDeylgeR-----SCAFVVPrgEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1057-1527 |
1.69e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 153.12 E-value: 1.69e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1057 LFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDY 1136
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1137 PDQRIEYILQDSGAKLLLKQegisvpDSYTGDV--IL--LDGSRTILSLPlDENDEGNPETAVTAENLA----------- 1201
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYE------REFAPRVaeVLprLPKLRTLVVVE-DGSGNDLLPGAVDYEDALaagsperdfge 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1202 ------YMIYTSGTTGQPKGVMvehhalvnlcfW-HHDAFS--------MTAEDRSAKYA----GFGFDASIWEMFP--- 1259
Cdd:PRK07798 161 rspddlYLLYTGGTTGMPKGVM-----------WrQEDIFRvllggrdfATGEPIEDEEElakrAAAGPGMRRFPAPplm 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1260 ----TWTIGAELH-----VIDEAIRLDIVRLNDYFETNGVTITFL-------PtqLAEQFMELENT---SLRVLLTGGDK 1320
Cdd:PRK07798 230 hgagQWAAFAALFsgqtvVLLPDVRFDADEVWRTIEREKVNVITIvgdamarP--LLDALEARGPYdlsSLFAIASGGAL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1321 LKRAVKKPY-------TLVNNYGPTEN----TVVATSAEIHPEEGSLSIGraiANTRVyILGEGNQVQP-EGVAGELcvA 1388
Cdd:PRK07798 308 FSPSVKEALlellpnvVLTDSIGSSETgfggSGTVAKGAVHTGGPRFTIG---PRTVV-LDEDGNPVEPgSGEIGWI--A 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1389 GRG-LARGYLNREDETAKRFvadPFVPGERMYRTGDLVKWVNGG-IEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQD 1466
Cdd:PRK07798 382 RRGhIPLGYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGtITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVAD 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 1467 AAVTAVKDKGGNTAIAAYVTPE---TADIEALKSTLKETLPDYMIP-AFWVTlNELPVTANGKVD 1527
Cdd:PRK07798 459 ALVVGVPDERWGQEVVAVVQLRegaRPDLAELRAHCRSSLAGYKVPrAIWFV-DEVQRSPAGKAD 522
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
17-501 |
2.42e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 151.96 E-value: 2.42e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 17 AQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERI 96
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 97 RYSLEDSGAKFAVVNERnMTAIGQYEGIIVSLDDGKWRNESK-------ERPSSISGSRNLAYVIYTSGTTGKPKGVQIE 169
Cdd:PRK06145 92 AYILGDAGAKLLLVDEE-FDAIVALETPKIVIDAAAQADSRRlaqggleIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 170 HRNltnyVSWFSEEA----GLTENDKTVLLSSY----AFDLgytSMFPVLLGGGELHIVQKetyTAPDEIAHYIKEHGIT 241
Cdd:PRK06145 171 YGN----LHWKSIDHvialGLTASERLLVVGPLyhvgAFDL---PGIAVLWVGGTLRIHRE---FDPEAVLAAIERHRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 242 YIKLTPSLFHTIVnTASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAI---AGRvdlyep 318
Cdd:PRK06145 241 CAWMAPVMLSRVL-TVPDRDRFDLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTlmeAGR------ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 319 dAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpyspgslMYKTGDVVRRLS 398
Cdd:PRK06145 314 -EIEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD-------WFRSGDVGYLDE 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 399 DGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQE---LCAYYTSDQDIEKAELRYQLSLTLPS 475
Cdd:PRK06145 386 EGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGEritAVVVLNPGATLTLEALDRHCRQRLAS 465
|
490 500
....*....|....*....|....*.
gi 2214269206 476 HMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK06145 466 FKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1068-1531 |
2.55e-38 |
|
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: 150.32 E-value: 2.55e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1068 RPAVTYNGQSWTYGELNAKANRLARILMD-CGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGeLGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKlllkqegisvpdsytgdVILLDGSRTilslpldendegnpetavTAENLAYMIYTSGTTGQPKGVMVEHHALVNL 1226
Cdd:cd05958 81 KARIT-----------------VALCAHALT------------------ASDDICILAFTSGTTGAPKATMHFHRDPLAS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1227 C-FWHHDAFSMTAEDR---SAKYA-GFGFDASiweMFPTWTIGAELHVIDEAIRLDIVRLNDYFetnGVTITF-LPTQLA 1300
Cdd:cd05958 126 AdRYAVNVLRLREDDRfvgSPPLAfTFGLGGV---LLFPFGVGASGVLLEEATPDLLLSAIARY---KPTVLFtAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1301 E-----QFMELENTSLRVLLTGGDKLKRAVKKPY------TLVNNYGPTENTVVATSA---EIHPeeGSLsiGRAIANTR 1366
Cdd:cd05958 200 AmlahpDAAGPDLSSLRKCVSAGEALPAALHRAWkeatgiPIIDGIGSTEMFHIFISArpgDARP--GAT--GKPVPGYE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1367 VYIL-GEGNQVqPEGVAGELCVAGrglargylnredETAKRFVADP----FVPGERMYrTGDL-VKWVNGGIEYIGRIDQ 1440
Cdd:cd05958 276 AKVVdDEGNPV-PDGTIGRLAVRG------------PTGCRYLADKrqrtYVQGGWNI-TGDTySRDPDGYFRHQGRSDD 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1441 QVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYV------TPETADIEALKSTLKETLPDYMIPAFWVT 1514
Cdd:cd05958 342 MIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVvlrpgvIPGPVLARELQDHAKAHIAPYKYPRAIEF 421
|
490
....*....|....*..
gi 2214269206 1515 LNELPVTANGKVDRKAL 1531
Cdd:cd05958 422 VTELPRTATGKLQRFAL 438
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1-495 |
4.58e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 151.62 E-value: 4.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1 MTQITEATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKA 80
Cdd:PRK08316 5 STRARRQTIGDILRRSARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 81 GAAFLPIDPD-TPEErIRYSLEDSGAKFAVV------NERNMTAIGQYEGIIVSL------DDGKWRN-------ESKER 140
Cdd:PRK08316 85 GAVHVPVNFMlTGEE-LAYILDHSGARAFLVdpalapTAEAALALLPVDTLILSLvlggreAPGGWLDfadwaeaGSVAE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 141 PSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLT-NYVSWFSeEAGLTENDKTV----LLSSYAFDlgyTSMFPVLLGGG 215
Cdd:PRK08316 164 PDVELADDDLAQILYTSGTESLPKGAMLTHRALIaEYVSCIV-AGDMSADDIPLhalpLYHCAQLD---VFLGPYLYVGA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 216 ELHIVQKETytaPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAKdANFESLRLIVLGGEkIIPTDVIA-FRKMYGHTE 294
Cdd:PRK08316 240 TNVILDAPD---PELILRTIEAERITSFFAPPTVWISLLRHPDFDT-RDLSSLRKGYYGAS-IMPVEVLKeLRERLPGLR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 295 FINHYGPTEatIGAIAgrvDLYEPDAFAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTA 373
Cdd:PRK08316 315 FYNCYGQTE--IAPLA---TVLGPEEHLRRPgSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTA 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 374 ERFVENpyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQE---L 450
Cdd:PRK08316 390 EAFRGG-------WFHSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEavtA 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2214269206 451 CAYYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:PRK08316 463 VVVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGK 507
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-440 |
4.58e-38 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 152.95 E-value: 4.58e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1 MTQITEA----TFAALFEKQAQQTPDHSA--VKAGGNL--LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMV 72
Cdd:COG1022 1 MSEFSDVppadTLPDLLRRRAARFPDRVAlrEKEDGIWqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 73 SILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNM-----TAIGQYEGI--IVSLDDGKWRNESK------- 138
Cdd:COG1022 81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEDQEQldkllEVRDELPSLrhIVVLDPRGLRDDPRllsldel 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 139 --------------ERPSSISGSrNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVL---LS-SYAF 200
Cdd:COG1022 161 lalgrevadpaeleARRAAVKPD-DLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSflpLAhVFER 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 201 DLGYTSMFpvllGGGELHIVQKetytaPDEIAHYIKEHGITYIKLTPSLFHTIVNT-------ASFAKDANFES------ 267
Cdd:COG1022 240 TVSYYALA----AGATVAFAES-----PDTLAEDLREVKPTFMLAVPRVWEKVYAGiqakaeeAGGLKRKLFRWalavgr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 268 --------------------------------------LRLIVLGGEKiIPTDVIAF------RKMYGhtefinhYGPTE 303
Cdd:COG1022 311 ryararlagkspslllrlkhaladklvfsklrealggrLRFAVSGGAA-LGPELARFfralgiPVLEG-------YGLTE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 304 ATiGAIAGRvdlyEPDAFaKRPTIGRPIANAgalvlneALKLvppGASGQLYITGQGLARGYLNRPQLTAERFVENPYsp 383
Cdd:COG1022 383 TS-PVITVN----RPGDN-RIGTVGPPLPGV-------EVKI---AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW-- 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 384 gslmYKTGDVVRRLSDGTLAFIGRADDQVKIR-GYRIEPKEIETVMLSLSGIQEAVVL 440
Cdd:COG1022 445 ----LHTGDIGELDEDGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV 498
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1065-1533 |
5.90e-38 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 150.78 E-value: 5.90e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1065 HKDRPAVTYNGQSWTYGELNAKANRLARILM-DCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEY 1143
Cdd:PRK06839 15 HPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1144 ILQDSGAKLLLKQEGISV------PDSYTGDVILLDGSRTILSLPLDENDEGNpetavtaENLAYMI-YTSGTTGQPKGV 1216
Cdd:PRK06839 95 QLKDSGTTVLFVEKTFQNmalsmqKVSYVQRVISITSLKEIEDRKIDNFVEKN-------ESASFIIcYTSGTTGKPKGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1217 MVEHhalVNLcFWH--HDAFS--MTAEDRSA------KYAGFGFDAsiwemFPTWTIGAELHVI-----DEAIRLdivrl 1281
Cdd:PRK06839 168 VLTQ---ENM-FWNalNNTFAidLTMHDRSIvllplfHIGGIGLFA-----FPTLFAGGVIIVPrkfepTKALSM----- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1282 ndyFETNGVTITF-LPT--QLAEQFMELENTSL---RVLLTGG----DKLKRA-VKKPYTLVNNYGPTENT-VVATSAEI 1349
Cdd:PRK06839 234 ---IEKHKVTVVMgVPTihQALINCSKFETTNLqsvRWFYNGGapcpEELMREfIDRGFLFGQGFGMTETSpTVFMLSEE 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1350 HPEEGSLSIGRAIANTRVYILGE-GNQVQPEGVaGELCVAGRGLARGYLNREDETAKRfVADPFvpgermYRTGDLVKWV 1428
Cdd:PRK06839 311 DARRKVGSIGKPVLFCDYELIDEnKNKVEVGEV-GELLIRGPNVMKEYWNRPDATEET-IQDGW------LCTGDLARVD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1429 NGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKD-KGGNTAIAAYVTPETADI--EALKSTLKETLP 1504
Cdd:PRK06839 383 EDGFVYIvGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHvKWGEIPIAFIVKKSSSVLieKDVIEHCRLFLA 462
|
490 500
....*....|....*....|....*....
gi 2214269206 1505 DYMIPAFWVTLNELPVTANGKVDRKALPE 1533
Cdd:PRK06839 463 KYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1077-1531 |
2.27e-37 |
|
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: 147.24 E-value: 2.27e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1077 SWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLkq 1156
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1157 egisvpdsytgdvilldgsrtilslpldendegnpeTAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSM 1236
Cdd:cd05935 79 ------------------------------------VGSELDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1237 TAEDRSAKYAGF----GFDASiweMFPTWTIGAELHVIDeaiRLDIVRLNDYFETNGVTI-TFLPTQLAEQFMELEN--- 1308
Cdd:cd05935 123 TPSDVILACLPLfhvtGFVGS---LNTAVYVGGTYVLMA---RWDRETALELIEKYKVTFwTNIPTMLVDLLATPEFktr 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1309 --TSLRVLLTGGDKLKRAV-KKPYTL-----VNNYGPTEnTVVATSAEIHPEEGSLSIGRAIANTRVYILG-EGNQVQPE 1379
Cdd:cd05935 197 dlSSLKVLTGGGAPMPPAVaEKLLKLtglrfVEGYGLTE-TMSQTHTNPPLRPKLQCLGIP*FGVDARVIDiETGRELPP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1380 GVAGELCVAGRGLARGYLNREDETAKRFVADpfvPGERMYRTGDL-VKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQL 1458
Cdd:cd05935 276 NEVGEIVVRGPQIFKGYWNRPEETEESFIEI---KGRRFFRTGDLgYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKL 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 1459 AQLSEVQDAAVTAVKDKGGNTAIAAYVT--PE---TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05935 353 YKHPAI*EVCVISVPDERVGEEVKAFIVlrPEyrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
28-439 |
3.93e-37 |
|
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: 148.54 E-value: 3.93e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 28 AGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPD-TPEErIRYSLEDSGAK 106
Cdd:cd05904 28 ATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLsTPAE-IAKQVKDSGAK 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 107 FAVVNERNMT----------AIGQYEGIIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNY 176
Cdd:cd05904 107 LAFTTAELAEklaslalpvvLLDSAEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAM 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 177 VSWF-SEEAGLTENDKTVLLSSYAFDL-GYTSMFPVLLG-GGELHIVQKetYTAPDEIAHyIKEHGITYIKLTPSLFHTI 253
Cdd:cd05904 187 VAQFvAGEGSNSDSEDVFLCVLPMFHIyGLSSFALGLLRlGATVVVMPR--FDLEELLAA-IERYKVTHLPVVPPIVLAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 254 VNTASfAKDANFESLRLIVLGGEKiIPTDVI-AFRKMYGHTEFINHYGPTEATigAIAGRVDLYEPDAfAKRPTIGRPIA 332
Cdd:cd05904 264 VKSPI-VDKYDLSSLRQIMSGAAP-LGKELIeAFRAKFPNVDLGQGYGMTEST--GVVAMCFAPEKDR-AKYGSVGRLVP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 333 NAGALVLN-EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpyspGSLmyKTGDVVRRLSDGTLAFIGRADDQ 411
Cdd:cd05904 339 NVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKE----GWL--HTGDLCYIDEDGYLFIVDRLKEL 412
|
410 420
....*....|....*....|....*...
gi 2214269206 412 VKIRGYRIEPKEIETVMLSLSGIQEAVV 439
Cdd:cd05904 413 IKYKGFQVAPAELEALLLSHPEILDAAV 440
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1041-1542 |
7.17e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 148.99 E-value: 7.17e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1041 WKGKALPVPTDKTVHqLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVL 1120
Cdd:PRK05605 22 WTPHDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1121 GVLKAGAAFVPIDPDYPDQRIEYILQDSGAKL---------------------------------LLKQEGISVP----- 1162
Cdd:PRK05605 101 AVLRLGAVVVEHNPLYTAHELEHPFEDHGARVaivwdkvaptverlrrttpletivsvnmiaampLLQRLALRLPipalr 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1163 ---DSYTGDV-------ILLDGSRtilslPLDENDEGNPEtaVTAENLAYMIYTSGTTGQPKGVMVEHHALVN------- 1225
Cdd:PRK05605 181 karAALTGPApgtvpweTLVDAAI-----GGDGSDVSHPR--PTPDDVALILYTSGTTGKPKGAQLTHRNLFAnaaqgka 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1226 ---------------LCFWHhdAFSMTAEdrsakyAGFGFdasiwemfptwTIGAELHVI---DEAIRLDIVRLNdyfet 1287
Cdd:PRK05605 254 wvpglgdgpervlaaLPMFH--AYGLTLC------LTLAV-----------SIGGELVLLpapDIDLILDAMKKH----- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1288 ngvTITFLP----------TQLAEQFMELenTSLRVLLTGGDKLKRAVKKPYT------LVNNYGPTENTVVATSAEIHP 1351
Cdd:PRK05605 310 ---PPTWLPgvpplyekiaEAAEERGVDL--SGVRNAFSGAMALPVSTVELWEkltgglLVEGYGLTETSPIIVGNPMSD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1352 EEGSLSIGRAIANTRVYILGEGN--QVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADpfvpgerMYRTGDLVKW-V 1428
Cdd:PRK05605 385 DRRPGYVGVPFPDTEVRIVDPEDpdETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMeE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1429 NGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAV-KDKGGNTAIAAYVTPETADI--EALKSTLKETLPD 1505
Cdd:PRK05605 458 DGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLpREDGSEEVVAAVVLEPGAALdpEGLRAYCREHLTR 537
|
570 580 590
....*....|....*....|....*....|....*..
gi 2214269206 1506 YMIPAFWVTLNELPVTANGKVDRKALPEpDIEAGSGE 1542
Cdd:PRK05605 538 YKVPRRFYHVDELPRDQLGKVRRREVRE-ELLEKLGA 573
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1031-1531 |
1.31e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 147.88 E-value: 1.31e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1031 ETEKQALLEAWKGKALPVPTDKTVHQLFEET---------VQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISP 1101
Cdd:PRK06178 3 EEAYLAELRALQQAAWPAGIPREPEYPHGERplteylrawARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1102 DDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKQEG----------------------- 1158
Cdd:PRK06178 83 GDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYELNDAGAEVLLALDQlapvveqvraetslrhvivtsla 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1159 --------ISVPDSYTGDVILLDGSRTILSLpLDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCfwh 1230
Cdd:PRK06178 163 dvlpaeptLPLPDSLRAPRLAAAGAIDLLPA-LRACTAPVPLPPPALDALAALNYTGGTTGMPKGCEHTQRDMVYTA--- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1231 hDAFSMTAEDRSAKYAGFGFDASIW---E----MFPTWTiGAELHVIDeaiRLDIVRLNDYFETNGVTITFLPTQLAEQF 1303
Cdd:PRK06178 239 -AAAYAVAVVGGEDSVFLSFLPEFWiagEnfglLFPLFS-GATLVLLA---RWDAVAFMAAVERYRVTRTVMLVDNAVEL 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1304 ME---LENTSLRVLLTGG-----DKLKRAVKKPY------TLVN-NYGPTE-NTVVATSAEIHPEEGSLS-----IGRAI 1362
Cdd:PRK06178 314 MDhprFAEYDLSSLRQVRvvsfvKKLNPDYRQRWraltgsVLAEaAWGMTEtHTCDTFTAGFQDDDFDLLsqpvfVGLPV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1363 ANTRVYILG-EGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVadpfvpgERMYRTGDLVKW-VNGGIEYIGRIDQ 1440
Cdd:PRK06178 394 PGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALR-------DGWLHTGDIGKIdEQGFLHYLGRRKE 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1441 QVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE---TADIEALKSTLKETLPDYMIPAFWVtLNE 1517
Cdd:PRK06178 467 MLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQLKpgaDLTAAALQAWCRENMAVYKVPEIRI-VDA 545
|
570
....*....|....
gi 2214269206 1518 LPVTANGKVDRKAL 1531
Cdd:PRK06178 546 LPMTATGKVRKQDL 559
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
8-495 |
3.52e-36 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 146.35 E-value: 3.52e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 8 TFAALFEKQAQQTPDHSAVKA---GGNL---LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAG 81
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVTAvrlGTGAprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 82 AAFLPIDPDTPEERIRYSLEDSGAKFAVVNER-------NMTA-----IGQYEGIIVSLDDG-----------KWRNESK 138
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKVLVVPKTfrgfdhaAMARrlrpeLPALRHVVVVGGDGadsfeallitpAWEQEPD 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 139 ERP---SSISGSRNLAYVIYTSGTTGKPKGVQIEHRNL-TNYVSwFSEEAGLTENDKTVLLSSYAFDLG--YTSMFPVLL 212
Cdd:PRK13295 185 APAilaRLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLmANIVP-YAERLGLGADDVILMASPMAHQTGfmYGLMMPVML 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 213 GGgelHIVQKETYTaPDEIAHYIKEHGITY-IKLTPSLfHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVIAFRKMYG 291
Cdd:PRK13295 264 GA---TAVLQDIWD-PARAAELIRTEGVTFtMASTPFL-TDLTRAVK-ESGRPVSSLRTFLCAGAPIPGALVERARAALG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 292 hTEFINHYGPTEAtigaiaGRVDLYEPDAFAKRP--TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRP 369
Cdd:PRK13295 338 -AKIVSAWGMTEN------GAVTLTKLDDPDERAstTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 370 QLTAERFvenpysPGslMYKTGDVVRRLSDGTLAFIGRADDqVKIRG-YRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQ 448
Cdd:PRK13295 411 QLNGTDA------DG--WFDTGDLARIDADGYIRISGRSKD-VIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPDERLG 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 449 E-LCAYYT--SDQDIEKAEL-RYQLSLTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:PRK13295 482 ErACAFVVprPGQSLDFEEMvEFLKAQKVAKQYIPERLVVRDALPRTPSGK 532
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1044-1531 |
5.80e-36 |
|
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: 144.39 E-value: 5.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1044 KALPVPTDKTVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVL 1123
Cdd:cd05920 7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1124 KAGAAFVPIDPDYPDQRIEYILQDSGAKLLLkqegisVPDSYTGDvilldgsrtilslplDENDEGNPETAVTAEnLAYM 1203
Cdd:cd05920 87 RLGAVPVLALPSHRRSELSAFCAHAEAVAYI------VPDRHAGF---------------DHRALARELAESIPE-VALF 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1204 IYTSGTTGQPKGVMVEHHALvnlcfwhhdAFSMTAE------DRSAKY-----AGFGFDASIWEMFPTWTIGAELHVIDE 1272
Cdd:cd05920 145 LLSGGTTGTPKLIPRTHNDY---------AYNVRASaevcglDQDTVYlavlpAAHNFPLACPGVLGTLLAGGRVVLAPD 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1273 AIRLDIVRLndyFETNGVTITFLPTQLAEQFME------LENTSLRVLLTGGDKLK----RAVKKPY--TLVNNYGPTEN 1340
Cdd:cd05920 216 PSPDAAFPL---IEREGVTVTALVPALVSLWLDaaasrrADLSSLRLLQVGGARLSpalaRRVPPVLgcTLQQVFGMAEG 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1341 TVVATSAEIHPEEGSLSIGRAI-ANTRVYILGE-GNQVqPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgerm 1418
Cdd:cd05920 293 LLNYTRLDDPDEVIIHTQGRPMsPDDEIRVVDEeGNPV-PPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1419 YRTGDLVKWV-NGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPETADIEA--L 1495
Cdd:cd05920 366 YRTGDLVRRTpDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRDPPPSAaqL 445
|
490 500 510
....*....|....*....|....*....|....*..
gi 2214269206 1496 KSTLKET-LPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05920 446 RRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1047-1469 |
7.39e-36 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 146.40 E-value: 7.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1047 PVPTDKTVHQLFEETVQRHKDRPAVTY--NG--QSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGV 1122
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALREkeDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAI 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1123 LKAGAAFVPIDPDYPDQRIEYILQDSGAKLLL----KQEG--ISVPDSYTG--DVILLDG---SRTILSLPLDE-----N 1186
Cdd:COG1022 86 LAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFvedqEQLDklLEVRDELPSlrHIVVLDPrglRDDPRLLSLDEllalgR 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1187 DEGNPET------AVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRS-----------------A 1243
Cdd:COG1022 166 EVADPAElearraAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTlsflplahvfertvsyyA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1244 KYAGF--GFDAS---------------------IWEMFPTwTIGAELH--------VIDEAIRLDIVRLNDYFETNGVTI 1292
Cdd:COG1022 246 LAAGAtvAFAESpdtlaedlrevkptfmlavprVWEKVYA-GIQAKAEeagglkrkLFRWALAVGRRYARARLAGKSPSL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1293 TF-LPTQLAEQ--FMELEN---TSLRVLLTGGDKLKRAVKKPY-----TLVNNYGPTENTVVATsaeIHPEEGSL--SIG 1359
Cdd:COG1022 325 LLrLKHALADKlvFSKLREalgGRLRFAVSGGAALGPELARFFralgiPVLEGYGLTETSPVIT---VNRPGDNRigTVG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1360 RAIANTRVYIlgegnqvqpeGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermYRTGDLVKWVNGG-IEYIGRI 1438
Cdd:COG1022 402 PPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGELDEDGfLRITGRK 465
|
490 500 510
....*....|....*....|....*....|..
gi 2214269206 1439 DQQVKVR-GYRIELSEIEVQLAQLSEVQDAAV 1469
Cdd:COG1022 466 KDLIVTSgGKNVAPQPIENALKASPLIEQAVV 497
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1060-1531 |
1.15e-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: 144.31 E-value: 1.15e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1060 ETVQRHKDRPAVTYngqswTYGELNAKANRLARILMDCGISPDDRVGVL---TKPSLEMSAAVLGvlkAGAAFVPIDPDY 1136
Cdd:cd12119 13 EIVSRTHEGEVHRY-----TYAEVAERARRLANALRRLGVKPGDRVATLawnTHRHLELYYAVPG---MGAVLHTINPRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1137 PDQRIEYILQDSGAKLLL-------KQEGI-SVPDSYTGDVILLDG-SRTILSLPLDEN-----DEGNPETAVTA--ENL 1200
Cdd:cd12119 85 FPEQIAYIINHAEDRVVFvdrdflpLLEAIaPRLPTVEHVVVMTDDaAMPEPAGVGVLAyeellAAESPEYDWPDfdENT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1201 AYMI-YTSGTTGQPKGVMVEHHALVnlcfwHHdAFSMTAEDrsakyaGFG-------------FDASIWEM-FPTWTIGA 1265
Cdd:cd12119 165 AAAIcYTSGTTGNPKGVVYSHRSLV-----LH-AMAALLTD------GLGlsesdvvlpvvpmFHVNAWGLpYAAAMVGA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1266 ELhVIDEAiRLDIVRLNDYFETNGVTITF-LPTQLAEQFMELENT-----SLRVLLTGGDKLKRAVKKPY-----TLVNN 1334
Cdd:cd12119 233 KL-VLPGP-YLDPASLAELIEREGVTFAAgVPTVWQGLLDHLEANgrdlsSLRRVVIGGSAVPRSLIEAFeergvRVIHA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1335 YGPTENTVVATSAEIHPEEGSLSI----------GRAIANTRVYILGEGNQVQP-EGVA-GELCVAGRGLARGYLNrEDE 1402
Cdd:cd12119 311 WGMTETSPLGTVARPPSEHSNLSEdeqlalrakqGRPVPGVELRIVDDDGRELPwDGKAvGELQVRGPWVTKSYYK-NDE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1403 TAKRFVADPFvpgermYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKD-KGGNTA 1480
Cdd:cd12119 390 ESEALTEDGW------LRTGDVATIdEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHpKWGERP 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 1481 IAAYVTPE--TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd12119 464 LAVVVLKEgaTVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
5-503 |
2.12e-35 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 144.12 E-value: 2.12e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 5 TEATFAALFEKQAQQTPDHSAVKAG-GNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAA 83
Cdd:PRK06087 21 GDASLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 84 FLPIDPDTPEERIRYSLEDSGAK--FAVVNERNMTAIGQYEGI---------IVSLDDGK------------WRNESKER 140
Cdd:PRK06087 101 SVPLLPSWREAELVWVLNKCQAKmfFAPTLFKQTRPVDLILPLqnqlpqlqqIVGVDKLApatsslslsqiiADYEPLTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 141 PSSISGSrNLAYVIYTSGTTGKPKGVQIEHRNLTnyvswFSEEA-----GLTENDkTVLLSSyafDLGYTSMF------P 209
Cdd:PRK06087 181 AITTHGD-ELAAVLFTSGTEGLPKGVMLTHNNIL-----ASERAycarlNLTWQD-VFMMPA---PLGHATGFlhgvtaP 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 210 VLLGGgelHIVQKETYTaPDEIAHYIKEHGITY-IKLTPSLFhTIVNTASfAKDANFESLRLIVLGGeKIIPTDVIafRK 288
Cdd:PRK06087 251 FLIGA---RSVLLDIFT-PDACLALLEQQRCTCmLGATPFIY-DLLNLLE-KQPADLSALRFFLCGG-TTIPKKVA--RE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 289 MYGH-TEFINHYGPTEATIGAIagrVDLYEPDAFAKRpTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLN 367
Cdd:PRK06087 322 CQQRgIKLLSVYGSTESSPHAV---VNLDDPLSRFMH-TDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLD 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 368 RPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDqVKIR-GYRIEPKEIETVMLSLSGIQEAVVLAVSEGG 446
Cdd:PRK06087 398 EPELTARALDEEGW------YYSGDLCRMDEAGYIKITGRKKD-IIVRgGENISSREVEDILLQHPKIHDACVVAMPDER 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 447 LQE-LCAYYT---SDQDIEKAELRYQLSLT-LPSHMIPAFFVQVDAIPLTANGKTDRNALPK 503
Cdd:PRK06087 471 LGErSCAYVVlkaPHHSLTLEEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
148-498 |
4.70e-35 |
|
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: 138.16 E-value: 4.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 148 RNLAYVIYTSGTTGKPKGVQIEHRNL-TNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGeLHIVQKE--T 224
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFfAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGG-LCVTGGEntT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 225 YTAPDEIahyIKEHGITYIKLTPSLFHTIVNtasFAKDAN--FESLRLIVLGGEKIIPTDViAFRKMYGHTEFINHYGPT 302
Cdd:cd17635 80 YKSLFKI---LTTNAVTTTCLVPTLLSKLVS---ELKSANatVPSLRLIGYGGSRAIAADV-RFIEATGLTNTAQVYGLS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 303 E-ATIGAIAGRVDLYEPDAfakrptIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpy 381
Cdd:cd17635 153 EtGTALCLPTDDDSIEINA------VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDG-- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 382 spgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYT--SDQD 459
Cdd:cd17635 225 -----WVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVvaSAEL 299
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2214269206 460 IEKA--ELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDR 498
Cdd:cd17635 300 DENAirALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1067-1531 |
7.48e-35 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 141.25 E-value: 7.48e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:PRK03640 17 DRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLD 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLkqegisVPDSYTGDVIlLDGSRTILSLPLDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVM--VEHHalv 1224
Cdd:PRK03640 97 DAEVKCLI------TDDDFEAKLI-PGISVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIqtYGNH--- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1225 nlcFWhhDAFS------MTAEDR----------SakyaGFgfdaSIweMFPTWTIGAELHVIDeaiRLDIVRLNDYFETN 1288
Cdd:PRK03640 167 ---WW--SAVGsalnlgLTEDDCwlaavpifhiS----GL----SI--LMRSVIYGMRVVLVE---KFDAEKINKLLQTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1289 GVT-ITFLPTQLAEQFMELE----NTSLRVLLTGG-----DKLKRAVKKPYTLVNNYGPTENT--VVATSAE-IHPEEGs 1355
Cdd:PRK03640 229 GVTiISVVSTMLQRLLERLGegtyPSSFRCMLLGGgpapkPLLEQCKEKGIPVYQSYGMTETAsqIVTLSPEdALTKLG- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1356 lSIGRAIANTRVYILGEGNQVQPeGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermyRTGDlvkwvnggieyI 1435
Cdd:PRK03640 308 -SAGKPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGD-----------I 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1436 GRIDQQ----VKVR--------GYRIELSEIEVQLAQLSEVQDAAVTAVKD-KGGNTAIAAYVTPETADIEALKSTLKET 1502
Cdd:PRK03640 368 GYLDEEgflyVLDRrsdliisgGENIYPAEIEEVLLSHPGVAEAGVVGVPDdKWGQVPVAFVVKSGEVTEEELRHFCEEK 447
|
490 500
....*....|....*....|....*....
gi 2214269206 1503 LPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK03640 448 LAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
17-508 |
1.88e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 141.33 E-value: 1.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 17 AQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERI 96
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 97 RYSLEDSGAKFAVVNERNMTAIGQY-------EGIIVSLDDGKWRNESKERPSSISGSR--------------------- 148
Cdd:PRK06178 123 SYELNDAGAEVLLALDQLAPVVEQVraetslrHVIVTSLADVLPAEPTLPLPDSLRAPRlaaagaidllpalractapvp 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 149 -------NLAYVIYTSGTTGKPKGVQIEHRNLTnYVSWFSEEAGLTENDKTVLLSSYA-F-----DLGYtsMFPVLLGGG 215
Cdd:PRK06178 203 lpppaldALAALNYTGGTTGMPKGCEHTQRDMV-YTAAAAYAVAVVGGEDSVFLSFLPeFwiageNFGL--LFPLFSGAT 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 216 ELHIVQKETYTAPDEIAHYikehGITYIKLTPSLFHTIVNTASFAkDANFESLR--LIVLGGEKIIPTDVIAFRKMYGHT 293
Cdd:PRK06178 280 LVLLARWDAVAFMAAVERY----RVTRTVMLVDNAVELMDHPRFA-EYDLSSLRqvRVVSFVKKLNPDYRQRWRALTGSV 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 294 EFINHYGPTEA------TIGAIAGRVDLYEPDAFakrptIGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLARGYL 366
Cdd:PRK06178 355 LAEAAWGMTEThtcdtfTAGFQDDDFDLLSQPVF-----VGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYW 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 367 NRPQLTAERFVENpyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQ-EAVVLAVSEG 445
Cdd:PRK06178 430 NKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLgSAVVGRPDPD 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 446 GLQELCAYYT--SDQDIEKAELRYQLSLTLPSHMIPAFFVqVDAIPLTANGKTDRNALpKPNAAQ 508
Cdd:PRK06178 503 KGQVPVAFVQlkPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL-QALAEE 565
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
5-497 |
1.96e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 140.79 E-value: 1.96e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 5 TEATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAF 84
Cdd:PRK07798 1 MAWNIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 85 LPIDPDTPEERIRYSLEDSGAKfAVVNERNMTAI-----GQYEGI--IVSLDDGkwrNESKERPSSISGSRNLA------ 151
Cdd:PRK07798 81 VNVNYRYVEDELRYLLDDSDAV-ALVYEREFAPRvaevlPRLPKLrtLVVVEDG---SGNDLLPGAVDYEDALAagsper 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 152 ----------YVIYTSGTTGKPKGVQIEH----RNLTNYVSWFSEEAGLTENDktvlLSSYAFDLGYTSMFPV------- 210
Cdd:PRK07798 157 dfgerspddlYLLYTGGTTGMPKGVMWRQedifRVLLGGRDFATGEPIEDEEE----LAKRAAAGPGMRRFPApplmhga 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 211 --------LLGGGELHIVQKETYTaPDEIAHYIKEHGITYIkltpslfhTIVNTAsFAK----------DANFESLRLIV 272
Cdd:PRK07798 233 gqwaafaaLFSGQTVVLLPDVRFD-ADEVWRTIEREKVNVI--------TIVGDA-MARplldaleargPYDLSSLFAIA 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 273 LGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIaGRVDLYEPDAFAKRPTIGrpianAGALVLNEALKLVPPGaSG 352
Cdd:PRK07798 303 SGGALFSPSVKEALLELLPNVVLTDSIGSSETGFGGS-GTVAKGAVHTGGPRFTIG-----PRTVVLDEDGNPVEPG-SG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 353 QLYITGQG--LARGYLNRPQLTAERFVE---NPYSpgslmyKTGDVVRRLSDGTLAFIGRadDQVKIR--GYRIEPKEIE 425
Cdd:PRK07798 376 EIGWIARRghIPLGYYKDPEKTAETFPTidgVRYA------IPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVE 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 426 TVMLSLSGIQEAVVLAV-SEGGLQELCA--YYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTD 497
Cdd:PRK07798 448 EALKAHPDVADALVVGVpDERWGQEVVAvvQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
6-501 |
2.01e-34 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 141.05 E-value: 2.01e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 6 EATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFL 85
Cdd:PRK06155 20 ERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 86 PIDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQYEGIIVSLDD-------GKWRNESKER------------PSSISG 146
Cdd:PRK06155 100 PINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDLPLPAvwlldapASVSVPAGWStaplppldapapAAAVQP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 147 SRNLAyVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDktVLLSSyaFDLGYT----SMFPVLLGGGELHIVQK 222
Cdd:PRK06155 180 GDTAA-ILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD--VLYTT--LPLFHTnalnAFFQALLAGATYVLEPR 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 223 etYTAP---DEIAhyikEHGITYIKLTPSLFHTIVNTASFAKDaNFESLRLIVLGGekIIPTDVIAFRKMYGhTEFINHY 299
Cdd:PRK06155 255 --FSASgfwPAVR----RHGATVTYLLGAMVSILLSQPARESD-RAHRVRVALGPG--VPAALHAAFRERFG-VDLLDGY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 300 GPTEATIgAIAGRVDlyepdafAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQ---GLARGYLNRPQLTAER 375
Cdd:PRK06155 325 GSTETNF-VIAVTHG-------SQRPgSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVEA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 376 FvenpyspGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV-SEGGLQELCAYY 454
Cdd:PRK06155 397 W-------RNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVpSELGEDEVMAAV 469
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2214269206 455 T--SDQDIEKAEL-RYQLSlTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK06155 470 VlrDGTALEPVALvRHCEP-RLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1048-1485 |
3.43e-34 |
|
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: 139.68 E-value: 3.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1048 VPTDKTVHQLFEETVQRHKDRPAV--TYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKA 1125
Cdd:cd05904 1 LPTDLPLDSVSFLFASAHPSRPALidAATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1126 GAAFVPIDPDYPDQRIEYILQDSGAKLLL-------KQEGISVPdsytgdVILLDGSRTIL---SLPLDENDEGN-PETA 1194
Cdd:cd05904 81 GAVVTTANPLSTPAEIAKQVKDSGAKLAFttaelaeKLASLALP------VVLLDSAEFDSlsfSDLLFEADEAEpPVVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1195 VTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAG------FGFDASiweMFPTWTIGAELH 1268
Cdd:cd05904 155 IKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQFVAGEGSNSDSEDVFLCVlpmfhiYGLSSF---ALGLLRLGATVV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1269 VIDeaiRLDIVRLNDYFETNGVtiTFLP------TQLAEQFME--LENTSLRVLLTGGDKLKR----AVKKPYTLVN--- 1333
Cdd:cd05904 232 VMP---RFDLEELLAAIERYKV--THLPvvppivLALVKSPIVdkYDLSSLRQIMSGAAPLGKelieAFRAKFPNVDlgq 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1334 NYGPTENTVVATSaEIHPEEGSL---SIGRAIANTRVYILG-EGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVA 1409
Cdd:cd05904 307 GYGMTESTGVVAM-CFAPEKDRAkygSVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDK 385
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214269206 1410 DPFVpgermyRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYV 1485
Cdd:cd05904 386 EGWL------HTGDLCYIDEDGYLFIvDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFV 456
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
28-497 |
4.30e-34 |
|
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: 139.00 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 28 AGGNLLTYRELDEQANQLAHHLRAQGAGnEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKF 107
Cdd:cd05909 3 TLGTSLTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 108 AVVNERNMTAIGQYEGI-------IVSLDD----------------GKWRNESKERPSSISG--SRNLAYVIYTSGTTGK 162
Cdd:cd05909 82 VLTSKQFIEKLKLHHLFdveydarIVYLEDlrakiskadkckaflaGKFPPKWLLRIFGVAPvqPDDPAVILFTSGSEGL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 163 PKGVQIEHRNLTNYVSWFSEEAGLTENDK--TVLLSSYAFDLGYTSMFPVLLGggeLHIVQKETYTAPDEIAHYIKEHGI 240
Cdd:cd05909 162 PKGVVLSHKNLLANVEQITAIFDPNPEDVvfGALPFFHSFGLTGCLWLPLLSG---IKVVFHPNPLDYKKIPELIYDKKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 241 TYIKLTPSLFHTIVNtasFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGhTEFINHYGPTEAtigaiAGRVDLYEPDA 320
Cdd:cd05909 239 TILLGTPTFLRGYAR---AAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKFG-IRILEGYGTTEC-----SPVISVNTPQS 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 321 FAKRPTIGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpyspgslMYKTGDVVRRLSD 399
Cdd:cd05909 310 PNKEGTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDG-------WYDTGDIGKIDGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 400 GTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQ-EAVVLAVSEGGLQELCAYYTSDQDIEKAELRYQL-SLTLPSHM 477
Cdd:cd05909 383 GFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILkNAGISNLA 462
|
490 500
....*....|....*....|
gi 2214269206 478 IPAFFVQVDAIPLTANGKTD 497
Cdd:cd05909 463 KPSYIHQVEEIPLLGTGKPD 482
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1059-1539 |
4.56e-34 |
|
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: 139.72 E-value: 4.56e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1059 EETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAG--AAFVPIDPDY 1136
Cdd:cd05906 21 ERGPTKGITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGfvPAPLTVPPTY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1137 PDQR-----IEYILQD-------SGAKLLLKQEGISVPDSYTGDVILldgsrTILSLPLDENDEGNPetAVTAENLAYMI 1204
Cdd:cd05906 101 DEPNarlrkLRHIWQLlgspvvlTDAELVAEFAGLETLSGLPGIRVL-----SIEELLDTAADHDLP--QSRPDDLALLM 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1205 YTSGTTGQPKGVMVEHHALVNLC---FWHHDAfsmTAEDRSAKYAGFGFDASIWEM--FPTWTIGAELHVIDEAIRLDIV 1279
Cdd:cd05906 174 LTSGSTGFPKAVPLTHRNILARSagkIQHNGL---TPQDVFLNWVPLDHVGGLVELhlRAVYLGCQQVHVPTEEILADPL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1280 RLNDYFETNGVTITFLP----TQLAEQFMELE-----NTSLRVLLTGGDKLKRAVK-------KPYTLVNN-----YGPT 1338
Cdd:cd05906 251 RWLDLIDRYRVTITWAPnfafALLNDLLEEIEdgtwdLSSLRYLVNAGEAVVAKTIrrllrllEPYGLPPDairpaFGMT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1339 ENTVVAT-----SAEIHPEEGSL-SIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPF 1412
Cdd:cd05906 331 ETCSGVIysrsfPTYDHSQALEFvSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1413 vpgermYRTGDLvKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQD--AAVTAVKDKGGNT-AIAAYVTPE 1488
Cdd:cd05906 411 ------FRTGDL-GFLDNGNLTItGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETeELAIFFVPE 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 1489 TADIEALKSTLKE----------TLPDYMIPafwVTLNELPVTANGKVDRKALPEpDIEAG 1539
Cdd:cd05906 484 YDLQDALSETLRAirsvvsrevgVSPAYLIP---LPKEEIPKTSLGKIQRSKLKA-AFEAG 540
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1052-1531 |
4.87e-34 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 139.43 E-value: 4.87e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1052 KTVHQLFEETVQRHKDRPAVTY---NG--QSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAG 1126
Cdd:PRK08008 7 QHLRQMWDDLADVYGHKTALIFessGGvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1127 AAFVPIDPDYPDQRIEYILQDSGAKLLLKQEG-------ISVPDSYTGDVILL--------DGSRTILSLPLDENDEGNP 1191
Cdd:PRK08008 87 AIMVPINARLLREESAWILQNSQASLLVTSAQfypmyrqIQQEDATPLRHICLtrvalpadDGVSSFTQLKAQQPATLCY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1192 ETAVTAENLAYMIYTSGTTGQPKGVMVEHHalvNLCF-WHHDAF--SMTAEDRsakY----AGFGFDASIWEMFPTWTIG 1264
Cdd:PRK08008 167 APPLSTDDTAEILFTSGTTSRPKGVVITHY---NLRFaGYYSAWqcALRDDDV---YltvmPAFHIDCQCTAAMAAFSAG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1265 AELHVIDE-AIRLDIVRLNDYfetnGVTIT-----FLPTQLAEQFMELE-NTSLRVL---LTGGDKLKRAVKKPY--TLV 1332
Cdd:PRK08008 241 ATFVLLEKySARAFWGQVCKY----RATITecipmMIRTLMVQPPSANDrQHCLREVmfyLNLSDQEKDAFEERFgvRLL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1333 NNYGPTEnTVVATSAEIHPEEGSL-SIGRAIANTRVYILGEGNQVQPEGVAGELC---VAGRGLARGYLNREDETAKRFV 1408
Cdd:PRK08008 317 TSYGMTE-TIVGIIGDRPGDKRRWpSIGRPGFCYEAEIRDDHNRPLPAGEIGEICikgVPGKTIFKEYYLDPKATAKVLE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1409 ADPFV-PGERMYRTGDlvkwvnGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP 1487
Cdd:PRK08008 396 ADGWLhTGDTGYVDEE------GFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 2214269206 1488 ---ETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK08008 470 negETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1067-1530 |
7.54e-34 |
|
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: 139.30 E-value: 7.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTY------NGQSWTYGELNAKANRLARILMDCGiSPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYP--- 1137
Cdd:cd05931 8 DRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTPgrh 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1138 DQRIEYILQDSGAKLLLKQEGISVPDSYTGDVILLDGSRTILSLPLDENDEGN--PETAVTAENLAYMIYTSGTTGQPKG 1215
Cdd:cd05931 87 AERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVVDLLPDTSAAdwPPPSPDPDDIAYLQYTSGSTGTPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1216 VMVEHHALVNLCFWHHDAFSMTAEDRSAK----YAGFGFDASIwemFPTWTIGAELHVIDEA---------IRLdivrLN 1282
Cdd:cd05931 167 VVVTHRNLLANVRQIRRAYGLDPGDVVVSwlplYHDMGLIGGL---LTPLYSGGPSVLMSPAaflrrplrwLRL----IS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1283 DYfetnGVTITFLPT---QLA------EQFMELENTSLRVLLTGG-----DKLKRAVKK--PY-----TLVNNYGPTENT 1341
Cdd:cd05931 240 RY----RATISAAPNfayDLCvrrvrdEDLEGLDLSSWRVALNGAepvrpATLRRFAEAfaPFgfrpeAFRPSYGLAEAT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1342 V-VATS-------------------AEIHPEEGS-----LSIGRAIANTRVYIL-GEGNQVQPEGVAGELCVAGRGLARG 1395
Cdd:cd05931 316 LfVSGGppgtgpvvlrvdrdalagrAVAVAADDPaarelVSCGRPLPDQEVRIVdPETGRELPDGEVGEIWVRGPSVASG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1396 YLNREDETAKRFVADPFVPGERMYRTGDLVKWVNGGIeYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQD----AAVT 1470
Cdd:cd05931 396 YWGRPEATAETFGALAATDEGGWLRTGDLGFLHDGEL-YItGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcvAAFS 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1471 AVKDKGGNTAIAAYV--TPETADIEALKSTLKETLPDymipAFWVTLNE--------LPVTANGKVDRKA 1530
Cdd:cd05931 475 VPDDGEERLVVVAEVerGADPADLAAIAAAIRAAVAR----EHGVAPADvvlvrpgsIPRTSSGKIQRRA 540
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1051-1537 |
8.69e-34 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 139.14 E-value: 8.69e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1051 DKTVHQLFEETVQRHKDRPAVTY--NGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAA 1128
Cdd:PRK12583 17 TQTIGDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1129 FVPIDPDYPDQRIEYILQDSGAKLLlkqegISVPDSYTGDVI---------LLDGSRTILS---LP-------LDEND-- 1187
Cdd:PRK12583 97 LVNINPAYRASELEYALGQSGVRWV-----ICADAFKTSDYHamlqellpgLAEGQPGALAcerLPelrgvvsLAPAPpp 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1188 --------EGNPETaVTAENLAY------------MIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAK--- 1244
Cdd:PRK12583 172 gflawhelQARGET-VSREALAErqasldrddpinIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVpvp 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1245 -YAGFGFdasIWEMFPTWTIGAELHVIDEAIRLDIVrLNDYFETNGVTITFLPTQ-LAE----QFMELENTSLRVLLTGG 1318
Cdd:PRK12583 251 lYHCFGM---VLANLGCMTVGACLVYPNEAFDPLAT-LQAVEEERCTALYGVPTMfIAEldhpQRGNFDLSSLRTGIMAG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1319 DKLKRAVKK--------PYTLVnNYGPTENTVVA--TSAEIHPEEGSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVA 1388
Cdd:PRK12583 327 APCPIEVMRrvmdemhmAEVQI-AYGMTETSPVSlqTTAADDLERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1389 GRGLARGYLNREDETAKRFVADPFvpgerMYrTGDL-VKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDA 1467
Cdd:PRK12583 406 GYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLaTMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADV 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 1468 AVTAVKDKGGNTAIAAYV---TPETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPDIE 1537
Cdd:PRK12583 480 QVFGVPDEKYGEEIVAWVrlhPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIE 552
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
14-495 |
9.52e-34 |
|
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: 139.63 E-value: 9.52e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 14 EKQAQQTPDHSAVKAGGNL------LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPI 87
Cdd:cd17634 60 DRHLRENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVI 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 88 DPDTPEERIRYSLEDSGAKFAV-----------VNERNMTA--------------IGQYEGIIVSLDDGKW--------R 134
Cdd:cd17634 140 FGGFAPEAVAGRIIDSSSRLLItadggvragrsVPLKKNVDdalnpnvtsvehviVLKRTGSDIDWQEGRDlwwrdliaK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 135 NESKERPSSISGSRNLaYVIYTSGTTGKPKGVQIEHRNLTNYVSW-----FSEEAGltenDktvlLSSYAFDLG------ 203
Cdd:cd17634 220 ASPEHQPEAMNAEDPL-FILYTSGTTGKPKGVLHTTGGYLVYAATtmkyvFDYGPG----D----IYWCTADVGwvtghs 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 204 YTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFA-KDANFESLRLIVLGGEKIIPTD 282
Cdd:cd17634 291 YLLYGPLACGATTLLYEGVPNWPTPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAiEGTDRSSLRILGSVGEPINPEA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 283 VIAFRKMYGHTE--FINHYGPTEATIGAIAGRVDLYEPDAfaKRPTigRPIANAGALVLNEALKLVPPGASGQLYITGQ- 359
Cdd:cd17634 371 YEWYWKKIGKEKcpVVDTWWQTETGGFMITPLPGAIELKA--GSAT--RPVFGVQPAVVDNEGHPQPGGTEGNLVITDPw 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 360 -GLARGYLNRPqltaERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAV 438
Cdd:cd17634 447 pGQTRTLFGDH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAA 522
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 439 VLAV-SEGGLQELCAYYT-----SDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:cd17634 523 VVGIpHAIKGQAPYAYVVlnhgvEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGK 585
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
34-501 |
1.23e-33 |
|
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: 138.15 E-value: 1.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNeR 113
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVD-R 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 114 NMTAIGQ--------YEGIIVSLDDGKWRNESKERPSS----ISGSR----------NLAYVI-YTSGTTGKPKGVQIEH 170
Cdd:cd12119 106 DFLPLLEaiaprlptVEHVVVMTDDAAMPEPAGVGVLAyeelLAAESpeydwpdfdeNTAAAIcYTSGTTGNPKGVVYSH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 171 RN--LTNYVSWFSEEAGLTENDkTVLLssyafdlgYTSMFPV---------LLGGGELhiVQKETYTAPDEIAHYIKEHG 239
Cdd:cd12119 186 RSlvLHAMAALLTDGLGLSESD-VVLP--------VVPMFHVnawglpyaaAMVGAKL--VLPGPYLDPASLAELIEREG 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 240 ITYIKLTPSLFHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVIAFRKMYghTEFINHYGPTEA-TIGAIAGR----VD 314
Cdd:cd12119 255 VTFAAGVPTVWQGLLDHLE-ANGRDLSSLRRVVIGGSAVPRSLIEAFEERG--VRVIHAWGMTETsPLGTVARPpsehSN 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 315 LYEPDAFAKRPTIGRPIANAGALVLNEALKLVP--PGASGQLYITGQGLARGYLNRPQlTAERFVENPYspgslmYKTGD 392
Cdd:cd12119 332 LSEDEQLALRAKQGRPVPGVELRIVDDDGRELPwdGKAVGELQVRGPWVTKSYYKNDE-ESEALTEDGW------LRTGD 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 393 VVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQE---LCAYYTSDQDIEKAELRYQL 469
Cdd:cd12119 405 VATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGErplAVVVLKEGATVTAEELLEFL 484
|
490 500 510
....*....|....*....|....*....|..
gi 2214269206 470 SLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd12119 485 ADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1067-1533 |
1.31e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 137.63 E-value: 1.31e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVT--YNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYI 1144
Cdd:PRK09088 10 QRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDAL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1145 LQDSGAKLLLKQEGISvpdsyTGDVILLDGSRTILSLpldENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALv 1224
Cdd:PRK09088 90 LQDAEPRLLLGDDAVA-----AGRTDVEDLAAFIASA---DALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERNL- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1225 nlcfwHHDAFSMTAEDRSAKYAGFGFDASIWEMF-------PTWTIGAELHVID--EAIRlDIVRLNDyfETNGVTITFL 1295
Cdd:PRK09088 161 -----QQTAHNFGVLGRVDAHSSFLCDAPMFHIIglitsvrPVLAVGGSILVSNgfEPKR-TLGRLGD--PALGITHYFC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1296 PTQLAEQFMELEN------TSLRVLLTGG-----DKLKRAVKKPYTLVNNYGPTE-NTVVATSAE---IHPEEGSLSIGR 1360
Cdd:PRK09088 233 VPQMAQAFRAQPGfdaaalRHLTALFTGGaphaaEDILGWLDDGIPMVDGFGMSEaGTVFGMSVDcdvIRAKAGAAGIPT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1361 AIANTRVyILGEGNQVqPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermYRTGDLVKWVNGGieYIGRIDQ 1440
Cdd:PRK09088 313 PTVQTRV-VDDQGNDC-PAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGDIARRDADG--FFWVVDR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1441 QVKV---RGYRIELSEIEVQLAQLSEVQDAAVTAVKDK--GGNTAIAAYVTPETA-DIEALKSTLKETLPDYMIPAFWVT 1514
Cdd:PRK09088 383 KKDMfisGGENVYPAEIEAVLADHPGIRECAVVGMADAqwGEVGYLAIVPADGAPlDLERIRSHLSTRLAKYKVPKHLRL 462
|
490
....*....|....*....
gi 2214269206 1515 LNELPVTANGKVDRKALPE 1533
Cdd:PRK09088 463 VDALPRTASGKLQKARLRD 481
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1050-1531 |
1.74e-33 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 137.96 E-value: 1.74e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1050 TDKTVHQLFEETVQRHKDRPAVTYN-GQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAA 1128
Cdd:PRK06087 21 GDASLADYWQQTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1129 FVPIDPDYPDQRIEYILQDSGAKLLL----------KQEGISVPDS--YTGDVILLDGSRTILSLP-----LDENDEGNP 1191
Cdd:PRK06087 101 SVPLLPSWREAELVWVLNKCQAKMFFaptlfkqtrpVDLILPLQNQlpQLQQIVGVDKLAPATSSLslsqiIADYEPLTT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1192 ETAVTAENLAYMIYTSGTTGQPKGVMVEHH----------ALVNLC----------------FWHHDAFSMTAEDRSAKY 1245
Cdd:PRK06087 181 AITTHGDELAAVLFTSGTEGLPKGVMLTHNnilaseraycARLNLTwqdvfmmpaplghatgFLHGVTAPFLIGARSVLL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1246 AGFGFDASIWEMFP---TWTIGAELHVIDeairldivrlndyfetngvtitfLPTQLAEQFMELEntSLRVLLTGG---- 1318
Cdd:PRK06087 261 DIFTPDACLALLEQqrcTCMLGATPFIYD-----------------------LLNLLEKQPADLS--ALRFFLCGGttip 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1319 -DKLKRAVKKPYTLVNNYGPTENT--VVATSAEIHPEEGSLSiGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARG 1395
Cdd:PRK06087 316 kKVARECQQRGIKLLSVYGSTESSphAVVNLDDPLSRFMHTD-GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1396 YLNREDETAKRFVADPFvpgermYRTGDLVKW-VNGGIEYIGRiDQQVKVR-GYRIELSEIEVQLAQLSEVQDAAVTAVK 1473
Cdd:PRK06087 395 YLDEPELTARALDEEGW------YYSGDLCRMdEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMP 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 1474 DKGGNTAIAAYV-------TPETADIEALKStlKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK06087 468 DERLGERSCAYVvlkaphhSLTLEEVVAFFS--RKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
13-503 |
1.80e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 136.83 E-value: 1.80e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 13 FEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIvAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTP 92
Cdd:PRK07638 7 YKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTI-AILLENRIEFLQLFAGAAMAGWTCVPLDIKWK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 93 EERIRYSLEDSGAKFAVVNERNMTAIGQYEGIIVSLDdgKWR---NESKERPSSISGSRNLA-YVIYTSGTTGKPKGVQI 168
Cdd:PRK07638 86 QDELKERLAISNADMIVTERYKLNDLPDEEGRVIEID--EWKrmiEKYLPTYAPIENVQNAPfYMGFTSGSTGKPKAFLR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 169 EHRNLTNYVSWFSEEAGLTENDKTV----LLSSYaFDLGYTSmfpVLLGGGELHIVQKETytaPDEIAHYIKEHGITYIK 244
Cdd:PRK07638 164 AQQSWLHSFDCNVHDFHMKREDSVLiagtLVHSL-FLYGAIS---TLYVGQTVHLMRKFI---PNQVLDKLETENISVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 245 LTPSLfhtivnTASFAKDANF-ESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIgaiagrVDLYEPDAFAK 323
Cdd:PRK07638 237 TVPTM------LESLYKENRViENKMKIISSGAKWEAEAKEKIKNIFPYAKLYEFYGASELSF------VTALVDEESER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 324 RPT-IGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAErfvenpYSPGSLMyKTGDVVRRLSDGTL 402
Cdd:PRK07638 305 RPNsVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIGGVLARE------LNADGWM-TVRDVGYEDEEGFI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 403 AFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYTsDQDIEKAELRYQLSLTLPSHMIPAFF 482
Cdd:PRK07638 378 YIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAII-KGSATKQQLKSFCLQRLSSFKIPKEW 456
|
490 500
....*....|....*....|.
gi 2214269206 483 VQVDAIPLTANGKTDRNALPK 503
Cdd:PRK07638 457 HFVDEIPYTNSGKIARMEAKS 477
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
33-501 |
2.38e-33 |
|
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: 137.41 E-value: 2.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDP----DTPEERIR-----YSLEDS 103
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVpptyDEPNARLRklrhiWQLLGS 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 104 G---AKFAVVNE-RNMTAIGQYEGIIVSLDDGKwRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSW 179
Cdd:cd05906 120 PvvlTDAELVAEfAGLETLSGLPGIRVLSIEEL-LDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 180 FSEEAGLTENDktVLLSSYAFD----LGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITyIKLTPSLFHTIVN 255
Cdd:cd05906 199 KIQHNGLTPQD--VFLNWVPLDhvggLVELHLRAVYLGCQQVHVPTEEILADPLRWLDLIDRYRVT-ITWAPNFAFALLN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 256 TASFA---KDANFESLRLIVLGGEKIIPTDVIAFRKM---YGHTEFINH--YGPTEATIGAIAGRVDLYEP----DAFAK 323
Cdd:cd05906 276 DLLEEiedGTWDLSSLRYLVNAGEAVVAKTIRRLLRLlepYGLPPDAIRpaFGMTETCSGVIYSRSFPTYDhsqaLEFVS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 324 rptIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVrRLSDGTLA 403
Cdd:cd05906 356 ---LGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------FRTGDLG-FLDNGNLT 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 404 FIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVS----EGGLQELCAYYTSDQDIEKA------ELRYQLSLTL 473
Cdd:cd05906 426 ITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAvrdpGAETEELAIFFVPEYDLQDAlsetlrAIRSVVSREV 505
|
490 500 510
....*....|....*....|....*....|.
