|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
3-2325 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1873.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3 LVTLSQEEIDTVIATVPDGVANVQDIyPLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDIL 82
Cdd:PRK12467 25 LEKMQEEGVSFANLPIPQVRSAFERI-PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 83 RTAICWQGlHQPVQVVWRQAPLTV--NTLTTTSSDTVPAQLRAATDPSNHRL-NLSNAPLLSAT---TAHDpvcgEWLLS 156
Cdd:PRK12467 104 RTRFVQDE-EGFRQVIDASLSLTIplDDLANEQGRARESQIEAYINEEVARPfDLANGPLLRVRllrLADD----EHVLV 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 157 LSIHHLISDHITQALIIDEIRLLL----EDRPEALPK-PLPYRNF-IAQILSVPLSEHEQ---YFRNRLADIDTPTA-PF 226
Cdd:PRK12467 179 VTLHHIISDGWSMRVLVEELVQLYsaysQGREPSLPAlPIQYADYaIWQRSWLEAGERERqlaYWQEQLGGEHTVLElPT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 227 DLVDVQGNGEDITEARLSLDSSLADALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQGNLgaDRVMG 306
Cdd:PRK12467 259 DRPRPAVPSYRGARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVET--ERLIG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 307 MFINTLPLRVSLRER-SVHDVVQATSHELMMLLAHEQAP---LALAQQCSQVPPPLPLFSTLFNYRHSQKDASSQFWEGM 382
Cdd:PRK12467 337 FFVNTQVLKAEVDPQaSFLELLQQVKRTALGAQAHQDLPfeqLVEALQPERSLSHSPLFQVMFNHQNTATGGRDREGAQL 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 383 RQLS------GRERTNYPITLSVDDLGDGFNLTAKTVMGVDPERIVHYMLTAIENLVTSLEKTPQQPALSQPILPKSERQ 456
Cdd:PRK12467 417 PGLTveelswARHTAQFDLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERA 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 457 QVLVDFNATDADFPREMlIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEM 536
Cdd:PRK12467 497 RELVRWNAPATEYAPDC-VHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEM 575
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 537 MVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQSAQVAQLN--STLPTVLLDTPAA--AACPDTNPVVQgLH 612
Cdd:PRK12467 576 VVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPvpAGLRSLCLDEPADllCGYSGHNPEVA-LD 654
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 613 AAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKN-WIQLLSGHTLVLVPDALRA 691
Cdd:PRK12467 655 PDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTElFGALASGATLHLLPPDCAR 734
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 692 DAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLgSDPAYQPAQVLIGGEAISPAVWSRLQSLSD-TRFINVYGPTECTVDA 770
Cdd:PRK12467 735 DAEAFAALMADQGVTVLKIVPSHLQALLQASR-VALPRPQRALVCGGEALQVDLLARVRALGPgARLINHYGPTETTVGV 813
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 771 TACVV---DRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSADpAARIY 847
Cdd:PRK12467 814 STYELsdeERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGAD-GGRLY 892
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 848 KTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIArEDSPGDTRLVAYL--CARPDAELHPA 925
Cdd:PRK12467 893 RTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLvpAAVADGAEHQA 971
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 926 ---ALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAPDQTAfATRDYEAPQGGIETALAALWQELLGLDRVGR 1002
Cdd:PRK12467 972 trdELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASA-VQATFVAPQTELEKRLAAIWADVLKVERVGL 1050
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1003 HDQFFALGGHSLLAVQLLNRMNKA-GMDVALATLFAHPTLCDLAAAVTATAHDAPFTLPVADRTQPLPLSFSQQRLWFLA 1081
Cdd:PRK12467 1051 TDNFFELGGHSLLATQVISRVRQRlGIQVPLRTLFEHQTLAGFAQAVAAQQQGAQPALPDVDRDQPLPLSYAQERQWFLW 1130
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1082 QLDPaASQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPD-TLGFSLSSHDLRKLDEAART 1160
Cdd:PRK12467 1131 QLEP-GSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQVIHPVgSLTLEEPLLLAADKDEAQLK 1209
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1161 TRVaelaEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALEGSEANLPPLPVQY 1240
Cdd:PRK12467 1210 VYV----EAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQY 1285
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1241 ADYAVWQRQWLQ-GETLNDLRdYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRLHALNRQQGTTLFMT 1319
Cdd:PRK12467 1286 ADYAVWQRQWMDaGERARQLA-YWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFML 1364
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1320 LLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQVRERALDAYAHQALPFEQV 1399
Cdd:PRK12467 1365 LLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQL 1444
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1400 VEILQPARSLSYSPIFQVMLSLNNTPAQAL-TLPDLTLSAVERPQHSTHFDLSLSLIETENGLNGGLVYATDLFDRETIL 1478
Cdd:PRK12467 1445 VEALQPERSLSHSPLFQVMFNHQRDDHQAQaQLPGLSVESLSWESQTAQFDLTLDTYESSEGLQASLTYATDLFEASTIE 1524
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1479 RVVGYVENILMAMADDVTQPVATLPILPDSERRQVMLDFNATEADFPHDALIHQLVEDQAARTPDTTAVLFEDQHLTYDA 1558
Cdd:PRK12467 1525 RLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIEDQAAATPEAVALVFGEQELTYGE 1604
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1559 LNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQAN--QR 1636
Cdd:PRK12467 1605 LNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHlqAR 1684
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1637 ALLTGDVPRILLDTAD--FSHLSEDNPHVpGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVL 1714
Cdd:PRK12467 1685 LPLPDGLRSLVLDQEDdwLEGYSDSNPAV-NLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADVVL 1763
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1715 QKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADCACDSLRRVICSG 1794
Cdd:PRK12467 1764 QFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVCGG 1843
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1795 EALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWACQPDD--HRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHI 1871
Cdd:PRK12467 1844 EALEVEALRPWLERLpDTGLFNLYGPTETAVDVTHWTCRRKDleGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYL 1923
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1872 GGVGVARGYLNRPDLTAERFIPDPFiNQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGV 1951
Cdd:PRK12467 1924 GGVGLARGYLNRPALTAERFVADPF-GTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGV 2002
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1952 QEAVVVArEDSPGDTRLVAYLCPQ----PGVTPDPADLRQQLGQHLA----EYMVPGAFVTLDAFPLTPNGKLDRKALPA 2023
Cdd:PRK12467 2003 REAVVIA-QDGANGKQLVAYVVPTdpglVDDDEAQVALRAILKNHLKaslpEYMVPAHLVFLARMPLTPNGKLDRKALPA 2081
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2024 PDQSAVaTRDYEAPQGEVETALAAVWQDLLGLTRVGRHDHFFALGGHSLLIVSLIERLRRAGLALDVRGVFSTPVLSDMA 2103
Cdd:PRK12467 2082 PDASEL-QQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLA 2160
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2104 qAILAHQDKPAVvvppnripADSTAITPDLlplvtltqpeidritdtvsggasniqdiyPLAPLQEgiLF--------HH 2175
Cdd:PRK12467 2161 -AVAQEGDGTVS--------IDQGPVTGDL-----------------------------PLLPIQQ--MFfaddiperHH 2200
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2176 LLQEqgdtyllrsmVAFTHRERLDAFL--SALQQVIDRHDILRTAVCWQDLSqpvqvvWRQAIL-PINHFEP---TSPED 2249
Cdd:PRK12467 2201 WNQS----------VLLEPREALDAELleAALQALLVHHDALRLGFVQEDGG------WSAMHRaPEQERRPllwQVVVA 2264
|
2330 2340 2350 2360 2370 2380 2390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 2250 VLAQLQAHTEPRTRRIDLSQAPLFRADIAHDPLQNEWLLaLSFHHLISDHMTLALIVGEIRLLLQHQADALPTPLP 2325
Cdd:PRK12467 2265 DKEELEALCEQAQRSLDLEEGPLLRAVLATLPDGSQRLL-LVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLP 2339
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1061-3182 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1756.21 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1061 VADRTQPLPLSFSQQRLWFLAQLDPAaSQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPD 1140
Cdd:PRK12467 43 VRSAFERIPLSYAQERQWFLWQLDPD-SAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDAS 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1141 tLGFSLSSHDLRKLDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAA 1220
Cdd:PRK12467 122 -LSLTIPLDDLANEQGRARESQIEAYINEEVARPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1221 LYQAALEGSEANLPPLPVQYADYAVWQRQWLQ-GETLNDLRdYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDA 1299
Cdd:PRK12467 201 LYSAYSQGREPSLPALPIQYADYAIWQRSWLEaGERERQLA-YWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQ 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1300 GQLRRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLD 1379
Cdd:PRK12467 280 ALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQ 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1380 QVRERALDAYAHQALPFEQVVEILQPARSLSYSPIFQVMLSLNNTPA-----QALTLPDLTLSAVERPQHSTHFDLSLSL 1454
Cdd:PRK12467 360 QVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTATggrdrEGAQLPGLTVEELSWARHTAQFDLALDT 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1455 IETENGLNGGLVYATDLFDRETILRVVGYVENILMAMADDVTQPVATLPILPDSERRQVMLDFNATEADFPHDAlIHQLV 1534
Cdd:PRK12467 440 YESAQGLWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDC-VHQLI 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1535 EDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPA 1614
Cdd:PRK12467 519 EAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQ 598
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1615 ERLAYMLDDASPVALLTQANQRALLT--GDVPRILLDTAD--FSHLSEDNPHVPgLDAHHLAYVIYTSGSTGKPKGVMNS 1690
Cdd:PRK12467 599 DRLAYMLDDSGVRLLLTQSHLLAQLPvpAGLRSLCLDEPAdlLCGYSGHNPEVA-LDPDNLAYVIYTSGSTGQPKGVAIS 677
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1691 HRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSM 1770
Cdd:PRK12467 678 HGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSH 757
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1771 LQQFVQWADADcACDSLRRVICSGEALPAELQQRFFA-RFNAQLHNLYGPTEAAIDVTFWACQPDDHRS-FVPIGRPIAN 1848
Cdd:PRK12467 758 LQALLQASRVA-LPRPQRALVCGGEALQVDLLARVRAlGPGARLINHYGPTETTVGVSTYELSDEERDFgNVPIGQPLAN 836
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1849 TQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFiNQPGARLYKTGDLARWLPDGSLEYLGRNDFQ 1928
Cdd:PRK12467 837 LGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPF-GADGGRLYRTGDLARYRADGVIEYLGRMDHQ 915
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1929 VKLRGFRIELGEIEARLMQCPGVQEAVVVArEDSPGDTRLVAYLCpqPGVTPDPA-------DLRQQLGQHLAEYMVPGA 2001
Cdd:PRK12467 916 VKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLV--PAAVADGAehqatrdELKAQLRQVLPDYMVPAH 992
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2002 FVTLDAFPLTPNGKLDRKALPAPDQSAVaTRDYEAPQGEVETALAAVWQDLLGLTRVGRHDHFFALGGHSLLIVSLIERL 2081
Cdd:PRK12467 993 LLLLDSLPLTPNGKLDRKALPKPDASAV-QATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRV 1071
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2082 RRA-GLALDVRGVFSTPVLSDMAQAILAHQdkpavvvpPNRIPAdstaitpdlLPLVTLTQPEidritdtvsggasniqd 2160
Cdd:PRK12467 1072 RQRlGIQVPLRTLFEHQTLAGFAQAVAAQQ--------QGAQPA---------LPDVDRDQPL----------------- 1117
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2161 iyPLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCwQDLSQPVQVVWRQAILPIN 2240
Cdd:PRK12467 1118 --PLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFV-QEDGRTRQVIHPVGSLTLE 1194
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2241 HFEPTSPEDVLAQLQAHTEPRTRR-IDLSQAPLFRAD---IAHDplqnEWLLALSFHHLISDHMTLALIVGEI----RLL 2312
Cdd:PRK12467 1195 EPLLLAADKDEAQLKVYVEAEARQpFDLEQGPLLRVGllrLAAD----EHVLVLTLHHIVSDGWSMQVLVDELvalyAAY 1270
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2313 LQHQADALPT-PLPYRNFIA---QTLSVPNSAHE-AYFRDKLA---DVDEPTAPFGLLNVQGSGGDIHeaRLVLDATLAS 2384
Cdd:PRK12467 1271 SQGQSLQLPAlPIQYADYAVwqrQWMDAGERARQlAYWKAQLGgeqPVLELPTDRPRPAVQSHRGARL--AFELPPALAE 1348
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2385 AIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRlaGAEGADRIMGMFINTLPLRISLadRGAAEVVERTS 2464
Cdd:PRK12467 1349 GLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANR--NRAETEGLIGFFVNTQVLRAEV--DGQASFQQLLQ 1424
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2465 HDLMTLLE---HEQAPlaLAQRCSGVAPPM-----PLFSTLLNYRhTQASSTDNTLSDIRV--LTSEERT-NYPLTLAVD 2533
Cdd:PRK12467 1425 QVKQAALEaqaHQDLP--FEQLVEALQPERslshsPLFQVMFNHQ-RDDHQAQAQLPGLSVesLSWESQTaQFDLTLDTY 1501
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2534 DRGEGFSLVAQTLEDIDPHRLLNYLMTAISSLVDALETEPQRSILNLPVLPDSERQQMLVDFNATDADIPRHALIHELFE 2613
Cdd:PRK12467 1502 ESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQLIE 1581
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2614 AQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVE 2693
Cdd:PRK12467 1582 DQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRE 1661
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2694 RLRYMLDDAKPVALISQSA---HLGIMNGsLPVILLDDGETRpFDNEPDTPLDARkqgLTPRHLAYVIYTSGSTGKPKGV 2770
Cdd:PRK12467 1662 RLAYMIEDSGIELLLTQSHlqaRLPLPDG-LRSLVLDQEDDW-LEGYSDSNPAVN---LAPQNLAYVIYTSGSTGRPKGA 1736
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2771 MVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQAT 2850
Cdd:PRK12467 1737 GNRHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFV 1816
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2851 PSTWRMLVEL--RDFALPPGFKALCGGEALPENLATALLQKV--TTLWNLYGPTETTIWSTLNGLTTPTPY------IGH 2920
Cdd:PRK12467 1817 PSMLQQLLQMdeQVEHPLSLRRVVCGGEALEVEALRPWLERLpdTGLFNLYGPTETAVDVTHWTCRRKDLEgrdsvpIGQ 1896
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2921 PIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsGAPEARMYKTGDLGRWLPDGTLEYLGR 3000
Cdd:PRK12467 1897 PIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPF-GTVGSRLYRTGDLARYRADGVIEYLGR 1975
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3001 NDFQVKVRGFRIELGEIETRLARCHGVHDAVVIArEDSPGDKRLVAYLLAQPDTVLEPAD--------LRQRLSEGVAEY 3072
Cdd:PRK12467 1976 IDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYVVPTDPGLVDDDEaqvalraiLKNHLKASLPEY 2054
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3073 MIPSAFVTLDAFPLTPNGKLDRKALPAPDQSAMaTRGYEAPQGDLEHALAQIWQTLLGVERVGRHDHFFELGGHSLLAVQ 3152
Cdd:PRK12467 2055 MVPAHLVFLARMPLTPNGKLDRKALPAPDASEL-QQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQ 2133
|
2170 2180 2190
....*....|....*....|....*....|
gi 641744967 3153 LNARIRAEFLTDIPiVAIFQHPQLSALAEV 3182
Cdd:PRK12467 2134 VVSRARQAGIRFTP-KDLFQHQTVQSLAAV 2162
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-2450 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1720.18 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2 PLVTLSQEEIDTViaTVPDGvaNVQDIYPLAPLQEGILFHYQLQEKGDTYLlnsllafdSQTRLD-------AFLDVLQQ 74
Cdd:PRK12316 1534 PLAGLSQAQLDAL--PLPAG--EIADIYPLSPMQQGMLFHSLYEQEAGDYI--------NQLRVDvqgldpdRFRAAWQA 1601
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 75 VIARHDILRTAICWQ-GLHQPVQVVWRQAPLTVNTLTTTSSDTVPAQLRAATDPSNHR-LNLSNAPLLSATTAHDPVcGE 152
Cdd:PRK12316 1602 TVDRHEILRSGFLWQdGLEQPLQVIHKQVELPFAELDWRGREDLGQALDALAQAERQKgFDLTRAPLLRLVLVRTGE-GR 1680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 153 WLLSLSIHHLISDHITQALIIDEIRLLLEDRPEALPKpLPYRNFIAQILSVPLSEHEQYFRNRLADIDTPTAPFDLVDVQ 232
Cdd:PRK12316 1681 HHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPG-GRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQAARTE 1759
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 233 GNGEDITEARLSLDSSLADALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQGNLGADRVMGMFINTL 312
Cdd:PRK12316 1760 DGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTL 1839
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 313 PLRVSLR-ERSVHDVVQATSHELMMLLAHEQAPLALAQQCSQVPPPlPLFSTLF---NYRHSQ-----KDASSQFWEgmr 383
Cdd:PRK12316 1840 PVIAAPRpDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGE-ALFDSLLvfeNYPVAEalkqgAPAGLVFGR--- 1915
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 384 qLSGRERTNYPITLSVDdLGDGFNLTAKTVMG----VDPERIVHYMLtaieNLVTSLEKTPQQPALSQPILPKSERQQVL 459
Cdd:PRK12316 1916 -VSNHEQTNYPLTLAVT-LGETLSLQYSYDRGhfdaAAIERLDRHLL----HLLEQMAEDAQAALGELALLDAGERQRIL 1989
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 460 VDFNATDADFPREMLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVG 539
Cdd:PRK12316 1990 ADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVA 2069
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 540 LLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQSAQVAQLNST--LPTVLLDTPAA-AACPDTNPVVQgLHAAHL 616
Cdd:PRK12316 2070 LLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPLPagVARLPLDRDAEwADYPDTAPAVQ-LAGENL 2148
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 617 AYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWIQ-LLSGHTLVLVPDALRaDAHQ 695
Cdd:PRK12316 2149 AYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHpLLNGARVLIRDDELW-DPEQ 2227
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 696 LWRYFARHAVDLFDCTPVQLQWLLD--AGLGSDPAYQpaQVLIGGEAISPAVWSR-LQSLSDTRFINVYGPTECTVDATA 772
Cdd:PRK12316 2228 LYDEMERHGVTILDFPPVYLQQLAEhaERDGRPPAVR--VYCFGGEAVPAASLRLaWEALRPVYLFNGYGPTEAVVTPLL 2305
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 773 CVVDRTQP----LPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSAdPAARIYK 848
Cdd:PRK12316 2306 WKCRPQDPcgaaYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSA-SGERLYR 2384
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 849 TGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAReDSPGDTRLVAYLCARPDAELHPAALR 928
Cdd:PRK12316 2385 TGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELR 2463
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 929 QQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAPDQTAfATRDYEAPQGGIETALAALWQELLGLDRVGRHDQFFA 1008
Cdd:PRK12316 2464 AWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQ-LRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFE 2542
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1009 LGGHSLLAVQLLNRMNKA-GMDVALATLFAHPTLCDLAAAVTATAHDAPFTLPVADRTQPLPLSFSQQRLWFLAQLDPAa 1087
Cdd:PRK12316 2543 LGGHSLLATQVVSRVRQDlGLEVPLRILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPE- 2621
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1088 SQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDTLGFSLSSHDLRKLDEAARttrvaELA 1167
Cdd:PRK12316 2622 SAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLEDCAGVADAAIR-----QRV 2696
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1168 EQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALEGSEANLPPLPVQYADYAVWQ 1247
Cdd:PRK12316 2697 AEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQ 2776
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1248 RQWLQGETLNDLRDYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRLHALNRQQGTTLFMTLLAAWSVV 1327
Cdd:PRK12316 2777 RAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVL 2856
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1328 LSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQVRERALDAYAHQALPFEQVVEILQPAR 1407
Cdd:PRK12316 2857 LHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPER 2936
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1408 SLSYSPIFQVMLSLNNTPAQALTLPDLTLSAVERPQHSTHFDLSLSLIETENGLNGGLVYATDLFDRETILRVVGYVENI 1487
Cdd:PRK12316 2937 SLSHSPLFQVMYNHQSGERAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNL 3016
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1488 LMAMADDVTQPVATLPILPDSERRQVMLDFNATEADFPHDALIHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLA 1567
Cdd:PRK12316 3017 LRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLA 3096
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1568 HHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQANQRALLTGDVPRIL 1647
Cdd:PRK12316 3097 HRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLD 3176
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1648 LDtADFSHLSEDNPHVpGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWE 1727
Cdd:PRK12316 3177 LD-RGDENYAEANPAI-RTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEE 3254
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1728 FFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADcACDSLRRVICSGEALPAELQQRFFA 1807
Cdd:PRK12316 3255 LFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAH-RCTSLKRIVCGGEALPADLQQQVFA 3333
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1808 RfnAQLHNLYGPTEAAIDVTFWACqPDDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLT 1887
Cdd:PRK12316 3334 G--LPLYNLYGPTEATITVTHWQC-VEEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLT 3410
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1888 AERFIPDPFinQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSpgdtR 1967
Cdd:PRK12316 3411 AERFVPDPF--VPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGR----Q 3484
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1968 LVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPAPDqSAVATRDYEAPQGEVETALAA 2047
Cdd:PRK12316 3485 LVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPD-AALLQQDYVAPVNELERRLAA 3563
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2048 VWQDLLGLTRVGRHDHFFALGGHSLLIVSLIERLRRAGLALDVRGVFSTPVLSDMAQAIlahqdkpavvvppnripadst 2127
Cdd:PRK12316 3564 IWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVA--------------------- 3622
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2128 aitpdllplvtltqpeidRITDTVSGGASNIQDIYPLAPLQEGIL------FHHLLQEQgdtyLLRSmvafthRERLD-- 2199
Cdd:PRK12316 3623 ------------------RVGGGVAVDQGPVSGETLLLPIQQQFFeepvpeRHHWNQSL----LLKP------REALDaa 3674
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2200 AFLSALQQVIDRHDILRTAVcwqdlsQPVQVVWRQAILPInhfepTSPEDVL--------AQLQAHTEPRTRRIDLSQAP 2271
Cdd:PRK12316 3675 ALEAALQALVEHHDALRLRF------VEDAGGWTAEHLPV-----ELGGALLwraelddaEELERLGEEAQRSLDLADGP 3743
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2272 LFRADIAHDPLQNEWLLaLSFHHLISDHMTLALIVGEIRLLLQHQADALPTPLPYRN--FIAQTLSVPNSAHE------- 2342
Cdd:PRK12316 3744 LLRALLATLADGSQRLL-LVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTssFKAWAERLQEHARGealkael 3822
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2343 AYFRDKLADVdepTAPFGLLNVQGSGGDIHEARLV--LDATLASAIRQQA-RHLGVSPGVLFHVAWAQVLAQTSGRDDVV 2419
Cdd:PRK12316 3823 AYWQEQLQGV---SSELPCDHPQGALQNRHAASVQtrLDRELTRRLLQQApAAYRTQVNDLLLTALARVVCRWTGEASAL 3899
|
2490 2500 2510
....*....|....*....|....*....|...
gi 641744967 2420 FGSVLLGRLAGAEGAD--RIMGMFINTLPLRIS 2450
Cdd:PRK12316 3900 VQLEGHGREDLFADIDlsRTVGWFTSLFPVRLS 3932
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
465-3191 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1668.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 465 TDAdFPREMLIQQRFEAQAEQTPEAIAVLF------EDQHLTYRELNRRANQLAHHLIALGvQPDDRVALCVERSLEMMV 538
Cdd:PRK05691 2 MDA-FELPLTLVQALQRRAAQTPDRLALRFladdpgEGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 539 GLLGILKAGAAYVPmdpAYPAE--------RLAYILDDAAPVALLTQSA---QVAQLN----STLPTVL-LDT-PAAAAC 601
Cdd:PRK05691 80 AFFGCLYAGVIAVP---AYPPEsarrhhqeRLLSIIADAEPRLLLTVADlrdSLLQMEelaaANAPELLcVDTlDPALAE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 602 PDTNPVVQGlhaAHLAYVIYTSGSTGRPKGVMVAHRNVINlatglhTLLALDHPSRIALNAsivfDASVKNWIQLLsgHT 681
Cdd:PRK05691 157 AWQEPALQP---DDIAFLQYTSGSTALPKGVQVSHGNLVA------NEQLIRHGFGIDLNP----DDVIVSWLPLY--HD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 682 LVL-----------VPDALRADAHQLWRyfarhavdlfdctpvQLQWLLDAGL-------GSDPAYQPAQVLIGGEAISP 743
Cdd:PRK05691 222 MGLiggllqpifsgVPCVLMSPAYFLER---------------PLRWLEAISEyggtisgGPDFAYRLCSERVSESALER 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 744 AVWS------------RLQSL------------SDTRFINVYGPTECT----------------VDATACVVDRTQP--- 780
Cdd:PRK05691 287 LDLSrwrvaysgsepiRQDSLerfaekfaacgfDPDSFFASYGLAEATlfvsggrrgqgipaleLDAEALARNRAEPgtg 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 781 --LPTIGKPLANTRLYILDAQDQPV-PIGVTGELHIGGAGVARGYLHRPDLTAERFIpdpfsaDPAARIY-KTGDLArWL 856
Cdd:PRK05691 367 svLMSCGRSQPGHAVLIVDPQSLEVlGDNRVGEIWASGPSIAHGYWRNPEASAKTFV------EHDGRTWlRTGDLG-FL 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 857 PDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGV---------------QDAVVIAREDSPGDTRLVAylcarPDAE 921
Cdd:PRK05691 440 RDGELFVTGRLKDMLIVRGHNLYPQDIEKTVEREVEVvrkgrvaafavnhqgEEGIGIAAEISRSVQKILP-----PQAL 514
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 922 LHpaALRQQLAASLADymIPSAFVTLD--ALPLTPNGKLDRKA---------------LPAPDQTAfaTRDYEAPQGGIE 984
Cdd:PRK05691 515 IK--SIRQAVAEACQE--APSVVLLLNpgALPKTSSGKLQRSAcrlrladgsldsyalFPALQAVE--AAQTAASGDELQ 588
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 985 TALAALWQELLGLDRVGRHDQFFALGGHSLLAVQLLNRM-NKAGMDVALATLFAHPTLCDLAAAVTATAHD---APFTLP 1060
Cdd:PRK05691 589 ARIAAIWCEQLKVEQVAADDHFFLLGGNSIAATQVVARLrDELGIDLNLRQLFEAPTLAAFSAAVARQLAGggaAQAAIA 668
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1061 VADRTQPLPLSFSQQRLWFLAQLDPAASqAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPd 1140
Cdd:PRK05691 669 RLPRGQALPQSLAQNRLWLLWQLDPQSA-AYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDA- 746
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1141 TLGFSLSSHDLRKLDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAA 1220
Cdd:PRK05691 747 QGEFALQRIDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSR 826
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1221 LYQAALEGSEANLPPLPVQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAG 1300
Cdd:PRK05691 827 LYAAACQGQTAELAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDAS 906
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1301 QLRRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQ 1380
Cdd:PRK05691 907 LSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQ 986
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1381 VRERALDAYAHQALPFEQVVEILQPARSlsySPIFQVMLSLNNTPAQAL-TLPDLTlsAVERPQHSTH--FDLSLSLIET 1457
Cdd:PRK05691 987 VRQATLGAQAHQDLPFEQLVEALPQARE---QGLFQVMFNHQQRDLSALrRLPGLL--AEELPWHSREakFDLQLHSEED 1061
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1458 ENG-LNGGLVYATDLFDRETILRVVGYVENILMAMADDVTQPVATLPILPDSERRQvMLDFNATEADFPHDALIHQLvED 1536
Cdd:PRK05691 1062 RNGrLTLSFDYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQ-LAQWGQAPCAPAQAWLPELL-NE 1139
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1537 QAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAER 1616
Cdd:PRK05691 1140 QARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAER 1219
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1617 LAYMLDDASPVALLTQANqralLTGDVPR------ILLDTAdfsHLSEDNPHVPGLDAH--HLAYVIYTSGSTGKPKGVM 1688
Cdd:PRK05691 1220 LAYMLADSGVELLLTQSH----LLERLPQaegvsaIALDSL---HLDSWPSQAPGLHLHgdNLAYVIYTSGSTGQPKGVG 1292
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1689 NSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVP 1768
Cdd:PRK05691 1293 NTHAALAERLQWMQATYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVP 1372
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1769 SMLQQFVQWADAdCACDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWACQPDDHrSFVPIGRPIA 1847
Cdd:PRK05691 1373 PLLQLFIDEPLA-AACTSLRRLFSGGEALPAELRNRVLQRLpQVQLHNRYGPTETAINVTHWQCQAEDG-ERSPIGRPLG 1450
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1848 NTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFiNQPGARLYKTGDLARWLPDGSLEYLGRNDF 1927
Cdd:PRK05691 1451 NVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPL-GEDGARLYRTGDRARWNADGALEYLGRLDQ 1529
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1928 QVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGdTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDA 2007
Cdd:PRK05691 1530 QVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAG-AQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQ 1608
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2008 FPLTPNGKLDRKALPAPDQSavaTRDYEAPQGEVETALAAVWQDLLGLTRVGRHDHFFALGGHSLLIVSLIERLRRA-GL 2086
Cdd:PRK05691 1609 MPLGPSGKLDRRALPEPVWQ---QREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQAcDV 1685
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2087 ALDVRGVFSTPVLSDMAQAILAHQDKPAvvvppnripadstaitpdllplvTLTQPEIDRITDTvsggasniQDIyPLAP 2166
Cdd:PRK05691 1686 ELPLRALFEASELGAFAEQVARIQAAGE-----------------------RNSQGAIARVDRS--------QPV-PLSY 1733
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2167 LQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRT------AVCWQDLSQP--VQVVWRQailp 2238
Cdd:PRK05691 1734 SQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTtfpsvdGVPVQQVAEDsgLRMDWQD---- 1809
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2239 INHFEPTSPEDVLAQL---QAHteprtRRIDLSQAPLFRADIAHDPLQnEWLLALSFHHLISDHMTLALIVGEIRLLLQH 2315
Cdd:PRK05691 1810 FSALPADARQQRLQQLadsEAH-----QPFDLERGPLLRACLVKAAER-EHYFVLTLHHIVTEGWAMDIFARELGALYEA 1883
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2316 QADALPTPLP--------YRNFIAQTLSVPNSAHE-AYFRDKLAD--------VDEPTAPfgllnVQGSGGDIHeaRLVL 2378
Cdd:PRK05691 1884 FLDDRESPLEplpvqyldYSVWQRQWLESGERQRQlDYWKAQLGNehpllelpADRPRPP-----VQSHRGELY--RFDL 1956
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2379 DATLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRL-AGAEGadrIMGMFINTLPLRISL-ADRGA 2456
Cdd:PRK05691 1957 SPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIrPESEG---LIGAFLNTQVLRCQLdGQMSV 2033
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2457 AEVVERTSHDLMTLLEHEQAPlaLAQRCSGVAPPM-----PLFSTLLNYRHTQASSTdNTLSDIRV--LTSEER-TNYPL 2528
Cdd:PRK05691 2034 SELLEQVRQTVIEGQSHQDLP--FDHLVEALQPPRsaaynPLFQVMCNVQRWEFQQS-RQLAGMTVeyLVNDARaTKFDL 2110
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2529 TLAVDDRGEGFSLVAQTLEDIDPHRLLNYLMTAISSLVDALETEPQRSILNLPVLPDSERQQMLVDFNATDADIPRHALI 2608
Cdd:PRK05691 2111 NLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLDQTL 2190
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2609 HELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDP 2688
Cdd:PRK05691 2191 HGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDP 2270
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2689 TYPVERLRYMLDDAKPVALISQSAHLGIMnGSLPV-----ILLDDGETrpFDNEPDTPLDARKQgltPRHLAYVIYTSGS 2763
Cdd:PRK05691 2271 EYPLERLHYMIEDSGIGLLLSDRALFEAL-GELPAgvarwCLEDDAAA--LAAYSDAPLPFLSL---PQHQAYLIYTSGS 2344
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2764 TGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAmLIERHA 2843
Cdd:PRK05691 2345 TGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEEICQ-LIREQQ 2423
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2844 VSFMQATPSTWRML---VELRDFALPpgfKALC--GGEAL-PENLA--TALLQKvTTLWNLYGPTETTIW-------STL 2908
Cdd:PRK05691 2424 VSILGFTPSYGSQLaqwLAGQGEQLP---VRMCitGGEALtGEHLQriRQAFAP-QLFFNAYGPTETVVMplaclapEQL 2499
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2909 NGLTTPTPyIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSgAPEARMYKTGDLGR 2988
Cdd:PRK05691 2500 EEGAASVP-IGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFA-ADGGRLYRTGDLVR 2577
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2989 WLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAReDSPGDKRLVAYLLAQPDTVLEPAD------LR 3062
Cdd:PRK05691 2578 LRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAVAGQDDEAQaalreaLK 2656
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3063 QRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAPDqSAMATRGYEAPQGDLEHALAQIWQTLLGVERVGRHDHFFE 3142
Cdd:PRK05691 2657 AHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPD-PELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFE 2735
|
2890 2900 2910 2920
....*....|....*....|....*....|....*....|....*....
gi 641744967 3143 LGGHSLLAVQLNARIRAEFLTDIPiVAIFQHPQLSALAEVILAAQIHAA 3191
Cdd:PRK05691 2736 LGGDSILSIQVVSRARQLGIHFSP-RDLFQHQTVQTLAAVATHSEAAQA 2783
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
30-2461 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1478.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 30 PLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAIcWQGLHQPVQVVWRQAPLTVNTL 109
Cdd:PRK05691 677 PQSLAQNRLWLLWQLDPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRF-YERDGVALQRIDAQGEFALQRI 755
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 110 TTTSSDTVPAQLRAAT---DPSNHRLNLSNAPLLSATTAH--DPvcgEWLLSLSIHHLISDHITQALIIDEIRLLLEDRP 184
Cdd:PRK05691 756 DLSDLPEAEREARAAQireEEARQPFDLEKGPLLRVTLVRldDE---EHQLLVTLHHIVADGWSLNILLDEFSRLYAAAC 832
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 185 EALP---KPLP-----YRNFIAQILSVPLSEHE-QYFRNRLADiDTPTAPFDLVDVQGNGEDITEARLSL--DSSLADAL 253
Cdd:PRK05691 833 QGQTaelAPLPlgyadYGAWQRQWLAQGEAARQlAYWKAQLGD-EQPVLELATDHPRSARQAHSAARYSLrvDASLSEAL 911
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 254 RRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQgnLGADRVMGMFINTLPLRVSLRER-SVHDVVQATSH 332
Cdd:PRK05691 912 RGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPR--LETQGLVGFFINTQVLRAQLDGRlPFTALLAQVRQ 989
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 333 ELMMLLAHEQAPLALAQQCSQVPPPLPLFSTLFNyrHSQKDASSQF-----------WEGMR-----QLSGRERTNYPIT 396
Cdd:PRK05691 990 ATLGAQAHQDLPFEQLVEALPQAREQGLFQVMFN--HQQRDLSALRrlpgllaeelpWHSREakfdlQLHSEEDRNGRLT 1067
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 397 LSVDDLGDGFNltAKTVmgvdpERIVHYMLtaieNLVTSLEKTPQQPALSQPILPKSERQQvLVDFNATDADfPREMLIQ 476
Cdd:PRK05691 1068 LSFDYAAELFD--AATI-----ERLAEHFL----ALLEQVCEDPQRALGDVQLLDAAERAQ-LAQWGQAPCA-PAQAWLP 1134
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 477 QRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPA 556
Cdd:PRK05691 1135 ELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPD 1214
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 557 YPAERLAYILDDAAPVALLTQSAQVAQLNST--LPTVLLDTPAAAACPDTNPVVQgLHAAHLAYVIYTSGSTGRPKGVMV 634
Cdd:PRK05691 1215 YPAERLAYMLADSGVELLLTQSHLLERLPQAegVSAIALDSLHLDSWPSQAPGLH-LHGDNLAYVIYTSGSTGQPKGVGN 1293
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 635 AHRNVINLATGLHTLLALDHPSRIALNASIVFDASV-KNWIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPV 713
Cdd:PRK05691 1294 THAALAERLQWMQATYALDDSDVLMQKAPISFDVSVwECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPP 1373
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 714 QLQWLLDAGLGSDpAYQPAQVLIGGEAISPAVWSR-LQSLSDTRFINVYGPTECTVDAT--ACVVDRTQPLPtIGKPLAN 790
Cdd:PRK05691 1374 LLQLFIDEPLAAA-CTSLRRLFSGGEALPAELRNRvLQRLPQVQLHNRYGPTETAINVThwQCQAEDGERSP-IGRPLGN 1451
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 791 TRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSaDPAARIYKTGDLARWLPDGNIDYLGRNDFQ 870
Cdd:PRK05691 1452 VLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLG-EDGARLYRTGDRARWNADGALEYLGRLDQQ 1530
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 871 IKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGdTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDAL 950
Cdd:PRK05691 1531 VKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAG-AQLVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQM 1609
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 951 PLTPNGKLDRKALPAPDqtaFATRDYEAPQGGIETALAALWQELLGLDRVGRHDQFFALGGHSLLAVQLLNRMNKA-GMD 1029
Cdd:PRK05691 1610 PLGPSGKLDRRALPEPV---WQQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQAcDVE 1686
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1030 VALATLFAHPTLCDLAAAV----TATAHDAPFTLPVADRTQPLPLSFSQQRLWFLAQLDPAaSQAYHLPAALHLTGRLDR 1105
Cdd:PRK05691 1687 LPLRALFEASELGAFAEQVariqAAGERNSQGAIARVDRSQPVPLSYSQQRMWFLWQMEPD-SPAYNVGGMARLSGVLDV 1765
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1106 PALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDTlGFSLSSHDLRKLDEAARTTRVAELAEQEARARFDLTQGPLIRG 1185
Cdd:PRK05691 1766 DRFEAALQALILRHETLRTTFPSVDGVPVQQVAEDS-GLRMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRA 1844
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1186 QLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALEGSEANLPPLPVQYADYAVWQRQWLQ-GETLNDLrDYWR 1264
Cdd:PRK05691 1845 CLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWLEsGERQRQL-DYWK 1923
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1265 DQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVA 1344
Cdd:PRK05691 1924 AQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVA 2003
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1345 NRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQVRERALDAYAHQALPFEQVVEILQPARSLSYSPIFQVMLSLNNT 1424
Cdd:PRK05691 2004 NRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRW 2083
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1425 P-AQALTLPDLTLSAVERPQHSTHFDLSLSLIETENGLNGGLVYATDLFDRETILRVVGYVENILMAMADDVTQPVATLP 1503
Cdd:PRK05691 2084 EfQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELP 2163
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1504 ILPDSERRQVMLDFNATEADFPHDALIHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAI 1583
Cdd:PRK05691 2164 LLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGL 2243
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1584 CVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTqanQRALLT--GDVP----RILL--DTADFSH 1655
Cdd:PRK05691 2244 ALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLS---DRALFEalGELPagvaRWCLedDAAALAA 2320
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1656 LSEDNPHVPGLdAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYG 1735
Cdd:PRK05691 2321 YSDAPLPFLSL-PQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCG 2399
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1736 ARLVMaRPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADCACDSLRRVICSGEALPAELQQRFFARFN-AQLH 1814
Cdd:PRK05691 2400 ARVVL-RAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFApQLFF 2478
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1815 NLYGPTEAAidVTFWAC----QPDDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAER 1890
Cdd:PRK05691 2479 NAYGPTETV--VMPLAClapeQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAER 2556
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1891 FIPDPFiNQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAReDSPGDTRLVA 1970
Cdd:PRK05691 2557 FVADPF-AADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAG 2634
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1971 YL-CPQPGVTPDPAD-----LRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPAPDqSAVATRDYEAPQGEVETA 2044
Cdd:PRK05691 2635 YLvSAVAGQDDEAQAalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPD-PELNRQAYQAPRSELEQQ 2713
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2045 LAAVWQDLLGLTRVGRHDHFFALGGHSLLIVSLIERLRRAGLALDVRGVFSTPVLSDMAqailahqdkpAVVvppnripa 2124
Cdd:PRK05691 2714 LAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLA----------AVA-------- 2775
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2125 dstaitpdllplvtltqpeidRITDTVSGGASNIQDIYPLAPLQEGILFHHLLQEQ--GDTYLLRSmvafthRERLDAFL 2202
Cdd:PRK05691 2776 ---------------------THSEAAQAEQGPLQGASGLTPIQHWFFDSPVPQPQhwNQALLLEP------RQALDPAL 2828
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2203 --SALQQVIDRHDILRTAVC-----WQDLSQPV---QVVWrqailpinHFEPTSPEDVLAqLQAHTEprtRRIDLSQAPL 2272
Cdd:PRK05691 2829 leQALQALVEHHDALRLRFSqadgrWQAEYRAVtaqELLW--------QVTVADFAECAA-LFADAQ---RSLDLQQGPL 2896
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2273 FRADIAHDPlQNEWLLALSFHHLISDHMTLALIVGEIRLLLQHQADALPTPLP-----YRNFIAQTLSVPNSAHeayFRD 2347
Cdd:PRK05691 2897 LRALLVDGP-QGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPaktsaFRDWAARLQAYAGSES---LRE 2972
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2348 KL----ADVDEPTAPFGLLNVQGSGGDIHeARLV---LDATLASAIRQQ---ARHLGVSPgvLFHVAWAQVLAQTSGRDD 2417
Cdd:PRK05691 2973 ELgwwqAQLGGPRAELPCDRPQGGNLNRH-AQTVsvrLDAERTRQLLQQapaAYRTQVND--LLLTALARVLCRWSGQPS 3049
|
2490 2500 2510 2520
....*....|....*....|....*....|....*....|....*.
gi 641744967 2418 VVFGSVLLGRLAGAEGAD--RIMGMFINTLPLRISLADRGAAEVVE 2461
Cdd:PRK05691 3050 VLVQLEGHGREALFDDIDltRSVGWFTSAYPLRLTPAPGDDAARGE 3095
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1069-3182 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1399.69 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1069 PLSFSQQRLWFLAQLDPAASqAYHLPAALHLTGrLDRPALTTALNGLVARHESLRTRFTSIDG--QPAQQIDpDTLGFSL 1146
Cdd:PRK12316 1558 PLSPMQQGMLFHSLYEQEAG-DYINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGleQPLQVIH-KQVELPF 1634
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1147 SSHDLRKLDEAARTtrVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAal 1226
Cdd:PRK12316 1635 AELDWRGREDLGQA--LDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAG-- 1710
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1227 egseaNLPPLPV-QYADYAVWqrqwLQGETLNDLRDYWRDQLqgapALLEIPT---DRPRPSVQRYAGDQVPFHLDAGQL 1302
Cdd:PRK12316 1711 -----QPVAAPGgRYRDYIAW----LQRQDAAASEAFWKEQL----AALEEPTrlaQAARTEDGQVGYGDHQQLLDPAQT 1777
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1303 RRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPR--QELEGMVGFFVNTLALRTEPGRCHAVADLLDQ 1380
Cdd:PRK12316 1778 RALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAelPGIEQQIGLFINTLPVIAAPRPDQSVADWLQE 1857
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1381 VRERALDAYAHQALPFEQVveilQPARSLSYSPIFQVMLSLNNTP-AQAL---TLPDLTLSAVERpQHSTHFDLSLSlIE 1456
Cdd:PRK12316 1858 VQALNLALREHEHTPLYDI----QRWAGQGGEALFDSLLVFENYPvAEALkqgAPAGLVFGRVSN-HEQTNYPLTLA-VT 1931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1457 TENGLNGGLVYATDLFDRETILRVVGYVENILMAMADDVTQPVATLPILPDSERRQVMLDFNATEADFPHDALIHQLVED 1536
Cdd:PRK12316 1932 LGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAE 2011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1537 QAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAER 1616
Cdd:PRK12316 2012 QAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAER 2091
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1617 LAYMLDDASPVALLTQAN--QRALLTGDVPRILLDT-ADFSHLSEDNPHVPgLDAHHLAYVIYTSGSTGKPKGVMNSHRA 1693
Cdd:PRK12316 2092 LAYMLEDSGAALLLTQRHllERLPLPAGVARLPLDRdAEWADYPDTAPAVQ-LAGENLAYVIYTSGSTGLPKGVAVSHGA 2170
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1694 LCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMaRPDGHKDAAYLAQLIERTGITTLHFVPSMLQQ 1773
Cdd:PRK12316 2171 LVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLI-RDDELWDPEQLYDEMERHGVTILDFPPVYLQQ 2249
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1774 FVQWADADCACDSLRRVICSGEALPAELQQRFFARFNAQ-LHNLYGPTEAAIDVTFWACQPDD--HRSFVPIGRPIANTQ 1850
Cdd:PRK12316 2250 LAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPVyLFNGYGPTEAVVTPLLWKCRPQDpcGAAYVPIGRALGNRR 2329
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1851 LYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFINqPGARLYKTGDLARWLPDGSLEYLGRNDFQVK 1930
Cdd:PRK12316 2330 AYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSA-SGERLYRTGDLARYRADGVVEYLGRIDHQVK 2408
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1931 LRGFRIELGEIEARLMQCPGVQEAVVVAReDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPL 2010
Cdd:PRK12316 2409 IRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPL 2487
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2011 TPNGKLDRKALPAPDQSAvATRDYEAPQGEVETALAAVWQDLLGLTRVGRHDHFFALGGHSLLIVSLIERLRRA-GLALD 2089
Cdd:PRK12316 2488 NPNGKLDRKALPKPDVSQ-LRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDlGLEVP 2566
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2090 VRGVFSTPVLSDMAQAILAHQdkpavvvppnripadsTAITPDLLPlVTLTQPeidritdtvsggasniqdiYPLAPLQE 2169
Cdd:PRK12316 2567 LRILFERPTLAAFAASLESGQ----------------TSRAPVLQK-VTRVQP-------------------LPLSHAQQ 2610
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2170 GILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCWQDLSqpvqvvWRQAILPINHFEPTSPED 2249
Cdd:PRK12316 2611 RQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQ------TRQVILPNMSLRIVLEDC 2684
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2250 VL----AQLQAHTEPRTRRIDLSQAPLFRADIAHDPLQNEWLLaLSFHHLISDHMTLALIVGEIRLLLQHQADALPTPLP 2325
Cdd:PRK12316 2685 AGvadaAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLV-ITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLP 2763
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2326 --------YRNFIAQTLSVPNSAHE-AYFRDKLADVDePTAPFGLLNVQGSGGDIHEARLV--LDATLASAIRQQARHLG 2394
Cdd:PRK12316 2764 plplqyadYAAWQRAWMDSGEGARQlDYWRERLGGEQ-PVLELPLDRPRPALQSHRGARLDvaLDVALSRELLALARREG 2842
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2395 VSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRlaGAEGADRIMGMFINTLPLRISLADRGA-AEVVERTSHDLMTLLEH 2473
Cdd:PRK12316 2843 VTLFMLLLASFQVLLHRYSGQSDIRVGVPIANR--NRAETERLIGFFVNTQVLRAQVDAQLAfRDLLGQVKEQALGAQAH 2920
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2474 EQAP---LALAQRCSGVAPPMPLFSTLLNyrHTQASSTDNTLSDIRVLT-----SEERTNYPLTLAVDDRGEGFSLVAQT 2545
Cdd:PRK12316 2921 QDLPfeqLVEALQPERSLSHSPLFQVMYN--HQSGERAAAQLPGLHIESfawdgAATQFDLALDTWESAEGLGASLTYAT 2998
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2546 leDIDPHRLLNYLMTAISSLVDALETEPQRSILNLPVLPDSERQQMLVDFNATDADIPRHALIHELFEAQVACTPDAIAV 2625
Cdd:PRK12316 2999 --DLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVAL 3076
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2626 VFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPV 2705
Cdd:PRK12316 3077 AFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQ 3156
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2706 ALISQSAHLGIMNGSLPVILLDDGETRPFDNEPDTpldarkqGLTPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMR 2785
Cdd:PRK12316 3157 LLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAI-------RTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQ 3229
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2786 KEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVELRDFAL 2865
Cdd:PRK12316 3230 QAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFLEEEDAHR 3309
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2866 PPGFK-ALCGGEALPENLATALLQKVtTLWNLYGPTETTIWSTLNGLTTP---TPYIGHPIANTQIYILDAQGRVVPLGV 2941
Cdd:PRK12316 3310 CTSLKrIVCGGEALPADLQQQVFAGL-PLYNLYGPTEATITVTHWQCVEEgkdAVPIGRPIANRACYILDGSLEPVPVGA 3388
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2942 AGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRL 3021
Cdd:PRK12316 3389 LGELYLGGEGLARGYHNRPGLTAERFVPDPF--VPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARL 3466
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3022 ARCHGVHDAVVIAREdspgDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAPD 3101
Cdd:PRK12316 3467 LEHPWVREAVVLAVD----GRQLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPD 3542
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3102 qSAMATRGYEAPQGDLEHALAQIWQTLLGVERVGRHDHFFELGGHSLLAVQLNARIRAEFLTDIPiVAIFQHPQLSALAE 3181
Cdd:PRK12316 3543 -AALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTP-KDLFQHQTIQGLAR 3620
|
.