gi 2214269206 474 ---PSHMIPaffVQVDAIPLTANGKTDRNAL 501
Cdd:cd05906 506 gvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1341-1623 |
3.03e-33 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 131.41 E-value: 3.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1341 TVVATSAEIHPEEGSLSIGRAIANTRVYILGEGNQVQPEGVAGElcVAGRGLARGYLNREDETAKRFVADPFVPGERMYR 1420
Cdd:COG3433 3 IATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGE--GGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1421 TGDLVKWVN----GGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGN---TAIAAYVTPETADIE 1493
Cdd:COG3433 81 QADDLRLLLrrglGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGlllIVGAVAALDGLAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1494 ALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPDIEAGSGEYKAPTTDM---EELLAGIWQDVLGMS--EVG 1568
Cdd:COG3433 161 ALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETaltEEELRADVAELLGVDpeEID 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 1569 VTDNFFSLGGDSIKGIQMASRLNQHGWKLEMKDLFQHPTIEELTQYVERAEGKQA 1623
Cdd:COG3433 241 PDDNLFDLGLDSIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
14-517 |
5.38e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 136.45 E-value: 5.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 14 EKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPD-TP 92
Cdd:PRK07786 24 ARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRlTP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 93 EErIRYSLEDSGAKfAVVNE----------RN--------MTAIGQYEGIIVSLDDGKWRNESKERPSSISGSrNLAYVI 154
Cdd:PRK07786 104 PE-IAFLVSDCGAH-VVVTEaalapvatavRDivpllstvVVAGGSSDDSVLGYEDLLAEAGPAHAPVDIPND-SPALIM 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 155 YTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDL-GYTSMFPVLLGGGELHIVQKETYTaPDEIAH 233
Cdd:PRK07786 181 YTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIaGIGSMLPGLLLGAPTVIYPLGAFD-PGQLLD 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 234 YIKEHGITYIKLTPSLFHTIVnTASFAKDANFeSLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEAT-IGAIagr 312
Cdd:PRK07786 260 VLEAEKVTGIFLVPAQWQAVC-AEQQARPRDL-ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSpVTCM--- 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 313 vdLYEPDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpyspgslMYKTGD 392
Cdd:PRK07786 335 --LLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGG-------WFHSGD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 393 VVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQE----LCAYYTSDQDIEKAELRYQ 468
Cdd:PRK07786 406 LVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEvpvaVAAVRNDDAALTLEDLAEF 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 469 LSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALPKPNAAQS---GGKALAAP 517
Cdd:PRK07786 486 LTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYGACVnveRRSASAGF 537
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
6-501 |
7.06e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 136.03 E-value: 7.06e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 6 EATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFL 85
Cdd:PRK06164 9 ADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 86 PIDPDTPEERIRYSLEDSGAK-------------FAVVNERNMTAIGQYEGIIVSLDD-----GKWRNESKE-------R 140
Cdd:PRK06164 89 AVNTRYRSHEVAHILGRGRARwlvvwpgfkgidfAAILAAVPPDALPPLRAIAVVDDAadatpAPAPGARVQlfalpdpA 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 141 PSSISGSR----NLAYVIYT-SGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGG 215
Cdd:PRK06164 169 PPAAAGERaadpDAGALLFTtSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 216 ELHIVqkETYTAPdEIAHYIKEHGITYIKLTPSLFHTIVNTAsfAKDANFESLRLivLGGEKIIPT--DVIAFRKMYGhT 293
Cdd:PRK06164 249 PLVCE--PVFDAA-RTARALRRHRVTHTFGNDEMLRRILDTA--GERADFPSARL--FGFASFAPAlgELAALARARG-V 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 294 EFINHYGPTEATIGAIAGRVDlyePDAFAKRPTIGRPIANAGALVLNEAL--KLVPPGASGQLYITGQGLARGYLNRPQL 371
Cdd:PRK06164 321 PLTGLYGSSEVQALVALQPAT---DPVSVRIEGGGRPASPEARVRARDPQdgALLPDGESGEIEIRAPSLMRGYLDNPDA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 372 TAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELC 451
Cdd:PRK06164 398 TARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 452 AYY--TSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLT--ANG-KTDRNAL 501
Cdd:PRK06164 472 AFVipTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesANGaKIQKHRL 526
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1077-1531 |
1.15e-32 |
|
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: 132.86 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1077 SWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLllkq 1156
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1157 egisvpdsytgdvilldgsrtilslpldendegnpetavtaENLAYMIYTSGTTGQPKGVMV--EHHalvnlcFWHhdAF 1234
Cdd:cd05912 77 -----------------------------------------DDIATIMYTSGTTGKPKGVQQtfGNH------WWS--AI 107
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1235 SmtaedrSAKYAGFGFDASIWEMFPTWTIGAeLHVIDEAIRLDI-VRLNDYFETNGVT----------ITFLPT---QLA 1300
Cdd:cd05912 108 G------SALNLGLTEDDNWLCALPLFHISG-LSILMRSVIYGMtVYLVDKFDAEQVLhlinsgkvtiISVVPTmlqRLL 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1301 EQFMELENTSLRVLLTGG-----DKLKRAVKKPYTLVNNYGPTE--NTVVATSAEIHPEEGSlSIGRAIANTRVYILGEG 1373
Cdd:cd05912 181 EILGEGYPNNLRCILLGGgpapkPLLEQCKEKGIPVYQSYGMTEtcSQIVTLSPEDALNKIG-SAGKPLFPVELKIEDDG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1374 nqvQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermyRTGDlvkwvnggieyIGRIDQQ----VKVR---- 1445
Cdd:cd05912 260 ---QPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGD-----------IGYLDEEgflyVLDRrsdl 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1446 ----GYRIELSEIEVQLAQLSEVQDAAVTAVKD-KGGNTAIAAYVTPETADIEALKSTLKETLPDYMIPAFWVTLNELPV 1520
Cdd:cd05912 319 iisgGENIYPAEIEEVLLSHPAIKEAGVVGIPDdKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPR 398
|
490
....*....|.
gi 2214269206 1521 TANGKVDRKAL 1531
Cdd:cd05912 399 TASGKLLRHEL 409
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1050-1526 |
1.24e-32 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 135.71 E-value: 1.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1050 TDKTVHQLFEETVQRHKDRPAVTYNGQS--WTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGA 1127
Cdd:PRK08315 14 LEQTIGQLLDRTAARYPDREALVYRDQGlrWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1128 AFVPIDPDYPDQRIEYILQDSGAKLLLKQEGIS-----------VPDSYTGD--------------VILLDGSRTILSLP 1182
Cdd:PRK08315 94 ILVTINPAYRLSELEYALNQSGCKALIAADGFKdsdyvamlyelAPELATCEpgqlqsarlpelrrVIFLGDEKHPGMLN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1183 LDE-----NDEGNPETAVTAENLAY-----MIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDR----------- 1241
Cdd:PRK08315 174 FDEllalgRAVDDAELAARQATLDPddpinIQYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRlcipvplyhcf 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1242 --------------SAKYAGFGFDAsiwemfptwtiGAELHVIDE----AIrldivrlndYfetnGVtitflPTQ-LAE- 1301
Cdd:PRK08315 254 gmvlgnlacvthgaTMVYPGEGFDP-----------LATLAAVEEerctAL---------Y----GV-----PTMfIAEl 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1302 ---QFMELENTSLRvllTG---G-----DKLKRAVKKPY----TLVnnYGPTENTVVATSAEIH-PEEGSLS-IGRAIAN 1364
Cdd:PRK08315 305 dhpDFARFDLSSLR---TGimaGspcpiEVMKRVIDKMHmsevTIA--YGMTETSPVSTQTRTDdPLEKRVTtVGRALPH 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1365 TRVYILG-EGNQVQPEGVAGELCVAGRGLARGYLNREDETAKrfVADPfvpgERMYRTGDL-VKWVNGGIEYIGRIDQQV 1442
Cdd:PRK08315 380 LEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAE--AIDA----DGWMHTGDLaVMDEEGYVNIVGRIKDMI 453
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1443 kVRG----Y-RielsEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP---ETADIEALKSTLKETLPDYMIPAFWVT 1514
Cdd:PRK08315 454 -IRGgeniYpR----EIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILrpgATLTEEDVRDFCRGKIAHYKIPRYIRF 528
|
570
....*....|..
gi 2214269206 1515 LNELPVTANGKV 1526
Cdd:PRK08315 529 VDEFPMTVTGKI 540
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1056-1531 |
2.17e-32 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 134.76 E-value: 2.17e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1056 QLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPD 1135
Cdd:PRK07059 27 DLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1136 YPDQRIEYILQDSGAKLLLKQEGIS--------------VPDSYTGDVILLDGS------RTI------LSLP--LDEND 1187
Cdd:PRK07059 107 YTPRELEHQLKDSGAEAIVVLENFAttvqqvlaktavkhVVVASMGDLLGFKGHivnfvvRRVkkmvpaWSLPghVRFND 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1188 ---EG-----NPETaVTAENLAYMIYTSGTTGQPKGVMVEHHALV----NLCFWHHDAFsmtaeDRSAKYAGFGFDASIw 1255
Cdd:PRK07059 187 alaEGarqtfKPVK-LGPDDVAFLQYTGGTTGVSKGATLLHRNIVanvlQMEAWLQPAF-----EKKPRPDQLNFVCAL- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1256 emfPTWTIGAeLHVID-EAIRL-----------DI---VRLNDYFETN---GVTITFLPTQLAEQFMELENTSLRVLLTG 1317
Cdd:PRK07059 260 ---PLYHIFA-LTVCGlLGMRTggrnilipnprDIpgfIKELKKYQVHifpAVNTLYNALLNNPDFDKLDFSKLIVANGG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1318 GDKLKRAVKKPYT------LVNNYGPTENTVVATSAEIHPEEGSLSIGRAIANTRVYILGE-GNQVqPEGVAGELCVAGR 1390
Cdd:PRK07059 336 GMAVQRPVAERWLemtgcpITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDdGNDL-PLGEPGEICIRGP 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1391 GLARGYLNREDETAKRFVADPFvpgermYRTGDL-VKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAV 1469
Cdd:PRK07059 415 QVMAGYWNRPDETAKVMTADGF------FRTGDVgVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAA 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2214269206 1470 TAVKDKGGNTAIAAYVTPETADI--EALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK07059 489 VGVPDEHSGEAVKLFVVKKDPALteEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1067-1531 |
2.34e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 133.19 E-value: 2.34e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARilmdcGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:PRK07787 15 IADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLKqegiSVPDSYTG----DVILLDGSrtilSLPLDENDEGNPetavtaenlAYMIYTSGTTGQPKGVMVEHHA 1222
Cdd:PRK07787 90 DSGAQAWLG----PAPDDPAGlphvPVRLHARS----WHRYPEPDPDAP---------ALIVYTSGTTGPPKGVVLSRRA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1223 LVNLCFWHHDAFSMTAED----------------------------------RSAKYAG-FGFDASIWEMFPT-WTIGAE 1266
Cdd:PRK07787 153 IAADLDALAEAWQWTADDvlvhglplfhvhglvlgvlgplrignrfvhtgrpTPEAYAQaLSEGGTLYFGVPTvWSRIAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1267 lhVIDEAIRLDIVRLndyfETNGVTItfLPTQLAEQFMELenTSLRVlltggdklkravkkpytlVNNYGPTEnTVVATS 1346
Cdd:PRK07787 233 --DPEAARALRGARL----LVSGSAA--LPVPVFDRLAAL--TGHRP------------------VERYGMTE-TLITLS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1347 AEIHPEEGSLSIGRAIANTRVYILGE-GNQVQPEGVA-GELCVAGRGLARGYLNREDETAKRFVADPFvpgermYRTGDL 1424
Cdd:PRK07787 284 TRADGERRPGWVGLPLAGVETRLVDEdGGPVPHDGETvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDV 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1425 -VKWVNGGIEYIGR--IDqQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPET-ADIEALKSTLK 1500
Cdd:PRK07787 358 aVVDPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADdVAADELIDFVA 436
|
490 500 510
....*....|....*....|....*....|.
gi 2214269206 1501 ETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK07787 437 QQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1052-1531 |
4.96e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 134.12 E-value: 4.96e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1052 KTVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMD-CGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFV 1130
Cdd:PRK05677 24 PNIQAVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQhTDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1131 PIDPDYPDQRIEYILQDSGAKLLL-------KQEGIsVPDSYTGDVI------LLDGSRTIL---------------SLP 1182
Cdd:PRK05677 104 NTNPLYTAREMEHQFNDSGAKALVclanmahLAEKV-LPKTGVKHVIvtevadMLPPLKRLLinavvkhvkkmvpayHLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1183 --LDEND-----EGNPETAVT--AENLAYMIYTSGTTGQPKGVMVEHHALVN-----------------------LCFWH 1230
Cdd:PRK05677 183 qaVKFNDalakgAGQPVTEANpqADDVAVLQYTGGTTGVAKGAMLTHRNLVAnmlqcralmgsnlnegceiliapLPLYH 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1231 HDAFSMTAedrsakyagfgfdasiweMFpTWTIGAELHVIDEAIRLD--IVRLNDYFETNGVTITFLPTQLA--EQFMEL 1306
Cdd:PRK05677 263 IYAFTFHC------------------MA-MMLIGNHNILISNPRDLPamVKELGKWKFSGFVGLNTLFVALCnnEAFRKL 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1307 ENTSLRVLLTGGDKLKRAVKKPYTLVNN------YGPTENTVVATsaeIHPEEGSL--SIGRAIANTRVYILGEGNQVQP 1378
Cdd:PRK05677 324 DFSALKLTLSGGMALQLATAERWKEVTGcaicegYGMTETSPVVS---VNPSQAIQvgTIGIPVPSTLCKVIDDDGNELP 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1379 EGVAGELCVAGRGLARGYLNREDETAKRFVADPFVpgermyRTGDL-VKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQ 1457
Cdd:PRK05677 401 LGEVGELCVKGPQVMKGYWQRPEATDEILDSDGWL------KTGDIaLIQEDGYMRIVDRKKDMILVSGFNVYPNELEDV 474
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214269206 1458 LAQLSEVQDAAVTAVKDKGGNTAIAAYVTP---ETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK05677 475 LAALPGVLQCAAIGVPDEKSGEAIKVFVVVkpgETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1044-1533 |
5.76e-32 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 133.55 E-value: 5.76e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1044 KALPVPTDKTVHQLfEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMD-CGISPDDRVGVLTKPSLEMSAAVLGV 1122
Cdd:PRK08314 3 KSLTLPETSLFHNL-EVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1123 LKAGAAFVPIDPDYPDQRIEYILQDSGAKL-------------------------------LLKQEGISVPDSYTGDVIL 1171
Cdd:PRK08314 82 LRANAVVVPVNPMNREEELAHYVTDSGARVaivgselapkvapavgnlrlrhvivaqysdyLPAEPEIAVPAWLRAEPPL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1172 --LDGSRTIL-SLPLDENDEGNPETAvTAENLAYMIYTSGTTGQPKGVMVEH----HALVNLCFWhhdaFSMTAEDRSAK 1244
Cdd:PRK08314 162 qaLAPGGVVAwKEALAAGLAPPPHTA-GPDDLAVLPYTSGTTGVPKGCMHTHrtvmANAVGSVLW----SNSTPESVVLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1245 YAGF--------GFDASIWE-----MFPTWTigaelhvIDEAIRLdivrlndyFETNGVTI-TFLPTQLAE-----QFME 1305
Cdd:PRK08314 237 VLPLfhvtgmvhSMNAPIYAgatvvLMPRWD-------REAAARL--------IERYRVTHwTNIPTMVVDflaspGLAE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1306 LENTSLRVLLTGGDKLKRAV----KKPYTL--VNNYGPTEntvvaTSAEIH------PEEGSLSIGRAIANTRVyILGEG 1373
Cdd:PRK08314 302 RDLSSLRYIGGGGAAMPEAVaerlKELTGLdyVEGYGLTE-----TMAQTHsnppdrPKLQCLGIPTFGVDARV-IDPET 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1374 NQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVAdpfVPGERMYRTGDLvkwvnggieyiGRIDQQ------------ 1441
Cdd:PRK08314 376 LEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDL-----------GRMDEEgyffitdrlkrm 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1442 VKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYV--------TPETADIEALKstlKETLPDYMIPAFWV 1513
Cdd:PRK08314 442 INASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGETVKAVVvlrpeargKTTEEEIIAWA---REHMAAYKYPRIVE 518
|
570 580
....*....|....*....|
gi 2214269206 1514 TLNELPVTANGKVDRKALPE 1533
Cdd:PRK08314 519 FVDSLPKSGSGKILWRQLQE 538
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
33-439 |
1.11e-31 |
|
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: 131.33 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNe 112
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 rnmtaigqyegiivslddgkwrneskerpssiSGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKT 192
Cdd:cd17640 85 --------------------------------NDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGDRF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 193 VLL----SSYAFDLGYTsmfpVLLGGGElhivqkETYTAPDEIAHYIKEHGITYIKLTPSLFHTI-------VNTASFAK 261
Cdd:cd17640 133 LSIlpiwHSYERSAEYF----IFACGCS------QAYTSIRTLKDDLKRVKPHYIVSVPRLWESLysgiqkqVSKSSPIK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 262 DANFESLrliVLGGEKI--------IPTDVIAFRKMYGhTEFINHYGPTEATIGAIAGRvdLYEPdafaKRPTIGRPIAN 333
Cdd:cd17640 203 QFLFLFF---LSGGIFKfgisgggaLPPHVDTFFEAIG-IEVLNGYGLTETSPVVSARR--LKCN----VRGSVGRPLPG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 334 AGA-LVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQV 412
Cdd:cd17640 273 TEIkIVDPEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAKDTI 346
|
410 420
....*....|....*....|....*...
gi 2214269206 413 KIR-GYRIEPKEIETVMLSLSGIQEAVV 439
Cdd:cd17640 347 VLSnGENVEPQPIEEALMRSPFIEQIMV 374
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
16-501 |
1.72e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 131.08 E-value: 1.72e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 16 QAQQTPDHSAVK--AGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPE 93
Cdd:PRK09088 4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 94 ERIRYSLEDSGAKFaVVNERNMTAIGQyegIIVSLDD----------GKWRNESKERPSSIsgsrnlayvIYTSGTTGKP 163
Cdd:PRK09088 84 SELDALLQDAEPRL-LLGDDAVAAGRT---DVEDLAAfiasadalepADTPSIPPERVSLI---------LFTSGTSGQP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 164 KGVQIEHRNLTNYVSWFSEeAGLTENDKTVLLSSYAFD-LGY-TSMFPVLLGGGELHIVQ----KETYTAPDEIAHyike 237
Cdd:PRK09088 151 KGVMLSERNLQQTAHNFGV-LGRVDAHSSFLCDAPMFHiIGLiTSVRPVLAVGGSILVSNgfepKRTLGRLGDPAL---- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 238 hGITYIKLTPSLFHTIVNTASFAKDAnFESLRLIVLGGEKIIPTDVIAFrkMYGHTEFINHYGPTEA-TIGAIAGRVDLY 316
Cdd:PRK09088 226 -GITHYFCVPQMAQAFRAQPGFDAAA-LRHLTALFTGGAPHAAEDILGW--LDDGIPMVDGFGMSEAgTVFGMSVDCDVI 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 317 EpdafAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRR 396
Cdd:PRK09088 302 R----AKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGDIARR 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 397 LSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSE---GGLQELCAYYTSDQDIEKAELRYQLSLTL 473
Cdd:PRK09088 372 DADGFFWVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADaqwGEVGYLAIVPADGAPLDLERIRSHLSTRL 451
|
490 500
....*....|....*....|....*...
gi 2214269206 474 PSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK09088 452 AKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
25-501 |
1.95e-31 |
|
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: 129.91 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 25 AVKAGGNLLTYRELDEQANQLAHHLRAQGA---GNEdiVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLE 101
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLVGELGivpGNR--VLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 102 DSGAKFAVVNERnmtaigqyegiivslddgkwrneskerpssISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFS 181
Cdd:cd05958 81 KARITVALCAHA------------------------------LTASDDICILAFTSGTTGAPKATMHFHRDPLASADRYA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 182 EEA-GLTENDKTVLLSSYAFDLGYTSM--FPVLLGGGELHIVQketyTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTAS 258
Cdd:cd05958 131 VNVlRLREDDRFVGSPPLAFTFGLGGVllFPFGVGASGVLLEE----ATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPD 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 259 FAKdANFESLRLIVLGGEKIIPTDVIAFRKMYGhTEFINHYGPTEATIGAIAGRVDlyepdafAKRP-TIGRPIANAGAL 337
Cdd:cd05958 207 AAG-PDLSSLRKCVSAGEALPAALHRAWKEATG-IPIIDGIGSTEMFHIFISARPG-------DARPgATGKPVPGYEAK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 338 VLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTaerfvenpYSPGSLMYkTGDVVRRLSDGTLAFIGRADDQVKIRGY 417
Cdd:cd05958 278 VVDDEGNPVPDGTIGRLAVRGPTGCRYLADKRQRT--------YVQGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGY 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 418 RIEPKEIETVMLSLSGIQE-AVVLAVSEGGLQELCAY------YTSDQDIeKAELRYQLSLTLPSHMIPAFFVQVDAIPL 490
Cdd:cd05958 349 NIAPPEVEDVLLQHPAVAEcAVVGHPDESRGVVVKAFvvlrpgVIPGPVL-ARELQDHAKAHIAPYKYPRAIEFVTELPR 427
|
490
....*....|.
gi 2214269206 491 TANGKTDRNAL 501
Cdd:cd05958 428 TATGKLQRFAL 438
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
33-441 |
2.29e-31 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 130.02 E-value: 2.29e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVne 112
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 rnmtaigqyegiivslddgkwrneskerpssiSGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKT 192
Cdd:cd05907 84 --------------------------------EDPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 193 VLL--SSYAFDLGYTSMFPVLLGGgelHIVqketYTAPDE-IAHYIKEHGITYIKLTPSLFHTIVNTASFAKD------- 262
Cdd:cd05907 132 LSFlpLAHVFERRAGLYVPLLAGA---RIY----FASSAEtLLDDLSEVRPTVFLAVPRVWEKVYAAIKVKAVpglkrkl 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 263 ---ANFESLRLIVLGGEKiIPTDVIAFRKMYGHTeFINHYGPTEaTIGAIAgrvdLYEPDAFaKRPTIGRPIANAGalvl 339
Cdd:cd05907 205 fdlAVGGRLRFAASGGAP-LPAELLHFFRALGIP-VYEGYGLTE-TSAVVT----LNPPGDN-RIGTVGKPLPGVE---- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 340 neaLKLVPpgaSGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADD-QVKIRGYR 418
Cdd:cd05907 273 ---VRIAD---DGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDlIITSGGKN 340
|
410 420
....*....|....*....|...
gi 2214269206 419 IEPKEIETVMLSLSGIQEAVVLA 441
Cdd:cd05907 341 ISPEPIENALKASPLISQAVVIG 363
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
155-501 |
2.62e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 127.39 E-value: 2.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 155 YTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDK-------------------------TVLLSSYAFDlgytsmfP 209
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRlcipvplfhcfgsvlgvlaclthgaTMVFPSPSFD-------P 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 210 VLLgggeLHIVQKETYTApdeiahyikEHGityiklTPSLFHTIVNTASFAKdANFESLRLIVLGGeKIIPTDVI-AFRK 288
Cdd:cd05917 82 LAV----LEAIEKEKCTA---------LHG------VPTMFIAELEHPDFDK-FDLSSLRTGIMAG-APCPPELMkRVIE 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 289 MYGHTEFINHYGPTEATIGAIAGRVDlyepDAFAKR-PTIGRPIANAGALVLNEALKLVPP-GASGQLYITGQGLARGYL 366
Cdd:cd05917 141 VMNMKDVTIAYGMTETSPVSTQTRTD----DSIEKRvNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 367 NRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVkIRG-YRIEPKEIETVMLSLSGIQEAVVLAVSEG 445
Cdd:cd05917 217 NDPEKTAEAIDGDGW------LHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDE 289
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 446 GL-QELCAYY--TSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd05917 290 RYgEEVCAWIrlKEGAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1052-1531 |
3.31e-31 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 131.54 E-value: 3.31e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1052 KTVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILM-DCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFV 1130
Cdd:PRK08751 25 RTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1131 PIDPDYPDQRIEYILQDSGAKLLLKQEGIS------VPDSYTGDVI------LLDGSRTIL---------SLPLDENDEG 1189
Cdd:PRK08751 105 NVNPLYTPRELKHQLIDSGASVLVVIDNFGttvqqvIADTPVKQVIttglgdMLGFPKAALvnfvvkyvkKLVPEYRING 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1190 N---------------PETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAK---------Y 1245
Cdd:PRK08751 185 AirfrealalgrkhsmPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEGCevvitalplY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1246 AGFGFDASIWEMFptwTIGAELHVIDE-------AIRLDIVRLNDYfetNGVTITFLPTQLAEQFMELENTSLRVLLTGG 1318
Cdd:PRK08751 265 HIFALTANGLVFM---KIGGCNHLISNprdmpgfVKELKKTRFTAF---TGVNTLFNGLLNTPGFDQIDFSSLKMTLGGG 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1319 DKLKRAVKKPY------TLVNNYGPTENTVVATSAEIHPEEGSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGL 1392
Cdd:PRK08751 339 MAVQRSVAERWkqvtglTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1393 ARGYLNREDETAKRFVADPFVpgermyRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTA 1471
Cdd:PRK08751 419 MKGYWKRPEETAKVMDADGWL------HTGDIARMDEQGFVYIvDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVG 492
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 1472 VKDKGGNTAIAAYVTPETADI--EALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK08751 493 VPDEKSGEIVKVVIVKKDPALtaEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
29-498 |
3.40e-31 |
|
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: 129.87 E-value: 3.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 29 GGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFa 108
Cdd:cd05914 4 GGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 109 vvnernmtaigqyegIIVSLDDgkwrneskerpssisgsrNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTE 188
Cdd:cd05914 83 ---------------IFVSDED------------------DVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 189 NDKTV--LLSSYAFDLGYTSMFPVLLGGgelHIV-------------QKETYT------APDEIAHYIKEHGITYIKLTP 247
Cdd:cd05914 130 GDKILsiLPLHHIYPLTFTLLLPLLNGA---HVVfldkipsakiialAFAQVTptlgvpVPLVIEKIFKMDIIPKLTLKK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 248 SLF--HTIVNTASFAK-------DANFESLRLIVLGGEKIIPtDVIAFRKMYGHTeFINHYGPTEatigaiAGRVDLYEP 318
Cdd:cd05914 207 FKFklAKKINNRKIRKlafkkvhEAFGGNIKEFVIGGAKINP-DVEEFLRTIGFP-YTIGYGMTE------TAPIISYSP 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 319 DAFAKRPTIGRPIANAGALVLNEAlklvPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLS 398
Cdd:cd05914 279 PNRIRLGSAGKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKIDA 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 399 DGTLAFIGRADDQ-VKIRGYRIEPKEIETVMLSLSGIQEAVVlAVSEGGLQELCAYYTSDQDIE-----------KAELR 466
Cdd:cd05914 349 EGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLV-VVQEKKLVALAYIDPDFLDVKalkqrniidaiKWEVR 427
|
490 500 510
....*....|....*....|....*....|...
gi 2214269206 467 YQLSLTLPSH-MIPAFFVQVDAIPLTANGKTDR 498
Cdd:cd05914 428 DKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
14-442 |
3.70e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 130.85 E-value: 3.70e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 14 EKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQ-GAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTP 92
Cdd:PRK08314 17 EVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 93 EERIRYSLEDSGAKFAVVN----ERNMTAIG--QYEGIIV--------------------------SLDDG---KWRNES 137
Cdd:PRK08314 97 EEELAHYVTDSGARVAIVGselaPKVAPAVGnlRLRHVIVaqysdylpaepeiavpawlraepplqALAPGgvvAWKEAL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 138 KER---PSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNL-TNYVS---WFseeaGLTENDktVLLSSYAF--DLGYTSMF 208
Cdd:PRK08314 177 AAGlapPPHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVmANAVGsvlWS----NSTPES--VVLAVLPLfhVTGMVHSM 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 209 --PVLLGGGELHIVQKETYTAPDEIAHYikehGITYIKLTPSLFHTIVNTASFAkDANFESLRLIVlGGEKIIPtDVIAf 286
Cdd:PRK08314 251 naPIYAGATVVLMPRWDREAAARLIERY----RVTHWTNIPTMVVDFLASPGLA-ERDLSSLRYIG-GGGAAMP-EAVA- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 287 RKMYGHT--EFINHYGPTEaTIGAIagrvdLYEPDAFAKRPTIGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLAR 363
Cdd:PRK08314 323 ERLKELTglDYVEGYGLTE-TMAQT-----HSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFK 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 364 GYLNRPQLTAERFVEnpySPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV 442
Cdd:PRK08314 397 GYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIAT 472
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1056-1539 |
4.04e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 130.55 E-value: 4.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1056 QLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPD 1135
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1136 YPDQRIEYILQDSGAKLLLKQ-------EGISVPDSYTGDVILLDGSRTILSLP--LDEN-DEGNPETAVTAENLAYMIY 1205
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHadfpehaAAVRAASPDLTHVVAIGGARAGLDYEalVARHlGARVANAAVDHDDPCWFFF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1206 TSGTTGQPKGVMVEHH--ALV---NLCfwhhDAFSMTAE-DRSAKYAGFGFDASIWEMFPTwTIGAELhVIDEAIRLDIV 1279
Cdd:PRK07470 171 TSGTTGRPKAAVLTHGqmAFVitnHLA----DLMPGTTEqDASLVVAPLSHGAGIHQLCQV-ARGAAT-VLLPSERFDPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1280 RLNDYFETNGVTITF-LPTQL--------AEQFmelENTSLRVLLTGGDKL-----KRAVKK-PYTLVNNYGPTENTVVA 1344
Cdd:PRK07470 245 EVWALVERHRVTNLFtVPTILkmlvehpaVDRY---DHSSLRYVIYAGAPMyradqKRALAKlGKVLVQYFGLGEVTGNI 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1345 T-------SAEIHPEEGSLSIGRAIANTRVYIL-GEGNQVQPeGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpge 1416
Cdd:PRK07470 322 TvlppalhDAEDGPDARIGTCGFERTGMEVQIQdDEGRELPP-GETGEICVIGPAVFAGYYNNPEANAKAFRDGWF---- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1417 rmyRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKD-KGGNTAIAAYVTPETADI-- 1492
Cdd:PRK07470 397 ---RTGDLGHLDARGFLYItGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDpVWGEVGVAVCVARDGAPVde 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1493 EALKSTLKETLPDYMIPA---FWvtlNELPVTANGKVDRKALPEPDIEAG 1539
Cdd:PRK07470 474 AELLAWLDGKVARYKLPKrffFW---DALPKSGYGKITKKMVREELEERG 520
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
28-442 |
4.14e-31 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 131.12 E-value: 4.14e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 28 AGGNLLTYRELDEQANQLAHHL-RAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAK 106
Cdd:PLN02574 62 STGFSISYSELQPLVKSMAAGLyHVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 107 FAVVNERNMTAIGQYEGIIVSL-DDGKWRNESKER--------------PSSISGSRNLAYVIYTSGTTGKPKGVQIEHR 171
Cdd:PLN02574 142 LAFTSPENVEKLSPLGVPVIGVpENYDFDSKRIEFpkfyelikedfdfvPKPVIKQDDVAAIMYSSGTTGASKGVVLTHR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 172 NLTNYVSWFSE-EAGLTEN---DKTVLLSSYAFDLGYTSMFPV-LLGGGELHIVQKEtYTApDEIAHYIKEHGITYIKLT 246
Cdd:PLN02574 222 NLIAMVELFVRfEASQYEYpgsDNVYLAALPMFHIYGLSLFVVgLLSLGSTIVVMRR-FDA-SDMVKVIDRFKVTHFPVV 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 247 PSLFHTIVNTASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGrvdlYEPDAFAKRPT 326
Cdd:PLN02574 300 PPILMALTKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPHVDFIQGYGMTESTAVGTRG----FNTEKLSKYSS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 327 IGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFI 405
Cdd:PLN02574 376 VGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW------LRTGDIAYFDEDGYLYIV 449
|
410 420 430
....*....|....*....|....*....|....*..
gi 2214269206 406 GRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV 442
Cdd:PLN02574 450 DRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAV 486
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1052-1531 |
6.68e-31 |
|
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: 129.55 E-value: 6.68e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1052 KTVHQLFEETVQRHKDRPAVTY--NGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAF 1129
Cdd:cd05923 1 QTVFEMLRRAASRAPDACAIADpaRGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1130 VPIDPDY-PDQRIEYILQDSGAKLLLKQEGISVPDSYTGDVILL-----DGSRTILSL-PLDENDEGNPETAvtaenlAY 1202
Cdd:cd05923 81 ALINPRLkAAELAELIERGEMTAAVIAVDAQVMDAIFQSGVRVLalsdlVGLGEPESAgPLIEDPPREPEQP------AF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1203 MIYTSGTTGQPKGVMVEHHAlvnlcfwhhdafsmtAEDRS---AKYAG--FGFDASIWEMFPTW-TIG------------ 1264
Cdd:cd05923 155 VFYTSGTTGLPKGAVIPQRA---------------AESRVlfmSTQAGlrHGRHNVVLGLMPLYhVIGffavlvaalald 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1265 AELHVIDEAIRLDIVRLndyFETNGVTITFL-PTQL-----AEQFMELENTSLRVLLTGG--------DKLKRAvkKPYT 1330
Cdd:cd05923 220 GTYVVVEEFDPADALKL---IEQERVTSLFAtPTHLdalaaAAEFAGLKLSSLRHVTFAGatmpdavlERVNQH--LPGE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1331 LVNNYGPTEntvvATSAEIHPEEGSLSIGRAIANTRVY---ILGEGNQVQPEGVAGELCVAGRGLA--RGYLNREDETAK 1405
Cdd:cd05923 295 KVNIYGTTE----AMNSLYMRDARTGTEMRPGFFSEVRivrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAK 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1406 RFVadpfvpgERMYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAY 1484
Cdd:cd05923 371 KLQ-------DGWYRTGDVGYVdPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTAC 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 1485 VTPETADIEAlkSTLKE-----TLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05923 444 VVPREGTLSA--DELDQfcrasELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1076-1510 |
7.40e-31 |
|
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA synthetases; This family includes long-chain fatty acid (C12-C20) CoA synthetases and Bubblegum-like very long-chain (>C20) fatty acid CoA synthetases. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Drosophila melanogaster mutant bubblegum (BGM) have elevated levels of very-long-chain fatty acids (VLCFA) caused by a defective gene later named bubblegum. The human homolog (hsBG) of bubblegum has been characterized as a very long chain fatty acid CoA synthetase that functions specifically in the brain; hsBG may play a central role in brain VLCFA metabolism and myelinogenesis. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341233 [Multi-domain] Cd Length: 452 Bit Score: 128.48 E-value: 7.40e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1076 QSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDP-DYPDQrIEYILQDSGAKLLL 1154
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPtSSAEQ-IAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1155 kqegisVPDsytgdvilldgsrtilslpldendegnpetavtAENLAYMIYTSGTTGQPKGVMVEHHALVNLC-----FW 1229
Cdd:cd05907 83 ------VED---------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNAlalaeRL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1230 HHDA---------FSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDIVRLndyFET--NGVTITFLPTQ 1298
Cdd:cd05907 124 PATEgdrhlsflpLAHVFERRAGLYVPLLAGARIYFASSAETLLDDLSEVRPTVFLAVPRV---WEKvyAAIKVKAVPGL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1299 LAEQFMELENTSLRVLLTGGDKLKRAVKKPY-----TLVNNYGPTENTVVATSAeiHPEEGSL-SIGRAIANTRVYIlge 1372
Cdd:cd05907 201 KRKLFDLAVGGRLRFAASGGAPLPAELLHFFralgiPVYEGYGLTETSAVVTLN--PPGDNRIgTVGKPLPGVEVRI--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1373 gnqvqpeGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermYRTGDLVKWVNGGIEYI-GRI-DQQVKVRGYRIE 1450
Cdd:cd05907 276 -------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHItGRKkDLIITSGGKNIS 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1451 LSEIEVQLAQLSEVQDAAVTAVKDKggntAIAAYVTPetaDIEALKSTLKETLPDYMIPA 1510
Cdd:cd05907 343 PEPIENALKASPLISQAVVIGDGRP----FLVALIVP---DPEALEAWAEEHGIAYTDVA 395
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1054-1531 |
9.92e-31 |
|
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: 130.69 E-value: 9.92e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1054 VHQLFEETVQRHKDRPAVTYNGQ-----SWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAA 1128
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1129 FVPIDPDYPDQRIEYILQDSGAKLLLKQEGIS---------------VPDSYTGDVILL-------DGSRTILSLPLDEN 1186
Cdd:cd05968 143 VVPIFSGFGKEAAATRLQDAEAKALITADGFTrrgrevnlkeeadkaCAQCPTVEKVVVvrhlgndFTPAKGRDLSYDEE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1187 DEGNPETA--VTAENLAYMIYTSGTTGQPKGVMVEH-----HALVNLCFwhhdAFSMTAEDRSAKYAGFGFDASIWEMFP 1259
Cdd:cd05968 223 KETAGDGAerTESEDPLMIIYTSGTTGKPKGTVHVHagfplKAAQDMYF----QFDLKPGDLLTWFTDLGWMMGPWLIFG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1260 TWTIGAELHVIDEAIRLDIV-RLNDYFETNGVTITFLPTQLAEQFMELEN--------TSLRVLLTGGDK--------LK 1322
Cdd:cd05968 299 GLILGATMVLYDGAPDHPKAdRLWRMVEDHEITHLGLSPTLIRALKPRGDapvnahdlSSLRVLGSTGEPwnpepwnwLF 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1323 RAVKKPYTLVNNY-GPTE-------NTVVatsAEIHPeegsLSIGRAIANTRVYILGE-GNQVQPEgvAGELCVAGR--G 1391
Cdd:cd05968 379 ETVGKGRNPIINYsGGTEisggilgNVLI---KPIKP----SSFNGPVPGMKADVLDEsGKPARPE--VGELVLLAPwpG 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1392 LARGYLnrEDEtaKRFVADPFVPGERMYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVT 1470
Cdd:cd05968 450 MTRGFW--RDE--DRYLETYWSRFDNVWVHGDFAYYDEEGYFYIlGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAI 525
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214269206 1471 AVKDKGGNTAIAAYVT--PETADIEALKSTLKETLPDYM----IPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05968 526 GVPHPVKGEAIVCFVVlkPGVTPTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
607-915 |
2.08e-30 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are 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. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). 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, these include the DCL-type, LCL-type, 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 domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 126.40 E-value: 2.08e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 607 MYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFM-EANGEPVQRIIEKAEVDLH 685
Cdd:cd19544 1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILwEGLSEPVQVVWRQAELPVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 686 --VFEAKEDEADQkIKEFIRP----FDLNDAPLIRAALLRIEA-KKHLLLLDMHHIIADGVSRGIFVKELA--LLYKGEQ 756
Cdd:cd19544 81 elTLDPGDDALAQ-LRARFDPrryrLDLRQAPLLRAHVAEDPAnGRWLLLLLFHHLISDHTSLELLLEEIQaiLAGRAAA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 757 LPEPtLHYKDFaVWQneAEQKERMKEHEAYWMSVLsGELPELDLP---LDyarppVQsfkGDtirfrtGSETAKAVEKLL 833
Cdd:cd19544 160 LPPP-VPYRNF-VAQ--ARLGASQAEHEAFFREML-GDVDEPTAPfglLD-----VQ---GD------GSDITEARLALD 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 834 AETGTTLHMV-------LHAVFHV----FLSKISGQRDIVIGSVTAGRTNA--DVQDMPGMFVNTLALRMEAKE------ 894
Cdd:cd19544 221 AELAQRLRAQarrlgvsPASLFHLawalVLARCSGRDDVVFGTVLSGRMQGgaGADRALGMFINTLPLRVRLGGrsvrea 300
|
330 340
....*....|....*....|..
gi 2214269206 895 -QQTFAELLELakqtnlsaLEH 915
Cdd:cd19544 301 vRQTHARLAEL--------LRH 314
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
150-501 |
2.65e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 131.58 E-value: 2.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 150 LAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDktVLLSS----YAFDLGYTSMFPVLLGGGelhivqkeTY 225
Cdd:PRK08633 784 TATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDD--VILSSlpffHSFGLTVTLWLPLLEGIK--------VV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 226 TAPD-----EIAHYIKEHGITYIKLTPSLFHTIVNTASfAKDANFESLRLIVLGGEKiIPTDV-IAFRKMYGHtEFINHY 299
Cdd:PRK08633 854 YHPDptdalGIAKLVAKHRATILLGTPTFLRLYLRNKK-LHPLMFASLRLVVAGAEK-LKPEVaDAFEEKFGI-RILEGY 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 300 GPTE----ATIGAIAGRVDLYEPDAFAKRPTIGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLARGYLNRPQLTAE 374
Cdd:PRK08633 931 GATEtspvASVNLPDVLAADFKRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 375 RFVEnpySPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGyriEpkeietvMLSLSGIQEAvVLAVSEGGLQELCAYY 454
Cdd:PRK08633 1011 VIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGG---E-------MVPLGAVEEE-LAKALGGEEVVFAVTA 1076
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 455 TSD-------------QDIEKAELRYQLS-LTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK08633 1077 VPDekkgeklvvlhtcGAEDVEELKRAIKeSGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1078-1531 |
4.94e-30 |
|
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: 125.69 E-value: 4.94e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1078 WTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKQE 1157
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1158 GisvpdsytgdviLLDgsRTilslpldendegnpetavTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMT 1237
Cdd:cd05969 81 E------------LYE--RT------------------DPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1238 AEDRSAKYAGFGFDA-SIWEMFPTWTIGAELhVIDEAiRLDIVRLNDYFETNGVTITF-LPT----------QLAEQFME 1305
Cdd:cd05969 129 PDDIYWCTADPGWVTgTVYGIWAPWLNGVTN-VVYEG-RFDAESWYGIIERVKVTVWYtAPTairmlmkegdELARKYDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1306 lenTSLRVLLTGGDKLK--------RAVKKPytLVNNYGPTEN--TVVATSAEIHPEEGSLsiGRAIANTRVYILGE-GN 1374
Cdd:cd05969 207 ---SSLRFIHSVGEPLNpeairwgmEVFGVP--IHDTWWQTETgsIMIANYPCMPIKPGSM--GKPLPGVKAAVVDEnGN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1375 QVQPeGVAGELCVAGR--GLARGYLNREDETAKRFVADPFVPGERMYRTGDLVKWvnggieYIGRIDQQVKVRGYRIELS 1452
Cdd:cd05969 280 ELPP-GTKGILALKPGwpSMFRGIWNDEERYKNSFIDGWYLTGDLAYRDEDGYFW------FVGRADDIIKTSGHRVGPF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1453 EIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVT------PETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKV 1526
Cdd:cd05969 353 EVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISlkegfePSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKI 432
|
....*
gi 2214269206 1527 DRKAL 1531
Cdd:cd05969 433 MRRVL 437
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
11-498 |
5.45e-30 |
|
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: 128.38 E-value: 5.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 11 ALFEKQAQQTPDHSAVKAGGN-----LLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFL 85
Cdd:cd05968 65 QLLDKWLADTRTRPALRWEGEdgtsrTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 86 PIDPDTPEERIRYSLEDSGAKFAVV--------NERNMTAIG--------QYEGIIV----SLDDG------KWRNESKE 139
Cdd:cd05968 145 PIFSGFGKEAAATRLQDAEAKALITadgftrrgREVNLKEEAdkacaqcpTVEKVVVvrhlGNDFTpakgrdLSYDEEKE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 140 RP---SSISGSRNLAYVIYTSGTTGKPKGVQIEHrnlTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTsMFPVLLGGGE 216
Cdd:cd05968 225 TAgdgAERTESEDPLMIIYTSGTTGKPKGTVHVH---AGFPLKAAQDMYFQFDLKPGDLLTWFTDLGWM-MGPWLIFGGL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 217 L---HIVQKETYT---APDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAKDA-NFESLRLIVLGGEKIIPTDVIAFRKM 289
Cdd:cd05968 301 IlgaTMVLYDGAPdhpKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAhDLSSLRVLGSTGEPWNPEPWNWLFET 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 290 YG--HTEFINHYGPTEATiGAIAGRVdLYEPdafAKRPTIGRPIANAGALVLNEALKLVPPgASGQLYITGQ--GLARGY 365
Cdd:cd05968 381 VGkgRNPIINYSGGTEIS-GGILGNV-LIKP---IKPSSFNGPVPGMKADVLDESGKPARP-EVGELVLLAPwpGMTRGF 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 366 LNRPqltaERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSE- 444
Cdd:cd05968 455 WRDE----DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHp 530
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 445 -GGLQELCAYYTSDQDIEKAELRYQLSLTLPSHM----IPAFFVQVDAIPLTANGKTDR 498
Cdd:cd05968 531 vKGEAIVCFVVLKPGVTPTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMR 589
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1051-1533 |
6.34e-30 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 127.09 E-value: 6.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1051 DKTVHQLFEETVQRHKDRPAVT-YNGQS-----WTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLK 1124
Cdd:PRK13295 23 DRTINDDLDACVASCPDKTAVTaVRLGTgaprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSR 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1125 AGAAFVPIDPDYPDQRIEYILQDSGAKLLLkqegisVPDSYTG------------------DVILLDGS-----RTILSL 1181
Cdd:PRK13295 103 IGAVLNPLMPIFRERELSFMLKHAESKVLV------VPKTFRGfdhaamarrlrpelpalrHVVVVGGDgadsfEALLIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1182 PLDENDEGNPET----AVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAED------RSAKYAGFGFD 1251
Cdd:PRK13295 177 PAWEQEPDAPAIlarlRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDvilmasPMAHQTGFMYG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1252 AsiweMFPTwTIGAelhvidEAIRLDI---VRLNDYFETNGVTIT-----FLpTQLAEQFMELENT--SLRVLLTGGDKL 1321
Cdd:PRK13295 257 L----MMPV-MLGA------TAVLQDIwdpARAAELIRTEGVTFTmastpFL-TDLTRAVKESGRPvsSLRTFLCAGAPI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1322 KRAVKKP------YTLVNNYGPTENTVVATsaeIHP----EEGSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRG 1391
Cdd:PRK13295 325 PGALVERaraalgAKIVSAWGMTENGAVTL---TKLddpdERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCS 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1392 LARGYLNREDETAkrfvadpfVPGERMYRTGDLVKWVNGGieYI---GRiDQQVKVRG-YRIELSEIEVQLAQLSEVQDA 1467
Cdd:PRK13295 402 NFGGYLKRPQLNG--------TDADGWFDTGDLARIDADG--YIrisGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1468 AVTAVKDKGGNTAIAAYVTP---ETADIEALKSTLKET-LPDYMIPAFWVTLNELPVTANGKVDRKALPE 1533
Cdd:PRK13295 471 AIVAYPDERLGERACAFVVPrpgQSLDFEEMVEFLKAQkVAKQYIPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1052-1535 |
6.46e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 127.46 E-value: 6.46e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1052 KTVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVP 1131
Cdd:PRK06710 24 QPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1132 IDPDYPDQRIEYILQDSGAKLLL----------------KQEGISVpdSYTGDVI---------LLDGSRTILSLPLDEN 1186
Cdd:PRK06710 104 TNPLYTERELEYQLHDSGAKVILcldlvfprvtnvqsatKIEHVIV--TRIADFLpfpknllypFVQKKQSNLVVKVSES 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1187 D--------EGNPETAVTA-----ENLAYMIYTSGTTGQPKGVMVEHHALVN----------------------LCFWHh 1231
Cdd:PRK06710 182 EtihlwnsvEKEVNTGVEVpcdpeNDLALLQYTGGTTGFPKGVMLTHKNLVSntlmgvqwlynckegeevvlgvLPFFH- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1232 dAFSMTAEDRSAKYAGFGFdasiwEMFPTWtigaELHVIDEAIRLDIVRLNDYFETngVTITFLPTQLAEQFmelENTSL 1311
Cdd:PRK06710 261 -VYGMTAVMNLSIMQGYKM-----VLIPKF----DMKMVFEAIKKHKVTLFPGAPT--IYIALLNSPLLKEY---DISSI 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1312 RVLLTGGDKLKRAVKKPY------TLVNNYGPTENTVVATSAEIHPEEGSLSIGRAIANTRVYILG-EGNQVQPEGVAGE 1384
Cdd:PRK06710 326 RACISGSAPLPVEVQEKFetvtggKLVEGYGLTESSPVTHSNFLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1385 LCVAGRGLARGYLNREDETAKrfvadpfVPGERMYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSE 1463
Cdd:PRK06710 406 IVVKGPQIMKGYWNKPEETAA-------VLQDGWLHTGDVGYMDEDGFFYVkDRKKDMIVASGFNVYPREVEEVLYEHEK 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 1464 VQDAAVTAVKDKGGNTAIAAYVTPETADI---EALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPD 1535
Cdd:PRK06710 479 VQEVVTIGVPDPYRGETVKAFVVLKEGTEcseEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1079-1531 |
7.12e-30 |
|
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: 125.32 E-value: 7.12e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1079 TYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLlkqeg 1158
Cdd:cd05973 2 TFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLV----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1159 isvpdsytgdVILLDGSRTILSLPLdendegnpetavtaenlaYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTA 1238
Cdd:cd05973 77 ----------VTDAANRHKLDSDPF------------------VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1239 ED--------------------------RSAKYAGfGFDASIwemfpTWTIGAELHVIDEAIRLDIVRLndyFETNGVTI 1292
Cdd:cd05973 129 EDsfwnaadpgwayglyyaitgplalghPTILLEG-GFSVES-----TWRVIERLGVTNLAGSPTAYRL---LMAAGAEV 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1293 TFLPTqlaeqfmelenTSLRVLLTGGDKLKRAVKKPY------TLVNNYGPTENTVVATS--AEIHP-EEGSLsiGRAIA 1363
Cdd:cd05973 200 PARPK-----------GRLRRVSSAGEPLTPEVIRWFdaalgvPIHDHYGQTELGMVLANhhALEHPvHAGSA--GRAMP 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1364 NTRVYILGEGNQVQPEGVAGELCVAGRGLA----RGYLNREDETakrfvadpfvPGERMYRTGDLVKW-VNGGIEYIGRI 1438
Cdd:cd05973 267 GWRVAVLDDDGDELGPGEPGRLAIDIANSPlmwfRGYQLPDTPA----------IDGGYYLTGDTVEFdPDGSFSFIGRA 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1439 DQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYV--------TPETADieALKSTLKETLPDYMIPA 1510
Cdd:cd05973 337 DDVITMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVvlrgghegTPALAD--ELQLHVKKRLSAHAYPR 414
|
490 500
....*....|....*....|.
gi 2214269206 1511 FWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05973 415 TIHFVDELPKTPSGKIQRFLL 435
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1053-1526 |
1.04e-29 |
|
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: 127.31 E-value: 1.04e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1053 TVHQLFEETVQRHKDRPAVTYNG------QSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAG 1126
Cdd:cd17634 54 LAANALDRHLRENGDRTAIIYEGddtsqsRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1127 AAFVPIDPDYPDQRIEYILQDSGAKLLLKQEG-------------------ISVPDSY-------TGDVILLDGSRTIL- 1179
Cdd:cd17634 134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITADGgvragrsvplkknvddalnPNVTSVEhvivlkrTGSDIDWQEGRDLWw 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1180 -SLPLDENDEGNPEtAVTAENLAYMIYTSGTTGQPKGVMVEHHA-LVNLCFWHHDAFSMTAEDRSAKYAGFGfdasiWEM 1257
Cdd:cd17634 214 rDLIAKASPEHQPE-AMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVG-----WVT 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1258 FPTWTI------GAELHVIDEA-IRLDIVRLNDYFETNGVTITFL-PTQL----AEQFMELENT---SLRVLLTGGDKL- 1321
Cdd:cd17634 288 GHSYLLygplacGATTLLYEGVpNWPTPARMWQVVDKHGVNILYTaPTAIralmAAGDDAIEGTdrsSLRILGSVGEPIn 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1322 --------KRAVKKPYTLVNNYGPTENT-VVATSAEIHPEEGSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGR-- 1390
Cdd:cd17634 368 peayewywKKIGKEKCPVVDTWWQTETGgFMITPLPGAIELKAGSATRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwp 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1391 GLARGYLNREDetakRFVADPFVPGERMYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAV 1469
Cdd:cd17634 448 GQTRTLFGDHE----RFEQTYFSTFKGMYFSGDGARRDEDGYYWItGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAV 523
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 1470 TAVKDKGGNTAIAAYVT--------PETADieALKSTLKETLPDYMIPAFWVTLNELPVTANGKV 1526
Cdd:cd17634 524 VGIPHAIKGQAPYAYVVlnhgvepsPELYA--ELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1200-1531 |
1.05e-29 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 122.05 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1200 LAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRS------AKYAGFGFdasIWEmfptWTI-GAELHVIDE 1272
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWllslplYHVGGLAI---LVR----SLLaGAELVLLER 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1273 --AIRLDIVRlndyfetNGVTITFL-PTQLAeqfMELEN-------TSLRVLLTGG-----DKLKRAVKKPYTLVNNYGP 1337
Cdd:cd17630 75 nqALAEDLAP-------PGVTHVSLvPTQLQ---RLLDSgqgpaalKSLRAVLLGGapippELLERAADRGIPLYTTYGM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1338 TEnTVVATSAEIHPEEGSLSIGRAIANTRVYILgegnqvqpegVAGELCVAGRGLARGYLNREDEtakrfvadPFVPGER 1417
Cdd:cd17630 145 TE-TASQVATKRPDGFGRGGVGVLLPGRELRIV----------EDGEIWVGGASLAMGYLRGQLV--------PEFNEDG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1418 MYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKG-GNTAIAAYVTPETADIEAL 1495
Cdd:cd17630 206 WFTTKDLGELhADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEElGQRPVAVIVGRGPADPAEL 285
|
330 340 350
....*....|....*....|....*....|....*.
gi 2214269206 1496 KSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd17630 286 RAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1065-1526 |
3.88e-29 |
|
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: 123.95 E-value: 3.88e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1065 HKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYI 1144
Cdd:cd12118 17 YPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1145 LQDSGAKLLLkqegisVPDSYTGDVILLDGSRTILSL-PLDENDegnpetaVTAENlaymiYTSGTTGQPKGVMVEH--- 1220
Cdd:cd12118 97 LRHSEAKVLF------VDREFEYEDLLAEGDPDFEWIpPADEWD-------PIALN-----YTSGTTGRPKGVVYHHrga 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1221 --HALVNLCFW---HHDAFSMTAEDrsakyagfgFDASIWeMFPtWTIGAE------LHVIDEAIRLDIVRLNDYFETNG 1289
Cdd:cd12118 159 ylNALANILEWemkQHPVYLWTLPM---------FHCNGW-CFP-WTVAAVggtnvcLRKVDAKAIYDLIEKHKVTHFCG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1290 VTITFlpTQLAEQfMELENTSL--RV-LLTGGDK-----LKRAVKKPYTLVNNYGPTENTVVATSAEIHPEEGSLSIG-R 1360
Cdd:cd12118 228 APTVL--NMLANA-PPSDARPLphRVhVMTAGAPppaavLAKMEELGFDVTHVYGLTETYGPATVCAWKPEWDELPTEeR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1361 AIANTR---VYILGEGNQV-QPEGV---------AGELCVAGRGLARGYLNREDETAKRFvADPFvpgermYRTGDL-VK 1426
Cdd:cd12118 305 ARLKARqgvRYVGLEEVDVlDPETMkpvprdgktIGEIVFRGNIVMKGYLKNPEATAEAF-RGGW------FHSGDLaVI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1427 WVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKD-KGGNTAiAAYVT---PETADIEALKSTLKET 1502
Cdd:cd12118 378 HPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDeKWGEVP-CAFVElkeGAKVTEEEIIAFCREH 456
|
490 500
....*....|....*....|....
gi 2214269206 1503 LPDYMIPAFwVTLNELPVTANGKV 1526
Cdd:cd12118 457 LAGFMVPKT-VVFGELPKTSTGKI 479
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
8-442 |
4.50e-29 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 124.99 E-value: 4.50e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 8 TFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQ-GAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLP 86
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 87 IDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQY---------------------EGIIVS---------LDDGKWRNE 136
Cdd:PRK08751 106 VNPLYTPRELKHQLIDSGASVLVVIDNFGTTVQQViadtpvkqvittglgdmlgfpKAALVNfvvkyvkklVPEYRINGA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 137 SKERPSSISGSR-----------NLAYVIYTSGTTGKPKGVQIEHRNLTNYV----SWFSEEAGLTENDKTVLLS---SY 198
Cdd:PRK08751 186 IRFREALALGRKhsmptlqiepdDIAFLQYTGGTTGVAKGAMLTHRNLVANMqqahQWLAGTGKLEEGCEVVITAlplYH 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 199 AFDLGYTSMFPVLLGGGElHIVqketyTAPDEIAHYIKE---HGITYIKLTPSLFHTIVNTASFAKdANFESLRlIVLGG 275
Cdd:PRK08751 266 IFALTANGLVFMKIGGCN-HLI-----SNPRDMPGFVKElkkTRFTAFTGVNTLFNGLLNTPGFDQ-IDFSSLK-MTLGG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 276 EKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVDLYEPDAfakrpTIGRPIANAGALVLNEALKLVPPGASGQLY 355
Cdd:PRK08751 338 GMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNG-----SIGLPIPSTDACIKDDAGTVLAIGEIGELC 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 356 ITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQ 435
Cdd:PRK08751 413 IKGPQVMKGYWKRPEETAKVMDADGW------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVL 486
|
....*..