gi 641744967 3182 V 3182
Cdd:PRK12316 3621 V 3621
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1051-2406 |
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: 1218.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1051 TAHDAPFTLPVADRTQPLPLSFSQQRLWFLAQLDPAaSQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSID 1130
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLG-SAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1131 GQPAQQIDPDtLGFSLSSHDLRKLDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWS 1210
Cdd:COG1020 80 GRPVQVIQPV-VAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1211 IGILARELAALYQAALEGSEANLPPLPVQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAPALLEIPTDRPRPSVQRYAG 1290
Cdd:COG1020 159 DGLLLAELLRLYLAAYAGAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1291 DQVPFHLDAGQLRRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGR 1370
Cdd:COG1020 239 ARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1371 CHAVADLLDQVRERALDAYAHQALPFEQVVEILQPARSLSYSPIFQVMLSLNNTPAQALTLPDLTLSAVERPQHSTHFDL 1450
Cdd:COG1020 319 DPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLELDSGTAKFDL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1451 SLSLIETENGLNGGLVYATDLFDRETILRVVGYVENILMAMADDVTQPVATLPILPDSERRQVMLDFNATEADFPHDALI 1530
Cdd:COG1020 399 TLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATL 478
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1531 HQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDP 1610
Cdd:COG1020 479 HELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDP 558
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1611 GYPAERLAYMLDDASPVALLTQANQRALLTG-DVPRILLDTADFSHLSEDNPHVPgLDAHHLAYVIYTSGSTGKPKGVMN 1689
Cdd:COG1020 559 AYPAERLAYMLEDAGARLVLTQSALAARLPElGVPVLALDALALAAEPATNPPVP-VTPDDLAYVIYTSGSTGRPKGVMV 637
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1690 SHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPS 1769
Cdd:COG1020 638 EHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPS 717
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1770 MLQQFVQWADAdcACDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWACQPDDHRS-FVPIGRPIA 1847
Cdd:COG1020 718 LLRALLDAAPE--ALPSLRLVLVGGEALPPELVRRWRARLpGARLVNLYGPTETTVDSTYYEVTPPDADGgSVPIGRPIA 795
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1848 NTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFiNQPGARLYKTGDLARWLPDGSLEYLGRNDF 1927
Cdd:COG1020 796 NTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPF-GFPGARLYRTGDLARWLPDGNLEFLGRADD 874
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1928 QVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDA 2007
Cdd:COG1020 875 QVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLP 954
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2008 FPLTPNGKLDRKALPAPDQSAVATrdYEAPQGEVETALAAVWQDLLGLTRVGRHDHFFALGGHSLLIVSLIERLRRAGLA 2087
Cdd:COG1020 955 LPLTGNGKLDRLALPAPAAAAAAA--AAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLL 1032
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2088 LDVRGVFSTPVLSDMAQAILAHQDKPAVVVPPNRIPADSTAITPDLLPLVTLTQpeidritdtvsggasniqdiypLAPL 2167
Cdd:COG1020 1033 LLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLAL----------------------LLLL 1090
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2168 QEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCWQDLSQPVQVVWRQAILPINHFEPTSP 2247
Cdd:COG1020 1091 ALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAA 1170
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2248 EDVLAQLQAHTEPRTRRIDLSQAPLFRADIAHDPLQNEWLLALSFHHLISDHMTLALIVGEIRLLLQHQADALPTPLPYR 2327
Cdd:COG1020 1171 AALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALA 1250
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 2328 NFIAQTLSVPNSAHEAYFRDKLADVDEPTAPFGLLNVQGSGGDIHEARLVLDATLASAIRQQARHLGVSPGVLFHVAWA 2406
Cdd:COG1020 1251 ALAALAAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1066-2459 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1184.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1066 QPLPLSFSQQRLWFLAQLDPAaSQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIdPDTLGFS 1145
Cdd:PRK12316 48 ERDRLSYAQQRMWFLWQLEPQ-SGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQV-PLDRPLE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1146 LSSHDLRKLDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAA 1225
Cdd:PRK12316 126 VEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAY 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1226 LEGSEANLPPLPVQYADYAVWQRQWLQ-GETLNDLrDYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAGQLRR 1304
Cdd:PRK12316 206 ATGAEPGLPALPIQYADYALWQRSWLEaGEQERQL-EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEA 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1305 LHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQVRER 1384
Cdd:PRK12316 285 LRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDT 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1385 ALDAYAHQALPFEQVVEILQPARSLSYSPIFQVMLSLNNTPAQ---ALTLPDLTLSAVERPQHSTHFDLSLSLIETENGL 1461
Cdd:PRK12316 365 VLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQPLVADieaLDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRL 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1462 NGGLVYATDLFDRETILRVVGYVENILMAMADDVTQPVATLPILPDSERRQVMLDFNATEADFPHDALIHQLVEDQAART 1541
Cdd:PRK12316 445 HAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERT 524
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1542 PDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYML 1621
Cdd:PRK12316 525 PEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYML 604
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1622 DDASPVALLTQANQRALL--TGDVPRILLD--TADFSHLSEDNPHVpGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNR 1697
Cdd:PRK12316 605 EDSGVQLLLSQSHLGRKLplAAGVQVLDLDrpAAWLEGYSEENPGT-ELNPENLAYVIYTSGSTGKPKGAGNRHRALSNR 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1698 LVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQW 1777
Cdd:PRK12316 684 LCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1778 ADADcACDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWACQPDDHRSfVPIGRPIANTQLYILDT 1856
Cdd:PRK12316 764 EDVA-SCTSLRRIVCSGEALPADAQEQVFAKLpQAGLYNLYGPTEAAIDVTHWTCVEEGGDS-VPIGRPIANLACYILDA 841
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1857 LGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFINqpGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRI 1936
Cdd:PRK12316 842 NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVA--GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRI 919
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1937 ELGEIEARLMQCPGVQEAVVVAREDSpgdtRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKL 2016
Cdd:PRK12316 920 ELGEIEARLLEHPWVREAAVLAVDGK----QLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKL 995
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2017 DRKALPAPDQSaVATRDYEAPQGEVETALAAVWQDLLGLTRVGRHDHFFALGGHSLLIVSLIERLRRAGLALDVRGVFST 2096
Cdd:PRK12316 996 DRKALPAPEAS-VAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQH 1074
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2097 PVLSDMAQAILAHQdkpavvvppnripadstAITPDLLPlvtltqpeidritdtVSGGAsniqdiyPLAPLQEGILFHHL 2176
Cdd:PRK12316 1075 QTIRSLALVAKAGQ-----------------ATAADQGP---------------ASGEV-------ALAPVQRWFFEQAI 1115
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2177 LQEQ--GDTYLLRSmvafthRERLDAFL--SALQQVIDRHDILRTAVCWQDLSqpvqvvWRQAilpinhFEPTSPEDVLA 2252
Cdd:PRK12316 1116 PQRQhwNQSLLLQA------RQPLDPDRlgRALERLVAHHDALRLRFREEDGG------WQQA------YAAPQAGEVLW 1177
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2253 Q--------LQAHTEPRTRRIDLSQAPLFRADIAHDPLQNEWLLaLSFHHLISDHMTLALIVGEIRLLLQHQADALPTPL 2324
Cdd:PRK12316 1178 QrqaaseeeLLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLL-LVIHHLVVDGVSWRILLEDLQRAYADLDADLPART 1256
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2325 PYRNFIAQTLS--VPNSAHE-AYFRDKLADvdeptAPFGLL--NVQGSGGDIHEARLV--LDATLASAIRQQArhlgvsP 2397
Cdd:PRK12316 1257 SSYQAWARRLHehAGARAEElDYWQAQLED-----APHELPceNPDGALENRHERKLElrLDAERTRQLLQEA------P 1325
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641744967 2398 GV-------LFHVAWAQVLAQTSGRDDVVFGSVLLGRLAGAEGAD--RIMGMFINTLPLRISLADRGAAEV 2459
Cdd:PRK12316 1326 AAyrtqvndLLLTALARVTCRWSGQASVLVQLEGHGREDLFEDIDlsRTVGWFTSLFPVRLTPAADLGESI 1396
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
16-1328 |
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: 940.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 16 ATVPDGVANVQDIYPLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAIC--WQGLHQ 93
Cdd:COG1020 5 AAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRtrAGRPVQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 94 PVQVVWRQAPLTVNTLTTTSSDTVPAQLRAATDPSNHRLNLSNAPLLSATTAHDPVcGEWLLSLSIHHLISDHITQALII 173
Cdd:COG1020 85 VIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLL-LLLLLLLALHHIISDGLSDGLLL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 174 DEIRLLLEDRPEALPKPLP---------YRNFIAQILSVPLSEHEQYFRNRLA-DIDTPTAPFDLVDVQGNGEDITEARL 243
Cdd:COG1020 164 AELLRLYLAAYAGAPLPLPplpiqyadyALWQREWLQGEELARQLAYWRQQLAgLPPLLELPTDRPRPAVQSYRGARVSF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 244 SLDSSLADALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQgnLGADRVMGMFINTLPLRVSLR-ERS 322
Cdd:COG1020 244 RLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLSgDPS 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 323 VHDVVQATSHELMMLLAHEQAPLALAQ---QCSQVPPPLPLFSTLFNYRHSQKDASSQFWEGMRQLS-GRERTNYPITLS 398
Cdd:COG1020 322 FAELLARVRETLLAAYAHQDLPFERLVeelQPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLElDSGTAKFDLTLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 399 VDDLGDGFNLTAKTVMGVDPERIVHYMLTAIENLVTSLEKTPQQPALSQPILPKSERQQVLVDFNATDADFPREMLIQQR 478
Cdd:COG1020 402 VVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHEL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 479 FEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYP 558
Cdd:COG1020 482 FEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYP 561
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 559 AERLAYILDDAAPVALLTQSAQVAQL-NSTLPTVLLDTPAAAACPDTNPVVqGLHAAHLAYVIYTSGSTGRPKGVMVAHR 637
Cdd:COG1020 562 AERLAYMLEDAGARLVLTQSALAARLpELGVPVLALDALALAAEPATNPPV-PVTPDDLAYVIYTSGSTGRPKGVMVEHR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 638 NVINLATGLHTLLALDHPSRIALNASIVFDASVKN-WIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQ 716
Cdd:COG1020 641 ALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEiFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 717 WLLDAGLGSDPayQPAQVLIGGEAISPAVWSRLQS-LSDTRFINVYGPTECTVDATACVV---DRTQPLPTIGKPLANTR 792
Cdd:COG1020 721 ALLDAAPEALP--SLRLVLVGGEALPPELVRRWRArLPGARLVNLYGPTETTVDSTYYEVtppDADGGSVPIGRPIANTR 798
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 793 LYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSAdPAARIYKTGDLARWLPDGNIDYLGRNDFQIK 872
Cdd:COG1020 799 VYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGF-PGARLYRTGDLARWLPDGNLEFLGRADDQVK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 873 VRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPL 952
Cdd:COG1020 878 IRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPL 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 953 TPNGKLDRKALPAPDQTafATRDYEAPQGGIETALAALWQELLGLDRVGRHDQFFALGGHSLLAVQLLNRMNKAGMDVAL 1032
Cdd:COG1020 958 TGNGKLDRLALPAPAAA--AAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLL 1035
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1033 ATLFAHPTLCDLAAAVTATAHDAPFTLPVADRTQPLPLSFSQQRLWFLAQLDPAASQAYHLPAALHLTGRLDRPALTTAL 1112
Cdd:COG1020 1036 LLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLL 1115
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1113 NGLVARHESLRTRFTSIDGQPAQQIDPDTLgfsLSSHDLRKLDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDD 1192
Cdd:COG1020 1116 ALLLALLAALRARRAVRQEGPRLRLLVALA---AALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLL 1192
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1193 NTHVLLLTQHHIISDGWSIGILARELAALYQAALEGSEANLPPLPVQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAPA 1272
Cdd:COG1020 1193 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALL 1272
|
1290 1300 1310 1320 1330
....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 1273 LLEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRLHALNRQQGTTLFMTLLAAWSVVL 1328
Cdd:COG1020 1273 LLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1059-2111 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 882.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1059 LPVADRTQPLPLSFSQQRLWFLAQLDPAASQaYHLPAALHLTGrLDRPALTTALNGLVARHESLRTRFTSID--GQPAQQ 1136
Cdd:PRK12316 4094 LPLGEIEDIYPLSPMQQGMLFHSLYEQEAGD-YINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGelGRPLQV 4171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1137 IDpDTLGFSLSSHDLRKldEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILAR 1216
Cdd:PRK12316 4172 VH-KQVSLPFAELDWRG--RADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLG 4248
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1217 ELAALYqaalegSEANLPPLPVQYADYAVWqrqwLQGETLNDLRDYWRDQLqgapALLEIPTdRPRPSVQRYAGDQVPFH 1296
Cdd:PRK12316 4249 EVLERY------SGRPPAQPGGRYRDYIAW----LQRQDAAASEAFWREQL----AALDEPT-RLAQAIARADLRSANGY 4313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1297 ------LDAGQLRRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRP--RQELEGMVGFFVNTLALRTEP 1368
Cdd:PRK12316 4314 gehvreLDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPaeLPGIEGQIGLFINTLPVIATP 4393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1369 GRCHAVADLLDQVRERALDAYAHQALPFEQvveiLQPARSLSYSPIFQVMLSLNNTPA----QALTLPDLTLSAVE-RPQ 1443
Cdd:PRK12316 4394 RAQQSVVEWLQQVQRQNLALREHEHTPLYE----IQRWAGQGGEALFDSLLVFENYPVsealQQGAPGGLRFGEVTnHEQ 4469
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1444 HSTHFDLSLSLIETengLNGGLVYATDLFDRETILRVVGYVENILMAMADDVTQPVATLPILPDSERRQVMLDFNATEAD 1523
Cdd:PRK12316 4470 TNYPLTLAVGLGET---LSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAG 4546
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1524 FPHDALIHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGA 1603
Cdd:PRK12316 4547 YPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGG 4626
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1604 AYVPLDPGYPAERLAYMLDDASPVALLTQAN--QRALLTGDVPRILLD-TADFSHLSEDNPHVPgLDAHHLAYVIYTSGS 1680
Cdd:PRK12316 4627 AYVPLDPEYPRERLAYMMEDSGAALLLTQSHllQRLPIPDGLASLALDrDEDWEGFPAHDPAVR-LHPDNLAYVIYTSGS 4705
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1681 TGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMaRPDGHKDAAYLAQLIERTG 1760
Cdd:PRK12316 4706 TGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVI-RDDSLWDPERLYAEIHEHR 4784
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1761 ITTLHFVPSMLQQFVQWADADCACDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWACQPDDH--R 1837
Cdd:PRK12316 4785 VTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQASYDLAWRALkPVYLFNGYGPTETTVTVLLWKARDGDAcgA 4864
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1838 SFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFiNQPGARLYKTGDLARWLPDG 1917
Cdd:PRK12316 4865 AYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPF-GAPGGRLYRTGDLARYRADG 4943
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1918 SLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGdTRLVAYLCPQ-PGVTPDP---ADLRQQLGQHL 1993
Cdd:PRK12316 4944 VIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG-KQLVGYVVPQdPALADADeaqAELRDELKAAL 5022
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1994 A----EYMVPGAFVTLDAFPLTPNGKLDRKALPAPDQSAvATRDYEAPQGEVETALAAVWQDLLGLTRVGRHDHFFALGG 2069
Cdd:PRK12316 5023 RerlpEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASL-LQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGG 5101
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|...
gi 641744967 2070 HSLLIVSLIERLRRA-GLALDVRGVFSTPVLSDMAQAiLAHQD 2111
Cdd:PRK12316 5102 HSLLAIQVTSRIQLElGLELPLRELFQTPTLAAFVEL-AAAAG 5143
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2159-3191 |
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: 868.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2159 QDIYPLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVC--WQDLSQPVQVVWRQAI 2236
Cdd:COG1020 15 AAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRtrAGRPVQVIQPVVAAPL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2237 LPINHFEPTSPEDVLAQLQAHTEPRTRRIDLSQAPLFRADIAHDPLQnEWLLALSFHHLISDHMTLALIVGEIRLLLQHQ 2316
Cdd:COG1020 95 PVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLL-LLLLLLALHHIISDGLSDGLLLAELLRLYLAA 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2317 ADALPTPLP---------YRNFIAQTLSVPNSAHEAYFRDKLA-DVDEPTAPFGLLNVQGSGGDIHEARLVLDATLASAI 2386
Cdd:COG1020 174 YAGAPLPLPplpiqyadyALWQREWLQGEELARQLAYWRQQLAgLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAAL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2387 RQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRlaGAEGADRIMGMFINTLPLRISL-ADRGAAEVVERTSH 2465
Cdd:COG1020 254 RALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGR--PRPELEGLVGFFVNTLPLRVDLsGDPSFAELLARVRE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2466 DLMTLLEHEQAPLALAQR---CSGVAPPMPLFSTLLNYRHTQASSTDNTLSDIRVLT-SEERTNYPLTLAVDDRGEGFSL 2541
Cdd:COG1020 332 TLLAAYAHQDLPFERLVEelqPERDLSRNPLFQVMFVLQNAPADELELPGLTLEPLElDSGTAKFDLTLTVVETGDGLRL 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2542 VAQTLEDIDPHRLLNYLMTAISSLVDALETEPQRSILNLPVLPDSERQQMLVDFNATDADIPRHALIHELFEAQVACTPD 2621
Cdd:COG1020 412 TLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYPADATLHELFEAQAARTPD 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2622 AIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDD 2701
Cdd:COG1020 492 AVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLED 571
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2702 AKPVALISQSAHLG-IMNGSLPVILLDDGEtrpFDNEPDTPLDArkqGLTPRHLAYVIYTSGSTGKPKGVMVEHANMVNF 2780
Cdd:COG1020 572 AGARLVLTQSALAArLPELGVPVLALDALA---LAAEPATNPPV---PVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNL 645
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2781 LCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVEL 2860
Cdd:COG1020 646 LAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLDA 725
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2861 RDFALPPGFKALCGGEALPENLATALLQKV--TTLWNLYGPTETTIWSTLNGLTTPTPY-----IGHPIANTQIYILDAQ 2933
Cdd:COG1020 726 APEALPSLRLVLVGGEALPPELVRRWRARLpgARLVNLYGPTETTVDSTYYEVTPPDADggsvpIGRPIANTRVYVLDAH 805
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2934 GRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsGAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIE 3013
Cdd:COG1020 806 LQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPF-GFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIE 884
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3014 LGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLD 3093
Cdd:COG1020 885 LGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLD 964
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3094 RKALPAPDQSAMATrgYEAPQGDLEHALAQIWQTLLGVERVGRHDHFFELGGHSLLAVQLNARIRAEFLTDIPIVAIFQH 3173
Cdd:COG1020 965 RLALPAPAAAAAAA--AAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLA 1042
|
1050
....*....|....*...
gi 641744967 3174 PQLSALAEVILAAQIHAA 3191
Cdd:COG1020 1043 AAAAAAAAAAAAAAAAAA 1060
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1061-2111 |
0e+00 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 865.51 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1061 VADRTQPLPLSFSQQRLWFLAQLDPAASqAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPD 1140
Cdd:PRK10252 1 AEPMSQHLPLVAAQPGIWMAEKLSPLPS-AWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1141 TLGFSLSSHDLRKLDEAARTTRVaeLAEQEARARFDLTQG-PLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELA 1219
Cdd:PRK10252 80 LTFPLPEIIDLRTQPDPHAAAQA--LMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1220 ALYQAALEGSEANLPPLPVQ---YADYAVWQrqwlQGETLNDLRDYWRDQLQGAPallEIPTDRPRPSVQRYAGD---QV 1293
Cdd:PRK10252 158 AIYCAWLRGEPTPASPFTPFadvVEEYQRYR----ASEAWQRDAAFWAEQRRQLP---PPASLSPAPLPGRSASAdilRL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1294 PFHLDAGQLRRLHALNRQ-QGTTLFMTLLAAWsvvLSRLSGQDDIVIGTPVANR---PRQELEGMVgffVNTLALRTEPG 1369
Cdd:PRK10252 231 KLEFTDGAFRQLAAQASGvQRPDLALALVALW---LGRLCGRMDYAAGFIFMRRlgsAALTATGPV---LNVLPLRVHIA 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1370 RCHAVADLLDQVRERALDAYAHQALPFEQVVEILQPA---RSLsYSPIFQVM-----LSLNNTPAQALTLpdlTLSAVEr 1441
Cdd:PRK10252 305 AQETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAagdEPL-FGPVLNIKvfdyqLDFPGVQAQTHTL---ATGPVN- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1442 pqhsthfDLSLSL-IETENGLNGGLVYATDLFDRETILRVVGYVENILMAMADDVTQPVATLPILPDSERRQVMlDFNAT 1520
Cdd:PRK10252 380 -------DLELALfPDEHGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLA-QVNAT 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1521 EADFPHDALIhQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILK 1600
Cdd:PRK10252 452 AVEIPETTLS-ALVAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVE 530
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1601 AGAAYVPLDPGYPAERLAYMLDDASPVALLTQANQRALLTgDVPRILLDTADFSHLSEDNPHVPGLDAHHLAYVIYTSGS 1680
Cdd:PRK10252 531 AGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFA-DVPDLTSLCYNAPLAPQGAAPLQLSQPHHTAYIIFTSGS 609
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1681 TGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTG 1760
Cdd:PRK10252 610 TGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYG 689
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1761 ITTLHFVPSMLQQFVQWAD---ADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTFWACQPDDHR 1837
Cdd:PRK10252 690 VTTTHFVPSMLAAFVASLTpegARQSCASLRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEELA 769
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1838 SF----VPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFInqPGARLYKTGDLARW 1913
Cdd:PRK10252 770 AVrgssVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA--PGERMYRTGDVARW 847
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1914 LPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAR-----EDSPGD-TRLVAYLCPQPGVTPDPADLRQ 1987
Cdd:PRK10252 848 LDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaAATGGDaRQLVGYLVSQSGLPLDTSALQA 927
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1988 QLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPAPD-QSAVATRdyeAPQGEVETALAAVWQDLLGLTRVGRHDHFFA 2066
Cdd:PRK10252 928 QLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPElKAQVPGR---APKTGTETIIAAAFSSLLGCDVVDADADFFA 1004
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*.
gi 641744967 2067 LGGHSLLIVSLIERLRRA-GLALDVRGVFSTPVLSDMAQAILAHQD 2111
Cdd:PRK10252 1005 LGGHSLLAMKLAAQLSRQfARQVTPGQVMVASTVAKLATLLDAEED 1050
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1059-2129 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 848.29 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1059 LPVADRTQPLPLSFSQQRLWFLAQLDPAASQaYHLPAALHLTGrLDRPALTTALNGLVARHESLRTRFTSIDG--QPAQQ 1136
Cdd:PRK12467 2638 VAVGDIEDIYPLSPMQQGMLFHTLYEGGAGD-YINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGEleEPLQV 2715
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1137 IDPD-TLGFSlsSHDLRklDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILA 1215
Cdd:PRK12467 2716 VYKQaRLPFS--RLDWR--DRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLL 2791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1216 RELAALYqaalegSEANLPPLPVQYADYAvwqrQWLQGETLNDLRDYWRDQLQ--GAPALLeIPTDRPRPSVQRYAGDQV 1293
Cdd:PRK12467 2792 GEVLQRY------FGQPPPAREGRYRDYI----AWLQAQDAEASEAFWKEQLAalEEPTRL-ARALYPAPAEAVAGHGAH 2860
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1294 PFHLDAGQLRRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQ--ELEGMVGFFVNTLALRTEPGRC 1371
Cdd:PRK12467 2861 YLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQlrGAEQQLGLFINTLPVIASPRAE 2940
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1372 HAVADLLDQVRERALDAYAHQALPFEQVveilQPARSLSYSPIFQVMLSLNNTP-AQAL---TLPDLTLSAVE-RPQHST 1446
Cdd:PRK12467 2941 QTVSDWLQQVQAQNLALREFEHTPLADI----QRWAGQGGEALFDSILVFENYPiSEALkqgAPSGLRFGAVSsREQTNY 3016
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1447 HFDLSLSLIETengLNGGLVYATDLFDRETILRVVGYVENILMAMADDVTQPVATLPILPDSERRQVMLDFNATEADFPH 1526
Cdd:PRK12467 3017 PLTLAVGLGDT---LELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPS 3093
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1527 DALIHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYV 1606
Cdd:PRK12467 3094 ERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYV 3173
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1607 PLDPGYPAERLAYMLDDASPVALLTQAN---QRALLTGDVpRILLDTADFSHLSEDNPhVPGLDAHHLAYVIYTSGSTGK 1683
Cdd:PRK12467 3174 PLDPEYPRERLAYMIEDSGVKLLLTQAHlleQLPAPAGDT-ALTLDRLDLNGYSENNP-STRVMGENLAYVIYTSGSTGK 3251
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1684 PKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMaRPDGHKDAAYLAQLIERTGITT 1763
Cdd:PRK12467 3252 PKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCLVV-RDNDLWDPEELWQAIHAHRISI 3330
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1764 LHFVPSMLQQFVQWAD-ADCAcdSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWACQPD--DHRSF 1839
Cdd:PRK12467 3331 ACFPPAYLQQFAEDAGgADCA--SLDIYVFGGEAVPPAAFEQVKRKLkPRGLTNGYGPTEAVVTVTLWKCGGDavCEAPY 3408
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1840 VPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFINQpGARLYKTGDLARWLPDGSL 1919
Cdd:PRK12467 3409 APIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGS-GGRLYRTGDLARYRADGVI 3487
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1920 EYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAReDSPGDTRLVAYLCPQpgvtpDP-ADLRQQLGQHLA---- 1994
Cdd:PRK12467 3488 EYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPA-----DPqGDWRETLRDHLAaslp 3561
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1995 EYMVPGAFVTLDAFPLTPNGKLDRKALPAPDqsAVATRDYEAPQGEVETALAAVWQDLLGLTRVGRHDHFFALGGHSLLI 2074
Cdd:PRK12467 3562 DYMVPAQLLVLAAMPLGPNGKVDRKALPDPD--AKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLA 3639
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 2075 VSLIERLRRA-GLALDVRGVFSTPVLSDMAQAILAHQDKPAVVVPPNRIPADSTAI 2129
Cdd:PRK12467 3640 LQVLSRIRQSlGLKLSLRDLMSAPTIAELAGYSPLGDVPVNLLLDLNRLETGFPAL 3695
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2129-3186 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 803.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2129 ITPDLLPLVTLTQPEIDritdTVSGGASNIQDIYPLAPLQEGILFHHLLQEQGDTYL--LRSMVAFTHRERldaFLSALQ 2206
Cdd:PRK12316 4074 VTPSDFPLAGLDQARLD----ALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYInqMRVDVQGLDVER---FRAAWQ 4146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2207 QVIDRHDILRTAVCWQD-LSQPVQVVWRQAILPINHFEPTSPEDVLAQLQA-HTEPRTRRIDLSQAPLFRADIAHDPlQN 2284
Cdd:PRK12316 4147 AALDRHDVLRSGFVWQGeLGRPLQVVHKQVSLPFAELDWRGRADLQAALDAlAAAERERGFDLQRAPLLRLVLVRTA-EG 4225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2285 EWLLALSFHHLISDHMTLALIVGEIrllLQHQADALPTP--LPYRNFIAQTLSVPNSAHEAYFRDKLADVDEPT------ 2356
Cdd:PRK12316 4226 RHHLIYTNHHILMDGWSNSQLLGEV---LERYSGRPPAQpgGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTrlaqai 4302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2357 APFGLLNVQGSGGDIHEarlvLDATLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRLAGAEGADR 2436
Cdd:PRK12316 4303 ARADLRSANGYGEHVRE----LDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEG 4378
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2437 IMGMFINTLPLRISL-ADRGAAEVVERTSHDLMTLLEHEQAPLALAQRCSGVAPPmPLFSTLLNYRHTQASST--DNTLS 2513
Cdd:PRK12316 4379 QIGLFINTLPVIATPrAQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGE-ALFDSLLVFENYPVSEAlqQGAPG 4457
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2514 DIRV--LTSEERTNYPLTLAVDdRGEGFSL---------VAQTLEDIDPHrllnylmtaISSLVDALETEPQRSILNLPV 2582
Cdd:PRK12316 4458 GLRFgeVTNHEQTNYPLTLAVG-LGETLSLqfsydrghfDAATIERLARH---------LTNLLEAMAEDPQRRLGELQL 4527
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2583 LPDSERQQMLVDFNATDADIPRHALIHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAIC 2662
Cdd:PRK12316 4528 LEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIA 4607
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2663 VERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQS---AHLGIMNG--SLPVILLDDGETRPfDNE 2737
Cdd:PRK12316 4608 MERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQShllQRLPIPDGlaSLALDRDEDWEGFP-AHD 4686
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2738 PDTPLDarkqgltPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLN 2817
Cdd:PRK12316 4687 PAVRLH-------PDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLIN 4759
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2818 GARLILATQAQAADAQQLAmLIERHAVSFMQATPSTWRMLVE--LRDFALPPGFKALCGGEALPENLATALLQ--KVTTL 2893
Cdd:PRK12316 4760 GASVVIRDDSLWDPERLYA-EIHEHRVTVLVFPPVYLQQLAEhaERDGEPPSLRVYCFGGEAVAQASYDLAWRalKPVYL 4838
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2894 WNLYGPTETTIWSTLNGLTTPTP------YIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERF 2967
Cdd:PRK12316 4839 FNGYGPTETTVTVLLWKARDGDAcgaaymPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERF 4918
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2968 ITDPFsGAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGdKRLVAY 3047
Cdd:PRK12316 4919 VPDPF-GAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG-KQLVGY 4996
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3048 LLAQpDTVLEPAD---------LRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAPDQSAmATRGYEAPQGDLE 3118
Cdd:PRK12316 4997 VVPQ-DPALADADeaqaelrdeLKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASL-LQQAYVAPRSELE 5074
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 3119 HALAQIWQTLLGVERVGRHDHFFELGGHSLLAVQLNARIRAEFLTDIPIVAIFQHPQLSALAEVILAA 3186
Cdd:PRK12316 5075 QQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAA 5142
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-1252 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 772.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2 PLVTLSQEEIDTViatvPDGVANVQDIYPLAPLQEGILFHYQLQEKGDTYLlnsllafdSQTRLD-------AFLDVLQQ 74
Cdd:PRK12467 2624 PLAGLSQEQLDRL----PVAVGDIEDIYPLSPMQQGMLFHTLYEGGAGDYI--------NQMRVDvegldveRFRTAWQA 2691
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 75 VIARHDILRTAICWQG-LHQPVQVVWRQAPLTVNTLTTTSSDTVPAQLR--AATDPSNHrLNLSNAPLLSAT---TAHDp 148
Cdd:PRK12467 2692 VIDRHEILRSGFLWDGeLEEPLQVVYKQARLPFSRLDWRDRADLEQALDalAAADRQQG-FDLLSAPLLRLTlvrTGED- 2769
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 149 vcgEWLLSLSIHHLISDHITQALIIDEIrlLLEDRPEALPKP-LPYRNFIAQILSVPLSEHEQYFRNRLADIDTPTA--- 224
Cdd:PRK12467 2770 ---RHHLIYTNHHILMDGWSGSQLLGEV--LQRYFGQPPPAReGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTRlar 2844
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 225 --PFDLVD-VQGNGEditeARLSLDSSLADALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQGNLGA 301
Cdd:PRK12467 2845 alYPAPAEaVAGHGA----HYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGA 2920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 302 DRVMGMFINTLPLRVSLR-ERSVHDVVQATSHELMMLLAHEQAPLALAQQCSQVPPPlPLFSTLF---NYRHSQ--KDAS 375
Cdd:PRK12467 2921 EQQLGLFINTLPVIASPRaEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGGE-ALFDSILvfeNYPISEalKQGA 2999
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 376 SQfweGMR--QLSGRERTNYPITLSV---DDLGDGFNLTAKTVMGVDPERIVHYMltaiENLVTSLEKTPQQPALSQPIL 450
Cdd:PRK12467 3000 PS---GLRfgAVSSREQTNYPLTLAVglgDTLELEFSYDRQHFDAAAIERLAESF----DRLLQAMLNNPAARLGELPTL 3072
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 451 PKSERQQVLVDFNATDADFPREMLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCV 530
Cdd:PRK12467 3073 AAHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAV 3152
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 531 ERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQSAQVAQLN--STLPTVLLDTPAAAACPDTNPVV 608
Cdd:PRK12467 3153 ERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQLPapAGDTALTLDRLDLNGYSENNPST 3232
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 609 QgLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWI-QLLSGHTLVLVPD 687
Cdd:PRK12467 3233 R-VMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLwTLICGGCLVVRDN 3311
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 688 ALRaDAHQLWRYFARHAVDLFDCTPVQLQWLL-DAGLGSDPAYQpaQVLIGGEAISPAVWSRLQS-LSDTRFINVYGPTE 765
Cdd:PRK12467 3312 DLW-DPEELWQAIHAHRISIACFPPAYLQQFAeDAGGADCASLD--IYVFGGEAVPPAAFEQVKRkLKPRGLTNGYGPTE 3388
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 766 CTVDAT--ACVVDRTQPLPT--IGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSaD 841
Cdd:PRK12467 3389 AVVTVTlwKCGGDAVCEAPYapIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFS-G 3467
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 842 PAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAReDSPGDTRLVAYLCARPDAE 921
Cdd:PRK12467 3468 SGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPADPQG 3546
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 922 LHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAPDqtAFATRDYEAPQGGIETALAALWQELLGLDRVG 1001
Cdd:PRK12467 3547 DWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPD--AKGSREYVAPRSEVEQQLAAIWADVLGVEQVG 3624
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1002 RHDQFFALGGHSLLAVQLLNRMNKA-GMDVALATLFAHPTLCDLAAAVtatahdapftlpvadrtqplplsfsqqrlwfl 1080
Cdd:PRK12467 3625 VTDNFFELGGDSLLALQVLSRIRQSlGLKLSLRDLMSAPTIAELAGYS-------------------------------- 3672
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1081 aqldpaasQAYHLPAALhltgRLDRPALTTALNGLVARHESLRTRFtsiDGQPAQQIdpdtlgfslsshdlrkldeaart 1160
Cdd:PRK12467 3673 --------PLGDVPVNL----LLDLNRLETGFPALFCRHEGLGTVF---DYEPLAVI----------------------- 3714
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1161 trvaelaeqeararfdltqgplirgqllqLDDNTHVLLLTQHHIISDGWsigilarelaalyqaalegSEANLPPLPVQY 1240
Cdd:PRK12467 3715 -----------------------------LEGDRHVLGLTCRHLLDDGW-------------------QDTSLQAMAVQY 3746
|
1290
....*....|..
gi 641744967 1241 ADYAVWQRQWLQ 1252
Cdd:PRK12467 3747 ADYILWQQAKGP 3758
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2124-3203 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 764.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2124 ADSTAITPDLLPLVTLTQPEIDRITDTVSggasNIQDIYPLAPLQEGILFHHLLQEQGDTYLLRSMVAFthrERLDA--F 2201
Cdd:PRK12467 2613 NDQRGVTPSDFPLAGLSQEQLDRLPVAVG----DIEDIYPLSPMQQGMLFHTLYEGGAGDYINQMRVDV---EGLDVerF 2685
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2202 LSALQQVIDRHDILRTAVCWQD-LSQPVQVVWRQAILPINHFEPTSPEDVLAQLQAHTEP-RTRRIDLSQAPLFRADIAH 2279
Cdd:PRK12467 2686 RTAWQAVIDRHEILRSGFLWDGeLEEPLQVVYKQARLPFSRLDWRDRADLEQALDALAAAdRQQGFDLLSAPLLRLTLVR 2765
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2280 DPlQNEWLLALSFHHLISDHMTLALIVGEIrllLQHQA-DALPTP-LPYRNFIAQTLSVPNSAHEAYFRDKLADVDEPT- 2356
Cdd:PRK12467 2766 TG-EDRHHLIYTNHHILMDGWSGSQLLGEV---LQRYFgQPPPAReGRYRDYIAWLQAQDAEASEAFWKEQLAALEEPTr 2841
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2357 --APFGLLNVQGSGGdiHEAR-LVLDATLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRLAGAEG 2433
Cdd:PRK12467 2842 laRALYPAPAEAVAG--HGAHyLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRG 2919
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2434 ADRIMGMFINTLPLRISL-ADRGAAEVVERTSHDLMTLLEHEQAPLALAQRCSGVaPPMPLFSTLL---NYRHTQASStD 2509
Cdd:PRK12467 2920 AEQQLGLFINTLPVIASPrAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQ-GGEALFDSILvfeNYPISEALK-Q 2997
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2510 NTLSDIRV--LTSEERTNYPLTLAV---DDRGEGFSLVAQTLEDIDPHRLLNYLMTAISSLVDAletePQRSILNLPVLP 2584
Cdd:PRK12467 2998 GAPSGLRFgaVSSREQTNYPLTLAVglgDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNN----PAARLGELPTLA 3073
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2585 DSERQQMLVDFNATDADIPRHALIHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVE 2664
Cdd:PRK12467 3074 AHERRQVLHAWNATAAAYPSERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVE 3153
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2665 RGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQSA---HLGIMNGSLpVILLDDGETRPF-DNEPDT 2740
Cdd:PRK12467 3154 RSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHlleQLPAPAGDT-ALTLDRLDLNGYsENNPST 3232
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2741 PLDarkqgltPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGAR 2820
Cdd:PRK12467 3233 RVM-------GENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGC 3305
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2821 LILATQAQAADAQQLAmLIERHAVSFMQATPSTWRMLVELRDFA-LPPGFKALCGGEALPENLATALLQKV--TTLWNLY 2897
Cdd:PRK12467 3306 LVVRDNDLWDPEELWQ-AIHAHRISIACFPPAYLQQFAEDAGGAdCASLDIYVFGGEAVPPAAFEQVKRKLkpRGLTNGY 3384
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2898 GPTETTI----WSTLNGLTTPTPY--IGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDP 2971
Cdd:PRK12467 3385 GPTEAVVtvtlWKCGGDAVCEAPYapIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADP 3464
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2972 FSGAPEaRMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAReDSPGDKRLVAYLLAQ 3051
Cdd:PRK12467 3465 FSGSGG-RLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPA 3542
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3052 pdtvLEPADLRQRLSEGVA----EYMIPSAFVTLDAFPLTPNGKLDRKALPAPDqsAMATRGYEAPQGDLEHALAQIWQT 3127
Cdd:PRK12467 3543 ----DPQGDWRETLRDHLAaslpDYMVPAQLLVLAAMPLGPNGKVDRKALPDPD--AKGSREYVAPRSEVEQQLAAIWAD 3616
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 3128 LLGVERVGRHDHFFELGGHSLLAVQLNARIRAEFLTDIPIVAIFQHPQLSALAEVILAAQIHAAWGNDTDALTHDL 3203
Cdd:PRK12467 3617 VLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSPLGDVPVNLLLDLNRLETGF 3692
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
3-1339 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 758.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3 LVTLSQEEIDTVIATVPDGVAnVQDIYPLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDIL 82
Cdd:PRK12316 25 LATLRGEGVDFSLFPIPAGVS-SAERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 83 RTAICwQGLHQPVQVVWRQAPLTVNTLTTTSSDTVPAQLR---AATDPSNHRLNLSNAPLL-------SATtahdpvcgE 152
Cdd:PRK12316 104 RTVFP-RGADDSLAQVPLDRPLEVEFEDCSGLPEAEQEARlrdEAQRESLQPFDLCEGPLLrvrllrlGEE--------E 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 153 WLLSLSIHHLISDHITQALIIDE-IRL---LLEDR-PEALPKPLPYRNF-IAQILSVPLSEHE---QYFRNRLAD----I 219
Cdd:PRK12316 175 HVLLLTLHHIVSDGWSMNVLIEEfSRFysaYATGAePGLPALPIQYADYaLWQRSWLEAGEQErqlEYWRAQLGEehpvL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 220 DTPT-APFDLV-DVQGngediTEARLSLDSSLADALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQG 297
Cdd:PRK12316 255 ELPTdHPRPAVpSYRG-----SRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 298 NLgaDRVMGMFINTLPLRVSLRER-SVHDVVQATSHELMMLLAHEQAPLALAQQCSQVPPPL---PLFSTLFNYRHSQKD 373
Cdd:PRK12316 330 EV--EGLIGFFVNTQVLRSVFDGRtRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLshsPLFQVMYNHQPLVAD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 374 AssqfwEGMRQLSGRE---------RTNYPITLSVDDLGDGFNLTAKTVMGVDPERIVHYMLTAIENLVTSLEKTPQQPA 444
Cdd:PRK12316 408 I-----EALDTVAGLEfgqlewksrTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 445 LSQPILPKSERQQVLVDFNATDADFPREMLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDD 524
Cdd:PRK12316 483 DELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDV 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 525 RVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQSAQVAQL--NSTLPTVLLDTPAA--AA 600
Cdd:PRK12316 563 LVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLplAAGVQVLDLDRPAAwlEG 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 601 CPDTNPVVQgLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASV-KNWIQLLSG 679
Cdd:PRK12316 643 YSEENPGTE-LNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVwEFFWPLMSG 721
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 680 HTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAglGSDPAYQPAQVLI-GGEAISPAVWSRL-QSLSDTRF 757
Cdd:PRK12316 722 ARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQD--EDVASCTSLRRIVcSGEALPADAQEQVfAKLPQAGL 799
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 758 INVYGPTECTVDAT--ACVVDRTQPLPtIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIP 835
Cdd:PRK12316 800 YNLYGPTEAAIDVThwTCVEEGGDSVP-IGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVP 878
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 836 DPFSAdpAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSpgdtRLVAYLC 915
Cdd:PRK12316 879 SPFVA--GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGK----QLVGYVV 952
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 916 ARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAPDQTAfATRDYEAPQGGIETALAALWQELL 995
Cdd:PRK12316 953 LESEGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASV-AQQGYVAPRNALERTLAAIWQDVL 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 996 GLDRVGRHDQFFALGGHSLLAVQLLNRMNKAGMDVALATLFAHPTLCDLAAAVTATAHDAPFTLPVADRTQPLPLsfsqQ 1075
Cdd:PRK12316 1032 GVERVGLDDNFFELGGDSIVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAKAGQATAADQGPASGEVALAPV----Q 1107
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1076 RlWFLAQLDPaasQAYHLPAALHLTGR--LDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDTLGFSLSSHDLrk 1153
Cdd:PRK12316 1108 R-WFFEQAIP---QRQHWNQSLLLQARqpLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGEVLWQRQA-- 1181
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1154 LDEAArttrVAELAEqEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALegseANL 1233
Cdd:PRK12316 1182 ASEEE----LLALCE-EAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLD----ADL 1252
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1234 PPLPVQYADYAvwQRQWLQGETLNDLRDYWRDQLQGAPAllEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRL----HALN 1309
Cdd:PRK12316 1253 PARTSSYQAWA--RRLHEHAGARAEELDYWQAQLEDAPH--ELPCENPDGALENRHERKLELRLDAERTRQLlqeaPAAY 1328
|
1370 1380 1390
....*....|....*....|....*....|
gi 641744967 1310 RQQGTTLFMTLLAAwsvVLSRLSGQDDIVI 1339
Cdd:PRK12316 1329 RTQVNDLLLTALAR---VTCRWSGQASVLV 1355
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1531-2021 |
0e+00 |
|
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: 745.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1531 HQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDP 1610
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1611 GYPAERLAYMLDDASPVALLTQANQRALLTGDVPRILLDTADFSHLSEDNPHVPgLDAHHLAYVIYTSGSTGKPKGVMNS 1690
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLVP-PRPDNLAYVIYTSGSTGRPKGVMVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1691 HRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSM 1770
Cdd:cd17646 160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSM 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1771 LQQFVQWADADcACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTFWACQPDDHRSFVPIGRPIANTQ 1850
Cdd:cd17646 240 LRVFLAEPAAG-SCASLRRVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSVPIGRPVPNTR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1851 LYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinQPGARLYKTGDLARWLPDGSLEYLGRNDFQVK 1930
Cdd:cd17646 319 LYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF--GPGSRMYRTGDLARWRPDGALEFLGRSDDQVK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1931 LRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVT-PDPADLRQQLGQHLAEYMVPGAFVTLDAFP 2009
Cdd:cd17646 397 IRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALP 476
|
490
....*....|..
gi 641744967 2010 LTPNGKLDRKAL 2021
Cdd:cd17646 477 LTANGKLDRAAL 488
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
30-1396 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 740.05 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 30 PLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICWQGlHQPVQVVWRQAPLTVNTL 109
Cdd:PRK12467 1118 PLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQED-GRTRQVIHPVGSLTLEEP 1196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 110 TTTSSDTVPAQLRAATDPSNHRL-NLSNAPLL------SATTAHdpvcgewLLSLSIHHLISDHITQALIIDEI----RL 178
Cdd:PRK12467 1197 LLLAADKDEAQLKVYVEAEARQPfDLEQGPLLrvgllrLAADEH-------VLVLTLHHIVSDGWSMQVLVDELvalyAA 1269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 179 LLEDRPEALPK-PLPYRNF-IAQILSVPLSEHEQ---YFRNRLADiDTPT--APFDLVDVQGNGEDITEARLSLDSSLAD 251
Cdd:PRK12467 1270 YSQGQSLQLPAlPIQYADYaVWQRQWMDAGERARqlaYWKAQLGG-EQPVleLPTDRPRPAVQSHRGARLAFELPPALAE 1348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 252 ALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQgnLGADRVMGMFINTLPLRVSLR-ERSVHDVVQAT 330
Cdd:PRK12467 1349 GLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNR--AETEGLIGFFVNTQVLRAEVDgQASFQQLLQQV 1426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 331 SHELMMLLAHEQAP---LALAQQCSQVPPPLPLFSTLFNYRHSQKDASSQFWE-GMRQLSGRERT-NYPITLSVDDLGDG 405
Cdd:PRK12467 1427 KQAALEAQAHQDLPfeqLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAQLPGlSVESLSWESQTaQFDLTLDTYESSEG 1506
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 406 fnLTAKTVMGVD------PERIV-HYMltaieNLVTSLEKTPQQPALSQPILPKSERQQVLVDFNATDADFPREMLIQQR 478
Cdd:PRK12467 1507 --LQASLTYATDlfeastIERLAgHWL-----NLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQL 1579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 479 FEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYP 558
Cdd:PRK12467 1580 IEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYP 1659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 559 AERLAYILDDAAPVALLTQSAQVAQLNST--LPTVLLDTPAA--AACPDTNPVVQgLHAAHLAYVIYTSGSTGRPKGVMV 634
Cdd:PRK12467 1660 RERLAYMIEDSGIELLLTQSHLQARLPLPdgLRSLVLDQEDDwlEGYSDSNPAVN-LAPQNLAYVIYTSGSTGRPKGAGN 1738
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 635 AHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWI-QLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPV 713
Cdd:PRK12467 1739 RHGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFwPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPS 1818
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 714 QLQWLLDAglgsDPAYQPA----QVLIGGEAISPAVWSR-LQSLSDTRFINVYGPTECTVDATACVVDRTQP-----LPt 783
Cdd:PRK12467 1819 MLQQLLQM----DEQVEHPlslrRVVCGGEALEVEALRPwLERLPDTGLFNLYGPTETAVDVTHWTCRRKDLegrdsVP- 1893
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 784 IGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsADPAARIYKTGDLARWLPDGNIDY 863
Cdd:PRK12467 1894 IGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPF-GTVGSRLYRTGDLARYRADGVIEY 1972
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 864 LGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIArEDSPGDTRLVAYLC----ARPDAELHPAA----LRQQLAASL 935
Cdd:PRK12467 1973 LGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIA-QDGANGKQLVAYVVptdpGLVDDDEAQVAlraiLKNHLKASL 2051
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 936 ADYMIPSAFVTLDALPLTPNGKLDRKALPAPDQTAFaTRDYEAPQGGIETALAALWQELLGLDRVGRHDQFFALGGHSLL 1015
Cdd:PRK12467 2052 PEYMVPAHLVFLARMPLTPNGKLDRKALPAPDASEL-QQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSII 2130
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1016 AVQLLNRMNKAGMDVALATLFAHPTLCDLAAavTATAHDAPFTLPVADRTQPLPLSfSQQRLWFlaQLDPAASQAYHLPA 1095
Cdd:PRK12467 2131 SIQVVSRARQAGIRFTPKDLFQHQTVQSLAA--VAQEGDGTVSIDQGPVTGDLPLL-PIQQMFF--ADDIPERHHWNQSV 2205
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1096 ALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQ-PAQQIDPDTLGFS-LSSHDLRKLDEaarttrVAELAEQeARA 1173
Cdd:PRK12467 2206 LLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGwSAMHRAPEQERRPlLWQVVVADKEE------LEALCEQ-AQR 2278
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1174 RFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALEGSEANLPPLPVQYADYAVWQRQWLQG 1253
Cdd:PRK12467 2279 SLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAAS 2358
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1254 ETLNDLRDYWRDQLQGAPAllEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRLhalnRQQGTTLFMT-----LLAAWSVVL 1328
Cdd:PRK12467 2359 AALADELGYWQAQLQGAST--ELPCDHPQGGLQRRHAASVTTHLDSEWTRRL----LQEAPAAYRTqvndlLLTALARVI 2432
|
1370 1380 1390 1400 1410 1420 1430
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641744967 1329 SRLSGQDDIVIGTPVANR----PRQELEGMVGFFVNTLALRTEPGRchAVADLLDQVRERaLDAYAHQALPF 1396
Cdd:PRK12467 2433 ARWTGQASTLIQLEGHGRedlfDEIDLTRTVGWFTSLYPVKLSPTA--SLATSIKTIKEQ-LRAVPNKGLGF 2501
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2-1050 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 736.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2 PLVTLSQEEIDTViatvPDGVANVQDIYPLAPLQEGILFHYQLQEKGDTYLlNSLLAFDSQTRLDAFLDVLQQVIARHDI 81
Cdd:PRK12316 4080 PLAGLDQARLDAL----PLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYI-NQMRVDVQGLDVERFRAAWQAALDRHDV 4154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 82 LRTAICWQG-LHQPVQVVWRQAPLTVNTLTTTSSDTVPAQLRAATDPSNHR-LNLSNAPLLSATTAHDPVcGEWLLSLSI 159
Cdd:PRK12316 4155 LRSGFVWQGeLGRPLQVVHKQVSLPFAELDWRGRADLQAALDALAAAERERgFDLQRAPLLRLVLVRTAE-GRHHLIYTN 4233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 160 HHLISDHITQALIIDEIRLLLEDRPEALPKpLPYRNFIAQILSVPLSEHEQYFRNRLADIDTPT------APFDLVDVQG 233
Cdd:PRK12316 4234 HHILMDGWSNSQLLGEVLERYSGRPPAQPG-GRYRDYIAWLQRQDAAASEAFWREQLAALDEPTrlaqaiARADLRSANG 4312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 234 NGEDITEarlsLDSSLADALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQGNLGADRVMGMFINTLP 313
Cdd:PRK12316 4313 YGEHVRE----LDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLP 4388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 314 LRVSLR-ERSVHDVVQATSHELMMLLAHEQAPLALAQQCSQVPPPlPLFSTLFNYR------HSQKDASsqfwEGMR--Q 384
Cdd:PRK12316 4389 VIATPRaQQSVVEWLQQVQRQNLALREHEHTPLYEIQRWAGQGGE-ALFDSLLVFEnypvseALQQGAP----GGLRfgE 4463
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 385 LSGRERTNYPITLSVDdLGDGFNLTAKTVMGVDPERIVHYMLTAIENLVTSLEKTPQQPALSQPILPKSERQQVLVDFNA 464
Cdd:PRK12316 4464 VTNHEQTNYPLTLAVG-LGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNR 4542
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 465 TDADFPREMLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGIL 544
Cdd:PRK12316 4543 TDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVL 4622
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 545 KAGAAYVPMDPAYPAERLAYILDDAAPVALLTQSAQVAQLNST--LPTVLLD-TPAAAACPDTNPVVQgLHAAHLAYVIY 621
Cdd:PRK12316 4623 KAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQSHLLQRLPIPdgLASLALDrDEDWEGFPAHDPAVR-LHPDNLAYVIY 4701
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 622 TSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWIQLLSGHTLVLVPDALRADAHQLWRYFA 701
Cdd:PRK12316 4702 TSGSTGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIH 4781
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 702 RHAVDLFDCTPVQLQWLL-DAGLGSDPAyQPAQVLIGGEAISPAVWSR-LQSLSDTRFINVYGPTECTVDATA-CVVDRT 778
Cdd:PRK12316 4782 EHRVTVLVFPPVYLQQLAeHAERDGEPP-SLRVYCFGGEAVAQASYDLaWRALKPVYLFNGYGPTETTVTVLLwKARDGD 4860
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 779 QPLPT---IGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSAdPAARIYKTGDLARW 855
Cdd:PRK12316 4861 ACGAAympIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGA-PGGRLYRTGDLARY 4939
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 856 LPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGdTRLVAYLC----ARPDAELHPAALRQQ- 930
Cdd:PRK12316 4940 RADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG-KQLVGYVVpqdpALADADEAQAELRDEl 5018
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 931 ---LAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAPDQTAfATRDYEAPQGGIETALAALWQELLGLDRVGRHDQFF 1007
Cdd:PRK12316 5019 kaaLRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASL-LQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFF 5097
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....
gi 641744967 1008 ALGGHSLLAVQLLNRMNKA-GMDVALATLFAHPTLCDLAAAVTA 1050
Cdd:PRK12316 5098 ELGGHSLLAIQVTSRIQLElGLELPLRELFQTPTLAAFVELAAA 5141
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
30-1369 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 734.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 30 PLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICWQGLHqpvqvvWRQAPLTVNTL 109
Cdd:PRK12316 2604 PLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQ------TRQVILPNMSL 2677
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 110 TTTSSDTV---PAQLRAATDPSNHR-LNLSNAPLLSATTAhDPVCGEWLLSLSIHHLISDHITQALIIDEIRLLLE---- 181
Cdd:PRK12316 2678 RIVLEDCAgvaDAAIRQRVAEEIQRpFDLARGPLLRVRLL-ALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAgarr 2756
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 182 -DRPEALPKPLPYRNFIAQ----ILSVPLSEHEQYFRNRLADIDTPTA-PFDLVDVQGNGEDITEARLSLDSSLADALRR 255
Cdd:PRK12316 2757 gEQPTLPPLPLQYADYAAWqrawMDSGEGARQLDYWRERLGGEQPVLElPLDRPRPALQSHRGARLDVALDVALSRELLA 2836
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 256 QARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRlqGNLGADRVMGMFINTLPLRVSLR-ERSVHDVVQATSHEL 334
Cdd:PRK12316 2837 LARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANR--NRAETERLIGFFVNTQVLRAQVDaQLAFRDLLGQVKEQA 2914
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 335 MMLLAHEQAP---LALAQQCSQVPPPLPLFSTLFNYRHSQKDASSQ---FWEGMRQLSGRERTNYPITLSVDDLGDGFNL 408
Cdd:PRK12316 2915 LGAQAHQDLPfeqLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLpglHIESFAWDGAATQFDLALDTWESAEGLGASL 2994
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 409 TAKTVMGvdPERIVHYMLTAIENLVTSLEKTPQQPALSQPILPKSERQQVLVDFNATDADFPREMLIQQRFEAQAEQTPE 488
Cdd:PRK12316 2995 TYATDLF--DARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPD 3072
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 489 AIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDD 568
Cdd:PRK12316 3073 AVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLED 3152
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 569 AAPVALLTQSAQVAQLNSTLPTVLLDtPAAAACPDTNPVVQGLhAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHT 648
Cdd:PRK12316 3153 SGAQLLLSQSHLRLPLAQGVQVLDLD-RGDENYAEANPAIRTM-PENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQ 3230
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 649 LLALDHPSRIALNASIVFDASVKN-WIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQWLLdAGLGSDP 727
Cdd:PRK12316 3231 AYGLGVGDRVLQFTTFSFDVFVEElFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLQAFL-EEEDAHR 3309
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 728 AYQPAQVLIGGEAISPAVWSRLqsLSDTRFINVYGPTECTVDATAC-VVDRTQPLPTIGKPLANTRLYILDAQDQPVPIG 806
Cdd:PRK12316 3310 CTSLKRIVCGGEALPADLQQQV--FAGLPLYNLYGPTEATITVTHWqCVEEGKDAVPIGRPIANRACYILDGSLEPVPVG 3387
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 807 VTGELHIGGAGVARGYLHRPDLTAERFIPDPFSadPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESR 886
Cdd:PRK12316 3388 ALGELYLGGEGLARGYHNRPGLTAERFVPDPFV--PGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEAR 3465
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 887 LLRCPGVQDAVVIAREDSpgdtRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAP 966
Cdd:PRK12316 3466 LLEHPWVREAVVLAVDGR----QLVAYVVPEDEAGDLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRP 3541
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 967 DqTAFATRDYEAPQGGIETALAALWQELLGLDRVGRHDQFFALGGHSLLAVQLLNRMNKAGMDVALATLFAHPTLCDLAA 1046
Cdd:PRK12316 3542 D-AALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLAR 3620
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1047 AVTATAHDAPFTLPV-------ADRTQPLPLSFSQQRLWFLAQLdpaasqayhlpaaLHLTGRLDRPALTTALNGLVARH 1119
Cdd:PRK12316 3621 VARVGGGVAVDQGPVsgetlllPIQQQFFEEPVPERHHWNQSLL-------------LKPREALDAAALEAALQALVEHH 3687
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1120 ESLRTRFTSIDGQPAQQIDPDTLGFSLSSHdlRKLDEAARTTRVAElaeqEARARFDLTQGPLIRGQLLQLDDNTHVLLL 1199
Cdd:PRK12316 3688 DALRLRFVEDAGGWTAEHLPVELGGALLWR--AELDDAEELERLGE----EAQRSLDLADGPLLRALLATLADGSQRLLL 3761
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1200 TQHHIISDGWSIGILARELAALYQAALEGSEANLPPLPVQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAPAllEIPTD 1279
Cdd:PRK12316 3762 VIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSS--ELPCD 3839
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1280 RPRPSVQRYAGDQVPFHLDAGQLRRL----HALNRQQGTTLFMTLLAAwsvVLSRLSGQDDIVIGTPVANRPRQ----EL 1351
Cdd:PRK12316 3840 HPQGALQNRHAASVQTRLDRELTRRLlqqaPAAYRTQVNDLLLTALAR---VVCRWTGEASALVQLEGHGREDLfadiDL 3916
|
1370
....*....|....*...
gi 641744967 1352 EGMVGFFVNTLALRTEPG 1369
Cdd:PRK12316 3917 SRTVGWFTSLFPVRLSPV 3934
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2129-3191 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 727.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2129 ITPDLLPLVTLTQPEIDRITdtVSGGAsnIQDIYPLAPLQEGILFHHLLQEQGDTYL--LRSMVafthrERLD--AFLSA 2204
Cdd:PRK12316 1528 VTPSDFPLAGLSQAQLDALP--LPAGE--IADIYPLSPMQQGMLFHSLYEQEAGDYInqLRVDV-----QGLDpdRFRAA 1598
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2205 LQQVIDRHDILRTAVCWQD-LSQPVQVVWRQAILPINHFEPTSPEDVLAQLQAHTEP-RTRRIDLSQAPLFRADIAHDPl 2282
Cdd:PRK12316 1599 WQATVDRHEILRSGFLWQDgLEQPLQVIHKQVELPFAELDWRGREDLGQALDALAQAeRQKGFDLTRAPLLRLVLVRTG- 1677
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2283 QNEWLLALSFHHLISDHMTLALIVGEIrllLQHQADALP--TPLPYRNFIAQTLSVPNSAHEAYFRDKLADVDEPTAPFG 2360
Cdd:PRK12316 1678 EGRHHLIYTNHHILMDGWSNAQLLGEV---LQRYAGQPVaaPGGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLAQ 1754
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2361 LLNVQGSGGDIHEARLVLDATLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRLAGAEGADRIMGM 2440
Cdd:PRK12316 1755 AARTEDGQVGYGDHQQLLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGL 1834
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2441 FINTLPLRIS-LADRGAAEVVERTSHDLMTLLEHEQAPLALAQRCSGVAPPmPLFSTLL---NYRHTQA--SSTDNTLSD 2514
Cdd:PRK12316 1835 FINTLPVIAApRPDQSVADWLQEVQALNLALREHEHTPLYDIQRWAGQGGE-ALFDSLLvfeNYPVAEAlkQGAPAGLVF 1913
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2515 IRVlTSEERTNYPLTLAVDdRGEGFSL---------VAQTLEDIDPHrLLNylmtaissLVDALETEPQRSILNLPVLPD 2585
Cdd:PRK12316 1914 GRV-SNHEQTNYPLTLAVT-LGETLSLqysydrghfDAAAIERLDRH-LLH--------LLEQMAEDAQAALGELALLDA 1982
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2586 SERQQMLVDFNATDADIPRHALIHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVER 2665
Cdd:PRK12316 1983 GERQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAER 2062
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2666 GLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQSAHLG--IMNGSLPVILLDdgetrPFDNEPDTPLD 2743
Cdd:PRK12316 2063 SFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQRHLLErlPLPAGVARLPLD-----RDAEWADYPDT 2137
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2744 ARKQGLTPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLIL 2823
Cdd:PRK12316 2138 APAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLI 2217
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2824 ATQAQAADAQQLAMlIERHAVSFMQATPSTWRMLVEL--RDFALPPGFKALCGGEALPENLATALLQKVTT--LWNLYGP 2899
Cdd:PRK12316 2218 RDDELWDPEQLYDE-MERHGVTILDFPPVYLQQLAEHaeRDGRPPAVRVYCFGGEAVPAASLRLAWEALRPvyLFNGYGP 2296
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2900 TETTIWSTL------NGLTTPTPYIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFS 2973
Cdd:PRK12316 2297 TEAVVTPLLwkcrpqDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFS 2376
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2974 gAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAReDSPGDKRLVAYLLAQPD 3053
Cdd:PRK12316 2377 -ASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDDA 2454
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3054 TVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAPDQSAmATRGYEAPQGDLEHALAQIWQTLLGVER 3133
Cdd:PRK12316 2455 AEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDVSQ-LRQAYVAPQEGLEQRLAAIWQAVLKVEQ 2533
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 3134 VGRHDHFFELGGHSLLAVQLNARIRAEFLTDIPIVAIFQHPQLSALAEVILAAQIHAA 3191
Cdd:PRK12316 2534 VGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRA 2591
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1542-2021 |
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: 703.90 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1542 PDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYML 1621
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1622 DDASPVALLTQANqralltgdvprilldtadfshlsednphvpgldahHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWM 1701
Cdd:cd05930 81 EDSGAKLVLTDPD-----------------------------------DLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADaD 1781
Cdd:cd05930 126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE-L 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1782 CACDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWACQPDD-HRSFVPIGRPIANTQLYILDTLGQ 1859
Cdd:cd05930 205 AALPSLRLVLVGGEALPPDLVRRWRELLpGARLVNLYGPTEATVDATYYRVPPDDeEDGRVPIGRPIPNTRVYVLDENLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1860 PVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFInqPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELG 1939
Cdd:cd05930 285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG--PGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1940 EIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRK 2019
Cdd:cd05930 363 EIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
..
gi 641744967 2020 AL 2021
Cdd:cd05930 443 AL 444
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
2161-2569 |
0e+00 |
|
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: 701.50 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2161 IYPLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCWQDLSQPVQVVWRQAILPIN 2240
Cdd:cd19544 1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGLSEPVQVVWRQAELPVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2241 HFEPTSPEDVLAQLQAHTEPRTRRIDLSQAPLFRADIAHDPLQNEWLLALSFHHLISDHMTLALIVGEIRLLLQHQADAL 2320
Cdd:cd19544 81 ELTLDPGDDALAQLRARFDPRRYRLDLRQAPLLRAHVAEDPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRAAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2321 PTPLPYRNFIAQTLSVPNSA-HEAYFRDKLADVDEPTAPFGLLNVQGSGGDIHEARLVLDATLASAIRQQARHLGVSPGV 2399
Cdd:cd19544 161 PPPVPYRNFVAQARLGASQAeHEAFFREMLGDVDEPTAPFGLLDVQGDGSDITEARLALDAELAQRLRAQARRLGVSPAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2400 LFHVAWAQVLAQTSGRDDVVFGSVLLGRLAGAEGADRIMGMFINTLPLRISLADRGAAEVVERTSHDLMTLLEHEQAPLA 2479
Cdd:cd19544 241 LFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLGGRSVREAVRQTHARLAELLRHEHASLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2480 LAQRCSGVAPPMPLFSTLLNYRHTQASSTDN---TLSDIRVLTSEERTNYPLTLAVDDRGEGFSLVAQTLEDIDPHRLLN 2556
Cdd:cd19544 321 LAQRCSGVPAPTPLFSALLNYRHSAAAAAAAalaAWEGIELLGGEERTNYPLTLSVDDLGDGFSLTAQVVAPIDAERVCA 400
|
410
....*....|...
gi 641744967 2557 YLMTAISSLVDAL 2569
Cdd:cd19544 401 YMETALEQLVDAL 413
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1067-1494 |
0e+00 |
|
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: 678.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1067 PLPLSFSQQRLWFLAQLDPAaSQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDtLGFSL 1146
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPG-SAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPP-LPLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1147 SSHDLRKLDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAAL 1226
Cdd:cd19531 79 PVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1227 EGSEANLPPLPVQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRLH 1306
Cdd:cd19531 159 AGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1307 ALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQVRERAL 1386
Cdd:cd19531 239 ALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1387 DAYAHQALPFEQVVEILQPARSLSYSPIFQVMLSLNNTPAQALTLPDLTLSAVERPQHSTHFDLSLSLIETENGLNGGLV 1466
Cdd:cd19531 319 EAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSLE 398
|
410 420
....*....|....*....|....*...
gi 641744967 1467 YATDLFDRETILRVVGYVENILMAMADD 1494
Cdd:cd19531 399 YNTDLFDAATIERMAGHFQTLLEAIVAD 426
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
28-436 |
0e+00 |
|
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: 674.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 28 IYPLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICWQGLHQPVQVVWRQAPLTVN 107
Cdd:cd19544 1 IYPLAPLQEGILFHHLLAEEGDPYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAILWEGLSEPVQVVWRQAELPVE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 108 TLTTTSSDTVPAQLRAATDPSNHRLNLSNAPLLSATTAHDPVCGEWLLSLSIHHLISDHITQALIIDEIRLLLEDRPEAL 187
Cdd:cd19544 81 ELTLDPGDDALAQLRARFDPRRYRLDLRQAPLLRAHVAEDPANGRWLLLLLFHHLISDHTSLELLLEEIQAILAGRAAAL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 188 PKPLPYRNFIAQILSVPLS-EHEQYFRNRLADIDTPTAPFDLVDVQGNGEDITEARLSLDSSLADALRRQARHLGISSSV 266
Cdd:cd19544 161 PPPVPYRNFVAQARLGASQaEHEAFFREMLGDVDEPTAPFGLLDVQGDGSDITEARLALDAELAQRLRAQARRLGVSPAS 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 267 LFHVAWAQVLALTSGRDDVVFGSVLSGRLQGNLGADRVMGMFINTLPLRVSLRERSVHDVVQATSHELMMLLAHEQAPLA 346
Cdd:cd19544 241 LFHLAWALVLARCSGRDDVVFGTVLSGRMQGGAGADRALGMFINTLPLRVRLGGRSVREAVRQTHARLAELLRHEHASLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 347 LAQQCSQVPPPLPLFSTLFNYRHSQK---DASSQFWEGMRQLSGRERTNYPITLSVDDLGDGFNLTAKTVMGVDPERIVH 423
Cdd:cd19544 321 LAQRCSGVPAPTPLFSALLNYRHSAAaaaAAALAAWEGIELLGGEERTNYPLTLSVDDLGDGFSLTAQVVAPIDAERVCA 400
|
410
....*....|...
gi 641744967 424 YMLTAIENLVTSL 436
Cdd:cd19544 401 YMETALEQLVDAL 413
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2163-3187 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 673.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2163 PLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCwQDLSQPVQVVWRQAILPInHF 2242
Cdd:PRK12467 51 PLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFV-QDEEGFRQVIDASLSLTI-PL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2243 E---PTSPEDVLAQLQAHTEPRTRR-IDLSQAPLFRADI---AHDplqnEWLLALSFHHLISDHMTLALIVGEIRLLL-- 2313
Cdd:PRK12467 129 DdlaNEQGRARESQIEAYINEEVARpFDLANGPLLRVRLlrlADD----EHVLVVTLHHIISDGWSMRVLVEELVQLYsa 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2314 --QHQADALPT-PLPYRNF-IAQTLSVPNSAHE---AYFRDKLAD---VDEPTAPFGLLNVQGSGGDIHEARLvlDATLA 2383
Cdd:PRK12467 205 ysQGREPSLPAlPIQYADYaIWQRSWLEAGERErqlAYWQEQLGGehtVLELPTDRPRPAVPSYRGARLRVDL--PQALS 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2384 SAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRlaGAEGADRIMGMFINTLPLRISLADRGA-AEVVER 2462
Cdd:PRK12467 283 AGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANR--NRVETERLIGFFVNTQVLKAEVDPQASfLELLQQ 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2463 TSHDLMTLLEHEQAPL-----ALA-QRCSGVAPpmpLFSTLLNYRHTQASSTDNTLSDIRVLTSEE------RTNYPLTL 2530
Cdd:PRK12467 361 VKRTALGAQAHQDLPFeqlveALQpERSLSHSP---LFQVMFNHQNTATGGRDREGAQLPGLTVEElswarhTAQFDLAL 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2531 AVDDRGEG----FSLVAQTLEDIDPHRLLNYLMtaisSLVDALETEPQRSILNLPVLPDSERQQMLVDFNATDADIPRHA 2606
Cdd:PRK12467 438 DTYESAQGlwaaFTYATDLFEATTIERLATHWR----NLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEYAPDC 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2607 lIHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPL 2686
Cdd:PRK12467 514 -VHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2687 DPTYPVERLRYMLDDAKPVALISQSAHLGIMN--GSLPVILLDDG----ETRPFDNePDTPLDarkqgltPRHLAYVIYT 2760
Cdd:PRK12467 593 DPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPvpAGLRSLCLDEPadllCGYSGHN-PEVALD-------PDNLAYVIYT 664
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2761 SGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIE 2840
Cdd:PRK12467 665 SGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMA 744
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2841 RHAVSFMQATPSTWRMLVELRDFALPPGFKAL-CGGEALPENLATALLQKV--TTLWNLYGPTETTIWST-----LNGLT 2912
Cdd:PRK12467 745 DQGVTVLKIVPSHLQALLQASRVALPRPQRALvCGGEALQVDLLARVRALGpgARLINHYGPTETTVGVStyelsDEERD 824
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2913 TPTPYIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsGAPEARMYKTGDLGRWLPD 2992
Cdd:PRK12467 825 FGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPF-GADGGRLYRTGDLARYRAD 903
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2993 GTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIArEDSPGDKRLVAYLLaqPDTVLEPA-------DLRQRL 3065
Cdd:PRK12467 904 GVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLA-QPGDAGLQLVAYLV--PAAVADGAehqatrdELKAQL 980
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3066 SEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAPDQSAMaTRGYEAPQGDLEHALAQIWQTLLGVERVGRHDHFFELGG 3145
Cdd:PRK12467 981 RQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAV-QATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGG 1059
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|..
gi 641744967 3146 HSLLAVQLNARIRAEFLTDIPIVAIFQHPQLSALAEVILAAQ 3187
Cdd:PRK12467 1060 HSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQ 1101
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2163-3191 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 631.61 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2163 PLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCWQDlSQPVQVVWRQAILPINHf 2242
Cdd:PRK12316 51 RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGA-DDSLAQVPLDRPLEVEF- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2243 eptspEDVLAQLQAHTEPRTRR---------IDLSQAPLFRADIAHDPLQnEWLLALSFHHLISDHMTLALIVGE-IRLL 2312
Cdd:PRK12316 129 -----EDCSGLPEAEQEARLRDeaqreslqpFDLCEGPLLRVRLLRLGEE-EHVLLLTLHHIVSDGWSMNVLIEEfSRFY 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2313 LQHQADALP--TPLP-----YRNFIAQTLSVPNSAHE-AYFRDKLAD--------VDEPTAPfgllnVQGSGGDIHEarL 2376
Cdd:PRK12316 203 SAYATGAEPglPALPiqyadYALWQRSWLEAGEQERQlEYWRAQLGEehpvlelpTDHPRPA-----VPSYRGSRYE--F 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2377 VLDATLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRLAGAegADRIMGMFINTLPLRISLADRGA 2456
Cdd:PRK12316 276 SIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAE--VEGLIGFFVNTQVLRSVFDGRTR 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2457 -AEVVERTSHDLMTLLEHEQAP---LALAQRCSGVAPPMPLFSTLLNYRHTQAS-STDNTLSDIRVLTSEER---TNYPL 2528
Cdd:PRK12316 354 vATLLAGVKDTVLGAQAHQDLPferLVEALKVERSLSHSPLFQVMYNHQPLVADiEALDTVAGLEFGQLEWKsrtTQFDL 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2529 TLAVDDRGEGFSLVAQTLEDIDPHRLLNYLMTAISSLVDALETEPQRSILNLPVLPDSERQQMLVDFNATDADIPRHALI 2608
Cdd:PRK12316 434 TLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGV 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2609 HELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDP 2688
Cdd:PRK12316 514 HRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDP 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2689 TYPVERLRYMLDDAKPVALISQSaHLGI---MNGSLPVILLDDGeTRPFDNEPDTPLDARkqgLTPRHLAYVIYTSGSTG 2765
Cdd:PRK12316 594 EYPAERLAYMLEDSGVQLLLSQS-HLGRklpLAAGVQVLDLDRP-AAWLEGYSEENPGTE---LNPENLAYVIYTSGSTG 668
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2766 KPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVS 2845
Cdd:PRK12316 669 KPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVD 748
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2846 FMQATPSTWRMLVELRDFALPPGFKAL-CGGEALPENLATALLQK--VTTLWNLYGPTETTI----WSTLNGLTTPTPyI 2918
Cdd:PRK12316 749 TLHFVPSMLQAFLQDEDVASCTSLRRIvCSGEALPADAQEQVFAKlpQAGLYNLYGPTEAAIdvthWTCVEEGGDSVP-I 827
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2919 GHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSGApeARMYKTGDLGRWLPDGTLEYL 2998
Cdd:PRK12316 828 GRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAG--ERMYRTGDLARYRADGVIEYA 905
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2999 GRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREdspgDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAF 3078
Cdd:PRK12316 906 GRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GKQLVGYVVLESEGGDWREALKAHLAASLPEYMVPAQW 981
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3079 VTLDAFPLTPNGKLDRKALPAPDQSaMATRGYEAPQGDLEHALAQIWQTLLGVERVGRHDHFFELGGHSLLAVQLNARIR 3158
Cdd:PRK12316 982 LALERLPLTPNGKLDRKALPAPEAS-VAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRAR 1060
|
1050 1060 1070
....*....|....*....|....*....|...
gi 641744967 3159 AEFLTDIPiVAIFQHPQLSALAEVILAAQIHAA 3191
Cdd:PRK12316 1061 QAGIQLSP-RDLFQHQTIRSLALVAKAGQATAA 1092
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
487-963 |
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: 622.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYIL 566
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 567 DDAAPVALLTQsaqvaqlnstlptvlldtpaaaacpdtnpvvqglhAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGL 646
Cdd:cd05930 81 EDSGAKLVLTD-----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 647 HTLLALDHPSRIALNASIVFDASVKN-WIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGS 725
Cdd:cd05930 126 QEAYPLTPGDRVLQFTSFSFDVSVWEiFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELELA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 726 DPAyQPAQVLIGGEAISPAVWSRLQSL-SDTRFINVYGPTECTVDATACVVDRTQPL---PTIGKPLANTRLYILDAQDQ 801
Cdd:cd05930 206 ALP-SLRLVLVGGEALPPDLVRRWRELlPGARLVNLYGPTEATVDATYYRVPPDDEEdgrVPIGRPIPNTRVYVLDENLR 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 802 PVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsaDPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAG 881
Cdd:cd05930 285 PVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPF--GPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 882 EIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRK 961
Cdd:cd05930 363 EIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRK 442
|
..
gi 641744967 962 AL 963
Cdd:cd05930 443 AL 444
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
2620-3097 |
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: 613.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALISQsahlgimngslpvillddgetrpfdnepdtpldarkqgltPRHLAYVIYTSGSTGKPKGVMVEHANMVN 2779
Cdd:cd05930 81 EDSGAKLVLTD----------------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2780 FLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVE 2859
Cdd:cd05930 121 LLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQ 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2860 LRDFALPPGFK-ALCGGEALPENLATALLQKV--TTLWNLYGPTETTIWSTLNGLTTPTPY-----IGHPIANTQIYILD 2931
Cdd:cd05930 201 ELELAALPSLRlVLVGGEALPPDLVRRWRELLpgARLVNLYGPTEATVDATYYRVPPDDEEdgrvpIGRPIPNTRVYVLD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2932 AQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFR 3011
Cdd:cd05930 281 ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPF--GPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYR 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3012 IELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGK 3091
Cdd:cd05930 359 IELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGK 438
|
....*.
gi 641744967 3092 LDRKAL 3097
Cdd:cd05930 439 VDRKAL 444
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
477-967 |
0e+00 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 605.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 477 QRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPA 556
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 557 YPAERLAYILDDAAPVALLTQSAQVAQLNSTLPTVLLDTPAAAACPDTN--PVVQglhAAHLAYVIYTSGSTGRPKGVMV 634
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENlePVSK---SDDLAYVIYTSGSTGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 635 AHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKN-WIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPV 713
Cdd:cd17655 158 EHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEiFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 714 QLQWLLDAGLGSDPAYQpaQVLIGGEAISPAV---WSRLQSLSdTRFINVYGPTECTVDATACVVD---RTQPLPTIGKP 787
Cdd:cd17655 238 HLKLLDAADDSEGLSLK--HLIVGGEALSTELakkIIELFGTN-PTITNAYGPTETTVDASIYQYEpetDQQVSVPIGKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 788 LANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSadPAARIYKTGDLARWLPDGNIDYLGRN 867
Cdd:cd17655 315 LGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFV--PGERMYRTGDLARWLPDGNIEFLGRI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 868 DFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCArpDAELHPAALRQQLAASLADYMIPSAFVTL 947
Cdd:cd17655 393 DHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVS--EKELPVAQLREFLARELPDYMIPSYFIKL 470
|
490 500
....*....|....*....|
gi 641744967 948 DALPLTPNGKLDRKALPAPD 967
Cdd:cd17655 471 DEIPLTPNGKVDRKALPEPD 490
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1532-2025 |
0e+00 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 597.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1532 QLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPG 1611
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1612 YPAERLAYMLDDASPVALLTQANQRALL--TGDVprILLDTADFSHLSEDNPHVPGlDAHHLAYVIYTSGSTGKPKGVMN 1689
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPPIafIGLI--DLLDEDTIYHEESENLEPVS-KSDDLAYVIYTSGSTGKPKGVMI 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1690 SHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPS 1769
Cdd:cd17655 158 EHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1770 MLQQFVQwADADCACdSLRRVICSGEALPAELQQRFFARF--NAQLHNLYGPTEAAIDVTFWACQPDDHRS-FVPIGRPI 1846
Cdd:cd17655 238 HLKLLDA-ADDSEGL-SLKHLIVGGEALSTELAKKIIELFgtNPTITNAYGPTETTVDASIYQYEPETDQQvSVPIGKPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1847 ANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFInqPGARLYKTGDLARWLPDGSLEYLGRND 1926
Cdd:cd17655 316 GNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFV--PGERMYRTGDLARWLPDGNIEFLGRID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1927 FQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTpdPADLRQQLGQHLAEYMVPGAFVTLD 2006
Cdd:cd17655 394 HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELP--VAQLREFLARELPDYMIPSYFIKLD 471
|
490
....*....|....*....
gi 641744967 2007 AFPLTPNGKLDRKALPAPD 2025
Cdd:cd17655 472 EIPLTPNGKVDRKALPEPD 490
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1534-2022 |
0e+00 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 596.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1534 VEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYP 1613
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1614 AERLAYMLDDASPVALLTQANQRALLTGDVPRILLDTADFSHLSEDNPHVPGLDAHHLAYVIYTSGSTGKPKGVMNSHRA 1693
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1694 LCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQ 1773
Cdd:cd17651 161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1774 FVQWADADCA-CDSLRRVICSGEALP-AELQQRFFARF-NAQLHNLYGPTEAAIdVTFWA--CQPDDHRSFVPIGRPIAN 1848
Cdd:cd17651 241 LAEHGRPLGVrLAALRYLLTGGEQLVlTEDLREFCAGLpGLRLHNHYGPTETHV-VTALSlpGDPAAWPAPPPIGRPIDN 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1849 TQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFInqPGARLYKTGDLARWLPDGSLEYLGRNDFQ 1928
Cdd:cd17651 320 TRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV--PGARMYRTGDLARWLPDGELEFLGRADDQ 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1929 VKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAF 2008
Cdd:cd17651 398 VKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLDAL 477
|
490
....*....|....
gi 641744967 2009 PLTPNGKLDRKALP 2022
Cdd:cd17651 478 PLTPNGKLDRRALP 491
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
2620-3097 |
0e+00 |
|
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: 591.96 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALISQSAHLGIMNGSLPVILLDDGETRPFDNEPDTPLDarkqgltPRHLAYVIYTSGSTGKPKGVMVEHANMVN 2779
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPVS-------PDDLAYVIYTSGSTGRPKGVVVSHRNLVN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2780 FLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVE 2859
Cdd:cd12116 154 FLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2860 lRDFALPPGFKALCGGEALPENLATALLQKVTTLWNLYGPTETTIWSTLNGLTTPTPY--IGHPIANTQIYILDAQGRVV 2937
Cdd:cd12116 234 -AGWQGRAGLTALCGGEALPPDLAARLLSRVGSLWNLYGPTETTIWSTAARVTAAAGPipIGRPLANTQVYVLDAALRPV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2938 PLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSGaPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEI 3017
Cdd:cd12116 313 PPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAG-PGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEI 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3018 ETRLARCHGVHDAVVIAREDsPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd12116 392 EAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
475-964 |
0e+00 |
|
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes Planktothrix agardhii anabaenopeptin synthetase (ApnA A1), which is capable of activating two chemically distinct amino acids (Arg and Tyr). Structural studies show that the architecture of the active site forces Arg to adopt a Tyr-like conformation, thus explaining the bispecificity. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341299 [Multi-domain] Cd Length: 465 Bit Score: 589.41 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 475 IQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMD 554
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 555 PAYPAERLAYILDDAAPVALLTQSAqvaqlnstlptvlldtpaaaacpdtnpvvqglhaaHLAYVIYTSGSTGRPKGVMV 634
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLLTQPE-----------------------------------NLAYVIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 635 AHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWIQ-LLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPV 713
Cdd:cd17644 127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVtLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 714 QLQWLLDAGLGS--DPAYQPAQVLIGGEAISPAVWSRLQSLS--DTRFINVYGPTECTVDATACVVDRTQPL----PTIG 785
Cdd:cd17644 207 YWHLLVLELLLStiDLPSSLRLVIVGGEAVQPELVRQWQKNVgnFIQLINVYGPTEATIAATVCRLTQLTERnitsVPIG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 786 KPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSADPAARIYKTGDLARWLPDGNIDYLG 865
Cdd:cd17644 287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESERLYKTGDLARYLPDGNIEYLG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 866 RNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFV 945
Cdd:cd17644 367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMIPSAFV 446
|
490
....*....|....*....
gi 641744967 946 TLDALPLTPNGKLDRKALP 964
Cdd:cd17644 447 VLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1532-2021 |
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: 584.55 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1532 QLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPG 1611
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1612 YPAERLAYMLDDASPVALLTQANQRALLTGDVPRILLDTADFSHlSEDNPHVPgLDAHHLAYVIYTSGSTGKPKGVMNSH 1691
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAG-PAGNPAVP-VSPDDLAYVMYTSGSTGRPKGVAVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1692 RALcNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSML 1771
Cdd:cd12117 159 RGV-VRLVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAALF 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1772 QQFVQwADADCaCDSLRRVICSGEALPAELQQRFFARFNA-QLHNLYGPTEAAIDVTFWAC-QPDDHRSFVPIGRPIANT 1849
Cdd:cd12117 238 NQLAD-EDPEC-FAGLRELLTGGEVVSPPHVRRVLAACPGlRLVNGYGPTENTTFTTSHVVtELDEVAGSIPIGRPIANT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1850 QLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinQPGARLYKTGDLARWLPDGSLEYLGRNDFQV 1929
Cdd:cd12117 316 RVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF--GPGERLYRTGDLARWLPDGRLEFLGRIDDQV 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1930 KLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVtpDPADLRQQLGQHLAEYMVPGAFVTLDAFP 2009
Cdd:cd12117 394 KIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGAL--DAAELRAFLRERLPAYMVPAAFVVLDELP 471
|
490
....*....|..
gi 641744967 2010 LTPNGKLDRKAL 2021
Cdd:cd12117 472 LTANGKVDRRAL 483
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
479-964 |
0e+00 |
|
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes virginiamycin S synthetase (VisG) in Streptomyces virginiae; VisG is involved in virginiamycin S (VS) biosynthesis as the provider of an L-pheGly molecule, a highly specific substrate for the last condensation step by VisF. This family also includes linear gramicidin synthetase B (LgrB) in Brevibacillus brevis. Substrate specificity analysis using residues of the substrate-binding pockets of all 16 adenylation domains has shown good agreement of the substrate amino acids predicted with the sequence of linear gramicidin. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341306 [Multi-domain] Cd Length: 491 Bit Score: 576.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 479 FEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYP 558
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 559 AERLAYILDDAAPVALLTQSA-QVAQLNSTLPTVLLDTPAAAACPDTNPVVqGLHAAHLAYVIYTSGSTGRPKGVMVAHR 637
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPAlAGELAVELVAVTLLDQPGAAAGADAEPDP-ALDADDLAYVIYTSGSTGRPKGVVMPHR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 638 NVINLATGLHTLLALDHPSRIALNASIVFDASVKN-WIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQ 716
Cdd:cd17651 160 SLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEiFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 717 WLLDAGlGSDPAYQPA--QVLIGGEA--ISPAVWSRLQSLSDTRFINVYGPTECTVdATACVVDRTQP----LPTIGKPL 788
Cdd:cd17651 240 ALAEHG-RPLGVRLAAlrYLLTGGEQlvLTEDLREFCAGLPGLRLHNHYGPTETHV-VTALSLPGDPAawpaPPPIGRPI 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 789 ANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSadPAARIYKTGDLARWLPDGNIDYLGRND 868
Cdd:cd17651 318 DNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV--PGARMYRTGDLARWLPDGELEFLGRAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 869 FQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLD 948
Cdd:cd17651 396 DQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSAFVLLD 475
|
490
....*....|....*.
gi 641744967 949 ALPLTPNGKLDRKALP 964
Cdd:cd17651 476 ALPLTPNGKLDRRALP 491
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1542-2021 |
0e+00 |
|
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: 575.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1542 PDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYML 1621
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1622 DDASPVALLTQANQRALLTGDVPRILLDTADfSHLSEDNPHvPGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWM 1701
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAA-AAAAPAAPR-TPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFV--QWAD 1779
Cdd:cd12116 159 RERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLdaGWQG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1780 AdcacDSLrRVICSGEALPAELQQRFFARfNAQLHNLYGPTEAaidvTFW--ACQPDDHRSFVPIGRPIANTQLYILDTL 1857
Cdd:cd12116 239 R----AGL-TALCGGEALPPDLAARLLSR-VGSLWNLYGPTET----TIWstAARVTAAAGPIPIGRPLANTQVYVLDAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1858 GQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFiNQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIE 1937
Cdd:cd12116 309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPF-AGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIE 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1938 LGEIEARLMQCPGVQEAVVVAREDsPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLD 2017
Cdd:cd12116 388 LGEIEAALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLD 466
|
....