gi 2214269206 436 EAVVLAV 442
Cdd:PRK08751 487 EVAAVGV 493
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
14-501 |
5.89e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 124.38 E-value: 5.89e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 14 EKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPE 93
Cdd:PRK06710 31 EQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 94 ERIRYSLEDSGAKF---------AVVNERNMTAI------------------------GQYEGIIVSLDDGK----WRNE 136
Cdd:PRK06710 111 RELEYQLHDSGAKVilcldlvfpRVTNVQSATKIehvivtriadflpfpknllypfvqKKQSNLVVKVSESEtihlWNSV 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 137 SKERPSSIS----GSRNLAYVIYTSGTTGKPKGVQIEHRNLTNY----VSWFSEeagLTENDKTVLLSSYAFDL-GYTSM 207
Cdd:PRK06710 191 EKEVNTGVEvpcdPENDLALLQYTGGTTGFPKGVMLTHKNLVSNtlmgVQWLYN---CKEGEEVVLGVLPFFHVyGMTAV 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 208 FPV-LLGGGELHIVQKETYTApdeIAHYIKEHGITYIKLTPSLFHTIVNTAsFAKDANFESLRLIVlGGEKIIPTDVI-A 285
Cdd:PRK06710 268 MNLsIMQGYKMVLIPKFDMKM---VFEAIKKHKVTLFPGAPTIYIALLNSP-LLKEYDISSIRACI-SGSAPLPVEVQeK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 286 FRKMYGhTEFINHYGPTEATigAIAGRVDLYEpdafaKR--PTIGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLA 362
Cdd:PRK06710 343 FETVTG-GKLVEGYGLTESS--PVTHSNFLWE-----KRvpGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKGPQIM 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 363 RGYLNRPQLTAERFVENpyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV 442
Cdd:PRK06710 415 KGYWNKPEETAAVLQDG-------WLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGV 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 443 SEGGLQELCAYYT---SDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK06710 488 PDPYRGETVKAFVvlkEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
17-500 |
8.10e-29 |
|
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: 123.89 E-value: 8.10e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 17 AQQTPDHSAV------KAGGNLLTYRELDEQANQLAHHLRAQGA-GneDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDP 89
Cdd:cd05931 3 AAARPDRPAYtflddeGGREETLTYAELDRRARAIAARLQAVGKpG--DRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 90 DTPE---ERIRYSLEDSGAKFAVVNERNMTAIGQYEGIIVSLDDGKWR-----NESKERPSSIS--GSRNLAYVIYTSGT 159
Cdd:cd05931 81 PTPGrhaERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLvvdllPDTSAADWPPPspDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 160 TGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLG--YTSMFPVLLGGgelHIVqketYTAPdeiAHYIKE 237
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGliGGLLTPLYSGG---PSV----LMSP---AAFLRR 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 238 hgityikltPSLF------HTIVNTA--SFA--------KDANFE-----SLRLIVLGGEKIIPTDVIAFRKM---YG-- 291
Cdd:cd05931 231 ---------PLRWlrlisrYRATISAapNFAydlcvrrvRDEDLEgldlsSWRVALNGAEPVRPATLRRFAEAfapFGfr 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 292 HTEFINHYGPTEATI---GAIAG---RVDLYEPDAFAKRPTI--------------GRPIANAGALVLNEA-LKLVPPGA 350
Cdd:cd05931 302 PEAFRPSYGLAEATLfvsGGPPGtgpVVLRVDRDALAGRAVAvaaddpaarelvscGRPLPDQEVRIVDPEtGRELPDGE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 351 SGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDvVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIE-TVML 429
Cdd:cd05931 382 VGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGD-LGFLHDGELYITGRLKDLIIVRGRNHYPQDIEaTAEE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 430 SLSGIQE--AVVLAVSEGGLQEL---CAYYTSDQDIEKAELRYQLSLTLPS-HMIPA---FFVQVDAIPLTANGKTDRNA 500
Cdd:cd05931 461 AHPALRPgcVAAFSVPDDGEERLvvvAEVERGADPADLAAIAAAIRAAVAReHGVAPadvVLVRPGSIPRTSSGKIQRRA 540
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1052-1534 |
9.68e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 123.78 E-value: 9.68e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1052 KTVHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMD-CGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFV 1130
Cdd:PRK12492 24 KSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1131 PIDPDYPDQRIEYILQDSGAKLL--------LKQEgiSVPDS--------YTGDVI----------LLDGSRTIL---SL 1181
Cdd:PRK12492 104 NTNPLYTAREMRHQFKDSGARALvylnmfgkLVQE--VLPDTgieylieaKMGDLLpaakgwlvntVVDKVKKMVpayHL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1182 PL---------DENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALV-NL-----CFWHH--DAFSMTAEDRSAK 1244
Cdd:PRK12492 182 PQavpfkqalrQGRGLSLKPVPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVaNMlqvraCLSQLgpDGQPLMKEGQEVM 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1245 ------YAGFGFDASIWEMFPTwtiGAELHVIDEA--IRLDIVRLNDYFETN--GVTITFLPTQLAEQFMELENTSLRVL 1314
Cdd:PRK12492 262 iaplplYHIYAFTANCMCMMVS---GNHNVLITNPrdIPGFIKELGKWRFSAllGLNTLFVALMDHPGFKDLDFSALKLT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1315 LTGGDKLKRAVKKPY------TLVNNYGPTENTVVAtSAEIHPEEGSL-SIGRAIANTRVYILGEGNQVQPEGVAGELCV 1387
Cdd:PRK12492 339 NSGGTALVKATAERWeqltgcTIVEGYGLTETSPVA-STNPYGELARLgTVGIPVPGTALKVIDDDGNELPLGERGELCI 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1388 AGRGLARGYLNREDETAKRFVAdpfvpgERMYRTGDL-VKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQD 1466
Cdd:PRK12492 418 KGPQVMKGYWQQPEATAEALDA------EGWFKTGDIaVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVAN 491
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1467 AAVTAVKDKGGNTAIAAYVTPE--TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEP 1534
Cdd:PRK12492 492 CAAIGVPDERSGEAVKLFVVARdpGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
5-481 |
2.32e-28 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 123.06 E-value: 2.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 5 TEATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAF 84
Cdd:PRK08279 35 SKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 85 LPIDPDTPEERIRYSLEDSGAKFAVVNE---------RNMTAIGQ---YEGIIVSLDDGKWRN---ESKERPSSISGSRN 149
Cdd:PRK08279 115 ALLNTQQRGAVLAHSLNLVDAKHLIVGEelveafeeaRADLARPPrlwVAGGDTLDDPEGYEDlaaAAAGAPTTNPASRS 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 150 ------LAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDK-------------TVLLSSyafdlgytsmfpV 210
Cdd:PRK08279 195 gvtakdTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVlycclplyhntggTVAWSS------------V 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 211 LLGGGELHIVQKetYTAP---DEIAHYikehGIT---YIKltpSLFHTIVNTASFAKDANfESLRLIV---LGGEkI--- 278
Cdd:PRK08279 263 LAAGATLALRRK--FSASrfwDDVRRY----RATafqYIG---ELCRYLLNQPPKPTDRD-HRLRLMIgngLRPD-Iwde 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 279 ------IPtDVIAFrkmYGHTE----FINHYGpteaTIGAIaGRVDLYE--PDAFAK-RPTIGRPIANAGALvlneaLKL 345
Cdd:PRK08279 332 fqqrfgIP-RILEF---YAASEgnvgFINVFN----FDGTV-GRVPLWLahPYAIVKyDVDTGEPVRDADGR-----CIK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 346 VPPGASGQLY--ITGQGLARGYlNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKE 423
Cdd:PRK08279 398 VKPGEVGLLIgrITDRGPFDGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTE 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2214269206 424 IETVMLSLSGIQEAVVLAVS----EG--GLQELCAyyTSDQDIEKAELRYQLSLTLPSHMIPAF 481
Cdd:PRK08279 477 VENALSGFPGVEEAVVYGVEvpgtDGraGMAAIVL--ADGAEFDLAALAAHLYERLPAYAVPLF 538
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
9-501 |
3.15e-28 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 121.52 E-value: 3.15e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 9 FAALFEkqAQQTPDHSAVKA-GGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPI 87
Cdd:PRK07514 6 FDALRA--AFADRDAPFIETpDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 88 DPD-TPEErIRYSLEDSGAKFAVVNERN---MTAIGQYEGI--IVSLDD---GKWRNESKERPSSIS----GSRNLAYVI 154
Cdd:PRK07514 84 NTAyTLAE-LDYFIGDAEPALVVCDPANfawLSKIAAAAGAphVETLDAdgtGSLLEAAAAAPDDFEtvprGADDLAAIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 155 YTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDktVLLssYAFDLGYT-----SMFPVLLGGGELHIVQKetyTAPD 229
Cdd:PRK07514 163 YTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDD--VLI--HALPIFHThglfvATNVALLAGASMIFLPK---FDPD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 230 EIAHYIKEhgITYIKLTPSLFHTIVNTASFAKDANfESLRLIVLGGEKIIPTDVIAFRKMYGHTeFINHYGPTEATI--- 306
Cdd:PRK07514 236 AVLALMPR--ATVMMGVPTFYTRLLQEPRLTREAA-AHMRLFISGSAPLLAETHREFQERTGHA-ILERYGMTETNMnts 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 307 ----GA-IAGrvdlyepdafakrpTIGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENP 380
Cdd:PRK07514 312 npydGErRAG--------------TVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 381 YspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV-----SEGGLQELCAyyT 455
Cdd:PRK07514 378 F------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVphpdfGEGVTAVVVP--K 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2214269206 456 SDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK07514 450 PGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
8-504 |
3.23e-28 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 121.79 E-value: 3.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 8 TFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIvMDRSAEVMV-SILGVMKAGAAFLP 86
Cdd:PRK13382 44 GPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGI-MCRNHRGFVeALLAANRIGADILL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 87 IDPDTPEERIRYSLEDSGAKFAVVNERNMTAIGQ------YEGIIVSLDDGKWRN------ESKERPSSISGSRNLAYVI 154
Cdd:PRK13382 123 LNTSFAGPALAEVVTREGVDTVIYDEEFSATVDRaladcpQATRIVAWTDEDHDLtvevliAAHAGQRPEPTGRKGRVIL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 155 YTSGTTGKPKGVQ-------IEHRNLTNYVSWFSEEagltendkTVLLSSYAFdlgYTSMFPVLLGGGELH--IVQKETY 225
Cdd:PRK13382 203 LTSGTTGTPKGARrsgpggiGTLKAILDRTPWRAEE--------PTVIVAPMF---HAWGFSQLVLAASLActIVTRRRF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 226 TaPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAKD-ANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFiNHYGPTEA 304
Cdd:PRK13382 272 D-PEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNrYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIY-NNYNATEA 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 305 TIGAIAGRVDLYE-PDafakrpTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRpqlTAERFVENpysp 383
Cdd:PRK13382 350 GMIATATPADLRAaPD------TAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDFHDG---- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 384 gslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV--SEGGlQELCAYYTSDQDIE 461
Cdd:PRK13382 417 ---FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVddEQYG-QRLAAFVVLKPGAS 492
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 2214269206 462 KA--ELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALPKP 504
Cdd:PRK13382 493 ATpeTLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
6-612 |
3.57e-28 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 123.22 E-value: 3.57e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 6 EATFAALFEKQAQQTPDhsavkaggnLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAG-AAF 84
Cdd:PRK06060 13 QASEAGWYDRPAFYAAD---------VVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGvMAF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 85 LPiDPDTPEERIRYSLEDSGAKFAVVNErNMTAIGQYEGIIVSLDdgKWRNESKERPS--SISGSRNLAYVIYTSGTTGK 162
Cdd:PRK06060 84 LA-NPELHRDDHALAARNTEPALVVTSD-ALRDRFQPSRVAEAAE--LMSEAARVAPGgyEPMGGDALAYATYTSGTTGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 163 PKGVQIEHRNLTNYVSWFSEEA-GLTENDktVLLSS----YAFDLGYTSMFPVLLGGGElhIVQKETYTApdEIAHYIK- 236
Cdd:PRK06060 160 PKAAIHRHADPLTFVDAMCRKAlRLTPED--TGLCSarmyFAYGLGNSVWFPLATGGSA--VINSAPVTP--EAAAILSa 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 237 --EHGITYikLTPSLFHTIVNTASfakDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRVD 314
Cdd:PRK06060 234 rfGPSVLY--GVPNFFARVIDSCS---PDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFVSNRVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 315 LYEPDAFAK--RPTIGRPIANAGALVlnealklvPPGASGQLYITGQGLARGYLNRPQ--LTAERFVEnpyspgslmykT 390
Cdd:PRK06060 309 EWRLGTLGRvlPPYEIRVVAPDGTTA--------GPGVEGDLWVRGPAIAKGYWNRPDspVANEGWLD-----------T 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 391 GDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEG-GLQELCAYY--TSDQDIEKAELRY 467
Cdd:PRK06060 370 RDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVREStGASTLQAFLvaTSGATIDGSVMRD 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 468 ---QLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL----------------------------PKPNA-AQSGGKA-- 513
Cdd:PRK06060 450 lhrGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGALrkqsptkpiwelsltepgsgvraqrddlSASNMtIAGGNDGga 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 514 -----LAAPETALE----ESLCRIWQKTLG---IEAIGIDDNFFDLGGHSLKGMMLIANIQAELEKSVPLKALFEQPTVR 581
Cdd:PRK06060 530 tlrerLVALRQERQrlvvDAVCAEAAKMLGepdPWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSIS 609
|
650 660 670
....*....|....*....|....*....|.
gi 2214269206 582 QLAAYMEASavsgghqvLKPADKQDMYPLSS 612
Cdd:PRK06060 610 GLAQYLEAE--------LAGGHGRLKSAGPV 632
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1078-1535 |
4.83e-28 |
|
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: 121.45 E-value: 4.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1078 WTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVP------------------------ID 1133
Cdd:cd05970 48 FTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPathqltakdivyriesadikmivaIA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1134 PDYPDQRIEYILQDSGAKLLLKQEGISVPDSYTGDVILLDGSRTILSLPLDENDEGNpetavtaENLAYMIYTSGTTGQP 1213
Cdd:cd05970 128 EDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNASPDFERPTANSYPCG-------EDILLVYFSSGTTGMP 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1214 KgvMVEH-------HaLVNLCFWHhdafSMTAEDRSAKYAGFGFDASIW-EMFPTWTIGAELHVIDEAiRLDIVRLNDYF 1285
Cdd:cd05970 201 K--MVEHdftyplgH-IVTAKYWQ----NVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFVYDYD-KFDPKALLEKL 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1286 ETNGVTiTFL--PT----QLAEQFMELENTSLRVLLTGGDKLKRAV------KKPYTLVNNYGPTENTV-VATSAEIHPE 1352
Cdd:cd05970 273 SKYGVT-TFCapPTiyrfLIREDLSRYDLSSLRYCTTAGEALNPEVfntfkeKTGIKLMEGFGQTETTLtIATFPWMEPK 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1353 EGSlsIGRAIANTRVYILGEGNQVQPEGVAGELCV---AGR--GLARGYLNREDETAKRFvadpfvpGERMYRTGDlVKW 1427
Cdd:cd05970 352 PGS--MGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKpvGLFGGYYKDAEKTAEVW-------HDGYYHTGD-AAW 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1428 VN--GGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYV------TPETADIEALKSTL 1499
Cdd:cd05970 422 MDedGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIvlakgyEPSEELKKELQDHV 501
|
490 500 510
....*....|....*....|....*....|....*.
gi 2214269206 1500 KETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPD 1535
Cdd:cd05970 502 KKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRERD 537
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1057-1533 |
6.26e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 121.00 E-value: 6.26e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1057 LFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDY 1136
Cdd:PRK06164 15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1137 PDQRIEYILQDSGAKLLLKQEGI----------SVPDSYTGD---VILLDGS------------RTILSLPLDENDEGNP 1191
Cdd:PRK06164 95 RSHEVAHILGRGRARWLVVWPGFkgidfaailaAVPPDALPPlraIAVVDDAadatpapapgarVQLFALPDPAPPAAAG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1192 ETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVnlcfwHH-----DAFSMTAEDR---SAKYAG-FGFDAsiweMFPTWT 1262
Cdd:PRK06164 175 ERAADPDAGALLFTTSGTTSGPKLVLHRQATLL-----RHaraiaRAYGYDPGAVllaALPFCGvFGFST----LLGALA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1263 IGAELH---VIDEAIRLDIVRlndyfeTNGVTITFLPTQLAEQFMELEN-----TSLRVLLTG------GDKLKRAVKKP 1328
Cdd:PRK06164 246 GGAPLVcepVFDAARTARALR------RHRVTHTFGNDEMLRRILDTAGeradfPSARLFGFAsfapalGELAALARARG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1329 YTLVNNYGPTEntVVATsaeihpeegsLSIGRAIANTRVYILGEGNQVQPE----------------GVAGELCVAGRGL 1392
Cdd:PRK06164 320 VPLTGLYGSSE--VQAL----------VALQPATDPVSVRIEGGGRPASPEarvrardpqdgallpdGESGEIEIRAPSL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1393 ARGYLNREDETAKRFVADPFvpgermYRTGDLVKWV-NGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTA 1471
Cdd:PRK06164 388 MRGYLDNPDATARALTDDGY------FRTGDLGYTRgDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVG 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 1472 VkDKGGNTAIAAYVTPE---TADIEALKSTLKETLPDYMIPA-FWVtLNELPVT--ANG-KVDRKALPE 1533
Cdd:PRK06164 462 A-TRDGKTVPVAFVIPTdgaSPDEAGLMAACREALAGFKVPArVQV-VEAFPVTesANGaKIQKHRLRE 528
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1034-1533 |
8.48e-28 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 123.50 E-value: 8.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1034 KQALLE----AWKGKalpVPTDKTVHQLFEETVQRHKDRPAVT-YNGQSWTYGELNAKANRLARILMDCgISPDDRVGVL 1108
Cdd:PRK08633 596 KQAVFElsfdSWKSR---KEALPPLAEAWIDTAKRNWSRLAVAdSTGGELSYGKALTGALALARLLKRE-LKDEENVGIL 671
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1109 TKPSLEMSAAVLGVLKAGAafVPIDpdypdqrIEYILQDSGAKLLLKQEGISVpdSYTGDVIL--LDGSRTILSLPLDEN 1186
Cdd:PRK08633 672 LPPSVAGALANLALLLAGK--VPVN-------LNYTASEAALKSAIEQAQIKT--VITSRKFLekLKNKGFDLELPENVK 740
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1187 -----D-------------------------EGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHH-------ALVNLcfw 1229
Cdd:PRK08633 741 viyleDlkakiskvdkltallaarllparllKRLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHnilsnieQISDV--- 817
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1230 hhdaFSMTAEDRSAK----YAGFGFDASIWemFPTWT-IGAELHvideAIRLDIVRLNDYFETNGVTI-----TFLPTQL 1299
Cdd:PRK08633 818 ----FNLRNDDVILSslpfFHSFGLTVTLW--LPLLEgIKVVYH----PDPTDALGIAKLVAKHRATIllgtpTFLRLYL 887
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1300 ------AEQFmelenTSLRVLLTGGDKLKRAVKKPY------TLVNNYGPTENTVVAT-------SAEIHPEEGSL--SI 1358
Cdd:PRK08633 888 rnkklhPLMF-----ASLRLVVAGAEKLKPEVADAFeekfgiRILEGYGATETSPVASvnlpdvlAADFKRQTGSKegSV 962
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1359 GRAIANTRVYILG-EGNQVQPEGVAGELCVAGRGLARGYLNREDETAKrFVADpfVPGERMYRTGDLVKWVNGGIEYI-G 1436
Cdd:PRK08633 963 GMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE-VIKD--IDGIGWYVTGDKGHLDEDGFLTItD 1039
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1437 RIDQQVKVRGYRIELSEIEVQLAQL--SEVQDAAVTAVKDKGGNTAIAAYVTPETADIEALKSTLKET-LPDYMIPAFWV 1513
Cdd:PRK08633 1040 RYSRFAKIGGEMVPLGAVEEELAKAlgGEEVVFAVTAVPDEKKGEKLVVLHTCGAEDVEELKRAIKESgLPNLWKPSRYF 1119
|
570 580
....*....|....*....|
gi 2214269206 1514 TLNELPVTANGKVDRKALPE 1533
Cdd:PRK08633 1120 KVEALPLLGSGKLDLKGLKE 1139
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
8-503 |
9.56e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 120.42 E-value: 9.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 8 TFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAiVMDRSAEVMV-SILGVMKAGAAFLP 86
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVA-VLARNHRGFVlALYAAGKVGARIIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 87 IDPDTPEERIRYSLEDSGAKFAVVNERNMTA-------IGQYEGIIVSLDDGKWR------------NESKERPSSISgs 147
Cdd:PRK07788 129 LNTGFSGPQLAEVAAREGVKALVYDDEFTDLlsalppdLGRLRAWGGNPDDDEPSgstdetlddliaGSSTAPLPKPP-- 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 148 RNLAYVIYTSGTTGKPKGVQIEHrnltnyVSWFSEEAGLTEN-----DKTVLLSSYAF-DLGYtSMFPVLLGGGElHIVQ 221
Cdd:PRK07788 207 KPGGIVILTSGTTGTPKGAPRPE------PSPLAPLAGLLSRvpfraGETTLLPAPMFhATGW-AHLTLAMALGS-TVVL 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 222 KETYTaPDEIAHYIKEHGITYIKLTPSLFHTIVNTASfAKDANFE--SLRLIVLGGEKIIPTDVIAFRKMYGhtEFI-NH 298
Cdd:PRK07788 279 RRRFD-PEATLEDIAKHKATALVVVPVMLSRILDLGP-EVLAKYDtsSLKIIFVSGSALSPELATRALEAFG--PVLyNL 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 299 YGPTEATIGAIAGRVDLYEPDAFAKRPTIGRPIAnagalVLNEALKLVPPGASGQLYITGQGLARGYlnrpqlTAERfve 378
Cdd:PRK07788 355 YGSTEVAFATIATPEDLAEAPGTVGRPPKGVTVK-----ILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR--- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 379 NPYSPGSLMyKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVS--EGGlQELCAYY-- 454
Cdd:PRK07788 421 DKQIIDGLL-SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDdeEFG-QRLRAFVvk 498
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2214269206 455 TSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALPK 503
Cdd:PRK07788 499 APGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1074-1531 |
1.20e-27 |
|
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: 119.36 E-value: 1.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1074 NGQSWTYGELNAKANRLARILMDcGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLL 1153
Cdd:cd05909 4 LGTSLTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1154 LK----QEGISVPD----SYTGDVILLDGSRTILSL------------PLDENDEGNPETAVTAENLAYMIYTSGTTGQP 1213
Cdd:cd05909 83 LTskqfIEKLKLHHlfdvEYDARIVYLEDLRAKISKadkckaflagkfPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1214 KGVMVEHHALV-NL--CFwhhDAFSMTAEDRSAK----YAGFGFDASIWemFPtwtIGAELHVIDEAIRLDIVRLNDYFE 1286
Cdd:cd05909 163 KGVVLSHKNLLaNVeqIT---AIFDPNPEDVVFGalpfFHSFGLTGCLW--LP---LLSGIKVVFHPNPLDYKKIPELIY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1287 TNGVTI-----TFL--------PTQLAeqfmelentSLRVLLTGGDKLKRAVKKPY------TLVNNYGPTENTVVAT-- 1345
Cdd:cd05909 235 DKKATIllgtpTFLrgyaraahPEDFS---------SLRLVVAGAEKLKDTLRQEFqekfgiRILEGYGTTECSPVISvn 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1346 SAEIHPEEGslSIGRAIANTRVYILG-EGNQVQPEGVAGELCVAGRGLARGYLNREDETAkrfvadpFVPGERMYRTGDL 1424
Cdd:cd05909 306 TPQSPNKEG--TVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDI 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1425 VKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQ-DAAVTAVKDKGGNTAIAAYVTPETADIEALKSTLKET 1502
Cdd:cd05909 377 GKIDGEGFLTItGRLSRFAKIAGEMVSLEAIEDILSEILPEDnEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLNDILKNA 456
|
490 500 510
....*....|....*....|....*....|
gi 2214269206 1503 -LPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05909 457 gISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
5-498 |
2.08e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 119.72 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 5 TEATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAF 84
Cdd:PRK05605 30 GDTTLVDLYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 85 LPIDPDTPEERIRYSLEDSGAKFAVVNER--------------------NMTA------------------------IGQ 120
Cdd:PRK05605 110 VEHNPLYTAHELEHPFEDHGARVAIVWDKvaptverlrrttpletivsvNMIAampllqrlalrlpipalrkaraalTGP 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 121 YEGII-----VS---LDDGKWRNESKERPSSIsgsrnlAYVIYTSGTTGKPKGVQIEHRNL-TNYV---SWFSeeaGLTE 188
Cdd:PRK05605 190 APGTVpwetlVDaaiGGDGSDVSHPRPTPDDV------ALILYTSGTTGKPKGAQLTHRNLfANAAqgkAWVP---GLGD 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 189 NDKTVLLS---SYAFDLGYTSMFPVLLgGGELHIVQKetyTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASfAKDANF 265
Cdd:PRK05605 261 GPERVLAAlpmFHAYGLTLCLTLAVSI-GGELVLLPA---PDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAE-ERGVDL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 266 ESLRlIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEaTIGAIAGrvdlyEPDAFAKRP-TIGRPIANAGALVLN-EAL 343
Cdd:PRK05605 336 SGVR-NAFSGAMALPVSTVELWEKLTGGLLVEGYGLTE-TSPIIVG-----NPMSDDRRPgYVGVPFPDTEVRIVDpEDP 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 344 -KLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPK 422
Cdd:PRK05605 409 dETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPA 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 423 EIETVMLSLSGIQEAVVLAV-SEGGLQELCAYYT--SDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDR 498
Cdd:PRK05605 482 EVEEVLREHPGVEDAAVVGLpREDGSEEVVAAVVlePGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
12-501 |
2.59e-27 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 119.39 E-value: 2.59e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 12 LFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQ-GAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDP- 89
Cdd:PRK08974 28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPl 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 90 DTPEErIRYSLEDSGAK-------FA-----VVNERN-----MTAIGQY----EGIIV---------------------- 126
Cdd:PRK08974 108 YTPRE-LEHQLNDSGAKaivivsnFAhtlekVVFKTPvkhviLTRMGDQlstaKGTLVnfvvkyikrlvpkyhlpdaisf 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 127 --SLDDGKWRNESKerpSSISGSrNLAYVIYTSGTTGKPKGVQIEHRN-LTNY--VSWFSEEAGLTENDKTVL-LSSY-A 199
Cdd:PRK08974 187 rsALHKGRRMQYVK---PELVPE-DLAFLQYTGGTTGVAKGAMLTHRNmLANLeqAKAAYGPLLHPGKELVVTaLPLYhI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 200 FDLGYTSMFPVLLGGGELHIvqketyTAPDEIAHYIKE---HGITYIKLTPSLFHTIVNTASFaKDANFESLRLIVLGGE 276
Cdd:PRK08974 263 FALTVNCLLFIELGGQNLLI------TNPRDIPGFVKElkkYPFTAITGVNTLFNALLNNEEF-QELDFSSLKLSVGGGM 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 277 KIIPTDVIAFRKMYGhTEFINHYGPTEATIGAIAGRVDLYEPDAfakrpTIGRPIANAGALVLNEALKLVPPGASGQLYI 356
Cdd:PRK08974 336 AVQQAVAERWVKLTG-QYLLEGYGLTECSPLVSVNPYDLDYYSG-----SIGLPVPSTEIKLVDDDGNEVPPGEPGELWV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 357 TGQGLARGYLNRPQLTAERFVEnpyspGSLmyKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQE 436
Cdd:PRK08974 410 KGPQVMLGYWQRPEATDEVIKD-----GWL--ATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLE 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214269206 437 AVVLAVSEGGLQELCAYYT--SDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK08974 483 VAAVGVPSEVSGEAVKIFVvkKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
149-498 |
2.80e-27 |
|
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: 114.81 E-value: 2.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 149 NLAYVIYTSGTTGKPKGVqiehrnLTNYVSWFseeAGLTENDKTVLLS-----------SYAFDLgYTSMFpVLLGGGEL 217
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAY------YRSERSWI---ESFVCNEDLFNISgedailapgplSHSLFL-YGAIS-ALYLGGTF 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 218 HIVQKetyTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTasfakDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFIN 297
Cdd:cd17633 70 IGQRK---FNPKSWIRKINQYNATVIYLVPTMLQALART-----LEPESKIKSIFSSGQKLFESTKKKLKNIFPKANLIE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 298 HYGPTEATIgaIAGRVdlyePDAFAKRPTIGRPIANAGALVLNEAlklvpPGASGQLYITGQGLARGYLnrpqltaerfV 377
Cdd:cd17633 142 FYGTSELSF--ITYNF----NQESRPPNSVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYV----------R 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 378 ENPYSPGSLMyKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVS-EGGLQELCAYYTS 456
Cdd:cd17633 201 GGFSNPDGWM-SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPdARFGEIAVALYSG 279
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 2214269206 457 DQDIEKAELRYqLSLTLPSHMIPAFFVQVDAIPLTANGKTDR 498
Cdd:cd17633 280 DKLTYKQLKRF-LKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1053-1549 |
5.97e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 117.82 E-value: 5.97e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1053 TVHQLFEEtvQRHKDRPAVTYNGQSWTYGELNAKANRLARILMdcGISPDDR---VGVLTKPSLEMSAAVLGVLKAGAAF 1129
Cdd:PRK13388 4 TIAQLLRD--RAGDDTIAVRYGDRTWTWREVLAEAAARAAALI--ALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1130 VPIDP---------DYPDQRIEYILQDSGAKLLLkqEGISVPdsytGDVILLDGSRTILSLpLDENDEGNPETAVTAENL 1200
Cdd:PRK13388 80 VGLNTtrrgaalaaDIRRADCQLLVTDAEHRPLL--DGLDLP----GVRVLDVDTPAYAEL-VAAAGALTPHREVDAMDP 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1201 AYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAED----------RSAKYAGFGfdasiwemfPTWTIGAELHVI 1270
Cdd:PRK13388 153 FMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDvcyvsmplfhSNAVMAGWA---------PAVASGAAVALP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1271 DE--AIR-LDIVRL--NDYFETNGVTITFLptqLA--EQFMELENTsLRVLL--TGGDKLKRAVKKPY--TLVNNYGPTE 1339
Cdd:PRK13388 224 AKfsASGfLDDVRRygATYFNYVGKPLAYI---LAtpERPDDADNP-LRVAFgnEASPRDIAEFSRRFgcQVEDGYGSSE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1340 NTVVATSAEIHPEEgslSIGRAIANTRVY-----------ILGE-GNQVQPEGVAGELC-VAGRGLARGYLNREDETAKR 1406
Cdd:PRK13388 300 GAVIVVREPGTPPG---SIGRGAPGVAIYnpetltecavaRFDAhGALLNADEAIGELVnTAGAGFFEGYYNNPEATAER 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1407 FvadpfvpgeR--MYRTGDLV-KWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKD-KGGNTAIA 1482
Cdd:PRK13388 377 M---------RhgMYWSGDLAyRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDeRVGDQVMA 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1483 AYVT--PETADIEALKSTL--KETLPDYMIPAF-WVTlNELPVTANGKVDRKAL-------PEPD---IEAGSGEYKAPT 1547
Cdd:PRK13388 448 ALVLrdGATFDPDAFAAFLaaQPDLGTKAWPRYvRIA-ADLPSTATNKVLKRELiaqgwatGDPVtlwVRRGGPAYRLMS 526
|
..
gi 2214269206 1548 TD 1549
Cdd:PRK13388 527 EP 528
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1062-1548 |
7.86e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 117.57 E-value: 7.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1062 VQRHK----DRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYP 1137
Cdd:PRK07786 23 LARHAlmqpDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1138 DQRIEYILQDSGAKLLLkQEGISVP-------DSYTGDVILLDGSRT---ILSLP--LDENDEGNPETAVTAENLAYMIY 1205
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVV-TEAALAPvatavrdIVPLLSTVVVAGGSSddsVLGYEdlLAEAGPAHAPVDIPNDSPALIMY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1206 TSGTTGQPKGVMVEH-----HALVNLCFWHHDafsmTAEDRSAKYAGFGFDASIWEMFPTWTIGAELhVIDEAIRLDIVR 1280
Cdd:PRK07786 182 TSGTTGRPKGAVLTHanltgQAMTCLRTNGAD----INSDVGFVGVPLFHIAGIGSMLPGLLLGAPT-VIYPLGAFDPGQ 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1281 LNDYFETNGVTITFL-PTQ----LAEQFMELENTSLRVLLTGG----DKLKRAVKKPY---TLVNNYGPTENTVVATSAE 1348
Cdd:PRK07786 257 LLDVLEAEKVTGIFLvPAQwqavCAEQQARPRDLALRVLSWGAapasDTLLRQMAATFpeaQILAAFGQTEMSPVTCMLL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1349 IHPEEGSL-SIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermyRTGDLVKW 1427
Cdd:PRK07786 337 GEDAIRKLgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF-------HSGDLVRQ 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1428 VNGGIEY-IGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKD-KGGNTAIA-AYVTPETAD--IEALKSTLKET 1502
Cdd:PRK07786 410 DEEGYVWvVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADeKWGEVPVAvAAVRNDDAAltLEDLAEFLTDR 489
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1503 LPDYMIPAFWVTLNELPVTANGKVD----RKALPEPDIeAGSGEYKAPTT 1548
Cdd:PRK07786 490 LARYKHPKALEIVDALPRNPAGKVLktelRERYGACVN-VERRSASAGFT 538
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1203-1528 |
9.80e-27 |
|
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: 113.91 E-value: 9.80e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1203 MIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDR----SAKYAGFGFDASIWEMF----------PTWTIGAELH 1268
Cdd:cd05917 7 IQFTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRlcipVPLFHCFGSVLGVLACLthgatmvfpsPSFDPLAVLE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1269 VIDEAirldivrlndyfetngvTITFL---PTQ-LAE----QFMELENTSLRVLLTGG-----DKLKRAVKKPYT--LVN 1333
Cdd:cd05917 87 AIEKE-----------------KCTALhgvPTMfIAElehpDFDKFDLSSLRTGIMAGapcppELMKRVIEVMNMkdVTI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1334 NYGPTENTVVATSAEIH--PEEGSLSIGRAIANTRVYILG-EGNQVQPEGVAGELCVAGRGLARGYLNREDETAKrfVAD 1410
Cdd:cd05917 150 AYGMTETSPVSTQTRTDdsIEKRVNTVGRIMPHTEAKIVDpEGGIVPPVGVPGELCIRGYSVMKGYWNDPEKTAE--AID 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1411 pfvpGERMYRTGDL-VKWVNGGIEYIGRIdQQVKVRG-YRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE 1488
Cdd:cd05917 228 ----GDGWLHTGDLaVMDEDGYCRIVGRI-KDMIIRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLK 302
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 2214269206 1489 ---TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDR 1528
Cdd:cd05917 303 egaELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
7-601 |
1.18e-26 |
|
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: 119.04 E-value: 1.18e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 7 ATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLP 86
Cdd:COG3319 1 AAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 87 IDPDTP----EERIRYSLEDSGAKFAVVNERNMTAIGQYEGIIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGK 162
Cdd:COG3319 81 LAALALalaaAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 163 PKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHyikeHGITY 242
Cdd:COG3319 161 AGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAA----LLALL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 243 IKLTPSLFHTIVNTASFAKDANFESLRLIVLGGEKIIPTDVIAFRkMYGHTEFINHYGPTEATIGAIAGRVDLYEPDAFA 322
Cdd:COG3319 237 LALLLLLLAALLLLLALALLLLLALLLLLGLLALLLALLLLLALL-LLAAAAALAAGGTATTAAVTTTAAAAAPGVAGAL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 323 KRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTL 402
Cdd:COG3319 316 GPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 403 AFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYTSDQDIEKAELRYQLSLTLPSHMIPAFF 482
Cdd:COG3319 396 LGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 483 VQVDAIPLTANGKTDRNALPKPNAAQSGGKALAAPETALEESLCRIWQKTLGIEAIGIDDNFFDLGGHSLKGMMLIANIQ 562
Cdd:COG3319 476 LLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLL 555
|
570 580 590
....*....|....*....|....*....|....*....
gi 2214269206 563 AELEKSVPLKALFEQPTVRQLAAYMEASAVSGGHQVLKP 601
Cdd:COG3319 556 ALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVP 594
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1066-1533 |
1.39e-26 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 116.51 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1066 KDRPAV-TYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYI 1144
Cdd:PRK07514 16 RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1145 LQDSGAKLLL----KQEGIS-------VPDSYTGDVillDGSRTILSLPLDENDEGNPeTAVTAENLAYMIYTSGTTGQP 1213
Cdd:PRK07514 96 IGDAEPALVVcdpaNFAWLSkiaaaagAPHVETLDA---DGTGSLLEAAAAAPDDFET-VPRGADDLAAILYTSGTTGRS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1214 KGVMVEHHALVNLCFWHHDAFSMTAEDRSakyagfgfdasiwemfptwtigaeLHVideairLDIVRLNDYF-ETNGVTI 1292
Cdd:PRK07514 172 KGAMLSHGNLLSNALTLVDYWRFTPDDVL------------------------IHA------LPIFHTHGLFvATNVALL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1293 T-----FLPTQLAEQFMEL--ENTSLR------VLLTGGDKLKRAVKKP------------------------YTLVNNY 1335
Cdd:PRK07514 222 AgasmiFLPKFDPDAVLALmpRATVMMgvptfyTRLLQEPRLTREAAAHmrlfisgsapllaethrefqertgHAILERY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1336 GPTEnTVVATSaeiHPEEGSL---SIGRAIANTRVYILG-EGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADP 1411
Cdd:PRK07514 302 GMTE-TNMNTS---NPYDGERragTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1412 FvpgermYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAV--KDKGgnTAIAAYVTPE 1488
Cdd:PRK07514 378 F------FITGDLGKIdERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVphPDFG--EGVTAVVVPK 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 2214269206 1489 ---TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPE 1533
Cdd:PRK07514 450 pgaALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
7-442 |
2.09e-26 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 116.66 E-value: 2.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 7 ATFAALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLP 86
Cdd:PRK07059 23 PSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 87 IDP-DTPEErIRYSLEDSGAK-------FA-----VVNERNM-----TAIGQ---YEGIIVSLddgKWRNESK-----ER 140
Cdd:PRK07059 103 VNPlYTPRE-LEHQLKDSGAEaivvlenFAttvqqVLAKTAVkhvvvASMGDllgFKGHIVNF---VVRRVKKmvpawSL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 141 PSSIS------------------GSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYV----SW----FSEEAGLTENDKTVL 194
Cdd:PRK07059 179 PGHVRfndalaegarqtfkpvklGPDDVAFLQYTGGTTGVSKGATLLHRNIVANVlqmeAWlqpaFEKKPRPDQLNFVCA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 195 LSSY-AFDLGYTSMFPVLLGGGELHIVQketytaPDEIAHYIKEHGITYIKLTP---SLFHTIVNTASFAKdANFESLRL 270
Cdd:PRK07059 259 LPLYhIFALTVCGLLGMRTGGRNILIPN------PRDIPGFIKELKKYQVHIFPavnTLYNALLNNPDFDK-LDFSKLIV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 271 IVLGGEKIipTDVIAFR--KMYGhTEFINHYGPTEATIGAIAGRVDLyepDAFAKrpTIGRPIANAGALVLNEALKLVPP 348
Cdd:PRK07059 332 ANGGGMAV--QRPVAERwlEMTG-CPITEGYGLSETSPVATCNPVDA---TEFSG--TIGLPLPSTEVSIRDDDGNDLPL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 349 GASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVM 428
Cdd:PRK07059 404 GEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVV 477
|
490
....*....|....
gi 2214269206 429 LSLSGIQEAVVLAV 442
Cdd:PRK07059 478 ASHPGVLEVAAVGV 491
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
150-501 |
3.42e-26 |
|
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: 111.65 E-value: 3.42e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 150 LAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTvLLSSYAFDL-GYTSMFPVLLGGGELHIVQKETYTAP 228
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSW-LLSLPLYHVgGLAILVRSLLAGAELVLLERNQALAE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 229 DeiahyIKEHGITYIKLTPSLFHTIVntASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMygHTEFINHYGPTEATIGA 308
Cdd:cd17630 81 D-----LAPPGVTHVSLVPTQLQRLL--DSGQGPAALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTETASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 309 IAGRVDLYepdafaKRPTIGRPIANAgalvlneALKLVPPGasgQLYITGQGLARGYLNRpqltaerfVENPYSPGSLMY 388
Cdd:cd17630 152 ATKRPDGF------GRGGVGVLLPGR-------ELRIVEDG---EIWVGGASLAMGYLRG--------QLVPEFNEDGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 389 KTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV--SEGGlQELCAYYTSDQDIEKAELR 466
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVpdEELG-QRPVAVIVGRGPADPAELR 286
|
330 340 350
....*....|....*....|....*....|....*
gi 2214269206 467 YQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd17630 287 AWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1079-1501 |
4.06e-26 |
|
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: 114.38 E-value: 4.06e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1079 TYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKqeg 1158
Cdd:cd17640 7 TYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1159 isvpdsytgdvilldgsrtilslpldENDEgnpetavtaENLAYMIYTSGTTGQPKGVMVEH----HALVNL-CF----- 1228
Cdd:cd17640 84 --------------------------ENDS---------DDLATIIYTSGTTGNPKGVMLTHanllHQIRSLsDIvppqp 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1229 ----------WHhdafsmtAEDRSAKYagFGFDASIWEMFPTW-TIGAELHVIDEAIRLDIVRLndyFET--NGVTITFL 1295
Cdd:cd17640 129 gdrflsilpiWH-------SYERSAEY--FIFACGCSQAYTSIrTLKDDLKRVKPHYIVSVPRL---WESlySGIQKQVS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1296 PTQLAEQFMELENTS---LRVLLTGGDKLKRAVKKPYT-----LVNNYGPTENTVVATSAEI-HPEEGslSIGRAIANTR 1366
Cdd:cd17640 197 KSSPIKQFLFLFFLSggiFKFGISGGGALPPHVDTFFEaigieVLNGYGLTETSPVVSARRLkCNVRG--SVGRPLPGTE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1367 VYILG-EGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermYRTGDLVKWVNGG-IEYIGRI-DQQVK 1443
Cdd:cd17640 275 IKIVDpEGNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGeLVLTGRAkDTIVL 348
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 1444 VRGYRIELSEIEVQLAQlSEVQDAAVTAVKDKggnTAIAAYVTPetaDIEALKSTLKE 1501
Cdd:cd17640 349 SNGENVEPQPIEEALMR-SPFIEQIMVVGQDQ---KRLGALIVP---NFEELEKWAKE 399
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
34-442 |
4.84e-26 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 114.78 E-value: 4.84e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNE- 112
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAq 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 -----RNMTAIGQY--EGIIVSlddgkwRNESKERPSSISGSRNL------------------AYVIYTSGTTGKPKGVQ 167
Cdd:PRK08008 119 fypmyRQIQQEDATplRHICLT------RVALPADDGVSSFTQLKaqqpatlcyapplstddtAEILFTSGTTSRPKGVV 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 168 IEHRNLT---NYVSWfseEAGLTENDktVLLS---SYAFDLGYTSMFPVLLGGGELHIVQKetYTApDEIAHYIKEHGIT 241
Cdd:PRK08008 193 ITHYNLRfagYYSAW---QCALRDDD--VYLTvmpAFHIDCQCTAAMAAFSAGATFVLLEK--YSA-RAFWGQVCKYRAT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 242 YIKLTPSLFHTIVNTASFAKDANFEsLR-----LIVLGGEKIiptdviAFRKMYGhTEFINHYGPTEATIGAIAGRvdly 316
Cdd:PRK08008 265 ITECIPMMIRTLMVQPPSANDRQHC-LRevmfyLNLSDQEKD------AFEERFG-VRLLTSYGMTETIVGIIGDR---- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 317 ePDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITG---QGLARGYLNRPQLTAERFvenpySPGSLMYkTGDV 393
Cdd:PRK08008 333 -PGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGvpgKTIFKEYYLDPKATAKVL-----EADGWLH-TGDT 405
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 2214269206 394 VRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV 442
Cdd:PRK08008 406 GYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGI 454
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
10-513 |
9.46e-26 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 114.21 E-value: 9.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 10 AALFEKQAQQTPDHSA--VKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPI 87
Cdd:PRK05852 19 ADLVEVAATRLPEAPAlvVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 88 DPDTPEERIRYSLEDSGAKFAVVN-----ERNMTAI-------------GQYEGII-VSLDDGKwrnESKERPSSISGSR 148
Cdd:PRK05852 99 DPALPIAEQRVRSQAAGARVVLIDadgphDRAEPTTrwwpltvnvggdsGPSGGTLsVHLDAAT---EPTPATSTPEGLR 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 149 -NLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGY-TSMFPVLLGGGELHIVQKETYT 226
Cdd:PRK05852 176 pDDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLiAALLATLASGGAVLLPARGRFS 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 227 APDEIAHyIKEHGITYIKLTPSLfHTIV----NTASFAKDAnfESLRLIVLGGEKIIPTDVIAFRKMYGhTEFINHYGPT 302
Cdd:PRK05852 256 AHTFWDD-IKAVGATWYTAVPTI-HQILleraATEPSGRKP--AALRFIRSCSAPLTAETAQALQTEFA-APVVCAFGMT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 303 EATIGAIAGRVDLYEPDAFAKRPT--IGRPIANAGALVLNEALKLvPPGASGQLYITGQGLARGYLNRPQLTAERFVENp 380
Cdd:PRK05852 331 EATHQVTTTQIEGIGQTENPVVSTglVGRSTGAQIRIVGSDGLPL-PAGAVGEVWLRGTTVVRGYLGDPTITAANFTDG- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 381 yspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYYTSDQD- 459
Cdd:PRK05852 409 ------WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPREs 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 460 --IEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALpkpnAAQSGGKA 513
Cdd:PRK05852 483 apPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV----AEQFGHSV 534
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
609-863 |
1.36e-25 |
|
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Epimerization (E) domains of nonribosomal peptide synthetases (NRPS) flip the chirality of the end amino acid of a peptide being manufactured by the NRPS. E-domains are homologous to the Condensation (C) domains. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. Specialized tailoring NRPS domains such as E-domains greatly increase the range of possible peptide products created by the NRPS machinery. 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 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: 380457 [Multi-domain] Cd Length: 428 Bit Score: 112.35 E-value: 1.36e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 609 PLSSAQKRMYVLNQLDRQtiSYNMpSVLL-MEGELDISRLRDSLNQLVNRHESLRTSFMEANGEPVQRIIEKAE--VDLH 685
Cdd:cd19534 3 PLTPIQRWFFEQNLAGRH--HFNQ-SVLLrVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEelFRLE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 686 VFEAKEDEADQKIKEFI----RPFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKGE------ 755
Cdd:cd19534 80 VVDLSSLAQAAAIEALAaeaqSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQAlagepi 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 756 QLPePTLHYKDFAVWQNEAEQKERMKEHEAYWMSVLSGELPEldLPLDYarppvQSFKGD--TIRFRTGSETAKAvekLL 833
Cdd:cd19534 160 PLP-SKTSFQTWAELLAEYAQSPALLEELAYWRELPAADYWG--LPKDP-----EQTYGDarTVSFTLDEEETEA---LL 228
|
250 260 270
....*....|....*....|....*....|....
gi 2214269206 834 AET----GTTLHMVLHAVFHVFLSKISGQRDIVI 863
Cdd:cd19534 229 QEAnaayRTEINDLLLAALALAFQDWTGRAPPAI 262
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
149-495 |
1.75e-25 |
|
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: 109.90 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 149 NLAYVIYTSGTTGKPKGVQIEHR-NLTNYVSWfSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELhIVQKETYTa 227
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRqTLRAAAAW-ADCADLTEDDRYLIINPFFHTFGYKAGIVACLLTGAT-VVPVAVFD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 228 PDEIAHYIKEHGITYIKLTPSLFHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEATIG 307
Cdd:cd17638 78 VDAILEAIERERITVLPGPPTLFQSLLDHPG-RKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEAGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 308 AIAGRVDlyepDAFAKRPTIGRPIANAGalvlnealklVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpyspGSLm 387
Cdd:cd17638 157 TMCRPGD----DAETVATTCGRACPGFE----------VRIADDGEVLVRGYNVMQGYLDDPEATAEAIDAD----GWL- 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 388 yKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQEL-CAY------YTSDQDI 460
Cdd:cd17638 218 -HTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVgKAFvvarpgVTLTEED 296
|
330 340 350
....*....|....*....|....*....|....*
gi 2214269206 461 EKAELRYQLSltlpSHMIPAFFVQVDAIPLTANGK 495
Cdd:cd17638 297 VIAWCRERLA----NYKVPRFVRFLDELPRNASGK 327
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1051-1533 |
2.24e-25 |
|
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: 113.01 E-value: 2.24e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1051 DKTVHQLFEETVQRHKDRPAVT-----YNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKA 1125
Cdd:cd17642 13 DGTAGEQLHKAMKRYASVPGTIaftdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1126 GAAFVPIDPDYPDQRIEYILQDSGAKLLL-------KQEGISVPDSYTGDVILLDGS---------RTILSLPLDENDEG 1189
Cdd:cd17642 93 GVGVAPTNDIYNERELDHSLNISKPTIVFcskkglqKVLNVQKKLKIIKTIIILDSKedykgyqclYTFITQNLPPGFNE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1190 N---PETAVTAENLAYMIYTSGTTGQPKGVMVEHH----------------------ALVNLCFWHHdAFSMTAedrSAK 1244
Cdd:cd17642 173 YdfkPPSFDRDEQVALIMNSSGSTGLPKGVQLTHKnivarfshardpifgnqiipdtAILTVIPFHH-GFGMFT---TLG 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1245 YAGFGFDASIwemfptwtigaeLHVIDEAIRLDivRLNDYfetnGVTITFL-PTQLA-----EQFMELENTSLRVLLTGG 1318
Cdd:cd17642 249 YLICGFRVVL------------MYKFEEELFLR--SLQDY----KVQSALLvPTLFAffaksTLVDKYDLSNLHEIASGG 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1319 DKLKR----AVKKPYTLV---NNYGPTENTvvaTSAEIHPEE----GSLSIGRAIANTRVYILGEGNQVQPEGvAGELCV 1387
Cdd:cd17642 311 APLSKevgeAVAKRFKLPgirQGYGLTETT---SAILITPEGddkpGAVGKVVPFFYAKVVDLDTGKTLGPNE-RGELCV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1388 AGRGLARGYLNREDETAKRFVADPFVpgermyRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQD 1466
Cdd:cd17642 387 KGPMIMKGYVNNPEATKALIDKDGWL------HSGDIAYYDEDGHFFIvDRLKSLIKYKGYQVPPAELESILLQHPKIFD 460
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 1467 AAVTAVKDKGGNTAIAAYVTPETAdiealKSTLKETLPDYM----IPAFW-----VTLNELPVTANGKVDRKALPE 1533
Cdd:cd17642 461 AGVAGIPDEDAGELPAAVVVLEAG-----KTMTEKEVMDYVasqvSTAKRlrggvKFVDEVPKGLTGKIDRRKIRE 531
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1071-1528 |
3.01e-25 |
|
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: 111.77 E-value: 3.01e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1071 VTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGA 1150
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1151 KLLlkqegisvpdsYTGDvilldgsrtilslpldendegnpetavtAENLAYMIYTSGTTGQPKGVMVEHHALVnlcfWH 1230
Cdd:cd05914 81 KAI-----------FVSD----------------------------EDDVALINYTSGTTGNSKGVMLTYRNIV----SN 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1231 HDAFS----MTAEDRSAKYAGFGfdaSIWEMFPTWTI----GAELHVIDEaIRLDIVRLNDYFETNGVTITFLPTQLAEQ 1302
Cdd:cd05914 118 VDGVKevvlLGKGDKILSILPLH---HIYPLTFTLLLpllnGAHVVFLDK-IPSAKIIALAFAQVTPTLGVPVPLVIEKI 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1303 F-MELENTS---------------------------------LRVLLTGGDKLKRAVKK-------PYTLvnNYGPTENT 1341
Cdd:cd05914 194 FkMDIIPKLtlkkfkfklakkinnrkirklafkkvheafggnIKEFVIGGAKINPDVEEflrtigfPYTI--GYGMTETA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1342 VVATSAEihPEEGSL-SIGRAIANTRVYILGEgnqvQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermYR 1420
Cdd:cd05914 272 PIISYSP--PNRIRLgSAGKVIDGVEVRIDSP----DPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FH 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1421 TGDLVKWVNGGIEYI-GRIDQQ-VKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGgntAIAAYVTPETADIEALK-- 1496
Cdd:cd05914 340 TGDLGKIDAEGYLYIrGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL---VALAYIDPDFLDVKALKqr 416
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 2214269206 1497 ---STLKET--------LPDY-MIPAFWVTLNELPVTANGKVDR 1528
Cdd:cd05914 417 niiDAIKWEvrdkvnqkVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
34-495 |
5.02e-25 |
|
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: 110.98 E-value: 5.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLR-AQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFavvne 112
Cdd:cd05937 7 TYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRF----- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 rnmtaigqyegIIVSLDDgkwrneskerpssisgsrnLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKT 192
Cdd:cd05937 82 -----------VIVDPDD-------------------PAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDRT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 193 V----LLSSYAFDLGYTSmfpVLLGGGELHIVQKetYTA----PDeiahyIKEHGITYIKLTPSLFHTIVNTASFAKDAN 264
Cdd:cd05937 132 YtcmpLYHGTAAFLGACN---CLMSGGTLALSRK--FSAsqfwKD-----VRDSGATIIQYVGELCRYLLSTPPSPYDRD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 265 FeslRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEA------------TIGAIAG----------------RVD-- 314
Cdd:cd05937 202 H---KVRVAWGNGLRPDIWERFRERFNVPEIGEFYAATEGvfaltnhnvgdfGAGAIGHhglirrwkfenqvvlvKMDpe 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 315 ----LYEP-DAFAKRPTIGRPianagalvlNEALKLVPPGAsgqlyitgQGLARGYLNRPQLTAERFVENPYSPGSLMYK 389
Cdd:cd05937 279 tddpIRDPkTGFCVRAPVGEP---------GEMLGRVPFKN--------REAFQGYLHNEDATESKLVRDVFRKGDIYFR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 390 TGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVS----EGglQELCAYYT-SDQDIEKAE 464
Cdd:cd05937 342 TGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKvpghDG--RAGCAAITlEESSAVPTE 419
|
490 500 510
....*....|....*....|....*....|....*.
gi 2214269206 465 LRYQL-----SLTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:cd05937 420 FTKSLlaslaRKNLPSYAVPLFLRLTEEVATTDNHK 455
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
17-498 |
7.16e-25 |
|
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: 111.43 E-value: 7.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 17 AQQTPDHSA---VKAGGN--LLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDT 91
Cdd:cd05970 27 AKEYPDKLAlvwCDDAGEerIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 92 PEERIRYSLEDSGAKFAV-VNERNMTAigQYEGIIVS-------------LDDGkWRN---------ESKERPS--SISG 146
Cdd:cd05970 107 TAKDIVYRIESADIKMIVaIAEDNIPE--EIEKAAPEcpskpklvwvgdpVPEG-WIDfrkliknasPDFERPTanSYPC 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 147 SRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDK--TVLLSSYAFDLgYTSMFPVLLGGGELHIVQKET 224
Cdd:cd05970 184 GEDILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLhlTVADTGWGKAV-WGKIYGQWIAGAAVFVYDYDK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 225 YTaPDEIAHYIKEHGITYIKLTPSLFHTIVNTAsfAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGhTEFINHYGPTEA 304
Cdd:cd05970 263 FD-PKALLEKLSKYGVTTFCAPPTIYRFLIRED--LSRYDLSSLRYCTTAGEALNPEVFNTFKEKTG-IKLMEGFGQTET 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 305 TIgaIAGRVDLYEPdafaKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQ-----GLARGYLNRPQLTAERFVEN 379
Cdd:cd05970 339 TL--TIATFPWMEP----KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 380 pyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSE---GGLQE----LCA 452
Cdd:cd05970 413 -------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDpirGQVVKativLAK 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2214269206 453 YYTSDQDIEKaELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDR 498
Cdd:cd05970 486 GYEPSEELKK-ELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
316-591 |
1.49e-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: 106.37 E-value: 1.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 316 YEPDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLArgYLNRPQLTAERFVENPYSPGSLMYKTGDVVR 395
Cdd:COG3433 9 APPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLL--LRIRLLAAAARAPFIPVPYPAQPGRQADDLR 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 396 RLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSE-----GGLQELCAYYTSDQDIEKAELRYQLS 470
Cdd:COG3433 87 LLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAAlrgagVGLLLIVGAVAALDGLAAAAALAALD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 471 LTLPSHMIPAFFVQVDAIPLTANGKTDRNALPKPNAAQSGG---KALAAPETALEESLCRIWQKTLGI--EAIGIDDNFF 545
Cdd:COG3433 167 KVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAaasPAPALETALTEEELRADVAELLGVdpEEIDPDDNLF 246
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 2214269206 546 DLGGHSLKGMMLIaniqAELEK---SVPLKALFEQPTVRQLAAYMEASA 591
Cdd:COG3433 247 DLGLDSIRLMQLV----ERWRKaglDVSFADLAEHPTLAAWWALLAAAQ 291
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
15-510 |
2.84e-24 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 109.71 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 15 KQAQQTPDHSAVKA--GGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTP 92
Cdd:PRK05857 22 EQARQQPEAIALRRcdGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 93 EERI-RYSLEDSGAKFAVVNERNMTAIGQYEGI----IVSLDDGKWRNESKERPSSISGSRNLAY-------VIYTSGTT 160
Cdd:PRK05857 102 IAAIeRFCQITDPAAALVAPGSKMASSAVPEALhsipVIAVDIAAVTRESEHSLDAASLAGNADQgsedplaMIFTSGTT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 161 GKPKGVQIEHRNL-----------TNYVSWFSEEAGLTENDKTVLLssyafdlGYTSMFPVLLGGGeLHIVQKETYTAPD 229
Cdd:PRK05857 182 GEPKAVLLANRTFfavpdilqkegLNWVTWVVGETTYSPLPATHIG-------GLWWILTCLMHGG-LCVTGGENTTSLL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 230 EIahyIKEHGITYIKLTPSLFHTIVNTASFAkDANFESLRLIVLGGEKIIPTDV-------IAFRKMYGHTEfinhYGPT 302
Cdd:PRK05857 254 EI---LTTNAVATTCLVPTLLSKLVSELKSA-NATVPSLRLVGYGGSRAIAADVrfieatgVRTAQVYGLSE----TGCT 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 303 EATIGAIAGRVDLYEPDAfakrptIGRPIANAGALVLNE--ALKLVPPGAS----GQLYITGQGLARGYLNRPQLTAERF 376
Cdd:PRK05857 326 ALCLPTDDGSIVKIEAGA------VGRPYPGVDVYLAATdgIGPTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAEVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 377 VENpyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSE---GGLQELCAY 453
Cdd:PRK05857 400 IDG-------WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDeefGALVGLAVV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 454 YTSDQDIEKA-ELRYQLSLTL----PSHMIPAFFVQVDAIPLTANGKTDRNALPKP-NAAQSG 510
Cdd:PRK05857 473 ASAELDESAArALKHTIAARFrresEPMARPSTIVIVTDIPRTQSGKVMRASLAAAaTADKAR 535
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1063-1535 |
5.63e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 108.86 E-value: 5.63e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1063 QRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIE 1142
Cdd:PRK07788 60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLA 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1143 YILQDSGAKLLLkqegisVPDSYTGDVIL----LDGSRTILSLPldENDEGNPETAVTAENLA----------------Y 1202
Cdd:PRK07788 140 EVAAREGVKALV------YDDEFTDLLSAlppdLGRLRAWGGNP--DDDEPSGSTDETLDDLIagsstaplpkppkpggI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1203 MIYTSGTTGQPKGVMVEH-HALVNLC-------FWHHDAFSMTAEdrsakyagfgfdasiweMFPTW-----TIGAEL-- 1267
Cdd:PRK07788 212 VILTSGTTGTPKGAPRPEpSPLAPLAgllsrvpFRAGETTLLPAP-----------------MFHATgwahlTLAMALgs 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1268 HVI-----DEAIRLDIVrlndyfETNGVT-ITFLPTQLAEQFMELENT-------SLRVLLTGGDKL-----KRAVKK-P 1328
Cdd:PRK07788 275 TVVlrrrfDPEATLEDI------AKHKATaLVVVPVMLSRILDLGPEVlakydtsSLKIIFVSGSALspelaTRALEAfG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1329 YTLVNNYGPTENTV--VATSAEIHPEEGSlsIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLN-REDETAK 1405
Cdd:PRK07788 349 PVLYNLYGSTEVAFatIATPEDLAEAPGT--VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDgRDKQIID 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1406 RFVAdpfvpgermyrTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAY 1484
Cdd:PRK07788 427 GLLS-----------SGDVGYFDEDGLLFVdGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAF 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 2214269206 1485 VTPE---TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPD 1535
Cdd:PRK07788 496 VVKApgaALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1043-1533 |
6.58e-24 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 108.44 E-value: 6.58e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1043 GKALPVPTD--KTVHQLFEETVQRHKDRPA--VTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAA 1118
Cdd:PRK05852 5 GGAAPMASDfgPRIADLVEVAATRLPEAPAlvVTADRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1119 VLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAK-LLLKQEGIS-----------VPDSYTGDVILLDGSrtiLSLPLDEN 1186
Cdd:PRK05852 85 LLAASRADLVVVPLDPALPIAEQRVRSQAAGARvVLIDADGPHdraepttrwwpLTVNVGGDSGPSGGT---LSVHLDAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1187 DEGNPETAvTAENL----AYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAK----YAGFGFDASiweMF 1258
Cdd:PRK05852 162 TEPTPATS-TPEGLrpddAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAvmplYHGHGLIAA---LL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1259 PTWTIGAELHVIDEAiRLDIVRLNDYFETNGVT-ITFLPTqLAEQFMELENTSLRVLLTGGDKLKRAVKKPYT------- 1330
Cdd:PRK05852 238 ATLASGGAVLLPARG-RFSAHTFWDDIKAVGATwYTAVPT-IHQILLERAATEPSGRKPAALRFIRSCSAPLTaetaqal 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1331 -------LVNNYGPTENTVVATSAEI----HPEEGSLSIGRAIANT--RVYILGEGNQVQPEGVAGELCVAGRGLARGYL 1397
Cdd:PRK05852 316 qtefaapVVCAFGMTEATHQVTTTQIegigQTENPVVSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1398 NREDETAKRFVadpfvpgERMYRTGDLVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKG 1476
Cdd:PRK05852 396 GDPTITAANFT-------DGWLRTGDLGSLsAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQL 468
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1477 -GNTAIAAYVTPETADIEA--LKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPE 1533
Cdd:PRK05852 469 yGEAVAAVIVPRESAPPTAeeLVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1057-1531 |
7.14e-24 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 108.60 E-value: 7.14e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1057 LFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILM-DCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPD 1135
Cdd:PRK08974 28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1136 YPDQRIEYILQDSGAKLLL-------KQEGIsVPDSYTGDVILLD-------GSRTILS--------------LP----- 1182
Cdd:PRK08974 108 YTPRELEHQLNDSGAKAIVivsnfahTLEKV-VFKTPVKHVILTRmgdqlstAKGTLVNfvvkyikrlvpkyhLPdaisf 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1183 LDENDEG------NPEtaVTAENLAYMIYTSGTTGQPKGVMVEHHalvnlcfwhhdafSMTAEDRSAKyagfgfdasiWE 1256
Cdd:PRK08974 187 RSALHKGrrmqyvKPE--LVPEDLAFLQYTGGTTGVAKGAMLTHR-------------NMLANLEQAK----------AA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1257 MFPTWTIGAELHVIdeAIRL---------------------------DI---VR-LNDYFET--NGVTITFLPTQLAEQF 1303
Cdd:PRK08974 242 YGPLLHPGKELVVT--ALPLyhifaltvncllfielggqnllitnprDIpgfVKeLKKYPFTaiTGVNTLFNALLNNEEF 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1304 MELENTSLRVLLTGGDKLKRAVKKPY------TLVNNYGPTENTVVATSAEIHPEEGSLSIGRAIANTRVYILGEGNQVQ 1377
Cdd:PRK08974 320 QELDFSSLKLSVGGGMAVQQAVAERWvkltgqYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEV 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1378 PEGVAGELCVAGRGLARGYLNREDETAKrFVADPFVpgermyRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEV 1456
Cdd:PRK08974 400 PPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGWL------ATGDIAVMDEEGFLRIvDRKKDMILVSGFNVYPNEIED 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214269206 1457 QLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPETADI--EALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK08974 473 VVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLteEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
14-442 |
7.40e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 108.24 E-value: 7.40e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 14 EKQAQQTPDHSAV--KAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPD- 90
Cdd:PRK13391 4 GIHAQTTPDKPAVimASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHl 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 91 TPEErIRYSLEDSGAKFAVVNER-------------------------NMTAIGQYEGIIVSLDDGKWRNESKERPssis 145
Cdd:PRK13391 84 TPAE-AAYIVDDSGARALITSAAkldvarallkqcpgvrhrlvldgdgELEGFVGYAEAVAGLPATPIADESLGTD---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 146 gsrnlayVIYTSGTTGKPKGV--QIEHRNL---TNYVSWFSEEAGLTENdkTVLLSS----YAFDLGYTsMFPVLLGGge 216
Cdd:PRK13391 159 -------MLYSSGTTGRPKGIkrPLPEQPPdtpLPLTAFLQRLWGFRSD--MVYLSPaplyHSAPQRAV-MLVIRLGG-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 217 LHIVQkETYTaPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAKDA-NFESLRlIVLGGEKIIPTDVIafRKMYGHTEF 295
Cdd:PRK13391 227 TVIVM-EHFD-AEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKyDLSSLE-VAIHAAAPCPPQVK--EQMIDWWGP 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 296 INH--YGPTEAtIGAIAGRvdlyEPDAFAKRPTIGRPIanAGAL-VLNEALKLVPPGASGQLYITGqGLARGYLNRPQLT 372
Cdd:PRK13391 302 IIHeyYAATEG-LGFTACD----SEEWLAHPGTVGRAM--FGDLhILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKT 373
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 373 AErfvenPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV 442
Cdd:PRK13391 374 AE-----ARHPDGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGV 438
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
639-918 |
1.39e-23 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. 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 Cyc-domains. 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: 380458 [Multi-domain] Cd Length: 423 Bit Score: 106.03 E-value: 1.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 639 EGE-LDISRLRDSLNQLVNRHESLRTSFMEaNGEpvQRIIEK------AEVDLHvfEAKEDEADQKIKEfIRP------F 705
Cdd:cd19535 33 DGEdLDPDRLERAWNKLIARHPMLRAVFLD-DGT--QQILPEvpwygiTVHDLR--GLSEEEAEAALEE-LRErlshrvL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 706 DLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYK--GEQLPEPTLHYKDFaVWQNEAEQKERMKEH 783
Cdd:cd19535 107 DVERGPLFDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEdpGEPLPPLELSFRDY-LLAEQALRETAYERA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 784 EAYWMSVLSgELPE-LDLPLdyARPPVQsfkGDTIRFRT-----GSETAKAVEKLLAETGTTLHMVLHAVFHVFLSKISG 857
Cdd:cd19535 186 RAYWQERLP-TLPPaPQLPL--AKDPEE---IKEPRFTRrehrlSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSG 259
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2214269206 858 QRDIVIgSVT-AGR--TNADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNLSALEHQEY 918
Cdd:cd19535 260 QPRFLL-NLTlFNRlpLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSY 322
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1080-1538 |
1.66e-23 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 107.09 E-value: 1.66e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1080 YGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLkqegi 1159
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI----- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1160 svpdsytGDVILLDGSR-------TILSLP----------LDEND---------------EGNPETAVTAENLAYMIYTS 1207
Cdd:PRK12406 89 -------AHADLLHGLAsalpagvTVLSVPtppeiaaayrISPALltppagaidwegwlaQQEPYDGPPVPQPQSMIYTS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1208 GTTGQPKGV---------------MVEH--------HALVNLCFWHH--DAFSMtaedRSAKYAGF-----GFDASiwem 1257
Cdd:PRK12406 162 GTTGHPKGVrraaptpeqaaaaeqMRALiyglkpgiRALLTGPLYHSapNAYGL----RAGRLGGVlvlqpRFDPE---- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1258 fptwtigaELHVIDEAIRLDIVRLndyFETNGVTITFLPTQLAEQFmelENTSLRVLLTGGDKLKRAVKKPY------TL 1331
Cdd:PRK12406 234 --------ELLQLIERHRITHMHM---VPTMFIRLLKLPEEVRAKY---DVSSLRHVIHAAAPCPADVKRAMiewwgpVI 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1332 VNNYGPTENTVV--ATSAEI--HPEegslSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLAR-GYLNREDETAKR 1406
Cdd:PRK12406 300 YEYYGSTESGAVtfATSEDAlsHPG----TVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1407 FVADPFVPGERMYRTGDlvkwvngGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYV 1485
Cdd:PRK12406 376 DRGGFITSGDVGYLDAD-------GYLFLcDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVV 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 1486 TPE---TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEPDIEA 1538
Cdd:PRK12406 449 EPQpgaTLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWAN 504
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
33-440 |
1.82e-23 |
|
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: 105.73 E-value: 1.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNE 112
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 rnmtaigqyegiivslddgkwrNESKERPSsisgsrnLAYviYTSGTTGKPKGVQIEHRNL------TNYvsWFseeaGL 186
Cdd:cd05974 81 ----------------------NTHADDPM-------LLY--FTSGTTSKPKLVEHTHRSYpvghlsTMY--WI----GL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 187 TENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIV--NTASFAKdan 264
Cdd:cd05974 124 KPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIqqDLASFDV--- 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 265 feSLRLIVLGGEKIIPTDVIAFRKMYGHTeFINHYGPTEATigAIAGRvdlyEPDAFAKRPTIGRPIANAGALVLNEALK 344
Cdd:cd05974 201 --KLREVVGAGEPLNPEVIEQVRRAWGLT-IRDGYGQTETT--ALVGN----SPGQPVKAGSMGRPLPGYRVALLDPDGA 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 345 lvpPGASGQLYIT-----GQGLARGYLNRPQLTAErfvenpySPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRI 419
Cdd:cd05974 272 ---PATEGEVALDlgdtrPVGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRI 341
|
410 420
....*....|....*....|.
gi 2214269206 420 EPKEIETVMLSLSGIQEAVVL 440
Cdd:cd05974 342 SPFELESVLIEHPAVAEAAVV 362
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
8-495 |
2.02e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 107.17 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 8 TFAALFEKQAQQTPDHSAV--KAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFL 85
Cdd:PRK12583 19 TIGDAFDATVARFPDREALvvRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 86 PIDPDTPEERIRYSLEDSGAKFAVVNERNMTAigQYEGIIVSL-------DDGKWRNE---------------------- 136
Cdd:PRK12583 99 NINPAYRASELEYALGQSGVRWVICADAFKTS--DYHAMLQELlpglaegQPGALACErlpelrgvvslapapppgflaw 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 137 ----------SKERPSSISGSRNLAYVI---YTSGTTGKPKGVQIEHRNLTNYvSWFSEEA-GLTENDKTVLLSSYAFDL 202
Cdd:PRK12583 177 helqargetvSREALAERQASLDRDDPIniqYTSGTTGFPKGATLSHHNILNN-GYFVAESlGLTEHDRLCVPVPLYHCF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 203 GYTSMFPVLLGGGELHIVQKETYTaPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAkDANFESLRLIVLGGEKIiPTD 282
Cdd:PRK12583 256 GMVLANLGCMTVGACLVYPNEAFD-PLATLQAVEEERCTALYGVPTMFIAELDHPQRG-NFDLSSLRTGIMAGAPC-PIE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 283 VIafRKMYGH---TEFINHYGPTEAT-IGAIAGRVDLYEpdafaKR-PTIGRPIANAGALVLNEALKLVPPGASGQLYIT 357
Cdd:PRK12583 333 VM--RRVMDEmhmAEVQIAYGMTETSpVSLQTTAADDLE-----RRvETVGRTQPHLEVKVVDPDGATVPRGEIGELCTR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 358 GQGLARGYLNRPQLTAERFVENPYspgslMYkTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEA 437
Cdd:PRK12583 406 GYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADV 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 438 VVLAV--SEGGlQELCAYYT--SDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:PRK12583 480 QVFGVpdEKYG-EEIVAWVRlhPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGK 540
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1060-1536 |
3.15e-23 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 106.90 E-value: 3.15e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1060 ETVQRH-----KDRPAVTYNG----QSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFV 1130
Cdd:PRK04319 47 EAIDRHadggrKDKVALRYLDasrkEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1131 PIDPDYPDQRIEYILQDSGAKLLlkqegISVPDSYT----------GDVILLDGSRT----ILSLP--LDENDEGNPETA 1194
Cdd:PRK04319 127 PLFEAFMEEAVRDRLEDSEAKVL-----ITTPALLErkpaddlpslKHVLLVGEDVEegpgTLDFNalMEQASDEFDIEW 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1195 VTAENLAYMIYTSGTTGQPKGVMvehHAlvnlcfwhHDAfsMTAEDRSAKYAgfgFDASIWEMF-----PTW-------T 1262
Cdd:PRK04319 202 TDREDGAILHYTSGSTGKPKGVL---HV--------HNA--MLQHYQTGKYV---LDLHEDDVYwctadPGWvtgtsygI 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1263 IGAELH----VIDEAiRLDIVRLNDYFETNGVTITF-LPT----------QLAEQFmelENTSLRVLLTGGDKL------ 1321
Cdd:PRK04319 266 FAPWLNgatnVIDGG-RFSPERWYRILEDYKVTVWYtAPTairmlmgagdDLVKKY---DLSSLRHILSVGEPLnpevvr 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1322 --KRAVKKPytLVNNYGPTE-------NTVvatSAEIHPeeGSLsiGRAIANTRVYILGEGNQVQPEGVAGELCVAgRG- 1391
Cdd:PRK04319 342 wgMKVFGLP--IHDNWWMTEtggimiaNYP---AMDIKP--GSM--GKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGw 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1392 --LARGYLNREDETAKRFVADPFVPGERMYRTGDLVKWvnggieYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAV 1469
Cdd:PRK04319 412 psMMRGIWNNPEKYESYFAGDWYVSGDSAYMDEDGYFW------FQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1470 TAVKDKGGNTAIAAYVT--PETADIEALKSTL----KETLPDYMIPAFWVTLNELPVTANGKVDR---KA----LPEPDI 1536
Cdd:PRK04319 486 IGKPDPVRGEIIKAFVAlrPGYEPSEELKEEIrgfvKKGLGAHAAPREIEFKDKLPKTRSGKIMRrvlKAwelgLPEGDL 565
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
28-501 |
3.19e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 106.60 E-value: 3.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 28 AGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKF 107
Cdd:PLN02330 51 VTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 108 AVVNERNMTAIGQYEGIIVSLDDGK------WRN--ESKERPSSISGSR-----NLAYVIYTSGTTGKPKGVQIEHRNLT 174
Cdd:PLN02330 131 IVTNDTNYGKVKGLGLPVIVLGEEKiegavnWKEllEAADRAGDTSDNEeilqtDLCALPFSSGTTGISKGVMLTHRNLV 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 175 NYV--SWFSEEAGLTENDKTVLLSSYAFDLGYTSM-FPVLLGGGELHIVQK-ETYTapdeIAHYIKEHGITYIKLTPSLF 250
Cdd:PLN02330 211 ANLcsSLFSVGPEMIGQVVTLGLIPFFHIYGITGIcCATLRNKGKVVVMSRfELRT----FLNALITQEVSFAPIVPPII 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 251 HTIVNTASFAK-DANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTE-ATIGAIAGrvDLYEPDAFAKRPTIG 328
Cdd:PLN02330 287 LNLVKNPIVEEfDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEhSCITLTHG--DPEKGHGIAKKNSVG 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 329 RPIANAGALVLN-EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGR 407
Cdd:PLN02330 365 FILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW------LHTGDIGYIDDDGDIFIVDR 438
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 408 ADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV--SEGGLQELCAYYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQ- 484
Cdd:PLN02330 439 IKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLpdEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQf 518
|
490
....*....|....*..
gi 2214269206 485 VDAIPLTANGKTDRNAL 501
Cdd:PLN02330 519 VDSIPKSLSGKIMRRLL 535
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1199-1528 |
3.31e-23 |
|
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: 102.87 E-value: 3.31e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1199 NLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRLDI 1278
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1279 VR-LNDYFETNGVTItflPTQLAEQFMELEN-TSLRVLLTGGDKL----KRAVKK--PYT-LVNNYGPTENTVVATSAEi 1349
Cdd:cd17633 81 IRkINQYNATVIYLV---PTMLQALARTLEPeSKIKSIFSSGQKLfestKKKLKNifPKAnLIEFYGTSELSFITYNFN- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1350 HPEEGSLSIGRAIANTRVYILGEGNqvqpeGVAGELCVAGRGLARGYLNREDETAKRFvadpfvpgermYRTGDlVKWV- 1428
Cdd:cd17633 157 QESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGD-IGYVd 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1429 -NGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPETADIEALKSTLKETLPDYM 1507
Cdd:cd17633 220 eEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYKQLKRFLKQKLSRYE 299
|
330 340
....*....|....*....|.
gi 2214269206 1508 IPAFWVTLNELPVTANGKVDR 1528
Cdd:cd17633 300 IPKKIIFVDSLPYTSSGKIAR 320
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
33-495 |
4.44e-23 |
|
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: 104.74 E-value: 4.44e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNe 112
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVD- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 rnmtaigqyegiivslddgkwrneskerpssisgsrnLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKT 192
Cdd:cd05940 83 -------------------------------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSDVL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 193 V----LLSSYAFDLGYTSMfpvLLGGGELHIVQKetYTAP---DEIAHYikehGITYIKLTPSLFHTIVNTASFAKDaNF 265
Cdd:cd05940 126 YtclpLYHSTALIVGWSAC---LASGATLVIRKK--FSASnfwDDIRKY----QATIFQYIGELCRYLLNQPPKPTE-RK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 266 ESLRLIvLG--------GEKIIPTDVIAFRKMYGHTE----FINHYGPTEAtIGAIAGRVDLYEPDAFAK-RPTIGRPIA 332
Cdd:cd05940 196 HKVRMI-FGnglrpdiwEEFKERFGVPRIAEFYAATEgnsgFINFFGKPGA-IGRNPSLLRKVAPLALVKyDLESGEPIR 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 333 NAGALVlnealKLVPPGASGQL--YITGQGLARGYLNrPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADD 410
Cdd:cd05940 274 DAEGRC-----IKVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFKKGDAWFNTGDLMRLDGEGFWYFVDRLGD 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 411 QVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVS----EG--GLQELCAYYTSDQDIEKaeLRYQLSLTLPSHMIPAFFVQ 484
Cdd:cd05940 348 TFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpgtDGraGMAAIVLQPNEEFDLSA--LAAHLEKNLPGYARPLFLRL 425
|
490
....*....|.
gi 2214269206 485 VDAIPLTANGK 495
Cdd:cd05940 426 QPEMEITGTFK 436
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
607-1012 |
5.53e-23 |
|
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: 104.32 E-value: 5.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 607 MYPLSSAQKRMYVLNQLDRQTISYNMPSVLLMEGELDISRLRDSLNQLVNRHESLRTSFM-EANGEPVQRIIEKAEVDLH 685
Cdd:cd19547 1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTwRDRAEPLQYVRDDLAPPWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 686 VFEAKEDEADQKIKEFIR--------PFDLNDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKG--- 754
Cdd:cd19547 81 LLDWSGEDPDRRAELLERlladdraaGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEElah 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 755 --EQLPEPTLHYKDFAVWQNeaEQKERMKEHEAYWMSVLSGELPEldlPLDYArPPVQSFKGDTIRFRTGSETAKAVEKL 832
Cdd:cd19547 161 grEPQLSPCRPYRDYVRWIR--ARTAQSEESERFWREYLRDLTPS---PFSTA-PADREGEFDTVVHEFPEQLTRLVNEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 833 LAETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTN--ADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTNL 910
Cdd:cd19547 235 ARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPelEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRDLA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 911 SALEHQEYPFEDLVNQLDLPRdMSRNPLFNVMVTTENPDKEQLTLQNLSISPYEAH-QGTSKFDLTLGGFTDENgIGLQL 989
Cdd:cd19547 315 TTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQIIDLHaQEKTEYPIGLIVLPLQK-LAFHF 392
|
410 420
....*....|....*....|...
gi 2214269206 990 EYATDLFAKETAEKWSEyVLRLL 1012
Cdd:cd19547 393 NYDTTHFTRAQVDRFIE-VFRLL 414
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
30-495 |
1.12e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 104.22 E-value: 1.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 30 GNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPD-TPEErIRYSLEDSGAKFA 108
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHlTAAE-IAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 109 VVNER---NMTAIGQYEGIIVSL---DDGK---WRNESKER----PSSISGSRNLAYVIYTSGTTGKPKGVQIE------ 169
Cdd:PRK08276 88 IVSAAladTAAELAAELPAGVPLllvVAGPvpgFRSYEEALaaqpDTPIADETAGADMLYSSGTTGRPKGIKRPlpgldp 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 170 ----HRNLTNYVSWFSEEAGltendkTVLLSS----YAFDLGYTSMfpVLLGGGELHIVQKETytaPDEIAHYIKEHGIT 241
Cdd:PRK08276 168 deapGMMLALLGFGMYGGPD------SVYLSPaplyHTAPLRFGMS--ALALGGTVVVMEKFD---AEEALALIERYRVT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 242 YIKLTPSLFHTIVNTASFAKDA-NFESLRLIVLGGEkiiPTDVIAFRKMyghtefINHYGPT--EATIGAIAGRVDLYEP 318
Cdd:PRK08276 237 HSQLVPTMFVRMLKLPEEVRARyDVSSLRVAIHAAA---PCPVEVKRAM------IDWWGPIihEYYASSEGGGVTVITS 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 319 DAFAKRP-TIGRPIAnAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVenpyspGSLMYKTGDVVRRL 397
Cdd:PRK08276 308 EDWLAHPgSVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN------PHGWVTVGDVGYLD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 398 SDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV--SEGGlQELCAYY-----TSDQDIEKAELRYQLS 470
Cdd:PRK08276 381 EDGYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVpdEEMG-ERVKAVVqpadgADAGDALAAELIAWLR 459
|
490 500
....*....|....*....|....*
gi 2214269206 471 LTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:PRK08276 460 GRLAHYKCPRSIDFEDELPRTPTGK 484
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1067-1544 |
1.60e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 103.71 E-value: 1.60e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWTYGELNAKANRLARILmDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDY-PDQRIEYIL 1145
Cdd:PRK07638 16 NKIAIKENDRVLTYKDWFESVCKVANWL-NEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWkQDELKERLA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1146 QDSGAKLLLKQEGISVPDSYTGDVILLDGSRTILSLPLDEndegnPETAVTAENLA-YMIYTSGTTGQPKGVMVEHHAlv 1224
Cdd:PRK07638 95 ISNADMIVTERYKLNDLPDEEGRVIEIDEWKRMIEKYLPT-----YAPIENVQNAPfYMGFTSGSTGKPKAFLRAQQS-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1225 nlcfWHH------DAFSMTAEDR-----SAKYAGFGFDAsiwemFPTWTIGAELHVIDEAIRLDIVrlnDYFETNGVTIT 1293
Cdd:PRK07638 168 ----WLHsfdcnvHDFHMKREDSvliagTLVHSLFLYGA-----ISTLYVGQTVHLMRKFIPNQVL---DKLETENISVM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1294 F-LPTQLaEQFMELE---NTSLRVLLTGGDKLKRAVKK-----PY-TLVNNYGPTENTVVATSaeiHPEEGSL---SIGR 1360
Cdd:PRK07638 236 YtVPTML-ESLYKENrviENKMKIISSGAKWEAEAKEKiknifPYaKLYEFYGASELSFVTAL---VDEESERrpnSVGR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1361 AIANTRVYILGE-GNQVQPeGVAGELCVAGRGLARGYLNRedetakrfVADPFVPGERMYRTGDLVKWVN--GGIEYIGR 1437
Cdd:PRK07638 312 PFHNVQVRICNEaGEEVQK-GEIGTVYVKSPQFFMGYIIG--------GVLARELNADGWMTVRDVGYEDeeGFIYIVGR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1438 IDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDK-GGNTAIAayVTPETADIEALKSTLKETLPDYMIPAFWVTLN 1516
Cdd:PRK07638 383 EKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSyWGEKPVA--IIKGSATKQQLKSFCLQRLSSFKIPKEWHFVD 460
|
490 500
....*....|....*....|....*...
gi 2214269206 1517 ELPVTANGKVDRKALpEPDIEAGSGEYK 1544
Cdd:PRK07638 461 EIPYTNSGKIARMEA-KSWIENQEKIYE 487
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
14-501 |
1.65e-22 |
|
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: 103.53 E-value: 1.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 14 EKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPE 93
Cdd:cd12118 11 ERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 94 ERIRYSLEDSGAKFAVVNERNmtaigQYEGIIVSLDDG-KWRNESKERpSSISgsrnlayVIYTSGTTGKPKGVQIEHRN 172
Cdd:cd12118 91 EEIAFILRHSEAKVLFVDREF-----EYEDLLAEGDPDfEWIPPADEW-DPIA-------LNYTSGTTGRPKGVVYHHRG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 173 -----LTNYVSWfseEAGltendktvLLSSYAFDL------GYTSMFPVLLGGGELHIVQKETYTApdeIAHYIKEHGIT 241
Cdd:cd12118 158 aylnaLANILEW---EMK--------QHPVYLWTLpmfhcnGWCFPWTVAAVGGTNVCLRKVDAKA---IYDLIEKHKVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 242 YIKLTPSLFHTIVNTASFAKDANFESLRLIVLGGEKiiPTDVIA------FRKM--YGHTEFinhYGPteATIGAIAGRV 313
Cdd:cd12118 224 HFCGAPTVLNMLANAPPSDARPLPHRVHVMTAGAPP--PAAVLAkmeelgFDVThvYGLTET---YGP--ATVCAWKPEW 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 314 DLYEPDAFAK---RPTIGRPIANAGALVLNEALKLVPPGAS--GQLYITGQGLARGYLNRPQLTAERFvENPYspgslmY 388
Cdd:cd12118 297 DELPTEERARlkaRQGVRYVGLEEVDVLDPETMKPVPRDGKtiGEIVFRGNIVMKGYLKNPEATAEAF-RGGW------F 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 389 KTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQE-LCAYYT--SDQDIEKAEL 465
Cdd:cd12118 370 HSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEvPCAFVElkEGAKVTEEEI 449
|
490 500 510
....*....|....*....|....*....|....*.
gi 2214269206 466 RYQLSLTLPSHMIPAFFVQVDaIPLTANGKTDRNAL 501
Cdd:cd12118 450 IAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
7-501 |
2.15e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 104.65 E-value: 2.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 7 ATFAALFEKQAQQTPDHSAVKA---GGNL-----LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVM 78
Cdd:PRK07529 25 ASTYELLSRAAARHPDAPALSFlldADPLdrpetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 79 KAGAAFlPIDPDTPEERIRYSLEDSGAKF---------------------------AVVNERNMTAIGQYEGIIVSLDDG 131
Cdd:PRK07529 105 AAGIAN-PINPLLEPEQIAELLRAAGAKVlvtlgpfpgtdiwqkvaevlaalpelrTVVEVDLARYLPGPKRLAVPLIRR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 132 KWRN--------------ESKERPSSISGSRNLAYViYTSGTTGKPKGVQIEHRNLTnYVSWFSEEAGLTENDKTVLLSS 197
Cdd:PRK07529 184 KAHArildfdaelarqpgDRLFSGRPIGPDDVAAYF-HTGGTTGMPKLAQHTHGNEV-ANAWLGALLLGLGPGDTVFCGL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 198 YAFDLG---YTSMFPVLLGGgelHIV--QKETYTAPDEIAHY---IKEHGITYIKLTPSLFHTIVNTASFAKDANfeSLR 269
Cdd:PRK07529 262 PLFHVNallVTGLAPLARGA---HVVlaTPQGYRGPGVIANFwkiVERYRINFLSGVPTVYAALLQVPVDGHDIS--SLR 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 270 lIVLGGEKIIPTDViaFRKMYGHT--EFINHYGPTEATIGAIAGRVDlyepdaFAKRP-TIGRPI--ANAGALVLNEA-- 342
Cdd:PRK07529 337 -YALCGAAPLPVEV--FRRFEAATgvRIVEGYGLTEATCVSSVNPPD------GERRIgSVGLRLpyQRVRVVILDDAgr 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 343 -LKLVPPGASGQLYITGQGLARGYL----NRPQLTAERFVenpyspgslmyKTGDVVRRLSDGTLAFIGRADDQVkIR-G 416
Cdd:PRK07529 408 yLRDCAVDEVGVLCIAGPNVFSGYLeaahNKGLWLEDGWL-----------NTGDLGRIDADGYFWLTGRAKDLI-IRgG 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 417 YRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQEL-CAYYT--SDQDIEKAELRYQLS------LTLPSHMIPaffvqVDA 487
Cdd:PRK07529 476 HNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELpVAYVQlkPGASATEAELLAFARdhiaerAAVPKHVRI-----LDA 550
|
570
....*....|....
gi 2214269206 488 IPLTANGKTDRNAL 501
Cdd:PRK07529 551 LPKTAVGKIFKPAL 564
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1058-1221 |
4.02e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 103.42 E-value: 4.02e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1058 FEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYP 1137
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1138 DQRIEYILQDSGAKLLLKQEG-----ISVPDSYTGDV-ILLDGSRTILSLPLDEN--------DEGNPET--AVTAENLA 1201
Cdd:PRK08279 123 GAVLAHSLNLVDAKHLIVGEElveafEEARADLARPPrLWVAGGDTLDDPEGYEDlaaaaagaPTTNPASrsGVTAKDTA 202
|
170 180
....*....|....*....|
gi 2214269206 1202 YMIYTSGTTGQPKGVMVEHH 1221
Cdd:PRK08279 203 FYIYTSGTTGLPKAAVMSHM 222
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1-495 |
4.17e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 102.97 E-value: 4.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1 MTQITEATFAALFEKQAQQTPDHSA-VKAGGNL-LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVM 78
Cdd:PRK08315 10 DVPLLEQTIGQLLDRTAARYPDREAlVYRDQGLrWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 79 KAGAAFLPIDPDTPEERIRYSLEDSGAKF-----------------AVVNERNMTAIGQYEG-------IIVSLDDGKWR 134
Cdd:PRK08315 90 KIGAILVTINPAYRLSELEYALNQSGCKAliaadgfkdsdyvamlyELAPELATCEPGQLQSarlpelrRVIFLGDEKHP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 135 -------------NESKERPSSISGSRNLAYVI---YTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDK------- 191
Cdd:PRK08315 170 gmlnfdellalgrAVDDAELAARQATLDPDDPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRlcipvpl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 192 -----TVLLSSYAFDLGYTSMFPvllggGE-------LHIVQKETYTAPdeiahyikeHGItyikltPSLFHTIVNTASF 259
Cdd:PRK08315 250 yhcfgMVLGNLACVTHGATMVYP-----GEgfdplatLAAVEEERCTAL---------YGV------PTMFIAELDHPDF 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 260 AKdANFESLRLIVLGGEkIIPTDVI--AFRKMYgHTEFINHYGPTEATIGAIAGRVDlyepDAFAKR-PTIGRPIANAGA 336
Cdd:PRK08315 310 AR-FDLSSLRTGIMAGS-PCPIEVMkrVIDKMH-MSEVTIAYGMTETSPVSTQTRTD----DPLEKRvTTVGRALPHLEV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 337 LVLNEAL-KLVPPGASGQLYITGQGLARGYLNRPQLTAERFvenpySPGSLMYkTGDVVRRLSDGTLAFIGRADDQVkIR 415
Cdd:PRK08315 383 KIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAI-----DADGWMH-TGDLAVMDEEGYVNIVGRIKDMI-IR 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 416 -GYRIEPKEIETVMLSLSGIQEAVVLAV-SEGGLQELCAYYT--SDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLT 491
Cdd:PRK08315 456 gGENIYPREIEEFLYTHPKIQDVQVVGVpDEKYGEEVCAWIIlrPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMT 535
|
....
gi 2214269206 492 ANGK 495
Cdd:PRK08315 536 VTGK 539
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1040-1531 |
4.63e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 103.50 E-value: 4.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1040 AWKGKALPVptdkTVHQLFEETVQRHKDRPAVTY--------NGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKP 1111
Cdd:PRK07529 17 PLAARDLPA----STYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1112 SLEMSAAVLGVLKAGAAFvPIDPDY-PDQrIEYILQDSGAKLLL------------KQEGI--SVPDSYTgdVILLDGSR 1176
Cdd:PRK07529 93 LPETHFALWGGEAAGIAN-PINPLLePEQ-IAELLRAAGAKVLVtlgpfpgtdiwqKVAEVlaALPELRT--VVEVDLAR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1177 TI-----LSLPLDENDEGN------------------PETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCfWHHDA 1233
Cdd:PRK07529 169 YLpgpkrLAVPLIRRKAHArildfdaelarqpgdrlfSGRPIGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANA-WLGAL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1234 FSMTAEDRSAkYAG---FGFDASIWEMFPTWTIGAelHVI--------DEAIRLDIVRLNDYFEtngvtITFL---PTQL 1299
Cdd:PRK07529 248 LLGLGPGDTV-FCGlplFHVNALLVTGLAPLARGA--HVVlatpqgyrGPGVIANFWKIVERYR-----INFLsgvPTVY 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1300 AeQFMEL-----ENTSLRVLLTGGDKLKRAVKKPY------TLVNNYGPTENTVVATsaeIHPEEGSL---SIGRAIANT 1365
Cdd:PRK07529 320 A-ALLQVpvdghDISSLRYALCGAAPLPVEVFRRFeaatgvRIVEGYGLTEATCVSS---VNPPDGERrigSVGLRLPYQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1366 RVYIL---GEGNQVQPEGVA--GELCVAGRGLARGYLNREDEtakrfvADPFVpGERMYRTGDLvkwvnggieyiGRIDQ 1440
Cdd:PRK07529 396 RVRVVildDAGRYLRDCAVDevGVLCIAGPNVFSGYLEAAHN------KGLWL-EDGWLNTGDL-----------GRIDA 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1441 Q--------VK---VR-GYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVT--PE-TADIEALKSTLKE---- 1501
Cdd:PRK07529 458 DgyfwltgrAKdliIRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELPVAYVQlkPGaSATEAELLAFARDhiae 537
|
570 580 590
....*....|....*....|....*....|..
gi 2214269206 1502 --TLPDYMIPafwvtLNELPVTANGKVDRKAL 1531
Cdd:PRK07529 538 raAVPKHVRI-----LDALPKTAVGKIFKPAL 564
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
605-916 |
5.18e-22 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 100.84 E-value: 5.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 605 QDMYPLSSAQKRMYVLNQldrqtisynmpsVLLMEGELDISRLRDSLNQLVNRHESLRTsfmeangepvqRIIEKAEVDL 684
Cdd:cd19545 9 EGLMALTARQPGAYVGQR------------VFELPPDIDLARLQAAWEQVVQANPILRT-----------RIVQSDSGGL 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 685 HVFEAKEDEADQK----IKEFI-----RPFDLnDAPLIRAALLRIEAKKHLLLLDMHHIIADGVSRGIFVKELALLYKGE 755
Cdd:cd19545 66 LQVVVKESPISWTestsLDEYLeedraAPMGL-GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 756 QLPEPtLHYKDFavwqNEAEQKERMKEHEAYWMSVLSG----ELPELDLPLDYARPpvqsfkgdtirfrTGSETAKAVEK 831
Cdd:cd19545 145 PVPQP-PPFSRF----VKYLRQLDDEAAAEFWRSYLAGldpaVFPPLPSSRYQPRP-------------DATLEHSISLP 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 832 LLAETGTTLHMVLHAVFHVFLSKISGQRDIVIGSVTAGRTN--ADVQDMPGMFVNTLALRMEAKEQQTFAELLELAKQTN 909
Cdd:cd19545 207 SSASSGVTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNApvPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDL 286
|
....*..
gi 2214269206 910 LSALEHQ 916
Cdd:cd19545 287 LDMIPFE 293
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
37-502 |
5.42e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 100.88 E-value: 5.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 37 ELDEQANQLAHHLR-AQGAGNEdiVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNErnm 115
Cdd:PRK08308 13 DFDLRLQRYEEMEQfQEAAGNR--FAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLLYGE--- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 116 taigqyEGIIVSLDDgkwrNESKERPSSISgsrnlayviYTSGTTGKPKgvQIEH------RNLTNYVSWFSEEAGLTEN 189
Cdd:PRK08308 88 ------SDFTKLEAV----NYLAEEPSLLQ---------YSSGTTGEPK--LIRRswteidREIEAYNEALNCEQDETPI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 190 DKTVLLSSYAFDLGytsmfpVLLG---GGELHIVqkeTYTAPDEIAHYIKEHGITYIKLTPSLFHTIvntASFAKDAnfE 266
Cdd:PRK08308 147 VACPVTHSYGLICG------VLAAltrGSKPVII---TNKNPKFALNILRNTPQHILYAVPLMLHIL---GRLLPGT--F 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 267 SLRLIVLGGeKIIPTDViaFRKMYGHTE-FINHYGPTEAtiGAIAGRVDLYEPDAfakrptIGRPIANAGAlvlnealkl 345
Cdd:PRK08308 213 QFHAVMTSG-TPLPEAW--FYKLRERTTyMMQQYGCSEA--GCVSICPDMKSHLD------LGNPLPHVSV--------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 346 vppgasgqlyITGQGLargylNRPQLTAERFVENPYSPGSLMYKTGDvvrrlsdGTLAFIGRADDQVKIRGYRIEPKEIE 425
Cdd:PRK08308 273 ----------SAGSDE-----NAPEEIVVKMGDKEIFTKDLGYKSER-------GTLHFMGRMDDVINVSGLNVYPIEVE 330
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 426 TVMLSLSGIQEAVVLAVSEGGLQE-LCAYYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALP 502
Cdd:PRK08308 331 DVMLRLPGVQEAVVYRGKDPVAGErVKAKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
11-512 |
9.42e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 102.15 E-value: 9.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 11 ALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQ-GAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDP 89
Cdd:PRK05677 28 AVLKQSCQRFADKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 90 DTPEERIRYSLEDSGAKfAVVNERNM------------------TAIGQYEGII------------------------VS 127
Cdd:PRK05677 108 LYTAREMEHQFNDSGAK-ALVCLANMahlaekvlpktgvkhvivTEVADMLPPLkrllinavvkhvkkmvpayhlpqaVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 128 LDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNL-TNYVSWFSEEAGLTENDKTVLLSS------YAF 200
Cdd:PRK05677 187 FNDALAKGAGQPVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLvANMLQCRALMGSNLNEGCEILIAPlplyhiYAF 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 201 DLgyTSMFPVLLGGGELHIvqketyTAPDEIAHYIKEHGIT----YIKLTpSLFHTIVNTASFaKDANFESLRLIVLGGE 276
Cdd:PRK05677 267 TF--HCMAMMLIGNHNILI------SNPRDLPAMVKELGKWkfsgFVGLN-TLFVALCNNEAF-RKLDFSALKLTLSGGM 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 277 KIIPTDVIAFRKMYGhTEFINHYGPTEATigaiagRVDLYEPDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYI 356
Cdd:PRK05677 337 ALQLATAERWKEVTG-CAICEGYGMTETS------PVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 357 TGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQE 436
Cdd:PRK05677 410 KGPQVMKGYWQRPEATDEILDSDGW------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQ 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 437 AVVLAVSEGGLQELCAYYT---SDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALPKPNAAQSGGK 512
Cdd:PRK05677 484 CAAIGVPDEKSGEAIKVFVvvkPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDEELKKAGLK 562
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
17-502 |
1.17e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 101.23 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 17 AQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERI 96
Cdd:PRK13383 45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 97 RYSLEDSGAKFAVVNERNMTAIGQYEGIIVSLDDGK-WRNESKERPSSISGSRnlaYVIYTSGTTGKPKGVQIEHRNLTN 175
Cdd:PRK13383 125 AAALRAHHISTVVADNEFAERIAGADDAVAVIDPATaGAEESGGRPAVAAPGR---IVLLTSGTTGKPKGVPRAPQLRSA 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 176 YVSWFS--EEAGLTENDKTVLLSSYAFDLGYTS-MFPVLLGGGelhIVQKETYTAPDEIAHyIKEHGITYIKLTPSLFHT 252
Cdd:PRK13383 202 VGVWVTilDRTRLRTGSRISVAMPMFHGLGLGMlMLTIALGGT---VLTHRHFDAEAALAQ-ASLHRADAFTAVPVVLAR 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 253 IVNTASFAKDAN-FESLRLIVLGGEKIIPTDVIAFRKMYGHTEFiNHYGPTEATIGAIAGRVDLYE-PDafakrpTIGRP 330
Cdd:PRK13383 278 ILELPPRVRARNpLPQLRVVMSSGDRLDPTLGQRFMDTYGDILY-NGYGSTEVGIGALATPADLRDaPE------TVGKP 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 331 IANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRpqlTAERFVENpyspgslMYKTGDVVRRLSDGTLAFIGRADD 410
Cdd:PRK13383 351 VAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDG---GGKAVVDG-------MTSTGDMGYLDNAGRLFIVGREDD 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 411 QVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGL-QELCAYYTS--DQDIEKAELRYQLSLTLPSHMIPAFFVQVDA 487
Cdd:PRK13383 421 MIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFgHRLAAFVVLhpGSGVDAAQLRDYLKDRVSRFEQPRDINIVSS 500
|
490
....*....|....*
gi 2214269206 488 IPLTANGKTDRNALP 502
Cdd:PRK13383 501 IPRNPTGKVLRKELP 515
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
10-495 |
1.63e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 100.89 E-value: 1.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 10 AALFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVaIVMDRSAEVMV-SILGVMKAGAAFLPID 88
Cdd:PRK07470 10 AHFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRI-LVHSRNCNQMFeSMFAAFRLGAVWVPTN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 89 -PDTPEErIRYSLEDSGAKFAVVN----------------ERNMTAIGQ------YEGIIVSLDDGKWRNESKER--Pss 143
Cdd:PRK07470 89 fRQTPDE-VAYLAEASGARAMICHadfpehaaavraaspdLTHVVAIGGaragldYEALVARHLGARVANAAVDHddP-- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 144 isgsrnlAYVIYTSGTTGKPKGVQIEHRNL----TNYVSWFSeeAGLTEND------------------------KTVLL 195
Cdd:PRK07470 166 -------CWFFFTSGTTGRPKAAVLTHGQMafviTNHLADLM--PGTTEQDaslvvaplshgagihqlcqvargaATVLL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 196 SSYAFDlgytsmfpvllgggelhivqketytaPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAKdANFESLRLIVLGG 275
Cdd:PRK07470 237 PSERFD--------------------------PAEVWALVERHRVTNLFTVPTILKMLVEHPAVDR-YDHSSLRYVIYAG 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 276 EKIIPTDVIAFRKMYGHTeFINHYGPTEATiGAIA---GRVDLYEPDAFAKRPTIGRPIANAGALVLNEALKLVPPGASG 352
Cdd:PRK07470 290 APMYRADQKRALAKLGKV-LVQYFGLGEVT-GNITvlpPALHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETG 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 353 QLYITGQGLARGYLNRPQLTAERFVENpyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLS 432
Cdd:PRK07470 368 EICVIGPAVFAGYYNNPEANAKAFRDG-------WFRTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHP 440
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214269206 433 GIQEAVVLAVSEGGLQE----LCAyYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:PRK07470 441 AVSEVAVLGVPDPVWGEvgvaVCV-ARDGAPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGK 506
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1045-1533 |
2.05e-21 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 100.82 E-value: 2.05e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1045 ALPVPTDKTVHQLFEETVQRHKDRPAVT--YNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGV 1122
Cdd:PLN02330 21 SVPVPDKLTLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1123 LKAGAAFVPIDPDYPDQRIEYILQDSGAKLLL-------KQEGISVPDSYTGDViLLDGSRTILSLpLDENDEGNPETA- 1194
Cdd:PLN02330 101 MAAGGVFSGANPTALESEIKKQAEAAGAKLIVtndtnygKVKGLGLPVIVLGEE-KIEGAVNWKEL-LEAADRAGDTSDn 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1195 --VTAENLAYMIYTSGTTGQPKGVMVEHHALV-NLCfwhHDAFSMTAEdRSAKYAGFGfdasiweMFPTWTIGAELHVID 1271
Cdd:PLN02330 179 eeILQTDLCALPFSSGTTGISKGVMLTHRNLVaNLC---SSLFSVGPE-MIGQVVTLG-------LIPFFHIYGITGICC 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1272 EAIRL--DIVRLNDY----FETNGVT--ITFLP-----------TQLAEQFmELENTSLRVLLTGGDKLKRAV------K 1326
Cdd:PLN02330 248 ATLRNkgKVVVMSRFelrtFLNALITqeVSFAPivppiilnlvkNPIVEEF-DLSKLKLQAIMTAAAPLAPELltafeaK 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1327 KPYTLVNN-YGPTENTVVaTSAEIHPEEG-----SLSIGRAIANTRV-YILGEGNQVQPEGVAGELCVAGRGLARGYLNR 1399
Cdd:PLN02330 327 FPGVQVQEaYGLTEHSCI-TLTHGDPEKGhgiakKNSVGFILPNLEVkFIDPDTGRSLPKNTPGELCVRSQCVMQGYYNN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1400 EDETAKRFVADPFVpgermyRTGDlVKWV--NGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGG 1477
Cdd:PLN02330 406 KEETDRTIDEDGWL------HTGD-IGYIddDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEA 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 1478 NTAIAAYV--TPETADIEA-LKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPE 1533
Cdd:PLN02330 479 GEIPAACVviNPKAKESEEdILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1198-1528 |
2.24e-21 |
|
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: 97.72 E-value: 2.24e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1198 ENLAYMIYTSGTTGQPKGVMVEHHALVN-LCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIRL 1276
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAvPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1277 DivRLNDYFETNGVTITFL-PTQLAEQFMELENT-----SLRVLLTGG-----DKLKRAVKKPYT-LVNNYGPTEnTVVA 1344
Cdd:cd17635 81 K--SLFKILTTNAVTTTCLvPTLLSKLVSELKSAnatvpSLRLIGYGGsraiaADVRFIEATGLTnTAQVYGLSE-TGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1345 TSAEIHPEEGSL-SIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVadpfvpgERMYRTGD 1423
Cdd:cd17635 158 LCLPTDDDSIEInAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI-------DGWVNTGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1424 LVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKG-GNTAIAAYVTPETAD---IEALKST 1498
Cdd:cd17635 231 LGERREDGFLFItGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEfGELVGLAVVASAELDenaIRALKHT 310
|
330 340 350
....*....|....*....|....*....|
gi 2214269206 1499 LKETLPDYMIPAFWVTLNELPVTANGKVDR 1528
Cdd:cd17635 311 IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1057-1534 |
2.80e-21 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 100.22 E-value: 2.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1057 LFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDY 1136
Cdd:PRK13382 48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1137 PDQRIEYILQDSGAKLLLKQEGIS---------VPDSyTGDVILLDGSRTILSLPLDENDEG-NPETAVTAENLayMIYT 1206
Cdd:PRK13382 128 AGPALAEVVTREGVDTVIYDEEFSatvdraladCPQA-TRIVAWTDEDHDLTVEVLIAAHAGqRPEPTGRKGRV--ILLT 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1207 SGTTGQPKGvmvehhalvnlcfwhhdafsmtaedrsAKYAGFG--------FDASIWE----------MFPTWtiGAELH 1268
Cdd:PRK13382 205 SGTTGTPKG---------------------------ARRSGPGgigtlkaiLDRTPWRaeeptvivapMFHAW--GFSQL 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1269 VIDEAIRLDIV-----------RLNDYFETNGVTItfLPTQLaEQFMEL--------ENTSLRVLLTGGDKLKRAVKKPY 1329
Cdd:PRK13382 256 VLAASLACTIVtrrrfdpeatlDLIDRHRATGLAV--VPVMF-DRIMDLpaevrnrySGRSLRFAAASGSRMRPDVVIAF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1330 ------TLVNNYGPTENTVVATS--AEI--HPEegslSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNR 1399
Cdd:PRK13382 333 mdqfgdVIYNNYNATEAGMIATAtpADLraAPD----TAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1400 EDetaKRFVadpfvpgERMYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGN 1478
Cdd:PRK13382 409 ST---KDFH-------DGFMASGDVGYLDENGRLFVvGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYG 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 1479 TAIAAYVTPE---TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEP 1534
Cdd:PRK13382 479 QRLAAFVVLKpgaSATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
34-442 |
2.98e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 100.46 E-value: 2.98e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDS-------GAK 106
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTlrvigmiGAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 107 FAVVNERNMTAIGQYE--GIIVSLDDGKWRNESKERPSSisGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEA 184
Cdd:PRK07768 111 AVVVGEPFLAAAPVLEekGIRVLTVADLLAADPIDPVET--GEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMFVAA 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 185 GLTEnDKTVLLS--SYAFDLGYTSMF--PVLLGGGELHIVQKETYTAPDEIAHYIKEHGITyIKLTPSLFHTIVNT--AS 258
Cdd:PRK07768 189 EFDV-ETDVMVSwlPLFHDMGMVGFLtvPMYFGAELVKVTPMDFLRDPLLWAELISKYRGT-MTAAPNFAYALLARrlRR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 259 FAKDANFE--SLRLIVLGGEKIIPTDVIAF-----RKMYGHTEFINHYGPTEATIGAIAG------RVDLYEPDAFA--- 322
Cdd:PRK07768 267 QAKPGAFDlsSLRFALNGAEPIDPADVEDLldagaRFGLRPEAILPAYGMAEATLAVSFSpcgaglVVDEVDADLLAalr 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 323 -----------KRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYlnrpqLTAERFVENPYSPGslMYKTG 391
Cdd:PRK07768 347 ravpatkgntrRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIPAQDADG--WLDTG 419
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 392 DVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV 442
Cdd:PRK07768 420 DLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAV 470
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
33-439 |
5.45e-21 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 99.58 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNE 112
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITTP 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 RNMTAIGQYE----------GIIVSLDDGKW------RNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRN-LTN 175
Cdd:PRK04319 154 ALLERKPADDlpslkhvllvGEDVEEGPGTLdfnalmEQASDEFDIEWTDREDGAILHYTSGSTGKPKGVLHVHNAmLQH 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 176 YVSwfseeagltendktvllSSYAFDL------------GY---TS--MF-PVLLG------GGEL------HIVQKET- 224
Cdd:PRK04319 234 YQT-----------------GKYVLDLheddvywctadpGWvtgTSygIFaPWLNGatnvidGGRFsperwyRILEDYKv 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 225 ---YTAPDEIAHYIKeHGityikltpslfhtivntASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTeFINHYGP 301
Cdd:PRK04319 297 tvwYTAPTAIRMLMG-AG-----------------DDLVKKYDLSSLRHILSVGEPLNPEVVRWGMKVFGLP-IHDNWWM 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 302 TEAtiGA--IAGRVdlyepdAFAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLYI-TG-QGLARGYLNRPQLTAERF 376
Cdd:PRK04319 358 TET--GGimIANYP------AMDIKPgSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkKGwPSMMRGIWNNPEKYESYF 429
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 377 VENpyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVV 439
Cdd:PRK04319 430 AGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
24-512 |
9.94e-21 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 98.23 E-value: 9.94e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 24 SAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPID-PDTPEErIRYSLED 102
Cdd:PRK12406 3 ATIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNwHFKPEE-IAYILED 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 103 SGAKFAVVNERNMTAIGQY--EGIIV-------------------------SLDDGKWRneSKERPSSISGSRNLAYVIY 155
Cdd:PRK12406 82 SGARVLIAHADLLHGLASAlpAGVTVlsvptppeiaaayrispalltppagAIDWEGWL--AQQEPYDGPPVPQPQSMIY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 156 TSGTTGKPKGVQ-----------IEHRNLTNYvswfseeaGLTENDKTVLL------SSYAFdlgytSMFPVLLGGgelh 218
Cdd:PRK12406 160 TSGTTGHPKGVRraaptpeqaaaAEQMRALIY--------GLKPGIRALLTgplyhsAPNAY-----GLRAGRLGG---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 219 IVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAKDA-NFESLRLIVLGGEKIiPTDVIafRKM---YGHTe 294
Cdd:PRK12406 223 VLVLQPRFDPEELLQLIERHRITHMHMVPTMFIRLLKLPEEVRAKyDVSSLRHVIHAAAPC-PADVK--RAMiewWGPV- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 295 FINHYGPTEatIGAIAGRVdlyEPDAFAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLAR-GYLNRPQLTA 373
Cdd:PRK12406 299 IYEYYGSTE--SGAVTFAT---SEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 374 ErfVENpyspGSLMyKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQE-LCA 452
Cdd:PRK12406 374 E--IDR----GGFI-TSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEaLMA 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 453 YYTSDQDIE--KAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALPKPNAAQSGGK 512
Cdd:PRK12406 447 VVEPQPGATldEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWANAGRK 508
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
34-503 |
1.55e-20 |
|
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: 97.92 E-value: 1.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLR-AQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNE 112
Cdd:cd05928 43 SFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 RNMTAIGQYEG--------IIVSLD--DGkW-------RNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNL-- 173
Cdd:cd05928 123 ELAPEVDSVASecpslktkLLVSEKsrDG-WlnfkellNEASTEHHCVETGSQEPMAIYFTSGTTGSPKMAEHSHSSLgl 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 174 ---TNYVSWFseeaGLTENDKTVLLSsyafDLGY-----TSMFPVLLGGGEL---HIVQKETYTAPDEIAHYikehGITY 242
Cdd:cd05928 202 glkVNGRYWL----DLTASDIMWNTS----DTGWiksawSSLFEPWIQGACVfvhHLPRFDPLVILKTLSSY----PITT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 243 IKLTPSLFHTIV--NTASFakdaNFESLRLIVLGGEKIIPTDVIAFRKMYGhTEFINHYGPTEatIGAIAGRVDLYEpda 320
Cdd:cd05928 270 FCGAPTVYRMLVqqDLSSY----KFPSLQHCVTGGEPLNPEVLEKWKAQTG-LDIYEGYGQTE--TGLICANFKGMK--- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 321 fAKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQ-----GLARGYLNRPQLTAERFVENpyspgslMYKTGDVVR 395
Cdd:cd05928 340 -IKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGD-------FYLTGDRGI 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 396 RLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELC--------AYYTSDQDIEKAELRY 467
Cdd:cd05928 412 MDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVkafvvlapQFLSHDPEQLTKELQQ 491
|
490 500 510
....*....|....*....|....*....|....*..