gi 641744967 2018 RKAL 2021
Cdd:cd12116 467 RKAL 470
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
477-963 |
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: 566.83 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 477 QRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPA 556
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 557 YPAERLAYILDDAAPVALLTQSAQVAQLNSTLPTVLLDTPAAAAcPDTNPVVqGLHAAHLAYVIYTSGSTGRPKGVMVAH 636
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAG-PAGNPAV-PVSPDDLAYVMYTSGSTGRPKGVAVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 637 RNVINLATGlHTLLALDHPSRIALNASIVFDASV-KNWIQLLSGHTLVLVPDALRADAHQLWRYFARHAVD-LFDCTPV- 713
Cdd:cd12117 159 RGVVRLVKN-TNYVTLGPDDRVLQTSPLAFDASTfEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTvLWLTAALf 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 714 -QL-----QWLldAGLGsdpayqpaQVLIGGEAISPA-VWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPLPT--- 783
Cdd:cd12117 238 nQLadedpECF--AGLR--------ELLTGGEVVSPPhVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVAGsip 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 784 IGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsaDPAARIYKTGDLARWLPDGNIDY 863
Cdd:cd12117 308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF--GPGERLYRTGDLARWLPDGRLEF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 864 LGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLcaRPDAELHPAALRQQLAASLADYMIPSA 943
Cdd:cd12117 386 LGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYV--VAEGALDAAELRAFLRERLPAYMVPAA 463
|
490 500
....*....|....*....|
gi 641744967 944 FVTLDALPLTPNGKLDRKAL 963
Cdd:cd12117 464 FVVLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1542-2022 |
1.02e-180 |
|
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: 562.26 E-value: 1.02e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1542 PDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYML 1621
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1622 DDASPVALLTQANqralltgdvprilldtadfshlsednphvpgldahHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWM 1701
Cdd:cd17652 81 ADARPALLLTTPD-----------------------------------NLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQqfvqWADAD 1781
Cdd:cd17652 126 IAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALA----ALPPD 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1782 CACDsLRRVICSGEALPAELQQRFFARfnAQLHNLYGPTEAAIDVTFWACQPDDHRsfVPIGRPIANTQLYILDTLGQPV 1861
Cdd:cd17652 202 DLPD-LRTLVVAGEACPAELVDRWAPG--RRMINAYGPTETTVCATMAGPLPGGGV--PPIGRPVPGTRVYVLDARLRPV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1862 PLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFiNQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEI 1941
Cdd:cd17652 277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPF-GAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1942 EARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd17652 356 EAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
.
gi 641744967 2022 P 2022
Cdd:cd17652 436 P 436
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1530-2022 |
6.07e-180 |
|
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: 561.29 E-value: 6.07e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLD 1609
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1610 PGYPAERLAYMLDDASPVALLTQAnqralltgdvprilldtadfshlsednphvpgldaHHLAYVIYTSGSTGKPKGVMN 1689
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLLTQP-----------------------------------ENLAYVIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1690 SHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPS 1769
Cdd:cd17644 127 EHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1770 MLQQfvqWADA----DCAC-DSLRRVICSGEA-LPAELQQRFFA-RFNAQLHNLYGPTEAAIDVTFwaCQPDDHRSF--- 1839
Cdd:cd17644 207 YWHL---LVLElllsTIDLpSSLRLVIVGGEAvQPELVRQWQKNvGNFIQLINVYGPTEATIAATV--CRLTQLTERnit 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1840 -VPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFINQPGARLYKTGDLARWLPDGS 1918
Cdd:cd17644 282 sVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESERLYKTGDLARYLPDGN 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1919 LEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMV 1998
Cdd:cd17644 362 IEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDYMI 441
|
490 500
....*....|....*....|....
gi 641744967 1999 PGAFVTLDAFPLTPNGKLDRKALP 2022
Cdd:cd17644 442 PSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1542-2021 |
8.09e-180 |
|
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: 560.39 E-value: 8.09e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1542 PDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYML 1621
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1622 DDASPVALLTqanqralltgdvprilldtadfshlsednphvpglDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWM 1701
Cdd:cd17643 81 ADSGPSLLLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADAD 1781
Cdd:cd17643 126 QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1782 C-ACDSLRRVICSGEALPAELQQRFFARFN---AQLHNLYGPTEAAIDVTFWACQPDD--HRSFVPIGRPIANTQLYILD 1855
Cdd:cd17643 206 GrDPLALRYVIFGGEALEAAMLRPWAGRFGldrPQLVNMYGITETTVHVTFRPLDAADlpAAAASPIGRPLPGLRVYVLD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1856 TLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFiNQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFR 1935
Cdd:cd17643 286 ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPF-GGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1936 IELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGK 2015
Cdd:cd17643 365 IELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNGK 444
|
....*.
gi 641744967 2016 LDRKAL 2021
Cdd:cd17643 445 LDRAAL 450
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1069-2106 |
1.52e-177 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 617.57 E-value: 1.52e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1069 PLSFSQQRLWFLAQLDPAASqAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDTLGFSLSS 1148
Cdd:PRK05691 3259 PLTPMQEGLLLHTLLEPGTG-LYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPIDY 3337
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1149 HDLRKLDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALEG 1228
Cdd:PRK05691 3338 LDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEG 3417
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1229 SEANLPPLPvQYADYAvwqrQWLQGETLNDLRDYWRDQLQGAPALLEIPTDRPrpSVQRYAGDQVPF-------HLDAGQ 1301
Cdd:PRK05691 3418 REAQLPVPP-RYRDYI----GWLQRQDLAQARQWWQDNLRGFERPTPIPSDRP--FLREHAGDSGGMvvgdcytRLDAAD 3490
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1302 LRRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQ--ELEGMVGFFVNTLALRT---EPGRCHAVAD 1376
Cdd:PRK05691 3491 GARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSmpQMQRTVGLFINSIALRVqlpAAGQRCSVRQ 3570
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1377 LLDQVRERALDAYAHQALPfeqVVEILQPARSLSYSPIFQVMLSLNNTPAQaltlpdltLSAVERPQH--------STHF 1448
Cdd:PRK05691 3571 WLQGLLDSNMELREYEYLP---LVAIQECSELPKGQPLFDSLFVFENAPVE--------VSVLDRAQSlnassdsgRTHT 3639
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1449 DLSLSLI---ETENGLNggLVYATDLFDRETILRVVGYVENILMAMADDVTQPVATLPILPDSERRQVMLDFNATEADFP 1525
Cdd:PRK05691 3640 NFPLTAVcypGDDLGLH--LSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYP 3717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1526 HDALIHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAY 1605
Cdd:PRK05691 3718 LEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGY 3797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1606 VPLDPGYPAERLAYMLD-DASPVALLTQA---NQRALLTG----DVPRILL-DTADFSHLSEDNPHVPGlDAHHLAYVIY 1676
Cdd:PRK05691 3798 LPLDPGLPAQRLQRIIElSRTPVLVCSAAcreQARALLDElgcaNRPRLLVwEEVQAGEVASHNPGIYS-GPDNLAYVIY 3876
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1677 TSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLI 1756
Cdd:PRK05691 3877 TSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHV 3956
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1757 ERTGITTLHFVPSMLQQFVqwADADCACDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWACQPDD 1835
Cdd:PRK05691 3957 QAQGITVLESVPSLIQGML--AEDRQALDGLRWMLPTGEAMPPELARQWLQRYpQIGLVNAYGPAECSDDVAFFRVDLAS 4034
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1836 HR-SFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFiNQPGARLYKTGDLARWL 1914
Cdd:PRK05691 4035 TRgSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPF-GAPGERLYRTGDLARRR 4113
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1915 PDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDtRLVAYLCPQPGVTpDPADLRQQLGQHL- 1993
Cdd:PRK05691 4114 SDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGK-HLVGYLVPHQTVL-AQGALLERIKQRLr 4191
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1994 ---AEYMVPGAFVTLDAFPLTPNGKLDRKALPAPDQSAVATRDYEAPQGEVETALAAVWQDLLGLTRVGRHDHFFALGGH 2070
Cdd:PRK05691 4192 aelPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGH 4271
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 641744967 2071 SLLIVSLIERLRRAgLALDV--RGVFSTPVLSDMAQAI 2106
Cdd:PRK05691 4272 SLLATQIASRVQKA-LQRNVplRAMFECSTVEELAEYI 4308
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2163-3191 |
6.63e-177 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 583.93 E-value: 6.63e-177
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2163 PLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCwQDLSQPVQVVWRQAILPINHF 2242
Cdd:PRK10252 9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFT-EDNGEVWQWVDPALTFPLPEI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2243 ----EPTSPEDV-LAQLQAHTEpRTRRIDLSQAPLFRADIAHDPlqNEWLLALSFHHLISDHMTLALIVGEIRLLLQHQA 2317
Cdd:PRK10252 88 idlrTQPDPHAAaQALMQADLQ-QDLRVDSGKPLVFHQLIQLGD--NRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2318 DALPTPLPyrNFIAQTLSVPN----SAHEAYFRD------KLADVDEPT--APfGLLNVQGSGGDIHeaRLVLDATlASA 2385
Cdd:PRK10252 165 RGEPTPAS--PFTPFADVVEEyqryRASEAWQRDaafwaeQRRQLPPPAslSP-APLPGRSASADIL--RLKLEFT-DGA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2386 IRQQARHLGVSPgvLFHVAWAQV---LAQTSGRDDVVFGSVLLGRLAGAegADRIMGMFINTLPLRISLADRGA-AEVVE 2461
Cdd:PRK10252 239 FRQLAAQASGVQ--RPDLALALValwLGRLCGRMDYAAGFIFMRRLGSA--ALTATGPVLNVLPLRVHIAAQETlPELAT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2462 RTSHDLMTLLEHEQAPLALAQRCSG-VAPPMPLFSTLLN-----YRHTqassTDNTLSDIRVLTSEERTNYPLTLAVDDR 2535
Cdd:PRK10252 315 RLAAQLKKMRRHQRYDAEQIVRDSGrAAGDEPLFGPVLNikvfdYQLD----FPGVQAQTHTLATGPVNDLELALFPDEH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2536 GeGFSLV----AQTLEDIDPHRLLNYLMTAISSLVDAletePQRSILNLPVLPDSERQQmLVDFNATDADIPRHALIhEL 2611
Cdd:PRK10252 391 G-GLSIEilanPQRYDEATLIAHAERLKALIAQFAAD----PALLCGDVDILLPGEYAQ-LAQVNATAVEIPETTLS-AL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2612 FEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYP 2691
Cdd:PRK10252 464 VAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYP 543
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2692 VERLRYMLDDAKPVALISQSAHLGIMNGslpvilLDDGETRPFDNePDTPLDARKQGLT-PRHLAYVIYTSGSTGKPKGV 2770
Cdd:PRK10252 544 DDRLKMMLEDARPSLLITTADQLPRFAD------VPDLTSLCYNA-PLAPQGAAPLQLSqPHHTAYIIFTSGSTGRPKGV 616
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2771 MVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQAT 2850
Cdd:PRK10252 617 MVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFV 696
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2851 PStwrML--------VELRDFALPPGFKALCGGEALPENLATALLQKVTT-LWNLYGPTE----TTIW-----STLNGLT 2912
Cdd:PRK10252 697 PS---MLaafvasltPEGARQSCASLRQVFCSGEALPADLCREWQQLTGApLHNLYGPTEaavdVSWYpafgeELAAVRG 773
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2913 TPTPyIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgAPEARMYKTGDLGRWLPD 2992
Cdd:PRK10252 774 SSVP-IGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPF--APGERMYRTGDVARWLDD 850
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2993 GTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAR-----EDSPGD-KRLVAYLLAQPDTVLEPADLRQRLS 3066
Cdd:PRK10252 851 GAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaAATGGDaRQLVGYLVSQSGLPLDTSALQAQLR 930
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3067 EGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAPD-QSAMATRgyeAPQGDLEHALAQIWQTLLGVERVGRHDHFFELGG 3145
Cdd:PRK10252 931 ERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPElKAQVPGR---APKTGTETIIAAAFSSLLGCDVVDADADFFALGG 1007
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*.
gi 641744967 3146 HSLLAVQLNARIRAEFLTDIPIVAIFQHPQLSALAEVILAAQIHAA 3191
Cdd:PRK10252 1008 HSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLATLLDAEEDESR 1053
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
487-964 |
5.87e-176 |
|
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: 548.78 E-value: 5.87e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYIL 566
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 567 DDAAPVALLTQsaqvaqlnstlptvlldtpaaaacpdtnpvvqglhAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGL 646
Cdd:cd17652 81 ADARPALLLTT-----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 647 HTLLALDHPSRIALNASIVFDASVKN-WIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLgs 725
Cdd:cd17652 126 IAAFDVGPGSRVLQFASPSFDASVWElLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDL-- 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 726 dPAYQpaQVLIGGEAISPAV---WSRlqslsDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQP 802
Cdd:cd17652 204 -PDLR--TLVVAGEACPAELvdrWAP-----GRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 803 VPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSAdPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGE 882
Cdd:cd17652 276 VPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGA-PGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 883 IESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKA 962
Cdd:cd17652 355 VEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRA 434
|
..
gi 641744967 963 LP 964
Cdd:cd17652 435 LP 436
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
2609-3097 |
2.60e-175 |
|
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: 549.19 E-value: 2.60e-175
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2609 HELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDP 2688
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2689 TYPVERLRYMLDDAKPVALISQSAHLGIMNGSLPVILLDDGEtrpFDNEPDTPLDARKQgltPRHLAYVIYTSGSTGKPK 2768
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEA---LAAPPATPPLVPPR---PDNLAYVIYTSGSTGRPK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2769 GVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQ 2848
Cdd:cd17646 155 GVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2849 ATPSTWRMLVELRDFALPPGFK-ALCGGEALPENLATALLQKV-TTLWNLYGPTETTIWSTL-----NGLTTPTPyIGHP 2921
Cdd:cd17646 235 FVPSMLRVFLAEPAAGSCASLRrVFCSGEALPPELAARFLALPgAELHNLYGPTEAAIDVTHwpvrgPAETPSVP-IGRP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2922 IANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgAPEARMYKTGDLGRWLPDGTLEYLGRN 3001
Cdd:cd17646 314 VPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF--GPGSRMYRTGDLARWRPDGALEFLGRS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3002 DFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPD-TVLEPADLRQRLSEGVAEYMIPSAFVT 3080
Cdd:cd17646 392 DDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGaAGPDTAALRAHLAERLPEYMVPAAFVV 471
|
490
....*....|....*..
gi 641744967 3081 LDAFPLTPNGKLDRKAL 3097
Cdd:cd17646 472 LDALPLTANGKLDRAAL 488
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1555-1956 |
2.69e-174 |
|
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: 542.63 E-value: 2.69e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1555 TYDALNRRANQLAHHLIDL-GVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQA 1633
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1634 NQRALLTGDVPRILLDTADFSHLSEDNPHVPGLDAH----HLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTP 1709
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPsgpdDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1710 DDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKD-AAYLAQLIERTGITTLHFVPSMLQQFVQWADAdcACDSLR 1788
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDdAALLAALIAEHPVTVLNLTPSLLALLAAALPP--ALASLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1789 RVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWACQPDDHRSF--VPIGRPIANTQLYILDTLGQPVPLGV 1865
Cdd:TIGR01733 239 LVILGGEALTPALVDRWRARGpGARLINLYGPTETTVWSTATLVDPDDAPREspVPIGRPLANTRLYVLDDDLRPVPVGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1866 AGELHIGGVGVARGYLNRPDLTAERFIPDPFINQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARL 1945
Cdd:TIGR01733 319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 398
|
410
....*....|.
gi 641744967 1946 MQCPGVQEAVV 1956
Cdd:TIGR01733 399 LRHPGVREAVV 409
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
479-963 |
2.85e-174 |
|
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341301 [Multi-domain] Cd Length: 488 Bit Score: 546.10 E-value: 2.85e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 479 FEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYP 558
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 559 AERLAYILDDAAPVALLTQSAQVAQLNSTLPTVLLDTPAAAACPDTNPVVqGLHAAHLAYVIYTSGSTGRPKGVMVAHRN 638
Cdd:cd17646 84 ADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPPATPPLV-PPRPDNLAYVIYTSGSTGRPKGVMVTHAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 639 VINLATGLHTLLALDHPSRIALNASIVFDASVKN-WIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQW 717
Cdd:cd17646 163 IVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWElFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLRV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 718 LLD-AGLGSDPAYQpaQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPLPT--IGKPLANTRLY 794
Cdd:cd17646 243 FLAePAAGSCASLR--RVFCSGEALPPELAARFLALPGAELHNLYGPTEAAIDVTHWPVRGPAETPSvpIGRPVPNTRLY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 795 ILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsaDPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVR 874
Cdd:cd17646 321 VLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPF--GPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIR 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 875 GFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAE-LHPAALRQQLAASLADYMIPSAFVTLDALPLT 953
Cdd:cd17646 399 GFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVVLDALPLT 478
|
490
....*....|
gi 641744967 954 PNGKLDRKAL 963
Cdd:cd17646 479 ANGKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
2610-3097 |
1.17e-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: 544.10 E-value: 1.17e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2610 ELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPT 2689
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2690 YPVERLRYMLDDAKPVALISQSAHLGIMNGSLPVILLDDGETRPFDNEPDTPLDarkqgltPRHLAYVIYTSGSTGKPKG 2769
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVS-------PDDLAYVMYTSGSTGRPKG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2770 VMVEHANMVNfLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQA 2849
Cdd:cd12117 154 VAVTHRGVVR-LVKNTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2850 TPSTWRMLVELRDFALPPGFKALCGGEALPENLATALLQKV--TTLWNLYGPTETTIWST--------LNGLTTPtpyIG 2919
Cdd:cd12117 233 TAALFNQLADEDPECFAGLRELLTGGEVVSPPHVRRVLAACpgLRLVNGYGPTENTTFTTshvvteldEVAGSIP---IG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2920 HPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgAPEARMYKTGDLGRWLPDGTLEYLG 2999
Cdd:cd12117 310 RPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPF--GPGERLYRTGDLARWLPDGRLEFLG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3000 RNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDtvLEPADLRQRLSEGVAEYMIPSAFV 3079
Cdd:cd12117 388 RIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGA--LDAAELRAFLRERLPAYMVPAAFV 465
|
490
....*....|....*...
gi 641744967 3080 TLDAFPLTPNGKLDRKAL 3097
Cdd:cd12117 466 VLDELPLTANGKVDRRAL 483
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
2610-3101 |
6.33e-173 |
|
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: 542.30 E-value: 6.33e-173
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2610 ELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPT 2689
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2690 YPVERLRYMLDDAKPVALISQSAHLGIMNGSLPVILLDDGETRpfdNEPDTPLDARKQgltPRHLAYVIYTSGSTGKPKG 2769
Cdd:cd17655 81 YPEERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIY---HEESENLEPVSK---SDDLAYVIYTSGSTGKPKG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2770 VMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQA 2849
Cdd:cd17655 155 VMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2850 TPSTWRMLVELRDFALPPGFKALCGGEALPENLATALLQKVT---TLWNLYGPTETTIWSTLNGL-----TTPTPYIGHP 2921
Cdd:cd17655 235 TPAHLKLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGtnpTITNAYGPTETTVDASIYQYepetdQQVSVPIGKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2922 IANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgAPEARMYKTGDLGRWLPDGTLEYLGRN 3001
Cdd:cd17655 315 LGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF--VPGERMYRTGDLARWLPDGNIEFLGRI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3002 DFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDtvLEPADLRQRLSEGVAEYMIPSAFVTL 3081
Cdd:cd17655 393 DHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKE--LPVAQLREFLARELPDYMIPSYFIKL 470
|
490 500
....*....|....*....|
gi 641744967 3082 DAFPLTPNGKLDRKALPAPD 3101
Cdd:cd17655 471 DEIPLTPNGKVDRKALPEPD 490
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
30-1067 |
5.07e-171 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 566.60 E-value: 5.07e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 30 PLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICwQGLHQPVQVVWRQAPLTVNTL 109
Cdd:PRK10252 9 PLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFT-EDNGEVWQWVDPALTFPLPEI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 110 tttssdtvpAQLRAATDPSNHRLNLSNAPLLSA--TTAHDP-------VCGE--WLLSLSIHHLISDHITQALIIDEI-- 176
Cdd:PRK10252 88 ---------IDLRTQPDPHAAAQALMQADLQQDlrVDSGKPlvfhqliQLGDnrWYWYQRYHHLLVDGFSFPAITRRIaa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 177 --RLLLEDRPEALPKPLPYRNFIAQILSVPLSEHEQ----YFRNRLADIDTPTApfdlvdvqgngedITEARLSLDSSLA 250
Cdd:PRK10252 159 iyCAWLRGEPTPASPFTPFADVVEEYQRYRASEAWQrdaaFWAEQRRQLPPPAS-------------LSPAPLPGRSASA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 251 DALRRQARHLGIS-SSVLFHVAWAQ----VLALT-------SGRDDVVFGSVLSGRLqGNlGADRVMGMFINTLPLRVSL 318
Cdd:PRK10252 226 DILRLKLEFTDGAfRQLAAQASGVQrpdlALALValwlgrlCGRMDYAAGFIFMRRL-GS-AALTATGPVLNVLPLRVHI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 319 -RERSVHDVVQATSHELMMLLAH-----EQ----APLALAQQcsqvppplPLFSTLFN-----YRHSQKDASSQfwegMR 383
Cdd:PRK10252 304 aAQETLPELATRLAAQLKKMRRHqrydaEQivrdSGRAAGDE--------PLFGPVLNikvfdYQLDFPGVQAQ----TH 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 384 QLSgrertnypiTLSVDDLGDGFNLTAKTVMGVD----PERIVHYMLTA-IENLVTSLEKTPQQPAL---SQPILPKSER 455
Cdd:PRK10252 372 TLA---------TGPVNDLELALFPDEHGGLSIEilanPQRYDEATLIAhAERLKALIAQFAADPALlcgDVDILLPGEY 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 456 QQvLVDFNATDADFPREMLIQQrFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLE 535
Cdd:PRK10252 443 AQ-LAQVNATAVEIPETTLSAL-VAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVF 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 536 MMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQSAQVAQLNSTLPTVLLDTPAAAACPDTNPVVQGlHAAH 615
Cdd:PRK10252 521 LTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLS-QPHH 599
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 616 LAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASV-KNWIQLLSGHTLVLV-PDALRaDA 693
Cdd:PRK10252 600 TAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLTADDVVLQKTPCSFDVSVwEFFWPFIAGAKLVMAePEAHR-DP 678
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 694 HQLWRYFARHAVDLFDCTPVQLQWLLdAGLGSDPAYQP----AQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVD 769
Cdd:PRK10252 679 LAMQQFFAEYGVTTTHFVPSMLAAFV-ASLTPEGARQScaslRQVFCSGEALPADLCREWQQLTGAPLHNLYGPTEAAVD 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 770 AT---ACVVD----RTQPLPtIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSadP 842
Cdd:PRK10252 758 VSwypAFGEElaavRGSSVP-IGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA--P 834
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 843 AARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAR-----EDSPGD-TRLVAYLCA 916
Cdd:PRK10252 835 GERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaAATGGDaRQLVGYLVS 914
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 917 RPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAPDQTA-FATRdyeAPQGGIETALAALWQELL 995
Cdd:PRK10252 915 QSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAqVPGR---APKTGTETIIAAAFSSLL 991
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 996 GLDRVGRHDQFFALGGHSLLAVQLLNRMNKA-GMDVALATLFAHPTLCDLAAAVTATAHDAPFT-----LPVADRTQP 1067
Cdd:PRK10252 992 GCDVVDADADFFALGGHSLLAMKLAAQLSRQfARQVTPGQVMVASTVAKLATLLDAEEDESRRLgfgtiLPLREGDGP 1069
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1530-2021 |
1.60e-169 |
|
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: 530.74 E-value: 1.60e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLD 1609
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1610 PGYPAERLAYMLDDASPVALLTqanqralltgdvprilldtadfshlsednphvpglDAHHLAYVIYTSGSTGKPKGVMN 1689
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVAI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1690 SHRALCNRLVWMQNTYrlTPDDR--VLQKTPFSFDVSVWEFFWPLLYGARLVMArpdghKDAAYLAQLIERTGITTLHFV 1767
Cdd:cd12115 126 EHRNAAAFLQWAAAAF--SAEELagVLASTSICFDLSVFELFGPLATGGKVVLA-----DNVLALPDLPAAAEVTLINTV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1768 PSMLQQFVQwadADCACDSLRRVICSGEALPAELQQRFFARFNA-QLHNLYGPTEAAIDVTFWACQPDDHRSfVPIGRPI 1846
Cdd:cd12115 199 PSAAAELLR---HDALPASVRVVNLAGEPLPRDLVQRLYARLQVeRVVNLYGPSEDTTYSTVAPVPPGASGE-VSIGRPL 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1847 ANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinQPGARLYKTGDLARWLPDGSLEYLGRND 1926
Cdd:cd12115 275 ANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF--GPGARLYRTGDLVRWRPDGLLEFLGRAD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1927 FQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLD 2006
Cdd:cd12115 353 NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLD 432
|
490
....*....|....*
gi 641744967 2007 AFPLTPNGKLDRKAL 2021
Cdd:cd12115 433 ALPLTPNGKIDRSAL 447
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
2612-3098 |
3.79e-168 |
|
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: 528.45 E-value: 3.79e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2612 FEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYP 2691
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2692 VERLRYMLDDAKPVALISQSAHLGIMNGSLPVILLDDGETRPfdNEPDTPLDARkqgLTPRHLAYVIYTSGSTGKPKGVM 2771
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAA--AGADAEPDPA---LDADDLAYVIYTSGSTGRPKGVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2772 VEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATP 2851
Cdd:cd17651 156 MPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2852 STWRMLVEL--RDFALPPGFKAL-CGGEALPenlATALLQKVTT------LWNLYGPTETTIWS--TLNGLTTP---TPY 2917
Cdd:cd17651 236 VALRALAEHgrPLGVRLAALRYLlTGGEQLV---LTEDLREFCAglpglrLHNHYGPTETHVVTalSLPGDPAAwpaPPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2918 IGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSgaPEARMYKTGDLGRWLPDGTLEY 2997
Cdd:cd17651 313 IGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV--PGARMYRTGDLARWLPDGELEF 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2998 LGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSA 3077
Cdd:cd17651 391 LGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAELRAALATHLPEYMVPSA 470
|
490 500
....*....|....*....|.
gi 641744967 3078 FVTLDAFPLTPNGKLDRKALP 3098
Cdd:cd17651 471 FVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1542-2022 |
4.19e-168 |
|
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: 526.55 E-value: 4.19e-168
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1542 PDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYML 1621
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1622 DDASPVALLTQANQralltgdvprilldtadfshlsednphvpgldahHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWM 1701
Cdd:cd17649 81 EDSGAGLLLTHHPR----------------------------------QLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADAD 1781
Cdd:cd17649 127 AERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1782 CACD--SLRRVICSGEALPAELQQRFFARfNAQLHNLYGPTEAAIDVTFWACQPDDHR--SFVPIGRPIANTQLYILDTL 1857
Cdd:cd17649 207 GDGRppSLRLYIFGGEALSPELLRRWLKA-PVRLFNAYGPTEATVTPLVWKCEAGAARagASMPIGRPLGGRSAYILDAD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1858 GQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFiNQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIE 1937
Cdd:cd17649 286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPF-GAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1938 LGEIEARLMQCPGVQEAVVVAReDSPGDTRLVAYLCPQPGVTP--DPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGK 2015
Cdd:cd17649 365 LGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQpeLRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGK 443
|
....*..
gi 641744967 2016 LDRKALP 2022
Cdd:cd17649 444 LDRKALP 450
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
487-963 |
1.28e-166 |
|
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: 522.25 E-value: 1.28e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYIL 566
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 567 DDAAPVALLTQsaqvaqlnstlptvlldtpaaaacpdtnpvvqglhAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGL 646
Cdd:cd17643 81 ADSGPSLLLTD-----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 647 HTLLALDHPSRIALNASIVFDASV-KNWIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGS 725
Cdd:cd17643 126 QRWFGFNEDDVWTLFHSYAFDFSVwEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 726 DPAyQPA--QVLIGGEAISPAV---WSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPLP----TIGKPLANTRLYIL 796
Cdd:cd17643 206 GRD-PLAlrYVIFGGEALEAAMlrpWAGRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAaaasPIGRPLPGLRVYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 797 DAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSAdPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGF 876
Cdd:cd17643 285 DADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGG-PGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 877 RIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNG 956
Cdd:cd17643 364 RIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPLTVNG 443
|
....*..
gi 641744967 957 KLDRKAL 963
Cdd:cd17643 444 KLDRAAL 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
487-963 |
3.14e-166 |
|
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: 522.24 E-value: 3.14e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYIL 566
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 567 DDAAPVALLTQSAQVAQLNSTLPTVLLDTPAAAACPDTNPVvqGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGL 646
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRT--PVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 647 HTLLALDHPSRIALNASIVFDASV-KNWIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLgs 725
Cdd:cd12116 159 RERLGLGPGDRLLAVTTYAFDISLlELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLDAGW-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 726 dPAYQPAQVLIGGEAISPAVWSRLQSLSdTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQPVPI 805
Cdd:cd12116 237 -QGRAGLTALCGGEALPPDLAARLLSRV-GSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 806 GVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsADPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIES 885
Cdd:cd12116 315 GVPGELYIGGDGVAQGYLGRPALTAERFVPDPF-AGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEA 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 886 RLLRCPGVQDAVVIAREDsPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd12116 394 ALAAHPGVAQAAVVVRED-GGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
2633-3032 |
1.22e-165 |
|
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: 517.59 E-value: 1.22e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2633 SYDELNRRANRLAHHLIS-FGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQS 2711
Cdd:TIGR01733 1 TYRELDERANRLARHLRAaGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2712 AHLGIMNG-SLPVILLDDGETRPFDNEPDTPLDARKQGltPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGI 2790
Cdd:TIGR01733 81 ALASRLAGlVLPVILLDPLELAALDDAPAPPPPDAPSG--PDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2791 AQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAM-LIERHAVSFMQATPSTWRMLVELRDFALPpGF 2869
Cdd:TIGR01733 159 DPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAaLIAEHPVTVLNLTPSLLALLAAALPPALA-SL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2870 KALC-GGEALPENLATALLQKV--TTLWNLYGPTETTIWST-------LNGLTTPTPyIGHPIANTQIYILDAQGRVVPL 2939
Cdd:TIGR01733 238 RLVIlGGEALTPALVDRWRARGpgARLINLYGPTETTVWSTatlvdpdDAPRESPVP-IGRPLANTRLYVLDDDLRPVPV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2940 GVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSGAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIET 3019
Cdd:TIGR01733 317 GVVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 396
|
410
....*....|...
gi 641744967 3020 RLARCHGVHDAVV 3032
Cdd:TIGR01733 397 ALLRHPGVREAVV 409
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
2620-3098 |
1.36e-165 |
|
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: 518.73 E-value: 1.36e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALISQsahlgimngslpvillddgetrpfdnepdtpldarkqgltPRHLAYVIYTSGSTGKPKGVMVEHANMVN 2779
Cdd:cd17652 81 ADARPALLLTT----------------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLAN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2780 FLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTwrmLVE 2859
Cdd:cd17652 121 LAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAA---LAA 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2860 LRDFALPPGFKALCGGEALPENLAtALLQKVTTLWNLYGPTETTIWSTLNGLTTP--TPYIGHPIANTQIYILDAQGRVV 2937
Cdd:cd17652 198 LPPDDLPDLRTLVVAGEACPAELV-DRWAPGRRMINAYGPTETTVCATMAGPLPGggVPPIGRPVPGTRVYVLDARLRPV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2938 PLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsGAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEI 3017
Cdd:cd17652 277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPF-GAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3018 ETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd17652 356 EAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRAL 435
|
.
gi 641744967 3098 P 3098
Cdd:cd17652 436 P 436
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
2608-3098 |
2.21e-165 |
|
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: 519.68 E-value: 2.21e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2608 IHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLD 2687
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2688 PTYPVERLRYMLDDAKPVALISQsahlgimngslpvillddgetrpfdnepdtpldarkqgltPRHLAYVIYTSGSTGKP 2767
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLLTQ----------------------------------------PENLAYVIYTSGSTGKP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2768 KGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFM 2847
Cdd:cd17644 122 KGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2848 QATPSTWRMLVE---LRDFALPPGFK-ALCGGEA-LPENLATalLQKVT----TLWNLYGPTETTIWSTLNGLTTPT--- 2915
Cdd:cd17644 202 SLPPAYWHLLVLellLSTIDLPSSLRlVIVGGEAvQPELVRQ--WQKNVgnfiQLINVYGPTEATIAATVCRLTQLTern 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2916 ---PYIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSGAPEARMYKTGDLGRWLPD 2992
Cdd:cd17644 280 itsVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSSESERLYKTGDLARYLPD 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2993 GTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEY 3072
Cdd:cd17644 360 GNIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVELRQFLKAKLPDY 439
|
490 500
....*....|....*....|....*.
gi 641744967 3073 MIPSAFVTLDAFPLTPNGKLDRKALP 3098
Cdd:cd17644 440 MIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-1048 |
2.71e-163 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 571.34 E-value: 2.71e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2 PLVTLSQEEIDTViatvPDGVANVQDIYPLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDI 81
Cdd:PRK05691 3235 PLAQLTQAQLDAL----PVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQDRYRINSALDPERFAQAWQAVVARHEA 3310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 82 LRTAICWQGLHQPVQVVWRQAPLTVNTL--TTTSSDTVPAQLRAATDPSNHR-LNLSNAPLLSATTAHDPVCGEWLLsLS 158
Cdd:PRK05691 3311 LRASFSWNAGETMLQVIHKPGRTPIDYLdwRGLPEDGQEQRLQALHKQEREAgFDLLNQPPFHLRLIRVDEARYWFM-MS 3389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 159 IHHLISDHITQALIIDEI----RLLLEDRPEALPKPLPYRNFIAQILSVPLSEHEQYFRNRLADIDTPTA-----PFdLV 229
Cdd:PRK05691 3390 NHHILIDAWCRSLLMNDFfeiyTALGEGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRGFERPTPipsdrPF-LR 3468
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 230 DVQGN--GEDITEARLSLDSSLADALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQGNLGADRVMGM 307
Cdd:PRK05691 3469 EHAGDsgGMVVGDCYTRLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSMPQMQRTVGL 3548
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 308 FINTLPLRVSLRE----RSVHDVVQATSHELMMLLAHEQAPLALAQQCSQVPPPLPLFSTLFNY-----------RHSQK 372
Cdd:PRK05691 3549 FINSIALRVQLPAagqrCSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKGQPLFDSLFVFenapvevsvldRAQSL 3628
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 373 DASSQfwegmrqlSGRERTNYPITLSV---DDLG-----DGFNLTAKTVmgvdpERivhyMLTAIENLVTSLEKTPQQPA 444
Cdd:PRK05691 3629 NASSD--------SGRTHTNFPLTAVCypgDDLGlhlsyDQRYFDAPTV-----ER----LLGEFKRLLLALVQGFHGDL 3691
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 445 LSQPILPKSERQQVLVDFNATDADFPREMLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDD 524
Cdd:PRK05691 3692 SELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQ 3771
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 525 RVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQSAQVAQLNSTL--------PTVLL-DT 595
Cdd:PRK05691 3772 PVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACREQARALLdelgcanrPRLLVwEE 3851
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 596 PAAAACPDTNPvvqGLHAA--HLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVknW 673
Cdd:PRK05691 3852 VQAGEVASHNP---GIYSGpdNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISV--W 3926
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 674 IQL---LSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQWLLDaglgsdpayQPAQVLIG-------GEAISP 743
Cdd:PRK05691 3927 QFLaapLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLA---------EDRQALDGlrwmlptGEAMPP 3997
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 744 AVWSR-LQSLSDTRFINVYGPTECTVDATACVVD----RTQPLPtIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGV 818
Cdd:PRK05691 3998 ELARQwLQRYPQIGLVNAYGPAECSDDVAFFRVDlastRGSYLP-IGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGV 4076
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 819 ARGYLHRPDLTAERFIPDPFSAdPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVV 898
Cdd:PRK05691 4077 GRGYVGDPLRTALAFVPHPFGA-PGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAV 4155
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 899 IAREDSPGDtRLVAYLCARpDAELHPAAL----RQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAPDQTAFATR 974
Cdd:PRK05691 4156 AVQEGVNGK-HLVGYLVPH-QTVLAQGALleriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQ 4233
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 975 DYEAPQGGIETALAALWQELLGLDRVGRHDQFFALGGHSLLAVQLLNRMNKA-GMDVALATLFAHPTLCDLAAAV 1048
Cdd:PRK05691 4234 AYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKAlQRNVPLRAMFECSTVEELAEYI 4308
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1067-1494 |
5.10e-161 |
|
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: 505.42 E-value: 5.10e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1067 PLPLSFSQQRLWFLAQLDPAASqAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQI-DPDTLGFS 1145
Cdd:cd19540 1 RIPLSFAQQRLWFLNRLDGPSA-AYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVlPAAEARPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1146 LSSHDLrklDEAARTTRVAELAeqeaRARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAA 1225
Cdd:cd19540 80 LTVVDV---TEDELAARLAEAA----RRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAAR 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1226 LEGSEANLPPLPVQYADYAVWQRQWLQGETLNDLR-----DYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAG 1300
Cdd:cd19540 153 RAGRAPDWAPLPVQYADYALWQRELLGDEDDPDSLaarqlAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1301 QLRRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQ 1380
Cdd:cd19540 233 LHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLAR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1381 VRERALDAYAHQALPFEQVVEILQPARSLSYSPIFQVMLSLNNTPAQALTLPDLTLSAVERPQHSTHFDLSLSLIETEN- 1459
Cdd:cd19540 313 VRETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTERRDa 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 641744967 1460 -----GLNGGLVYATDLFDRETILRVVGYVENILMAMADD 1494
Cdd:cd19540 393 dgapaGLTGELEYATDLFDRSTAERLADRFVRVLEAVVAD 432
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2125-3183 |
1.08e-160 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 562.87 E-value: 1.08e-160
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2125 DSTAITPDLLPLVTLTQPEIDritdTVSGGASNIQDIYPLAPLQEGILFHHLLQEQGDTYLLRSmvafthRERLDA---- 2200
Cdd:PRK05691 3225 GAGGLTPSDFPLAQLTQAQLD----ALPVPAAEIEDVYPLTPMQEGLLLHTLLEPGTGLYYMQD------RYRINSaldp 3294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2201 --FLSALQQVIDRHDILRTAVCWQDLSQPVQVVWRQAILPINHFEPTS-PEDVLAQ-LQA-HTEPRTRRIDLSQAPLFRA 2275
Cdd:PRK05691 3295 erFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPIDYLDWRGlPEDGQEQrLQAlHKQEREAGFDLLNQPPFHL 3374
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2276 DIAHDPLQNEWLLaLSFHHLISDHMTLALIVGEI----RLLLQHQADALPTPLPYRNFIAQTLSVPNSAHEAYFRDKLAD 2351
Cdd:PRK05691 3375 RLIRVDEARYWFM-MSNHHILIDAWCRSLLMNDFfeiyTALGEGREAQLPVPPRYRDYIGWLQRQDLAQARQWWQDNLRG 3453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2352 VDEPTA-----PFGLLNVQGSGGDIHEARLV-LDATLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLL 2425
Cdd:PRK05691 3454 FERPTPipsdrPFLREHAGDSGGMVVGDCYTrLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVA 3533
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2426 GRLAGAEGADRIMGMFINTLPLRISLADRGA-AEVVERTSHDL---MTLLEHEQAPLALAQRCSGVAPPMPLFSTLLNYR 2501
Cdd:PRK05691 3534 GRPVSMPQMQRTVGLFINSIALRVQLPAAGQrCSVRQWLQGLLdsnMELREYEYLPLVAIQECSELPKGQPLFDSLFVFE 3613
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2502 HT--QASSTD-----NTLSDirvlTSEERTNYPLTlAV----DDRGEGFSLVAQTLEDIDPHRLLNYLMTAISSLVDALE 2570
Cdd:PRK05691 3614 NApvEVSVLDraqslNASSD----SGRTHTNFPLT-AVcypgDDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFH 3688
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2571 TEpqrsILNLPVLPDSERQQMLVDFNATDADIPRHALIHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLIS 2650
Cdd:PRK05691 3689 GD----LSELPLLGEQERDFLLDGCNRSERDYPLEQSYVRLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRA 3764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2651 FGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQSAHLgimngSLPVILLD--D 2728
Cdd:PRK05691 3765 AGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAACR-----EQARALLDelG 3839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2729 GETRP----FDNEPDTPLDARKQGL--TPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSL 2802
Cdd:PRK05691 3840 CANRPrllvWEEVQAGEVASHNPGIysGPDNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQ 3919
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2803 SFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPS-TWRMLVELRDfALPPGFKALCGGEALPEN 2881
Cdd:PRK05691 3920 SFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSlIQGMLAEDRQ-ALDGLRWMLPTGEAMPPE 3998
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2882 LATALLQKVTT--LWNLYGPTETT---IWSTLNGLTTPTPY--IGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVR 2954
Cdd:PRK05691 3999 LARQWLQRYPQigLVNAYGPAECSddvAFFRVDLASTRGSYlpIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGR 4078
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2955 GYLGRPDLTAERFITDPFsGAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIA 3034
Cdd:PRK05691 4079 GYVGDPLRTALAFVPHPF-GAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAV 4157
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3035 REDSPGdKRLVAYLLAQpDTVLEPADL----RQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAPDQSAMATRGY 3110
Cdd:PRK05691 4158 QEGVNG-KHLVGYLVPH-QTVLAQGALleriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAY 4235
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 3111 EAPQGDLEHALAQIWQTLLGVERVGRHDHFFELGGHSLLAVQLNARIRAEFLTDIPIVAIFQHPQLSALAEVI 3183
Cdd:PRK05691 4236 LAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI 4308
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
487-964 |
1.68e-159 |
|
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: 501.90 E-value: 1.68e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYIL 566
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 567 DDAAPVALLTQsaqvaqlnstlptvlldtpaaaacpdtnpvvqglHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGL 646
Cdd:cd17649 81 EDSGAGLLLTH----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 647 HTLLALDHPSRIALNASIVFDASVKNWIQ-LLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQL-QWLLDAGLG 724
Cdd:cd17649 127 AERYGLTPGDRELQFASFNFDGAHEQLLPpLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLqQLAEEADRT 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 725 SDPAYQPAQVLI-GGEAISPAVWSRLQSlSDTRFINVYGPTECTVDATACVV----DRTQPLPTIGKPLANTRLYILDAQ 799
Cdd:cd17649 207 GDGRPPSLRLYIfGGEALSPELLRRWLK-APVRLFNAYGPTEATVTPLVWKCeagaARAGASMPIGRPLGGRSAYILDAD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 800 DQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSAdPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIE 879
Cdd:cd17649 286 LNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGA-PGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 880 AGEIESRLLRCPGVQDAVVIAReDSPGDTRLVAYLCARPDAELH--PAALRQQLAASLADYMIPSAFVTLDALPLTPNGK 957
Cdd:cd17649 365 LGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPelRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGK 443
|
....*..
gi 641744967 958 LDRKALP 964
Cdd:cd17649 444 LDRKALP 450
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
2620-3097 |
6.75e-159 |
|
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: 500.30 E-value: 6.75e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALISQsahlgimngslpvillddgetrpfdnepdtpldarkqgltPRHLAYVIYTSGSTGKPKGVMVEHANMVN 2779
Cdd:cd17643 81 ADSGPSLLLTD----------------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2780 FLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVE 2859
Cdd:cd17643 121 LFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2860 --LRDFALPPGFK-ALCGGEALPENLATALLQKV----TTLWNLYGPTETTIWSTLNGLTTPTPY------IGHPIANTQ 2926
Cdd:cd17643 201 aaDRDGRDPLALRyVIFGGEALEAAMLRPWAGRFgldrPQLVNMYGITETTVHVTFRPLDAADLPaaaaspIGRPLPGLR 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2927 IYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSGAPEaRMYKTGDLGRWLPDGTLEYLGRNDFQVK 3006
Cdd:cd17643 281 VYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGS-RMYRTGDLARRLPDGELEYLGRADEQVK 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3007 VRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPL 3086
Cdd:cd17643 360 IRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVPLDALPL 439
|
490
....*....|.
gi 641744967 3087 TPNGKLDRKAL 3097
Cdd:cd17643 440 TVNGKLDRAAL 450
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
2608-3097 |
1.33e-158 |
|
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: 499.15 E-value: 1.33e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2608 IHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLD 2687
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2688 PTYPVERLRYMLDDAKPVALISQsahlgimngslpvillddgetrpfdnepdtpldarkqgltPRHLAYVIYTSGSTGKP 2767
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLTD----------------------------------------PDDLAYVIYTSGSTGRP 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2768 KGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLamlieRHAVSFM 2847
Cdd:cd12115 121 KGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPA-----AAEVTLI 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2848 QATPSTWRMLVELRdfALPPGFKALC-GGEALPENLATALLQK--VTTLWNLYGPTETTIWSTLNGLTT---PTPYIGHP 2921
Cdd:cd12115 196 NTVPSAAAELLRHD--ALPASVRVVNlAGEPLPRDLVQRLYARlqVERVVNLYGPSEDTTYSTVAPVPPgasGEVSIGRP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2922 IANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSgaPEARMYKTGDLGRWLPDGTLEYLGRN 3001
Cdd:cd12115 274 LANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG--PGARLYRTGDLVRWRPDGLLEFLGRA 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3002 DFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTL 3081
Cdd:cd12115 352 DNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRL 431
|
490
....*....|....*.