gi 2214269206 468 QL-SLTLPsHMIPAFFVQVDAIPLTANGKTDRNALPK 503
Cdd:cd05928 492 HVkSVTAP-YKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1018-1532 |
1.83e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 97.76 E-value: 1.83e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1018 NPNQPLSSLLLVTEtekqalleAWKGKALPvptdktvHQLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDC 1097
Cdd:PRK13383 16 NPPSPRAVLRLLRE--------ASRGGTNP-------YTLLAVTAARWPGRTAIIDDDGALSYRELQRATESLARRLTRD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1098 GISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKQEGISVPDSYTGDVILLDGSRT 1177
Cdd:PRK13383 81 GVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPAT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1178 ILSlpldENDEGNPETAVTAEnlaYMIYTSGTTGQPKGVMVEHHALVNLCFWhhdafsMTAEDRS------------AKY 1245
Cdd:PRK13383 161 AGA----EESGGRPAVAAPGR---IVLLTSGTTGKPKGVPRAPQLRSAVGVW------VTILDRTrlrtgsrisvamPMF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1246 AGFGFDASIWEMFPTWTIGAELHVIDEAIrLDIVRLNdyfETNGVTItfLPTQLAeQFMELENT--------SLRVLLTG 1317
Cdd:PRK13383 228 HGLGLGMLMLTIALGGTVLTHRHFDAEAA-LAQASLH---RADAFTA--VPVVLA-RILELPPRvrarnplpQLRVVMSS 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1318 GDKLKRAVKKPY------TLVNNYGPTENTV--VATSAEIH--PEegslSIGRAIANTRVYILGEGNQVQPEGVAGELCV 1387
Cdd:PRK13383 301 GDRLDPTLGQRFmdtygdILYNGYGSTEVGIgaLATPADLRdaPE----TVGKPVAGCPVRILDRNNRPVGPRVTGRIFV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1388 AGRGLARGYlnrEDETAKRFVadpfvpgERMYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQD 1466
Cdd:PRK13383 377 GGELAGTRY---TDGGGKAVV-------DGMTSTGDMGYLDNAGRLFIvGREDDMIISGGENVYPRAVENALAAHPAVAD 446
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 1467 AAVTAVKDKGGNTAIAAYVTPETA---DIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALP 1532
Cdd:PRK13383 447 NAVIGVPDERFGHRLAAFVVLHPGsgvDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1665-1837 |
2.16e-20 |
|
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: 96.27 E-value: 2.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1665 DPERVEKTLQALIEHHDALRMVYREENGDIVQVYKPigESKVSFEIVDLYGSDEEMLRSQIKLLANKL-QSSLDLRNGPL 1743
Cdd:cd19531 37 DVAALERALNELVARHEALRTTFVEVDGEPVQVILP--PLPLPLPVVDLSGLPEAEREAEAQRLAREEaRRPFDLARGPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1744 LKAEQYRTEAGDH-LLIAVHHLVVDGVSWRILLEDFASGYMQAEKEESLVFP----QktnsFKDWA----EELaafsQSA 1814
Cdd:cd19531 115 LRATLLRLGEDEHvLLLTMHHIVSDGWSMGVLLRELAALYAAFLAGRPSPLPplpiQ----YADYAvwqrEWL----QGE 186
|
170 180
....*....|....*....|....*
gi 2214269206 1815 HLLQQAEYW-SQIA-AEQVSPLPKD 1837
Cdd:cd19531 187 VLERQLAYWrEQLAgAPPVLELPTD 211
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
34-501 |
3.36e-20 |
|
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: 96.83 E-value: 3.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNER 113
Cdd:cd17642 46 SYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIVFCSKK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 114 NMTAIGQY-------EGII-----------------VSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIE 169
Cdd:cd17642 126 GLQKVLNVqkklkiiKTIIildskedykgyqclytfITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGLPKGVQLT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 170 HRNLtnyVSWFSEEA----GLTENDKTVLLSSYAF--------DLGY-TSMFPVLLgggeLHIVQKETYTAPdeiahyIK 236
Cdd:cd17642 206 HKNI---VARFSHARdpifGNQIIPDTAILTVIPFhhgfgmftTLGYlICGFRVVL----MYKFEEELFLRS------LQ 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 237 EHGITYIKLTPSLFhTIVNTASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYgHTEFINH-YGPTEATIgAIagrvdL 315
Cdd:cd17642 273 DYKVQSALLVPTLF-AFFAKSTLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRF-KLPGIRQgYGLTETTS-AI-----L 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 316 YEPDAFAKRPTIGRPIANAGALVLN-EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENpyspGSLmyKTGDVV 394
Cdd:cd17642 345 ITPEGDDKPGAVGKVVPFFYAKVVDlDTGKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKD----GWL--HSGDIA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 395 RRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQELCAYY----TSDQDIEKAELRYQLS 470
Cdd:cd17642 419 YYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVvvleAGKTMTEKEVMDYVAS 498
|
490 500 510
....*....|....*....|....*....|.
gi 2214269206 471 LTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd17642 499 QVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
24-503 |
4.11e-20 |
|
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: 97.00 E-value: 4.11e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 24 SAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGA-------AFLP------IDPD 90
Cdd:cd05967 74 SPVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAihsvvfgGFAAkelasrIDDA 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 91 TPE------------ERIRY------SLEDSG---AKFAVVNERNMTAigqyeGIIVSLDDGKWRNESKER----PSSIS 145
Cdd:cd05967 154 KPKlivtascgiepgKVVPYkplldkALELSGhkpHHVLVLNRPQVPA-----DLTKPGRDLDWSELLAKAepvdCVPVA 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 146 GSRNLaYVIYTSGTTGKPKGVQiehRNLTNY---VSW-FSEEAGLTENDktVLLSsyAFDLG------YTSMFPVLLGGG 215
Cdd:cd05967 229 ATDPL-YILYTSGTTGKPKGVV---RDNGGHavaLNWsMRNIYGIKPGD--VWWA--ASDVGwvvghsYIVYGPLLHGAT 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 216 ELHIVQKETYTaPDEIAHY--IKEHGITYIKLTPSLFHTIVN---TASFAKDANFESLRLIVLGGEKIIPtDVIAFRKMY 290
Cdd:cd05967 301 TVLYEGKPVGT-PDPGAFWrvIEKYQVNALFTAPTAIRAIRKedpDGKYIKKYDLSSLRTLFLAGERLDP-PTLEWAENT 378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 291 GHTEFINHYGPTEaTIGAIAGrvdlyEPDAFAKRP----TIGRPIANAGALVLNEALKLVPPGASGQLYITGQgLARGYL 366
Cdd:cd05967 379 LGVPVIDHWWQTE-TGWPITA-----NPVGLEPLPikagSPGKPVPGYQVQVLDEDGEPVGPNELGNIVIKLP-LPPGCL 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 367 NRPQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEG- 445
Cdd:cd05967 452 LTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRDEl 531
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 446 ------GLQELCAYYT-SDQDIEK---AELRYQLSltlPshmIPAF--FVQVDAIPLTANGKTDRNALPK 503
Cdd:cd05967 532 kgqvplGLVVLKEGVKiTAEELEKelvALVREQIG---P---VAAFrlVIFVKRLPKTRSGKILRRTLRK 595
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
33-503 |
4.16e-20 |
|
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: 97.25 E-value: 4.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAA----FLPIDPDTPEERIryslEDSGAKFA 108
Cdd:cd05966 85 ITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVhsvvFAGFSAESLADRI----NDAQCKLV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 109 VvnernmTAIGQYEG----------------------IIV--------SLDDG--KW-----RNESKERPSSISGSRNLA 151
Cdd:cd05966 161 I------TADGGYRGgkviplkeivdealekcpsvekVLVvkrtggevPMTEGrdLWwhdlmAKQSPECEPEWMDSEDPL 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 152 YVIYTSGTTGKPKGVQieHRnLTNYVSWfseeAGLTendktvllSSYAFDLGYTSMF------------------PVLLG 213
Cdd:cd05966 235 FILYTSGSTGKPKGVV--HT-TGGYLLY----AATT--------FKYVFDYHPDDIYwctadigwitghsyivygPLANG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 214 GGELHIVQKETYTAPDEIAHYIKEHGITyikltpsLFHTiVNTA---------SFAKDANFESLRliVLG--GEKIIPTd 282
Cdd:cd05966 300 ATTVMFEGTPTYPDPGRYWDIVEKHKVT-------IFYT-APTAiralmkfgdEWVKKHDLSSLR--VLGsvGEPINPE- 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 283 viAFRKMYghtefiNHYGPTEATIgaiagrVDLY---E---------PDAFAKRP-TIGRPIANAGALVLNEALKLVPPG 349
Cdd:cd05966 369 --AWMWYY------EVIGKERCPI------VDTWwqtEtggimitplPGATPLKPgSATRPFFGIEPAILDEEGNEVEGE 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 350 ASGQLYITGQ--GLARGYLNRPqltaERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETV 427
Cdd:cd05966 435 VEGYLVIKRPwpGMARTIYGDH----ERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESA 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 428 MLSLSGIQEAVVLAVSE---GglQELCAY------YTSDQDIEKaELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDR 498
Cdd:cd05966 511 LVAHPAVAEAAVVGRPHdikG--EAIYAFvtlkdgEEPSDELRK-ELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMR 587
|
....*
gi 2214269206 499 NALPK 503
Cdd:cd05966 588 RILRK 592
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
12-501 |
5.26e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 96.43 E-value: 5.26e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 12 LFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQG---AGneDIVAIVMDRSAEVMVSILGVMKAGAAFLPID 88
Cdd:PRK12492 29 VFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHTdlvPG--DRIAVQMPNVLQYPIAVFGALRAGLIVVNTN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 89 PDTPEERIRYSLEDSGAKFAVVneRNM-----------TAIgQY-------------EGIIVS--LDDGKWRNESKERPS 142
Cdd:PRK12492 107 PLYTAREMRHQFKDSGARALVY--LNMfgklvqevlpdTGI-EYlieakmgdllpaaKGWLVNtvVDKVKKMVPAYHLPQ 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 143 SISGSRNL------------------AYVIYTSGTTGKPKGVQIEHRNLTNYV-------SWFSEEAG-LTENDKTVLLS 196
Cdd:PRK12492 184 AVPFKQALrqgrglslkpvpvglddiAVLQYTGGTTGLAKGAMLTHGNLVANMlqvraclSQLGPDGQpLMKEGQEVMIA 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 197 S------YAFDLGYTSMfpVLLGGGELHIvqketyTAPDEIAHYIKEHG---ITYIKLTPSLFHTIVNTASFaKDANFES 267
Cdd:PRK12492 264 PlplyhiYAFTANCMCM--MVSGNHNVLI------TNPRDIPGFIKELGkwrFSALLGLNTLFVALMDHPGF-KDLDFSA 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 268 LRLIVLGGEKIIPTDVIAFRKMYGHTeFINHYGPTEATIGAIAgrvdlyEP-DAFAKRPTIGRPIANAGALVLNEALKLV 346
Cdd:PRK12492 335 LKLTNSGGTALVKATAERWEQLTGCT-IVEGYGLTETSPVAST------NPyGELARLGTVGIPVPGTALKVIDDDGNEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 347 PPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIET 426
Cdd:PRK12492 408 PLGERGELCIKGPQVMKGYWQQPEATAEALDAEGW------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIED 481
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214269206 427 VMLSLSGIQEAVVLAVSEGGLQELCAYYT--SDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK12492 482 VVMAHPKVANCAAIGVPDERSGEAVKLFVvaRDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1199-1526 |
7.65e-20 |
|
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: 92.95 E-value: 7.65e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1199 NLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDR----SAKYAGFGFDASIWEMFPTwtiGAElhVIDEAI 1274
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRyliiNPFFHTFGYKAGIVACLLT---GAT--VVPVAV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1275 rLDIVRLNDYFETNgvTITFLP-------TQLAEQFM-ELENTSLRVLLTGgdklkrAVKKPYTLVNN------------ 1334
Cdd:cd17638 76 -FDVDAILEAIERE--RITVLPgpptlfqSLLDHPGRkKFDLSSLRAAVTG------AATVPVELVRRmrselgfetvlt 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1335 -YGPTE-NTVVATSAEIHPEEGSLSIGRAIANTRVYILGegnqvqpegvAGELCVAGRGLARGYLNREDETAKRFVADPF 1412
Cdd:cd17638 147 aYGLTEaGVATMCRPGDDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1413 VpgermyRTGDLVKWVNGG-IEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVT---PE 1488
Cdd:cd17638 217 L------HTGDVGELDERGyLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVarpGV 290
|
330 340 350
....*....|....*....|....*....|....*...
gi 2214269206 1489 TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKV 1526
Cdd:cd17638 291 TLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
153-498 |
7.89e-20 |
|
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: 93.10 E-value: 7.89e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 153 VIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKetyTAPDEIA 232
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVMEK---FDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 233 HYIKEHGITYIKLTPSLFHTIVNTASfAKDANFESLRlIVLGGEkiIPTDVIAFRKMYGHTeFINHYGPTEAtigaiAGR 312
Cdd:cd17637 82 ELIEEEKVTLMGSFPPILSNLLDAAE-KSGVDLSSLR-HVLGLD--APETIQRFEETTGAT-FWSLYGQTET-----SGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 313 VDLYEpdaFAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFvENPYspgslmYKTG 391
Cdd:cd17637 152 VTLSP---YRERPgSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-RNGW------HHTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 392 DVVRRLSDGTLAFIGR--ADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEG----GLQELC-----AYYTSDQDI 460
Cdd:cd17637 222 DLGRFDEDGYLWYAGRkpEKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPkwgeGIKAVCvlkpgATLTADELI 301
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 2214269206 461 E-KAEL--RYQLsltlpshmiPAFFVQVDAIPLTANGKTDR 498
Cdd:cd17637 302 EfVGSRiaRYKK---------PRYVVFVEALPKTADGSIDR 333
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1067-1627 |
8.56e-20 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 96.64 E-value: 8.56e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVtYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYpdQRIEYILQ 1146
Cdd:PRK06060 21 DRPAF-YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPEL--HRDDHALA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 --DSGAKLLLKQEgiSVPDSYTGDVILlDGSRTILSLPLDENDEGNPetaVTAENLAYMIYTSGTTGQPKGVMVEH---H 1221
Cdd:PRK06060 98 arNTEPALVVTSD--ALRDRFQPSRVA-EAAELMSEAARVAPGGYEP---MGGDALAYATYTSGTTGPPKAAIHRHadpL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1222 ALVN-LCfwhHDAFSMTAED---RSAK-YAGFGFDASIWemFPTWTIGA----ELHVIDEAIRLdivrLNDYFETN---G 1289
Cdd:PRK06060 172 TFVDaMC---RKALRLTPEDtglCSARmYFAYGLGNSVW--FPLATGGSavinSAPVTPEAAAI----LSARFGPSvlyG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1290 VTITF---LPTQLAEQFmelenTSLRVLLTGGDKLKRAVKKPYT-------LVNNYGPTE--NTVVATSAEihpEEGSLS 1357
Cdd:PRK06060 243 VPNFFarvIDSCSPDSF-----RSLRCVVSAGEALELGLAERLMeffggipILDGIGSTEvgQTFVSNRVD---EWRLGT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1358 IGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNRedetakrfvADPFVPGERMYRTGDLVKWVNGG-IEYIG 1436
Cdd:PRK06060 315 LGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNR---------PDSPVANEGWLDTRDRVCIDSDGwVTYRC 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1437 RIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPETAD------IEALKSTLKETLPDYMIPA 1510
Cdd:PRK06060 386 RADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGAtidgsvMRDLHRGLLNRLSAFKVPH 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1511 FWVTLNELPVTANGKVDRKAL-----PEPDIEAGSGEYKAPT---------------------TDMEELLAGIWQD---- 1560
Cdd:PRK06060 466 RFAVVDRLPRTPNGKLVRGALrkqspTKPIWELSLTEPGSGVraqrddlsasnmtiaggndggATLRERLVALRQErqrl 545
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1561 -----------VLGMSEVGVTDN---FFSLGGDSIKGIQMASRLN-QHGWKLEMKDLFQHPTIEELTQYVErAEGKQADQ 1625
Cdd:PRK06060 546 vvdavcaeaakMLGEPDPWSVDQdlaFSELGFDSQMTVTLCKRLAaVTGLRLPETVGWDYGSISGLAQYLE-AELAGGHG 624
|
..
gi 2214269206 1626 GP 1627
Cdd:PRK06060 625 RL 626
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
32-476 |
1.11e-19 |
|
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: 94.45 E-value: 1.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 32 LLTYRELDEQANQLAHHLRAQGAGnEDIVAIVMDR-SAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSgakfavv 110
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIR-RGMRAVLMVPpGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 111 nernmtAIGQYEGIIVSLDDgkwrneskerpssisgsrnlAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTEND 190
Cdd:cd05910 74 ------EPDAFIGIPKADEP--------------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 191 KTV----LLSSYAFDLGYTSMFPVLlgggelhIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTiVNTASFAKDANFE 266
Cdd:cd05910 128 VDLatfpLFALFGPALGLTSVIPDM-------DPTRPARADPQKLVGAIRQYGVSIVFGSPALLER-VARYCAQHGITLP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 267 SLRLIVLGGEKIIPTDVIAFRKMYG-HTEFINHYGPTEA-TIGAIAGRVDLYEPDAFAKR---PTIGRPIA--------- 332
Cdd:cd05910 200 SLRRVLSAGAPVPIALAARLRKMLSdEAEILTPYGATEAlPVSSIGSRELLATTTAATSGgagTCVGRPIPgvrvriiei 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 333 NAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAerFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQV 412
Cdd:cd05910 280 DDEPIAEWDDTLELPRGEIGEITVTGPTVTPTYVNRPVATA--LAKIDDNSEGFWHRMGDLGYLDDEGRLWFCGRKAHRV 357
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 413 KIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQE--LCAYYTSDQDIEKAELRYQLSLTLPSH 476
Cdd:cd05910 358 ITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLpvLCVEPLPGTITPRARLEQELRALAKDY 423
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1078-1531 |
1.95e-19 |
|
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: 94.45 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1078 WTYGELNAKANRLARILMD-CGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKQ 1156
Cdd:cd05928 42 WSFRELGSLSRKAANVLSGaCGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1157 EGI-SVPDSYTGDVILL-----------DGSRTILSLPLDENDEGNPETAVTAENLAyMIYTSGTTGQPKgvMVEHH--- 1221
Cdd:cd05928 122 DELaPEVDSVASECPSLktkllvseksrDGWLNFKELLNEASTEHHCVETGSQEPMA-IYFTSGTTGSPK--MAEHShss 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1222 ----ALVNLCFWhhdaFSMTAEDRSAKYAGFGF-DASIWEMFPTWTIGA-----ELHVIDEAIRLDIvrLNDYFETngvT 1291
Cdd:cd05928 199 lglgLKVNGRYW----LDLTASDIMWNTSDTGWiKSAWSSLFEPWIQGAcvfvhHLPRFDPLVILKT--LSSYPIT---T 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1292 ITFLPTQ----LAEQFMELENTSLRVLLTGGDKLKRAVKKPYT------LVNNYGPTENTVVATS---AEIHPEegslSI 1358
Cdd:cd05928 270 FCGAPTVyrmlVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKaqtgldIYEGYGQTETGLICANfkgMKIKPG----SM 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1359 GRAIANTRVYILGEGNQVQPEGVAGELCVAGR-----GLARGYLNREDETAKRFVADPFVPGERMYRTGDlvkwvnGGIE 1433
Cdd:cd05928 346 GKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGDFYLTGDRGIMDED------GYFW 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1434 YIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYV--TPE--TADIEALKSTLKE-----TLP 1504
Cdd:cd05928 420 FMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVvlAPQflSHDPEQLTKELQQhvksvTAP 499
|
490 500
....*....|....*....|....*..
gi 2214269206 1505 dYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05928 500 -YKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1069-1534 |
4.77e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 93.04 E-value: 4.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1069 PAVT--YNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQ 1146
Cdd:PRK08276 1 PAVImaPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1147 DSGAKLLLKQEG-------------ISVPDSYT--GDVillDGSRtilslPLDENDEGNPETAVTAENLAY-MIYTSGTT 1210
Cdd:PRK08276 81 DSGAKVLIVSAAladtaaelaaelpAGVPLLLVvaGPV---PGFR-----SYEEALAAQPDTPIADETAGAdMLYSSGTT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1211 GQPKGVMVEhhaLVnlcfwhHDAFSMTAEDRSAKyAGFGFD----------ASIWEMFPTWTIGAELH-----VIDEaiR 1275
Cdd:PRK08276 153 GRPKGIKRP---LP------GLDPDEAPGMMLAL-LGFGMYggpdsvylspAPLYHTAPLRFGMSALAlggtvVVME--K 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1276 LDIVRLNDYFETNGVTIT-FLPTQ------LAEqfmELEN----TSLRVLLTGGDKLKRAVKK-------PyTLVNNYGP 1337
Cdd:PRK08276 221 FDAEEALALIERYRVTHSqLVPTMfvrmlkLPE---EVRArydvSSLRVAIHAAAPCPVEVKRamidwwgP-IIHEYYAS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1338 TE--NTVVATSAE--IHPeeGslSIGRAIAnTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADPFV 1413
Cdd:PRK08276 297 SEggGVTVITSEDwlAHP--G--SVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWV 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1414 PgermyrTGDlVKWVNG-GIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYV------ 1485
Cdd:PRK08276 372 T------VGD-VGYLDEdGYLYLtDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVqpadga 444
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 2214269206 1486 TPETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALPEP 1534
Cdd:PRK08276 445 DAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDR 493
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1079-1531 |
4.94e-19 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 92.25 E-value: 4.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1079 TYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPidpdypdqrieyilqdsgAKLLLKqeg 1158
Cdd:cd05974 2 SFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLT--- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1159 isvPDSYTGDVILLDGSRTILslplDENdegnpetavTAENLAYMIY-TSGTTGQPKGVMVEHHAL----VNLCFWhhda 1233
Cdd:cd05974 61 ---PDDLRDRVDRGGAVYAAV----DEN---------THADDPMLLYfTSGTTSKPKLVEHTHRSYpvghLSTMYW---- 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1234 FSMTAEDRSAKYAGFGFDASIWE-MFPTWTIGAELHVIDEAiRLDIVRLNDYFETNGVTITFLPTQLAEQFMELENTSLR 1312
Cdd:cd05974 121 IGLKPGDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNYA-RFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFD 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1313 VLL----TGGDKLK----RAVKKPY--TLVNNYGPTENTVVATSAEIHPEEGSlSIGRAIANTRVYILgegNQVQPEGVA 1382
Cdd:cd05974 200 VKLrevvGAGEPLNpeviEQVRRAWglTIRDGYGQTETTALVGNSPGQPVKAG-SMGRPLPGYRVALL---DPDGAPATE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1383 GELCV---AGR--GLARGYLNREDETAKrfvadpfVPGERMYRTGDLV-KWVNGGIEYIGRIDQQVKVRGYRIELSEIEV 1456
Cdd:cd05974 276 GEVALdlgDTRpvGLMKGYAGDPDKTAH-------AMRGGYYRTGDIAmRDEDGYLTYVGRADDVFKSSDYRISPFELES 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1457 QLAQLSEVQDAAVTAVKDKGGNTAIAAYV--------TPETAdIEALKSTlKETLPDYMiPAFWVTLNELPVTANGKVDR 1528
Cdd:cd05974 349 VLIEHPAVAEAAVVPSPDPVRLSVPKAFIvlragyepSPETA-LEIFRFS-RERLAPYK-RIRRLEFAELPKTISGKIRR 425
|
...
gi 2214269206 1529 KAL 1531
Cdd:cd05974 426 VEL 428
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1196-1527 |
7.61e-19 |
|
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: 90.52 E-value: 7.61e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1196 TAENLaYMIYTSGTTGQPKGVMvehhalvnlcfW-HHDAFSMT----------------AEDRSAKYAGFGF-------- 1250
Cdd:cd05924 2 SADDL-YILYTGGTTGMPKGVM-----------WrQEDIFRMLmggadfgtgeftpsedAHKAAAAAAGTVMfpapplmh 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1251 DASIWEMFPTWTIGAELHVIDEaiRLDIVRLNDYFETNGVTITFL-------PtqLAEQFMELEN---TSLRVLLTGGDK 1320
Cdd:cd05924 70 GTGSWTAFGGLLGGQTVVLPDD--RFDPEEVWRTIEKHKVTSMTIvgdamarP--LIDALRDAGPydlSSLFAISSGGAL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1321 LKRAVK------KPY-TLVNNYGPTE--NTVVATSAEIHPEEGSlsigRAIANTRVYILGEGNQVQPEGVAGELCVAGRG 1391
Cdd:cd05924 146 LSPEVKqgllelVPNiTLVDAFGSSEtgFTGSGHSAGSGPETGP----FTRANPDTVVLDDDGRVVPPGSGGVGWIARRG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1392 L-ARGYLNREDETAKRFvadPFVPGERMYRTGDLVKWVNGG-IEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAV 1469
Cdd:cd05924 222 HiPLGYYGDEAKTAETF---PEVDGVRYAVPGDRATVEADGtVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLV 298
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 1470 TAVKD-KGGN--TAIAAYVTPETADIEALKSTLKETLPDYMIP-AFWVTlNELPVTANGKVD 1527
Cdd:cd05924 299 VGRPDeRWGQevVAVVQLREGAGVDLEELREHCRTRIARYKLPkQVVFV-DEIERSPAGKAD 359
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
1053-1531 |
7.94e-19 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 92.92 E-value: 7.94e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1053 TVHQLFEETVQRHKDRPAVTYNG---QSWTYGELNAKANRLARILMD-CGISPDDRVGVLTKPSLEMSAAVLGVLKAGAA 1128
Cdd:PRK05620 11 SLTRILEYGSTVHGDTTVTTWGGaeqEQTTFAAIGARAAALAHALHDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGAV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1129 FVPIDPDYPDQRIEYILQDSGAKLLL------KQEGISVPDSYTGDVI--------------------------LLDGSR 1176
Cdd:PRK05620 91 FNPLNKQLMNDQIVHIINHAEDEVIVadprlaEQLGEILKECPCVRAVvfigpsdadsaaahmpegikvysyeaLLDGRS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1177 TILSLPldENDEGNPetavtaenlAYMIYTSGTTGQPKGVMVEHHALvnlcfWHHdAFSMTAEDRSAKYAGFGFDASI-- 1254
Cdd:PRK05620 171 TVYDWP--ELDETTA---------AAICYSTGTTGAPKGVVYSHRSL-----YLQ-SLSLRTTDSLAVTHGESFLCCVpi 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1255 -----WEM-FPTWTIGAELHVIDEAirLDIVRLNDYFET------NGVTItfLPTQLAEQFMEL--ENTSLRVLLTGGDK 1320
Cdd:PRK05620 234 yhvlsWGVpLAAFMSGTPLVFPGPD--LSAPTLAKIIATamprvaHGVPT--LWIQLMVHYLKNppERMSLQEIYVGGSA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1321 LKRAVKKPYT------LVNNYGPTENTVVATSAeiHPEEG---------SLSIGRAIANTRVYILGEGNQVQP-EGVAGE 1384
Cdd:PRK05620 310 VPPILIKAWEerygvdVVHVWGMTETSPVGTVA--RPPSGvsgearwayRVSQGRFPASLEYRIVNDGQVMEStDRNEGE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1385 LCVAGRGLARGYLN----REDETAKRFVADPFVPGERMY------RTGDlVKWVN--GGIEYIGRIDQQVKVRGYRIELS 1452
Cdd:PRK05620 388 IQVRGNWVTASYYHspteEGGGAASTFRGEDVEDANDRFtadgwlRTGD-VGSVTrdGFLTIHDRARDVIRSGGEWIYSA 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1453 EIEVQLAQLSEVQDAAVTAVKD-KGGN-----TAIAAYVTPETADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKV 1526
Cdd:PRK05620 467 QLENYIMAAPEVVECAVIGYPDdKWGErplavTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKF 546
|
....*
gi 2214269206 1527 DRKAL 1531
Cdd:PRK05620 547 DKKDL 551
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
146-501 |
8.15e-19 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 92.57 E-value: 8.15e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 146 GSRNLAYVIYTSGTTGKPKGVQIEHRNLTNyvswfSEEAGL-----TENDktVLLS----SYAFDLGYTSMFPVLLGgge 216
Cdd:PRK06334 181 DPEDVAVILFTSGTEKLPKGVPLTHANLLA-----NQRACLkffspKEDD--VMMSflppFHAYGFNSCTLFPLLSG--- 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 217 LHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASfAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFI 296
Cdd:PRK06334 251 VPVVFAYNPLYPKKIVEMIDEAKVTFLGSTPVFFDYILKTAK-KQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLR 329
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 297 NHYGPTEATigaiaGRVDLYEPDAFAKRPTIGRPIANAGALVLNEALKL-VPPGASGQLYITGQGLARGYL-NRPqltAE 374
Cdd:PRK06334 330 QGYGTTECS-----PVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLgEDF---GQ 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 375 RFVEnpySPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEA-----VVLAVSEGGLQE 449
Cdd:PRK06334 402 GFVE---LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAAdhagpLVVCGLPGEKVR 478
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2214269206 450 LCAYYTSDQDIEKAE--LRyqlSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK06334 479 LCLFTTFPTSISEVNdiLK---NSKTSSILKISYHHQVESIPMLGTGKPDYCSL 529
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
12-501 |
1.15e-18 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 91.98 E-value: 1.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 12 LFEKQAQqtPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAflPIDP-- 89
Cdd:PRK10946 30 ILTRHAA--SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNAlf 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 90 -------DTPEERIRYSL--EDSGAKFAVVNERNMTAIGQYEGIIVSLDDG--------KWRNESKER-PSSISGSRNLA 151
Cdd:PRK10946 106 shqrselNAYASQIEPALliADRQHALFSDDDFLNTLVAEHSSLRVVLLLNddgehsldDAINHPAEDfTATPSPADEVA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 152 YVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENdkTVLL----SSYAFDLGYTSMFPVLLGGGELHIvqketytA 227
Cdd:PRK10946 186 FFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQ--TRYLcalpAAHNYPMSSPGALGVFLAGGTVVL-------A 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 228 PDEIA----HYIKEHGITYIKLTPSLFHTIVNTASFAKD-ANFESLRLIVLGGEKI-------IPtDVIA--FRKMYGHT 293
Cdd:PRK10946 257 PDPSAtlcfPLIEKHQVNVTALVPPAVSLWLQAIAEGGSrAQLASLKLLQVGGARLsetlarrIP-AELGcqLQQVFGMA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 294 EFINHYGpteatigaiagRVDLYEPDAFAkrpTIGRPIANAGAL-VLNEALKLVPPGASGQLYITGQGLARGYLNRPQLT 372
Cdd:PRK10946 336 EGLVNYT-----------RLDDSDERIFT---TQGRPMSPDDEVwVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 373 AERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQE-LC 451
Cdd:PRK10946 402 ASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEkSC 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 452 AYYTSDQDIEKAELR-YQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK10946 476 AFLVVKEPLKAVQLRrFLREQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
33-503 |
1.65e-18 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. 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.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 90.95 E-value: 1.65e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKfavvne 112
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAK------ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 rnmtaigqyeGIIVSLDDGKWRNESKERPSSISGS-RNLAYVIYTSGTTGKPKGVQIEHrnltnyVSWFSEEAGltendk 191
Cdd:cd05939 78 ----------ALIFNLLDPLLTQSSTEPPSQDDVNfRDKLFYIYTSGTTGLPKAAVIVH------SRYYRIAAG------ 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 192 tvllSSYAF-----DLGYTSMfP--------VLLGGGELH---IVQKETYTAPDEIAHYIKeHGITYIKLTPSLFHTIVN 255
Cdd:cd05939 136 ----AYYAFgmrpeDVVYDCL-PlyhsaggiMGVGQALLHgstVVIRKKFSASNFWDDCVK-YNCTIVQYIGEICRYLLA 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 256 TaSFAKDANFESLRLIVLGG--EKIIPTDVIAFR-----KMYGHTEFINHYGPTEATIGAIaGRVDLYEPDAFAKR---- 324
Cdd:cd05939 210 Q-PPSEEEQKHNVRLAVGNGlrPQIWEQFVRRFGipqigEFYGATEGNSSLVNIDNHVGAC-GFNSRILPSVYPIRlikv 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 325 -PTIGRPIANAGALVLnealkLVPPGASGQLY---ITGQGLAR--GYLNRPQlTAERFVENPYSPGSLMYKTGDVVRRLS 398
Cdd:cd05939 288 dEDTGELIRDSDGLCI-----PCQPGEPGLLVgkiIQNDPLRRfdGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 399 DGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQ---ELCAYYTSDQDIEKAELRYQLSLTLPS 475
Cdd:cd05939 362 LGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEgraGMAAIVDPERKVDLDRFSAVLAKSLPP 441
|
490 500
....*....|....*....|....*...
gi 2214269206 476 HMIPAFFVQVDAIPLTANGKTDRNALPK 503
Cdd:cd05939 442 YARPQFIRLLPEVDKTGTFKLQKTDLQK 469
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1080-1528 |
1.68e-18 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 91.99 E-value: 1.68e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1080 YGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPID-PDYPDQRIEYI------LQDSGAKL 1152
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYIaqlrgmLASAQPAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1153 LLKQEGIS--VPDSYTGDVILLDGSRTILSLPlDENDEGNPEtaVTAENLAYMIYTSGTTGQPKGVMVEHHALV-NLCFW 1229
Cdd:PRK09192 132 IITPDELLpwVNEATHGNPLLHVLSHAWFKAL-PEADVALPR--PTPDDIAYLQYSSGSTRFPRGVIITHRALMaNLRAI 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1230 HHDAFSMTAEDRSAKYAGFGFDASIWEMFPTwTIGAELHVI-----DEAIR----LD-IVRlndyfetNGVTITFLPT-- 1297
Cdd:PRK09192 209 SHDGLKVRPGDRCVSWLPFYHDMGLVGFLLT-PVATQLSVDylptrDFARRplqwLDlISR-------NRGTISYSPPfg 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1298 ------QLAEQ-FMELENTSLRVLLTGGD-----KLKRAVKK-------PYTLVNNYGPTENT----------------- 1341
Cdd:PRK09192 281 yelcarRVNSKdLAELDLSCWRVAGIGADmirpdVLHQFAEAfapagfdDKAFMPSYGLAEATlavsfsplgsgivveev 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1342 ----------VVATSAEIHPEEGSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREdETAKRFVADP 1411
Cdd:PRK09192 361 drdrleyqgkAVAPGAETRRVRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDE-ESQDVLAADG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1412 FVpgermyRTGDLVKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQ--DAAVTAVKDKGGNtAIAAYVTPET 1489
Cdd:PRK09192 440 WL------DTGDLGYLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGE-KIVLLVQCRI 512
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2214269206 1490 ADIEALKStLKETLPDYMIPAFWVTL-------NELPVTANGKVDR 1528
Cdd:PRK09192 513 SDEERRGQ-LIHALAALVRSEFGVEAavelvppHSLPRTSSGKLSR 557
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
16-495 |
2.12e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 90.84 E-value: 2.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 16 QAQQTPDHSAVKAG--GNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPE 93
Cdd:PRK13390 6 HAQIAPDRPAVIVAetGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 94 ERIRYSLEDSGAKfAVVNERNMTAIGQYEGIIVSLD-------DGKWRNESK---------ERPSSisgsrnlAYVIYTS 157
Cdd:PRK13390 86 PEADYIVGDSGAR-VLVASAALDGLAAKVGADLPLRlsfggeiDGFGSFEAAlagagprltEQPCG-------AVMLYSS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 158 GTTGKPKGVQ--IEHRNLTN----YVSWFSEEAGLTENDktVLLSS----YAFDLGYTSMFPVLlgGGElhIVQKETYTA 227
Cdd:PRK13390 158 GTTGFPKGIQpdLPGRDVDApgdpIVAIARAFYDISESD--IYYSSapiyHAAPLRWCSMVHAL--GGT--VVLAKRFDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 228 PDEIAHyIKEHGITYIKLTPSLFHTIVN-TASFAKDANFESLRLIVLGGEKiIPTDVI-AFRKMYGHTEFiNHYGPTEAt 305
Cdd:PRK13390 232 QATLGH-VERYRITVTQMVPTMFVRLLKlDADVRTRYDVSSLRAVIHAAAP-CPVDVKhAMIDWLGPIVY-EYYSSTEA- 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 306 igaiAGRVDLYEPDAFAKRPTIGRPIANAGALVLNEALKLvPPGASGQLYITGQGLARGYLNRPQLTAErfVENPYSPgs 385
Cdd:PRK13390 308 ----HGMTFIDSPDWLAHPGSVGRSVLGDLHICDDDGNEL-PAGRIGTVYFERDRLPFRYLNDPEKTAA--AQHPAHP-- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 386 LMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV--SEGGLQ-----ELCAYYTSDQ 458
Cdd:PRK13390 379 FWTTVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVpdPEMGEQvkaviQLVEGIRGSD 458
|
490 500 510
....*....|....*....|....*....|....*..
gi 2214269206 459 DIEKAELRYQLSlTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:PRK13390 459 ELARELIDYTRS-RIAHYKAPRSVEFVDELPRTPTGK 494
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
7-501 |
3.32e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 90.51 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 7 ATFAALFEKQAQQtpDHSAVKAGGNLLTYRELDEQANQLAHHLRAQ-GAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFL 85
Cdd:PRK07867 5 PTVAELLLPLAED--DDRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALSGIVPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 86 PIDPDTPEERIRYSLEDSGAKFaVVNERNMTAI--GQYEGI-IVSLDDGKWRNE------SKERPSSISGSrNLAYVIYT 156
Cdd:PRK07867 83 GLNPTRRGAALARDIAHADCQL-VLTESAHAELldGLDPGVrVINVDSPAWADElaahrdAEPPFRVADPD-DLFMLIFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 157 SGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDkTVLLS-----SYAFDLGYTsmfPVLLGGGELHIVQKetYTA---- 227
Cdd:PRK07867 161 SGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDD-VCYVSmplfhSNAVMAGWA---VALAAGASIALRRK--FSAsgfl 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 228 PDeiahyIKEHGITYIKLTPSLFHTIVNTASFAKDANfESLRlIVLGGEKIiPTDVIAFRKMYGhTEFINHYGPTE---- 303
Cdd:PRK07867 235 PD-----VRRYGATYANYVGKPLSYVLATPERPDDAD-NPLR-IVYGNEGA-PGDIARFARRFG-CVVVDGFGSTEggva 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 304 ---------ATIGAIAGRVDLYEPDAFAKRPTiGRpIANAGALVLNEALklvppgasGQLY-ITGQGLARGYLNRPQLTA 373
Cdd:PRK07867 306 itrtpdtppGALGPLPPGVAIVDPDTGTECPP-AE-DADGRLLNADEAI--------GELVnTAGPGGFEGYYNDPEADA 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 374 ERFVENpyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV--SEGGLQ--- 448
Cdd:PRK07867 376 ERMRGG-------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVpdPVVGDQvma 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 449 --ELCAYYTSDQDIEKAELRYQLSLTlpSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK07867 449 alVLAPGAKFDPDAFAEFLAAQPDLG--PKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
23-499 |
3.77e-18 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 90.63 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 23 HSAVKAGGN-LLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDpdtpeerIRYSLE 101
Cdd:PLN02860 22 NAVVTISGNrRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLN-------YRWSFE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 102 DsgAKFA---------------------------------VVNERNMTAIGQYEGIIVSLDDGKWRNESKERPSSISGSR 148
Cdd:PLN02860 95 E--AKSAmllvrpvmlvtdetcsswyeelqndrlpslmwqVFLESPSSSVFIFLNSFLTTEMLKQRALGTTELDYAWAPD 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 149 NLAYVIYTSGTTGKPKGVQIEHRNLTnyVSWFSEEA--GLTENDKTVLLSSYAFDLGYTS-MFPVLLGGGELHIVQKETY 225
Cdd:PLN02860 173 DAVLICFTSGTTGRPKGVTISHSALI--VQSLAKIAivGYGEDDVYLHTAPLCHIGGLSSaLAMLMVGACHVLLPKFDAK 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 226 TAPDEIahyiKEHGITYIKLTPSLFHTIVNTASFAK-DANFESLRLIVLGGEKIiPTDVI-AFRKMYGHTEFINHYGPTE 303
Cdd:PLN02860 251 AALQAI----KQHNVTSMITVPAMMADLISLTRKSMtWKVFPSVRKILNGGGSL-SSRLLpDAKKLFPNAKLFSAYGMTE 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 304 A----TIgaiagrVDLYEPDAFAKRPTIGRPIANA--------GALVLNEA----LKLVPPGASGqlyiTGQGLARGyln 367
Cdd:PLN02860 326 AcsslTF------MTLHDPTLESPKQTLQTVNQTKsssvhqpqGVCVGKPAphveLKIGLDESSR----VGRILTRG--- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 368 rPQLTAERFVENPYSPGSLM----YKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVS 443
Cdd:PLN02860 393 -PHVMLGYWGQNSETASVLSndgwLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVP 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 444 EGGLQELCA--------YYTSDQDIEKAELRYQLS----------LTLPSHMIPAFFVQ-VDAIPLTANGKTDRN 499
Cdd:PLN02860 472 DSRLTEMVVacvrlrdgWIWSDNEKENAKKNLTLSsetlrhhcreKNLSRFKIPKLFVQwRKPFPLTTTGKIRRD 546
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
12-444 |
4.96e-18 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 90.04 E-value: 4.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 12 LFEKqAQQTPDHSAVKAG--GNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDP 89
Cdd:PLN02246 29 CFER-LSEFSDRPCLIDGatGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 90 -DTPEErIRYSLEDSGAKFAVVNER---NMTAIGQYEGI-IVSLDDGK----------WRNESKERPSSISGSRNLAyVI 154
Cdd:PLN02246 108 fYTPAE-IAKQAKASGAKLIITQSCyvdKLKGLAEDDGVtVVTIDDPPegclhfseltQADENELPEVEISPDDVVA-LP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 155 YTSGTTGKPKGVQIEHRNLTNYVSWFSEEA----GLTENDktVLLSS------YAFDlgyTSMFPVLLGGGELHIVQKET 224
Cdd:PLN02246 186 YSSGTTGLPKGVMLTHKGLVTSVAQQVDGEnpnlYFHSDD--VILCVlpmfhiYSLN---SVLLCGLRVGAAILIMPKFE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 225 YTAPDEIahyIKEHGITYIKLTPSLFHTIVNTASFAKDaNFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHYGPTEa 304
Cdd:PLN02246 261 IGALLEL---IQRHKVTIAPFVPPIVLAIAKSPVVEKY-DLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTE- 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 305 tigaiAGRVdLYEPDAFAKRPTIGRPIAnAGALVLNEALKLVPP--GAS------GQLYITGQGLARGYLNRPQLTAERF 376
Cdd:PLN02246 336 -----AGPV-LAMCLAFAKEPFPVKSGS-CGTVVRNAELKIVDPetGASlprnqpGEICIRGPQIMKGYLNDPEATANTI 408
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 377 VENpyspGSLmyKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSE 444
Cdd:PLN02246 409 DKD----GWL--HTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKD 470
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
33-439 |
6.50e-18 |
|
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: 89.58 E-value: 6.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGA--GNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIdPDT-PEERIRYSLEDSGAKFAV 109
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPL-YDTlGPEAIEYILNHAEISIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 110 VnERNMTaigqyegiIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTE- 188
Cdd:cd05927 85 C-DAGVK--------VYSLEEFEKLGKKNKVPPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNk 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 189 -NDKTVLLS----SYAFD-LGYTSMFPVllgGGELHIVQKETYTAPDEiahyIKEHGITYIKLTPSLFH----------- 251
Cdd:cd05927 156 iNPTDVYISylplAHIFErVVEALFLYH---GAKIGFYSGDIRLLLDD----IKALKPTVFPGVPRVLNriydkifnkvq 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 252 -------TIVNTASFAKDANFES------------------------LRLIVLGGEKIIPTDVIAFRKMYGhTEFINHYG 300
Cdd:cd05927 229 akgplkrKLFNFALNYKLAELRSgvvraspfwdklvfnkikqalggnVRLMLTGSAPLSPEVLEFLRVALG-CPVLEGYG 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 301 PTEATIGAIAGRVDlyEPDAfakrPTIGRPIANagalvlNEA-LKLVP--------PGASGQLYITGQGLARGYLNRPQL 371
Cdd:cd05927 308 QTECTAGATLTLPG--DTSV----GHVGGPLPC------AEVkLVDVPemnydakdPNPRGEVCIRGPNVFSGYYKDPEK 375
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 372 TAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKI-RGYRIEPKEIETVMLSLSGIQEAVV 439
Cdd:cd05927 376 TAEALDEDGW------LHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFV 438
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
152-497 |
6.51e-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: 87.82 E-value: 6.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 152 YVIYTSGTTGKPKGVQIEHrnltnyVSWFSEEAGLTENDKTVLLSSYAFDL-----GYTSMFPV---------------L 211
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQ------EDIFRMLMGGADFGTGEFTPSEDAHKaaaaaAGTVMFPApplmhgtgswtafggL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 212 LGGGELHIVQKEtyTAPDEIAHYIKEHGITYIKLTPSLF-HTIVNTASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMY 290
Cdd:cd05924 81 LGGQTVVLPDDR--FDPEEVWRTIEKHKVTSMTIVGDAMaRPLIDALRDAGPYDLSSLFAISSGGALLSPEVKQGLLELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 291 GHTEFINHYGPTEA---TIGAIAGRVDLYEPdafakrptigRPIANAGALVLNEALKLVPPGASGQLYITGQGL-ARGYL 366
Cdd:cd05924 159 PNITLVDAFGSSETgftGSGHSAGSGPETGP----------FTRANPDTVVLDDDGRVVPPGSGGVGWIARRGHiPLGYY 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 367 NRPQLTAERFVEnpysPGSLMYK-TGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV-SE 444
Cdd:cd05924 229 GDEAKTAETFPE----VDGVRYAvPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRpDE 304
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 445 GGLQELCAYYTSDQ--DIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTD 497
Cdd:cd05924 305 RWGQEVVAVVQLREgaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1075-1525 |
7.72e-18 |
|
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: 88.95 E-value: 7.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1075 GQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLL 1154
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1155 kqegisvpdsytgdvilldgsrtilslpldendegnpetaVTAenlAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAF 1234
Cdd:cd05940 81 ----------------------------------------VDA---ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1235 SMTAEDR----------SAKYAGFG--------------FDAS-IWEmfptwtigaelhvideairlDIVRLN-DYFETN 1288
Cdd:cd05940 118 GALPSDVlytclplyhsTALIVGWSaclasgatlvirkkFSASnFWD--------------------DIRKYQaTIFQYI 177
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1289 GVTITFLPTQLAEqfmELENT-SLRVLLTGG------DKLKRAVKKPyTLVNNYGPTENTV-----------VATSAEIH 1350
Cdd:cd05940 178 GELCRYLLNQPPK---PTERKhKVRMIFGNGlrpdiwEEFKERFGVP-RIAEFYAATEGNSgfinffgkpgaIGRNPSLL 253
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1351 PEEGSLSIGRAIANTRVYILGEGNQVQ--PEGVAGELCVAGRGLAR--GYLNREdETAKRFVADPFVPGERMYRTGDLVK 1426
Cdd:cd05940 254 RKVAPLALVKYDLESGEPIRDAEGRCIkvPRGEPGLLISRINPLEPfdGYTDPA-ATEKKILRDVFKKGDAWFNTGDLMR 332
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1427 WV-NGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVK--DKGGNTAIAAYVTPETA--DIEALKSTLKE 1501
Cdd:cd05940 333 LDgEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQvpGTDGRAGMAAIVLQPNEefDLSALAAHLEK 412
|
490 500
....*....|....*....|....
gi 2214269206 1502 TLPDYMIPAFWVTLNELPVTANGK 1525
Cdd:cd05940 413 NLPGYARPLFLRLQPEMEITGTFK 436
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1049-1539 |
1.06e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 88.97 E-value: 1.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1049 PTDKTVHQLFEEtvQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDcgISPDDR---VGVLTKPSLEMSAAVLGVLKA 1125
Cdd:PRK07867 2 SSAPTVAELLLP--LAEDDDRGLYFEDSFTSWREHIRGSAARAAALRA--RLDPTRpphVGVLLDNTPEFSLLLGAAALS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1126 GAAFVPIDPDypdQRIEYILQD---SGAKLLLKQEG-ISVPDSYTGDVILLDGSRTILSLPLDENDEGNPE-TAVTAENL 1200
Cdd:PRK07867 78 GIVPVGLNPT---RRGAALARDiahADCQLVLTESAhAELLDGLDPGVRVINVDSPAWADELAAHRDAEPPfRVADPDDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1201 AYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSakYAG---FGFDASIWEMFPTWTIGAELhvideAIR-- 1275
Cdd:PRK07867 155 FMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVC--YVSmplFHSNAVMAGWAVALAAGASI-----ALRrk 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1276 ------LDIVRL--NDYFETNGVTITFLptqLA--EQFMELENTsLRVLL----TGGDKLKRAVKKPYTLVNNYGPTENT 1341
Cdd:PRK07867 228 fsasgfLPDVRRygATYANYVGKPLSYV---LAtpERPDDADNP-LRIVYgnegAPGDIARFARRFGCVVVDGFGSTEGG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1342 VVATSAEIHPEeGSLsiGRAIANTRVY-----------ILGEGNQVQPEGVAGELC-VAGRGLARGYLNREDETAKRFVa 1409
Cdd:PRK07867 304 VAITRTPDTPP-GAL--GPLPPGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMR- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1410 dpfvpgERMYRTGDLV-KWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKG-GNTAIAAYVTP 1487
Cdd:PRK07867 380 ------GGVYWSGDLAyRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVvGDQVMAALVLA 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2214269206 1488 ETA--DIEALKSTLKETlPDY---MIPAFWVTLNELPVTANGKVDRKALPEPDIEAG 1539
Cdd:PRK07867 454 PGAkfDPDAFAEFLAAQ-PDLgpkQWPSYVRVCAELPRTATFKVLKRQLSAEGVDCA 509
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
6-407 |
1.09e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 89.33 E-value: 1.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 6 EATFAALFEKQAQQTPDHS--AVKAGGN----LLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMK 79
Cdd:PRK12582 48 PRSIPHLLAKWAAEAPDRPwlAQREPGHgqwrKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 80 AGAAFLPIDP-----DTPEERIRYSLE---------DSGAKF----AVVNERNMTAI---GQYEGI-IVSLDD---GKWR 134
Cdd:PRK12582 128 AGVPAAPVSPayslmSHDHAKLKHLFDlvkprvvfaQSGAPFaralAALDLLDVTVVhvtGPGEGIaSIAFADlaaTPPT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 135 NESKERPSSIsGSRNLAYVIYTSGTTGKPKGVQIEHR----NLTNYVSWFSEEAgltENDKTVLLS----SYAFdlGYTS 206
Cdd:PRK12582 208 AAVAAAIAAI-TPDTVAKYLFTSGSTGMPKAVINTQRmmcaNIAMQEQLRPREP---DPPPPVSLDwmpwNHTM--GGNA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 207 MF-PVLLGGGELHIvqKETYTAPDEIAHYIK---EHGITYIKLTPSLFHTIVntASFAKDAN-----FESLRLIVLGGEK 277
Cdd:PRK12582 282 NFnGLLWGGGTLYI--DDGKPLPGMFEETIRnlrEISPTVYGNVPAGYAMLA--EAMEKDDAlrrsfFKNLRLMAYGGAT 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 278 iIPTDV---------------IAFRKMYGHTEfinhYGPTEATIGAIAGRVDLyepdafakrptIGRPIANAgalvlneA 342
Cdd:PRK12582 358 -LSDDLyermqalavrttghrIPFYTGYGATE----TAPTTTGTHWDTERVGL-----------IGLPLPGV-------E 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 343 LKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVR-----RLSDGtLAFIGR 407
Cdd:PRK12582 415 LKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARfvdpdDPEKG-LIFDGR 477
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1046-1474 |
1.15e-17 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 88.88 E-value: 1.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1046 LPVPTDKTVHQLFEETVQRHKDRPAVT--YNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVL 1123
Cdd:PLN02246 17 IYIPNHLPLHDYCFERLSEFSDRPCLIdgATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGAS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1124 KAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKQ-------EGISVPDSYTgdVILLDGSRTI---LSLPLDENDEGNPET 1193
Cdd:PLN02246 97 RRGAVTTTANPFYTPAEIAKQAKASGAKLIITQscyvdklKGLAEDDGVT--VVTIDDPPEGclhFSELTQADENELPEV 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1194 AVTAENLAYMIYTSGTTGQPKGVMVEHHALV------------NLCFWHHDA----------FSMTaedrsakyagfgfd 1251
Cdd:PLN02246 175 EISPDDVVALPYSSGTTGLPKGVMLTHKGLVtsvaqqvdgenpNLYFHSDDVilcvlpmfhiYSLN-------------- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1252 aSIweMFPTWTIGAELHVIDeaiRLDIVRLNDYFETNGVTITFL--PTQLA-EQFMELEN---TSLRVLLTG----GDKL 1321
Cdd:PLN02246 241 -SV--LLCGLRVGAAILIMP---KFEIGALLELIQRHKVTIAPFvpPIVLAiAKSPVVEKydlSSIRMVLSGaaplGKEL 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1322 KRAV--KKP-YTLVNNYGPTE-NTVVATS---AEIHPEEGSLSIGRAIANTRVYILG-EGNQVQPEGVAGELCVAGRGLA 1393
Cdd:PLN02246 315 EDAFraKLPnAVLGQGYGMTEaGPVLAMClafAKEPFPVKSGSCGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIM 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1394 RGYLNREDETAKRFVADPFVpgermyRTGDlVKWVNGGIEY--IGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTA 1471
Cdd:PLN02246 395 KGYLNDPEATANTIDKDGWL------HTGD-IGYIDDDDELfiVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVP 467
|
...
gi 2214269206 1472 VKD 1474
Cdd:PLN02246 468 MKD 470
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
1075-1531 |
1.77e-17 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. 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.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 87.87 E-value: 1.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1075 GQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLL 1154
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1155 kqegisvpdsytgdVILLDgsrtilslPLDENDEGNPETAVTAE---NLAYmIYTSGTTGQPKGVMVEHHALVNLCFWHH 1231
Cdd:cd05939 81 --------------FNLLD--------PLLTQSSTEPPSQDDVNfrdKLFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAY 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1232 DAFSMTAEDRsakyagfgfdasIWEMFPTW-------TIG-AELHVIDEAIR---------LDIVRLNdyfetngVTIT- 1293
Cdd:cd05939 138 YAFGMRPEDV------------VYDCLPLYhsaggimGVGqALLHGSTVVIRkkfsasnfwDDCVKYN-------CTIVq 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1294 -------FLptqLAEQFMELENTSlRVLLTGGDKLKRAVKKPYTLVNN-------YGPTE---------NTVVATS---- 1346
Cdd:cd05939 199 yigeicrYL---LAQPPSEEEQKH-NVRLAVGNGLRPQIWEQFVRRFGipqigefYGATEgnsslvnidNHVGACGfnsr 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1347 --AEIHPeegsLSIGRAIANTRVYILGEGNQVQP--EGVAGELC---VAGRGLAR--GYLNrEDETAKRFVADPFVPGER 1417
Cdd:cd05939 275 ilPSVYP----IRLIKVDEDTGELIRDSDGLCIPcqPGEPGLLVgkiIQNDPLRRfdGYVN-EGATNKKIARDVFKKGDS 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1418 MYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKG--GNTAIAAYVTPE-TADIE 1493
Cdd:cd05939 350 AFLSGDVLVMDELGYLYFkDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGveGRAGMAAIVDPErKVDLD 429
|
490 500 510
....*....|....*....|....*....|....*...