gi 641744967 3082 DAFPLTPNGKLDRKAL 3097
Cdd:cd12115 432 DALPLTPNGKIDRSAL 447
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
500-898 |
1.67e-158 |
|
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: 497.17 E-value: 1.67e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 500 TYRELNRRANQLAHHLIAL-GVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQS 578
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 AQVAQLNSTLPTVLL----DTPAAAACPDTNPVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDH 654
Cdd:TIGR01733 81 ALASRLAGLVLPVILldplELAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 655 PSRIALNASIVFDASV-KNWIQLLSGHTLVLVPDALRADAHQLWRYF-ARHAVDLFDCTPVQLQWLLDAGLGSDPAYQpa 732
Cdd:TIGR01733 161 DDRVLQFASLSFDASVeEIFGALLAGATLVVPPEDEERDDAALLAALiAEHPVTVLNLTPSLLALLAAALPPALASLR-- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 733 QVLIGGEAISPAVWSRLQSL-SDTRFINVYGPTECTVDATACVVD-----RTQPLPtIGKPLANTRLYILDAQDQPVPIG 806
Cdd:TIGR01733 239 LVILGGEALTPALVDRWRARgPGARLINLYGPTETTVWSTATLVDpddapRESPVP-IGRPLANTRLYVLDDDLRPVPVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 807 VTGELHIGGAGVARGYLHRPDLTAERFIPDPFSADPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESR 886
Cdd:TIGR01733 318 VVGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAA 397
|
410
....*....|..
gi 641744967 887 LLRCPGVQDAVV 898
Cdd:TIGR01733 398 LLRHPGVREAVV 409
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1541-2022 |
1.32e-152 |
|
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: 483.51 E-value: 1.32e-152
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1541 TPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYM 1620
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1621 LDDASPVALLTQANQRALLTGDVPRILLDTADFSHLSEDNPHVPgLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVW 1700
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYI-NNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1701 MQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQ-FVQWAD 1779
Cdd:cd17656 160 EREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFiFSEREF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1780 ADCACDSLRRVICSGEALP-AELQQRFFARFNAQLHNLYGPTEAAIdVTFWACQPDDH-RSFVPIGRPIANTQLYILDTL 1857
Cdd:cd17656 240 INRFPTCVKHIITAGEQLViTNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTINPEAEiPELPPIGKPISNTWIYILDQE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1858 GQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIE 1937
Cdd:cd17656 319 QQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF--DPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIE 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1938 LGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTpdPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLD 2017
Cdd:cd17656 397 LGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELN--ISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVD 474
|
....*
gi 641744967 2018 RKALP 2022
Cdd:cd17656 475 RKALP 479
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
475-963 |
4.11e-151 |
|
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: 477.58 E-value: 4.11e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 475 IQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMD 554
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 555 PAYPAERLAYILDDAAPVALLTQSAqvaqlnstlptvlldtpaaaacpdtnpvvqglhaaHLAYVIYTSGSTGRPKGVMV 634
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLTDPD-----------------------------------DLAYVIYTSGSTGRPKGVAI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 635 AHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWIQLLS-GHTLVLVPDALradahQLWRYFARHAVDLFDCTPV 713
Cdd:cd12115 126 EHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLAtGGKVVLADNVL-----ALPDLPAAAEVTLINTVPS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 714 QLQWLLDAglgsDPAYQPAQVL-IGGEAISPAVWSRLQS-LSDTRFINVYGPTECTVDATACVVDR-TQPLPTIGKPLAN 790
Cdd:cd12115 201 AAAELLRH----DALPASVRVVnLAGEPLPRDLVQRLYArLQVERVVNLYGPSEDTTYSTVAPVPPgASGEVSIGRPLAN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 791 TRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsaDPAARIYKTGDLARWLPDGNIDYLGRNDFQ 870
Cdd:cd12115 277 TQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPF--GPGARLYRTGDLVRWRPDGLLEFLGRADNQ 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 871 IKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDAL 950
Cdd:cd12115 355 VKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDAL 434
|
490
....*....|...
gi 641744967 951 PLTPNGKLDRKAL 963
Cdd:cd12115 435 PLTPNGKIDRSAL 447
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
2620-3098 |
1.67e-150 |
|
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: 476.09 E-value: 1.67e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALISQsahlgimngslpvillddgetrpfdnepdtpldarkqglTPRHLAYVIYTSGSTGKPKGVMVEHANMVN 2779
Cdd:cd17649 81 EDSGAGLLLTH---------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2780 FLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVE 2859
Cdd:cd17649 122 HCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAE 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2860 LRDFALPPGFKAL----CGGEALPENLATALLQKVTTLWNLYGPTETTIWSTL------NGLTTPTPYIGHPIANTQIYI 2929
Cdd:cd17649 202 EADRTGDGRPPSLrlyiFGGEALSPELLRRWLKAPVRLFNAYGPTEATVTPLVwkceagAARAGASMPIGRPLGGRSAYI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2930 LDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsGAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRG 3009
Cdd:cd17649 282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPF-GAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3010 FRIELGEIETRLARCHGVHDAVVIAReDSPGDKRLVAYLLAQPDTVLE--PADLRQRLSEGVAEYMIPSAFVTLDAFPLT 3087
Cdd:cd17649 361 FRIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPelRAQLRTALRASLPDYMVPAHLVFLARLPLT 439
|
490
....*....|.
gi 641744967 3088 PNGKLDRKALP 3098
Cdd:cd17649 440 PNGKLDRKALP 450
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
487-963 |
2.34e-150 |
|
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: 475.42 E-value: 2.34e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYIL 566
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 567 DDAAPVALLTQsaqvaqlnstlptvlldtpaaaacPDtnpvvqglhaaHLAYVIYTSGSTGRPKGVMVAHRNVINLATGL 646
Cdd:cd17650 81 EDSGAKLLLTQ------------------------PE-----------DLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 647 HTLLALDH-PSRIALNASIVFDASVKNWIQ-LLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLG 724
Cdd:cd17650 126 RREYELDSfPVRLLQMASFSFDVFAGDFARsLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 725 SDPAYQPAQVLIGGEAISPAVWSRLQS---LSDTRFINVYGPTECTVDATACVVDRTqPLPT-----IGKPLANTRLYIL 796
Cdd:cd17650 206 NGLDLSAMRLLIVGSDGCKAQDFKTLAarfGQGMRIINSYGVTEATIDSTYYEEGRD-PLGDsanvpIGRPLPNTAMYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 797 DAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSadPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGF 876
Cdd:cd17650 285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFA--PGERMYRTGDLARWRADGNVELLGRVDHQVKIRGF 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 877 RIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCarPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNG 956
Cdd:cd17650 363 RIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV--AAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNG 440
|
....*..
gi 641744967 957 KLDRKAL 963
Cdd:cd17650 441 KVDRRAL 447
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1542-2021 |
6.96e-149 |
|
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: 472.53 E-value: 6.96e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1542 PDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYML 1621
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1622 DDASPVALLTQANQrALLTGDVPRILLDTADFSHLSEDNPHVPgLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWM 1701
Cdd:cd12114 81 ADAGARLVLTDGPD-AQLDVAVFDVLILDLDALAAPAPPPPVD-VAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWA-DA 1780
Cdd:cd12114 159 NRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLeAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1781 DCACDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWACQP-DDHRSFVPIGRPIANTQLYILDTLG 1858
Cdd:cd12114 239 QALLPSLRLVLLSGDWIPLDLPARLRALApDARLISLGGATEASIWSIYHPIDEvPPDWRSIPYGRPLANQRYRVLDPRG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1859 QPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPfinqPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIEL 1938
Cdd:cd12114 319 RDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP----DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1939 GEIEARLMQCPGVQEAVVVAReDSPGDTRLVAYLCPQPGVTPD-PADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLD 2017
Cdd:cd12114 395 GEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPIaPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVD 473
|
....
gi 641744967 2018 RKAL 2021
Cdd:cd12114 474 RAAL 477
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1531-2022 |
3.22e-147 |
|
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: 466.26 E-value: 3.22e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1531 HQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDP 1610
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1611 GYPAERLAYMLDDASPVALLTQANQralltgdvprilldtadfshlsednphvpgldahhLAYVIYTSGSTGKPKGVMNS 1690
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTNPDD-----------------------------------LAYVIYTSGSTGLPKGVMIE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1691 HRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITtLHFVPSM 1770
Cdd:cd17645 126 HHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT-ISFLPTG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1771 L-QQFVQWADAdcacdSLRRVICSGEALpaelqqRFFARFNAQLHNLYGPTEAAIDVTFWACQPDDHRsfVPIGRPIANT 1849
Cdd:cd17645 205 AaEQFMQLDNQ-----SLRVLLTGGDKL------KKIERKGYKLVNNYGPTENTVVATSFEIDKPYAN--IPIGKPIDNT 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1850 QLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFInqPGARLYKTGDLARWLPDGSLEYLGRNDFQV 1929
Cdd:cd17645 272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFV--PGERMYRTGDLAKFLPDGNIEFLGRLDQQV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1930 KLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVtpDPADLRQQLGQHLAEYMVPGAFVTLDAFP 2009
Cdd:cd17645 350 KIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEI--PHEELREWLKNDLPDYMIPTYFVHLKALP 427
|
490
....*....|...
gi 641744967 2010 LTPNGKLDRKALP 2022
Cdd:cd17645 428 LTANGKVDRKALP 440
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1542-2021 |
8.02e-146 |
|
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: 462.71 E-value: 8.02e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1542 PDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYML 1621
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1622 DDASPVALLTQanqralltgdvprilldtadfshlsednphvPGldahHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWM 1701
Cdd:cd17650 81 EDSGAKLLLTQ-------------------------------PE----DLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLTPDD-RVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSM---LQQFVQW 1777
Cdd:cd17650 126 RREYELDSFPvRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALirpVMAYVYR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1778 ADADCacDSLRRVICSGEALPAELQQRFFARFNAQLH--NLYGPTEAAIDVTFW--ACQPDDHRSFVPIGRPIANTQLYI 1853
Cdd:cd17650 206 NGLDL--SAMRLLIVGSDGCKAQDFKTLAARFGQGMRiiNSYGVTEATIDSTYYeeGRDPLGDSANVPIGRPLPNTAMYV 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1854 LDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRG 1933
Cdd:cd17650 284 LDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF--APGERMYRTGDLARWRADGNVELLGRVDHQVKIRG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1934 FRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPgvTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPN 2013
Cdd:cd17650 362 FRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAA--TLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPN 439
|
....*...
gi 641744967 2014 GKLDRKAL 2021
Cdd:cd17650 440 GKVDRRAL 447
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1530-2021 |
1.68e-142 |
|
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: 454.31 E-value: 1.68e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLD 1609
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1610 PGYPAERLAYMLDDASPVALLTqanqralltgdvprilldtadfshlsednphvpgLDAHHLAYVIYTSGSTGKPKGVMN 1689
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLT----------------------------------SSPSDAAYVIFTSGSTGKPKGVVI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1690 SHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAayLAQLIERTGITTLHFVPS 1769
Cdd:cd05918 127 EHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLND--LAGFINRLRVTWAFLTPS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1770 MLQQfVQWADadcaCDSLRRVICSGEALPAELQQRFFARfnAQLHNLYGPTEAAIDVTFWACQPDDHRSFvpIGRPIANT 1849
Cdd:cd05918 205 VARL-LDPED----VPSLRTLVLGGEALTQSDVDTWADR--VRLINAYGPAECTIAATVSPVVPSTDPRN--IGRPLGAT 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1850 qLYILD--TLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDP-----FINQPGARLYKTGDLARWLPDGSLEYL 1922
Cdd:cd05918 276 -CWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqEGSGRGRRLYRTGDLVRYNPDGSLEYV 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1923 GRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVA---REDSPGDTRLVAYLCPQPGVT-----------------PDP 1982
Cdd:cd05918 355 GRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEvvkPKDGSSSPQLVAFVVLDGSSSgsgdgdslflepsdefrALV 434
|
490 500 510
....*....|....*....|....*....|....*....
gi 641744967 1983 ADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05918 435 AELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
487-964 |
4.80e-142 |
|
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: 451.85 E-value: 4.80e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQHLTYRELNRRANQLAHHLIALG-VQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYI 565
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 566 LDDAAPVALLTQSAQvaqlnstlptvlldtpaaaacpdtnpvvqglhaahLAYVIYTSGSTGRPKGVMVAHRNVINLATG 645
Cdd:cd17648 81 LEDTGARVVITNSTD-----------------------------------LAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 646 LHTLLALDHPS--RIALNASIVFDASVKNW-IQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQwLLDag 722
Cdd:cd17648 126 LSERYFGRDNGdeAVLFFSNYVFDFFVEQMtLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQ-QYD-- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 723 LGSDPAYQpaQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDAtacvVDRTQPLP-----TIGKPLANTRLYILD 797
Cdd:cd17648 203 LARLPHLK--RVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTN----HKRFFPGDqrfdkSLGRPVRNTKCYVLN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 798 AQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSADPA------ARIYKTGDLARWLPDGNIDYLGRNDFQI 871
Cdd:cd17648 277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQErargrnARLYKTGDLVRWLPSGELEYLGRNDFQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 872 KVRGFRIEAGEIESRLLRCPGVQDAVVIARED-----SPGDTRLVAYLCarPDAELHPAA-LRQQLAASLADYMIPSAFV 945
Cdd:cd17648 357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqSRIQKYLVGYYL--PEPGHVPESdLLSFLRAKLPRYMVPARLV 434
|
490
....*....|....*....
gi 641744967 946 TLDALPLTPNGKLDRKALP 964
Cdd:cd17648 435 RLEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
486-964 |
5.40e-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: 450.00 E-value: 5.40e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 486 TPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYI 565
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 566 LDDAAPVALLTQSAQVAQLNSTLPTVLLDTPAAAACPDTNpVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATG 645
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSN-IDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 646 LHTLLALDHPSRIALNASIVFDASVKNWIQ-LLSGHTLVLVPDALRADAHQLWRYFARHAVDLFdCTPVQLQWLL--DAG 722
Cdd:cd17656 160 EREKTNINFSDKVLQFATCSFDVCYQEIFStLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVV-FLPVAFLKFIfsERE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 723 LGSDPAYQPAQVLIGGEAIspAVWSRLQSLSDTRFI---NVYGPTECTVdATACVVDRTQP---LPTIGKPLANTRLYIL 796
Cdd:cd17656 239 FINRFPTCVKHIITAGEQL--VITNEFKEMLHEHNVhlhNHYGPSETHV-VTTYTINPEAEipeLPPIGKPISNTWIYIL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 797 DAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsaDPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGF 876
Cdd:cd17656 316 DQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF--DPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGY 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 877 RIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCarPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNG 956
Cdd:cd17656 394 RIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNG 471
|
....*...
gi 641744967 957 KLDRKALP 964
Cdd:cd17656 472 KVDRKALP 479
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1542-2022 |
5.24e-140 |
|
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: 446.08 E-value: 5.24e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1542 PDTTAVLFEDQHLTYDALNRRANQLAHHLIDLG-VKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYM 1620
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1621 LDDaspvallTQAnqRALLTGdvprilldtadfshlSEDnphvpgldahhLAYVIYTSGSTGKPKGVMNSHRALCNRLVW 1700
Cdd:cd17648 81 LED-------TGA--RVVITN---------------STD-----------LAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1701 MQNTY--RLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFvqwa 1778
Cdd:cd17648 126 LSERYfgRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQY---- 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1779 daDCA-CDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAID--VTFWacqPDDHRSFVPIGRPIANTQLYILD 1855
Cdd:cd17648 202 --DLArLPHLKRVDAAGEEFTAPVFEKLRSRFAGLIINAYGPTETTVTnhKRFF---PGDQRFDKSLGRPVRNTKCYVLN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1856 TLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFIN----QPG--ARLYKTGDLARWLPDGSLEYLGRNDFQV 1929
Cdd:cd17648 277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTeqerARGrnARLYKTGDLVRWLPSGELEYLGRNDFQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1930 KLRGFRIELGEIEARLMQCPGVQEAVVVARED-----SPGDTRLVAYLCPQPGVTPDpADLRQQLGQHLAEYMVPGAFVT 2004
Cdd:cd17648 357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqSRIQKYLVGYYLPEPGHVPE-SDLLSFLRAKLPRYMVPARLVR 435
|
490
....*....|....*...
gi 641744967 2005 LDAFPLTPNGKLDRKALP 2022
Cdd:cd17648 436 LEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
476-964 |
3.71e-139 |
|
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: 443.15 E-value: 3.71e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 476 QQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDP 555
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 556 AYPAERLAYILDDAAPVALLTQSAQvaqlnstlptvlldtpaaaacpdtnpvvqglhaahLAYVIYTSGSTGRPKGVMVA 635
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTNPDD-----------------------------------LAYVIYTSGSTGLPKGVMIE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 636 HRNVINLATGLHTLLALDHPSRIALNASIVFDASVKN-WIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDL-FDCTPV 713
Cdd:cd17645 126 HHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEiFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITIsFLPTGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 714 QLQWL-LDAglgsdpayQPAQVLI-GGEAISPAVWSRLQslsdtrFINVYGPTECTVDATACVVDRTQPLPTIGKPLANT 791
Cdd:cd17645 206 AEQFMqLDN--------QSLRVLLtGGDKLKKIERKGYK------LVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNT 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 792 RLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSadPAARIYKTGDLARWLPDGNIDYLGRNDFQI 871
Cdd:cd17645 272 RVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFV--PGERMYRTGDLAKFLPDGNIEFLGRLDQQV 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 872 KVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAElhPAALRQQLAASLADYMIPSAFVTLDALP 951
Cdd:cd17645 350 KIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIP--HEELREWLKNDLPDYMIPTYFVHLKALP 427
|
490
....*....|...
gi 641744967 952 LTPNGKLDRKALP 964
Cdd:cd17645 428 LTANGKVDRKALP 440
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
2619-3098 |
2.10e-138 |
|
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: 442.68 E-value: 2.10e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2619 TPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYM 2698
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2699 LDDAKPVALISQsAHLGIM---NGSLpVILLDDGETRPFDNEPDTPLDArkqgltpRHLAYVIYTSGSTGKPKGVMVEHA 2775
Cdd:cd17656 81 MLDSGVRVVLTQ-RHLKSKlsfNKST-ILLEDPSISQEDTSNIDYINNS-------DDLLYIIYTSGTTGKPKGVQLEHK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2776 NMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWR 2855
Cdd:cd17656 152 NMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2856 MLVELRDFA--LPPGFK-ALCGGEALPEN--LATALLQKVTTLWNLYGPTETTIWSTLN---GLTTPT-PYIGHPIANTQ 2926
Cdd:cd17656 232 FIFSEREFInrFPTCVKhIITAGEQLVITneFKEMLHEHNVHLHNHYGPSETHVVTTYTinpEAEIPElPPIGKPISNTW 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2927 IYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSgaPEARMYKTGDLGRWLPDGTLEYLGRNDFQVK 3006
Cdd:cd17656 312 IYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFD--PNERMYRTGDLARYLPDGNIEFLGRADHQVK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3007 VRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLaqPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPL 3086
Cdd:cd17656 390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFV--MEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPL 467
|
490
....*....|..
gi 641744967 3087 TPNGKLDRKALP 3098
Cdd:cd17656 468 TPNGKVDRKALP 479
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
487-963 |
2.87e-136 |
|
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: 436.32 E-value: 2.87e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYIL 566
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 567 DDAAPVALLTQSAQVAQLNSTLPTVLLDTPAAAACPDTNPVVQGLHAahLAYVIYTSGSTGRPKGVMVAHRNVINLATGL 646
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDD--LAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 647 HTLLALDHPSRIALNASIVFDASVKNWIQLLS-GHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGS 725
Cdd:cd12114 159 NRRFAVGPDDRVLALSSLSFDLSVYDIFGALSaGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 726 DPAYQP-AQVLIGGEAISPAVWSRLQSL-SDTRFINVYGPTECTVDATACVVDRTQP-LPTI--GKPLANTRLYILDAQD 800
Cdd:cd12114 239 QALLPSlRLVLLSGDWIPLDLPARLRALaPDARLISLGGATEASIWSIYHPIDEVPPdWRSIpyGRPLANQRYRVLDPRG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 801 QPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPfsadPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEA 880
Cdd:cd12114 319 RDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP----DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIEL 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 881 GEIESRLLRCPGVQDAVVIAReDSPGDTRLVAYLCARPDA-ELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLD 959
Cdd:cd12114 395 GEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGtPIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVD 473
|
....
gi 641744967 960 RKAL 963
Cdd:cd12114 474 RAAL 477
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
2620-3097 |
1.33e-134 |
|
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: 430.35 E-value: 1.33e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAkpvalisqsahlgimngSLPVILLDdgetrpfdnepdtpldarkqgltPRHLAYVIYTSGSTGKPKGVMVEHANMVN 2779
Cdd:cd17650 81 EDS-----------------GAKLLLTQ-----------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAH 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2780 FLCSMRKEPGIAQEDV-LLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLV 2858
Cdd:cd17650 121 AAHAWRREYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVM 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2859 EL--RDFALPPGFKALCGGEAL-----PENLATALLQKvTTLWNLYGPTETTIWSTL---------NGLTTPtpyIGHPI 2922
Cdd:cd17650 201 AYvyRNGLDLSAMRLLIVGSDGckaqdFKTLAARFGQG-MRIINSYGVTEATIDSTYyeegrdplgDSANVP---IGRPL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2923 ANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgAPEARMYKTGDLGRWLPDGTLEYLGRND 3002
Cdd:cd17650 277 PNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPF--APGERMYRTGDLARWRADGNVELLGRVD 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3003 FQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLaqPDTVLEPADLRQRLSEGVAEYMIPSAFVTLD 3082
Cdd:cd17650 355 HQVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVV--AAATLNTAELRAFLAKELPSYMIPSYYVQLD 432
|
490
....*....|....*
gi 641744967 3083 AFPLTPNGKLDRKAL 3097
Cdd:cd17650 433 ALPLTPNGKVDRRAL 447
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1530-2023 |
1.91e-133 |
|
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: 426.92 E-value: 1.91e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLD 1609
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1610 PGYPAERLAYMLDDASPVALLTqanqralltgdvprilldtadfshlsednphvpgldahhlAYVIYTSGSTGKPKGVMN 1689
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVML 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1690 SHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVS-VWEFFWPLLYGARLVMARpdgHKDAAYLAQLIERTGITTLHFVP 1768
Cdd:COG0318 121 THRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1769 SMLQQFVQWADADCAC-DSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTfwaCQPDDH--RSFVPIGRP 1845
Cdd:COG0318 198 TMLARLLRHPEFARYDlSSLRLVVSGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVT---VNPEDPgeRRPGSVGRP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1846 IANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFiPDPFinqpgarlYKTGDLARWLPDGSLEYLGRN 1925
Cdd:COG0318 275 LPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW--------LRTGDLGRLDEDGYLYIVGRK 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1926 DFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTL 2005
Cdd:COG0318 346 KDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFV 425
|
490
....*....|....*...
gi 641744967 2006 DAFPLTPNGKLDRKALPA 2023
Cdd:COG0318 426 DELPRTASGKIDRRALRE 443
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
2620-3098 |
3.44e-133 |
|
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: 426.43 E-value: 3.44e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFG-VRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYM 2698
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2699 LDDAKPVALISqsahlgimngslpvillddgetrpfdnepdtpldarkqglTPRHLAYVIYTSGSTGKPKGVMVEHANMV 2778
Cdd:cd17648 81 LEDTGARVVIT----------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2779 NFLCSMRKEPGIAQED--VLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPStwrm 2856
Cdd:cd17648 121 NLRTSLSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPS---- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2857 LVELRDFALPPGFK-ALCGGEALPENLATALLQKVTTL-WNLYGPTETTIWSTLNGLTTPTPY---IGHPIANTQIYILD 2931
Cdd:cd17648 197 VLQQYDLARLPHLKrVDAAGEEFTAPVFEKLRSRFAGLiINAYGPTETTVTNHKRFFPGDQRFdksLGRPVRNTKCYVLN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2932 AQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSGAPE------ARMYKTGDLGRWLPDGTLEYLGRNDFQV 3005
Cdd:cd17648 277 DAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQErargrnARLYKTGDLVRWLPSGELEYLGRNDFQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3006 KVRGFRIELGEIETRLARCHGVHDAVVIARED-----SPGDKRLVAYLLAQPDTVLEpADLRQRLSEGVAEYMIPSAFVT 3080
Cdd:cd17648 357 KIRGQRIEPGEVEAALASYPGVRECAVVAKEDasqaqSRIQKYLVGYYLPEPGHVPE-SDLLSFLRAKLPRYMVPARLVR 435
|
490
....*....|....*...
gi 641744967 3081 LDAFPLTPNGKLDRKALP 3098
Cdd:cd17648 436 LEGIPVTINGKLDVRALP 453
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1538-2021 |
6.14e-133 |
|
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: 425.51 E-value: 6.14e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERL 1617
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1618 AYMLDDASPVALLTqanqralltgdvprilldtadfshlsednphvpglDAHHLAYVIYTSGSTGKPKGVMNSHRALCNR 1697
Cdd:cd05945 81 REILDAAKPALLIA-----------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1698 LVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQ-FVQ 1776
Cdd:cd05945 126 TNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAAMcLLS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1777 WADADCACDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWACQPDDHRSF--VPIGRPIANTQLYI 1853
Cdd:cd05945 206 PTFTPESLPSLRHFLFCGEVLPHKTARALQQRFpDARIYNTYGPTEATVAVTYIEVTPEVLDGYdrLPIGYAKPGAKLVI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1854 LDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPfinqpGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRG 1933
Cdd:cd05945 286 LDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-----GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1934 FRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVT-PDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTP 2012
Cdd:cd05945 361 YRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEaGLTKAIKAELAERLPPYMIPRRFVYLDELPLNA 440
|
....*....
gi 641744967 2013 NGKLDRKAL 2021
Cdd:cd05945 441 NGKIDRKAL 449
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
2608-3097 |
1.60e-131 |
|
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: 422.72 E-value: 1.60e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2608 IHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLD 2687
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2688 PTYPVERLRYMLDDAK-PVALISQsahlgimngslpvillddgetrpfdnepdtpldarkqgltPRHLAYVIYTSGSTGK 2766
Cdd:cd05918 81 PSHPLQRLQEILQDTGaKVVLTSS----------------------------------------PSDAAYVIFTSGSTGK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2767 PKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLamLIERHAVSF 2846
Cdd:cd05918 121 PKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLNDLAG--FINRLRVTW 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2847 MQATPSTWRMLvelrDFALPPGFKALC-GGEALPENLATALLQKVTtLWNLYGPTETTIWSTLN--GLTTPTPYIGHPIA 2923
Cdd:cd05918 199 AFLTPSVARLL----DPEDVPSLRTLVlGGEALTQSDVDTWADRVR-LINAYGPAECTIAATVSpvVPSTDPRNIGRPLG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2924 NTqIYILDAQ--GRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDP-----FSGAPEARMYKTGDLGRWLPDGTLE 2996
Cdd:cd05918 274 AT-CWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqEGSGRGRRLYRTGDLVRYNPDGSLE 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2997 YLGRNDFQVKVRGFRIELGEIETRLARC-HGVHDAVV--IAREDSPGDKRLVAYLLAQ-----------------PDTVL 3056
Cdd:cd05918 353 YVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVevVKPKDGSSSPQLVAFVVLDgsssgsgdgdslflepsDEFRA 432
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 641744967 3057 EPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05918 433 LVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1532-2021 |
1.96e-131 |
|
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: 420.56 E-value: 1.96e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1532 QLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPG 1611
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1612 YPAERLAYMLDDASPVALLTQANQralltgdvprilldtadfshlsednphvpgldaHHLAYVIYTSGSTGKPKGVMNSH 1691
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTTDSP---------------------------------DDLAYIIFTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1692 RALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDghkdaAYLAQLIerTGITTLHFVPSML 1771
Cdd:cd17653 128 RGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPS-----DPFAHVA--RTVDALMSTPSIL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1772 QQFvqwADADcaCDSLRRVICSGEALPAELQQRFfaRFNAQLHNLYGPTEAAIDVTFWACQPDDhrsFVPIGRPIANTQL 1851
Cdd:cd17653 201 STL---SPQD--FPNLKTIFLGGEAVPPSLLDRW--SPGRRLYNAYGPTECTISSTMTELLPGQ---PVTIGKPIPNSTC 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1852 YILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKL 1931
Cdd:cd17653 271 YILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF--WPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKV 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1932 RGFRIELGEIEARLMQ-CPGVQEAVVVAREDspgdtRLVAYLCPQpgvTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPL 2010
Cdd:cd17653 349 RGFRINLEEIEEVVLQsQPEVTQAAAIVVNG-----RLVAFVTPE---TVDVDGLRSELAKHLPSYAVPDRIIALDSFPL 420
|
490
....*....|.
gi 641744967 2011 TPNGKLDRKAL 2021
Cdd:cd17653 421 TANGKVDRKAL 431
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
475-963 |
2.24e-131 |
|
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: 422.34 E-value: 2.24e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 475 IQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMD 554
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 555 PAYPAERLAYILDDA-APVALltqsaqvaqlnstlptvlldtpaaAACPDtnpvvqglhaaHLAYVIYTSGSTGRPKGVM 633
Cdd:cd05918 81 PSHPLQRLQEILQDTgAKVVL------------------------TSSPS-----------DAAYVIFTSGSTGKPKGVV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 634 VAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKN-WIQLLSGHTLVLVPDALRADAhqLWRYFARHAVDLFDCTP 712
Cdd:cd05918 126 IEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEiFTTLAAGGCLCIPSEEDRLND--LAGFINRLRVTWAFLTP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 713 -VqlqwlldAGLgsdpaYQPAQV------LIGGEAISPAV---WSrlqslSDTRFINVYGPTECTVDATACVVDRTQPLP 782
Cdd:cd05918 204 sV-------ARL-----LDPEDVpslrtlVLGGEALTQSDvdtWA-----DRVRLINAYGPAECTIAATVSPVVPSTDPR 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 783 TIGKPLAnTRLYILDAQD--QPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDP-----FSADPAARIYKTGDLARW 855
Cdd:cd05918 267 NIGRPLG-ATCWVVDPDNhdRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqEGSGRGRRLYRTGDLVRY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 856 LPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVV---IAREDSPGDTRLVAYLCARPDAELHP-------- 924
Cdd:cd05918 346 NPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVvevVKPKDGSSSPQLVAFVVLDGSSSGSGdgdslfle 425
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 641744967 925 ---------AALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05918 426 psdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
1068-1477 |
2.01e-130 |
|
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: 417.44 E-value: 2.01e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1068 LPLSFSQQRLWFLAQLDpAASQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDtlGFSLS 1147
Cdd:cd19538 2 IPLSFAQRRLWFLHQLE-GPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEE--DEATP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1148 SHDLRKLDEAArttrVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALE 1227
Cdd:cd19538 79 KLEIKEVDEEE----LESEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1228 GSEANLPPLPVQYADYAVWQRQWLQGETLNDLR-----DYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAGQL 1302
Cdd:cd19538 155 GEAPELAPLPVQYADYALWQQELLGDESDPDSLiarqlAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELH 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1303 RRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQVR 1382
Cdd:cd19538 235 QQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1383 ERALDAYAHQALPFEQVVEILQPARSLSYSPIFQVMLSLNNTPAQALTLPDLTLSAVERPQHSTHFDLSLSLIE-----T 1457
Cdd:cd19538 315 ETNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFELREqyndgT 394
|
410 420
....*....|....*....|
gi 641744967 1458 ENGLNGGLVYATDLFDRETI 1477
Cdd:cd19538 395 PNGIEGFIEYRTDLFDHETI 414
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
2609-3098 |
9.16e-130 |
|
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: 416.19 E-value: 9.16e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2609 HELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDP 2688
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2689 TYPVERLRYMLDDAKPVALISQsahlgimngslpvillddgetrpfdnepdtpldarkqgltPRHLAYVIYTSGSTGKPK 2768
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLTN----------------------------------------PDDLAYVIYTSGSTGLPK 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2769 GVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVS--- 2845
Cdd:cd17645 121 GVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITisf 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2846 --------FMQATPSTWRMLvelrdfalppgfkaLCGGEALpenlaTALLQKVTTLWNLYGPTETTIWSTLNGLTTPTPY 2917
Cdd:cd17645 201 lptgaaeqFMQLDNQSLRVL--------------LTGGDKL-----KKIERKGYKLVNNYGPTENTVVATSFEIDKPYAN 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2918 --IGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgAPEARMYKTGDLGRWLPDGTL 2995
Cdd:cd17645 262 ipIGKPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF--VPGERMYRTGDLAKFLPDGNI 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2996 EYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLaqPDTVLEPADLRQRLSEGVAEYMIP 3075
Cdd:cd17645 340 EFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVT--APEEIPHEELREWLKNDLPDYMIP 417
|
490 500
....*....|....*....|...
gi 641744967 3076 SAFVTLDAFPLTPNGKLDRKALP 3098
Cdd:cd17645 418 TYFVHLKALPLTANGKVDRKALP 440
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
2620-3097 |
2.12e-128 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Streptoalloteichus tallysomycin biosynthesis genes; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions. This family includes the TLM biosynthetic gene cluster from Streptoalloteichus that consists of nine NRPS genes; the N-terminal module of TlmVI (NRPS-5) and the starter module of BlmVI (NRPS-5) are comprised of the acyl CoA ligase (AL) and acyl carrier protein (ACP)-like domains, which are thought to be involved in the biosynthesis of the beta-aminoalaninamide moiety.
Pssm-ID: 341279 [Multi-domain] Cd Length: 477 Bit Score: 413.59 E-value: 2.12e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAkpvalisqSAHLGIMNGSLPVILLDDGETRPFDNEPDTPLDAR-KQGLTPRHLAYVIYTSGSTGKPKGVMVEHANMV 2778
Cdd:cd12114 81 ADA--------GARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPpPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAAL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2779 NFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLV 2858
Cdd:cd12114 153 NTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2859 E-LRDF-ALPPGFKA-LCGGEALPENLATAL--LQKVTTLWNLYGPTETTIWSTLNGLTTPT------PYiGHPIANTQI 2927
Cdd:cd12114 233 DvLEAAqALLPSLRLvLLSGDWIPLDLPARLraLAPDARLISLGGATEASIWSIYHPIDEVPpdwrsiPY-GRPLANQRY 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2928 YILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPfsgaPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKV 3007
Cdd:cd12114 312 RVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP----DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3008 RGFRIELGEIETRLARCHGVHDAVVIAReDSPGDKRLVAYLLAQPD-TVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPL 3086
Cdd:cd12114 388 RGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDgTPIAPDALRAFLAQTLPAYMIPSRVIALEALPL 466
|
490
....*....|.
gi 641744967 3087 TPNGKLDRKAL 3097
Cdd:cd12114 467 TANGKVDRAAL 477
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1534-1932 |
8.64e-128 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 409.39 E-value: 8.64e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1534 VEDQAARTPDTTAVL-FEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGY 1612
Cdd:pfam00501 1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1613 PAERLAYMLDDASPVALLTQANQRA------------------LLTGDVPRILLDTADFSHLSEDNPHVPGLDAHHLAYV 1674
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLeellealgklevvklvlvLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1675 IYTSGSTGKPKGVMNSHRALCNRLVWMQNTY----RLTPDDRVLQKTPFSFDVSV-WEFFWPLLYGARLVMARPDGHKDA 1749
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1750 AYLAQLIERTGITTLHFVPSMLQQFVQ-WADADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTF 1828
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEaGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1829 WACQPDDHRSFVPIGRPIANTQLYILDTL-GQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDpfinqpgaRLYKT 1907
Cdd:pfam00501 321 PLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED--------GWYRT 392
|
410 420
....*....|....*....|....*
gi 641744967 1908 GDLARWLPDGSLEYLGRNDFQVKLR 1932
Cdd:pfam00501 393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
477-963 |
7.80e-125 |
|
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: 401.69 E-value: 7.80e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 477 QRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPA 556
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 557 YPAERLAYILDDAAPVALLTQSAqvaqlnstlptvlldtpaaaacPDTnpvvqglhaahLAYVIYTSGSTGRPKGVMVAH 636
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTTDS----------------------PDD-----------LAYIIFTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 637 RNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWIQLLS-GHTLVLvpdalrADAHQLWRYFARhAVDLFDCTPVQL 715
Cdd:cd17653 128 RGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCnGGTLVL------ADPSDPFAHVAR-TVDALMSTPSIL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 716 QWLldaglgsDPAYQPA--QVLIGGEAISPavwsrlqSLSDT-----RFINVYGPTECTVDATACVVDRTQPLpTIGKPL 788
Cdd:cd17653 201 STL-------SPQDFPNlkTIFLGGEAVPP-------SLLDRwspgrRLYNAYGPTECTISSTMTELLPGQPV-TIGKPI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 789 ANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsaDPAARIYKTGDLARWLPDGNIDYLGRND 868
Cdd:cd17653 266 PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF--WPGSRMYRTGDYGRWTEDGGLEFLGRED 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 869 FQIKVRGFRIEAGEIESRLLR-CPGVQDAVVIAREDspgdtRLVAYlcARPdAELHPAALRQQLAASLADYMIPSAFVTL 947
Cdd:cd17653 344 NQVKVRGFRINLEEIEEVVLQsQPEVTQAAAIVVNG-----RLVAF--VTP-ETVDVDGLRSELAKHLPSYAVPDRIIAL 415
|
490
....*....|....*.
gi 641744967 948 DALPLTPNGKLDRKAL 963
Cdd:cd17653 416 DSFPLTANGKVDRKAL 431
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1069-1512 |
9.36e-125 |
|
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: 402.10 E-value: 9.36e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1069 PLSFSQQRLWFLAQLDPAASqAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFT-SIDGQPAQQIDpDTLGFSLS 1147
Cdd:pfam00668 6 PLSPAQKRMWFLEKLEPHSS-AYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQVIL-EERPFELE 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1148 SHDLRKLDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALE 1227
Cdd:pfam00668 84 IIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1228 GSEANLPPLPvQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRLHA 1307
Cdd:pfam00668 164 GEPLPLPPKT-PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1308 LNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQVRERALD 1387
Cdd:pfam00668 243 LAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQEDLLS 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1388 AYAHQALPFEQVVEILQPARSLSYSPIFQVMLSLNNTPAQ-----ALTLPDLTLSAVERPQHSTHFDLSLSLIETENGLN 1462
Cdd:pfam00668 323 AEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQdsqeeEFQLSELDLSVSSVIEEEAKYDLSLTASERGGGLT 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 641744967 1463 GGLVYATDLFDRETILRVVGYVENILMAMADDVTQPVATLPILPDSERRQ 1512
Cdd:pfam00668 403 IKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQK 452
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
2616-3097 |
1.65e-122 |
|
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: 395.46 E-value: 1.65e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2616 VACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERL 2695
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2696 RYMLDDAKPVALISqsahlgimngslpvillddgetrpfdnepdtpldarkqglTPRHLAYVIYTSGSTGKPKGVMVEHA 2775
Cdd:cd05945 81 REILDAAKPALLIA----------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHD 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2776 NMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWR 2855
Cdd:cd05945 121 NLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPSFAA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2856 MLVELRDFAlPPGFKAL-----CgGEALPENLATALLQKV--TTLWNLYGPTETTIWSTLNGLT-------TPTPyIGHP 2921
Cdd:cd05945 201 MCLLSPTFT-PESLPSLrhflfC-GEVLPHKTARALQQRFpdARIYNTYGPTEATVAVTYIEVTpevldgyDRLP-IGYA 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2922 IANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSGApearmYKTGDLGRWLPDGTLEYLGRN 3001
Cdd:cd05945 278 KPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRA-----YRTGDLVRLEADGLLFYRGRL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3002 DFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQP-DTVLEPADLRQRLSEGVAEYMIPSAFVT 3080
Cdd:cd05945 353 DFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPgAEAGLTKAIKAELAERLPPYMIPRRFVY 432
|
490
....*....|....*..
gi 641744967 3081 LDAFPLTPNGKLDRKAL 3097
Cdd:cd05945 433 LDELPLNANGKIDRKAL 449
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
483-963 |
2.99e-121 |
|
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: 392.00 E-value: 2.99e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERL 562
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 563 AYILDDAAPVALLTQsaqvaqlnstlptvlldtpaaaacPDTNpvvqglhaahlAYVIYTSGSTGRPKGVMVAHRNVINL 642
Cdd:cd05945 81 REILDAAKPALLIAD------------------------GDDN-----------AYIIFTSGSTGRPKGVQISHDNLVSF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 643 ATGLHTLLALDHPSRIALNASIVFDASVKNWI-QLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTP--VQLQwLL 719
Cdd:cd05945 126 TNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYpALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPsfAAMC-LL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 720 DAGLgsDPAYQPA--QVLIGGEAISPAVWSRLQS-LSDTRFINVYGPTECTVDATACVVDRTQ-----PLPtIGKPLANT 791
Cdd:cd05945 205 SPTF--TPESLPSlrHFLFCGEVLPHKTARALQQrFPDARIYNTYGPTEATVAVTYIEVTPEVldgydRLP-IGYAKPGA 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 792 RLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPfsadpAARIYKTGDLARWLPDGNIDYLGRNDFQI 871
Cdd:cd05945 282 KLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE-----GQRAYRTGDLVRLEADGLLFYRGRLDFQV 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 872 KVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAE-LHPAALRQQLAASLADYMIPSAFVTLDAL 950
Cdd:cd05945 357 KLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEaGLTKAIKAELAERLPPYMIPRRFVYLDEL 436
|
490
....*....|...
gi 641744967 951 PLTPNGKLDRKAL 963
Cdd:cd05945 437 PLNANGKIDRKAL 449
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
475-965 |
6.25e-121 |
|
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: 391.10 E-value: 6.25e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 475 IQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMD 554
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 555 PAYPAERLAYILDDAAPVALLTqsaqvaqlnstlptvlldtpaaaacpdtnpvvqglhaahlAYVIYTSGSTGRPKGVMV 634
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVML 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 635 AHRNVINLATGLHTLLALDHPSRIALNASIVFDA--SVKNWIQLLSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTP 712
Cdd:COG0318 121 THRNLLANAAAIAAALGLTPGDVVLVALPLFHVFglTVGLLAPLLAGATLVLLP---RFDPERVLELIERERVTVLFGVP 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 713 VQLQWLLDAGLGSDPAYQPAQVLI-GGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVD-RTQPLPTIGKPLAN 790
Cdd:COG0318 198 TMLARLLRHPEFARYDLSSLRLVVsGGAPLPPELLERFEERFGVRIVEGYGLTETSPVVTVNPEDpGERRPGSVGRPLPG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 791 TRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFiPDPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQ 870
Cdd:COG0318 278 VEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW--------LRTGDLGRLDEDGYLYIVGRKKDM 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 871 IKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDAL 950
Cdd:COG0318 349 IISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVEFVDEL 428
|
490
....*....|....*
gi 641744967 951 PLTPNGKLDRKALPA 965
Cdd:COG0318 429 PRTASGKIDRRALRE 443
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
479-874 |
7.11e-119 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 383.59 E-value: 7.11e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 479 FEAQAEQTPEAIAVL-FEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAY 557
Cdd:pfam00501 1 LERQAARTPDKTALEvGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 558 PAERLAYILDDAAPVALLTQSAQVAQ--------LNSTLPTVLLDTPA----------AAACPDTNPVVQGLHAAHLAYV 619
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEellealgkLEVVKLVLVLDRDPvlkeeplpeeAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 620 IYTSGSTGRPKGVMVAHRNVINLATGL----HTLLALDHPSRIALNASIVFDASVKN--WIQLLSGHTLVLVPDALRADA 693
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLglLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 694 HQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQ-VLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATA 772
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLRlVLSGGAPLPPELARRFRELFGGALVNGYGLTETTGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 773 CV--VDRTQPLPTIGKPLANTRLYILDAQD-QPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKT 849
Cdd:pfam00501 321 PLplDEDLRSLGSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGW--------YRT 392
|
410 420
....*....|....*....|....*
gi 641744967 850 GDLARWLPDGNIDYLGRNDFQIKVR 874
Cdd:pfam00501 393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
2610-3097 |
6.60e-117 |
|
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: 378.58 E-value: 6.60e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2610 ELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPT 2689
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2690 YPVERLRYMLDDAKPVALISQSAhlgimngslpvillddgetrpfdnepdtpldarkqgltPRHLAYVIYTSGSTGKPKG 2769
Cdd:cd17653 81 LPSARIQAILRTSGATLLLTTDS--------------------------------------PDDLAYIIFTSGSTGIPKG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2770 VMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAmlierhaVSFMQA 2849
Cdd:cd17653 123 VMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVART-------VDALMS 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2850 TPStwrMLVELRDFALPPGFKALCGGEALPENLATALLqKVTTLWNLYGPTETTIWSTLNGLTTPTP-YIGHPIANTQIY 2928
Cdd:cd17653 196 TPS---ILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWS-PGRRLYNAYGPTECTISSTMTELLPGQPvTIGKPIPNSTCY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2929 ILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSgaPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVR 3008
Cdd:cd17653 272 ILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFW--PGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVR 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3009 GFRIELGEIE-TRLARCHGVHDAVVIAREDspgdkRLVAylLAQPDTVLEpADLRQRLSEGVAEYMIPSAFVTLDAFPLT 3087
Cdd:cd17653 350 GFRINLEEIEeVVLQSQPEVTQAAAIVVNG-----RLVA--FVTPETVDV-DGLRSELAKHLPSYAVPDRIIALDSFPLT 421
|
490
....*....|
gi 641744967 3088 PNGKLDRKAL 3097
Cdd:cd17653 422 ANGKVDRKAL 431
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
2612-3008 |
2.46e-116 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 376.27 E-value: 2.46e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2612 FEAQVACTPDAIAVVFGE-ASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTY 2690
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2691 PVERLRYMLDDAKPVALISQSAHLGIMNGSL--------PVILLD-----DGETRPFDNEPDTPLDARKQGLTPRHLAYV 2757
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELLEAlgklevvkLVLVLDrdpvlKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2758 IYTSGSTGKPKGVMVEHANMVNFLCSMRKEP----GIAQEDVLLGVTSLSFDIS-ILEIFLPLLNGARLILATQAQAADA 2832
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRprgfGLGPDDRVLSTLPLFHDFGlSLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2833 QQLAMLIERHAVSFMQATPSTWRMLVELRDF--ALPPGFKA-LCGGEALPENLATALLQKV-TTLWNLYGPTETTIWST- 2907
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPkrALLSSLRLvLSGGAPLPPELARRFRELFgGALVNGYGLTETTGVVTt 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2908 ---LNGLTTPTPYIGHPIANTQIYILDAQ-GRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDpfsgapeaRMYKT 2983
Cdd:pfam00501 321 plpLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED--------GWYRT 392
|
410 420
....*....|....*....|....*
gi 641744967 2984 GDLGRWLPDGTLEYLGRNDFQVKVR 3008
Cdd:pfam00501 393 GDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
2608-3099 |
2.13e-113 |
|
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: 369.52 E-value: 2.13e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2608 IHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLD 2687
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2688 PTYPVERLRYMLDDAKPVALISqsahlgimngslpvillddgetrpfdnepdtpldarkqgltprhlAYVIYTSGSTGKP 2767
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2768 KGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDIS-ILEIFLPLLNGARLILATQAQAADAQQlamLIERHAVSF 2846
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGlTVGLLAPLLAGATLVLLPRFDPERVLE---LIERERVTV 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2847 MQATPSTWRMLVELRDFA---LPPGFKALCGGEALPENLATALLQKV-TTLWNLYGPTETTIWSTLNGLTTPTPY---IG 2919
Cdd:COG0318 193 LFGVPTMLARLLRHPEFArydLSSLRLVVSGGAPLPPELLERFEERFgVRIVEGYGLTETSPVVTVNPEDPGERRpgsVG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2920 HPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFitdpfsgapEARMYKTGDLGRWLPDGTLEYLG 2999
Cdd:COG0318 273 RPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF---------RDGWLRTGDLGRLDEDGYLYIVG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3000 RNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFV 3079
Cdd:COG0318 344 RKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEELRAFLRERLARYKVPRRVE 423
|
490 500
....*....|....*....|
gi 641744967 3080 TLDAFPLTPNGKLDRKALPA 3099
Cdd:COG0318 424 FVDELPRTASGKIDRRALRE 443
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
2161-2569 |
1.38e-109 |
|
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: 357.14 E-value: 1.38e-109
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2161 IYPLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCWQDLSQPVQVVWRQAILPIN 2240
Cdd:cd19536 1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2241 HFEPTSPEDVLAQLQAHTE-PRTRRIDLSQAPLFRADIAHDPLQNEWLLALSFHHLISDHMTLALIVGEIRLLLQHQAD- 2318
Cdd:cd19536 81 ELDLTPLEEQLDPLRAYKEeTKIRRFDLGRAPLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEy 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2319 ---ALPTPLPYRNFIAQTL-SVPNSAHEAYFRDKLADVDEPTAPFGLLNVQGsgGDIHEARLVLDATLASAIRQQARHLG 2394
Cdd:cd19536 161 kplSLPPAQPYRDFVAHERaSIQQAASERYWREYLAGATLATLPALSEAVGG--GPEQDSELLVSVPLPVRSRSLAKRSG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2395 VSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRLAGAEGADRIMGMFINTLPLRISLADRGAAEVVERTSHDLMTLLEHE 2474
Cdd:cd19536 239 IPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLSEETVEDLLKRAQEQELESLSHE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2475 QAPLALAQRCSgvaPPMPLFSTLLNYRH-----TQASSTDNTLSDIRVLTSEERTNYPLTLAVDDR-GEGFSLVA---QT 2545
Cdd:cd19536 319 QVPLADIQRCS---EGEPLFDSIVNFRHfdldfGLPEWGSDEGMRRGLLFSEFKSNYDVNLSVLPKqDRLELKLAynsQV 395
|
410 420
....*....|....*....|....
gi 641744967 2546 LEDIDPHRLLNYLMTAISSLVDAL 2569
Cdd:cd19536 396 LDEEQAQRLAAYYKSAIAELATAP 419
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1069-1494 |
3.17e-107 |
|
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: 350.53 E-value: 3.17e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1069 PLSFSQQRLWFLAQLDPAaSQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSID-GQPAQQIDPDTlgfsls 1147
Cdd:cd19539 3 PLSFAQERLWFIDQGEDG-GPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPG------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1148 SHDLRKLDE----AARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQ 1223
Cdd:cd19539 76 PAPLEVRDLsdpdSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1224 AALEGSEANLPPLPVQYADYAVWQRQWLQGETLNDLRDYWRDQLQGApALLEIPTDRPRPSVQRYAGDQVPFHLDAGQLR 1303
Cdd:cd19539 156 ARRKGPAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGA-EPTALPTDRPRPAGFPYPGADLRFELDAELVA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1304 RLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQVRE 1383
Cdd:cd19539 235 ALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRK 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1384 RALDAYAHQALPFEQVVEILQPARSLSYSPIFQVMLSLNNTPAQALTLP-DLTLSAVERPQHSTHFDLSLSLIETENGLN 1462
Cdd:cd19539 315 ALVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAgGLSYTEGSDIPDGAKFDLNLTVTEEGTGLR 394
|
410 420 430
....*....|....*....|....*....|..
gi 641744967 1463 GGLVYATDLFDRETILRVVGYVENILMAMADD 1494
Cdd:cd19539 395 GSLGYATSLFDEETIQGFLADYLQVLRQLLAN 426
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
28-436 |
2.27e-104 |
|
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: 342.12 E-value: 2.27e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 28 IYPLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICWQGLHQPVQVVWRQAPLTVN 107
Cdd:cd19536 1 MYPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 108 TLTTTSSDTVPAQLRAATDPSNHR-LNLSNAPLLSATTAHDPVCGEWLLSLSIHHLISDHITQALIIDEIRL----LLED 182
Cdd:cd19536 81 ELDLTPLEEQLDPLRAYKEETKIRrFDLGRAPLVRAALVRKDERERFLLVISDHHSILDGWSLYLLVKEILAvynqLLEY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 183 RPEALPKPLPYRNFIAQILSVPLS-EHEQYFRNRLADIDTPTAPFdLVDVQGnGEDITEARLSLDSSLADALRRQARHLG 261
Cdd:cd19536 161 KPLSLPPAQPYRDFVAHERASIQQaASERYWREYLAGATLATLPA-LSEAVG-GGPEQDSELLVSVPLPVRSRSLAKRSG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 262 ISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQGNLGADRVMGMFINTLPLRVSLRERSVHDVVQATSHELMMLLAHE 341
Cdd:cd19536 239 IPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTLSEETVEDLLKRAQEQELESLSHE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 342 QAPLALAQQCSQVPpplPLFSTLFNYRHSQKDASSQFW-----EGMRQLSGRERTNYPITLSVDDLGD----GFNLTAKT 412
Cdd:cd19536 319 QVPLADIQRCSEGE---PLFDSIVNFRHFDLDFGLPEWgsdegMRRGLLFSEFKSNYDVNLSVLPKQDrlelKLAYNSQV 395
|
410 420
....*....|....*....|....
gi 641744967 413 VMGVDPERIVHYMLTAIENLVTSL 436
Cdd:cd19536 396 LDEEQAQRLAAYYKSAIAELATAP 419
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
1263-2106 |
3.58e-97 |
|
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: 347.44 E-value: 3.58e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1263 WRDQLQgAPALLEIPTDRPRPSVQRYAgdQVPFHLDAGQLRRLHAlnrqQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTP 1342
Cdd:TIGR03443 2 WSERLD-NPTLSVLPHDYLRPANNRLV--EATYSLQLPSAEVTAG----GGSTPFIILLAAFAALVYRLTGDEDIVLGTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1343 VANRPRQelegmvgffvntLALRTEPGRCHAVADLLDQVRERALDAYAHQALPFEQVVEILQPARSL-SYSPIFQVmlsl 1421
Cdd:TIGR03443 75 SNKSGRP------------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLeRTPPLFRL---- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1422 nntpaQALTLPDLTLSAVErpQHSThFDLSLSLIETENGLNGGLVYATDLFDRETILRVVGYVENILMAMADDVTQPVAT 1501
Cdd:TIGR03443 139 -----AFQDAPDNQQTTYS--TGST-TDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1502 LPILPDSERRqvMLDFNATEADFP-HDALIHQLVEDQAARTPDTTAVLFEDQHL---------TYDALNRRANQLAHHLI 1571
Cdd:TIGR03443 211 VSLITPSQKS--LLPDPTKDLDWSgFRGAIHDIFADNAEKHPDRTCVVETPSFLdpssktrsfTYKQINEASNILAHYLL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1572 DLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVAL--LTQANQRALLTGD------- 1642
Cdd:TIGR03443 289 KTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALivIEKAGTLDQLVRDyidkele 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1643 ----VPRI-LLDTADFSHLSEDNPHVPGLdAHHLAY------VI----------YTSGSTGKPKGVMNSHRALCNRLVWM 1701
Cdd:TIGR03443 369 lrteIPALaLQDDGSLVGGSLEGGETDVL-APYQALkdtptgVVvgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFPWM 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVqwADAD 1781
Cdd:TIGR03443 448 AKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLS--AQAT 525
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1782 CACDSLRRVICSGEALPAE----LQQrfFARfNAQLHNLYGPTEA------------AIDVTFWACQPDdhrsFVPIGRP 1845
Cdd:TIGR03443 526 TPIPSLHHAFFVGDILTKRdclrLQT--LAE-NVCIVNMYGTTETqravsyfeipsrSSDSTFLKNLKD----VMPAGKG 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1846 IANTQLYIL---DTlGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFI-----------NQPGA--------- 1902
Cdd:TIGR03443 599 MKNVQLLVVnrnDR-TQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVdpshwidldkeNNKPErefwlgprd 677
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1903 RLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPG----- 1977
Cdd:TIGR03443 678 RLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDKsdele 757
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1978 ---------VTPDPA------------DLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPAPDQ---SAVATRD 2033
Cdd:TIGR03443 758 efksevddeESSDPVvkglikyrklikDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTaqlAAVAKNR 837
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2034 Y----EAPQGEVETALAAVWQDLL--GLTRVGRHDHFFALGGHSLLIVSLIERLRRAgLALDVR--GVFSTPVLSDMAQA 2105
Cdd:TIGR03443 838 SasaaDEEFTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKK-LNVELPlgLIFKSPTIKGFAKE 916
|
.
gi 641744967 2106 I 2106
Cdd:TIGR03443 917 V 917
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1529-2021 |
6.17e-93 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 312.21 E-value: 6.17e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1529 LIHQLvEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLgvKPDDRIAICV--ERSLDMVIGLLAILKAGAAYV 1606
Cdd:PRK04813 4 IIETI-EEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSL--KLPDKSPIIVfgHMSPEMLATFLGAVKAGHAYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1607 PLDPGYPAERLAYMLDDASPVALLTQANQRALLTgDVPRILLD----------TADFSHlsednpHVPGLDAhhlAYVIY 1676
Cdd:PRK04813 81 PVDVSSPAERIEMIIEVAKPSLIIATEELPLEIL-GIPVITLDelkdifatgnPYDFDH------AVKGDDN---YYIIF 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1677 TSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLI 1756
Cdd:PRK04813 151 TSGTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1757 ERTGITTLHFVPSmlqqFVQWADADCACD-----SLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWA 1830
Cdd:PRK04813 231 PQLPINVWVSTPS----FADMCLLDPSFNeehlpNLTHFLFCGEELPHKTAKKLLERFpSATIYNTYGPTEATVAVTSIE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1831 CQPD--DHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPfinqpGARLYKTG 1908
Cdd:PRK04813 307 ITDEmlDQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTFD-----GQPAYHTG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1909 DLARwLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADL--- 1985
Cdd:PRK04813 382 DAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEEDFEREFELtka 460
|
490 500 510
....*....|....*....|....*....|....*..
gi 641744967 1986 -RQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK04813 461 iKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1067-1479 |
2.92e-89 |
|
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: 298.79 E-value: 2.92e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1067 PLPLSFSQQRLWFLAQL--DPAAsqaYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIdPDTLGF 1144
Cdd:cd20483 1 PRPMSTFQRRLWFLHNFleDKTF---LNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQV-LDDPSF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1145 SLSSHDLRklDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQA 1224
Cdd:cd20483 77 HLIVIDLS--EAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1225 ALEG-SEANLPPLPVQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAPA---LLEIPTdRPRPSVQRYAGDQVPFHLDAG 1300
Cdd:cd20483 155 LRAGrDLATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPDaskLLPFAK-AERPPVKDYERSTVEATLDKE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1301 QLRRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQ 1380
Cdd:cd20483 234 LLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1381 VRERALDAYAHQALPFEQVVEILQPARSLSYSPIFQVMLS--LNNTPAQALTlPDLTLSAVERPQHSTHFDLSLSLIET- 1457
Cdd:cd20483 314 TKTTCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNyqVHGKFPEYDT-GDFKFTDYDHYDIPTACDIALEAEEDp 392
|
410 420
....*....|....*....|..
gi 641744967 1458 ENGLNGGLVYATDLFDRETILR 1479
Cdd:cd20483 393 DGGLDLRLEFSTTLYDSADMER 414
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1067-1492 |
5.19e-88 |
|
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: 295.09 E-value: 5.19e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1067 PLPLSFSQQRLWFLAQLDPAASqAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDTLGFSL 1146
Cdd:cd19066 1 KIPLSPMQRGMWFLKKLATDPS-AFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1147 SSHDLRKLDEaaRTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAAL 1226
Cdd:cd19066 80 EIIDLRNLAD--PEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1227 EGSEAnLPPLPVQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRLH 1306
Cdd:cd19066 158 RQKPT-LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1307 ALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQVRERAL 1386
Cdd:cd19066 237 EVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1387 DAYAHQALPFEQVVEILQPARSLSYSPIFQVMLSLNNTPAQALTLPDLTLSAVE-RPQHSTHFDLSLSLIETENG-LNGG 1464
Cdd:cd19066 317 EAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVyTSSEGTVFDLDLEASEDPDGdLLLR 396
|
410 420
....*....|....*....|....*...
gi 641744967 1465 LVYATDLFDRETILRvvgYVENILMAMA 1492
Cdd:cd19066 397 LEYSRGVYDERTIDR---FAERYMTALR 421
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1070-1317 |
5.90e-88 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 287.71 E-value: 5.90e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1070 LSFSQQRLWFLAQldpaASQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDtLGFSLSSH 1149
Cdd:COG4908 1 LSPAQKRFLFLEP----GSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPD-ADLPLEVV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1150 DLRKLDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALEGS 1229
Cdd:COG4908 76 DLSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1230 EANLPPLPVQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRLHALN 1309
Cdd:COG4908 156 PPPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALA 235
|
....*...
gi 641744967 1310 RQQGTTLF 1317
Cdd:COG4908 236 KAHGATVN 243
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
473-963 |
2.21e-87 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 296.42 E-value: 2.21e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 473 MLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALgvQPDDRVALCV--ERSLEMMVGLLGILKAGAAY 550
Cdd:PRK04813 2 MDIIETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSL--KLPDKSPIIVfgHMSPEMLATFLGAVKAGHAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 551 VPMDPAYPAERLAYILDDAAPVALLTqsaqVAQLNSTL-------PTVLLDTPAAAACPDTNPVVQGlhaAHLAYVIYTS 623
Cdd:PRK04813 80 IPVDVSSPAERIEMIIEVAKPSLIIA----TEELPLEIlgipvitLDELKDIFATGNPYDFDHAVKG---DDNYYIIFTS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 624 GSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWI-QLLSGHTLVLVPDALRADAHQLWRYFAR 702
Cdd:PRK04813 153 GTTGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYpTLASGGTLVALPKDMTANFKQLFETLPQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 703 HAVDLFDCTP--VQLQwLLDAGLGSDPAYQPAQVLIGGEAISPAVWSRL-QSLSDTRFINVYGPTECTVDATAC-----V 774
Cdd:PRK04813 233 LPINVWVSTPsfADMC-LLDPSFNEEHLPNLTHFLFCGEELPHKTAKKLlERFPSATIYNTYGPTEATVAVTSIeitdeM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 775 VDRTQPLPtIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFipdpFSADpAARIYKTGDLAR 854
Cdd:PRK04813 312 LDQYKRLP-IGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFD-GQPAYHTGDAGY 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 855 wLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARP-----DAELhPAALRQ 929
Cdd:PRK04813 386 -LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPKEedferEFEL-TKAIKK 463
|
490 500 510
....*....|....*....|....*....|....
gi 641744967 930 QLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK04813 464 ELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
1529-2021 |
9.74e-86 |
|
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: 291.28 E-value: 9.74e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1529 LIHQLvEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPL 1608
Cdd:TIGR01734 2 LIEAI-QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1609 DPGYPAERLAYMLDDASPVALLTQANQRALLTgDVPRI---LLDTADFSHLSEDNPH-VPGLDAHhlaYVIYTSGSTGKP 1684
Cdd:TIGR01734 81 DTSIPSERIEMIIEAAGPELVIHTAELSIDAV-GTQIItlsALEQAETSGGPVSFDHaVKGDDNY---YIIYTSGSTGNP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1685 KGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTL 1764
Cdd:TIGR01734 157 KGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGLNVW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1765 HFVPSmlqqFVQWADADCACD-----SLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWACQPD--DH 1836
Cdd:TIGR01734 237 VSTPS----FVDMCLLDPNFNqenypHLTHFLFCGEELPVKTAKALLERFpKATIYNTYGPTEATVAVTSVKITQEilDQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1837 RSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDpfinqPGARLYKTGDLARwLPD 1916
Cdd:TIGR01734 313 YPRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH-----EGQPAYRTGDAGT-ITD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1917 GSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGD-TRLVAYLCPQPGVTPDPADL----RQQLGQ 1991
Cdd:TIGR01734 387 GQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAIVPETEDFEKEFQLtkaiKKELKK 466
|
490 500 510
....*....|....*....|....*....|
gi 641744967 1992 HLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:TIGR01734 467 SLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
2607-3097 |
2.32e-85 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 290.26 E-value: 2.32e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2607 LIHELFE-AQVacTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGvrPDERVAICVERGL--DMVVGLLGILKAGGAY 2683
Cdd:PRK04813 4 IIETIEEfAQT--QPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLK--LPDKSPIIVFGHMspEMLATFLGAVKAGHAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2684 VPLDPTYPVERLRYMLDDAKPVALISQSAhLGIMNGSLPVILLDDGETRPFDNEPDTPLDARKQGLTprhlAYVIYTSGS 2763
Cdd:PRK04813 80 IPVDVSSPAERIEMIIEVAKPSLIIATEE-LPLEILGIPVITLDELKDIFATGNPYDFDHAVKGDDN----YYIIFTSGT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2764 TGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHA 2843
Cdd:PRK04813 155 TGKPKGVQISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2844 VSFMQATPSTWRMLVELRDF--ALPPGFKA--LCGgEALPENLATALLQKV--TTLWNLYGPTETT-----IWSTLNGLT 2912
Cdd:PRK04813 235 INVWVSTPSFADMCLLDPSFneEHLPNLTHflFCG-EELPHKTAKKLLERFpsATIYNTYGPTEATvavtsIEITDEMLD 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2913 T--PTPyIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITdpFSGAPEarmYKTGDLGRwL 2990
Cdd:PRK04813 314 QykRLP-IGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT--FDGQPA---YHTGDAGY-L 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2991 PDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIaredsPGDK-----RLVAYLLAQPDTVLEPADL---- 3061
Cdd:PRK04813 387 EDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVV-----PYNKdhkvqYLIAYVVPKEEDFEREFELtkai 461
|
490 500 510
....*....|....*....|....*....|....*.
gi 641744967 3062 RQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK04813 462 KKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1068-1494 |
4.00e-84 |
|
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: 283.71 E-value: 4.00e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1068 LPLSFSQQRLWFLAQLDPAaSQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTS-IDGQPAQQIDPDtLGFSL 1146
Cdd:cd19543 2 YPLSPMQEGMLFHSLLDPG-SGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWeGLGEPLQVVLKD-RKLPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1147 SSHDLRKLDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAAL 1226
Cdd:cd19543 80 RELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1227 EGSEANLPPlPVQYADYAvwqrQWLQGETLNDLRDYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRLH 1306
Cdd:cd19543 160 EGQPPSLPP-VRPYRDYI----AWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1307 ALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPrQELEG---MVGFFVNTLALRTEPGRCHAVADLLDQVRE 1383
Cdd:cd19543 235 ELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRP-AELPGietMVGLFINTLPVRVRLDPDQTVLELLKDLQA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1384 RALDAYAHQALPFeqvVEIlQpARSLSYSPIFQVMLSLNNTP--AQALTLPD---LTLSAVERPQHsTHFDLSLSLIETE 1458
Cdd:cd19543 314 QQLELREHEYVPL---YEI-Q-AWSEGKQALFDHLLVFENYPvdESLEEEQDedgLRITDVSAEEQ-TNYPLTVVAIPGE 387
|
410 420 430
....*....|....*....|....*....|....*.
gi 641744967 1459 nGLNGGLVYATDLFDRETILRVVGYVENILMAMADD 1494
Cdd:cd19543 388 -ELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
2372-3180 |
1.13e-83 |
|
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: 305.07 E-value: 1.13e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2372 HEARLVlDATLASAIRQQARHL--GVSPGVLFHVAWAQVLAQTSGRDDVVFGSvllgrlAGAEGADRimgmFINTLPLRI 2449
Cdd:TIGR03443 22 ANNRLV-EATYSLQLPSAEVTAggGSTPFIILLAAFAALVYRLTGDEDIVLGT------SSNKSGRP----FVLRLNITP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2450 SLAdrgAAEVVERTSHDLMTLLEHEQAPLA-LA---QRCSGVAPPMPLFStlLNYRHTQASSTDN----TLSDIRVLTSE 2521
Cdd:TIGR03443 91 ELS---FLQLYAKVSEEEKEGASDIGVPFDeLSehiQAAKKLERTPPLFR--LAFQDAPDNQQTTystgSTTDLTVFLTP 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2522 ERTNYPLTLAVDDRGegFSlvaqtledidpHRLLNYLMTAISSLVDALETEPQRSILNLPVLPDSERQqMLVDfNATDAD 2601
Cdd:TIGR03443 166 SSPELELSIYYNSLL--FS-----------SDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKS-LLPD-PTKDLD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2602 IP--RHAlIHELFEAQVACTPDAIAVVFGEASL---------SYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMV 2670
Cdd:TIGR03443 231 WSgfRGA-IHDIFADNAEKHPDRTCVVETPSFLdpssktrsfTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLV 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2671 VGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALI--------SQSAHLGImNGSLPVI-------LLDDGET---R 2732
Cdd:TIGR03443 310 VAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIviekagtlDQLVRDYI-DKELELRteipalaLQDDGSLvggS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2733 PFDNEPDT--PLDARKQGLT-----PRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFD 2805
Cdd:TIGR03443 389 LEGGETDVlaPYQALKDTPTgvvvgPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHD 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2806 ISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVELRDFALPPGFKALCGGEALPENLATA 2885
Cdd:TIGR03443 469 PIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAMGQLLSAQATTPIPSLHHAFFVGDILTKRDCLR 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2886 L--LQKVTTLWNLYGPTET-------TIWST------LNGLTTPTPyIGHPIANTQIYILDAQGRVVPLGVA--GEIHIA 2948
Cdd:TIGR03443 549 LqtLAENVCIVNMYGTTETqravsyfEIPSRssdstfLKNLKDVMP-AGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVR 627
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2949 GAGVVRGYLGRPDLTAERFIT------------DPFSGAPEA--------RMYKTGDLGRWLPDGTLEYLGRNDFQVKVR 3008
Cdd:TIGR03443 628 AGGLAEGYLGLPELNAEKFVNnwfvdpshwidlDKENNKPERefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIR 707
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3009 GFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTV-LEPA-------------------------DLR 3062
Cdd:TIGR03443 708 GFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDKSDeLEEFksevddeessdpvvkglikyrklikDIR 787
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3063 QRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAPD--QSAMATRGYEAPQGD-----LEHALAQIWQTLL--GVER 3133
Cdd:TIGR03443 788 EYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDtaQLAAVAKNRSASAADeefteTEREIRDLWLELLpnRPAT 867
|
890 900 910 920
....*....|....*....|....*....|....*....|....*..
gi 641744967 3134 VGRHDHFFELGGHSLLAVQLNARIRAEFLTDIPIVAIFQHPQLSALA 3180
Cdd:TIGR03443 868 ISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGFA 914
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1670-2017 |
1.15e-83 |
|
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: 279.17 E-value: 1.15e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1670 HLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDghkDA 1749
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF---DP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1750 AYLAQLIERTGITTLHFVPSMLQQFV-QWADADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTF 1828
Cdd:cd04433 78 EAALELIEREKVTILLGVPTLLARLLkAPESAGYDLSSLRALVSGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1829 WaCQPDDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFipdpfinqpGARLYKTG 1908
Cdd:cd04433 158 G-PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD---------EDGWYRTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1909 DLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQ 1988
Cdd:cd04433 228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAH 307
|
330 340
....*....|....*....|....*....
gi 641744967 1989 LGQHLAEYMVPGAFVTLDAFPLTPNGKLD 2017
Cdd:cd04433 308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1531-2021 |
2.77e-82 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 283.54 E-value: 2.77e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1531 HQLVEDQAARTPDTTAVLFED-----QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAY 1605
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1606 VPLDPGYPAERLAYMLDDASPVALLTQAnqrALLTGDVPRILLDTAD--------------FSHLSEDnPHVPG------ 1665
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITAD---GGLRGGKVIDLKEKVDealeelpslehvivVGRTGAD-VPMEGdldwde 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1666 -------------LDAHHLAYVIYTSGSTGKPKGVMNSHRALcnrLVW----MQNTYRLTPDDRVLQKTPFSFDVSVW-E 1727
Cdd:COG0365 168 llaaasaefepepTDADDPLFILYTSGTTGKPKGVVHTHGGY---LVHaattAKYVLDLKPGDVFWCTADIGWATGHSyI 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1728 FFWPLLYGARLVM--ARPDgHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWAD---ADCACDSLRRVICSGEALPAELQ 1802
Cdd:COG0365 245 VYGPLLNGATVVLyeGRPD-FPDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDeplKKYDLSSLRLLGSAGEPLNPEVW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1803 QRFFARFNAQLHNLYGPTEA-AIDVTFWACQPddhrsFVP--IGRPIANTQLYILDTLGQPVPLGVAGELHIGG--VGVA 1877
Cdd:COG0365 324 EWWYEAVGVPIVDGWGQTETgGIFISNLPGLP-----VKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMF 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1878 RGYLNRPDLTAERFipdpFINQPGarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVV 1957
Cdd:COG0365 399 RGYWNDPERYRETY----FGRFPG--WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 1958 AREDSPGDTRLVAYLCPQPGVTPDPA---DLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:COG0365 473 GVPDEIRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
1064-1494 |
3.17e-82 |
|
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: 278.98 E-value: 3.17e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1064 RTQPLPLSFSQQRLWFLAQLDPAaSQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQI-DPDTL 1142
Cdd:cd19546 1 RPDEVPATAGQLRTWLLARLDEE-TRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIlDADAA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1143 GFSLsshdlrKLDEAARTTRVAELAEQEARaRFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALY 1222
Cdd:cd19546 80 RPEL------PVVPATEEELPALLADRAAH-LFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAY 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1223 QAALEGSEANLPPLPVQYADYAVWQRQWLQGET-----LNDLRDYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHL 1297
Cdd:cd19546 153 GARREGRAPERAPLPLQFADYALWERELLAGEDdrdslIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1298 DAGQLRRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQ-ELEGMVGFFVNTLALRTEPGRCHAVAD 1376
Cdd:cd19546 233 DAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTFRE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1377 LLDQVRERALDAYAHQALPFEQVVEILQPARSLSYSPIFQVMLSL---NNTPAQALTLPDLTLSAVERPQHSTHFDLSLS 1453
Cdd:cd19546 313 LLGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVrddDNDPWDAPELPGLRTSPVPLGTEAMELDLSLA 392
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 641744967 1454 LIETEN------GLNGGLVYATDLFDRETILRVVGYVENILMAMADD 1494
Cdd:cd19546 393 LTERRNddgdpdGLDGSLRYAADLFDRATAAALARRLVRVLEQVAAD 439
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
1529-2023 |
1.62e-81 |
|
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: 279.74 E-value: 1.62e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1529 LIHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPL 1608
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1609 DPGYPAERLAYMLDDASPVALLTQANQRALLTGDVP-----RILLDTADFSHLSEDNPH------------------VPG 1665
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPgchdlRTLIIVGDPAHASEGHPGeepaswpkllalgdadppHPV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1666 LDAHhLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDG 1745
Cdd:TIGR03098 161 IDSD-MAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1746 HKDaayLAQLIERTGITTLHFVPSMLQQFVQWADADCACDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEaAI 1824
Cdd:TIGR03098 240 PRD---VLKALEKHGITGLAAVPPLWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFLpNARLFLMYGLTE-AF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1825 DVTFWACQPDDHRSfVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPfINQPGARL 1904
Cdd:TIGR03098 316 RSTYLPPEEVDRRP-DSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLP-PFPGELHL 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1905 YKT----GDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTP 1980
Cdd:TIGR03098 394 PELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEEL 473
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 641744967 1981 DPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPA 2023
Cdd:TIGR03098 474 DRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1532-2021 |
2.54e-81 |
|
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: 277.52 E-value: 2.54e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1532 QLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPG 1611
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1612 YPAERLAYMLDDASPVALLTqanqralltgdvprilldTADFSHL---SEDNPHVPGLDAHHLAYVIYTSGSTGKPKGVM 1688
Cdd:cd05936 83 YTPRELEHILNDSGAKALIV------------------AVSFTDLlaaGAPLGERVALTPEDVAVLQYTSGTTGVPKGAM 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1689 NSHRAL-CNRLV---WMQNtyRLTPDDRVLQKTP----FSFDVSVwefFWPLLYGARLVM---ARPDGhkdaayLAQLIE 1757
Cdd:cd05936 145 LTHRNLvANALQikaWLED--LLEGDDVVLAALPlfhvFGLTVAL---LLPLALGATIVLiprFRPIG------VLKEIR 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1758 RTGITTLHFVPSMLQQFVQwADADCACD--SLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTFwaCQPDD 1835
Cdd:cd05936 214 KHRVTIFPGVPTMYIALLN-APEFKKRDfsSLRLCISGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAV--NPLDG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1836 HRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlyKTGDLARWLP 1915
Cdd:cd05936 291 PRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL---------RTGDIGYMDE 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1916 DGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAE 1995
Cdd:cd05936 362 DGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAG 441
|
490 500
....*....|....*....|....*.
gi 641744967 1996 YMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05936 442 YKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
475-963 |
2.84e-80 |
|
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: 275.48 E-value: 2.84e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 475 IQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMD 554
Cdd:TIGR01734 2 LIEAIQAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPVD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 555 PAYPAERLAYILDDAAPVALLTQSAqvaqlnstLPTVLLDTPAAaacpdTNPVVQGLHAAHLA-------------YVIY 621
Cdd:TIGR01734 82 TSIPSERIEMIIEAAGPELVIHTAE--------LSIDAVGTQII-----TLSALEQAETSGGPvsfdhavkgddnyYIIY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 622 TSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWI-QLLSGHTLVLVPDALRADAHQLWRYF 700
Cdd:TIGR01734 149 TSGSTGNPKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYpCLASGGTLHCLDKDITNNFKLLFEEL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 701 ARHAVDLFDCTP--VQLQwLLDAGLGSDPAYQPAQVLIGGEAISPAVWSRL-QSLSDTRFINVYGPTECTVDATAC---- 773
Cdd:TIGR01734 229 PKTGLNVWVSTPsfVDMC-LLDPNFNQENYPHLTHFLFCGEELPVKTAKALlERFPKATIYNTYGPTEATVAVTSVkitq 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 774 -VVDRTQPLPtIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFipdpFSADpAARIYKTGDL 852
Cdd:TIGR01734 308 eILDQYPRLP-IGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAF----FSHE-GQPAYRTGDA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 853 ARwLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGD-TRLVAYLCARPD----AELHPAAL 927
Cdd:TIGR01734 382 GT-ITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAIVPETEdfekEFQLTKAI 460
|
490 500 510
....*....|....*....|....*....|....*.
gi 641744967 928 RQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:TIGR01734 461 KKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
2607-3097 |
5.29e-80 |
|
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: 274.71 E-value: 5.29e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2607 LIHELFeAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPL 2686
Cdd:TIGR01734 2 LIEAIQ-AFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2687 DPTYPVERLRYMLDDAKPVALISQSAhLGIMNGSLPVI---LLDDGETRPFDNEPDTPLDARKQgltprhlAYVIYTSGS 2763
Cdd:TIGR01734 81 DTSIPSERIEMIIEAAGPELVIHTAE-LSIDAVGTQIItlsALEQAETSGGPVSFDHAVKGDDN-------YYIIYTSGS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2764 TGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHA 2843
Cdd:TIGR01734 153 TGNPKGVQISHDNLVSFTNWMLADFPLSEGKQFLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2844 VSFMQATPSTWRMLVelrdfaLPPGFKA----------LCgGEALPENLATALLQKV--TTLWNLYGPTETTIWSTLNGL 2911
Cdd:TIGR01734 233 LNVWVSTPSFVDMCL------LDPNFNQenyphlthflFC-GEELPVKTAKALLERFpkATIYNTYGPTEATVAVTSVKI 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2912 T------TPTPYIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITdpFSGAPEarmYKTGD 2985
Cdd:TIGR01734 306 TqeildqYPRLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFS--HEGQPA---YRTGD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2986 LGRwLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDsPGDKrlVAYLLAQpdTVLEPAD----- 3060
Cdd:TIGR01734 381 AGT-ITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYN-KDHK--VEYLIAA--IVPETEDfekef 454
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 641744967 3061 -----LRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:TIGR01734 455 qltkaIKKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1523-2021 |
1.05e-77 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 268.59 E-value: 1.05e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1523 DFPHDALIHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAG 1602
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1603 AAYVPLDPGYPAERLAYMLDDASPVALLTQANQRALLTGDVPR-------ILLDTADFSHLSEDNPHV------------ 1663
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPQlptvrtvIVEGDGPAAPLAPEVGEYeellaaasdtfd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1664 -PGLDAHHLAYVIYTSGSTGKPKGVMNSHRAL------CNRlvWMqntyRLTPDDRVLQKTPFsFDVSVWEFFW-PLLYG 1735
Cdd:PRK06187 161 fPDIDENDAAAMLYTSGTTGHPKGVVLSHRNLflhslaVCA--WL----KLSRDDVYLVIVPM-FHVHAWGLPYlALMAG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1736 ARLVMARpdgHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADCAcD--SLRRVICSGEALPAELQQRFFARFNAQL 1813
Cdd:PRK06187 234 AKQVIPR---RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFV-DfsSLRLVIYGGAALPPALLREFKEKFGIDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1814 HNLYGPTEAAIDVTFwaCQPDDH---RSFVPI--GRPIANTQLYILDTLGQPVP--LGVAGELHIGGVGVARGYLNRPDL 1886
Cdd:PRK06187 310 VQGYGMTETSPVVSV--LPPEDQlpgQWTKRRsaGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEA 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1887 TAERFIPDpfinqpgarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDT 1966
Cdd:PRK06187 388 TAETIDGG---------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGE 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 1967 RLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK06187 459 RPVAVVVLKPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1555-2024 |
1.31e-74 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 259.76 E-value: 1.31e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1555 TYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALltqan 1634
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGL----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1635 qralltgdvprILLDTADFSHLSEDNPHVPgldahhlayviYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVL 1714
Cdd:cd17647 97 -----------IVIRAAGVVVGPDSNPTLS-----------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1715 QKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVqwADADCACDSLRRVICSG 1794
Cdd:cd17647 155 MLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLT--AQATTPFPKLHHAFFVG 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1795 EALpaelQQRFFARF-----NAQLHNLYGPTEAAIDVTFW---ACQPDDH-----RSFVPIGRPIANTQLYILDTL--GQ 1859
Cdd:cd17647 233 DIL----TKRDCLRLqtlaeNVRIVNMYGTTETQRAVSYFevpSRSSDPTflknlKDVMPAGRGMLNVQLLVVNRNdrTQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1860 PVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFINQ--------------------PGARLYKTGDLARWLPDGSL 1919
Cdd:cd17647 309 ICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPdhwnyldkdnnepwrqfwlgPRDRLYRTGDLGRYLPNGDC 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1920 EYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQP---------------GVTPDPA- 1983
Cdd:cd17647 389 ECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFdkpddesfaqedvpkEVSTDPIv 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 641744967 1984 -----------DLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPAP 2024
Cdd:cd17647 469 kgligyrklikDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1069-1494 |
5.34e-74 |
|
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: 254.30 E-value: 5.34e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1069 PLSFSQQRLWFLAQL--DPAAsqaYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRF--TSIDGQPAQQIdpdtlgF 1144
Cdd:cd19532 3 PMSFGQSRFWFLQQYleDPTT---FNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGV------L 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1145 SLSSHDLRKLDEAARTTRVAELAEQEARArFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQA 1224
Cdd:cd19532 74 ASSPLRLEHVQISDEAEVEEEFERLKNHV-YDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1225 AlegseaNLPPLPVQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAPA---LLEIPTDRPRPSVQRYAGDQVPFHLDAGQ 1301
Cdd:cd19532 153 Q------PLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEplpLLPFAKVKSRPPLTRYDTHTAERRLDAAL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1302 LRRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQV 1381
Cdd:cd19532 227 AARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKET 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1382 RERALDAYAHQALPFEQVVEILQPARSLSYSPIFQVMlsLNNTPAQALTLP----DLTLSAVERPQHSthFDLSLSLIET 1457
Cdd:cd19532 307 RDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVF--INYRQGVAESRPfgdcELEGEEFEDARTP--YDLSLDIIDN 382
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 641744967 1458 ENGlnGGLVYAT---DLFDRE---TILRvvGYVeNILMAMADD 1494
Cdd:cd19532 383 PDG--DCLLTLKvqsSLYSEEdaeLLLD--SYV-NLLEAFARD 420
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1538-2018 |
2.44e-73 |
|
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: 252.92 E-value: 2.44e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERL 1617
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1618 AYMLDDASPVALLtqanqralltgdvprilldtadfshlsednphvpgldaHHLAYVIYTSGSTGKPKGVMNSHRALCNR 1697
Cdd:cd17631 85 AYILADSGAKVLF--------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1698 LVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLY-GARLVMARpdgHKDAAYLAQLIERTGITTLHFVPSMLQQFVQ 1776
Cdd:cd17631 127 AVNALAALDLGPDDVLLVVAPLFHIGGLGVFTLPTLLrGGTVVILR---KFDPETVLDLIERHRVTSFFLVPTMIQALLQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1777 ---WADADCAcdSLRRVICSGEALPAELQQRFfARFNAQLHNLYGPTEAAIDVTFwaCQPDDHRS-FVPIGRPIANTQLY 1852
Cdd:cd17631 204 hprFATTDLS--SLRAVIYGGAPMPERLLRAL-QARGVKFVQGYGMTETSPGVTF--LSPEDHRRkLGSAGRPVFFVEVR 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1853 ILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlyKTGDLARWLPDGSLEYLGRNDFQVKLR 1932
Cdd:cd17631 279 IVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF---------HTGDLGRLDEDGYLYIVDRKKDMIISG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1933 GFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTP 2012
Cdd:cd17631 350 GENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNA 429
|
....*.
gi 641744967 2013 NGKLDR 2018
Cdd:cd17631 430 TGKILK 435
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
2161-2567 |
8.92e-72 |
|
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: 248.27 E-value: 8.92e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2161 IYPLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCWQDLSQPVQVVWRQAILPIN 2240
Cdd:cd19543 1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2241 HFEPT--SPEDVLAQLQAH-TEPRTRRIDLSQAPLFRADIAHDPlQNEWLLALSFHHLISDHMTLALIVGEI----RLLL 2313
Cdd:cd19543 81 ELDLShlSEAEQEAELEALaEEDRERGFDLARAPLMRLTLIRLG-DDRYRLVWSFHHILLDGWSLPILLKELfaiyAALG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2314 QHQADALPTPLPYRNFIAQTLSVPNSAHEAYFRDKLADVDEPTA-PFGLLNVQGSGGDIHEARLVLDATLASAIRQQARH 2392
Cdd:cd19543 160 EGQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPlPKELPADADGSYEPGEVSFELSAELTARLQELARQ 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2393 LGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRLAGAEGADRIMGMFINTLPLRISL-ADRGAAEVVERTSHDLMTLL 2471
Cdd:cd19543 240 HGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLdPDQTVLELLKDLQAQQLELR 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2472 EHEQAPLALAQRCSgvAPPMPLFSTLL---NYRHTQASSTDNTLSDIRV--LTSEERTNYPLTLAVdDRGEGFSLV---- 2542
Cdd:cd19543 320 EHEYVPLYEIQAWS--EGKQALFDHLLvfeNYPVDESLEEEQDEDGLRItdVSAEEQTNYPLTVVA-IPGEELTIKlsyd 396
|
410 420
....*....|....*....|....*
gi 641744967 2543 AQTLEDIDPHRLLNYLMTAISSLVD 2567
Cdd:cd19543 397 AEVFDEATIERLLGHLRRVLEQVAA 421
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
468-963 |
1.26e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 250.87 E-value: 1.26e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 468 DFPREMLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAG 547
Cdd:PRK06187 1 MQDYPLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 548 AAYVPMDPAYPAERLAYILDDAAPVALLTQS---AQVAQLNSTLPTV----LLDTPAAAACPDTNPVVQGLHAAH----- 615
Cdd:PRK06187 81 AVLHPINIRLKPEEIAYILNDAEDRVVLVDSefvPLLAAILPQLPTVrtviVEGDGPAAPLAPEVGEYEELLAAAsdtfd 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 616 --------LAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALdHPSRIALNASIVFDASVKNW--IQLLSGHTLVLv 685
Cdd:PRK06187 161 fpdidendAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKL-SRDDVYLVIVPMFHVHAWGLpyLALMAGAKQVI- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 686 PDalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQP-AQVLIGGEAISPAVWSRLQSLSDTRFINVYGPT 764
Cdd:PRK06187 239 PR--RFDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSSlRLVIYGGAALPPALLREFKEKFGIDLVQGYGMT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 765 ECTVDATAC-----VVDRTQPLPTIGKPLANTRLYILDAQDQPVP--IGVTGELHIGGAGVARGYLHRPDLTAERFIPDp 837
Cdd:PRK06187 317 ETSPVVSVLppedqLPGQWTKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 838 fsadpaarIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCAR 917
Cdd:PRK06187 396 --------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVLK 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 641744967 918 PDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK06187 468 PGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1530-2021 |
8.74e-71 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 248.28 E-value: 8.74e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLD 1609
Cdd:PRK07656 7 LPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLN 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1610 PGYPAERLAYMLDDASPVALLTQAnqrALLTGDVPR----------ILLDT-------------ADFSHLSEDNPHVPGL 1666
Cdd:PRK07656 87 TRYTADEAAYILARGDAKALFVLG---LFLGVDYSAttrlpalehvVICETeeddphtekmktfTDFLAAGDPAERAPEV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1667 DAHHLAYVIYTSGSTGKPKGVMNSHRalcnrlvwmqNTYR----------LTPDDRVLQKTPFsFDVSVWEFFW--PLLY 1734
Cdd:PRK07656 164 DPDDVADILFTSGTTGRPKGAMLTHR----------QLLSnaadwaeylgLTEGDRYLAANPF-FHVFGYKAGVnaPLMR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1735 GARLVMARpdgHKDAAYLAQLIERTGITTLHFVPSMLQ---QFVQWADADCAcdSLRRVICSGEALPAELQQRFFARFNA 1811
Cdd:PRK07656 233 GATILPLP---VFDPDEVFRLIETERITVLPGPPTMYNsllQHPDRSAEDLS--SLRLAVTGAASMPVALLERFESELGV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1812 Q-LHNLYGPTEAAIDVTFwaCQPDDHRSFVP--IGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTA 1888
Cdd:PRK07656 308 DiVLTGYGLSEASGVTTF--NRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATA 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1889 ERFIPDPFinqpgarLYkTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVaredspG--DT 1966
Cdd:PRK07656 386 AAIDADGW-------LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI------GvpDE 451
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 1967 RL----VAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK07656 452 RLgevgKAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
483-963 |
3.30e-70 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 248.49 E-value: 3.30e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFED-----QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAY 557
Cdd:COG0365 19 AEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 558 PAERLAYILDDAAPVALLTQSAQ------------VAQLNSTLPTV----LLDTP--------------AAAACPDTNPV 607
Cdd:COG0365 99 GAEALADRIEDAEAKVLITADGGlrggkvidlkekVDEALEELPSLehviVVGRTgadvpmegdldwdeLLAAASAEFEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 608 VQgLHAAHLAYVIYTSGSTGRPKGVMVAHRNVInLATGLHTLLALD-HPSRIALNASIVFdasvknWI---------QLL 677
Cdd:COG0365 179 EP-TDADDPLFILYTSGTTGKPKGVVHTHGGYL-VHAATTAKYVLDlKPGDVFWCTADIG------WAtghsyivygPLL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 678 SGHTLVLVPDALRA-DAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQV-LIG--GEAISPAVWSRLQSLS 753
Cdd:COG0365 251 NGATVVLYEGRPDFpDPGRLWELIEKYGVTVFFTAPTAIRALMKAGDEPLKKYDLSSLrLLGsaGEPLNPEVWEWWYEAV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 754 DTRFINVYGPTECTvdatACVVdrtQPLP-------TIGKPLANTRLYILDAQDQPVPIGVTGELHIGGA--GVARGYLH 824
Cdd:COG0365 331 GVPIVDGWGQTETG----GIFI---SNLPglpvkpgSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWN 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 825 RPDLTAERFipdpFSADPaaRIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDS 904
Cdd:COG0365 404 DPERYRETY----FGRFP--GWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDE 477
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641744967 905 PGDTRLVAYLCARPDAELHPA---ALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:COG0365 478 IRGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
479-963 |
1.19e-69 |
|
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: 243.62 E-value: 1.19e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 479 FEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYP 558
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 559 AERLAYILDDAAPVALLTqsaqvaqlNSTLPTVLldtpaaaACPDTNPVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRN 638
Cdd:cd05936 85 PRELEHILNDSGAKALIV--------AVSFTDLL-------AAGAPLGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 639 -VINLATGLHTLLALDHPSRIALNASIVFDA---SVKNWIQLLSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQ 714
Cdd:cd05936 150 lVANALQIKAWLEDLLEGDDVVLAALPLFHVfglTVALLLPLALGATIVLIP---RFRPIGVLKEIRKHRVTIFPGVPTM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 715 LQWLLDAglGSDPAYQPAQVLI---GGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANT 791
Cdd:cd05936 227 YIALLNA--PEFKKRDFSSLRLcisGGAPLPVEVAERFEELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 792 RLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariyKTGDLARWLPDGNIDYLGRNDFQI 871
Cdd:cd05936 305 EVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL---------RTGDIGYMDEDGYFFIVDRKKDMI 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 872 KVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALP 951
Cdd:cd05936 376 IVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELP 455
|
490
....*....|..