gi 2214269206 1494 ALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05939 430 RFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1079-1531 |
4.09e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 86.75 E-value: 4.09e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1079 TYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGaklllkqeg 1158
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAE--------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1159 isvPDSYTGdvilldgsrtilsLPLdendegnpetavtAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTA 1238
Cdd:cd05910 75 ---PDAFIG-------------IPK-------------ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1239 EDRSakYAGF----------GFDASIWEMFPTWTIGAELHVIDEAIR---LDIV--------RLNDYFETNGVTitfLPt 1297
Cdd:cd05910 126 GEVD--LATFplfalfgpalGLTSVIPDMDPTRPARADPQKLVGAIRqygVSIVfgspalleRVARYCAQHGIT---LP- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1298 qlaeqfmelentSLRVLLTGG--------DKLKRAVKKPYTLVNNYGPTE---------NTVVATSAEIHPEEGSLSIGR 1360
Cdd:cd05910 200 ------------SLRRVLSAGapvpialaARLRKMLSDEAEILTPYGATEalpvssigsRELLATTTAATSGGAGTCVGR 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1361 AIANTRVYILG---------EGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADpfvPGERM-YRTGDLVKWVNG 1430
Cdd:cd05910 268 PIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDD---NSEGFwHRMGDLGYLDDE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1431 G-IEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAY------VTPETADIEALKSTLKETL 1503
Cdd:cd05910 345 GrLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVGKPGCQLPVLCVeplpgtITPRARLEQELRALAKDYP 424
|
490 500 510
....*....|....*....|....*....|
gi 2214269206 1504 PDYMIPAFwVTLNELPVTA--NGKVDRKAL 1531
Cdd:cd05910 425 HTQRIGRF-LIHPSFPVDIrhNAKIFREKL 453
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
149-501 |
4.96e-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: 85.22 E-value: 4.96e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 149 NLAYVIYTSGTTGKPKGVQIEHRNLTnYVSWFSEEAGLTENDKTVLLSSYAFDLG--YTSMFPVLLGGGELHIVQKETYT 226
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEV-YNAWMLALNSLFDPDDVLLCGLPLFHVNgsVVTLLTPLASGAHVVLAGPAGYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 227 AP---DEIAHYIKEHGITYIKLTPSLfhtIVNTASFAKDANFESLRLiVLGGEKIIPTDVIA-FRKMYGHTeFINHYGPT 302
Cdd:cd05944 82 NPglfDNFWKLVERYRITSLSTVPTV---YAALLQVPVNADISSLRF-AMSGAAPLPVELRArFEDATGLP-VVEGYGLT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 303 EATIGaiagrVDLYEPDAfAKRP-TIGRPIANAGALVLNE-----ALKLVPPGASGQLYITGQGLARGYL----NRPQLT 372
Cdd:cd05944 157 EATCL-----VAVNPPDG-PKRPgSVGLRLPYARVRIKVLdgvgrLLRDCAPDEVGEICVAGPGVFGGYLytegNKNAFV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 373 AERFVenpyspgslmyKTGDVVRRLSDGTLAFIGRADDQVkIRG-YRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQEL- 450
Cdd:cd05944 231 ADGWL-----------NTGDLGRLDADGYLFITGRAKDLI-IRGgHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELp 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 2214269206 451 CAYYTSDQD--IEKAELRYQLSLTLPSH-MIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd05944 299 VAYVQLKPGavVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
29-443 |
5.77e-17 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 86.58 E-value: 5.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 29 GGNLLTYRELDEQANQLAHHLRAQGAGNE-DIVAIVMDRSAEVMVSILGVMKAG--AAFLP------------------- 86
Cdd:cd05938 2 EGETYTYRDVDRRSNQAARALLAHAGLRPgDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNtnirsksllhcfrccgakv 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 87 --IDPDTPE--ERIRYSLEDSGAKFAVVNERNMTaigqyEGIIVSLDdgKWRNESKERP-----SSISGSRNLAYvIYTS 157
Cdd:cd05938 82 lvVAPELQEavEEVLPALRADGVSVWYLSHTSNT-----EGVISLLD--KVDAASDEPVpaslrAHVTIKSPALY-IYTS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 158 GTTGKPKGVQIEHRNLTnYVSWFSEEAGLTENDKTVLlssyAFDLGYTSMFpvLLG-GGELHI----VQKETYTAP---D 229
Cdd:cd05938 154 GTTGLPKAARISHLRVL-QCSGFLSLCGVTADDVIYI----TLPLYHSSGF--LLGiGGCIELgatcVLKPKFSASqfwD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 230 EiahyIKEHGITYIKLTPSLFHTIVNTASFAKDANfESLRLIVLGGekiIPTDV----------IAFRKMYGHTE----F 295
Cdd:cd05938 227 D----CRKHNVTVIQYIGELLRYLCNQPQSPNDRD-HKVRLAIGNG---LRADVwreflrrfgpIRIREFYGSTEgnigF 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 296 INHYGpteaTIGAIaGRVD----LYEPDAFAK-RPTIGRPIANAGALVLNealklVPPGASGQLY--ITGQGLARGYLNR 368
Cdd:cd05938 299 FNYTG----KIGAV-GRVSylykLLFPFELIKfDVEKEEPVRDAQGFCIP-----VAKGEPGLLVakITQQSPFLGYAGD 368
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 369 PQLTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVS 443
Cdd:cd05938 369 KEQTEKKLLRDVFKKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGVT 443
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1062-1531 |
6.78e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 86.28 E-value: 6.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1062 VQRHKDRPAVTY--NGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQ 1139
Cdd:PRK13391 7 AQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1140 RIEYILQDSGAKLLlkqegisVPDSYTGDV--------------ILLDGSRTILSL-PLDENDEGNPETAVTAENL-AYM 1203
Cdd:PRK13391 87 EAAYIVDDSGARAL-------ITSAAKLDVarallkqcpgvrhrLVLDGDGELEGFvGYAEAVAGLPATPIADESLgTDM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1204 IYTSGTTGQPKGVMVE--HHALV---NLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDeaiRLDI 1278
Cdd:PRK13391 160 LYSSGTTGRPKGIKRPlpEQPPDtplPLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVME---HFDA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1279 VRLNDYFETNGVTIT-FLPTQL-------AEQFMELENTSLRVLLTGGDKLKRAVKKpyTLVNNYGP--------TEN-- 1340
Cdd:PRK13391 237 EQYLALIEEYGVTHTqLVPTMFsrmlklpEEVRDKYDLSSLEVAIHAAAPCPPQVKE--QMIDWWGPiiheyyaaTEGlg 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1341 TVVATSAE--IHPEegslSIGRAIANTrVYILGEGNQVQPEGVAGELCVAGrGLARGYLNREDETAKRFVADPfvpgeRM 1418
Cdd:PRK13391 315 FTACDSEEwlAHPG----TVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG-----TW 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1419 YRTGDlVKWVNGGiEYIGRIDQQVKV---RGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTP-----ETA 1490
Cdd:PRK13391 384 STVGD-IGYVDED-GYLYLTDRAAFMiisGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQPvdgvdPGP 461
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 2214269206 1491 DIEA-LKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK13391 462 ALAAeLIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1046-1531 |
6.84e-17 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 86.43 E-value: 6.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1046 LPVPTD---KTVHQLFeeTVQRHKDRPAVT--YNGQSWTYGELNAKANRLARILMDC-GISPDDRVGVLTKPSLEMSAAV 1119
Cdd:PLN02574 32 VPLPSDpnlDAVSFIF--SHHNHNGDTALIdsSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIF 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1120 LGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLL------------LKQEGISVPDSYTGDVILLDGSrTILSLPLDEND 1187
Cdd:PLN02574 110 LAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAftspenveklspLGVPVIGVPENYDFDSKRIEFP-KFYELIKEDFD 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1188 EGnPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLC--FWHHDAfsmtaedrsAKYAGFGFDASIWEMFPTWTI-- 1263
Cdd:PLN02574 189 FV-PKPVIKQDDVAAIMYSSGTTGASKGVVLTHRNLIAMVelFVRFEA---------SQYEYPGSDNVYLAALPMFHIyg 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1264 -----------GAELHVIDEAIRLDIVRLNDYFEtngvtITFLPTqLAEQFMELENT----------SLRVLLTGGDKLK 1322
Cdd:PLN02574 259 lslfvvgllslGSTIVVMRRFDASDMVKVIDRFK-----VTHFPV-VPPILMALTKKakgvcgevlkSLKQVSCGAAPLS 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1323 RAVKKPYT-------LVNNYGPTENTVVATSAeIHPEEGS--LSIGRAIANTRVYILG-EGNQVQPEGVAGELCVAGRGL 1392
Cdd:PLN02574 333 GKFIQDFVqtlphvdFIQGYGMTESTAVGTRG-FNTEKLSkySSVGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGV 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1393 ARGYLNREDETAKRFVADPFVpgermyRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTA 1471
Cdd:PLN02574 412 MKGYLNNPKATQSTIDKDGWL------RTGDIAYFDEDGYLYIvDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTA 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 1472 VKDKGGNTAIAAYVT--PETA-DIEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PLN02574 486 VPDKECGEIPVAFVVrrQGSTlSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
153-497 |
8.73e-17 |
|
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: 83.89 E-value: 8.73e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 153 VIYTSGTTGKPKGVQIEHRNLTnYVSWFSEEAGLTENDKTVLLSSYAFDLGyTSMF--PVLLGGGELHIVQKetyTAPDE 230
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALL-AQALVLAVLQAIDEGTVFLNSGPLFHIG-TLMFtlATFHAGGTNVFVRR---VDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 231 IAHYIKEHGITYIKLTPSLFHTIVNtASFAKDANFESLRLIVL--GGEKIIPTDVIAF-RKMYGhtefinhYGPTE---- 303
Cdd:cd17636 80 VLELIEAERCTHAFLLPPTIDQIVE-LNADGLYDLSSLRSSPAapEWNDMATVDTSPWgRKPGG-------YGQTEvmgl 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 304 ATIGAIAGRvdlyepdafaKRPTIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVenpysp 383
Cdd:cd17636 152 ATFAALGGG----------AIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 384 gSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV-SEGGLQELCAYYT--SDQDI 460
Cdd:cd17636 216 -GGWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVpDPRWAQSVKAIVVlkPGASV 294
|
330 340 350
....*....|....*....|....*....|....*..
gi 2214269206 461 EKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTD 497
Cdd:cd17636 295 TEAELIEHCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1171-1531 |
1.25e-16 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 83.94 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1171 LLDGSRTILsLPLDENDEGNPETAVTA--------ENLAYMIYTSGTTGQPKGVMVEHHALVNlcfwhhdafsmTAEdrs 1242
Cdd:PRK07824 1 ALAGRAPAL-LPVPAQDERRAALLRDAlrvgepidDDVALVVATSGTTGTPKGAMLTAAALTA-----------SAD--- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1243 AKYAGFGFDASIWEMFPTWTIgAELHVI-------DEAIRLDI---------VRLNDYFETNGVTITFLPTQLAEQFMEL 1306
Cdd:PRK07824 66 ATHDRLGGPGQWLLALPAHHI-AGLQVLvrsviagSEPVELDVsagfdptalPRAVAELGGGRRYTSLVPMQLAKALDDP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1307 ENT-SLR----VLLTGG----DKLKRAVKKPYTLVNNYGPTEntvvaTSAeihpeeGSLSIGRAIANTRVYILGegnqvq 1377
Cdd:PRK07824 145 AATaALAeldaVLVGGGpapaPVLDAAAAAGINVVRTYGMSE-----TSG------GCVYDGVPLDGVRVRVED------ 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1378 pegvaGELCVAGRGLARGYLNREDEtakrfvaDPFV-PGerMYRTGDLVKWVNGGIEYIGRIDQQVKVRGYRIELSEIEV 1456
Cdd:PRK07824 208 -----GRIALGGPTLAKGYRNPVDP-------DPFAePG--WFRTDDLGALDDGVLTVLGRADDAISTGGLTVLPQVVEA 273
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 1457 QLAQLSEVQDAAVTAVKD-KGGNTAIAAYV-TPETAD-IEALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK07824 274 ALATHPAVADCAVFGLPDdRLGQRVVAAVVgDGGPAPtLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
17-501 |
1.49e-16 |
|
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: 85.12 E-value: 1.49e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 17 AQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERI 96
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 97 RYSLEDSGAkFAVVnernmtaigqyegIIVSLDDGKWRNESKERPSS------ISGSRNLAYVIYTSGTTGKPKGVQIEH 170
Cdd:cd05929 82 CAIIEIKAA-ALVC-------------GLFTGGGALDGLEDYEAAEGgspetpIEDEAAGWKMLYSGGTTGRPKGIKRGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 171 rnltnyvswfseEAGLTENDKTV---LLSSYAFDLGYTSMFP------------VLLGGGELHIVQKetyTAPDEIAHYI 235
Cdd:cd05929 148 ------------PGGPPDNDTLMaaaLGFGPGADSVYLSPAPlyhaapfrwsmtALFMGGTLVLMEK---FDPEEFLRLI 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 236 KEHGITYIKLTPSLFHTIVNTASFAKDA-NFESLR----------------LIVLGGEKIIptdviafrkmyghtEFinh 298
Cdd:cd05929 213 ERYRVTFAQFVPTMFVRLLKLPEAVRNAyDLSSLKrvihaaapcppwvkeqWIDWGGPIIW--------------EY--- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 299 YGPTEAtIG--AIAGRvdlyepDAFAKRPTIGRPIAnAGALVLNEALKLVPPGASGQLYITGqGLARGYLNRPQLTAERF 376
Cdd:cd05929 276 YGGTEG-QGltIINGE------EWLTHPGSVGRAVL-GKVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAAR 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 377 VENPYSpgSLmyktGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGL-QELCAYY- 454
Cdd:cd05929 347 NEGGWS--TL----GDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELgQRVHAVVq 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 455 ----TSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:cd05929 421 papgADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
17-442 |
1.69e-16 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 84.54 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 17 AQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERI 96
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 97 RYSLEDSGAKFAVVNERNMTAIGqyegiivsLDDGKWRNESKERPSSISGSRnLAYVIYTSGTTGKPKGVQIEHRN-LTN 175
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENTFSA--------LTSLHLQLVEGAHAVAWQPQR-LATMTLTSGSTGLPKAAVHTAQAhLAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 176 ---YVSWFSeeagLTENDkTVLLSsyafdlgyTSMFPV---------LLGGGELHIVQKEtytapdEIAHYIkeHGITYI 243
Cdd:PRK09029 164 aegVLSLMP----FTAQD-SWLLS--------LPLFHVsgqgivwrwLYAGATLVVRDKQ------PLEQAL--AGCTHA 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 244 KLTPSLFHTIvntasFAKDANFESLRLIVLGGEKIIPTDVIAFRKM-------YGHTEFinhygpteatigaiAGRVdly 316
Cdd:PRK09029 223 SLVPTQLWRL-----LDNRSEPLSLKAVLLGGAAIPVELTEQAEQQgircwcgYGLTEM--------------ASTV--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 317 epdaFAKRPTiGRPiaNAGALVLNEALKLVppgaSGQLYITGQGLARGYLNRPQLTaerfvenPYSPGSLMYKTGDvvR- 395
Cdd:PRK09029 281 ----CAKRAD-GLA--GVGSPLPGREVKLV----DGEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRD--Rg 340
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 2214269206 396 RLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV 442
Cdd:PRK09029 341 EWQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPV 387
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
1062-1531 |
2.05e-16 |
|
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: 85.38 E-value: 2.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1062 VQRHKDRPAVTYNGQS------WTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAA----FVP 1131
Cdd:TIGR02188 67 LEARPDKVAIIWEGDEpgevrkITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIhsvvFGG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1132 IDPDYPDQRIeyilQDSGAKLL----------------------LKQEGISVPD----SYTG-DVILLDGSRTI--LSLP 1182
Cdd:TIGR02188 147 FSAEALADRI----NDAGAKLVitadeglrggkviplkaivdeaLEKCPVSVEHvlvvRRTGnPVVPWVEGRDVwwHDLM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1183 LDENDEGNPEtAVTAENLAYMIYTSGTTGQPKGVMvehHA----LVNLCFWHHDAFSMTAEDRsakyagFGFDASI-W-- 1255
Cdd:TIGR02188 223 AKASAYCEPE-PMDSEDPLFILYTSGSTGKPKGVL---HTtggyLLYAAMTMKYVFDIKDGDI------FWCTADVgWit 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1256 ----------------EMF---PTWTigaelhvideairlDIVRLNDYFETNGVTITFL-PTQLaEQFMELEN------- 1308
Cdd:TIGR02188 293 ghsyivygplangattVMFegvPTYP--------------DPGRFWEIIEKHKVTIFYTaPTAI-RALMRLGDewvkkhd 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1309 -TSLRVLLTGGDKLKRAVKKPYTlvNNYGPTENTVVAT-------SAEIHPEEGSL-----SIGRAIANTRVYIL-GEGN 1374
Cdd:TIGR02188 358 lSSLRLLGSVGEPINPEAWMWYY--KVVGKERCPIVDTwwqtetgGIMITPLPGATptkpgSATLPFFGIEPAVVdEEGN 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1375 QVQPEGVAGELCVAGR--GLARGYLNREDetakRFVADPFVPGERMYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIEL 1451
Cdd:TIGR02188 436 PVEGPGEGGYLVIKQPwpGMLRTIYGDHE----RFVDTYFSPFPGYYFTGDGARRDKDGYIWItGRVDDVINVSGHRLGT 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1452 SEIEVQLAQLSEVQDAAVTAVKD--KGgnTAIAAYVT-----PETADIEA-LKSTLKETLPDYMIPA--FWVtlNELPVT 1521
Cdd:TIGR02188 512 AEIESALVSHPAVAEAAVVGIPDdiKG--QAIYAFVTlkdgyEPDDELRKeLRKHVRKEIGPIAKPDkiRFV--PGLPKT 587
|
570
....*....|
gi 2214269206 1522 ANGKVDRKAL 1531
Cdd:TIGR02188 588 RSGKIMRRLL 597
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
33-413 |
3.43e-16 |
|
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: 84.19 E-value: 3.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGaafLPIDP--DT-PEERIRYSLEDSGAkfav 109
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTvyATlGEDALIHSLNETEC---- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 110 vnernmtaigqyEGIIVSlddgkwrneskerpssiSGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTEN 189
Cdd:cd17639 79 ------------SAIFTD-----------------GKPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 190 DKTVLLS----SYAFDLGYTSMFpvLLGGGELHIVQKETYTapDEIahYIKEHG-ITYIKLT-----PSLFHTI------ 253
Cdd:cd17639 130 PDDRYLAylplAHIFELAAENVC--LYRGGTIGYGSPRTLT--DKS--KRGCKGdLTEFKPTlmvgvPAIWDTIrkgvla 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 254 -VNTASFAKDANFES-----LRLIVLGGEKIIpTDVIAFRK----MYGHT---------------EFIN--------HYG 300
Cdd:cd17639 204 kLNPMGGLKRTLFWTayqskLKALKEGPGTPL-LDELVFKKvraaLGGRLrymlsggaplsadtqEFLNivlcpviqGYG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 301 PTEATIGAIAGRVDLYEPDafakrpTIGRPIANAGALVLN-EALKLVP--PGASGQLYITGQGLARGYLNRPQLTAERFV 377
Cdd:cd17639 283 LTETCAGGTVQDPGDLETG------RVGPPLPCCEIKLVDwEEGGYSTdkPPPRGEILIRGPNVFKGYYKNPEKTKEAFD 356
|
410 420 430
....*....|....*....|....*....|....*.
gi 2214269206 378 ENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVK 413
Cdd:cd17639 357 GDGW------FHTGDIGEFHPDGTLKIIDRKKDLVK 386
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1634-2058 |
4.97e-16 |
|
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: 83.02 E-value: 4.97e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1634 LTPIQRWF-FE--KNFTNKHHWNQSVMlHAKKGFDPERVEKTLQALIEHHDALRMVYREENGDI-VQVYkpIGESKVSFE 1709
Cdd:cd19543 4 LSPMQEGMlFHslLDPGSGAYVEQMVI-TLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEpLQVV--LKDRKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1710 IVDLYGSDEEMLRSQIK-LLANKLQSSLDLRNGPLLKAEQYRTEAGDH-LLIAVHHLVVDGVSWRILLEDFASGYmQAEK 1787
Cdd:cd19543 81 ELDLSHLSEAEQEAELEaLAEEDRERGFDLARAPLMRLTLIRLGDDRYrLVWSFHHILLDGWSLPILLKELFAIY-AALG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1788 EESLVFPQKTNSFKDWAEELAAFSQSAHLlqqaEYWS-QIAA-EQVSPLPKDCETEQRIVKDTSSVLCELTAEDTKHLLT 1865
Cdd:cd19543 160 EGQPPSLPPVRPYRDYIAWLQRQDKEAAE----AYWReYLAGfEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQE 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1866 DVHQpYGTEINDILLSALGLTMkewtkgAKIGinleghGREDIIPNVNIS----------RTVGWFTAQYPVVLDIsDAD 1935
Cdd:cd19543 236 LARQ-HGVTLNTVVQGAWALLL------SRYS------GRDDVVFGTTVSgrpaelpgieTMVGLFINTLPVRVRL-DPD 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1936 AsavikTVKENLRRIPDKGVgygilryfteTAETKGFTP--EI-SFNYLGQ--FDS----------EVKTDFFEPSAFDM 2000
Cdd:cd19543 302 Q-----TVLELLKDLQAQQL----------ELREHEYVPlyEIqAWSEGKQalFDHllvfenypvdESLEEEQDEDGLRI 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 2001 gRQVSGESEALYALSFSGMiRNGRFVLSCSYNEKEFERATVEEQMERFKENLLMLIRH 2058
Cdd:cd19543 367 -TDVSAEEQTNYPLTVVAI-PGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1063-1531 |
7.21e-16 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 82.61 E-value: 7.21e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1063 QRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIE 1142
Cdd:PRK09029 14 QVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1143 YILQdsgaklllkqegisvpdSYTGDVIL-LDGSRTILSLPLDENDEGNPETAVT--AENLAYMIYTSGTTGQPKGVMVE 1219
Cdd:PRK09029 94 ELLP-----------------SLTLDFALvLEGENTFSALTSLHLQLVEGAHAVAwqPQRLATMTLTSGSTGLPKAAVHT 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1220 HHA-LVN---LCfwhhDAFSMTAEDR----------SakyaGFGFdasIWEmfptW-TIGAELHVIDEAirldivrlnDY 1284
Cdd:PRK09029 157 AQAhLASaegVL----SLMPFTAQDSwllslplfhvS----GQGI---VWR----WlYAGATLVVRDKQ---------PL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1285 FET-NGVTITFL-PTQLAEQFMELEN-TSLRVLLTGGDKLkravkkPYTLVNN-----------YGPTE--NTVVATSAE 1348
Cdd:PRK09029 213 EQAlAGCTHASLvPTQLWRLLDNRSEpLSLKAVLLGGAAI------PVELTEQaeqqgircwcgYGLTEmaSTVCAKRAD 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1349 IHPEEGSLSIGRAIantRVyilgegnqvqpegVAGELCVAGRGLARGYLnREDETAkrfvadPFVPGERMYRTGDLVKWV 1428
Cdd:PRK09029 287 GLAGVGSPLPGREV---KL-------------VDGEIWLRGASLALGYW-RQGQLV------PLVNDEGWFATRDRGEWQ 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1429 NGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKG-GNTAIAAYVTPETADIEALKSTLKETLPDYM 1507
Cdd:PRK09029 344 NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEfGQRPVAVVESDSEAAVVNLAEWLQDKLARFQ 423
|
490 500
....*....|....*....|....*.
gi 2214269206 1508 IPAFWVTLNElpVTANG--KVDRKAL 1531
Cdd:PRK09029 424 QPVAYYLLPP--ELKNGgiKISRQAL 447
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1063-1424 |
1.06e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 82.64 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1063 QRHKDRPAV----------TYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPI 1132
Cdd:PRK09274 17 QERPDQLAVavpggrgadgKLAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1133 DPDYPDQRIEYILQDSGAKLLlkqegISVPDSYTGDVILLDGSRTILSL----------------PLDENDEGNPETAVT 1196
Cdd:PRK09274 97 DPGMGIKNLKQCLAEAQPDAF-----IGIPKAHLARRLFGWGKPSVRRLvtvggrllwggttlatLLRDGAAAPFPMADL 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1197 AEN-LAYMIYTSGTTGQPKGVMVEH-------HALvnlcfwhHDAFSMTAEDRSakYAGF----------GFDASIWEMF 1258
Cdd:PRK09274 172 APDdMAAILFTSGSTGTPKGVVYTHgmfeaqiEAL-------REDYGIEPGEID--LPTFplfalfgpalGMTSVIPDMD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1259 PTWTIGAELHVIDEAIRLD-----------IVRLNDYFETNGVTitfLPtqlaeqfmelentSLRVLLTGG--------D 1319
Cdd:PRK09274 243 PTRPATVDPAKLFAAIERYgvtnlfgspalLERLGRYGEANGIK---LP-------------SLRRVISAGapvpiaviE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1320 KLKRAVKKPYTLVNNYGPTENTVVAT--SAEIHPEEGSLS-------IGRAIANTRVYILG---------EGNQVQPEGV 1381
Cdd:PRK09274 307 RFRAMLPPDAEILTPYGATEALPISSieSREILFATRAATdngagicVGRPVDGVEVRIIAisdapipewDDALRLATGE 386
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 2214269206 1382 AGELCVAGRGLARGYLNREDETAKRFVADPfvPGERMYRTGDL 1424
Cdd:PRK09274 387 IGEIVVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDL 427
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
516-589 |
1.51e-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: 73.35 E-value: 1.51e-15
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214269206 516 APETALEESLCRIWQKTLGI--EAIGIDDNFF-DLGGHSLKGMMLIANIQAELEKSVPLKALFEQPTVRQLAAYMEA 589
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
151-497 |
2.10e-15 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 82.71 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 151 AYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDK--TVLLSSYAFDLGYTSMFPVLLGggelhiVQKETYTAP 228
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKvfNALPVFHSFGLTGGLVLPLLSG------VKVFLYPSP 869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 229 deiAHY--IKEhgITYIKLTPSLFHTIVNTASFAKDAN---FESLRLIVLGGEKIIPTDVIAFRKMYGHTEFiNHYGPTE 303
Cdd:PRK06814 870 ---LHYriIPE--LIYDTNATILFGTDTFLNGYARYAHpydFRSLRYVFAGAEKVKEETRQTWMEKFGIRIL-EGYGVTE 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 304 ATIGaIAgrvdLYEPdAFAKRPTIGRpianagALVLNEAlKLVP-PGAS--GQLYITGQGLARGYLNrpqltaerfVENP 380
Cdd:PRK06814 944 TAPV-IA----LNTP-MHNKAGTVGR------LLPGIEY-RLEPvPGIDegGRLFVRGPNVMLGYLR---------AENP 1001
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 381 YS---PGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYriepkeietvMLSLSGIQEA----------VVLAVSEGGL 447
Cdd:PRK06814 1002 GVlepPADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGE----------MISLAAVEELaaelwpdalhAAVSIPDARK 1071
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 448 QELCAYYTSDQDIEKAE-LRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTD 497
Cdd:PRK06814 1072 GERIILLTTASDATRAAfLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1061-1531 |
2.33e-15 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 81.57 E-value: 2.33e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1061 TVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAfvPIDPDYPDQR 1140
Cdd:PRK10946 32 TRHAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1141 IE---YILQ--------DSGAKLL--------LKQEGISVpdsytgDVILLDGSRTILSLP--LDENDEGNPETAVTAEN 1199
Cdd:PRK10946 110 SElnaYASQiepalliaDRQHALFsdddflntLVAEHSSL------RVVLLLNDDGEHSLDdaINHPAEDFTATPSPADE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1200 LAYMIYTSGTTGQPKGVMVEHH-------ALVNLCfwhhdafSMTAEDR-------------------SAKYAG----FG 1249
Cdd:PRK10946 184 VAFFQLSGGSTGTPKLIPRTHNdyyysvrRSVEIC-------GFTPQTRylcalpaahnypmsspgalGVFLAGgtvvLA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1250 FDASIWEMFPtwtigaelhvIDEAIRLDIVRLndyfETNGVTITFLPTQLAEQFMELEntSLRVLLTGGDKLKRAVKKPY 1329
Cdd:PRK10946 257 PDPSATLCFP----------LIEKHQVNVTAL----VPPAVSLWLQAIAEGGSRAQLA--SLKLLQVGGARLSETLARRI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1330 T------LVNNYGPTENTVVATSAEIHPEEGSLSIGRAIA-NTRVYILGE-GNQVqPEGVAGELCVAGRGLARGYLNRED 1401
Cdd:PRK10946 321 PaelgcqLQQVFGMAEGLVNYTRLDDSDERIFTTQGRPMSpDDEVWVADAdGNPL-PQGEVGRLMTRGPYTFRGYYKSPQ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1402 ETAKRFVADPFvpgermYRTGDLVKWVNGG-IEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKG-GNT 1479
Cdd:PRK10946 400 HNASAFDANGF------YCSGDLVSIDPDGyITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELmGEK 473
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 1480 AIAAYVTPETADIEALKSTLKET-LPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK10946 474 SCAFLVVKEPLKAVQLRRFLREQgIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
7-469 |
2.55e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 81.48 E-value: 2.55e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 7 ATFAALFEKQAQQTPDHSAVKAGGNL----------LTYRELDEQANQLAHHLRAQGAGNEDiVAIVMDR-SAEVMVSIL 75
Cdd:PRK09274 6 ANIARHLPRAAQERPDQLAVAVPGGRgadgklaydeLSFAELDARSDAIAHGLNAAGIGRGM-RAVLMVTpSLEFFALTF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 76 GVMKAGAAFLPIDPDTPEERIRYSLEDSGAKfavvnernmTAIGQYEGII---------------VSLDDGK-WRNESKE 139
Cdd:PRK09274 85 ALFKAGAVPVLVDPGMGIKNLKQCLAEAQPD---------AFIGIPKAHLarrlfgwgkpsvrrlVTVGGRLlWGGTTLA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 140 RPSSISGSRN----------LAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDktvllssyaFDLgytSMFP 209
Cdd:PRK09274 156 TLLRDGAAAPfpmadlapddMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGE---------IDL---PTFP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 210 VL------LGGGElhIV-----QKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNtASFAKDANFESLRLIVLGGEKI 278
Cdd:PRK09274 224 LFalfgpaLGMTS--VIpdmdpTRPATVDPAKLFAAIERYGVTNLFGSPALLERLGR-YGEANGIKLPSLRRVISAGAPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 279 iPTDVIA-FRKMYGH-TEFINHYGPTEAT-IGAIAGRVDLYEPDAFAKR---PTIGRPIAnaGALV------------LN 340
Cdd:PRK09274 301 -PIAVIErFRAMLPPdAEILTPYGATEALpISSIESREILFATRAATDNgagICVGRPVD--GVEVriiaisdapipeWD 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 341 EALKLvPPGASGQLYITGQGLARGYLNRPQLTAERFVENPysPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIE 420
Cdd:PRK09274 378 DALRL-ATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLY 454
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 421 PKEIETVMLSLSGIQEAVVLAVSEGGLQE--LCAYYTSDQDIEKAELRYQL 469
Cdd:PRK09274 455 TIPCERIFNTHPGVKRSALVGVGVPGAQRpvLCVELEPGVACSKSALYQEL 505
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
34-441 |
3.26e-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: 81.00 E-value: 3.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRysledsgAKFAVVNer 113
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEHKL-------KLNKVWN-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 114 nmTAIGQYegiiVSLDDGKWRnESKERpssisgsrnLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTV 193
Cdd:cd05908 88 --TLKNPY----LITEEEVLC-ELADE---------LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 194 LLSSYAFDLGYTS--MFPVLLGGGELHIVQKETYTAPDEIAHYIKEHGITYIKlTPS----LFHTIVNTASfAKDANFES 267
Cdd:cd05908 152 SWMPLTHDMGLIAfhLAPLIAGMNQYLMPTRLFIRRPILWLKKASEHKATIVS-SPNfgykYFLKTLKPEK-ANDWDLSS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 268 LRLIVLGGEKIIP------TDVIAFRKMyGHTEFINHYGPTEATIGAIAGRVDLY----------------EPDAFAKRP 325
Cdd:cd05908 230 IRMILNGAEPIDYelchefLDHMSKYGL-KRNAILPVYGLAEASVGASLPKAQSPfktitlgrrhvthgepEPEVDKKDS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 326 ------TIGRPIANAGALVLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDvVRRLSD 399
Cdd:cd05908 309 ecltfvEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW------LKTGD-LGFIRN 381
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 2214269206 400 GTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLA 441
Cdd:cd05908 382 GRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVA 423
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
31-440 |
3.56e-15 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 81.32 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 31 NLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVV 110
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 111 -------------------------NERNMTaiGQYEGIIVSLDD--GKWRNESKERP-------SSISGSrNLAYVIYT 156
Cdd:cd17641 90 edeeqvdklleiadripsvryviycDPRGMR--KYDDPRLISFEDvvALGRALDRRDPglyerevAAGKGE-DVAVLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 157 SGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKtvllssyafdlgYTSMFPV-------------LLGGGELHIVQKE 223
Cdd:cd17641 167 SGTTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDE------------YVSVLPLpwigeqmysvgqaLVCGFIVNFPEEP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 224 TYTAPDeiahyIKEHGITYIKLTPSLFHTIV------------------------------------------NTASFAK 261
Cdd:cd17641 235 ETMMED-----LREIGPTFVLLPPRVWEGIAadvrarmmdatpfkrfmfelgmklglraldrgkrgrpvslwlRLASWLA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 262 DA----------NFESLRLIVLGGEKIIPtDVIAF--------RKMYGHTEFINHYgpteaTIGAiAGRVDlyePDafak 323
Cdd:cd17641 310 DAllfrplrdrlGFSRLRSAATGGAALGP-DTFRFfhaigvplKQLYGQTELAGAY-----TVHR-DGDVD---PD---- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 324 rpTIGRPIANAGALVLNEalklvppgasGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLA 403
Cdd:cd17641 376 --TVGVPFPGTEVRIDEV----------GEILVRSPGVFVGYYKNPEATAEDFDEDGW------LHTGDAGYFKENGHLV 437
|
490 500 510
....*....|....*....|....*....|....*...
gi 2214269206 404 FIGRADDQVKI-RGYRIEPKEIETVMLSLSGIQEAVVL 440
Cdd:cd17641 438 VIDRAKDVGTTsDGTRFSPQFIENKLKFSPYIAEAVVL 475
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1634-1885 |
4.87e-15 |
|
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: 79.72 E-value: 4.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1634 LTPIQR--WFFEKNFTNKHHWNQSVMLHAKKGFDPERVEKTLQALIEHHDALRMVYREENGDIVQVYKPigESKVSFEIV 1711
Cdd:cd19533 4 LTSAQRgvWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDP--YTPVPIRHI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1712 DLygSDEEMLRSQIK-LLANKLQSSLDLRNGPLLKAEQYRTEAGDHLLIA-VHHLVVDGVSWRILLEDFASGYmQAEKEE 1789
Cdd:cd19533 82 DL--SGDPDPEGAAQqWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQrVHHIVMDGFSFALFGQRVAEIY-TALLKG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1790 SLVFPQKTNSFKDWAEELAAFSQSAHLLQQAEYWsqiaAEQVSPLPKDCETEQRIVKDTSSVLC---ELTAEDTKHLLTD 1866
Cdd:cd19533 159 RPAPPAPFGSFLDLVEEEQAYRQSERFERDRAFW----TEQFEDLPEPVSLARRAPGRSLAFLRrtaELPPELTRTLLEA 234
|
250
....*....|....*....
gi 2214269206 1867 VhQPYGTEINDILLSALGL 1885
Cdd:cd19533 235 A-EAHGASWPSFFIALVAA 252
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
33-196 |
6.27e-15 |
|
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: 80.21 E-value: 6.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVV-- 110
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 111 -NERNMTAIGQYEGIIVSL--------DDGKWRNESKERPSSIS----GSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYV 177
Cdd:cd05932 87 lDDWKAMAPGVPEGLISISlpppsaanCQYQWDDLIAQHPPLEErptrFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAA 166
|
170
....*....|....*....
gi 2214269206 178 SWFSEEAGLTENDKtvLLS 196
Cdd:cd05932 167 QAGIEHIGTEENDR--MLS 183
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
26-425 |
1.02e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 79.77 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 26 VKAGGNLLTYRELDEQAN-----------QLAHHLRAQGA------GNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPI- 87
Cdd:PRK07769 31 AKVRGDKLAYRFLDFSTErdgvardltwsQFGARNRAVGArlqqvtKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLf 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 88 DPDTP--EERIRYSLEDsgAKFAVVnernMTAIGQYEGIivslddgkwRN-----ESKERPSSIS--------GSR---- 148
Cdd:PRK07769 111 DPAEPghVGRLHAVLDD--CTPSAI----LTTTDSAEGV---------RKffrarPAKERPRVIAvdavpdevGATwvpp 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 149 -----NLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGY-TSMFPVLLGGgelHIvqk 222
Cdd:PRK07769 176 eanedTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLiTVLLPALLGH---YI--- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 223 eTYTAPdeiAHYIKEHGiTYIKLTPSLFHTIVNTASFAKDANFE-------------SLRL-----IVLGGEKIIPTDVI 284
Cdd:PRK07769 250 -TFMSP---AAFVRRPG-RWIRELARKPGGTGGTFSAAPNFAFEhaaarglpkdgepPLDLsnvkgLLNGSEPVSPASMR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 285 AFRKMYG-----HTEFINHYGPTEAT--IGAI-----------------AGR---VDLYEPDAFAKrPTIGRPIANAGAL 337
Cdd:PRK07769 325 KFNEAFApyglpPTAIKPSYGMAEATlfVSTTpmdeeptviyvdrdelnAGRfveVPADAPNAVAQ-VSAGKVGVSEWAV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 338 VLN-EALKLVPPGASGQLYITGQGLARGYLNRPQLTAERF---VENPYSP--------GSLMYKTGDVVRRLsDGTLAFI 405
Cdd:PRK07769 404 IVDpETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLSEshaegapdDALWVRTGDYGVYF-DGELYIT 482
|
490 500
....*....|....*....|
gi 2214269206 406 GRADDQVKIRGYRIEPKEIE 425
Cdd:PRK07769 483 GRVKDLVIIDGRNHYPQDLE 502
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
151-497 |
1.22e-14 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 79.75 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 151 AYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKtvLLSS----YAFDLGyTSMFPVLLGGGELHIvqketYT 226
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDR--FMSAlplfHSFGLT-VGLFTPLLTGAEVFL-----YP 439
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 227 APdeiAHYIKEHGITYIKLTPSLFHT---IVNTASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGhTEFINHYGPTE 303
Cdd:PRK08043 440 SP---LHYRIVPELVYDRNCTVLFGTstfLGNYARFANPYDFARLRYVVAGAEKLQESTKQLWQDKFG-LRILEGYGVTE 515
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 304 AtigaiAGRVDLYEPDAfAKRPTIGRPIANAGAlvlnealKLVP-PGAS--GQLYITGQGLARGYLNrpqltaerfVENP 380
Cdd:PRK08043 516 C-----APVVSINVPMA-AKPGTVGRILPGMDA-------RLLSvPGIEqgGRLQLKGPNIMNGYLR---------VEKP 573
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 381 Y---SP------GSL---MYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQ 448
Cdd:PRK08043 574 GvleVPtaenarGEMergWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKG 653
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 2214269206 449 ELCAYYTSDQDIEKAEL-RYQLSLTLPSHMIPAFFVQVDAIPLTANGKTD 497
Cdd:PRK08043 654 EALVLFTTDSELTREKLqQYAREHGVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
8-519 |
1.77e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 78.92 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 8 TFAALFEKQAQQtpDHSAVKAGGNLLTYRE-LDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLP 86
Cdd:PRK13388 4 TIAQLLRDRAGD--DTIAVRYGDRTWTWREvLAEAAARAAALIALADPDRPLHVGVLLGNTPEMLFWLAAAALGGYVLVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 87 IDP----DTPEERIRYSledsGAKFAVVNERNMtaiGQYEGI------IVSLDDGKWRN----ESKERPSSISGSRNLAY 152
Cdd:PRK13388 82 LNTtrrgAALAADIRRA----DCQLLVTDAEHR---PLLDGLdlpgvrVLDVDTPAYAElvaaAGALTPHREVDAMDPFM 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 153 VIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDktvllssyafdLGYTSM--F----------PVLLGGGElhIV 220
Cdd:PRK13388 155 LIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDD-----------VCYVSMplFhsnavmagwaPAVASGAA--VA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 221 QKETYTA----PDeiahyIKEHGITYIKLTPSLFHTIVNTASFAKDANfESLRlIVLGGEKIiPTDVIAFRKMYGhTEFI 296
Cdd:PRK13388 222 LPAKFSAsgflDD-----VRRYGATYFNYVGKPLAYILATPERPDDAD-NPLR-VAFGNEAS-PRDIAEFSRRFG-CQVE 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 297 NHYGPTEAtiGAIAGRVDLYEPDAFAkRPTIGRPIANAGAL------VLNEALKLV-PPGASGQLYIT-GQGLARGYLNR 368
Cdd:PRK13388 293 DGYGSSEG--AVIVVREPGTPPGSIG-RGAPGVAIYNPETLtecavaRFDAHGALLnADEAIGELVNTaGAGFFEGYYNN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 369 PQLTAERFVENpyspgslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSE--GG 446
Cdd:PRK13388 370 PEATAERMRHG-------MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDerVG 442
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 447 LQELCAYYTSD-QDIEKAELRYQLSLT--LPSHMIPAFFVQVDAIPLTANGKTDRNALpkpnaaQSGGKALAAPET 519
Cdd:PRK13388 443 DQVMAALVLRDgATFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKREL------IAQGWATGDPVT 512
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1057-1531 |
4.05e-14 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 77.74 E-value: 4.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1057 LFEETVQRHKDRPAVTY----NGQS-WTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVP 1131
Cdd:PRK05857 16 VLDRVFEQARQQPEAIAlrrcDGTSaLRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVM 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1132 IDPDYPDQRIEYILQDSGAKLLLKQEGISVPDSYTGDVILLDGSRTILSLPLDENDEGNPETAVTAENLAY-------MI 1204
Cdd:PRK05857 96 ADGNLPIAAIERFCQITDPAAALVAPGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASLAGNADQgsedplaMI 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1205 YTSGTTGQPKGVMvehhaLVNLCFWhhdAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVIDEAIR--------L 1276
Cdd:PRK05857 176 FTSGTTGEPKAVL-----LANRTFF---AVPDILQKEGLNWVTWVVGETTYSPLPATHIGGLWWILTCLMHgglcvtggE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1277 DIVRLNDYFETNGVTITFL-PTQLAEQFMELENT-----SLRVLLTGGdklKRAVKKPYTLVNN--------YGPTENTV 1342
Cdd:PRK05857 248 NTTSLLEILTTNAVATTCLvPTLLSKLVSELKSAnatvpSLRLVGYGG---SRAIAADVRFIEAtgvrtaqvYGLSETGC 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1343 VATSaeIHPEEGSLS------IGRAIANTRVYILGEGN------QVQPEGVAGELCVAGRGLARGYLNREDETaKRFVAD 1410
Cdd:PRK05857 325 TALC--LPTDDGSIVkieagaVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPERT-AEVLID 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1411 PFVpgermyRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPET 1489
Cdd:PRK05857 402 GWV------NTGDLLERREDGFFYIkGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLAVVASA 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1490 ADIEALKSTLKETLP--------DYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PRK05857 476 ELDESAARALKHTIAarfrresePMARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1545-1618 |
4.86e-14 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 69.11 E-value: 4.86e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 1545 APTTDMEELLAGIWQDVLGM--SEVGVTDNFFS-LGGDSIKGIQMASRLNQH-GWKLEMKDLFQHPTIEELTQYVERA 1618
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLEEK 78
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
13-504 |
9.25e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 76.60 E-value: 9.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 13 FEKQAQQT-PDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDT 91
Cdd:PLN03102 19 FLKRASECyPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 92 PEERIRYSLEDSGAK-------FAVVNERNMTAIGQYEG------IIVSLDDGKWRNESKE------------RPSS--- 143
Cdd:PLN03102 99 DATSIAAILRHAKPKilfvdrsFEPLAREVLHLLSSEDSnlnlpvIFIHEIDFPKRPSSEEldyecliqrgepTPSLvar 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 144 ---ISGSRNLAYVIYTSGTTGKPKGVQIEHRNLtnYVSWFSEEAGLTENDKTVLLSSYA-FDL-GYTSMFPVLLGGGElh 218
Cdd:PLN03102 179 mfrIQDEHDPISLNYTSGTTADPKGVVISHRGA--YLSTLSAIIGWEMGTCPVYLWTLPmFHCnGWTFTWGTAARGGT-- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 219 IVQKETYTAPdEIAHYIKEHGITYIKLTPSLFHTIVNTASFakDANFESLRLIVLGGEKIIPTDVI------AFRKMYGh 292
Cdd:PLN03102 255 SVCMRHVTAP-EIYKNIEMHNVTHMCCVPTVFNILLKGNSL--DLSPRSGPVHVLTGGSPPPAALVkkvqrlGFQVMHA- 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 293 tefinhYGPTEATiGAIA--------GRVDLYEPDAFAKRPTIgRPIANAGALVLN-EALKLVPPGAS--GQLYITGQGL 361
Cdd:PLN03102 331 ------YGLTEAT-GPVLfcewqdewNRLPENQQMELKARQGV-SILGLADVDVKNkETQESVPRDGKtmGEIVIKGSSI 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 362 ARGYLNRPQLTAERFVEnpyspGSLmyKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLA 441
Cdd:PLN03102 403 MKGYLKNPKATSEAFKH-----GWL--NTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVA 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 442 VSEGGLQEL-CAYYTSDQDIEKAELRYQLSLT------------LPSHMIPAFFVQVDAIPLTANGKtdrnaLPKP 504
Cdd:PLN03102 476 MPHPTWGETpCAFVVLEKGETTKEDRVDKLVTrerdlieycrenLPHFMCPRKVVFLQELPKNGNGK-----ILKP 546
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
1053-1548 |
1.44e-13 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 75.94 E-value: 1.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1053 TVHQLFEETVQRHKDRPAVTYNGQS----WTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAA 1128
Cdd:PRK06018 11 LCHRIIDHAARIHGNREVVTRSVEGpivrTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAI 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1129 FVPIDPD-YPDQrIEYILQDSGAKLLLKQ-------EGIS--VPdSYTGDVILLDGS---RTilSLP--------LDEND 1187
Cdd:PRK06018 91 CHTVNPRlFPEQ-IAWIINHAEDRVVITDltfvpilEKIAdkLP-SVERYVVLTDAAhmpQT--TLKnavayeewIAEAD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1188 eGNPETAVTAENLAY-MIYTSGTTGQPKGVMVEH-----HALVNLcfwHHDAFSMTAEDRSAKYAGFgFDASIWEM-FPT 1260
Cdd:PRK06018 167 -GDFAWKTFDENTAAgMCYTSGTTGDPKGVLYSHrsnvlHALMAN---NGDALGTSAADTMLPVVPL-FHANSWGIaFSA 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1261 WTIGAELhVIDEAiRLDIVRLNDYFETNGVTITF-LPT--QLAEQFMELENTS---LRVLLTGGDKLKRAVKKPYT---- 1330
Cdd:PRK06018 242 PSMGTKL-VMPGA-KLDGASVYELLDTEKVTFTAgVPTvwLMLLQYMEKEGLKlphLKMVVCGGSAMPRSMIKAFEdmgv 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1331 -LVNNYGPTENTVVATSAEIHPEEGSLSI----------GRAIANTRVYILG-EGNQVQPEGVA-GELCVAGRGLARGYL 1397
Cdd:PRK06018 320 eVRHAWGMTEMSPLGTLAALKPPFSKLPGdarldvlqkqGYPPFGVEMKITDdAGKELPWDGKTfGRLKVRGPAVAAAYY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1398 NREDETakrFVADPFvpgermYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAV-KDK 1475
Cdd:PRK06018 400 RVDGEI---LDDDGF------FDTGDVATIDAYGYMRItDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVyHPK 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1476 GGNTAIAAYVTPETadiealKSTLKETLPDYM---IPAFW-----VTLNELPVTANGKVDRKALPEPdieagSGEYKAPT 1547
Cdd:PRK06018 471 WDERPLLIVQLKPG------ETATREEILKYMdgkIAKWWmpddvAFVDAIPHTATGKILKTALREQ-----FKDYKLPT 539
|
.
gi 2214269206 1548 T 1548
Cdd:PRK06018 540 A 540
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1073-1531 |
1.45e-13 |
|
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: 75.55 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1073 YNGQSWTYGELNAKANRLARILMDC-GISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAK 1151
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1152 LLLkqegisvpdsytgdvilldgsrtilslpldendegnpetaVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHH 1231
Cdd:cd05937 81 FVI----------------------------------------VDPDDPAILIYTSGTTGLPKAAAISWRRTLVTSNLLS 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1232 DAFSMTAEDR----------SAKYAGF------GFDASIWEMFPTWTIGAELH--------VIDEAIR-LDIVRLNDYFE 1286
Cdd:cd05937 121 HDLNLKNGDRtytcmplyhgTAAFLGAcnclmsGGTLALSRKFSASQFWKDVRdsgatiiqYVGELCRyLLSTPPSPYDR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1287 TNGVTITF---LPTQLAEQFMELENTS----LRVLLTGGDKLKRAVKKPYTL--VNNYGPT-----ENTVVATsaEIHPE 1352
Cdd:cd05937 201 DHKVRVAWgngLRPDIWERFRERFNVPeigeFYAATEGVFALTNHNVGDFGAgaIGHHGLIrrwkfENQVVLV--KMDPE 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1353 EGSL----SIGRAIantrvyilgegnqVQPEGVAGELCVA----GRGLARGYLNREDETAKRFVADPFVPGERMYRTGDL 1424
Cdd:cd05937 279 TDDPirdpKTGFCV-------------RAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1425 VKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKG-----GNTAIA---AYVTPETADIEAL 1495
Cdd:cd05937 346 LRQdADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGhdgraGCAAITleeSSAVPTEFTKSLL 425
|
490 500 510
....*....|....*....|....*....|....*.
gi 2214269206 1496 KSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05937 426 ASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1076-1505 |
1.50e-13 |
|
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: 75.58 E-value: 1.50e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1076 QSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLK 1155
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1156 QEGISVPDSYTGdviLLDGSRTILSLPLDE--NDE--------GNPETAVT---AENLAYMIYTSGTTGQPKGVMVEHHA 1222
Cdd:cd05932 85 GKLDDWKAMAPG---VPEGLISISLPPPSAanCQYqwddliaqHPPLEERPtrfPEQLATLIYTSGTTGQPKGVMLTFGS 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1223 LVnlcfWHHDA----FSMTAEDRSAKYAG--------FGFDASIWEMFPTW------TIGAELHVIDEAIRLDIVRLNDY 1284
Cdd:cd05932 162 FA----WAAQAgiehIGTEENDRMLSYLPlahvtervFVEGGSLYGGVLVAfaesldTFVEDVQRARPTLFFSVPRLWTK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1285 FETNgvTITFLPTQLAEQFMELENTS---------------LRVLLTGGDKLKRAVKKPY-----TLVNNYGPTENtvVA 1344
Cdd:cd05932 238 FQQG--VQDKIPQQKLNLLLKIPVVNslvkrkvlkglgldqCRLAGCGSAPVPPALLEWYrslglNILEAYGMTEN--FA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1345 TSAEIHP---EEGslSIGRAIANTRVYIlgegnqvqpeGVAGELCVAGRGLARGYLNREDETAKRFVADPFVpgermyRT 1421
Cdd:cd05932 314 YSHLNYPgrdKIG--TVGNAGPGVEVRI----------SEDGEILVRSPALMMGYYKDPEATAEAFTADGFL------RT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1422 GDLVKW-VNGGIEYIGRIDQQVKV-RGYRIELSEIEVQLAQLSEVQDAAVTAvkdkGGNTAIAAYVTP--------ETAD 1491
Cdd:cd05932 376 GDKGELdADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIG----SGLPAPLALVVLseearlraDAFA 451
|
490
....*....|....
gi 2214269206 1492 IEALKSTLKETLPD 1505
Cdd:cd05932 452 RAELEASLRAHLAR 465
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
33-466 |
1.55e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 75.95 E-value: 1.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAA----FLPIDPDTPEERIryslEDSGAKFA 108
Cdd:PRK00174 99 ITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVhsvvFGGFSAEALADRI----IDAGAKLV 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 109 VvnernmTAIGQYEG----------------------IIV--------SLDDGK--W-----RNESKERPSSISGSRNLA 151
Cdd:PRK00174 175 I------TADEGVRGgkpiplkanvdealancpsvekVIVvrrtggdvDWVEGRdlWwhelvAGASDECEPEPMDAEDPL 248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 152 YVIYTSGTTGKPKGVQieHrnlTN--YVSWfseeAGLTENdktvllssYAFDL----------------GYTSMF--PVL 211
Cdd:PRK00174 249 FILYTSGSTGKPKGVL--H---TTggYLVY----AAMTMK--------YVFDYkdgdvywctadvgwvtGHSYIVygPLA 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 212 LGGGELHIVQKETYTAPDEIAHYIKEHGITyikltpsLFHTiVNTA--SFAKDA-------NFESLRLivLG--GEKIIP 280
Cdd:PRK00174 312 NGATTLMFEGVPNYPDPGRFWEVIDKHKVT-------IFYT-APTAirALMKEGdehpkkyDLSSLRL--LGsvGEPINP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 281 TdviAFRKMY-----GHTEFINHYGPTEAtiGAI-----AGRVDLyepdafaKRPTIGRPIANAGALVLNEALKLVPPGA 350
Cdd:PRK00174 382 E---AWEWYYkvvggERCPIVDTWWQTET--GGImitplPGATPL-------KPGSATRPLPGIQPAVVDEEGNPLEGGE 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 351 SGQLYITGQ--GLARGYLNRPqltaERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVM 428
Cdd:PRK00174 450 GGNLVIKDPwpGMMRTIYGDH----ERFVKTYFSTFKGMYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESAL 525
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 2214269206 429 LSLSGIQEAVVLAVSE---GglQELCAYYTSDQDIE-----KAELR 466
Cdd:PRK00174 526 VAHPKVAEAAVVGRPDdikG--QGIYAFVTLKGGEEpsdelRKELR 569
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
11-500 |
2.43e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 75.36 E-value: 2.43e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 11 ALFEKQAQQTPDHSA-------VKAGG--NLLTYRELDEQANQLAHHLRAQGA-GneDIVAIVMDRSAEVMVSILGVMKA 80
Cdd:PRK05850 5 SLLRERASLQPDDAAftfidyeQDPAGvaETLTWSQLYRRTLNVAEELRRHGStG--DRAVILAPQGLEYIVAFLGALQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 81 GAAFLPIDPDTP---EERIRYSLEDSGAKF-----AVVN---ERNMTAIGQYEGIIVSLD--DGKWRNESKERPSSISGS 147
Cdd:PRK05850 83 GLIAVPLSVPQGgahDERVSAVLRDTSPSVvlttsAVVDdvtEYVAPQPGQSAPPVIEVDllDLDSPRGSDARPRDLPST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 148 rnlAYVIYTSGTTGKPKGVQIEHRNLT-NYV----SWFSEEAGLTENDKTVlLSSYAFdlgYTSM-------FPVLLG-G 214
Cdd:PRK05850 163 ---AYLQYTSGSTRTPAGVMVSHRNVIaNFEqlmsDYFGDTGGVPPPDTTV-VSWLPF---YHDMglvlgvcAPILGGcP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 215 GELhivqketyTAPdeIAHYIKEhgITYIKLTPSLFHTIVNTASFA--------KDANFESLRL-----IVLGGEKIIPT 281
Cdd:PRK05850 236 AVL--------TSP--VAFLQRP--ARWMQLLASNPHAFSAAPNFAfelavrktSDDDMAGLDLggvlgIISGSERVHPA 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 282 DVIAFRKMYGHTEFINH-----YGPTEATIGAI-------------------AGRVDLYEPDAFAKRPTIGRPIANAGAL 337
Cdd:PRK05850 304 TLKRFADRFAPFNLRETairpsYGLAEATVYVAtrepgqppesvrfdyeklsAGHAKRCETGGGTPLVSYGSPRSPTVRI 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 338 VLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERF---VENPySPGS-----LmyKTGD--VVrrlSDGTLAFIGR 407
Cdd:PRK05850 384 VDPDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDP-SPGTpegpwL--RTGDlgFI---SEGELFIVGR 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 408 ADDQVKIRGYRIEPKEIETVmlslsgIQE-----AVVLAVSEGGLQELCAYY----TSDQDIE--------KAELRYQLS 470
Cdd:PRK05850 458 IKDLLIVDGRNHYPDDIEAT------IQEitggrVAAISVPDDGTEKLVAIIelkkRGDSDEEamdrlrtvKREVTSAIS 531
|
570 580 590
....*....|....*....|....*....|...
gi 2214269206 471 ltlPSH-MIPAFFVQV--DAIPLTANGKTDRNA 500
Cdd:PRK05850 532 ---KSHgLSVADLVLVapGSIPITTSGKIRRAA 561
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
12-501 |
3.34e-13 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 74.88 E-value: 3.34e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 12 LFEKQAQQTPDHSAVKAGGNLLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDT 91
Cdd:PLN02479 25 FLERAAVVHPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 92 PEERIRYSLEDSGAKFAVVNERNMTAIGQYEGIIVSLDDGKWR-------NESKERPSSI----------------SGSR 148
Cdd:PLN02479 105 NAPTIAFLLEHSKSEVVMVDQEFFTLAEEALKILAEKKKSSFKpplliviGDPTCDPKSLqyalgkgaieyekfleTGDP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 149 NLAY-----------VIYTSGTTGKPKGVQIEHRN-----LTNYVSWfseeaGLTENdktvllSSYAFDLG--------Y 204
Cdd:PLN02479 185 EFAWkppadewqsiaLGYTSGTTASPKGVVLHHRGaylmaLSNALIW-----GMNEG------AVYLWTLPmfhcngwcF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 205 TSMFPVLLGGGEL--HIVQKETYTApdeiahyIKEHGITYIKLTPSLFHTIVNTAsfAKDANFESLRLI-VLGGEKIIPT 281
Cdd:PLN02479 254 TWTLAALCGTNIClrQVTAKAIYSA-------IANYGVTHFCAAPVVLNTIVNAP--KSETILPLPRVVhVMTAGAAPPP 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 282 DVIA------FR--KMYGHTEfinHYGPTeaTIGAIAGRVDLYEPDAFAK---RPTIgRPIANAGALVLN-EALKLVPP- 348
Cdd:PLN02479 325 SVLFamsekgFRvtHTYGLSE---TYGPS--TVCAWKPEWDSLPPEEQARlnaRQGV-RYIGLEGLDVVDtKTMKPVPAd 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 349 GAS-GQLYITGQGLARGYLNRPQLTAERFvENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETV 427
Cdd:PLN02479 399 GKTmGEIVMRGNMVMKGYLKNPKANEEAF-ANGW------FHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENV 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 428 MLSLSGIQEAVVLAVSEGGLQEL-CAYYTSDQDIEKAELRYQLS-------LTLPSHMIPAFFVqVDAIPLTANGKTDRN 499
Cdd:PLN02479 472 VYTHPAVLEASVVARPDERWGESpCAFVTLKPGVDKSDEAALAEdimkfcrERLPAYWVPKSVV-FGPLPKTATGKIQKH 550
|
..
gi 2214269206 500 AL 501
Cdd:PLN02479 551 VL 552
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
7-498 |
5.22e-13 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 74.27 E-value: 5.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 7 ATFAALFEKQAQQTPDHSAVKAGGNL---LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAA 83
Cdd:PRK09192 21 PTLVEALDYAALGEAGMNFYDRRGQLeeaLPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 84 FLPIDPDTP-------EERIRYSLEDSGAKFAVVNER-----NMTAIGQYEGIIVSLDDGKWRNESKERPSSISgSRNLA 151
Cdd:PRK09192 101 PVPLPLPMGfggresyIAQLRGMLASAQPAAIITPDEllpwvNEATHGNPLLHVLSHAWFKALPEADVALPRPT-PDDIA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 152 YVIYTSGTTGKPKGVQIEHRNL-TNY----------------VSW--FSEEAGLTENDKTVLLSSYAFDLGYTSMF---P 209
Cdd:PRK09192 180 YLQYSSGSTRFPRGVIITHRALmANLraishdglkvrpgdrcVSWlpFYHDMGLVGFLLTPVATQLSVDYLPTRDFarrP 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 210 VLLgggeLHIVQKETYTapdeiahyikehgITYiklTPSLFHTI----VNTASFAkDANFESLRLIVLGGEkIIPTDVI- 284
Cdd:PRK09192 260 LQW----LDLISRNRGT-------------ISY---SPPFGYELcarrVNSKDLA-ELDLSCWRVAGIGAD-MIRPDVLh 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 285 ----AFRKM-YGHTEFINHYGPTEATI---------GAIAGRVDL--YEPDAFAKRPTIG----RPIANAG-AL------ 337
Cdd:PRK09192 318 qfaeAFAPAgFDDKAFMPSYGLAEATLavsfsplgsGIVVEEVDRdrLEYQGKAVAPGAEtrrvRTFVNCGkALpgheie 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 338 VLNEALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYktgdvvrrLSDGTLAFIGRADDQVKIRGY 417
Cdd:PRK09192 398 IRNEAGMPLPERVVGHICVRGPSLMSGYFRDEESQDVLAADGWLDTGDLGY--------LLDGYLYITGRAKDLIIINGR 469
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 418 RIEPKEIETVMLSLSGIQ--EAVVLAVSEGGLQELCAYY---TSDQDiEKAELRYQLSLTLPShmipAFFVQVD------ 486
Cdd:PRK09192 470 NIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIVLLVqcrISDEE-RRGQLIHALAALVRS----EFGVEAAvelvpp 544
|
570
....*....|...
gi 2214269206 487 -AIPLTANGKTDR 498
Cdd:PRK09192 545 hSLPRTSSGKLSR 557
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1197-1471 |
5.48e-13 |
|
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: 73.68 E-value: 5.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1197 AENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGFGFDASIWEMFPTWTIGAELHVI---DEA 1273
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAGMNQYLmptRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1274 IRLDIVRLNDYFEtNGVTIT---------FLPTQLAEQFMELENTSLRVLLTGGDK---------LKRAVK---KPYTLV 1332
Cdd:cd05908 185 IRRPILWLKKASE-HKATIVsspnfgykyFLKTLKPEKANDWDLSSIRMILNGAEPidyelchefLDHMSKyglKRNAIL 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1333 NNYGPTENTVVATSAEIH-----------------PEEGS----------LSIGRAIANTRVYILGEGNQVQPEGVAGEL 1385
Cdd:cd05908 264 PVYGLAEASVGASLPKAQspfktitlgrrhvthgePEPEVdkkdsecltfVEVGKPIDETDIRICDEDNKILPDGYIGHI 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1386 CVAGRGLARGYLNREDETAKRFVADPFVpgermyRTGDLVKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQ 1465
Cdd:cd05908 344 QIRGKNVTPGYYNNPEATAKVFTDDGWL------KTGDLGFIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVE 417
|
....*.