gi 641744967 952 LTPNGKLDRKAL 963
Cdd:cd05936 456 KSAVGKILRREL 467
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
615-959 |
2.52e-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: 237.95 E-value: 2.52e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 615 HLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIaLNASIVFDASVKNWIQ--LLSGHTLVLVPdalRAD 692
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVF-LSTLPLFHIGGLFGLLgaLLAGGTVVLLP---KFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 693 AHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLI-GGEAISPAVWSRLQSLSDTRFINVYGPTECTVDAT 771
Cdd:cd04433 77 PEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVsGGAPLPPELLERFEEAPGIKLVNGYGLTETGGTVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 772 ACVVDRTQPLP-TIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAErFIPDPFsadpaariYKTG 850
Cdd:cd04433 157 TGPPDDDARKPgSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAA-VDEDGW--------YRTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 851 DLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQ 930
Cdd:cd04433 228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAH 307
|
330 340
....*....|....*....|....*....
gi 641744967 931 LAASLADYMIPSAFVTLDALPLTPNGKLD 959
Cdd:cd04433 308 VRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
475-1048 |
2.18e-68 |
|
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: 256.53 E-value: 2.18e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 475 IQQRFEAQAEQTPEAIAVLFEDQHL---------TYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILK 545
Cdd:TIGR03443 238 IHDIFADNAEKHPDRTCVVETPSFLdpssktrsfTYKQINEASNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLK 317
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 546 AGAAYVPMDPAYPAERLAYILDDAAPVAL--LTQSAQVAQ-----------LNSTLPTVLL------------------- 593
Cdd:TIGR03443 318 AGATFSVIDPAYPPARQTIYLSVAKPRALivIEKAGTLDQlvrdyidkeleLRTEIPALALqddgslvggsleggetdvl 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 594 -------DTPAAAAC-PDTNPVVQglhaahlayviYTSGSTGRPKGVMvahrnvinlatGLHTLLA-----------LDH 654
Cdd:TIGR03443 398 apyqalkDTPTGVVVgPDSNPTLS-----------FTSGSEGIPKGVL-----------GRHFSLAyyfpwmakrfgLSE 455
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 655 PSRIALNASIVFDAsvknwIQ------LLSGHTLvLVPDAlrAD---AHQLWRYFARHAVDLFDCTPVQLQwLLDAGLGS 725
Cdd:TIGR03443 456 NDKFTMLSGIAHDP-----IQrdmftpLFLGAQL-LVPTA--DDigtPGRLAEWMAKYGATVTHLTPAMGQ-LLSAQATT 526
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 726 D-PAYQPAqvLIGGEAISPAVWSRLQSLSDTRFI-NVYGPTEC----------TVDATACVVDRTQPLPTIGKPLANTRL 793
Cdd:TIGR03443 527 PiPSLHHA--FFVGDILTKRDCLRLQTLAENVCIvNMYGTTETqravsyfeipSRSSDSTFLKNLKDVMPAGKGMKNVQL 604
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 794 YILDAQD--QPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPD--------------------PFSADPAARIYKTGD 851
Cdd:TIGR03443 605 LVVNRNDrtQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNwfvdpshwidldkennkperEFWLGPRDRLYRTGD 684
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 852 LARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPD-AELHPAA---- 926
Cdd:TIGR03443 685 LGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDKsDELEEFKsevd 764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 927 ---------------------LRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAPD--QTAFATRDY-----EA 978
Cdd:TIGR03443 765 deessdpvvkglikyrklikdIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDtaQLAAVAKNRsasaaDE 844
|
650 660 670 680 690 700 710
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 979 PQGGIETALAALWQELL--GLDRVGRHDQFFALGGHSLLAVQLLNRMNKAGM-DVALATLFAHPTLCDLAAAV 1048
Cdd:TIGR03443 845 EFTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNvELPLGLIFKSPTIKGFAKEV 917
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1069-1494 |
9.51e-68 |
|
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: 236.83 E-value: 9.51e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1069 PLSFSQQRLWFLAQLDPAASqAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDtLGFSLSS 1148
Cdd:cd20484 3 PLSEGQKGLWMLQKMSPEMS-AYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPS-KPLSFQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1149 HDLRKLDEAarttRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALEG 1228
Cdd:cd20484 81 EDISSLKES----EIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1229 SEANLPPLPVQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRLHAL 1308
Cdd:cd20484 157 KQPTLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1309 NRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQVRERALDA 1388
Cdd:cd20484 237 ARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1389 YAHQALPFEQVVEILQPARSLSYSPIFQVMLS----LNNTPAQALTLP---DLTLSAVERPQHSTHFDLSLSLIETENGL 1461
Cdd:cd20484 317 LDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFyqnfLQSTSLQQFLAEyqdVLSIEFVEGIHQEGEYELVLEVYEQEDRF 396
|
410 420 430
....*....|....*....|....*....|...
gi 641744967 1462 NGGLVYATDLFDRETILRVVGYVENILMAMADD 1494
Cdd:cd20484 397 TLNIKYNPDLFDASTIERMMEHYVKLAEELIAN 429
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
2610-3097 |
1.21e-67 |
|
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: 237.85 E-value: 1.21e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2610 ELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPT 2689
Cdd:cd05936 3 DLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2690 YPVERLRYMLDDAKPVALISqsahlgimngslpvillddgeTRPFDN--EPDTPLDaRKQGLTPRHLAYVIYTSGSTGKP 2767
Cdd:cd05936 83 YTPRELEHILNDSGAKALIV---------------------AVSFTDllAAGAPLG-ERVALTPEDVAVLQYTSGTTGVP 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2768 KGVMVEHANMV-NFL-CSMRKEPGIAQEDVLLGVTSL--SFDISIlEIFLPLLNGARLILATQAQAADAQQlamLIERHA 2843
Cdd:cd05936 141 KGAMLTHRNLVaNALqIKAWLEDLLEGDDVVLAALPLfhVFGLTV-ALLLPLALGATIVLIPRFRPIGVLK---EIRKHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2844 VSFMQATPSTWRMLVELRDF--ALPPGFK-ALCGGEALPENLATALLQKV-TTLWNLYGPTETTIWSTLNGLTTPTP--Y 2917
Cdd:cd05936 217 VTIFPGVPTMYIALLNAPEFkkRDFSSLRlCISGGAPLPVEVAERFEELTgVPIVEGYGLTETSPVVAVNPLDGPRKpgS 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2918 IGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFiTDPFsgapearmYKTGDLGRWLPDGTLEY 2997
Cdd:cd05936 297 IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF-VDGW--------LRTGDIGYMDEDGYFFI 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2998 LGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSA 3077
Cdd:cd05936 368 VDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQ 447
|
490 500
....*....|....*....|
gi 641744967 3078 FVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05936 448 VEFRDELPKSAVGKILRREL 467
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
2631-3100 |
1.29e-66 |
|
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: 236.65 E-value: 1.29e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2631 SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQ 2710
Cdd:cd17647 20 SFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVI 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2711 SAhLGIMNGslpvillddgetrpfdnePDTpldarkqglTPRhlayVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGI 2790
Cdd:cd17647 100 RA-AGVVVG------------------PDS---------NPT----LSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2791 AQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVELRDFALPPGFK 2870
Cdd:cd17647 148 SENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAMGQLLTAQATTPFPKLHH 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2871 ALCGGEALPEN--LATALLQKVTTLWNLYGPTETT-------IWST------LNGLTTPTPyIGHPIANTQIYILDAQGR 2935
Cdd:cd17647 228 AFFVGDILTKRdcLRLQTLAENVRIVNMYGTTETQravsyfeVPSRssdptfLKNLKDVMP-AGRGMLNVQLLVVNRNDR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2936 --VVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITD--------------------PFSGAPEARMYKTGDLGRWLPDG 2993
Cdd:cd17647 307 tqICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNwfvepdhwnyldkdnnepwrQFWLGPRDRLYRTGDLGRYLPNG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2994 TLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPD--------TVLEPA------ 3059
Cdd:cd17647 387 DCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDkpddesfaQEDVPKevstdp 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 641744967 3060 -------------DLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAP 3100
Cdd:cd17647 467 ivkgligyrklikDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
2620-3097 |
6.05e-66 |
|
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: 232.36 E-value: 6.05e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGE----ASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERL 2695
Cdd:cd17654 1 PDRPALIIDQttsdTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2696 RYMLDDAKpVALISQSAHlgimNGSLPVILLDdgETRPFDNepdtpldarkqgLTPRHLAYVIYTSGSTGKPKGVMVEHA 2775
Cdd:cd17654 81 LTVMKKCH-VSYLLQNKE----LDNAPLSFTP--EHRHFNI------------RTDECLAYVIHTSGTTGTPKIVAVPHK 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2776 NMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILA-TQAQAADAQQLAMLIERHAVSFMQATPSTW 2854
Cdd:cd17654 142 CILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVpTSVKVLPSKLADILFKRHRITVLQATPTLF 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2855 RML-VELRDFALPPGFKAL----CGGEALPENLATALLQKV---TTLWNLYGPTETTIWSTLN---GLTTPTPyIGHPIA 2923
Cdd:cd17654 222 RRFgSQSIKSTVLSATSSLrvlaLGGEPFPSLVILSSWRGKgnrTRIFNIYGITEVSCWALAYkvpEEDSPVQ-LGSPLL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2924 NTQIYILDAQGRvvplGVAGEIHIagAGVVRGYlgrpdltaerfITDPFSGAPEARMYKTGDLGRwLPDGTLEYLGRNDF 3003
Cdd:cd17654 301 GTVIEVRDQNGS----EGTGQVFL--GGLNRVC-----------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGRKDS 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3004 QVKVRGFRIELGEIETRLARCHGVhDAVVIAREDspgDKRLVAYLLAQPDTVLEPADLRQRLsegVAEYMIPSAFVTLDA 3083
Cdd:cd17654 363 QIKRRGKRINLDLIQQVIESCLGV-ESCAVTLSD---QQRLIAFIVGESSSSRIHKELQLTL---LSSHAIPDTFVQIDK 435
|
490
....*....|....
gi 641744967 3084 FPLTPNGKLDRKAL 3097
Cdd:cd17654 436 LPLTSHGKVDKSEL 449
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
2753-3093 |
2.06e-65 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 226.40 E-value: 2.06e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2753 HLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADA 2832
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2833 QqlaMLIERHAVSFMQATPSTWRMLVEL---RDFALPPGFKALCGGEALPENLATALLQKV-TTLWNLYGPTETTIWSTL 2908
Cdd:cd04433 81 L---ELIEREKVTILLGVPTLLARLLKApesAGYDLSSLRALVSGGAPLPPELLERFEEAPgIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2909 NGLTTPT---PYIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFitdpfsgapEARMYKTGD 2985
Cdd:cd04433 158 GPPDDDArkpGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD---------EDGWYRTGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2986 LGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRL 3065
Cdd:cd04433 229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEELRAHV 308
|
330 340
....*....|....*....|....*...
gi 641744967 3066 SEGVAEYMIPSAFVTLDAFPLTPNGKLD 3093
Cdd:cd04433 309 RERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1550-2016 |
2.23e-65 |
|
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: 231.72 E-value: 2.23e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1550 EDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVAL 1629
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1630 LTQAN-----QRAL-LTGDVPRI-LLDTADFSHLS-------------EDNPHVPGLDAHHLAYVIYTSGSTGKPKGVMN 1689
Cdd:cd05911 87 FTDPDglekvKEAAkELGPKDKIiVLDDKPDGVLSiedllsptlgeedEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1690 SHRALCNRL--VWMQNTYRLTPDDRVLQKTPFsFDVS-VWEFFWPLLYGARLV-MARPdghkDAAYLAQLIERTGITTLH 1765
Cdd:cd05911 167 SHRNLIANLsqVQTFLYGNDGSNDVILGFLPL-YHIYgLFTTLASLLNGATVIiMPKF----DSELFLDLIEKYKITFLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1766 FVPSMLQQFVQWADADCA-CDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEaaidVTFWACQPDDHRSFVP-I 1842
Cdd:cd05911 242 LVPPIAAALAKSPLLDKYdLSSLRVILSGGAPLSKELQELLAKRFpNATIKQGYGMTE----TGGILTVNPDGDDKPGsV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1843 GRPIANTQLYILDTLG-QPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSLEY 1921
Cdd:cd05911 318 GRLLPNVEAKIVDDDGkDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW--------LHTGDIGYFDEDGYLYI 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1922 LGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEY--MVP 1999
Cdd:cd05911 390 VDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYkqLRG 469
|
490
....*....|....*..
gi 641744967 2000 GAFVTlDAFPLTPNGKL 2016
Cdd:cd05911 470 GVVFV-DEIPKSASGKI 485
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1554-2021 |
2.51e-65 |
|
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: 231.82 E-value: 2.51e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQA 1633
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1634 N-----QRALLTgDVPRIL---LDTADFsHLSEDNPHVPGLDAHH-------------LAYVIYTSGSTGKPKGVMNSHR 1692
Cdd:cd05926 95 GelgpaSRAASK-LGLAILelaLDVGVL-IRAPSAESLSNLLADKknaksegvplpddLALILHTSGTTGRPKGVPLTHR 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1693 ALCNRLVWMQNTYRLTPDDRVLQKTPFsFDVS--VWEFFWPLLYGARLVMarPDGHkDAAYLAQLIERTGITTLHFVPSM 1770
Cdd:cd05926 173 NLAASATNITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSVVL--PPRF-SASTFWPDVRDYNATWYTAVPTI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1771 LQQFVQWADADC--ACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTfwaCQP--DDHRSFVPIGRPi 1846
Cdd:cd05926 249 HQILLNRPEPNPesPPPKLRFIRSCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMT---SNPlpPGPRKPGSVGKP- 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1847 ANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSLEYLGRND 1926
Cdd:cd05926 325 VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW--------FRTGDLGYLDADGYLFLTGRIK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1927 FQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLD 2006
Cdd:cd05926 397 ELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVD 476
|
490
....*....|....*
gi 641744967 2007 AFPLTPNGKLDRKAL 2021
Cdd:cd05926 477 ELPKTATGKIQRRKV 491
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
496-964 |
3.87e-65 |
|
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: 228.72 E-value: 3.87e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 496 DQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALL 575
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 576 TQsaqvaqlnstlptvlldtpaaaacpdtnpvvqglhaahLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALdHP 655
Cdd:cd05934 81 VD--------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGL-GE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 656 SRIALNASIVF--DASVKNWIQ-LLSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPA 732
Cdd:cd05934 122 DDVYLTVLPLFhiNAQAVSVLAaLSVGATLVLLP---RFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 733 QVlIGGEAISPAVWSRLQSLSDTRFINVYGPTEcTVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELH 812
Cdd:cd05934 199 RA-AYGAPNPPELHEEFEERFGVRLLEGYGMTE-TIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGELV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 813 I---GGAGVARGYLHRPDLTAERFipdpfsadpAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLR 889
Cdd:cd05934 277 IrglRGWGFFKGYYNMPEATAEAM---------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAILR 347
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 890 CPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALP 964
Cdd:cd05934 348 HPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
483-960 |
1.76e-63 |
|
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: 224.41 E-value: 1.76e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERL 562
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 563 AYILDDAAPvalltqsaqvaqlnstlpTVLLDTPAaaacpdtnpvvqglhaahlaYVIYTSGSTGRPKGVMVAHRNVINL 642
Cdd:cd17631 85 AYILADSGA------------------KVLFDDLA--------------------LLMYTSGTTGRPKGAMLTHRNLLWN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 643 ATGLHTLLALDHPSRIALNASI--VFDASVKNWIQLLSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLD 720
Cdd:cd17631 127 AVNALAALDLGPDDVLLVVAPLfhIGGLGVFTLPTLLRGGTVVILR---KFDPETVLDLIERHRVTSFFLVPTMIQALLQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 721 AGLGSDPAYQPAQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPLP-TIGKPLANTRLYILDAQ 799
Cdd:cd17631 204 HPRFATTDLSSLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTFLSPEDHRRKLgSAGRPVFFVEVRIVDPD 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 800 DQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariyKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIE 879
Cdd:cd17631 284 GREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF---------HTGDLGRLDEDGYLYIVDRKKDMIISGGENVY 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 880 AGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLD 959
Cdd:cd17631 355 PAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKIL 434
|
.
gi 641744967 960 R 960
Cdd:cd17631 435 K 435
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
480-965 |
1.13e-61 |
|
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: 221.96 E-value: 1.13e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 480 EAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPA 559
Cdd:TIGR03098 7 EDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 560 ERLAYILDDAAPVALLTQSAQVAQLNSTLPT-------VLLDTPA----------------AAACPDTNPVVQGLhAAHL 616
Cdd:TIGR03098 87 EQVAHILADCNVRLLVTSSERLDLLHPALPGchdlrtlIIVGDPAhaseghpgeepaswpkLLALGDADPPHPVI-DSDM 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 617 AYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKnwiQLLS----GHTLVLVPDALRAD 692
Cdd:TIGR03098 166 AAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFN---QLTTafyvGATVVLHDYLLPRD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 693 ahqLWRYFARHAVDLFDCTP------VQLQWLLDAGlgsdpayQPAQVLIG-GEAISPAVWSRLQS-LSDTRFINVYGPT 764
Cdd:TIGR03098 243 ---VLKALEKHGITGLAAVPplwaqlAQLDWPESAA-------PSLRYLTNsGGAMPRATLSRLRSfLPNARLFLMYGLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 765 EcTVDATACVVDRTQPLPT-IGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSAD-- 841
Cdd:TIGR03098 313 E-AFRSTYLPPEEVDRRPDsIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPPFPGel 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 842 --PAARIYkTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPD 919
Cdd:TIGR03098 392 hlPELAVW-SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGG 470
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 641744967 920 AELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPA 965
Cdd:TIGR03098 471 EELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
28-399 |
3.86e-61 |
|
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: 217.46 E-value: 3.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 28 IYPLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICWQGLHQPVQVVWRQAPLTVN 107
Cdd:cd19543 1 IYPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 108 T--LTTTSSDTVPAQLRA-ATDPSNHRLNLSNAPLLSAT---TAHDpvcgEWLLSLSIHHLISDHITQALIIDEI----R 177
Cdd:cd19543 81 EldLSHLSEAEQEAELEAlAEEDRERGFDLARAPLMRLTlirLGDD----RYRLVWSFHHILLDGWSLPILLKELfaiyA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 178 LLLEDRPEALPKPLPYRNFIAQILSVPLSEHEQYFRNRLADIDTPTA-PFDLVDVQGNGEDITEARLSLDSSLADALRRQ 256
Cdd:cd19543 157 ALGEGQPPSLPPVRPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPlPKELPADADGSYEPGEVSFELSAELTARLQEL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 257 ARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQGNLGADRVMGMFINTLPLRVSLRER-SVHDVVQATSHELM 335
Cdd:cd19543 237 ARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDqTVLELLKDLQAQQL 316
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 336 MLLAHEQAPLALAQQCSQVPPplPLFSTLF---NYRHSQKDASSQFWEG--MRQLSGRERTNYPITLSV 399
Cdd:cd19543 317 ELREHEYVPLYEIQAWSEGKQ--ALFDHLLvfeNYPVDESLEEEQDEDGlrITDVSAEEQTNYPLTVVA 383
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
2607-3097 |
3.94e-61 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 220.44 E-value: 3.94e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2607 LIHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPL 2686
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2687 DPTYPVERLRYMLDDAKPVALISQSAHLGIMNGSLP-------VILLDDGETRPF-----------DNEPDTPLDARkqg 2748
Cdd:PRK06187 87 NIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAILPqlptvrtVIVEGDGPAAPLapevgeyeellAAASDTFDFPD--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2749 LTPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLsFDISILEI-FLPLLNGARLILATQA 2827
Cdd:PRK06187 164 IDENDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPM-FHVHAWGLpYLALMAGAKQVIPRRF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2828 QAADAQQlamLIERHAVSFMQATPSTWRMLVElrdfALPPGFK-------ALCGGEALPENLATALLQKV-TTLWNLYGP 2899
Cdd:PRK06187 243 DPENLLD---LIETERVTFFFAVPTIWQMLLK----APRAYFVdfsslrlVIYGGAALPPALLREFKEKFgIDLVQGYGM 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2900 TETTIWSTLN----GLTTPTPYI---GHPIANTQIYILDAQGRVVP--LGVAGEIHIAGAGVVRGYLGRPDLTAERFITD 2970
Cdd:PRK06187 316 TETSPVVSVLppedQLPGQWTKRrsaGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2971 pfsgapearMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLA 3050
Cdd:PRK06187 396 ---------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVVL 466
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 641744967 3051 QPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK06187 467 KPGATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1543-2021 |
4.26e-61 |
|
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: 217.93 E-value: 4.26e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1543 DTTAVLFEDQHLTYDALNRRANQLAHHLIDLG-VKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYML 1621
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1622 DDASPvalltqanqralltgdvpRILLDtadfshlsednphvpgldahhLAYVIYTSGSTGKPKGVMNSHRALCNRLVWM 1701
Cdd:cd05941 81 TDSEP------------------SLVLD---------------------PALILYTSGTTGRPKGVVLTHANLAANVRAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLTPDDRVLQKTPFsFDVS--VWEFFWPLLYGARLVMARPDghkDAAYLAQLIERTGITTLHFVPSMLQQFVQWAD 1779
Cdd:cd05941 122 VDAWRWTEDDVLLHVLPL-HHVHglVNALLCPLFAGASVEFLPKF---DPKEVAISRLMPSITVFMGVPTIYTRLLQYYE 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1780 ADC---------ACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTfwaCQPDDHRSFVPIGRPIANTQ 1850
Cdd:cd05941 198 AHFtdpqfaraaAAERLRLMVSGSAALPVPTLEEWEAITGHTLLERYGMTEIGMALS---NPLDGERRPGTVGMPLPGVQ 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1851 LYILDTL-GQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSLEYLGR-NDFQ 1928
Cdd:cd05941 275 ARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW--------FKTGDLGVVDEDGYYWILGRsSVDI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1929 VKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTP-DPADLRQQLGQHLAEYMVPGAFVTLDA 2007
Cdd:cd05941 347 IKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAAlSLEELKEWAKQRLAPYKRPRRLILVDE 426
|
490
....*....|....
gi 641744967 2008 FPLTPNGKLDRKAL 2021
Cdd:cd05941 427 LPRNAMGKVNKKEL 440
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1551-2022 |
4.36e-61 |
|
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: 217.16 E-value: 4.36e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1551 DQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALL 1630
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1631 TQanqralltgdvprilldtadfshlsednphvpgldahhLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPD 1710
Cdd:cd05934 81 VD--------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGED 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1711 DRVLQKTP-FSFDVSVWEFFWPLLYGARLVMARPdgHKDAAYLAQlIERTGITTLHFVPSMLQQFVQWADADCACDSLRR 1789
Cdd:cd05934 123 DVYLTVLPlFHINAQAVSVLAALSVGATLVLLPR--FSASRFWSD-VRRYGATVTNYLGAMLSYLLAQPPSPDDRAHRLR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1790 VICSGEAlPAELQQRFFARFNAQLHNLYGPTEAAIDVtfwACQPDDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGEL 1869
Cdd:cd05934 200 AAYGAPN-PPELHEEFEERFGVRLLEGYGMTETIVGV---IGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAGEPGEL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1870 HIGGV---GVARGYLNRPDLTAERFiPDPFinqpgarlYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLM 1946
Cdd:cd05934 276 VIRGLrgwGFFKGYYNMPEATAEAM-RNGW--------FHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVERAIL 346
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 1947 QCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALP 2022
Cdd:cd05934 347 RHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1542-2021 |
3.08e-60 |
|
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: 215.41 E-value: 3.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1542 PDTTAVLFE----DQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERL 1617
Cdd:cd17654 1 PDRPALIIDqttsDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1618 AYMLDDASPVALLTQANQRALltgdvPRILLDTADFSHLSEDnphvpgldaHHLAYVIYTSGSTGKPKGVMNSHRALCNR 1697
Cdd:cd17654 81 LTVMKKCHVSYLLQNKELDNA-----PLSFTPEHRHFNIRTD---------ECLAYVIHTSGTTGTPKIVAVPHKCILPN 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1698 LVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQ-LIERTGITTLHFVPSMLQQFVQ 1776
Cdd:cd17654 147 IQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRFGS 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1777 WADAD---CACDSLRRVICSGEALPAELQQRFFARFNAQLH--NLYGPTEAAIDVTFWACQPDDhrSFVPIGRPIANTQL 1851
Cdd:cd17654 227 QSIKStvlSATSSLRVLALGGEPFPSLVILSSWRGKGNRTRifNIYGITEVSCWALAYKVPEED--SPVQLGSPLLGTVI 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1852 YILDTLGQPvplgVAGELHIGgvGVARGYlnrpdltaerFIPDPfINQPGARLYKTGDLARwLPDGSLEYLGRNDFQVKL 1931
Cdd:cd17654 305 EVRDQNGSE----GTGQVFLG--GLNRVC----------ILDDE-VTVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKR 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1932 RGFRIELGEIEARLMQCPGVqEAVVVAREDspgDTRLVAYLCPQPGVTPDPADLRQQLgqhLAEYMVPGAFVTLDAFPLT 2011
Cdd:cd17654 367 RGKRINLDLIQQVIESCLGV-ESCAVTLSD---QQRLIAFIVGESSSSRIHKELQLTL---LSSHAIPDTFVQIDKLPLT 439
|
490
....*....|
gi 641744967 2012 PNGKLDRKAL 2021
Cdd:cd17654 440 SHGKVDKSEL 449
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
500-966 |
4.68e-60 |
|
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: 217.39 E-value: 4.68e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 500 TYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALltqsa 579
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGL----- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 580 qvaqlnstlptVLLDTPAAAACPDTNPVVQglhaahlayviYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIA 659
Cdd:cd17647 97 -----------IVIRAAGVVVGPDSNPTLS-----------FTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 660 LNASIVFDASVKN-WIQLLSGHTLvLVPDALR-ADAHQLWRYFARHAVDLFDCTPVQLQwLLDAGlGSDPAYQPAQVLIG 737
Cdd:cd17647 155 MLSGIAHDPIQRDmFTPLFLGAQL-LVPTQDDiGTPGRLAEWMAKYGATVTHLTPAMGQ-LLTAQ-ATTPFPKLHHAFFV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 738 GEAISPAVWSRLQSLSDT-RFINVYGPTECTVDATACVVDRTQPLPTI----------GKPLANTRLYILDAQD--QPVP 804
Cdd:cd17647 232 GDILTKRDCLRLQTLAENvRIVNMYGTTETQRAVSYFEVPSRSSDPTFlknlkdvmpaGRGMLNVQLLVVNRNDrtQICG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 805 IGVTGELHIGGAGVARGYLHRPDLTAERFI------PD--------------PFSADPAARIYKTGDLARWLPDGNIDYL 864
Cdd:cd17647 312 IGEVGEIYVRAGGLAEGYRGLPELNKEKFVnnwfvePDhwnyldkdnnepwrQFWLGPRDRLYRTGDLGRYLPNGDCECC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 865 GRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAEL---------------------- 922
Cdd:cd17647 392 GRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDdesfaqedvpkevstdpivkgl 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 641744967 923 ---HPAA--LRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAP 966
Cdd:cd17647 472 igyRKLIkdIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1554-2016 |
5.40e-60 |
|
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: 214.55 E-value: 5.40e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASpvalltqa 1633
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAK-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1634 nqralltgdvPRILLDTADFSHLSednpHVPGLDAhhLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRV 1713
Cdd:cd05903 74 ----------AKVFVVPERFRQFD----PAAMPDA--VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1714 LQKTPFS-FDVSVWEFFWPLLYGARLVMARPdghKDAAYLAQLIERTGITTLHFVPSMLQQFVQWAD-ADCACDSLRRVI 1791
Cdd:cd05903 138 LVASPMAhQTGFVYGFTLPLLLGAPVVLQDI---WDPDKALALMREHGVTFMMGATPFLTDLLNAVEeAGEPLSRLRTFV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1792 CSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTFWACQPDDHRSFVPiGRPIANTQLYILDTLGQPVPLGVAGELHI 1871
Cdd:cd05903 215 CGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEDRRLYTD-GRPLPGVEIKVVDDTGATLAPGVEGELLS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1872 GGVGVARGYLNRPDLTAeRFIPDPFinqpgarlYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGV 1951
Cdd:cd05903 294 RGPSVFLGYLDRPDLTA-DAAPEGW--------FRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPGV 364
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 1952 QEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQL-GQHLAEYMVPGAFVTLDAFPLTPNGKL 2016
Cdd:cd05903 365 IEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
470-963 |
9.98e-60 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 215.92 E-value: 9.98e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 470 PREMLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAA 549
Cdd:PRK07656 2 NEWMTLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 550 YVPMDPAYPAERLAYILDDAAPVALLTQSAQVAQLNST---LPT----VLLDTPAAA-------------ACPDTNPVVQ 609
Cdd:PRK07656 82 VVPLNTRYTADEAAYILARGDAKALFVLGLFLGVDYSAttrLPAlehvVICETEEDDphtekmktftdflAAGDPAERAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 610 GLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSR--IALNASIVFDASVkNWIQ-LLSGHTLVLVP 686
Cdd:PRK07656 162 EVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGDRylAANPFFHVFGYKA-GVNApLMRGATILPLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 687 dalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLI-GGEAISPAVWSRLQSLSDTRFI-NVYGPT 764
Cdd:PRK07656 241 ---VFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVtGAASMPVALLERFESELGVDIVlTGYGLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 765 ECTVDATACVVDRTQPLP--TIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadp 842
Cdd:PRK07656 318 EASGVTTFNRLDDDRKTVagTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW---- 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 843 aarIYkTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIaredspG--DTRL----VAYLCA 916
Cdd:PRK07656 394 ---LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI------GvpDERLgevgKAYVVL 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 641744967 917 RPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK07656 464 KPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
2609-3106 |
6.29e-59 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 215.36 E-value: 6.29e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2609 HELFEAQVACTPDAIAVVF-----GEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAY 2683
Cdd:COG0365 12 YNCLDRHAEGRGDKVALIWegedgEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVH 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2684 VPLDPTYPVERLRYMLDDAKPVALISQSAhlGIMNG-----------------SLPVILLDDGETRPFDNEPDTPLDARK 2746
Cdd:COG0365 92 SPVFPGFGAEALADRIEDAEAKVLITADG--GLRGGkvidlkekvdealeelpSLEHVIVVGRTGADVPMEGDLDWDELL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2747 QGLTPR---------HLAYVIYTSGSTGKPKGVMVEHAN-MVNFLCSMRKEPGIAQEDVLLGVTSLSF-----DIsileI 2811
Cdd:COG0365 170 AAASAEfepeptdadDPLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVFWCTADIGWatghsYI----V 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2812 FLPLLNGARLILATQAQAADAQQLAM-LIERHAVSFMQATPSTWRML-----VELRDFALPPgFKAL-CGGEALPENLAT 2884
Cdd:COG0365 246 YGPLLNGATVVLYEGRPDFPDPGRLWeLIEKYGVTVFFTAPTAIRALmkagdEPLKKYDLSS-LRLLgSAGEPLNPEVWE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2885 ALLQKV-TTLWNLYGPTETT-IWSTLNGLTTPTP-YIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGA--GVVRGYLGR 2959
Cdd:COG0365 325 WWYEAVgVPIVDGWGQTETGgIFISNLPGLPVKPgSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPwpGMFRGYWND 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2960 PDLTAERFiTDPFSGapearMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSP 3039
Cdd:COG0365 405 PERYRETY-FGRFPG-----WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEI 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 3040 GDKRLVAYLLAQPDTVLEPA---DLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL-------PAPDQSAMA 3106
Cdd:COG0365 479 RGQVVKAFVVLKPGVEPSDElakELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLLrkiaegrPLGDTSTLE 555
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
2607-3099 |
2.27e-58 |
|
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: 212.33 E-value: 2.27e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2607 LIHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPL 2686
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2687 DPTYPVERLRYMLDDAKPVALISQSAHLGIMNGSLP-------VILLDDGETRPFDNEPDTPLDARK-QGLTPRH----- 2753
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVRLLVTSSERLDLLHPALPgchdlrtLIIVGDPAHASEGHPGEEPASWPKlLALGDADpphpv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2754 ----LAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQA 2829
Cdd:TIGR03098 161 idsdMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVLHDYLLP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2830 ADAQQlamLIERHAVSFMQATPSTWRMLVELrdfALPPG------FKALCGGeALPENLATALLQKV--TTLWNLYGPTE 2901
Cdd:TIGR03098 241 RDVLK---ALEKHGITGLAAVPPLWAQLAQL---DWPESaapslrYLTNSGG-AMPRATLSRLRSFLpnARLFLMYGLTE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2902 TTIWSTLN-GLTTPTP-YIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERF-ITDPFSGA--- 2975
Cdd:TIGR03098 314 AFRSTYLPpEEVDRRPdSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFrPLPPFPGElhl 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2976 PEARMYkTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTV 3055
Cdd:TIGR03098 394 PELAVW-SGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDPTLGQAIVLVVTPPGGEE 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 641744967 3056 LEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPA 3099
Cdd:TIGR03098 473 LDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1545-2021 |
4.95e-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: 208.86 E-value: 4.95e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1545 TAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDA 1624
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1625 SPVALLTqanqralltgdvprilldtadfshlsednphvpglDAHHLAYVIYTSGSTGKPKGVMNSHRAL---CNRlvWM 1701
Cdd:cd05919 82 EARLVVT-----------------------------------SADDIAYLLYSSGTTGPPKGVMHAHRDPllfADA--MA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLTPDDRVL--QKTPFSFDV--SVWeffWPLLYGARLVMArpDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQW 1777
Cdd:cd05919 125 REALGLTPGDRVFssAKMFFGYGLgnSLW---FPLAVGASAVLN--PGWPTAERVLATLARFRPTVLYGVPTFYANLLDS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1778 ADADCACD-SLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIdvTFWACQPDDHRsFVPIGRPIANTQLYILDT 1856
Cdd:cd05919 200 CAGSPDALrSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGH--IFLSNRPGAWR-LGSTGRPVPGYEIRLVDE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1857 LGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFipdpfinQPGarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRI 1936
Cdd:cd05919 277 EGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF-------NGG--WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWV 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1937 ELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPAdLRQQLGQHLAE----YMVPGAFVTLDAFPLTP 2012
Cdd:cd05919 348 SPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQES-LARDIHRHLLErlsaHKVPRRIAFVDELPRTA 426
|
....*....
gi 641744967 2013 NGKLDRKAL 2021
Cdd:cd05919 427 TGKLQRFKL 435
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1533-2021 |
1.07e-57 |
|
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: 209.92 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1533 LVEDQAARTPDTTAVLFEDQ-HLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPG 1611
Cdd:cd05959 8 LVDLNLNEGRGDKTAFIDDAgSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1612 YPAERLAYMLDD-------ASP--VALLTQANQRALLTG---DVPRILLDTADFSHLSEDNPHVPGLD------AHHLAY 1673
Cdd:cd05959 88 LTPDDYAYYLEDsrarvvvVSGelAPVLAAALTKSEHTLvvlIVSGGAGPEAGALLLAELVAAEAEQLkpaathADDPAF 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1674 VIYTSGSTGKPKGVMNSHRALcnrlVWMQNTY-----RLTPDDRVLQ--KTPFSFDVSVWEFFwPLLYGARLVM--ARPD 1744
Cdd:cd05959 168 WLYSSGSTGRPKGVVHLHADI----YWTAELYarnvlGIREDDVCFSaaKLFFAYGLGNSLTF-PLSVGATTVLmpERPT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1745 ghkdAAYLAQLIERTGITTLHFVP----SMLQQFVQWADADcacDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPT 1820
Cdd:cd05959 243 ----PAAVFKRIRRYRPTVFFGVPtlyaAMLAAPNLPSRDL---SSLRLCVSAGEALPAEVGERWKARFGLDILDGIGST 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1821 EAA-IdvtFWACQPDDHRsFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIpdpfinq 1899
Cdd:cd05959 316 EMLhI---FLSNRPGRVR-YGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ------- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1900 pgARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVT 1979
Cdd:cd05959 385 --GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPGYE 462
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 641744967 1980 P---DPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05959 463 DseaLEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
2619-3094 |
1.62e-57 |
|
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: 207.08 E-value: 1.62e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2619 TPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYM 2698
Cdd:cd17631 8 HPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2699 LDDakpvalisqsahlgimngSLPVILLDDgetrpfdnepdtpldarkqgltprhLAYVIYTSGSTGKPKGVMVEHANMV 2778
Cdd:cd17631 88 LAD------------------SGAKVLFDD-------------------------LALLMYTSGTTGRPKGAMLTHRNLL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2779 NFLCSMRKEPGIAQEDVLLGVTSLsFDISILEIFLP--LLNGARLILATQAQAADAQQlamLIERHAVSFMQATPSTWRM 2856
Cdd:cd17631 125 WNAVNALAALDLGPDDVLLVVAPL-FHIGGLGVFTLptLLRGGTVVILRKFDPETVLD---LIERHRVTSFFLVPTMIQA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2857 LVELRDFALP--PGFKALC-GGEALPENLATALLQKVTTLWNLYGPTETTiwstlNGLTTPTP--------YIGHPIANT 2925
Cdd:cd17631 201 LLQHPRFATTdlSSLRAVIyGGAPMPERLLRALQARGVKFVQGYGMTETS-----PGVTFLSPedhrrklgSAGRPVFFV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2926 QIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmyKTGDLGRWLPDGTLEYLGRNDFQV 3005
Cdd:cd17631 276 EVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF---------HTGDLGRLDEDGYLYIVDRKKDMI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3006 KVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFP 3085
Cdd:cd17631 347 ISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDALP 426
|
....*....
gi 641744967 3086 LTPNGKLDR 3094
Cdd:cd17631 427 RNATGKILK 435
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1530-2021 |
1.92e-57 |
|
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: 210.00 E-value: 1.92e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLd 1609
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPVFA- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1610 pgYPAER---LAYMLDDASPVALLTQA-----NQRAL---LTGDVPR----ILLDTAD----FSHLSED--NPHVPGLDA 1668
Cdd:COG1021 106 --LPAHRraeISHFAEQSEAVAYIIPDrhrgfDYRALareLQAEVPSlrhvLVVGDAGeftsLDALLAApaDLSEPRPDP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1669 HHLAYVIYTSGSTGKPKGVMNSHralcnrlvwmqNTY-----------RLTPDDRVLQKTP--FSFDVSVWEFFWPLLYG 1735
Cdd:COG1021 184 DDVAFFQLSGGTTGLPKLIPRTH-----------DDYlysvrasaeicGLDADTVYLAALPaaHNFPLSSPGVLGVLYAG 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1736 ARLVMArPDGHKDAAYlaQLIERTGITTLHFVPSMLQ---QFVQWADADCAcdSLRRVICSGEALPAELQQRFFARFNAQ 1812
Cdd:COG1021 253 GTVVLA-PDPSPDTAF--PLIERERVTVTALVPPLALlwlDAAERSRYDLS--SLRVLQVGGAKLSPELARRVRPALGCT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1813 LHNLYGPTEAAIDVTfwacQPDD--HRSFVPIGRPI-ANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAE 1889
Cdd:COG1021 328 LQQVFGMAEGLVNYT----RLDDpeEVILTTQGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNAR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1890 RFIPDPFinqpgarlYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLV 1969
Cdd:COG1021 404 AFTPDGF--------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSC 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 641744967 1970 AYLCPQpGVTPDPADLRQQL-GQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:COG1021 476 AFVVPR-GEPLTLAELRRFLrERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1561-2021 |
1.25e-56 |
|
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: 205.37 E-value: 1.25e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1561 RRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAA----YVPLDPGYPAERLAYMLDDASPVALLTQANQR 1636
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1637 ALL------TGDvPRILLDTADFSHLSEDNPHVPgLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPD 1710
Cdd:cd05922 81 DRLrdalpaSPD-PGTVLDADGIRAARASAPAHE-VSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1711 DRVLQKTPFSFDVSVWEFFWPLLYGARLVMArPDGHKDAAYLaQLIERTGITTLHFVPSMLQQFVQWADADCACDSLRRV 1790
Cdd:cd05922 159 DRALTVLPLSYDYGLSVLNTHLLRGATLVLT-NDGVLDDAFW-EDLREHGATGLAGVPSTYAMLTRLGFDPAKLPSLRYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1791 ICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFwaCQPDD-HRSFVPIGRPIANTQLYILDTLGQPVPLGVAGE 1868
Cdd:cd05922 237 TQAGGRLPQETIARLRELLpGAQVYVMYGQTEATRRMTY--LPPERiLEKPGSIGLAIPGGEFEILDDDGTPTPPGEPGE 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1869 LHIGGVGVARGYLNRPdltaeRFIPDPfiNQPGARLYkTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQC 1948
Cdd:cd05922 315 IVHRGPNVMKGYWNDP-----PYRRKE--GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSI 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 1949 PGVQEAVVVAREDSPGDtRLVAYLCPQPGVtpDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05922 387 GLIIEAAAVGLPDPLGE-KLALFVTAPDKI--DPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
499-963 |
1.44e-56 |
|
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: 206.39 E-value: 1.44e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQS 578
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPK 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 A------------QVAQLNSTLPTVLLDTPAAA----ACPDTNPVVQGLHAAH---LAYVIYTSGSTGRPKGVMVAHRNV 639
Cdd:cd05926 95 GelgpasraasklGLAILELALDVGVLIRAPSAeslsNLLADKKNAKSEGVPLpddLALILHTSGTTGRPKGVPLTHRNL 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 640 INLATGLHTLLALDhPSRIALNASIVFD-----ASVKNwiQLLSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQ 714
Cdd:cd05926 175 AASATNITNTYKLT-PDDRTLVVMPLFHvhglvASLLS--TLAAGGSVVLPP---RFSASTFWPDVRDYNATWYTAVPTI 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 715 LQWLLdaglgSDPAYQPAQVLI-------GGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATacvvdrTQPLP----- 782
Cdd:cd05926 249 HQILL-----NRPEPNPESPPPklrfirsCSASLPPAVLEALEATFGAPVLEAYGMTEAAHQMT------SNPLPpgprk 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 783 --TIGKPlANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGN 860
Cdd:cd05926 318 pgSVGKP-VGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW--------FRTGDLGYLDADGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 861 IDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMI 940
Cdd:cd05926 389 LFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTEEELRAFCRKHLAAFKV 468
|
490 500
....*....|....*....|...
gi 641744967 941 PSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05926 469 PKKVYFVDELPKTATGKIQRRKV 491
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
495-958 |
1.52e-56 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 205.91 E-value: 1.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 495 EDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAP--- 571
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPkvi 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 572 -------------VALLTQSAQVAQLNSTLPTVL----LDTPAAAACPDTNPVVQGLHAAHLAYVIYTSGSTGRPKGVMV 634
Cdd:cd05911 87 ftdpdglekvkeaAKELGPKDKIIVLDDKPDGVLsiedLLSPTLGEEDEDLPPPLKDGKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 635 AHRNVINlatglHTLLALDHPSRIALNASIVFDASVKNWI--------QLLSGHTLVLVPdalRADAHQLWRYFARHAVD 706
Cdd:cd05911 167 SHRNLIA-----NLSQVQTFLYGNDGSNDVILGFLPLYHIyglfttlaSLLNGATVIIMP---KFDSELFLDLIEKYKIT 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 707 LFDCTPVQLQWLLDaglgsDPAYQPAQ------VLIGGEAISPAVWSRLQSL-SDTRFINVYGPTECTVdATACVVDRTQ 779
Cdd:cd05911 239 FLYLVPPIAAALAK-----SPLLDKYDlsslrvILSGGAPLSKELQELLAKRfPNATIKQGYGMTETGG-ILTVNPDGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 780 PLPTIGKPLANTRLYILDAQ-DQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPD 858
Cdd:cd05911 313 KPGSVGRLLPNVEAKIVDDDgKDSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW--------LHTGDIGYFDED 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 859 GNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADY 938
Cdd:cd05911 385 GYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASY 464
|
490 500
....*....|....*....|....*.