gi 2214269206 1466 DAAVTA 1471
Cdd:cd05908 418 LGRVVA 423
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
1281-1533 |
6.12e-13 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 73.49 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1281 LNDYFetngvtITFLPTQLaEQFMELENTSLR----VLLTGG----DKLKRAVKKPYTLVNNYGPTEntvvaTSAEI--- 1349
Cdd:PRK07445 206 PSDFF------LSLVPTQL-QRLLQLRPQWLAqfrtILLGGApawpSLLEQARQLQLRLAPTYGMTE-----TASQIatl 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1350 HPEE---GSLSIGRAIANTRVYIlgegnqvqPEGVAGELCVAGRGLARGYLnredetakrfvaDPFVPGERMYRTGDLVK 1426
Cdd:PRK07445 274 KPDDflaGNNSSGQVLPHAQITI--------PANQTGNITIQAQSLALGYY------------PQILDSQGIFETDDLGY 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1427 WVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKG-GNTAIAAYV-TPETADIEALKSTLKETL 1503
Cdd:PRK07445 334 LDAQGYLHIlGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHwGEVVTAIYVpKDPSISLEELKTAIKDQL 413
|
250 260 270
....*....|....*....|....*....|
gi 2214269206 1504 PDYMIPAFWVTLNELPVTANGKVDRKALPE 1533
Cdd:PRK07445 414 SPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1552-1610 |
6.29e-13 |
|
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: 65.28 E-value: 6.29e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 1552 ELLAGIWQDVLGMS--EVGVTDNFFSLGGDSIKGIQMASRLNQH-GWKLEMKDLFQHPTIEE 1610
Cdd:pfam00550 1 ERLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
48-498 |
7.14e-13 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 73.65 E-value: 7.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 48 HLRAQGA----GNED---IVAIVMDRSAEVMVSILGVMKAGAA--FLP-----IDPDtpeeriRYSlEDSGAKFAVVNER 113
Cdd:PRK05851 38 HGRAENVaarlLDRDrpgAVGLVGEPTVELVAAIQGAWLAGAAvsILPgpvrgADDG------RWA-DATLTRFAGIGVR 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 114 NMTAIGQY-------EGIIVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGL 186
Cdd:PRK05851 111 TVLSHGSHlerlravDSSVTVHDLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 187 TENDKTVL--LSSYaFDLGYTSMFPVLLGGGELHIVQKETYTA-PDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAKDA 263
Cdd:PRK05851 191 DAATDVGCswLPLY-HDMGLAFLLTAALAGAPLWLAPTTAFSAsPFRWLSWLSDSRATLTAAPNFAYNLIGKYARRVSDV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 264 NFESLRLIVLGGEkiiPTDVIAFRKMYGHTE--------FINHYGPTEAT---------IGAIAGRVDLYEPDAFAKRPT 326
Cdd:PRK05851 270 DLGALRVALNGGE---PVDCDGFERFATAMApfgfdagaAAPSYGLAESTcavtvpvpgIGLRVDEVTTDDGSGARRHAV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 327 IGRPIANAgalvlneALKLVPPGAS--------GQLYITGQGLARGYLNrpqltaerfvENPYSPGSlMYKTGDVvRRLS 398
Cdd:PRK05851 347 LGNPIPGM-------EVRISPGDGAagvagreiGEIEIRGASMMSGYLG----------QAPIDPDD-WFPTGDL-GYLV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 399 DGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEG------GLQELCAYYTSDQDIEKAELRYQLSL- 471
Cdd:PRK05851 408 DGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGegsarpGLVIAAEFRGPDEAGARSEVVQRVASe 487
|
490 500
....*....|....*....|....*....
gi 2214269206 472 --TLPSHMIpafFVQVDAIPLTANGKTDR 498
Cdd:PRK05851 488 cgVVPSDVV---FVAPGSLPRTSSGKLRR 513
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1047-1443 |
7.26e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 73.93 E-value: 7.26e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1047 PVPTDKTVHQLFEETVQRHKDRPAV---TYNGQSW---TYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVL 1120
Cdd:PRK12582 44 LGPYPRSIPHLLAKWAAEAPDRPWLaqrEPGHGQWrkvTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1121 GVLKAGAAFVPIDPDYP----D-QRIEYILQDSGAKLLLKQEG------ISVPDSYTGDVILLDGSRT-ILSLPLDENDE 1188
Cdd:PRK12582 124 AAMQAGVPAAPVSPAYSlmshDhAKLKHLFDLVKPRVVFAQSGapfaraLAALDLLDVTVVHVTGPGEgIASIAFADLAA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1189 GNPETAVTA-------ENLAYMIYTSGTTGQPKGV------------MVE----------HHALVNLCFWHHdAFSMTAe 1239
Cdd:PRK12582 204 TPPTAAVAAaiaaitpDTVAKYLFTSGSTGMPKAVintqrmmcaniaMQEqlrprepdppPPVSLDWMPWNH-TMGGNA- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1240 drsakyagfGFDASIWE--------------MFPTwTIgAELHVI---------------------DEAIRLDIVRLNDY 1284
Cdd:PRK12582 282 ---------NFNGLLWGggtlyiddgkplpgMFEE-TI-RNLREIsptvygnvpagyamlaeamekDDALRRSFFKNLRL 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1285 FETNGVTitfLPTQLAEQFMEL--ENTSLRVLLTGGdklkravkkpytlvnnYGPTENTVVATSAEIHPEegslsigrai 1362
Cdd:PRK12582 351 MAYGGAT---LSDDLYERMQALavRTTGHRIPFYTG----------------YGATETAPTTTGTHWDTE---------- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1363 antRVYILG---EGNQVQ--PEGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermYRTGDLVKWV-----NGGI 1432
Cdd:PRK12582 402 ---RVGLIGlplPGVELKlaPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF------YRLGDAARFVdpddpEKGL 472
|
490
....*....|.
gi 2214269206 1433 EYIGRIDQQVK 1443
Cdd:PRK12582 473 IFDGRVAEDFK 483
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1203-1527 |
7.55e-13 |
|
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: 71.95 E-value: 7.55e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1203 MIYTSGTTGQPKGVMVEHHALV--NLcfwhhDAFSMTAEDRSAKY--AGFGFD-ASIWEMFPTWTIGAELHVIDeaiRLD 1277
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLaqAL-----VLAVLQAIDEGTVFlnSGPLFHiGTLMFTLATFHAGGTNVFVR---RVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1278 IVRLNDYFETNGVTITFLPTQLAEQFMELEN------TSLRVLLT-------GGDKLKRAVKKPYtlvnNYGPTENTVVA 1344
Cdd:cd17636 77 AEEVLELIEAERCTHAFLLPPTIDQIVELNAdglydlSSLRSSPAapewndmATVDTSPWGRKPG----GYGQTEVMGLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1345 TSAEIhPEEGSLSIGRAIANTRVYILGE-GNQVqPEGVAGELCVAGRGLARGYLNREDETAKRFVAdpfvpgeRMYRTGD 1423
Cdd:cd17636 153 TFAAL-GGGAIGGAGRPSPLVQVRILDEdGREV-PDGEVGEIVARGPTVMAGYWNRPEVNARRTRG-------GWHHTND 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1424 LVKW-VNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE---TADIEALKSTL 1499
Cdd:cd17636 224 LGRRePDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKpgaSVTEAELIEHC 303
|
330 340
....*....|....*....|....*...
gi 2214269206 1500 KETLPDYMIPAFWVTLNELPVTANGKVD 1527
Cdd:cd17636 304 RARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1059-1533 |
1.10e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 73.06 E-value: 1.10e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1059 EETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPD 1138
Cdd:PRK08162 25 ERAAEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1139 QRIEYILQDSGAKLLLKqegisvpDSYTGDVI-----LLDGSRTIL----------SLPLDEND------EGNPETAVTA 1197
Cdd:PRK08162 105 ASIAFMLRHGEAKVLIV-------DTEFAEVArealaLLPGPKPLVidvddpeypgGRFIGALDyeaflaSGDPDFAWTL 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1198 -----ENLAyMIYTSGTTGQPKGVmVEHH------ALVNLCFWhhdafSMTaedRSAKYagfgfdasIWEM--------- 1257
Cdd:PRK08162 178 padewDAIA-LNYTSGTTGNPKGV-VYHHrgaylnALSNILAW-----GMP---KHPVY--------LWTLpmfhcngwc 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1258 FPtWTIGAELHVIDEAIRLDIVRLNDYFETNGVT-----------ITFLPTQLAEQFmeleNTSLRVLLTGG-------D 1319
Cdd:PRK08162 240 FP-WTVAARAGTNVCLRKVDPKLIFDLIREHGVThycgapivlsaLINAPAEWRAGI----DHPVHAMVAGAappaaviA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1320 KLKRA---VKKPYTLVNNYGPtentvvATSAEIHPEEGSLSIG-RAIANTR---VYILGEGNQV-QPEGVA--------- 1382
Cdd:PRK08162 315 KMEEIgfdLTHVYGLTETYGP------ATVCAWQPEWDALPLDeRAQLKARqgvRYPLQEGVTVlDPDTMQpvpadgeti 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1383 GELCVAGRGLARGYLNREDETAKRFVADPFvpgermyRTGDLVKWVNGGieYIgridqQVKVR--------GYRIELSEI 1454
Cdd:PRK08162 389 GEIMFRGNIVMKGYLKNPKATEEAFAGGWF-------HTGDLAVLHPDG--YI-----KIKDRskdiiisgGENISSIEV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1455 EVQLAQLSEVQDAAVTAVKD-KGGNTAiAAYVTPE---TADIEALKSTLKETLPDYMIPAFwVTLNELPVTANGKVDRKA 1530
Cdd:PRK08162 455 EDVLYRHPAVLVAAVVAKPDpKWGEVP-CAFVELKdgaSATEEEIIAHCREHLAGFKVPKA-VVFGELPKTSTGKIQKFV 532
|
...
gi 2214269206 1531 LPE 1533
Cdd:PRK08162 533 LRE 535
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
1670-1837 |
1.15e-12 |
|
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: 72.30 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1670 EKTLQALIEHHDALRMVYREENGDIVQVYKPIGESKVSFEIVDLygsDEEMLRSQIKLLAnklQSSLDLRNGPLLKAEQY 1749
Cdd:cd19538 42 QQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLEIKEV---DEEELESEINEAV---RYPFDLSEEPPFRATLF 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1750 RTEAGDH-LLIAVHHLVVDGVSWRILLEDFASGYMQAEKEESLVFPQKTNSFKD---WAEEL--AAFSQSAHLLQQAEYW 1823
Cdd:cd19538 116 ELGENEHvLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPELAPLPVQYADyalWQQELlgDESDPDSLIARQLAYW 195
|
170
....*....|....*..
gi 2214269206 1824 SQIAA---EQVsPLPKD 1837
Cdd:cd19538 196 KKQLAglpDEI-ELPTD 211
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1058-1525 |
1.17e-12 |
|
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: 73.07 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1058 FEETVQRHK--DRPAVTYNG-----QSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFV 1130
Cdd:cd05943 72 YAENLLRHAdaDDPAAIYAAedgerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWS 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1131 PIDPDYPDQ----RIEYI----------------LQDSGAKLLLKQEGIsvPD-------SYTGDVILLDGSRTILSLPL 1183
Cdd:cd05943 152 SCSPDFGVPgvldRFGQIepkvlfavdaytyngkRHDVREKVAELVKGL--PSllavvvvPYTVAAGQPDLSKIAKALTL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1184 DE----NDEGNPE-TAVTAENLAYMIYTSGTTGQPK-------GVMVEH---HALvnlcfwHHDafsMTAEDRSakyagF 1248
Cdd:cd05943 230 EDflatGAAGELEfEPLPFDHPLYILYSSGTTGLPKcivhgagGTLLQHlkeHIL------HCD---LRPGDRL-----F 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1249 GFDASIWEMFpTWTI-----GAELHVIDEA-IRLDIVRLNDYFETNGVTI-----TFLPTQLAEQFMELEN---TSLRVL 1314
Cdd:cd05943 296 YYTTCGWMMW-NWLVsglavGATIVLYDGSpFYPDTNALWDLADEEGITVfgtsaKYLDALEKAGLKPAEThdlSSLRTI 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1315 LTGGDKLK--------RAVKKPYTLVNNYGPTEntVVATSAEIHPeegSLSIGRAIANTRVyiLG--------EGNQVQp 1378
Cdd:cd05943 375 LSTGSPLKpesfdyvyDHIKPDVLLASISGGTD--IISCFVGGNP---LLPVYRGEIQCRG--LGmaveafdeEGKPVW- 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1379 eGVAGEL-CVAGR-GLARGYLNreDETAKRFVADPF--VPGerMYRTGDLVKWVN-GGIEYIGRIDQQVKVRGYRIELSE 1453
Cdd:cd05943 447 -GEKGELvCTKPFpSMPVGFWN--DPDGSRYRAAYFakYPG--VWAHGDWIEITPrGGVVILGRSDGTLNPGGVRIGTAE 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1454 IEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYV--------TPETAdiEALKSTLKETLPDYMIPAFWVTLNELPVTANGK 1525
Cdd:cd05943 522 IYRVVEKIPEVEDSLVVGQEWKDGDERVILFVklregvelDDELR--KRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
33-501 |
1.17e-12 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 72.89 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQ-GAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVN 111
Cdd:PRK05620 39 TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 112 ERNMTAIGQY-------EGIIVSLDDgKWRNESKERPSSIS--------------------GSRNLAYVIYTSGTTGKPK 164
Cdd:PRK05620 119 PRLAEQLGEIlkecpcvRAVVFIGPS-DADSAAAHMPEGIKvysyealldgrstvydwpelDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 165 GVQIEHRNL-TNYVSWFSEEAGLTENDKTVLLS-------SYAFDLG-YTSMFPVLLGGGELhivqketytAPDEIAHYI 235
Cdd:PRK05620 198 GVVYSHRSLyLQSLSLRTTDSLAVTHGESFLCCvpiyhvlSWGVPLAaFMSGTPLVFPGPDL---------SAPTLAKII 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 236 KE------HGItyikltPSLFHTIVnTASFAKDANFESLRLIVLGGEKIIPTDVIAFRKMYGhTEFINHYGPTE-ATIGA 308
Cdd:PRK05620 269 ATamprvaHGV------PTLWIQLM-VHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYG-VDVVHVWGMTEtSPVGT 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 309 IAgrvdlyEPDA-------FAKRPTIGRPIANAGALVLNEALKLVPPGAS-GQLYITGQGLARGYLNRPQLT----AERF 376
Cdd:PRK05620 341 VA------RPPSgvsgearWAYRVSQGRFPASLEYRIVNDGQVMESTDRNeGEIQVRGNWVTASYYHSPTEEgggaASTF 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 377 VENPYSPGSLMY------KTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV-----SEG 445
Cdd:PRK05620 415 RGEDVEDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYpddkwGER 494
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 2214269206 446 GLQELCAYYTSDQDIEKAE-LRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK05620 495 PLAVTVLAPGIEPTRETAErLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1664-1835 |
1.39e-12 |
|
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: 72.10 E-value: 1.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1664 FDPERVEKTLQALIEHHDALRMVY--REENGDIVQVYkpIGESKVSFEIVDlyGSDEEmlrsQIKLLANKLQS-SLDLRN 1740
Cdd:cd19532 36 LDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGV--LASSPLRLEHVQ--ISDEA----EVEEEFERLKNhVYDLES 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1741 GPLLKAEQYRTEAGDH-LLIAVHHLVVDGVSWRILLEDFASGYmqaekeESLVFPQKTNSFKDWAEELAAFSQSAHLLQQ 1819
Cdd:cd19532 108 GETMRIVLLSLSPTEHyLIFGYHHIAMDGVSFQIFLRDLERAY------NGQPLLPPPLQYLDFAARQRQDYESGALDED 181
|
170
....*....|....*.
gi 2214269206 1820 AEYWSQIAAEQVSPLP 1835
Cdd:cd19532 182 LAYWKSEFSTLPEPLP 197
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1062-1553 |
1.44e-12 |
|
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: 72.73 E-value: 1.44e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1062 VQRH-----KDRPAVTY------NGQSWTYGELNAKANRLARILMDCGISPDDRVgVLTKPSL-EMSAAVLGVLKAGA-- 1127
Cdd:cd05967 56 LDRHveagrGDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRV-IIYMPMIpEAAIAMLACARIGAih 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1128 -----AFVP------ID---------PDY---PDQRIEYI------LQDSG---AKLLLKQEGISVPDsytgdviLLDGS 1175
Cdd:cd05967 135 svvfgGFAAkelasrIDdakpklivtASCgiePGKVVPYKplldkaLELSGhkpHHVLVLNRPQVPAD-------LTKPG 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1176 RTILSLPLDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVM--VEHHAlVNLCFWHHDAFSMTAEDR--SAKYAGF--- 1248
Cdd:cd05967 208 RDLDWSELLAKAEPVDCVPVAATDPLYILYTSGTTGKPKGVVrdNGGHA-VALNWSMRNIYGIKPGDVwwAASDVGWvvg 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1249 -----------GFDASIWEMFPTWT--IGAELHVIDE-----------AIRldIVRLNDyfeTNGvtitflptQLAEQFm 1304
Cdd:cd05967 287 hsyivygpllhGATTVLYEGKPVGTpdPGAFWRVIEKyqvnalftaptAIR--AIRKED---PDG--------KYIKKY- 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1305 elENTSLRVLLTGGDKL--------KRAVKKPytLVNNYGPTEN----TVVATSAEIHPEEGSlSIGRAIANTRVYILGE 1372
Cdd:cd05967 353 --DLSSLRTLFLAGERLdpptlewaENTLGVP--VIDHWWQTETgwpiTANPVGLEPLPIKAG-SPGKPVPGYQVQVLDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1373 -GNQVQPeGVAGELCVAGRgLARGYLN---REDEtakRFVADPF--VPGerMYRTGDL-VKWVNGGIEYIGRIDQQVKVR 1445
Cdd:cd05967 428 dGEPVGP-NELGNIVIKLP-LPPGCLLtlwKNDE---RFKKLYLskFPG--YYDTGDAgYKDEDGYLFIMGRTDDVINVA 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1446 GYRIELSEIEVQLAQLSEVQDAAVTAVKDK-GGNTAIAAYVTPETADI------EALKSTLKETLPDYMIPAFWVTLNEL 1518
Cdd:cd05967 501 GHRLSTGEMEESVLSHPAVAECAVVGVRDElKGQVPLGLVVLKEGVKItaeeleKELVALVREQIGPVAAFRLVIFVKRL 580
|
570 580 590
....*....|....*....|....*....|....*..
gi 2214269206 1519 PVTANGKVDRKALpePDIEAGSgEYKAPTT--DMEEL 1553
Cdd:cd05967 581 PKTRSGKILRRTL--RKIADGE-DYTIPSTieDPSVL 614
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1309-1531 |
2.21e-12 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 70.97 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1309 TSLRVLLTGGDKLKRAVKKPY------TLVNNYGPTENTVVATsaeIHPEEGSL---SIGRAIANTRVYIL---GEGNQV 1376
Cdd:cd05944 121 SSLRFAMSGAAPLPVELRARFedatglPVVEGYGLTEATCLVA---VNPPDGPKrpgSVGLRLPYARVRIKvldGVGRLL 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1377 QPEGV--AGELCVAGRGLARGYLNREDETakrfvaDPFVpGERMYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSE 1453
Cdd:cd05944 198 RDCAPdeVGEICVAGPGVFGGYLYTEGNK------NAFV-ADGWLNTGDLGRLDADGYLFItGRAKDLIIRGGHNIDPAL 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1454 IEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVT---PETADIEALKSTLKETLPDY-MIPAFWVTLNELPVTANGKVDRK 1529
Cdd:cd05944 271 IEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQlkpGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKP 350
|
..
gi 2214269206 1530 AL 1531
Cdd:cd05944 351 AL 352
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1067-1541 |
2.21e-12 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 72.11 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYNGQSWtyGELNAKANRLARILMDCGisPDDRVGVLTKPSLEMSAAVLGVLKAGAAfVPIDPDY-----PDQRI 1141
Cdd:PRK05851 23 DRESGLWRRHPW--PEVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAA-VSILPGPvrgadDGRWA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1142 EYILQ---DSGAKLLLKQ----EGISVPDS--YTGDVILLDGSRTilSLPLDENDEGNPetavtaenlAYMIYTSGTTGQ 1212
Cdd:PRK05851 98 DATLTrfaGIGVRTVLSHgshlERLRAVDSsvTVHDLATAAHTNR--SASLTPPDSGGP---------AVLQGTAGSTGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1213 PKGVMVEHHA-LVNL----------------CFW---HHD---AFSMTAedrsaKYAGfgfdASIWEMfPTWTIGAElhv 1269
Cdd:PRK05851 167 PRTAILSPGAvLSNLrglnarvgldaatdvgCSWlplYHDmglAFLLTA-----ALAG----APLWLA-PTTAFSAS--- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1270 ideairldIVRLNDYFETNGVTITFLPT-------QLAEQFMELENTSLRVLLTGG------------DKLKRAVKKPYT 1330
Cdd:PRK05851 234 --------PFRWLSWLSDSRATLTAAPNfaynligKYARRVSDVDLGALRVALNGGepvdcdgferfaTAMAPFGFDAGA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1331 LVNNYGPTENTVVATSAE----------IHPEEGSLS----IGRAIANTRVYIL-GEGNQVQPEGVAGELCVAGRGLARG 1395
Cdd:PRK05851 306 AAPSYGLAESTCAVTVPVpgiglrvdevTTDDGSGARrhavLGNPIPGMEVRISpGDGAAGVAGREIGEIEIRGASMMSG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1396 YLNredetakrfvADPFVPGErMYRTGDLVKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDK 1475
Cdd:PRK05851 386 YLG----------QAPIDPDD-WFPTGDLGYLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTG 454
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 1476 GGNT----AIAA-YVTPE--TADIEALKSTLKETlpdYMIPAFWVTL--NELPVTANGKVDRKALPEpDIEAGSG 1541
Cdd:PRK05851 455 EGSArpglVIAAeFRGPDeaGARSEVVQRVASEC---GVVPSDVVFVapGSLPRTSSGKLRRLAVKR-SLEAADG 525
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1062-1531 |
2.92e-12 |
|
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: 71.82 E-value: 2.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1062 VQRHKDRPAVTYNG------QSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAA----FVP 1131
Cdd:cd05966 63 LKERGDKVAIIWEGdepdqsRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVhsvvFAG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1132 IDPDYPDQRIEyilqDSGAKLL--------------LK-------QEGISVPD----SYTGDVILLDGSRTIL--SLPLD 1184
Cdd:cd05966 143 FSAESLADRIN----DAQCKLVitadggyrggkvipLKeivdealEKCPSVEKvlvvKRTGGEVPMTEGRDLWwhDLMAK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1185 ENDEGNPEtAVTAENLAYMIYTSGTTGQPKGVMvehHA----LVNLCFWHHDAFSMTAEDRsakyagFGFDASI-W---- 1255
Cdd:cd05966 219 QSPECEPE-WMDSEDPLFILYTSGSTGKPKGVV---HTtggyLLYAATTFKYVFDYHPDDI------YWCTADIgWitgh 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1256 --------------EMF---PTWTigaelhviDEAIRLDIVrlndyfETNGVTITFL-PTQLaEQFMELEN--------T 1309
Cdd:cd05966 289 syivygplangattVMFegtPTYP--------DPGRYWDIV------EKHKVTIFYTaPTAI-RALMKFGDewvkkhdlS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1310 SLRVLLTGGDKLKRAVKKPY---------TLVNNYGPTE-----NTVVATSAEIHPeeGSlsigraiaNTR------VYI 1369
Cdd:cd05966 354 SLRVLGSVGEPINPEAWMWYyevigkercPIVDTWWQTEtggimITPLPGATPLKP--GS--------ATRpffgiePAI 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1370 LGEGNQVQPEGVAGELCVAGR--GLARGYLNREDetakRFVADPFVPGERMYRTGDLVK-------WVnggieyIGRIDQ 1440
Cdd:cd05966 424 LDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARrdedgyyWI------TGRVDD 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1441 QVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKD--KGgnTAIAAYVT------PETADIEALKSTLKETL-----PDYM 1507
Cdd:cd05966 494 VINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHdiKG--EAIYAFVTlkdgeePSDELRKELRKHVRKEIgpiatPDKI 571
|
570 580
....*....|....*....|....
gi 2214269206 1508 IpafWVTlnELPVTANGKVDRKAL 1531
Cdd:cd05966 572 Q---FVP--GLPKTRSGKIMRRIL 590
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1635-1825 |
3.39e-12 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 70.80 E-value: 3.39e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1635 TPIQRWFFEKNFTNKHHWNQSVMLHAKKGFDPERVEKTLQALIEHHDALRMVYREENGD--IVQ-VYKpigesKVSFEIV 1711
Cdd:cd19542 5 TPMQEGMLLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEgtFLQvVLK-----SLDPPIE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1712 DLYGSDEEmlrsqiklLANKLQSSLDLRNG---PLLKAEQYRTEAGDH-LLIAVHHLVVDGVSWRILLEDFASGYmqaek 1787
Cdd:cd19542 80 EVETDEDS--------LDALTRDLLDDPTLfgqPPHRLTLLETSSGEVyLVLRISHALYDGVSLPIILRDLAAAY----- 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 2214269206 1788 EESLVFPqkTNSFKDWAEELAAFSQSAHLlqqaEYWSQ 1825
Cdd:cd19542 147 NGQLLPP--APPFSDYISYLQSQSQEESL----QYWRK 178
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1079-1437 |
3.45e-12 |
|
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: 71.48 E-value: 3.45e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1079 TYGELNAKANRLARILMDCGI--SPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLLKQ 1156
Cdd:cd05927 7 SYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCD 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1157 EGISVpdsYTGDVILLDGSRtilslpldendegNPETAV--TAENLAYMIYTSGTTGQPKGVMVEHHALVN----LCFWH 1230
Cdd:cd05927 87 AGVKV---YSLEEFEKLGKK-------------NKVPPPppKPEDLATICYTSGTTGNPKGVMLTHGNIVSnvagVFKIL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1231 HDAFSMTAEDRSAKY-------------------AGFGF----------DasIWEMFPTWTIGAE--LHVIDEAIRLDIV 1279
Cdd:cd05927 151 EILNKINPTDVYISYlplahifervvealflyhgAKIGFysgdirllldD--IKALKPTVFPGVPrvLNRIYDKIFNKVQ 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1280 R----------------LNDYFETNGVTITFLPTQLAEQFMELENTSLRVLLTGGDKLKRAVKKPY------TLVNNYGP 1337
Cdd:cd05927 229 AkgplkrklfnfalnykLAELRSGVVRASPFWDKLVFNKIKQALGGNVRLMLTGSAPLSPEVLEFLrvalgcPVLEGYGQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1338 TENTVVATSAeiHPEEGSL-SIGRAIANtrvyilgegNQVQPEGV------------AGELCVAGRGLARGYLNREDETA 1404
Cdd:cd05927 309 TECTAGATLT--LPGDTSVgHVGGPLPC---------AEVKLVDVpemnydakdpnpRGEVCIRGPNVFSGYYKDPEKTA 377
|
410 420 430
....*....|....*....|....*....|....
gi 2214269206 1405 KRFVADPFvpgermYRTGDLVKWV-NGGIEYIGR 1437
Cdd:cd05927 378 EALDEDGW------LHTGDIGEWLpNGTLKIIDR 405
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1065-1531 |
3.56e-12 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 71.41 E-value: 3.56e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1065 HKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYI 1144
Cdd:PLN02479 33 HPTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1145 LQDSGAK-LLLKQEGISVPDSYTGdvILLDGSRTILSLPL-----DEN---------------------DEGNPETAVTA 1197
Cdd:PLN02479 113 LEHSKSEvVMVDQEFFTLAEEALK--ILAEKKKSSFKPPLlivigDPTcdpkslqyalgkgaieyekflETGDPEFAWKP 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1198 -----ENLAyMIYTSGTTGQPKGVMVEHH-----ALVNLCFWhhdafsmtAEDRSAKYagfgfdasIWE--MFP------ 1259
Cdd:PLN02479 191 padewQSIA-LGYTSGTTASPKGVVLHHRgaylmALSNALIW--------GMNEGAVY--------LWTlpMFHcngwcf 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1260 TWTIGAEL-------HVIDEAIRLDIVRlndyfetNGVT------------------ITFLPTQLAEQFMELENTSLRVL 1314
Cdd:PLN02479 254 TWTLAALCgtniclrQVTAKAIYSAIAN-------YGVThfcaapvvlntivnapksETILPLPRVVHVMTAGAAPPPSV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1315 LTGGDKLKRAVKKPYTLVNNYGPTenTVVATSaeihPEEGSLS-IGRAIANTRV---YILGEG-NQVQPEGVA------- 1382
Cdd:PLN02479 327 LFAMSEKGFRVTHTYGLSETYGPS--TVCAWK----PEWDSLPpEEQARLNARQgvrYIGLEGlDVVDTKTMKpvpadgk 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1383 --GELCVAGRGLARGYLNREDETAKRFVADpfvpgerMYRTGDL-VKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLA 1459
Cdd:PLN02479 401 tmGEIVMRGNMVMKGYLKNPKANEEAFANG-------WFHSGDLgVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVY 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1460 QLSEVQDAAVTAVKDKGGNTAIAAYVTP----ETADIEALKSTL----KETLPDYMIPAFwVTLNELPVTANGKVDRKAL 1531
Cdd:PLN02479 474 THPAVLEASVVARPDERWGESPCAFVTLkpgvDKSDEAALAEDImkfcRERLPAYWVPKS-VVFGPLPKTATGKIQKHVL 552
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1634-1947 |
4.24e-12 |
|
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: 70.49 E-value: 4.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1634 LTPIQR--WFFEK--NFTNKHHWNQSVMLHAkkGFDPERVEKTLQALIEHHDALRMVYREENGDI-VQVYKPIGESKVSF 1708
Cdd:cd19539 4 LSFAQErlWFIDQgeDGGPAYNIPGAWRLTG--PLDVEALREALRDVVARHEALRTLLVRDDGGVpRQEILPPGPAPLEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1709 EIVDLYGSDeemLRSQIKLLANKLQSS-LDLRNGPLLKAEQYRTEAGDH-LLIAVHHLVVDGVSWRILLEDFASGYMQAE 1786
Cdd:cd19539 82 RDLSDPDSD---RERRLEELLRERESRgFDLDEEPPIRAVLGRFDPDDHvLVLVAHHTAFDAWSLDVFARDLAALYAARR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1787 KEESLVFPQKTNSFKDWAEELAAFSQSAHLLQQAEYWSQ-IAAEQVSPLPKDCETEQRIVKDTSSVLCELTAEDTKHlLT 1865
Cdd:cd19539 159 KGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRrLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAA-LR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1866 DVHQPYGTEINDILLSALGLTMKEWTkgakiginleghGREDI---IPNVN-----ISRTVGWFTAQYPVVLDISD-ADA 1936
Cdd:cd19539 238 ELAKRARSSLFMVLLAAYCVLLRRYT------------GQTDIvvgTPVAGrnhprFESTVGFFVNLLPLRVDVSDcATF 305
|
330
....*....|.
gi 2214269206 1937 SAVIKTVKENL 1947
Cdd:cd19539 306 RDLIARVRKAL 316
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1067-1446 |
4.96e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 71.13 E-value: 4.96e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTYN--GQSW-------TYGELNAKANRLARILMDCGiSPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYP 1137
Cdd:PRK05850 16 DDAAFTFIdyEQDPagvaetlTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAVPLSVPQG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1138 ---DQRIEYILQDSGAKLLLKQEgiSVPDSYTGDVILLDGSRT-----ILSLPLDENDEGNPeTAVTAENLAYMIYTSGT 1209
Cdd:PRK05850 95 gahDERVSAVLRDTSPSVVLTTS--AVVDDVTEYVAPQPGQSAppvieVDLLDLDSPRGSDA-RPRDLPSTAYLQYTSGS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1210 TGQPKGVMVEHHAL-VNLcfwhhdAFSMtaedrSAKYAGFGFDASIWEMFPTW-----TIGAELHVIdeairLDIVrlnd 1283
Cdd:PRK05850 172 TRTPAGVMVSHRNViANF------EQLM-----SDYFGDTGGVPPPDTTVVSWlpfyhDMGLVLGVC-----APIL---- 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1284 yfetNGVT------ITFL--PT----QLAEQF----------MEL--ENTS-----------LRVLLTGGDK-----LKR 1323
Cdd:PRK05850 232 ----GGCPavltspVAFLqrPArwmqLLASNPhafsaapnfaFELavRKTSdddmagldlggVLGIISGSERvhpatLKR 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1324 AVKK--PYTLVNN-----YGPTENTV-VATSAEIHPEEG------SLSIGRAI-----ANTR-----------VYIL-GE 1372
Cdd:PRK05850 308 FADRfaPFNLRETairpsYGLAEATVyVATREPGQPPESvrfdyeKLSAGHAKrcetgGGTPlvsygsprsptVRIVdPD 387
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 1373 GNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVA-----DPFVPGERMYRTGDLVKWVNGGIEYIGRIDQQVKVRG 1446
Cdd:PRK05850 388 TCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFGAtlvdpSPGTPEGPWLRTGDLGFISEGELFIVGRIKDLLIVDG 466
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
523-582 |
5.89e-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: 5.89e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 523 ESLCRIWQKTLGI--EAIGIDDNFFDLGGHSLKGMMLIANIQAELEKSVPLKALFEQPTVRQ 582
Cdd:pfam00550 1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1073-1240 |
7.73e-12 |
|
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar proteins; Fatty acid transport proteins (FATP) of this family transport long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes hsFATP2, hsFATP5, and hsFATP6, and similar proteins. Each FATP has unique patterns of tissue distribution. These FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. The hsFATP proteins exist in two splice variants; the b variant, lacking exon 3, has no acyl-CoA synthetase activity. FATPs are key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341261 [Multi-domain] Cd Length: 537 Bit Score: 70.40 E-value: 7.73e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1073 YNGQSWTYGELNAKANRLARILMD-CGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAK 1151
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1152 LL----------------LKQEGISVpdSYTGDVILLDGSRTILSLPLDENDEGNPETA---VTAENLAYMIYTSGTTGQ 1212
Cdd:cd05938 81 VLvvapelqeaveevlpaLRADGVSV--WYLSHTSNTEGVISLLDKVDAASDEPVPASLrahVTIKSPALYIYTSGTTGL 158
|
170 180
....*....|....*....|....*...
gi 2214269206 1213 PKGVMVEHHALVNLCFWHHdAFSMTAED 1240
Cdd:cd05938 159 PKAARISHLRVLQCSGFLS-LCGVTADD 185
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1063-1531 |
1.03e-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: 69.71 E-value: 1.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1063 QRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIE 1142
Cdd:cd05929 3 ARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEAC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1143 YILQDSGAKLLLKQEGisVPDSYTGDVILldgsrtilslplDENDEGNPETAVTAE-NLAYMIYTSGTTGQPKGVMVEHH 1221
Cdd:cd05929 83 AIIEIKAAALVCGLFT--GGGALDGLEDY------------EAAEGGSPETPIEDEaAGWKMLYSGGTTGRPKGIKRGLP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1222 alvnlCFWHHDAFSMTAEDRSakyaGFGFDASIWEMFP-------TWTIGAELH----VIDEaiRLDIVRLNDYFETNGV 1290
Cdd:cd05929 149 -----GGPPDNDTLMAAALGF----GPGADSVYLSPAPlyhaapfRWSMTALFMggtlVLME--KFDPEEFLRLIERYRV 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1291 T-ITFLPT------QLAEQFMELEN-TSLRVLLTGGDKLKRAVKK------PYTLVNNYGPTE-NTVVATSAE---IHPE 1352
Cdd:cd05929 218 TfAQFVPTmfvrllKLPEAVRNAYDlSSLKRVIHAAAPCPPWVKEqwidwgGPIIWEYYGGTEgQGLTIINGEewlTHPG 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1353 egslSIGRAIANtRVYILGEGNQVQPEGVAGELCVAGrGLARGYLNREDETAKRFVADPFVPgermyrTGDlVKWVNG-G 1431
Cdd:cd05929 298 ----SVGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAARNEGGWST------LGD-VGYLDEdG 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1432 IEYIG-RIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE------TADIEALKSTLKETLP 1504
Cdd:cd05929 365 YLYLTdRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPApgadagTALAEELIAFLRDRLS 444
|
490 500
....*....|....*....|....*..
gi 2214269206 1505 DYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:cd05929 445 RYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1634-1949 |
1.26e-11 |
|
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: 69.01 E-value: 1.26e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1634 LTPIQRWFFeknftnKHHWNQ--------SVMLHAKKGFDPERVEKTLQALIEHHDALRMVYREEN-GDIVQVYKPIGES 1704
Cdd:cd19536 4 LSSLQEGML------FHSLLNpggsvylhNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGlGQPVQVVHRQAQV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1705 KVsfEIVDLYGSDEEMLRSQiKLLANKLQSSLDLRNGPLLKAE-QYRTEAGDHLL-IAVHHLVVDGVSWRILLEDFASGY 1782
Cdd:cd19536 78 PV--TELDLTPLEEQLDPLR-AYKEETKIRRFDLGRAPLVRAAlVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVY 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1783 MQAEKEESLVFPQkTNSFKDW-AEELAAFSQSAHLLqqaeYWSQ-IAAEQVSPLPKDCET-----EQRIVKDTSSVLCEL 1855
Cdd:cd19536 155 NQLLEYKPLSLPP-AQPYRDFvAHERASIQQAASER----YWREyLAGATLATLPALSEAvgggpEQDSELLVSVPLPVR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1856 TAEDTKhlltdvhqPYGTEINDILLSALGLTMKEWTKGAKIGINLEGHGREDIIPNVNisRTVGWFTAQYPVVLDISDAD 1935
Cdd:cd19536 230 SRSLAK--------RSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAE--RLLGLFLNTLPLRVTLSEET 299
|
330
....*....|....
gi 2214269206 1936 ASAVIKTVKENLRR 1949
Cdd:cd19536 300 VEDLLKRAQEQELE 313
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1065-1531 |
1.54e-11 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 69.66 E-value: 1.54e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1065 HKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYI 1144
Cdd:PLN03102 27 YPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1145 LQDSGAKLL--------LKQEGISVPDSYTGD----VILL---DGSRTILSLPLDEN---DEGNPETAVTAENLAY---- 1202
Cdd:PLN03102 107 LRHAKPKILfvdrsfepLAREVLHLLSSEDSNlnlpVIFIheiDFPKRPSSEELDYEcliQRGEPTPSLVARMFRIqdeh 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1203 ----MIYTSGTTGQPKGVMVEHH-----ALVNLCFWHHDAFSMTAEDRSAkyagfgFDASIWEMfpTWTIGAE------- 1266
Cdd:PLN03102 187 dpisLNYTSGTTADPKGVVISHRgaylsTLSAIIGWEMGTCPVYLWTLPM------FHCNGWTF--TWGTAARggtsvcm 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1267 LHVIDEAIRLDIvrlndyfETNGVT-ITFLPT----QLAEQFMELENTSLRV-LLTGGDK-----LKRAVKKPYTLVNNY 1335
Cdd:PLN03102 259 RHVTAPEIYKNI-------EMHNVThMCCVPTvfniLLKGNSLDLSPRSGPVhVLTGGSPppaalVKKVQRLGFQVMHAY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1336 GPTENTVVATSAEIHPEEGSLSIGRAI---ANTRVYILGEG-----NQVQPEGVA------GELCVAGRGLARGYLNRED 1401
Cdd:PLN03102 332 GLTEATGPVLFCEWQDEWNRLPENQQMelkARQGVSILGLAdvdvkNKETQESVPrdgktmGEIVIKGSSIMKGYLKNPK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1402 ETAKRFvadpfvpGERMYRTGDL-VKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTA 1480
Cdd:PLN03102 412 ATSEAF-------KHGWLNTGDVgVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGET 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2214269206 1481 IAAYVTPETADIEALKSTLK-------------ETLPDYMIPAFWVTLNELPVTANGKVDRKAL 1531
Cdd:PLN03102 485 PCAFVVLEKGETTKEDRVDKlvtrerdlieycrENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
151-501 |
1.66e-11 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 68.15 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 151 AYVIYTSGTTGKPKGVQIE-----------HRNLTNYVSWF-----SEEAGLTendktVLLSSyafdlgytsmfpvLLGG 214
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTaaaltasadatHDRLGGPGQWLlalpaHHIAGLQ-----VLVRS-------------VIAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 215 GELHIVQKETYTAPDEIAHYIKE--HGITYIKLTPS-LFHTIVNTASFAKDANFESlrlIVLGGEKIiPTDVIAFRKMYG 291
Cdd:PRK07824 100 SEPVELDVSAGFDPTALPRAVAElgGGRRYTSLVPMqLAKALDDPAATAALAELDA---VLVGGGPA-PAPVLDAAAAAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 292 HTeFINHYGPTEATIGAIagrvdlYEpdafakrptiGRPIANAGALVLNealklvppgasGQLYITGQGLARGYLNRPQL 371
Cdd:PRK07824 176 IN-VVRTYGMSETSGGCV------YD----------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVDP 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 372 TAerFVEnpysPGslMYKTGDVvRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGL-QEL 450
Cdd:PRK07824 228 DP--FAE----PG--WFRTDDL-GALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLgQRV 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 451 CAYYTSDQD--IEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNAL 501
Cdd:PRK07824 299 VAAVVGDGGpaPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
33-414 |
1.80e-11 |
|
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: 69.41 E-value: 1.80e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAH-HLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVN 111
Cdd:cd17632 68 ITYAELWERVGAVAAaHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLAVS 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 112 ERNMTAIGQ---------------YE--------------------GIIVSLDDGKWRNESKERPSSI----SGSRNLAY 152
Cdd:cd17632 148 AEHLDLAVEavleggtpprlvvfdHRpevdahraalesarerlaavGIPVTTLTLIAVRGRDLPPAPLfrpePDDDPLAL 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 153 VIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVL----LSSYAfdlGYTSMFPVLLGGG------------- 215
Cdd:cd17632 228 LIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLnfmpMSHIA---GRISLYGTLARGGtayfaaasdmstl 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 216 --ELHIVQKETYTAPDEIAHYIKEHgitYIKLTPSLFHTIVNTASFAKDANFEsLRLIVLGGEKI--------IPTDVIA 285
Cdd:cd17632 305 fdDLALVRPTELFLVPRVCDMLFQR---YQAELDRRSVAGADAETLAERVKAE-LRERVLGGRLLaavcgsapLSAEMKA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 286 FRKMYGHTEFINHYGPTEATIGAIAGRVdlyepdafaKRPTigrpianagalVLNEALKLVP---------PGASGQLYI 356
Cdd:cd17632 381 FMESLLDLDLHDGYGSTEAGAVILDGVI---------VRPP-----------VLDYKLVDVPelgyfrtdrPHPRGELLV 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 357 TGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKI 414
Cdd:cd17632 441 KTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVMAELGPDRLVYVDRRNNVLKL 492
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1048-1527 |
1.82e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 69.99 E-value: 1.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1048 VPTDKTVHQLFEETVQRH-KDRPAVT-YNGQSWTYGELNAKANRLARILMDcGISPDDRVGVLTKPSLEMSAAVLGVLKA 1125
Cdd:PRK06814 627 SDYDRTLFEALIEAAKIHgFKKLAVEdPVNGPLTYRKLLTGAFVLGRKLKK-NTPPGENVGVMLPNANGAAVTFFALQSA 705
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1126 GaaFVP------------------------------IDPDYPDQRIEYIlqDSGAKLLLKQE---GISVPDSYTGdviLL 1172
Cdd:PRK06814 706 G--RVPaminfsagianilsackaaqvktvltsrafIEKARLGPLIEAL--EFGIRIIYLEDvraQIGLADKIKG---LL 778
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1173 DGSRtilslPLDENDEGNPETAvtaenlAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAK----YAGF 1248
Cdd:PRK06814 779 AGRF-----PLVYFCNRDPDDP------AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNalpvFHSF 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1249 GFDAS----IWEMFPTWTIGAELH--VIDEAIrldivrlndyFETNGvTI-----TFLpTQLAEQFMELENTSLRVLLTG 1317
Cdd:PRK06814 848 GLTGGlvlpLLSGVKVFLYPSPLHyrIIPELI----------YDTNA-TIlfgtdTFL-NGYARYAHPYDFRSLRYVFAG 915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1318 GDKLKRAVKKPYT------LVNNYGPTENT-VVATSAEIHPEEGSlsIGRAIAntrvyilGEGNQVQP-EGV--AGELCV 1387
Cdd:PRK06814 916 AEKVKEETRQTWMekfgirILEGYGVTETApVIALNTPMHNKAGT--VGRLLP-------GIEYRLEPvPGIdeGGRLFV 986
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1388 AGRGLARGYLnredETAKRFVADPfvPGERMYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQD 1466
Cdd:PRK06814 987 RGPNVMLGYL----RAENPGVLEP--PADGWYDTGDIVTIDEEGFITIkGRAKRFAKIAGEMISLAAVEELAAELWPDAL 1060
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 1467 AAVTAVKDKGGNTAIAAYVTPETADIEALKSTLKET-LPDYMIPAFWVTLNELPVTANGKVD 1527
Cdd:PRK06814 1061 HAAVSIPDARKGERIILLTTASDATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
22-500 |
2.31e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 69.00 E-value: 2.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 22 DHSAVKAGGNL-LTYRELDEQANQLAHHLRaQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPI-DPDTP--EERIR 97
Cdd:PRK12476 57 DHSHSAAGCAVeLTWTQLGVRLRAVGARLQ-QVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLD 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 98 YSLEDS--------GAKFAVVNE--RNMTAIGQYEGIIVSlddgkwrneskERPSSISGS--------RNLAYVIYTSGT 159
Cdd:PRK12476 136 TALRDAeptvvlttTAAAEAVEGflRNLPRLRRPRVIAID-----------AIPDSAGESfvpveldtDDVSHLQYTSGS 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 160 TGKPKGVQIEHRNL-TNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTS-MFPVLLGGgelHIvqkeTYTAPDEIAH---- 233
Cdd:PRK12476 205 TRPPVGVEITHRAVgTNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMiGFPAVYGG---HS----TLMSPTAFVRrpqr 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 234 YIKE------HGITyIKLTPSLFHTIVNTASFAKDANFESLRLIVL--GGEKIIPTDVIAFRKM---YG--HTEFINHYG 300
Cdd:PRK12476 278 WIKAlsegsrTGRV-VTAAPNFAYEWAAQRGLPAEGDDIDLSNVVLiiGSEPVSIDAVTTFNKAfapYGlpRTAFKPSYG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 301 PTEATI-----------GAI-----------AGRVDLYEPDAFAKrPTIGRPIANAGALVLNEALKL-VPPGASGQLYIT 357
Cdd:PRK12476 357 IAEATLfvatiapdaepSVVyldreqlgagrAVRVAADAPNAVAH-VSCGQVARSQWAVIVDPDTGAeLPDGEVGEIWLH 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 358 GQGLARGYLNRPQLTAERF---VENPYSPGS---------LMYKTGDVVRRLsDGTLAFIGRADDQVKIRGYRIEPKEIE 425
Cdd:PRK12476 436 GDNIGRGYWGRPEETERTFgakLQSRLAEGShadgaaddgTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIE 514
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 426 -TVMLSLSGIQEAVVLA--VSEGGLQELC-----AYYTSDQD----IE--KAELRYQlsltlpsHMIPAF---FVQVDAI 488
Cdd:PRK12476 515 aTVAEASPMVRRGYVTAftVPAEDNERLVivaerAAGTSRADpapaIDaiRAAVSRR-------HGLAVAdvrLVPAGAI 587
|
570
....*....|..
gi 2214269206 489 PLTANGKTDRNA 500
Cdd:PRK12476 588 PRTTSGKLARRA 599
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
33-508 |
3.98e-11 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 68.39 E-value: 3.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAA----FLPIDPDTPEERI------------ 96
Cdd:PLN02654 121 LTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVhsvvFAGFSAESLAQRIvdckpkvvitcn 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 97 -------RYSLEDSGAKFAVVNERNMTAIG---QYEG-IIVSLDDGKWRNESK--------ERPSSIS----GSRNLAYV 153
Cdd:PLN02654 201 avkrgpkTINLKDIVDAALDESAKNGVSVGiclTYENqLAMKREDTKWQEGRDvwwqdvvpNYPTKCEvewvDAEDPLFL 280
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 154 IYTSGTTGKPKGVQiehRNLTNYVSWfseeagltendkTVLLSSYAFDL------------------GYTSMFPVLLGGG 215
Cdd:PLN02654 281 LYTSGSTGKPKGVL---HTTGGYMVY------------TATTFKYAFDYkptdvywctadcgwitghSYVTYGPMLNGAT 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 216 ELHIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTAS-FAKDANFESLRLIVLGGEKIIPTdviAFRkmyghtE 294
Cdd:PLN02654 346 VLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDeYVTRHSRKSLRVLGSVGEPINPS---AWR------W 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 295 FINHYGPTEATIG------AIAGRVDLYEPDAFAKRP-TIGRPIANAGALVLNEALKLVPPGASGQLYITGQ--GLARGY 365
Cdd:PLN02654 417 FFNVVGDSRCPISdtwwqtETGGFMITPLPGAWPQKPgSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSwpGAFRTL 496
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 366 LNrpqlTAERFVENPYSPGSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVS-E 444
Cdd:PLN02654 497 YG----DHERYETTYFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEhE 572
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 445 GGLQELCAYYTSDQDIE-KAELRYQLSLTLPSHMipAFFVQVDAI------PLTANGKTDRNALPKPNAAQ 508
Cdd:PLN02654 573 VKGQGIYAFVTLVEGVPySEELRKSLILTVRNQI--GAFAAPDKIhwapglPKTRSGKIMRRILRKIASRQ 641
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1453-1525 |
4.03e-11 |
|
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: 60.64 E-value: 4.03e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 1453 EIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYVTPE---TADIEALKSTLKETLPDYMIPAFWVTLNELPVTANGK 1525
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKpgvELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1662-1825 |
1.79e-10 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. 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 Cyc-domains. 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: 380458 [Multi-domain] Cd Length: 423 Bit Score: 65.59 E-value: 1.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1662 KGFDPERVEKTLQALIEHHDALRMVYrEENGD--IV-QVYKPIgeskvsFEIVDLYGSDEEMLRSQIKLLANKL-QSSLD 1737
Cdd:cd19535 35 EDLDPDRLERAWNKLIARHPMLRAVF-LDDGTqqILpEVPWYG------ITVHDLRGLSEEEAEAALEELRERLsHRVLD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1738 LRNGP-------LLKAEQYRteagdhLLIAVHHLVVDGVSWRILLEDFASGYMQAEKEeslvFPQKTNSFKDWAEELAAF 1810
Cdd:cd19535 108 VERGPlfdirlsLLPEGRTR------LHLSIDLLVADALSLQILLRELAALYEDPGEP----LPPLELSFRDYLLAEQAL 177
|
170
....*....|....*.
gi 2214269206 1811 SQSAHllQQA-EYWSQ 1825
Cdd:cd19535 178 RETAY--ERArAYWQE 191
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1067-1526 |
1.55e-09 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 62.72 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1067 DRPAVTY--NGQSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYI 1144
Cdd:PRK13390 12 DRPAVIVaeTGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1145 LQDSGAKLLLKQ---EGISVPDSYTGDVILLDGSRTilslpldeNDEGNPETAVTAENL--------AYMIYTSGTTGQP 1213
Cdd:PRK13390 92 VGDSGARVLVASaalDGLAAKVGADLPLRLSFGGEI--------DGFGSFEAALAGAGPrlteqpcgAVMLYSSGTTGFP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1214 KGVMVEhhalvnLCFWHHDAfsmtAEDRSAKYAGFGFD----------ASIWEMFP-TWTigAELHVIDEAI----RLDI 1278
Cdd:PRK13390 164 KGIQPD------LPGRDVDA----PGDPIVAIARAFYDisesdiyyssAPIYHAAPlRWC--SMVHALGGTVvlakRFDA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1279 VRLNDYFETNGVTIT-FLPTQL-------AEQFMELENTSLRVLLTGGDKLKRAVKkpYTLVNNYGP--------TEN-- 1340
Cdd:PRK13390 232 QATLGHVERYRITVTqMVPTMFvrllkldADVRTRYDVSSLRAVIHAAAPCPVDVK--HAMIDWLGPivyeyyssTEAhg 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1341 -TVVATSAEI-HPEegslSIGRAIANTRVYILGEGNQVqPEGVAGELCVAGRGLARGYLNREDETAK-RFVADPFvpger 1417
Cdd:PRK13390 310 mTFIDSPDWLaHPG----SVGRSVLGDLHICDDDGNEL-PAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPF----- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1418 MYRTGDLVKWVNGGIEYIG-RIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAyVTPETADIEALK 1496
Cdd:PRK13390 380 WTTVGDLGSVDEDGYLYLAdRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKA-VIQLVEGIRGSD 458
|
490 500 510
....*....|....*....|....*....|....*..
gi 2214269206 1497 STLKE-------TLPDYMIPAFWVTLNELPVTANGKV 1526
Cdd:PRK13390 459 ELARElidytrsRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
7-407 |
2.00e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 62.59 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 7 ATFAALFEKQAQQTPDHSAV-KAGGN----LLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAG 81
Cdd:PRK08180 39 RRLTDRLVHWAQEAPDRVFLaERGADggwrRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 82 AAFLPIDP-----DTPEERIRYSLE---------DSGAKFA------------VVNERNMTAigqyEGIIVSLDDGKWRN 135
Cdd:PRK08180 119 VPYAPVSPayslvSQDFGKLRHVLElltpglvfaDDGAAFAralaavvpadveVVAVRGAVP----GRAATPFAALLATP 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 136 ESKE--------RPSSIsgsrnlAYVIYTSGTTGKPKGVQIEHRNLT-NyvswfseeagltendKTVLLSSYAFdLGYTS 206
Cdd:PRK08180 195 PTAAvdaahaavGPDTI------AKFLFTSGSTGLPKAVINTHRMLCaN---------------QQMLAQTFPF-LAEEP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 207 mfPVLL---------GGGelHIVqketytapdeiaHYIKEHGIT-YI---KLTPSLFH-TIVN------TASFA------ 260
Cdd:PRK08180 253 --PVLVdwlpwnhtfGGN--HNL------------GIVLYNGGTlYIddgKPTPGGFDeTLRNlreispTVYFNvpkgwe 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 261 -------KDAN-----FESLRLIVLGGEKiIPTDViaFRKMYGHTE--------FINHYGPTEATIGAIagrvdlyepda 320
Cdd:PRK08180 317 mlvpaleRDAAlrrrfFSRLKLLFYAGAA-LSQDV--WDRLDRVAEatcgerirMMTGLGMTETAPSAT----------- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 321 FAKRPT-----IGRPIANAgalvlneALKLVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVR 395
Cdd:PRK08180 383 FTTGPLsragnIGLPAPGC-------EVKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVR 449
|
490
....*....|....*..
gi 2214269206 396 -----RLSDGtLAFIGR 407
Cdd:PRK08180 450 fvdpaDPERG-LMFDGR 465
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
1415-1532 |
2.45e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 61.98 E-value: 2.45e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1415 GERMYRTGDLVKWV-NGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDK-GGNTAIAAYVTPETADI 1492
Cdd:PRK08308 289 GDKEIFTKDLGYKSeRGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPvAGERVKAKVISHEEIDP 368
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 2214269206 1493 EALKSTLKETLPDYMIPAFWVTLNELPVTANGKVDRKALP 1532
Cdd:PRK08308 369 VQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1203-1528 |
3.87e-09 |
|
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: 60.75 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1203 MIYTSGTTGQPKGVMVEHHALV--NLCFWHhdAFSMTAEDRSAK------YAGFGFdasiweMFPTWTIGAeLHVIDEai 1274
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIaaNLQLIH--AMGLTEADVYLNmlplfhIAGLNL------ALATFHAGG-ANVVME-- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1275 RLDIVRLNDYFETNGVTI--TFLP--TQLAEqfmELENT-----SLRVL--LTGGDKLKRAVKK-PYTLVNNYGPTENTV 1342
Cdd:cd17637 74 KFDPAEALELIEEEKVTLmgSFPPilSNLLD---AAEKSgvdlsSLRHVlgLDAPETIQRFEETtGATFWSLYGQTETSG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1343 VATSAEIhpEEGSLSIGRAIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFVADpfvpgerMYRTG 1422
Cdd:cd17637 151 LVTLSPY--RERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WHHTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1423 DLVKWVNGG-IEYIGRIDQQ--VKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAY-VTPETADIEA--LK 1496
Cdd:cd17637 222 DLGRFDEDGyLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVcVLKPGATLTAdeLI 301
|
330 340 350
....*....|....*....|....*....|..
gi 2214269206 1497 STLKETLPDYMIPAFWVTLNELPVTANGKVDR 1528
Cdd:cd17637 302 EFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1640-1825 |
6.36e-09 |
|
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: 60.41 E-value: 6.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1640 WFFEKNFTNKHHWNQSVMLHAKKGFDPERVEKTLQALIEHHDALRMVYREENGDIVQVYKPigESKVSFEIVDLYGSDEE 1719
Cdd:cd20484 12 WMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEP--SKPLSFQEEDISSLKES 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1720 MLrsqIKLLANKLQSSLDLRNGPLLKAEQY-RTEAGDHLLIAVHHLVVDGVSWRILLEDFASGY---MQAEKEESLVFPQ 1795
Cdd:cd20484 90 EI---IAYLREKAKEPFVLENGPLMRVHLFsRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYqalLQGKQPTLASSPA 166
|
170 180 190
....*....|....*....|....*....|.
gi 2214269206 1796 KTNSFKDWAEE-LAAFSQSAHLLqqaeYWSQ 1825
Cdd:cd20484 167 SYYDFVAWEQDmLAGAEGEEHRA----YWKQ 193
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
299-503 |
6.63e-09 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 60.78 E-value: 6.63e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 299 YGPTEAtigaiAGRVDLYEPDAF-AKRPTIGRPIANAgalvlneALKLVPpGASGQLYITGQGLARGYLnrPQLTAerfv 377
Cdd:PRK07445 261 YGMTET-----ASQIATLKPDDFlAGNNSSGQVLPHA-------QITIPA-NQTGNITIQAQSLALGYY--PQILD---- 321
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 378 enpySPGSLmyKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAV--SEGGLQELCAYYT 455
Cdd:PRK07445 322 ----SQGIF--ETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLpdPHWGEVVTAIYVP 395
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2214269206 456 SDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALPK 503
Cdd:PRK07445 396 KDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
34-507 |
6.70e-09 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 60.92 E-value: 6.70e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSL---ED-------- 102
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIGAICHTVNPRLFPEQIAWIInhaEDrvvitdlt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 103 -------------SGAKFAVVNER---------NMTAigqYEGIIVSLD-DGKWRNESKerpssisgsRNLAYVIYTSGT 159
Cdd:PRK06018 121 fvpilekiadklpSVERYVVLTDAahmpqttlkNAVA---YEEWIAEADgDFAWKTFDE---------NTAAGMCYTSGT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 160 TGKPKGVQIEHRN--LTNYVSWFSEEAGLTENDKTV----LLSSYAFDLGYT--SMFPVLLGGG---------ELHIVQK 222
Cdd:PRK06018 189 TGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLpvvpLFHANSWGIAFSapSMGTKLVMPGakldgasvyELLDTEK 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 223 ETYTAPdeiahyikehgityiklTPSLFHTIVNTASfAKDANFESLRLIVLGGEKIiPTDVI-AFRKMygHTEFINHYGP 301
Cdd:PRK06018 269 VTFTAG-----------------VPTVWLMLLQYME-KEGLKLPHLKMVVCGGSAM-PRSMIkAFEDM--GVEVRHAWGM 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 302 TE----ATIGAIAGRVDLYEPDA-FAKRPTIGRPIANAGALVLNEALKLVP--PGASGQLYITGQGLARGYL--NRPQLT 372
Cdd:PRK06018 328 TEmsplGTLAALKPPFSKLPGDArLDVLQKQGYPPFGVEMKITDDAGKELPwdGKTFGRLKVRGPAVAAAYYrvDGEILD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 373 AERFvenpyspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEAVVLAVSEGGLQE--- 449
Cdd:PRK06018 408 DDGF-----------FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDErpl 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 450 LCAYYTSDQDIEKAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGKTDRNALPK-------PNAA 507
Cdd:PRK06018 477 LIVQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALREqfkdyklPTAA 541
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1101-1446 |
7.84e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 60.90 E-value: 7.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1101 PDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPI-DPDYPDQ--RIEYILQDSGAKLLLKQ----EGI-----SVPDSYTGD 1168
Cdd:PRK07769 78 PGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCTPSAILTTtdsaEGVrkffrARPAKERPR 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1169 VILLDgsrtilSLPlDENDEGNPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVNLCFWHHDAFSMTAEDRSAKYAGF 1248
Cdd:PRK07769 158 VIAVD------AVP-DEVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPF 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1249 GFDAS-IWEMFPTwTIGAELHVIDEA---------IRLDIVRLNDYFETNGVTITF---------LPTQlAEQFMELENt 1309
Cdd:PRK07769 231 FHDMGlITVLLPA-LLGHYITFMSPAafvrrpgrwIRELARKPGGTGGTFSAAPNFafehaaargLPKD-GEPPLDLSN- 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1310 sLRVLLTGGDKLKRA-VKK------PYTLVN-----NYGPTENT--VVATSAE-----IHPEEGSLSIGR---------- 1360
Cdd:PRK07769 308 -VKGLLNGSEPVSPAsMRKfneafaPYGLPPtaikpSYGMAEATlfVSTTPMDeeptvIYVDRDELNAGRfvevpadapn 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1361 ----------AIANTRVYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFV-----------ADPFVPGERMY 1419
Cdd:PRK07769 387 avaqvsagkvGVSEWAVIVDPETASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFQnilksrlseshAEGAPDDALWV 466
|
410 420
....*....|....*....|....*..
gi 2214269206 1420 RTGDLVKWVNGGIEYIGRIDQQVKVRG 1446
Cdd:PRK07769 467 RTGDYGVYFDGELYITGRVKDLVIIDG 493
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1063-1438 |
1.27e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 59.89 E-value: 1.27e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1063 QRHKDRPAVTYNGQS--W---TYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDY- 1136
Cdd:PRK08180 50 QEAPDRVFLAERGADggWrrlTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYs 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1137 -PDQ---RIEYILQ---------DSGAKLllkQEGISVPDSYTGDVILL---DGSRTILSL-------PLDENDEGNPet 1193
Cdd:PRK08180 130 lVSQdfgKLRHVLElltpglvfaDDGAAF---ARALAAVVPADVEVVAVrgaVPGRAATPFaallatpPTAAVDAAHA-- 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1194 AVTAENLAYMIYTSGTTGQPKGVMVEHHAL------VNLCF---------------WHHDA-----FSMTAEDRSAKY-- 1245
Cdd:PRK08180 205 AVGPDTIAKFLFTSGSTGLPKAVINTHRMLcanqqmLAQTFpflaeeppvlvdwlpWNHTFggnhnLGIVLYNGGTLYid 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1246 -----AGfGFDASI---WEMFPTW----TIGAELhvideairldivrLNDYFETNGvtitflptQLAEQFMElentSLRV 1313
Cdd:PRK08180 285 dgkptPG-GFDETLrnlREISPTVyfnvPKGWEM-------------LVPALERDA--------ALRRRFFS----RLKL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1314 LLTGG--------DKL----KRAVKKPYTLVNNYGPTENTVVATSaeIH-PEEGSLSIGRAIAntrvyilgeGNQVQ--P 1378
Cdd:PRK08180 339 LFYAGaalsqdvwDRLdrvaEATCGERIRMMTGLGMTETAPSATF--TTgPLSRAGNIGLPAP---------GCEVKlvP 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 1379 EGVAGELCVAGRGLARGYLNREDETAKRFVADPFvpgermYRTGDLVKWV-----NGGIEYIGRI 1438
Cdd:PRK08180 408 VGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY------YRSGDAVRFVdpadpERGLMFDGRI 466
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
153-429 |
1.31e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 60.12 E-value: 1.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 153 VIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLS----SYAFDlgYTSMFPVLLGGGELHI-------VQ 221
Cdd:PTZ00342 309 IVYTSGTSGKPKGVMLSNKNLYNTVVPLCKHSIFKKYNPKTHLSylpiSHIYE--RVIAYLSFMLGGTINIwskdinyFS 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 222 KETYTAPDEIA-------HYIKEHGITYIKLTPSLFHTIV----------NTASFA-------------KDANFESLRLI 271
Cdd:PTZ00342 387 KDIYNSKGNILagvpkvfNRIYTNIMTEINNLPPLKRFLVkkilslrksnNNGGFSkflegithisskiKDKVNPNLEVI 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 272 VLGGEKIIPtDVIAFRKMYGHTEFINHYGPTEATiGAIAGR-VDLYEPDafakrpTIGRPIANagalvlNEALKLV---- 346
Cdd:PTZ00342 467 LNGGGKLSP-KIAEELSVLLNVNYYQGYGLTETT-GPIFVQhADDNNTE------SIGGPISP------NTKYKVRtwet 532
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 347 ------PPgaSGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGRADDQVKIRgyriE 420
Cdd:PTZ00342 533 ykatdtLP--KGELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRSKGLVKLS----Q 600
|
....*....
gi 2214269206 421 PKEIETVML 429
Cdd:PTZ00342 601 GEYIETDML 609
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
511-586 |
1.43e-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: 53.79 E-value: 1.43e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 511 GKALAAPETALEESLCRIWQKTLGI---EAIGIDDNFFDLGGHSLKGMMLIANIQAELEKSVPLKALFEQPTVRQLAAY 586
Cdd:smart00823 3 ALPPAERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEH 81
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
156-470 |
1.66e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 59.39 E-value: 1.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 156 TSGTTGKPKGV-----------QIEHRNLTNyvswfseeAGLTENDKTVLLSSYAF------------DLGYTsMFPVll 212
Cdd:COG1541 91 SSGTTGKPTVVgytrkdldrwaELFARSLRA--------AGVRPGDRVQNAFGYGLftgglglhygaeRLGAT-VIPA-- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 213 GGGElhivqketytaPDEIAHYIKEHGITYIKLTPSLFHTIvntASFAKDANFE----SLRLIVLGGEKIIPTDVIAFRK 288
Cdd:COG1541 160 GGGN-----------TERQLRLMQDFGPTVLVGTPSYLLYL---AEVAEEEGIDprdlSLKKGIFGGEPWSEEMRKEIEE 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 289 MYGhTEFINHYGPTEATIGaIAgrvdlYE----------PDAFAkrPTIGRPianagalvlnEALKLVPPGASGQLYITG 358
Cdd:COG1541 226 RWG-IKAYDIYGLTEVGPG-VA-----YEceaqdglhiwEDHFL--VEIIDP----------ETGEPVPEGEEGELVVTT 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 359 qglargylnrpqLTAErfvenpyspGSLM--YKTGDVVRRLSDG-----TLAFI----GRADDQVKIRGYRIEPKEIETV 427
Cdd:COG1541 287 ------------LTKE---------AMPLirYRTGDLTRLLPEPcpcgrTHPRIgrilGRADDMLIIRGVNVFPSQIEEV 345
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 2214269206 428 MLSLSGIQEAVVLAVS-EGGLQELCAYYTSDQDIEKAELRYQLS 470
Cdd:COG1541 346 LLRIPEVGPEYQIVVDrEGGLDELTVRVELAPGASLEALAEAIA 389
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1036-1229 |
2.19e-08 |
|
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: 59.39 E-value: 2.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1036 ALLEAWKGKALPVPtdktvhQLFEETVQRHKDRPAV---------------TYNGQSW-----TYGELNAKANRLARIL- 1094
Cdd:cd17632 12 AVTEAIRRPGLRLA------QIIATVMTGYADRPALgqratelvtdpatgrTTLRLLPrfetiTYAELWERVGAVAAAHd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1095 MDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLL--------LKQEgiSVPDSYT 1166
Cdd:cd17632 86 PEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLavsaehldLAVE--AVLEGGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1167 GDVIL--------------LDGSR----------TILSLPLDENDEGNP----ETAVTAENLAYMIYTSGTTGQPKGVMV 1218
Cdd:cd17632 164 PPRLVvfdhrpevdahraaLESARerlaavgipvTTLTLIAVRGRDLPPaplfRPEPDDDPLALLIYTSGSTGTPKGAMY 243
|
250
....*....|.
gi 2214269206 1219 EHHALVNlcFW 1229
Cdd:cd17632 244 TERLVAT--FW 252
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
152-429 |
2.23e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 59.37 E-value: 2.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 152 YVIYTSGTTGKPKGVQieHRNLTNYV----SWFSeeagLTENDKTVLLSSYAfDLGYTSM---FPVLLGGGELHIVQKET 224
Cdd:PTZ00237 258 YILYTSGTTGNSKAVV--RSNGPHLVglkyYWRS----IIEKDIPTVVFSHS-SIGWVSFhgfLYGSLSLGNTFVMFEGG 330
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 225 YTAPDEIAHY----IKEHGITYIKLTPSLFHTIVNTASFAKDA----NFESLRLIVLGGEKI---IPtDVIAfRKMygHT 293
Cdd:PTZ00237 331 IIKNKHIEDDlwntIEKHKVTHTLTLPKTIRYLIKTDPEATIIrskyDLSNLKEIWCGGEVIeesIP-EYIE-NKL--KI 406
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 294 EFINHYGPTEATIGAIAGRVDLYEPDAFAKRPTIG-RP-IANAGALVLNE------ALKL-VPPGASGQLYitgqglarg 364
Cdd:PTZ00237 407 KSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFiKPsILSEDGKELNVneigevAFKLpMPPSFATTFY--------- 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2214269206 365 ylNRPQLTAERFVENP--YSPGSLMYKTgdvvrrlSDGTLAFIGRADDQVKIRGYRIEPKEIETVML 429
Cdd:PTZ00237 478 --KNDEKFKQLFSKFPgyYNSGDLGFKD-------ENGYYTIVSRSDDQIKISGNKVQLNTIETSIL 535
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
423-495 |
2.26e-08 |
|
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: 52.93 E-value: 2.26e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 423 EIETVMLSLSGIQEAVVLAVS-EGGLQELCAYYTSDQDIE--KAELRYQLSLTLPSHMIPAFFVQVDAIPLTANGK 495
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPdELKGEAPVAFVVLKPGVEllEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1038-1530 |
2.31e-08 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 59.37 E-value: 2.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1038 LEAWKGKALPVPTdkTVHQLFEETVQRHKDRPAVTY-------NGQ----SWTY--GELNAKANRLARIlmdcgISPDDR 1104
Cdd:PRK12476 22 LDADGNIALPPGT--TLISLIERNIANVGDTVAYRYldhshsaAGCavelTWTQlgVRLRAVGARLQQV-----AGPGDR 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1105 VGVLTKPSLEMSAAVLGVLKAGAAFVPI-DPDYPD--QRIEYILQDSGAKLLLKQEgiSVPDSYTGDVILLDGSRTILSL 1181
Cdd:PRK12476 95 VAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPGhaERLDTALRDAEPTVVLTTT--AAAEAVEGFLRNLPRLRRPRVI 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1182 PLDENDEGNPETAVTAE----NLAYMIYTSGTTGQPKGVMVEHHAL-VNL----------------CFW---HHD-AFSM 1236
Cdd:PRK12476 173 AIDAIPDSAGESFVPVEldtdDVSHLQYTSGSTRPPVGVEITHRAVgTNLvqmilsidlldrnthgVSWlplYHDmGLSM 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1237 taedrsakyagFGFDA----SIWEMFPTWTIGAELHVIDEairldivrLNDYfETNGVTITFLPTqlaeqfMELENTSLR 1312
Cdd:PRK12476 253 -----------IGFPAvyggHSTLMSPTAFVRRPQRWIKA--------LSEG-SRTGRVVTAAPN------FAYEWAAQR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1313 VLLTGGDKLK---------------RAVKK------PYTLVNN-----YGPTENTV-VAT---SAE---IHPEEGSLSIG 1359
Cdd:PRK12476 307 GLPAEGDDIDlsnvvliigsepvsiDAVTTfnkafaPYGLPRTafkpsYGIAEATLfVATiapDAEpsvVYLDREQLGAG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1360 RA------------------IANTR--VYILGEGNQVQPEGVAGELCVAGRGLARGYLNREDETAKRFV----------- 1408
Cdd:PRK12476 387 RAvrvaadapnavahvscgqVARSQwaVIVDPDTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGaklqsrlaegs 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1409 -ADPFVPGERMYRTGDLVKWVNGGIEYIGRIDQQVKVRGYRIELSEIEVQLAQLSEVQD----AAVTAVKDKGGNTAIAA 1483
Cdd:PRK12476 467 hADGAADDGTWLRTGDLGVYLDGELYITGRIADLIVIDGRNHYPQDIEATVAEASPMVRrgyvTAFTVPAEDNERLVIVA 546
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 1484 YVTPET--AD----IEALKSTL--KETLP--DY-MIPAfwvtlNELPVTANGKVDRKA 1530
Cdd:PRK12476 547 ERAAGTsrADpapaIDAIRAAVsrRHGLAvaDVrLVPA-----GAIPRTTSGKLARRA 599
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
1194-1503 |
2.32e-08 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 58.62 E-value: 2.32e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1194 AVTAENLAYMIYTSGTTGQPKGVM-----VEHHA-LVNLCFWhhdAFSMTAEDR---SAKY----AGFGFDASIWEM--- 1257
Cdd:COG1541 79 AVPLEEIVRIHASSGTTGKPTVVGytrkdLDRWAeLFARSLR---AAGVRPGDRvqnAFGYglftGGLGLHYGAERLgat 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1258 -FPTWTIGAELHVidEAIRLdivrlndyFETNGVTITflPTQL-------AEQFMELENTSLRVLLTGG----DKLKRAV 1325
Cdd:COG1541 156 vIPAGGGNTERQL--RLMQD--------FGPTVLVGT--PSYLlylaevaEEEGIDPRDLSLKKGIFGGepwsEEMRKEI 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1326 KKPY--TLVNNYGptentvvatSAEIHPeegslsigraiantrvyilgegnqvqpeGVAGElCVAGRGLargYLNrED-- 1401
Cdd:COG1541 224 EERWgiKAYDIYG---------LTEVGP----------------------------GVAYE-CEAQDGL---HIW-EDhf 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1402 -------ETAkrfvaDPFVPGER------------M----YRTGDLVKWVNGG---------IEYI-GRIDQQVKVRGYR 1448
Cdd:COG1541 262 lveiidpETG-----EPVPEGEEgelvvttltkeaMplirYRTGDLTRLLPEPcpcgrthprIGRIlGRADDMLIIRGVN 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 1449 IELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYV-TPETADIEALKSTLKETL 1503
Cdd:COG1541 337 VFPSQIEEVLLRIPEVGPEYQIVVDREGGLDELTVRVeLAPGASLEALAEAIAAAL 392
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1066-1227 |
2.48e-08 |
|
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: 58.90 E-value: 2.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1066 KDRPAVTYngqswTYGELNAKANRLARILMD-CGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYI 1144
Cdd:cd05905 8 KGKEATTL-----TWGKLLSRAEKIAAVLQKkVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1145 LQDSGAKL------LLKQEGISVPDSYTGDVI--------LLDGSRTILSLPLDENDEGNPETAvTAENLAYMIYTSGTT 1210
Cdd:cd05905 83 LGTCKVRValtveaCLKGLPKKLLKSKTAAEIakkkgwpkILDFVKIPKSKRSKLKKWGPHPPT-RDGDTAYIEYSFSSD 161
|
170
....*....|....*..
gi 2214269206 1211 GQPKGVMVEHHALVNLC 1227
Cdd:cd05905 162 GSLSGVAVSHSSLLAHC 178
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1550-1617 |
3.04e-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: 52.64 E-value: 3.04e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 1550 MEELLAGIWQDVLGMS---EVGVTDNFFSLGGDSIKGIQMASRLNQH-GWKLEMKDLFQHPTIEELTQYVER 1617
Cdd:smart00823 13 LLDLVREQVAAVLGHAaaeAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1079-1224 |
7.64e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 57.31 E-value: 7.64e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1079 TYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDS-------GAK 1151
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAEDTlrvigmiGAK 110
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 1152 LLLkqegisVPDSYTGDVILLDGsRTILSLPLDENDEGNPETAV--TAENLAYMIYTSGTTGQPKGVMVEHHALV 1224
Cdd:PRK07768 111 AVV------VGEPFLAAAPVLEE-KGIRVLTVADLLAADPIDPVetGEDDLALMQLTSGSTGSPKAVQITHGNLY 178
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1074-1495 |
7.73e-08 |
|
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: 57.22 E-value: 7.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1074 NGQSW-TYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKl 1152
Cdd:cd17639 1 GEYKYmSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1153 llkqegisvpdsytgdVILLDGSrtilslpldendegnpetavtAENLAYMIYTSGTTGQPKGVMVEHHALV-------- 1224
Cdd:cd17639 80 ----------------AIFTDGK---------------------PDDLACIMYTSGSTGNPKGVMLTHGNLVagiaglgd 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1225 NLCFWHHDA------------FSMTAED----RSAKyAGFG-----FDAS-------IWEMFPTWTIGAELhvIDEAIRL 1276
Cdd:cd17639 123 RVPELLGPDdrylaylplahiFELAAENvclyRGGT-IGYGsprtlTDKSkrgckgdLTEFKPTLMVGVPA--IWDTIRK 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1277 DIV-RLND-------YFET----------NGVTITFLPTQLAEQFMELENTSLRVLLTGGDKLKRAVKKPYTLV-----N 1333
Cdd:cd17639 200 GVLaKLNPmgglkrtLFWTayqsklkalkEGPGTPLLDELVFKKVRAALGGRLRYMLSGGAPLSADTQEFLNIVlcpviQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1334 NYGPTENTVVATSAEI-HPEEGSlsIGRAIANTRVYILG--EGNQV--QPEGvAGELCVAGRGLARGYLNREDETAKRFV 1408
Cdd:cd17639 280 GYGLTETCAGGTVQDPgDLETGR--VGPPLPCCEIKLVDweEGGYStdKPPP-RGEILIRGPNVFKGYYKNPEKTKEAFD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1409 ADpfvpgeRMYRTGDLVKWV-NGGIEYIGRIDQQVKVR-GYRIELSEIEVQLAQLSEVQDAAVTAVKDKggnTAIAAYVT 1486
Cdd:cd17639 357 GD------GWFHTGDIGEFHpDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDK---SYPVAIVV 427
|
....*....
gi 2214269206 1487 PETADIEAL 1495
Cdd:cd17639 428 PNEKHLTKL 436
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1673-1782 |
7.91e-08 |
|
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: 57.05 E-value: 7.91e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1673 LQALIEHHDALRMVYREENGDIVQVYKPIGESKVSFEIVDLygsDEEMLRSQiklLANKLQSSLDLRNGPLLKAEQYRTE 1752
Cdd:cd19540 45 LADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDLTVVDV---TEDELAAR---LAEAARRGFDLTAELPLRARLFRLG 118
|
90 100 110
....*....|....*....|....*....|.
gi 2214269206 1753 AGDH-LLIAVHHLVVDGVSWRILLEDFASGY 1782
Cdd:cd19540 119 PDEHvLVLVVHHIAADGWSMAPLARDLATAY 149
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1198-1455 |
8.35e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 57.13 E-value: 8.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1198 ENLAYMIYTSGTTGQPKGVMVEHHALV---NLCFwhhDAFSMTAEDRSAKYA----GFGFDASiwEMFPtwtIGAELHVI 1270
Cdd:PRK06334 183 EDVAVILFTSGTEKLPKGVPLTHANLLanqRACL---KFFSPKEDDVMMSFLppfhAYGFNSC--TLFP---LLSGVPVV 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1271 DEAIRLD---IVRLND-----YFETNGVTITFLPTQLAEQFMELEntSLRVLLTGGDKLKRA----VKKPY---TLVNNY 1335
Cdd:PRK06334 255 FAYNPLYpkkIVEMIDeakvtFLGSTPVFFDYILKTAKKQESCLP--SLRFVVIGGDAFKDSlyqeALKTFphiQLRQGY 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1336 GPTENTVVATSAEIHPEEGSLSIGRAIANTRVYILGEGNQVQ-PEGVAGELCVAGRGLARGYLNrEDETaKRFVAdpfVP 1414
Cdd:PRK06334 333 GTTECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKVPvSSGETGLVLTRGTSLFSGYLG-EDFG-QGFVE---LG 407
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2214269206 1415 GERMYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIE 1455
Cdd:PRK06334 408 GETWYVTGDLGYVDRHGELFLkGRLSRFVKIGAEMVSLEALE 449
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
34-427 |
1.34e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 56.95 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 34 TYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNER 113
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSIVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 114 N--------------MTAIGQYEGI--------------IVSLDDGKWRNESKERPSSISGSRNLAYVIYTSGTTGKPKG 165
Cdd:PLN02614 161 KiselfktcpnsteyMKTVVSFGGVsreqkeeaetfglvIYAWDEFLKLGEGKQYDLPIKKKSDICTIMYTSGTTGDPKG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 166 VQIEHRNLTN---------------------YVSWFS---------EEA--------GLTENDKTVLLSSYA-------- 199
Cdd:PLN02614 241 VMISNESIVTliagvirllksanaaltvkdvYLSYLPlahifdrviEECfiqhgaaiGFWRGDVKLLIEDLGelkptifc 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 200 -----FDLGYTSMFPVLLGGGelhIVQKETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNTASFAKDANFEslrlIVLG 274
Cdd:PLN02614 321 avprvLDRVYSGLQKKLSDGG---FLKKFVFDSAFSYKFGNMKKGQSHVEASPLCDKLVFNKVKQGLGGNVR----IILS 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 275 GEKIIPTDVIAFRKMYGHTEFINHYGPTEATIGAIAGRvdlyePDAFAKRPTIGRPIANagalvLNEALKLVP------- 347
Cdd:PLN02614 394 GAAPLASHVESFLRVVACCHVLQGYGLTESCAGTFVSL-----PDELDMLGTVGPPVPN-----VDIRLESVPemeydal 463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 348 -PGASGQLYITGQGLARGYLNRPQLTAERFVEnpyspGSLmyKTGDVVRRLSDGTLAFIGRADDQVKI-RGYRIEPKEIE 425
Cdd:PLN02614 464 aSTPRGEICIRGKTLFSGYYKREDLTKEVLID-----GWL--HTGDVGEWQPNGSMKIIDRKKNIFKLsQGEYVAVENIE 536
|
..
gi 2214269206 426 TV 427
Cdd:PLN02614 537 NI 538
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1626-1835 |
3.58e-07 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 55.82 E-value: 3.58e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1626 GPVEGEVILTPIQR--WFFEKNFTNKHHWN--QSVMLHAKkgFDPERVEKTLQALIEHHDALRMVYREENGDIVQVYKPi 1701
Cdd:PRK10252 2 EPMSQHLPLVAAQPgiWMAEKLSPLPSAWSvaHYVELTGE--LDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDP- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1702 GESKVSFEIVDLYGSDEEmLRSQIKLLANKLQSSLDLRNGPLLKAEQYRTEAGDHLL--IAVHHLVVDGVSWRILLEDFA 1779
Cdd:PRK10252 79 ALTFPLPEIIDLRTQPDP-HAAAQALMQADLQQDLRVDSGKPLVFHQLIQLGDNRWYwyQRYHHLLVDGFSFPAITRRIA 157
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 2214269206 1780 SGY---MQAEKEESLVFPqktnSFKDWAEELAAFSQSAHLLQQAEYWsqiaAEQVSPLP 1835
Cdd:PRK10252 158 AIYcawLRGEPTPASPFT----PFADVVEEYQRYRASEAWQRDAAFW----AEQRRQLP 208
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
33-407 |
5.35e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 54.98 E-value: 5.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNE 112
Cdd:PTZ00216 122 ITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 113 RN-------MTAIGQYEGIIVSLDD------------GKW-------RNESKERPSSISGSRN-LAYVIYTSGTTGKPKG 165
Cdd:PTZ00216 202 KNvpnllrlMKSGGMPNTTIIYLDSlpasvdtegcrlVAWtdvvakgHSAGSHHPLNIPENNDdLALIMYTSGTTGDPKG 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 166 VQIEHRNLTNYVS----WFSEEAGLTENDKTVLlsSY-----AFDLGYTSMF---PVLLGGGelhivqkETYTAPDEIAh 233
Cdd:PTZ00216 282 VMHTHGSLTAGILaledRLNDLIGPPEEDETYC--SYlplahIMEFGVTNIFlarGALIGFG-------SPRTLTDTFA- 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 234 yiKEHG------ITYIKLTPSLFHTIVNTASfAK------------DANFESlRLIVLGGEKIIP---TDVIA-FRKMYG 291
Cdd:PTZ00216 352 --RPHGdltefrPVFLIGVPRIFDTIKKAVE-AKlppvgslkrrvfDHAYQS-RLRALKEGKDTPywnEKVFSaPRAVLG 427
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 292 H----------------TEFIN--------HYGPTEAT-IGAIAGRVDLyEPdafakrptigrpiANAGALVLNEALKLV 346
Cdd:PTZ00216 428 GrvramlsgggplsaatQEFVNvvfgmviqGWGLTETVcCGGIQRTGDL-EP-------------NAVGQLLKGVEMKLL 493
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 347 ---------PPGASGQLYITGQGLARGYLNRPQLTAERFVENPYspgslmYKTGDVVRRLSDGTLAFIGR 407
Cdd:PTZ00216 494 dteeykhtdTPEPRGEILLRGPFLFKGYYKQEELTREVLDEDGW------FHTGDVGSIAANGTLRIIGR 557
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
1065-1495 |
1.94e-06 |
|
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: 52.82 E-value: 1.94e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1065 HKDRP--AVTYNGQSW---TYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYpdq 1139
Cdd:cd05921 8 APDRTwlAEREGNGGWrrvTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAY--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1140 riEYILQDSgAKL-----LLKQEGISVPDSYTG----DVILLDGSRTILSLPLDENDE--------GNPET--------A 1194
Cdd:cd05921 85 --SLMSQDL-AKLkhlfeLLKPGLVFAQDAAPFaralAAIFPLGTPLVVSRNAVAGRGaisfaelaATPPTaavdaafaA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1195 VTAENLAYMIYTSGTTGQPKGVMVEHH---------------------ALVNLCFWHHDA-----FSMTAEDRSAKY--- 1245
Cdd:cd05921 162 VGPDTVAKFLFTSGSTGLPKAVINTQRmlcanqamleqtypffgeeppVLVDWLPWNHTFggnhnFNLVLYNGGTLYidd 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1246 -----AGFGFD-ASIWEMFPTW----TIGAELHVidEAIRLDIVrlndyfetngvtitflptqLAEQFMElentSLRVLL 1315
Cdd:cd05921 242 gkpmpGGFEETlRNLREISPTVyfnvPAGWEMLV--AALEKDEA-------------------LRRRFFK----RLKLMF 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1316 TGG--------DKLKR-AVK---KPYTLVNNYGPTENTVVATSaeIH-PEEGSLSIGRAIANTRVYILgegnqvqPEGVA 1382
Cdd:cd05921 297 YAGaglsqdvwDRLQAlAVAtvgERIPMMAGLGATETAPTATF--THwPTERSGLIGLPAPGTELKLV-------PSGGK 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1383 GELCVAGRGLARGYLNREDETAKRFVADPFvpgermYRTGDLVKWV-----NGGIEYIGRIDQQVKVR-GYRIELSEIEV 1456
Cdd:cd05921 368 YEVRVKGPNVTPGYWRQPELTAQAFDEEGF------YCLGDAAKLAdpddpAKGLVFDGRVAEDFKLAsGTWVSVGPLRA 441
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 2214269206 1457 QL--AQLSEVQDAAVTAVkdkgGNTAIAAYVTPETADIEAL 1495
Cdd:cd05921 442 RAvaACAPLVHDAVVAGE----DRAEVGALVFPDLLACRRL 478
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
33-442 |
2.16e-06 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 53.03 E-value: 2.16e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGA-------AFLP------IDPDTP------- 92
Cdd:PRK10524 85 YTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAihsvvfgGFAShslaarIDDAKPvlivsad 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 93 ---------------EERIRYS--------LEDSG-AKFAVVNERNM---TAIGQYEGIIVSLDdgkWRnESKErPSsis 145
Cdd:PRK10524 165 agsrggkvvpykpllDEAIALAqhkprhvlLVDRGlAPMARVAGRDVdyaTLRAQHLGARVPVE---WL-ESNE-PS--- 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 146 gsrnlaYVIYTSGTTGKPKGVQiehRNLTNY-VSW-------FSEEAGltendKTVLLSSyafDLG------YTSMFPVL 211
Cdd:PRK10524 237 ------YILYTSGTTGKPKGVQ---RDTGGYaVALatsmdtiFGGKAG-----ETFFCAS---DIGwvvghsYIVYAPLL 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 212 lgGGELHIVQKETYTAPDE-IAHYIKE-HGITYIKLTPslfhtivnTA---------SFAKDANFESLRLIVLGGEkiiP 280
Cdd:PRK10524 300 --AGMATIMYEGLPTRPDAgIWWRIVEkYKVNRMFSAP--------TAirvlkkqdpALLRKHDLSSLRALFLAGE---P 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 281 TDVIAFRKMYGH--TEFINHYGPTEA--TIGAIAGRVDlYEPDAFAkrpTIGRPIANAGALVLNEAL-KLVPPGASGQLY 355
Cdd:PRK10524 367 LDEPTASWISEAlgVPVIDNYWQTETgwPILAIARGVE-DRPTRLG---SPGVPMYGYNVKLLNEVTgEPCGPNEKGVLV 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 356 ITGQgLARGYLNRPQLTAERFVENPYSP-GSLMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGI 434
Cdd:PRK10524 443 IEGP-LPPGCMQTVWGDDDRFVKTYWSLfGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGHRLGTREIEESISSHPAV 521
|
....*...
gi 2214269206 435 QEAVVLAV 442
Cdd:PRK10524 522 AEVAVVGV 529
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1058-1241 |
2.67e-06 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 52.49 E-value: 2.67e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1058 FEETVQRHK--DRPAVTYNG-----QSWTYGELNAKANRLARILMDCGISPDDRV-GVLTkpslEMSAAVLGVLKA---G 1126
Cdd:PRK03584 88 YAENLLRHRrdDRPAIIFRGedgprRELSWAELRRQVAALAAALRALGVGPGDRVaAYLP----NIPETVVAMLATaslG 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1127 AAFVPIDPDY-PD------QRIE-YIL------------QDSGAKL--LLKQEG-----ISVPdsYTGDVIllDGSRTIL 1179
Cdd:PRK03584 164 AIWSSCSPDFgVQgvldrfGQIEpKVLiavdgyryggkaFDRRAKVaeLRAALPslehvVVVP--YLGPAA--AAAALPG 239
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2214269206 1180 SLPLDENDEGNPETAVTAENLA-----YMIYTSGTTGQPK-------GVMVEHHALVNLcfwHHDafsMTAEDR 1241
Cdd:PRK03584 240 ALLWEDFLAPAEAAELEFEPVPfdhplWILYSSGTTGLPKcivhghgGILLEHLKELGL---HCD---LGPGDR 307
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
153-501 |
3.74e-06 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 51.74 E-value: 3.74e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 153 VIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTENDKTVLLSSYAFDLGYTSMFPVLLGGGELHIVQKETyTAPDeIA 232
Cdd:PLN03051 124 ILFSSGTTGEPKAIPWTHLSPLRCASDGWAHMDIQPGDVVCWPTNLGWMMGPWLLYSAFLNGATLALYGGAP-LGRG-FG 201
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 233 HYIKEHGITYIKLTPSLFHTIVNTASFAKDA-NFESLRLIVLGGEKIIPTDVIAFRKMYGHTEFINHY-GPTEATIGAIA 310
Cdd:PLN03051 202 KFVQDAGVTVLGLVPSIVKAWRHTGAFAMEGlDWSKLRVFASTGEASAVDDVLWLSSVRGYYKPVIEYcGGTELASGYIS 281
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 311 GrvDLYEPDAFAkrpTIGRPIANAGALVLNEAlklVPPGASGQLYITGQGLARGYLNRPQLTAERFVENPYSPGSLMYKT 390
Cdd:PLN03051 282 S--TLLQPQAPG---AFSTASLGTRFVLLNDN---GVPYPDDQPCVGEVALAPPMLGASDRLLNADHDKVYYKGMPMYGS 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 391 --------GDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVML-SLSGIQE--AVVLAVSEGGLQELCAYY----- 454
Cdd:PLN03051 354 kgmplrrhGDIMKRTPGGYFCVQGRADDTMNLGGIKTSSVEIERACDrAVAGIAEtaAVGVAPPDGGPELLVIFLvlgee 433
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 455 -TSDQDIEKAELRYQLSLTLPSHMIPAFFVQ----VDAIPLTANGKTDRNAL 501
Cdd:PLN03051 434 kKGFDQARPEALQKKFQEAIQTNLNPLFKVSrvkiVPELPRNASNKLLRRVL 485
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
33-495 |
5.18e-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: 51.50 E-value: 5.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDT-------------PE-----E 94
Cdd:cd05943 99 VTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFgvpgvldrfgqiePKvlfavD 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 95 RIRYS--LEDSGAKFAVVNERNMTAIgqyEGIIVSLDDGKWRNESKERPSSISGSRNLA------------------YVI 154
Cdd:cd05943 179 AYTYNgkRHDVREKVAELVKGLPSLL---AVVVVPYTVAAGQPDLSKIAKALTLEDFLAtgaagelefeplpfdhplYIL 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 155 YTSGTTGKPKGvqIEHRnltnyvswfseeAG--LTENDKTVLLSSyafDLG-------YTS--------MFPVLLGGGEL 217
Cdd:cd05943 256 YSSGTTGLPKC--IVHG------------AGgtLLQHLKEHILHC---DLRpgdrlfyYTTcgwmmwnwLVSGLAVGATI 318
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 218 HIVQ-KETYTAPDEIAHYIKEHGITYIKLTPSLFHTIVNT-ASFAKDANFESLRLIVLGGEKIIPTdviAFrkmyghtEF 295
Cdd:cd05943 319 VLYDgSPFYPDTNALWDLADEEGITVFGTSAKYLDALEKAgLKPAETHDLSSLRTILSTGSPLKPE---SF-------DY 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 296 INHYGPTEATIGAIAGRVDLYEpdAFAkrptIGRPIA----------NAGALV--LNEALKLVPpGASGQLYITGQGLAR 363
Cdd:cd05943 389 VYDHIKPDVLLASISGGTDIIS--CFV----GGNPLLpvyrgeiqcrGLGMAVeaFDEEGKPVW-GEKGELVCTKPFPSM 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 364 --GYLNRPQltAERFVENPYS--PGslMYKTGDVVRRLSDGTLAFIGRADDQVKIRGYRIEPKEIETVMLSLSGIQEA-- 437
Cdd:cd05943 462 pvGFWNDPD--GSRYRAAYFAkyPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSlv 537
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2214269206 438 -----------VVLAVSEGGLQELcayytsDQDIE---KAELRYQLSltlPSHmIPAFFVQVDAIPLTANGK 495
Cdd:cd05943 538 vgqewkdgderVILFVKLREGVEL------DDELRkriRSTIRSALS---PRH-VPAKIIAVPDIPRTLSGK 599
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
32-174 |
7.72e-06 |
|
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: 51.20 E-value: 7.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 32 LLTYRELDEQANQLAHHLRAQGAGNEDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVN 111
Cdd:cd05933 8 TLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVVE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 112 ER--------------NMTAIGQYEGIIVSLDDG--KWR-----------NESKERPSSISGSRnLAYVIYTSGTTGKPK 164
Cdd:cd05933 88 NQkqlqkilqiqdklpHLKAIIQYKEPLKEKEPNlySWDefmelgrsipdEQLDAIISSQKPNQ-CCTLIYTSGTTGMPK 166
|
170
....*....|
gi 2214269206 165 GVQIEHRNLT 174
Cdd:cd05933 167 GVMLSHDNIT 176
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1673-1776 |
1.90e-05 |
|
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); Dual function Epimerization/Condensation (E/C) domains have both an epimerization and a DCL condensation activity. Dual E/C domains first epimerize the substrate amino acid to produce a D-configuration, then catalyze the condensation between the D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. They are 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. These Dual E/C domains contain an extended His-motif (HHx(N)GD) near the N-terminus of the domain in addition to the standard Condensation (C) domain active site motif (HHxxxD). 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, these include the DCL-type, LCL-type, 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 domains, and the X-domain.
Pssm-ID: 380466 [Multi-domain] Cd Length: 413 Bit Score: 49.36 E-value: 1.90e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1673 LQALIEHHDALR-MVYREENGDIVQ-VYKpigESKVSFEIVDLygSDEEMLRSQIKLLANKLQSSLDLRNGPLLKAEQYR 1750
Cdd:cd19544 45 LQQVIDRHDILRtAILWEGLSEPVQvVWR---QAELPVEELTL--DPGDDALAQLRARFDPRRYRLDLRQAPLLRAHVAE 119
|
90 100
....*....|....*....|....*...
gi 2214269206 1751 TEAGD--HLLIAVHHLVVDGVSWRILLE 1776
Cdd:cd19544 120 DPANGrwLLLLLFHHLISDHTSLELLLE 147
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
1076-1446 |
2.40e-05 |
|
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: 49.28 E-value: 2.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1076 QSWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDSGAKLLL- 1154
Cdd:cd05933 7 HTLTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1155 ---KQ-EGISVPDSYTGD---VILLDGS-----------RTILSLPLDENDEG--NPETAVTAENLAYMIYTSGTTGQPK 1214
Cdd:cd05933 87 enqKQlQKILQIQDKLPHlkaIIQYKEPlkekepnlyswDEFMELGRSIPDEQldAIISSQKPNQCCTLIYTSGTTGMPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1215 GVMVEHHALVnlcfWHHDAFSMTAEDRSAK----------------------YAGFGFDASIW----------------E 1256
Cdd:cd05933 167 GVMLSHDNIT----WTAKAASQHMDLRPATvgqesvvsylplshiaaqildiWLPIKVGGQVYfaqpdalkgtlvktlrE 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1257 MFPTWTIGA--------ELHVIDEAIRLDIVRLNDY------FETN-----GVTITFLPTQLAEQFM------ELENTSL 1311
Cdd:cd05933 243 VRPTAFMGVprvwekiqEKMKAVGAKSGTLKRKIASwakgvgLETNlklmgGESPSPLFYRLAKKLVfkkvrkALGLDRC 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1312 RVLLTGGDKLKRAVKKPY-----TLVNNYGPTENTVVAT--SAEIHpeeGSLSIGRAIANTRVYIlgegnqVQP--EGVa 1382
Cdd:cd05933 323 QKFFTGAAPISRETLEFFlslniPIMELYGMSETSGPHTisNPQAY---RLLSCGKALPGCKTKI------HNPdaDGI- 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2214269206 1383 GELCVAGRGLARGYLNREDETAKRFVADPFVpgermyRTGDLVKWVNGGIEYI-GRIDQQVKVRG 1446
Cdd:cd05933 393 GEICFWGRHVFMGYLNMEDKTEEAIDEDGWL------HSGDLGKLDEDGFLYItGRIKELIITAG 451
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
138-414 |
2.95e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 49.04 E-value: 2.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 138 KERPSSISGSR--NLAYVIYTSGTTGKPKGVQIEHRNLTNYV---SWFSE--EAGLTENDktVLLS-------------S 197
Cdd:PLN02430 208 KENPSETNPPKplDICTIMYTSGTSGDPKGVVLTHEAVATFVrgvDLFMEqfEDKMTHDD--VYLSflplahildrmieE 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 198 YAF----DLGY------------TSMFPVLLGG----------------GELHIVQKETYTAPDEIAHYIKEHGITYIKL 245
Cdd:PLN02430 286 YFFrkgaSVGYyhgdlnalrddlMELKPTLLAGvprvferihegiqkalQELNPRRRLIFNALYKYKLAWMNRGYSHKKA 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 246 TPslfhtIVNTASFAKDANF--ESLRLIVLGGEKiIPTDVIAFRKMYGHTEFINHYGPTEAtigaiAGRVDLYEPDAFAK 323
Cdd:PLN02430 366 SP-----MADFLAFRKVKAKlgGRLRLLISGGAP-LSTEIEEFLRVTSCAFVVQGYGLTET-----LGPTTLGFPDEMCM 434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 324 RPTIGRPiANAGALVLNEALKL------VPPgaSGQLYITGQGLARGYLNRPQLTAERFVENpyspgslMYKTGDVVRRL 397
Cdd:PLN02430 435 LGTVGAP-AVYNELRLEEVPEMgydplgEPP--RGEICVRGKCLFSGYYKNPELTEEVMKDG-------WFHTGDIGEIL 504
|
330
....*....|....*..
gi 2214269206 398 SDGTLAFIGRADDQVKI 414
Cdd:PLN02430 505 PNGVLKIIDRKKNLIKL 521
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
33-444 |
3.44e-05 |
|
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: 48.88 E-value: 3.44e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 33 LTYRELDEQANQLAHHLRAQG---AGneDIVAIVMDRSAEVMVSILGVMKAGAAFLPIDP---------DTPEERIRYSL 100
Cdd:cd05905 15 LTWGKLLSRAEKIAAVLQKKVglkPG--DRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPpdisqqlgfLLGTCKVRVAL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 101 ED----SGAKFAVVNERNMTAIGQYEGI--IVSLDDGKWRNESKERPSSISGSRN---LAYVIYTSGTTGKPKGVQIEHR 171
Cdd:cd05905 93 TVeaclKGLPKKLLKSKTAAEIAKKKGWpkILDFVKIPKSKRSKLKKWGPHPPTRdgdTAYIEYSFSSDGSLSGVAVSHS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 172 NLTNYVSWFSEEAGLTENDK---------------TVLLSSYAfdlGYTSMF---PVLLGGGELHIVQKETYTAPDEiah 233
Cdd:cd05905 173 SLLAHCRALKEACELYESRPlvtvldfksglglwhGCLLSVYS---GHHTILippELMKTNPLLWLQTLSQYKVRDA--- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 234 YIKEHGITYIKLTPSlfhtIVNTASFAKDANFESLR-LIVLGGEKIIPTDVIAFRKMYGH---------TEFINHYGP-- 301
Cdd:cd05905 247 YVKLRTLHWCLKDLS----STLASLKNRDVNLSSLRmCMVPCENRPRISSCDSFLKLFQTlglspravsTEFGTRVNPfi 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 302 -TEATIGAIAGRVDLyepDAFAKRPTIGRP-IANAG-ALVLNEALKlVPPGAS-----------------GQLYITGQGL 361
Cdd:cd05905 323 cWQGTSGPEPSRVYL---DMRALRHGVVRLdERDKPnSLPLQDSGK-VLPGAQvaivnpetkglckdgeiGEIWVNSPAN 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 362 ARGYLNRPQLT-AERFVENPYS----PGSLMY-KTGDV--VRRLS--------DGTLAFIGRADDQVKIRGYRIEPKEIE 425
Cdd:cd05905 399 ASGYFLLDGETnDTFKVFPSTRlstgITNNSYaRTGLLgfLRPTKctdlnveeHDLLFVVGSIDETLEVRGLRHHPSDIE 478
|
490 500
....*....|....*....|
gi 2214269206 426 -TVMLSLSGIQEAVVLAVSE 444
Cdd:cd05905 479 aTVMRVHPYRGRCAVFSITG 498
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
1056-1136 |
3.91e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 48.95 E-value: 3.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1056 QLFEETVQRHKDRPAVTYNGQSWTYGELNAKANRLARILMDCGISPDDRVGVL--TKPSLEMSAAVLGVLKAGAAFVPID 1133
Cdd:PRK07868 451 RIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLmeTRPSALVAIAALSRLGAVAVLMPPD 530
|
...
gi 2214269206 1134 PDY 1136
Cdd:PRK07868 531 TDL 533
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1077-1531 |
4.09e-05 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 48.74 E-value: 4.09e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1077 SWTYGELNAKANRLARILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAA----FVPIDPDYPDQRI-----EYILQD 1147
Cdd:PLN02654 120 SLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVhsvvFAGFSAESLAQRIvdckpKVVITC 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1148 SGAK-----LLLK-----------QEGISVpdsytgDVILLDGSRTILSLPLDENDEGN-----------PETA----VT 1196
Cdd:PLN02654 200 NAVKrgpktINLKdivdaaldesaKNGVSV------GICLTYENQLAMKREDTKWQEGRdvwwqdvvpnyPTKCevewVD 273
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1197 AENLAYMIYTSGTTGQPKGV-------MVEHHALVNLCFWHH--DAFSMTAE---DRSAKYAGFGfdasiwemfPTWTiG 1264
Cdd:PLN02654 274 AEDPLFLLYTSGSTGKPKGVlhttggyMVYTATTFKYAFDYKptDVYWCTADcgwITGHSYVTYG---------PMLN-G 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1265 AELHVIDEAIRL-DIVRLNDYFETNGVTITFLPTQLAEQFME--------LENTSLRVLLTGGDKLKRAVKKPYTLV--N 1333
Cdd:PLN02654 344 ATVLVFEGAPNYpDSGRCWDIVDKYKVTIFYTAPTLVRSLMRdgdeyvtrHSRKSLRVLGSVGEPINPSAWRWFFNVvgD 423
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1334 NYGPTENTVVATSA---EIHPEEGSLSIGRAIANTRVY-----ILGE-GNQVQPEgVAGELCVAGR--GLARGYLNREDe 1402
Cdd:PLN02654 424 SRCPISDTWWQTETggfMITPLPGAWPQKPGSATFPFFgvqpvIVDEkGKEIEGE-CSGYLCVKKSwpGAFRTLYGDHE- 501
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1403 takRFVADPFVPGERMYRTGDLVKWVNGGIEYI-GRIDQQVKVRGYRIELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAI 1481
Cdd:PLN02654 502 ---RYETTYFKPFAGYYFSGDGCSRDKDGYYWLtGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEVKGQGI 578
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 1482 AAYVT-----PETADI-EALKSTLKETLPDYMIP--AFWVTlnELPVTANGKVDRKAL 1531
Cdd:PLN02654 579 YAFVTlvegvPYSEELrKSLILTVRNQIGAFAAPdkIHWAP--GLPKTRSGKIMRRIL 634
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
7-178 |
5.04e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 48.57 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 7 ATFAALFEKQAQQTPDH------------SAVKAGGN-----------LLTYRELDEQANQLAHHLRAQGAGNEDIVAIV 63
Cdd:PLN02387 58 TTLAALFEQSCKKYSDKrllgtrklisreFETSSDGRkfeklhlgeyeWITYGQVFERVCNFASGLVALGHNKEERVAIF 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 64 MDRSAEVMVSILGVMKAGAAFLPIDPDTPEERIRYSLEDSGAKFAVVNERNMTAI----GQYEGI--IVSLDD------- 130
Cdd:PLN02387 138 ADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSKQLKKLidisSQLETVkrVIYMDDegvdsds 217
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2214269206 131 -----GKWRNES--------KERPS--SISGSRNLAYVIYTSGTTGKPKGVQIEHRNLTNYVS 178
Cdd:PLN02387 218 slsgsSNWTVSSfseveklgKENPVdpDLPSPNDIAVIMYTSGSTGLPKGVMMTHGNIVATVA 280
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1190-1528 |
5.11e-05 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 48.26 E-value: 5.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1190 NPETAVTAENLAYMIYTSGTTGQPKGVMVEHHALVnlcfwhhdAFSMtaedrsAKYA--GFGFDASIWEMFPTWTIG--- 1264
Cdd:PLN02860 164 ELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALI--------VQSL------AKIAivGYGEDDVYLHTAPLCHIGgls 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1265 ---AEL-----HVI----DEAIRLDIVrlndyfETNGVT--ITfLPTQLAEqFMEL--------ENTSLRVLLTGG---- 1318
Cdd:PLN02860 230 salAMLmvgacHVLlpkfDAKAALQAI------KQHNVTsmIT-VPAMMAD-LISLtrksmtwkVFPSVRKILNGGgsls 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1319 -DKLKRAVK--KPYTLVNNYGPTENTVVATSAEIHpeEGSLSIGRAIANTRVYILGEGNQvQPEGVagelCVA------- 1388
Cdd:PLN02860 302 sRLLPDAKKlfPNAKLFSAYGMTEACSSLTFMTLH--DPTLESPKQTLQTVNQTKSSSVH-QPQGV----CVGkpaphve 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1389 -----------GRGLARG------YLNREDETAKRFVADPFVPgermyrTGDlVKWVN--GGIEYIGRIDQQVKVRGYRI 1449
Cdd:PLN02860 375 lkigldessrvGRILTRGphvmlgYWGQNSETASVLSNDGWLD------TGD-IGWIDkaGNLWLIGRSNDRIKTGGENV 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1450 ELSEIEVQLAQLSEVQDAAVTAVKDKGGNTAIAAYV------TPETADIEALKSTL---KETLPD---------YMIPAF 1511
Cdd:PLN02860 448 YPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVrlrdgwIWSDNEKENAKKNLtlsSETLRHhcreknlsrFKIPKL 527
|
410
....*....|....*...
gi 2214269206 1512 WVTLNE-LPVTANGKVDR 1528
Cdd:PLN02860 528 FVQWRKpFPLTTTGKIRR 545
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1665-2056 |
1.56e-04 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 47.09 E-value: 1.56e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1665 DPERVEKTLQALIEHHDALRMVYREENG-DIVQVYKPIGESKVSFEivDLYGSDEEMLRSQIK-LLANKLQSSLDLRNGP 1742
Cdd:PRK05691 3293 DPERFAQAWQAVVARHEALRASFSWNAGeTMLQVIHKPGRTPIDYL--DWRGLPEDGQEQRLQaLHKQEREAGFDLLNQP 3370
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1743 LLKAEQYRT-EAGDHLLIAVHHLVVDGVSWRILLEDFASGYMQ--AEKEESLVFPQKTNSFKDWAeelaafsQSAHLLQQ 1819
Cdd:PRK05691 3371 PFHLRLIRVdEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTAlgEGREAQLPVPPRYRDYIGWL-------QRQDLAQA 3443
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1820 AEYWSQIAA--EQVSPLPKD--------CETEQRIVKDTSSvlcELTAEDTkHLLTDVHQPYGTEINDILLSALGLTMKE 1889
Cdd:PRK05691 3444 RQWWQDNLRgfERPTPIPSDrpflrehaGDSGGMVVGDCYT---RLDAADG-ARLRELAQAHQLTVNTFAQAAWALVLRR 3519
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1890 WTKGAKIGINLEGHGREDIIPnvNISRTVGWFTAQYPVVLDISDADASAvikTVKENLRRIPDKGVG-----YGILRYFT 1964
Cdd:PRK05691 3520 YSGDRDVLFGVTVAGRPVSMP--QMQRTVGLFINSIALRVQLPAAGQRC---SVRQWLQGLLDSNMElreyeYLPLVAIQ 3594
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1965 ETAET-KGftpEISFNYLGQFDSEVktdfFEPSAFDMGRQVSGESEA--------LYALSFSGmirnGRFVLSCSYNEKE 2035
Cdd:PRK05691 3595 ECSELpKG---QPLFDSLFVFENAP----VEVSVLDRAQSLNASSDSgrthtnfpLTAVCYPG----DDLGLHLSYDQRY 3663
|
410 420
....*....|....*....|.
gi 2214269206 2036 FERATVEEQMERFKENLLMLI 2056
Cdd:PRK05691 3664 FDAPTVERLLGEFKRLLLALV 3684
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1198-1224 |
1.69e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 46.63 E-value: 1.69e-04
10 20
....*....|....*....|....*..
gi 2214269206 1198 ENLAYMIYTSGTTGQPKGVMVEHHALV 1224
Cdd:PLN02736 221 EDVATICYTSGTTGTPKGVVLTHGNLI 247
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1622-1782 |
2.70e-04 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 46.49 E-value: 2.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1622 QADQGPVEGEVI-----LTPIQRWFFEKNFTNK---HHWNQsvMLHAKKGFDPERVEKTLQALIEHHDALR--MVYREEN 1691
Cdd:PRK12316 4088 RLDALPLPLGEIediypLSPMQQGMLFHSLYEQeagDYINQ--MRVDVQGLDVERFRAAWQAALDRHDVLRsgFVWQGEL 4165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1692 GDIVQVYKPigESKVSFEIVDLYGSdEEMLRSQIKLLANKLQSSLDLRNGPLLKAEQYRTEAGDHLLIAV-HHLVVDGVS 1770
Cdd:PRK12316 4166 GRPLQVVHK--QVSLPFAELDWRGR-ADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTnHHILMDGWS 4242
|
170
....*....|..
gi 2214269206 1771 WRILLEDFASGY 1782
Cdd:PRK12316 4243 NSQLLGEVLERY 4254
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
156-450 |
3.00e-04 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 45.69 E-value: 3.00e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 156 TSGTTGKPKGV---QIEHRNLTNYVSWFSEEAGLTENDktVLLSSYAFDLgYTSMFPVLLG------------GG--ELH 218
Cdd:cd05913 86 SSGTTGKPTVVgytKNDLDVWAELVARCLDAAGVTPGD--RVQNAYGYGL-FTGGLGFHYGaerlgalvipagGGntERQ 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 219 IvqketytapdEIahyIKEHGITYIKLTPSLFHTIvntASFAKDANFE----SLRLIVLGGEKIIPTDVIAFRKMYGhTE 294
Cdd:cd05913 163 L----------QL---IKDFGPTVLCCTPSYALYL---AEEAEEEGIDprelSLKVGIFGAEPWTEEMRKRIERRLG-IK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 295 FINHYGPTEATIGAIAG----RVDLY--EpDAFAkrPTIGRPianagalvlnEALKLVPPGASGQLYITgqglargylnr 368
Cdd:cd05913 226 AYDIYGLTEIIGPGVAFeceeKDGLHiwE-DHFI--PEIIDP----------ETGEPVPPGEVGELVFT----------- 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 369 pQLTAErfvenpYSPgSLMYKTGDVVRrLSDGTLA----------FIGRADDQVKIRGYRIEPKEIETVMLSLSG-IQEA 437
Cdd:cd05913 282 -TLTKE------AMP-LIRYRTRDITR-LLPGPCPcgrthrridrITGRSDDMLIIRGVNVFPSQIEDVLLKIPGlGPHY 352
|
330
....*....|...
gi 2214269206 438 VVLAVSEGGLQEL 450
Cdd:cd05913 353 QLILTRQEHLDEL 365
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1036-1224 |
4.51e-04 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 45.49 E-value: 4.51e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1036 ALLE-AWKGKAlpvptdkTVHQLFEETVQRHKDRP------------AVTYNGQS----------W-TYGELNAKANRLA 1091
Cdd:PLN02387 48 ELVEtPWEGAT-------TLAALFEQSCKKYSDKRllgtrklisrefETSSDGRKfeklhlgeyeWiTYGQVFERVCNFA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1092 RILMDCGISPDDRVGVLTKPSLEMSAAVLGVLKAGAAFVPIDPDYPDQRIEYILQDS-------GAKLLLKQEGISVPDS 1164
Cdd:PLN02387 121 SGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETevttvicDSKQLKKLIDISSQLE 200
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2214269206 1165 YTGDVILLD--GSRTILSLPLDEN------------DEGNPETAV--TAENLAYMIYTSGTTGQPKGVMVEHHALV 1224
Cdd:PLN02387 201 TVKRVIYMDdeGVDSDSSLSGSSNwtvssfseveklGKENPVDPDlpSPNDIAVIMYTSGSTGLPKGVMMTHGNIV 276
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
125-190 |
8.57e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 44.32 E-value: 8.57e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2214269206 125 IVSLDdgKWRNESKERPSSISGSRN--LAYVIYTSGTTGKPKGVQIEHRNLTNYVSWFSEEAGLTEND 190
Cdd:PLN02736 198 IVTYS--KLLAQGRSSPQPFRPPKPedVATICYTSGTTGTPKGVVLTHGNLIANVAGSSLSTKFYPSD 263
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1174-1224 |
9.90e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 44.20 E-value: 9.90e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2214269206 1174 GSRTILSLPLDENDegnpetavtaenLAYMIYTSGTTGQPKGVMVEHHALV 1224
Cdd:PTZ00216 252 GSHHPLNIPENNDD------------LALIMYTSGTTGDPKGVMHTHGSLT 290
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1372-1531 |
3.40e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 42.44 E-value: 3.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1372 EGNQVqPEGVAGELCVAGR--GLARGYLNREDetakRFVADPFVPGERMYRTGDLVK-------WVnggieyIGRIDQQV 1442
Cdd:PRK00174 441 EGNPL-EGGEGGNLVIKDPwpGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGARrdedgyyWI------TGRVDDVL 509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2214269206 1443 KVRGYRIELSEIEVQLAQLSEVQDAAVTAVKD--KGgnTAIAAYVTP---ETADiEALKSTLKETL---------PDYMi 1508
Cdd:PRK00174 510 NVSGHRLGTAEIESALVAHPKVAEAAVVGRPDdiKG--QGIYAFVTLkggEEPS-DELRKELRNWVrkeigpiakPDVI- 585
|
170 180
....*....|....*....|...
gi 2214269206 1509 paFWVTlnELPVTANGKVDRKAL 1531
Cdd:PRK00174 586 --QFAP--GLPKTRSGKIMRRIL 604
|
|
| |