gi 641744967 939 ------MIpsaFVtlDALPLTPNGKL 958
Cdd:cd05911 465 kqlrggVV---FV--DEIPKSASGKI 485
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
499-963 |
1.07e-55 |
|
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: 1.07e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQS 578
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 AQ-VAQLNSTLPTVLLDTPaaaacpdtnpvvqglHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDhPSR 657
Cdd:cd17654 97 ELdNAPLSFTPEHRHFNIR---------------TDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNIT-SED 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 658 IALNASI-VFDASVKNWI-QLLSGHTLVLVPDALRADAHQLWR-YFARHAVDLFDCTPVQLQWLLDAGLGSD--PAYQPA 732
Cdd:cd17654 161 ILFLTSPlTFDPSVVEIFlSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRFGSQSIKSTvlSATSSL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 733 QVL-IGGEA--ISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQPvpigVTG 809
Cdd:cd17654 241 RVLaLGGEPfpSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSE----GTG 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 810 ELHIGgaGVARGYlhrpdltaerFIPDPFSAdPAARIYKTGDLARwLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLR 889
Cdd:cd17654 317 QVFLG--GLNRVC----------ILDDEVTV-PKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQQVIES 382
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 890 CPGVQdAVVIAREDspgDTRLVAYLCARP-DAELHPAALRQQLAAsladYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd17654 383 CLGVE-SCAVTLSD---QQRLIAFIVGESsSSRIHKELQLTLLSS----HAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
479-959 |
1.53e-55 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 204.35 E-value: 1.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 479 FEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYP 558
Cdd:PRK07798 9 FEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 559 AERLAYILDDAAPVALLTQS---AQVAQLNSTLPTVLL-----DTPAAAACPDTNPVVQGLHAAHLA-----------YV 619
Cdd:PRK07798 89 EDELRYLLDDSDAVALVYERefaPRVAEVLPRLPKLRTlvvveDGSGNDLLPGAVDYEDALAAGSPErdfgerspddlYL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 620 IYTSGSTGRPKGVMVAHRNV-------INLATG--LHTLlaLDHPSRIALN-ASIVFDAS--------VKNWIQLLSGHT 681
Cdd:PRK07798 169 LYTGGTTGMPKGVMWRQEDIfrvllggRDFATGepIEDE--EELAKRAAAGpGMRRFPAPplmhgagqWAAFAALFSGQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 682 LVLVPDAlRADAHQLWRYFARHAVDLFDCT------PvqlqwLLDAGLGSDPAYQPAQVLI--GGEAISPAVWSRLQSLS 753
Cdd:PRK07798 247 VVLLPDV-RFDADEVWRTIEREKVNVITIVgdamarP-----LLDALEARGPYDLSSLFAIasGGALFSPSVKEALLELL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 754 DTR-FINVYGPTECTVDATACVVDRTQP--LPTIGkplANTRLYILDAQDQPVP--IGVTGELHIGGAgVARGYLHRPDL 828
Cdd:PRK07798 321 PNVvLTDSIGSSETGFGGSGTVAKGAVHtgGPRFT---IGPRTVVLDEDGNPVEpgSGEIGWIARRGH-IPLGYYKDPEK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 829 TAERFipdpFSADpAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDT 908
Cdd:PRK07798 397 TAETF----PTID-GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQ 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 641744967 909 RLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLD 959
Cdd:PRK07798 472 EVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1550-2021 |
2.69e-55 |
|
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: 203.25 E-value: 2.69e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1550 EDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAicverSLDM-----VIGLLAILKAGAAYVPLDPGYPAERLAYMLDDA 1624
Cdd:cd12119 22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVA-----TLAWnthrhLELYYAVPGMGAVLHTINPRLFPEQIAYIINHA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1625 SPVALLTQANQRALLTGDVPR-------ILLDTADFSHLSEDNP---------------HVPGLDAHHLAYVIYTSGSTG 1682
Cdd:cd12119 97 EDRVVFVDRDFLPLLEAIAPRlptvehvVVMTDDAAMPEPAGVGvlayeellaaespeyDWPDFDENTAAAICYTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1683 KPKGVMNSHRALcnrlvWMQNTYRLTPD-------DRVLQKTPFsFDVSVWEF-FWPLLYGARLVMarPDGHKDAAYLAQ 1754
Cdd:cd12119 177 NPKGVVYSHRSL-----VLHAMAALLTDglglsesDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL--PGPYLDPASLAE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1755 LIERTGITTLHFVPSMLQQFVQWADA-DCACDSLRRVICSGEALPAELQQRFFARFNAQLHnLYGPTEAAIDVTFwaCQP 1833
Cdd:cd12119 249 LIEREGVTFAAGVPTVWQGLLDHLEAnGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIH-AWGMTETSPLGTV--ARP 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1834 DDHRSFVPI----------GRPIANTQLYILDTLGQPVPL-GVA-GELHIGGVGVARGYLNRPDlTAERFIPDPFInqpg 1901
Cdd:cd12119 326 PSEHSNLSEdeqlalrakqGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDE-ESEALTEDGWL---- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1902 arlyKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPD 1981
Cdd:cd12119 401 ----RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVT 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 641744967 1982 PADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd12119 477 AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
499-958 |
1.45e-53 |
|
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: 195.68 E-value: 1.45e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTqs 578
Cdd:cd05903 2 LTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVV-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 aqvaqlnstlPTVLLDTPAAAAcPDTnpvvqglhaahLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRI 658
Cdd:cd05903 80 ----------PERFRQFDPAAM-PDA-----------VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGDVF 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 659 aLNASivfdaSVKNWIQLLSGHTLVLVpdaLRADAHQLWRYFARHAVDLFD---CTPVQ-----LQWLLDAGLGSDPAYQ 730
Cdd:cd05903 138 -LVAS-----PMAHQTGFVYGFTLPLL---LGAPVVLQDIWDPDKALALMRehgVTFMMgatpfLTDLLNAVEEAGEPLS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 731 PAQVLI-GGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVDRT-QPLPTIGKPLANTRLYILDAQDQPVPIGVT 808
Cdd:cd05903 209 RLRTFVcGGATVPRSLARRAAELLGAKVCSAYGSTECPGAVTSITPAPEdRRLYTDGRPLPGVEIKVVDDTGATLAPGVE 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 809 GELHIGGAGVARGYLHRPDLTAeRFIPDPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLL 888
Cdd:cd05903 289 GELLSRGPSVFLGYLDRPDLTA-DAAPEGW--------FRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLL 359
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641744967 889 RCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQL-AASLADYMIPSAFVTLDALPLTPNGKL 958
Cdd:cd05903 360 GHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1068-1498 |
1.62e-53 |
|
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: 194.90 E-value: 1.62e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1068 LPLSFSQQRLWFLAQLDPAASQaYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDTLgFSLS 1147
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEGSI-YNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTP-VPIR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1148 SHDLRKlDEAARTTrVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALE 1227
Cdd:cd19533 80 HIDLSG-DPDPEGA-AQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1228 GSEANLPPLPvQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAP--ALLEIPTDRPRPSVQRYAGDQVPfhLDAGQLRRL 1305
Cdd:cd19533 158 GRPAPPAPFG-SFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPepVSLARRAPGRSLAFLRRTAELPP--ELTRTLLEA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1306 HALNRQQGTTLFMTLLAAWsvvLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALR--TEPGRchAVADLLDQVRE 1383
Cdd:cd19533 235 AEAHGASWPSFFIALVAAY---LHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRltVDPQQ--TFAELVAQVSR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1384 RALDAYAHQALPFEQVVEILQPARSLsySPIFQVmlSLNNTPAQaltlPDLTLSAVERPQHsTHF-----DLSLSLIET- 1457
Cdd:cd19533 310 ELRSLLRHQRYRYEDLRRDLGLTGEL--HPLFGP--TVNYMPFD----YGLDFGGVVGLTH-NLSsgptnDLSIFVYDRd 380
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 641744967 1458 -ENGLNGGLVYATDLFDRETILRvvgYVENILMAMADDVTQP 1498
Cdd:cd19533 381 dESGLRIDFDANPALYSGEDLAR---HQERLLRLLEEAAADP 419
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
2631-3092 |
7.55e-53 |
|
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: 193.75 E-value: 7.55e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2631 SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQ 2710
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2711 sahlgimngslpvillddGETRPFDNEPDtpldarkqgltPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGI 2790
Cdd:cd05903 81 ------------------ERFRQFDPAAM-----------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2791 AQEDVLLGVTSLSFDI-SILEIFLPLLNGARLILATQAQAADAQQlamLIERHAVSFMQATPSTWRMLVELRDFA---LP 2866
Cdd:cd05903 132 GPGDVFLVASPMAHQTgFVYGFTLPLLLGAPVVLQDIWDPDKALA---LMREHGVTFMMGATPFLTDLLNAVEEAgepLS 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2867 PGFKALCGGEALPENL----ATALLQKVTTLWnlyGPTETtiwSTLNGLTTPTPYI------GHPIANTQIYILDAQGRV 2936
Cdd:cd05903 209 RLRTFVCGGATVPRSLarraAELLGAKVCSAY---GSTEC---PGAVTSITPAPEDrrlytdGRPLPGVEIKVVDDTGAT 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2937 VPLGVAGEIHIAGAGVVRGYLGRPDLTAErfitdpfsgAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGE 3016
Cdd:cd05903 283 LAPGVEGELLSRGPSVFLGYLDRPDLTAD---------AAPEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLE 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 3017 IETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLS-EGVAEYMIPSAFVTLDAFPLTPNGKL 3092
Cdd:cd05903 354 VEDLLLGHPGVIEAAVVALPDERLGERACAVVVTKSGALLTFDELVAYLDrQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1555-2021 |
1.07e-51 |
|
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: 190.34 E-value: 1.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1555 TYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTqan 1634
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1635 qralltgdvprillDTADfshlsednphvpgldahHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVL 1714
Cdd:cd05971 85 --------------DGSD-----------------DPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDL 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1715 QKTPFS-------FDVsvweFFWPLLYGARLVMARPDGHkDAAYLAQLIERTGITTLHFVPSML----QQFVQWADADCa 1783
Cdd:cd05971 134 YWTPADwawigglLDV----LLPSLYFGVPVLAHRMTKF-DPKAALDLMSRYGVTTAFLPPTALkmmrQQGEQLKHAQV- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1784 cdSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTfwacqpdDHRSFVPI-----GRPIANTQLYILDTLG 1858
Cdd:cd05971 208 --KLRAIATGGESLGEELLGWAREQFGVEVNEFYGQTECNLVIG-------NCSALFPIkpgsmGKPIPGHRVAIVDDNG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1859 QPVPLGVAGElhiggVGVAR-------GYLNRPDLTAERFIPDPFinqpgarlyKTGDLARWLPDGSLEYLGRNDFQVKL 1931
Cdd:cd05971 279 TPLPPGEVGE-----IAVELpdpvaflGYWNNPSATEKKMAGDWL---------LTGDLGRKDSDGYFWYVGRDDDVITS 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1932 RGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPA---DLRQQLGQHLAEYMVPGAFVTLDAF 2008
Cdd:cd05971 345 SGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEFVNEL 424
|
490
....*....|...
gi 641744967 2009 PLTPNGKLDRKAL 2021
Cdd:cd05971 425 PRTATGKIRRREL 437
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
2161-2573 |
1.26e-51 |
|
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: 189.05 E-value: 1.26e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2161 IYPLAPLQEGILFHHLlqEQGDTYLLRSMVAFthRERLDA--FLSALQQVIDRHDILRTA-VCWQDLSQPVQVVWRQAIL 2237
Cdd:cd19542 1 IYPCTPMQEGMLLSQL--RSPGLYFNHFVFDL--DSSVDVerLRNAWRQLVQRHDILRTVfVESSAEGTFLQVVLKSLDP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2238 PINHFEptSPEDVLAQlqaHTEPRTRRIDLSQAPLFRADIAHDPlQNEWLLALSFHHLISDHMTLALIVGEIRLLLQHQA 2317
Cdd:cd19542 77 PIEEVE--TDEDSLDA---LTRDLLDDPTLFGQPPHRLTLLETS-SGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2318 daLPTPLPYRNFIAQTLSVPNSAHEAYFRDKLADVdEPTAPFGLLNVQGSGGDIHearlVLDATLASaIRQQARHLGVSP 2397
Cdd:cd19542 151 --LPPAPPFSDYISYLQSQSQEESLQYWRKYLQGA-SPCAFPSLSPKRPAERSLS----STRRSLAK-LEAFCASLGVTL 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2398 GVLFHVAWAQVLAQTSGRDDVVFGSVLLGRLAGAEGADRIMGMFINTLPLRISLA-DRGAAEVVERTSHDLMTLLEHEQA 2476
Cdd:cd19542 223 ASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDpDWTVLDLLRQLQQQYLRSLPHQHL 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2477 PLALAQRCSGVAPPMPLFSTLLNYRHTQA--SSTDNTLSDIRVLTSEERTNYPLTLAVDDRGEGFSLVAQTLEDIDPHRL 2554
Cdd:cd19542 303 SLREIQRALGLWPSGTLFNTLVSYQNFEAspESELSGSSVFELSAAEDPTEYPVAVEVEPSGDSLKVSLAYSTSVLSEEQ 382
|
410
....*....|....*....
gi 641744967 2555 LNYLMTAISSLVDALETEP 2573
Cdd:cd19542 383 AEELLEQFDDILEALLANP 401
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
488-963 |
2.76e-51 |
|
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: 189.04 E-value: 2.76e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 488 EAIAVLFEDQHLTYRELNRRANQLAHHLIALG-VQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYIL 566
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 567 DDAAPvalltqsaqvaqlnstlpTVLLDtpaaaacpdtnpvvqglhaahLAYVIYTSGSTGRPKGVMVAHRNVINLATGL 646
Cdd:cd05941 81 TDSEP------------------SLVLD---------------------PALILYTSGTTGRPKGVVLTHANLAANVRAL 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 647 ----------HTLLALD----HPSRIALNASivfdasvknwiqLLSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTP 712
Cdd:cd05941 122 vdawrwteddVLLHVLPlhhvHGLVNALLCP------------LFAGASVEFLP---KFDPKEVAISRLMPSITVFMGVP 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 713 ------VQLQWLLDAGLGSDPAYQPAQVLI---GGEAISPAVWSRLQSLSDTRFINVYGPTEcTVDATACVVDRTQPLPT 783
Cdd:cd05941 187 tiytrlLQYYEAHFTDPQFARAAAAERLRLmvsGSAALPVPTLEEWEAITGHTLLERYGMTE-IGMALSNPLDGERRPGT 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 784 IGKPLANTRLYILDAQ-DQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNID 862
Cdd:cd05941 266 VGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW--------FKTGDLGVVDEDGYYW 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 863 YLGR-NDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAE-LHPAALRQQLAASLADYMI 940
Cdd:cd05941 338 ILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAaLSLEELKEWAKQRLAPYKR 417
|
490 500
....*....|....*....|...
gi 641744967 941 PSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05941 418 PRRLILVDELPRNAMGKVNKKEL 440
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1520-2021 |
5.80e-51 |
|
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: 189.46 E-value: 5.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1520 TEADFPHDALIHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAIL 1599
Cdd:cd05920 7 RAAGYWQDEPLGDLLARSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1600 KAGAAYVPLDPGYPAERLAYMLDDASPVALLTQANQRalltGDVPRilldtADFSHLSEDNPHVpgldahhlAYVIYTSG 1679
Cdd:cd05920 87 RLGAVPVLALPSHRRSELSAFCAHAEAVAYIVPDRHA----GFDHR-----ALARELAESIPEV--------ALFLLSGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1680 STGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTP--FSFDVSVWEFFWPLLYGARLVMArPDGHKDAAYlaQLIE 1757
Cdd:cd05920 150 TTGTPKLIPRTHNDYAYNVRASAEVCGLDQDTVYLAVLPaaHNFPLACPGVLGTLLAGGRVVLA-PDPSPDAAF--PLIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1758 RTGITTLHFVPSMLQQFVQ---WADADCAcdSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTfwacQPD 1834
Cdd:cd05920 227 REGVTVTALVPALVSLWLDaaaSRRADLS--SLRLLQVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYT----RLD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1835 D--HRSFVPIGRPI-ANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLA 1911
Cdd:cd05920 301 DpdEVIIHTQGRPMsPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF--------YRTGDLV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1912 RWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPgVTPDPADLRQQL-G 1990
Cdd:cd05920 373 RRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD-PPPSAAQLRRFLrE 451
|
490 500 510
....*....|....*....|....*....|.
gi 641744967 1991 QHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05920 452 RGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
483-963 |
6.43e-51 |
|
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: 189.46 E-value: 6.43e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERL 562
Cdd:cd05920 25 AARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 563 AYILDDAAPVALLtqsaqVAQLNSTLPTVLLDTPAAAACPDTnpvvqglhaahlAYVIYTSGSTGRPKGVMVAHRNVINL 642
Cdd:cd05920 105 SAFCAHAEAVAYI-----VPDRHAGFDHRALARELAESIPEV------------ALFLLSGGTTGTPKLIPRTHNDYAYN 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 643 ATGLHTLLALDHPSR--IALNASIVFDASVKNWI-QLLSGHTLVLVPDALRADAHQLwryFARHAVDLFDCTPVQLQWLL 719
Cdd:cd05920 168 VRASAEVCGLDQDTVylAVLPAAHNFPLACPGVLgTLLAGGRVVLAPDPSPDAAFPL---IEREGVTVTALVPALVSLWL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 720 DAGLGSDPAYQPAQVL-IGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATAC-----VVDRTQplptiGKPL-ANTR 792
Cdd:cd05920 245 DAAASRRADLSSLRLLqVGGARLSPALARRVPPVLGCTLQQVFGMAEGLLNYTRLddpdeVIIHTQ-----GRPMsPDDE 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 793 LYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQIK 872
Cdd:cd05920 320 IRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF--------YRTGDLVRRTPDGYLVVEGRIKDQIN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 873 VRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARpDAELHPAALRQQL-AASLADYMIPSAFVTLDALP 951
Cdd:cd05920 392 RGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR-DPPPSAAQLRRFLrERGLAAYKLPDRIEFVDSLP 470
|
490
....*....|..
gi 641744967 952 LTPNGKLDRKAL 963
Cdd:cd05920 471 LTAVGKIDKKAL 482
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
2631-3092 |
7.40e-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: 7.40e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2631 SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQ 2710
Cdd:cd05911 10 ELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2711 SAHL----GIMNGSLP---VILLDDGE---------TRPFDNEPDTPLDARKqGLTPRHLAYVIYTSGSTGKPKGVMVEH 2774
Cdd:cd05911 90 PDGLekvkEAAKELGPkdkIIVLDDKPdgvlsiedlLSPTLGEEDEDLPPPL-KDGKDDTAAILYSSGTTGLPKGVCLSH 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2775 ANMVN--FLCSMRKEPGIAQEDVLLGVTSLsFDISILEIFL-PLLNGARLILatqAQAADAQQLAMLIERHAVSFMQATP 2851
Cdd:cd05911 169 RNLIAnlSQVQTFLYGNDGSNDVILGFLPL-YHIYGLFTTLaSLLNGATVII---MPKFDSELFLDLIEKYKITFLYLVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2852 STWRMLVE---LRDFALPPGFKALCGGEALPENLAtALLQKVTTLWNL---YGPTETTIWSTLNGLTTPTP-YIGHPIAN 2924
Cdd:cd05911 245 PIAAALAKsplLDKYDLSSLRVILSGGAPLSKELQ-ELLAKRFPNATIkqgYGMTETGGILTVNPDGDDKPgSVGRLLPN 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2925 TQIYILDAQGR-VVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDF 3003
Cdd:cd05911 324 VEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW--------LHTGDIGYFDEDGYLYIVDRKKE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3004 QVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEY------MIpsa 3077
Cdd:cd05911 396 LIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVRKPGEKLTEKEVKDYVAKKVASYkqlrggVV--- 472
|
490
....*....|....*
gi 641744967 3078 FVtlDAFPLTPNGKL 3092
Cdd:cd05911 473 FV--DEIPKSASGKI 485
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1533-2017 |
8.08e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 190.48 E-value: 8.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1533 LVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGY 1612
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1613 PAERLAYMLDDASPVALLTQ-------ANQRALLTGdvPRILLDTADFSHLSEDNPHVPGLDAhhLA------------- 1672
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYErefaprvAEVLPRLPK--LRTLVVVEDGSGNDLLPGAVDYEDA--LAagsperdfgersp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1673 ---YVIYTSGSTGKPKGVMNSH----RALCNRLVWMQNTYRLTPDDRVLQKT-----------PFSFDVSVWEFFWPLLY 1734
Cdd:PRK07798 164 ddlYLLYTGGTTGMPKGVMWRQedifRVLLGGRDFATGEPIEDEEELAKRAAagpgmrrfpapPLMHGAGQWAAFAALFS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1735 GARLVMArPDGHKDAAYLAQLIERTGITTLHFV------PsMLQQFVQWADADCAcdSLRRVICSGEALPAELQQRFFAR 1808
Cdd:PRK07798 244 GQTVVLL-PDVRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEARGPYDLS--SLFAIASGGALFSPSVKEALLEL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1809 F-NAQLHNLYGPTEA---AIDVTFWACQPDDHRSFvPIGRPIAntqlyILDTLGQPVPLG--VAGELHIGGVgVARGYLN 1882
Cdd:PRK07798 320 LpNVVLTDSIGSSETgfgGSGTVAKGAVHTGGPRF-TIGPRTV-----VLDEDGNPVEPGsgEIGWIARRGH-IPLGYYK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1883 RPDLTAERFipdPFINqpGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDS 1962
Cdd:PRK07798 393 DPEKTAETF---PTID--GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDE 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 1963 PGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLD 2017
Cdd:PRK07798 468 RWGQEVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1538-2016 |
9.44e-51 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 189.76 E-value: 9.44e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERL 1617
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1618 AYMLDDASPVALLTQANQRALL-------------------TGDVPRILLDTADFSHLSEDNPHVPGLDAHHLAYVIYTS 1678
Cdd:PRK08316 101 AYILDHSGARAFLVDPALAPTAeaalallpvdtlilslvlgGREAPGGWLDFADWAEAGSVAEPDVELADDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1679 GSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPF----SFDVsvweFFWPLLY-GAR-LVMARPdghkDAAYL 1752
Cdd:PRK08316 181 GTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPLyhcaQLDV----FLGPYLYvGATnVILDAP----DPELI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1753 AQLIERTGITTLhFVP-----SMLQ--QFvqwADADCAcdSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAI 1824
Cdd:PRK08316 253 LRTIEAERITSF-FAPptvwiSLLRhpDF---DTRDLS--SLRKGYYGASIMPVEVLKELRERLpGLRFYNCYGQTEIAP 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1825 DVTfwACQPDDH-RSFVPIGRPIANTQLYILDTLGQPVPLGVAGELhiggvgVAR------GYLNRPDLTAERFIPDPFi 1897
Cdd:PRK08316 327 LAT--VLGPEEHlRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEI------VHRspqlmlGYWDDPEKTAEAFRGGWF- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1898 nqpgarlyKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPG 1977
Cdd:PRK08316 398 --------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG 469
|
490 500 510
....*....|....*....|....*....|....*....
gi 641744967 1978 VTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKL 2016
Cdd:PRK08316 470 ATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1554-2021 |
1.23e-50 |
|
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: 186.77 E-value: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTqa 1633
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1634 nqralltgdvprilldtadfshlsednphvpglDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRV 1713
Cdd:cd05972 79 ---------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDDIH 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1714 LQKTPFSFDVSVW-EFFWPLLYGARLVMARPDGHKDAAYLaQLIERTGITTLHFVPSMLQQFVQWADADCACDSLRRVIC 1792
Cdd:cd05972 126 WNIADPGWAKGAWsSFFGPWLLGATVFVYEGPRFDAERIL-ELLERYGVTSFCGPPTAYRMLIKQDLSSYKFSHLRLVVS 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1793 SGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTFWACQPDDHRSfvpIGRPIANTQLYILDTLGQPVPLGVAGEL--H 1870
Cdd:cd05972 205 AGEPLNPEVIEWWRAATGLPIRDGYGQTETGLTVGNFPDMPVKPGS---MGRPTPGYDVAIIDDDGRELPPGEEGDIaiK 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1871 IGGVGVARGYLNRPDLTAERFIPDpfinqpgarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPG 1950
Cdd:cd05972 282 LPPPGLFLGYVGDPEKTEASIRGD---------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALLEHPA 352
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 1951 VQEAVVVAREDsPGDTRLV-AYLCPQPGVTPDPA---DLRQQLGQHLAEYMVPG--AFVtlDAFPLTPNGKLDRKAL 2021
Cdd:cd05972 353 VAEAAVVGSPD-PVRGEVVkAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPReiEFV--EELPKTISGKIRRVEL 426
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
2158-2592 |
1.48e-50 |
|
Condensation domain; This domain is found in many multi-domain enzymes which synthesize peptide antibiotics. This domain catalyzes a condensation reaction to form peptide bonds in non- ribosomal peptide biosynthesis. It is usually found to the carboxy side of a phosphopantetheine binding domain (pfam00550). It has been shown that mutations in the HHXXXDG motif abolish activity suggesting this is part of the active site.
Pssm-ID: 395541 [Multi-domain] Cd Length: 454 Bit Score: 187.54 E-value: 1.48e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2158 IQDIYPLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCWQDLSQPVQVVWRQA-- 2235
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERpf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2236 ---ILPINHFEPTSPEDVLAQLQahTEPRTRRIDLSQAPLFRADIaHDPLQNEWLLALSFHHLISDHMTLALIVGEIRLL 2312
Cdd:pfam00668 81 eleIIDISDLSESEEEEAIEAFI--QRDLQSPFDLEKGPLFRAGL-FRIAENRHHLLLSMHHIIVDGVSLGILLRDLADL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2313 LQHQADALPTPLP----YRNFIAQTLSVPNSA----HEAYFRDKLADVDEPTApfgLLNV----QGSGGDIHEARLVLDA 2380
Cdd:pfam00668 158 YQQLLKGEPLPLPpktpYKDYAEWLQQYLQSEdyqkDAAYWLEQLEGELPVLQ---LPKDyarpADRSFKGDRLSFTLDE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2381 TLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRlaGAEGADRIMGMFINTLPLRI-SLADRGAAEV 2459
Cdd:pfam00668 235 DTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR--PSPDIERMVGMFVNTLPLRIdPKGGKTFSEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2460 VERTSHDLMTLLEHEQAPLALAQRCSGV---APPMPLFSTLL---NYRHTQASSTDNTLS--DIRVLTS-EERTNYPLTL 2530
Cdd:pfam00668 313 IKRVQEDLLSAEPHQGYPFGDLVNDLRLprdLSRHPLFDPMFsfqNYLGQDSQEEEFQLSelDLSVSSViEEEAKYDLSL 392
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 2531 AVDDRGEGFSL--VAQT----LEDIDphRLLNYLMTAISSLVDALEtEPQRSILnlpVLPDSERQQML 2592
Cdd:pfam00668 393 TASERGGGLTIkiDYNTslfdEETIE--RFAEHFKELLEQAIAHPS-QPLSELD---LLSDAEKQKLL 454
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
28-436 |
2.05e-50 |
|
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: 185.59 E-value: 2.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 28 IYPLAPLQEGILFhyQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICWQGLHQP-VQVVWRQAPLTV 106
Cdd:cd19542 1 IYPCTPMQEGMLL--SQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAEGTfLQVVLKSLDPPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 107 NTLTTTSsdtvpAQLRAATDPSNHRLNLSNAPLLSATTAHDPVcGEWLLSLSIHHLISDHITQALIIDEIRLLLEDRPea 186
Cdd:cd19542 79 EEVETDE-----DSLDALTRDLLDDPTLFGQPPHRLTLLETSS-GEVYLVLRISHALYDGVSLPIILRDLAAAYNGQL-- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 187 LPKPLPYRNFIAQILSVPLSEHEQYFRNRLADIdTPTAPFDLVDVQGngediTEARLSLDSSLADALRRQARHLGISSSV 266
Cdd:cd19542 151 LPPAPPFSDYISYLQSQSQEESLQYWRKYLQGA-SPCAFPSLSPKRP-----AERSLSSTRRSLAKLEAFCASLGVTLAS 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 267 LFHVAWAQVLALTSGRDDVVFGSVLSGRLQGNLGADRVMGMFINTLPLRVSL-RERSVHDVVQATSHELMMLLAHEQAPL 345
Cdd:cd19542 225 LFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLdPDWTVLDLLRQLQQQYLRSLPHQHLSL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 346 ALAQQCSQVPPPLPLFSTLFNYRHSQKDASSQFWEG--MRQLSGRERTNYPITLSVDDLGDG--FNLTAKT-VMGVD-PE 419
Cdd:cd19542 305 REIQRALGLWPSGTLFNTLVSYQNFEASPESELSGSsvFELSAAEDPTEYPVAVEVEPSGDSlkVSLAYSTsVLSEEqAE 384
|
410
....*....|....*..
gi 641744967 420 RIVHYMLTAIENLVTSL 436
Cdd:cd19542 385 ELLEQFDDILEALLANP 401
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
491-963 |
2.12e-50 |
|
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: 186.51 E-value: 2.12e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 491 AVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAA 570
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 571 PVALLTqsaqvaqlnstlptvlldtpaaaacpdtnpvvqglHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHT-L 649
Cdd:cd05919 83 ARLVVT-----------------------------------SADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAReA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 650 LALDHPSRIALNASIVFDASVKN--WIQLLSGHTLVLVPDALRADAhqLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDP 727
Cdd:cd05919 128 LGLTPGDRVFSSAKMFFGYGLGNslWFPLAVGASAVLNPGWPTAER--VLATLARFRPTVLYGVPTFYANLLDSCAGSPD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 728 AYQPAQVLI-GGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPlPTIGKPLANTRLYILDAQDQPVPIG 806
Cdd:cd05919 206 ALRSLRLCVsAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSNRPGAWRL-GSTGRPVPGYEIRLVDEEGHTIPPG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 807 VTGELHIGGAGVARGYLHRPDLTAERFipdpfsadpAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESR 886
Cdd:cd05919 285 EEGDLLVRGPSAAVGYWNNPEKSRATF---------NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPVEVESL 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 887 LLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDA---ELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05919 356 IIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAapqESLARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
2621-3097 |
6.28e-50 |
|
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: 185.19 E-value: 6.28e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2621 DAIAVVFGEASLSYDELNRRANRLAHHLI-SFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALISqsahlgimngslpvillddgetrpfdnepdtpldarkqgltprhLAYVIYTSGSTGKPKGVMVEHANMVN 2779
Cdd:cd05941 81 TDSEPSLVLD--------------------------------------------PALILYTSGTTGRPKGVVLTHANLAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2780 FLCSMRKEPGIAQEDVLLGVTSLsFDIS--ILEIFLPLLNGARLILATQAQAADAQQLAMliERHAVSFMqATPSTWRML 2857
Cdd:cd05941 117 NVRALVDAWRWTEDDVLLHVLPL-HHVHglVNALLCPLFAGASVEFLPKFDPKEVAISRL--MPSITVFM-GVPTIYTRL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2858 VELRDFALPPGFKAL-----------CGGEALPENLaTALLQKVT--TLWNLYGPTETtiwstlnGLTTPTPY------- 2917
Cdd:cd05941 193 LQYYEAHFTDPQFARaaaaerlrlmvSGSAALPVPT-LEEWEAITghTLLERYGMTEI-------GMALSNPLdgerrpg 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2918 -IGHPIANTQIYILDAQ-GRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTL 2995
Cdd:cd05941 265 tVGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW--------FKTGDLGVVDEDGYY 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2996 EYLGR-NDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPD-TVLEPADLRQRLSEGVAEYM 3073
Cdd:cd05941 337 WILGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGaAALSLEELKEWAKQRLAPYK 416
|
490 500
....*....|....*....|....
gi 641744967 3074 IPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05941 417 RPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1534-2021 |
8.64e-50 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 186.22 E-value: 8.64e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1534 VEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLI-DLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGY 1612
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1613 PAERLAYMLDDASPVALLTQ---ANQRALLTGDV----PRILLDTADFSHLSEDNPHVPGLDAHHLayVIYTSGSTGKPK 1685
Cdd:PRK06839 88 TENELIFQLKDSGTTVLFVEktfQNMALSMQKVSyvqrVISITSLKEIEDRKIDNFVEKNESASFI--ICYTSGTTGKPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1686 G-VMNSHRALCNRLvwmQNTYR--LTPDDRVLQKTPFSFDVSVWEFFWP-LLYGARLVMARpdgHKDAAYLAQLIERTGI 1761
Cdd:PRK06839 166 GaVLTQENMFWNAL---NNTFAidLTMHDRSIVLLPLFHIGGIGLFAFPtLFAGGVIIVPR---KFEPTKALSMIEKHKV 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1762 TTLHFVPSMLQQFVQWAD-ADCACDSLRRVICSGEALPAELQQRFFARfNAQLHNLYGPTEAAIDVtFWACQPDDHRSFV 1840
Cdd:PRK06839 240 TVVMGVPTIHQALINCSKfETTNLQSVRWFYNGGAPCPEELMREFIDR-GFLFGQGFGMTETSPTV-FMLSEEDARRKVG 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1841 PIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERfIPDPFINqpgarlykTGDLARWLPDGSLE 1920
Cdd:PRK06839 318 SIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGWLC--------TGDLARVDEDGFVY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1921 YLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPG 2000
Cdd:PRK06839 389 IVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKIPK 468
|
490 500
....*....|....*....|.
gi 641744967 2001 AFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK06839 469 EIVFLKELPKNATGKIQKAQL 489
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1068-1494 |
9.05e-50 |
|
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: 184.19 E-value: 9.05e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1068 LPLSFSQQRLWFLAQLDPAASqAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDTLGFSLS 1147
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGS-VYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1148 SHDLRKLDEAarTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLL-LTQHHIISDGWSIGILARELAALYQAAL 1226
Cdd:cd19536 81 ELDLTPLEEQ--LDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1227 EGSEANLPPlPVQYADYAVWQR-QWLQGETLNdlrdYWRDQLQGA-----PALLEIPTDRP-RPSVQRyagdqVPFHLDA 1299
Cdd:cd19536 159 EYKPLSLPP-AQPYRDFVAHERaSIQQAASER----YWREYLAGAtlatlPALSEAVGGGPeQDSELL-----VSVPLPV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1300 gqlrRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQ--ELEGMVGFFVNTLALRTEPGRcHAVADL 1377
Cdd:cd19536 229 ----RSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEEttGAERLLGLFLNTLPLRVTLSE-ETVEDL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1378 LDQVRERALDAYAHQALPfeqVVEILQPARSLsysPIFQVMLSLNNTP-AQALTLPDLTLSAVERPQHS---THFDLSLS 1453
Cdd:cd19536 304 LKRAQEQELESLSHEQVP---LADIQRCSEGE---PLFDSIVNFRHFDlDFGLPEWGSDEGMRRGLLFSefkSNYDVNLS 377
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 641744967 1454 LIETENGLNGGLVYATDLFDRETILRVVGYVENILMAMADD 1494
Cdd:cd19536 378 VLPKQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATA 418
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
506-963 |
1.40e-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: 184.57 E-value: 1.40e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 506 RRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAA----YVPMDPAYPAERLAYILDDAAPVALLTQSAQV 581
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 582 AQLNSTL-----PTVLLDTPAAAACPDTNPVVQGLHAaHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPS 656
Cdd:cd05922 81 DRLRDALpaspdPGTVLDADGIRAARASAPAHEVSHE-DLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 657 RIALNASIVFDA--SVKNwIQLLSGHTLVLVPDALRADAhqLWRYFARHAVDLFDCTPVQLQWLLDAGLgsDPAYQP--- 731
Cdd:cd05922 160 RALTVLPLSYDYglSVLN-THLLRGATLVLTNDGVLDDA--FWEDLREHGATGLAGVPSTYAMLTRLGF--DPAKLPslr 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 732 --AQVligGEAISPAVWSRLQSL-SDTRFINVYGPTECTVDATACVVDRTQPLPT-IGKPLANTRLYILDAQDQPVPIGV 807
Cdd:cd05922 235 ylTQA---GGRLPQETIARLRELlPGAQVYVMYGQTEATRRMTYLPPERILEKPGsIGLAIPGGEFEILDDDGTPTPPGE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 808 TGELHIGGAGVARGYLHRPdltaeRFIPDPfsADPAARIYkTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRL 887
Cdd:cd05922 312 PGEIVHRGPNVMKGYWNDP-----PYRRKE--GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAA 383
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 888 LRCPGVQDAVVIAREDSPGDtRLVayLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05922 384 RSIGLIIEAAAVGLPDPLGE-KLA--LFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
479-963 |
2.13e-49 |
|
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: 186.12 E-value: 2.13e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 479 FEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVpMdpAYP 558
Cdd:COG1021 31 LRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGAIPV-F--ALP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 559 AER---LAYILDDAAPVALLTQS-----------AQVAQLNSTLPTV--------------LLDTPAAAACPDTNPvvqg 610
Cdd:COG1021 108 AHRraeISHFAEQSEAVAYIIPDrhrgfdyralaRELQAEVPSLRHVlvvgdageftsldaLLAAPADLSEPRPDP---- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 611 lhaAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSR------IALNASI----VFDAsvknwiqLLSGH 680
Cdd:COG1021 184 ---DDVAFFQLSGGTTGLPKLIPRTHDDYLYSVRASAEICGLDADTVylaalpAAHNFPLsspgVLGV-------LYAGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 681 TLVLVPDAlraDAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVL-IGGEAISPAVWSRLQSLSDTRFIN 759
Cdd:COG1021 254 TVVLAPDP---SPDTAFPLIERERVTVTALVPPLALLWLDAAERSRYDLSSLRVLqVGGAKLSPELARRVRPALGCTLQQ 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 760 VYGPTE----CT-VDATACVVDRTQplptiGKPLAN---TRlyILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAE 831
Cdd:COG1021 331 VFGMAEglvnYTrLDDPEEVILTTQ-----GRPISPddeVR--IVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNAR 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 832 RFIPDPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLV 911
Cdd:COG1021 404 AFTPDGF--------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYLGERSC 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 641744967 912 AYLCARpDAELHPAALRQQLAAS-LADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:COG1021 476 AFVVPR-GEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1554-2021 |
4.69e-49 |
|
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: 182.29 E-value: 4.69e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQA 1633
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1634 NQralltgdvprilldtadfshlsEDnphvpgldahhLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRV 1713
Cdd:cd05935 82 EL----------------------DD-----------LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSDVI 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1714 LQKTPFsFDVS--VWEFFWPLLYGARLV-MARPDghKDAAylAQLIERTGITTLHFVPSMLQQFV---QWADADCAcdSL 1787
Cdd:cd05935 129 LACLPL-FHVTgfVGSLNTAVYVGGTYVlMARWD--RETA--LELIEKYKVTFWTNIPTMLVDLLatpEFKTRDLS--SL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1788 RRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTFwacQPDDHRSFVPIGRPIANTQLYILD-TLGQPVPLGVA 1866
Cdd:cd05935 202 KVLTGGGAPMPPAVAEKLLKLTGLRFVEGYGLTETMSQTHT---NPPLRPKLQCLGIP*FGVDARVIDiETGRELPPNEV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1867 GELHIGGVGVARGYLNRPDLTAERFIPDPfinqpGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLM 1946
Cdd:cd05935 279 GEIVVRGPQIFKGYWNRPEETEESFIEIK-----GRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLY 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 1947 QCPGVQEAVVVAREDSPGDTRLVAYLCPQPGV--TPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05935 354 KHPAI*EVCVISVPDERVGEEVKAFIVLRPEYrgKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
2620-3097 |
6.45e-49 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 184.34 E-value: 6.45e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:PRK07656 19 GDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALISQSAHLGI---MNGSLP----VILLDDGETRPFDNEPDT--------PLDARKQGLTPRHLAYVIYTSGST 2764
Cdd:PRK07656 99 ARGDAKALFVLGLFLGVdysATTRLPalehVVICETEEDDPHTEKMKTftdflaagDPAERAPEVDPDDVADILFTSGTT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2765 GKPKGVMVEHANMVNflcsmrkepgiAQEDV--LLGVTSLSFDISILEIF----------LPLLNGARLILATQAQAADA 2832
Cdd:PRK07656 179 GRPKGAMLTHRQLLS-----------NAADWaeYLGLTEGDRYLAANPFFhvfgykagvnAPLMRGATILPLPVFDPDEV 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2833 QQlamLIERHAVSFMQATPSTWRML---VELRDFALPPGFKALCGGEALPENLATALLQK--VTTLWNLYGPTETTIWST 2907
Cdd:PRK07656 248 FR---LIETERITVLPGPPTMYNSLlqhPDRSAEDLSSLRLAVTGAASMPVALLERFESElgVDIVLTGYGLSEASGVTT 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2908 LNGL-----TTPTPyIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearMYk 2982
Cdd:PRK07656 325 FNRLdddrkTVAGT-IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW-------LH- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2983 TGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIaredspG--DKRL----VAYLLAQPDTVL 3056
Cdd:PRK07656 396 TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVI------GvpDERLgevgKAYVVLKPGAEL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 641744967 3057 EPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK07656 470 TEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1503-2021 |
1.19e-48 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 184.49 E-value: 1.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1503 PILpDSERRQVMldfnaTEADFPHDALIHQLVEDQAARTPDTTAVL------FEDQHLTYDALNRRANQLAHHLIDLGVK 1576
Cdd:PRK13295 5 AVL-LPPRRAAS-----IAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1577 PDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQANQR-----ALLTG------DVPR 1645
Cdd:PRK13295 79 RGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTFRgfdhaAMARRlrpelpALRH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1646 ILL---DTAD-F-SHLS----EDNPHVPGL------DAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPD 1710
Cdd:PRK13295 159 VVVvggDGADsFeALLItpawEQEPDAPAIlarlrpGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGAD 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1711 DRVLQKTPFSFDVSvweffwpLLYGARL-VMARPDG----HKDAAYLAQLIERTGIT-TLHFVP--SMLQQFVQWADADC 1782
Cdd:PRK13295 239 DVILMASPMAHQTG-------FMYGLMMpVMLGATAvlqdIWDPARAAELIRTEGVTfTMASTPflTDLTRAVKESGRPV 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1783 AcdSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIdVTFWACQPDDHRSFVPIGRPIANTQLYILDTLGQPVP 1862
Cdd:PRK13295 312 S--SLRTFLCAGAPIPGALVERARAALGAKIVSAWGMTENGA-VTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1863 LGVAGELHIGGVGVARGYLNRPDLTAERFipDPFinqpgarlYKTGDLARWLPDGSLEYLGRNDfQVKLRGFR-IELGEI 1941
Cdd:PRK13295 389 AGQIGRLQVRGCSNFGGYLKRPQLNGTDA--DGW--------FDTGDLARIDADGYIRISGRSK-DVIIRGGEnIPVVEI 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1942 EARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLG-QHLAEYMVPGAFVTLDAFPLTPNGKLDRKA 2020
Cdd:PRK13295 458 EALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLKaQKVAKQYIPERLVVRDALPRTPSGKIQKFR 537
|
.
gi 641744967 2021 L 2021
Cdd:PRK13295 538 L 538
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1539-2024 |
2.45e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 182.88 E-value: 2.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1539 ARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLA 1618
Cdd:PRK06188 23 KRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1619 YMLDDASPVALLTQANQ---------------RALLT-GDVPrillDTADFSHLS---EDNPHVPGLDAHHLAYVIYTSG 1679
Cdd:PRK06188 103 YVLEDAGISTLIVDPAPfveralallarvpslKHVLTlGPVP----DGVDLLAAAakfGPAPLVAAALPPDIAGLAYTGG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1680 STGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVweFFWP-LLYGARLVMARpdGHKDAAYLAqLIER 1758
Cdd:PRK06188 179 TTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPtLLRGGTVIVLA--KFDPAEVLR-AIEE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1759 TGITTLHFVPSMLQQFVQWADADCA-CDSLRRVICSGEAL-PAELQQRFfARFNAQLHNLYGPTEAAIDVTFWACQ---P 1833
Cdd:PRK06188 254 QRITATFLVPTMIYALLDHPDLRTRdLSSLETVYYGASPMsPVRLAEAI-ERFGPIFAQYYGQTEAPMVITYLRKRdhdP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1834 DDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFipdpfinqPGARLYkTGDLARW 1913
Cdd:PRK06188 333 DDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF--------RDGWLH-TGDVARE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1914 LPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHL 1993
Cdd:PRK06188 404 DEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERK 483
|
490 500 510
....*....|....*....|....*....|.
gi 641744967 1994 AEYMVPGAFVTLDAFPLTPNGKLDRKALPAP 2024
Cdd:PRK06188 484 GSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1538-2024 |
4.45e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 180.57 E-value: 4.45e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLFEDQHLTYDALNRRANQLAHhlidlGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERL 1617
Cdd:PRK07787 10 AAAADIADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAER 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1618 AYMLDDASPVALLTQANQRAlltGDVPRILLDTADFSHLSEDNPhvpglDAHHLAYVIYTSGSTGKPKGVMNSHRALCNR 1697
Cdd:PRK07787 85 RHILADSGAQAWLGPAPDDP---AGLPHVPVRLHARSWHRYPEP-----DPDAPALIVYTSGTTGPPKGVVLSRRAIAAD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1698 LVWMQNTYRLTPDDRVLQKTPFsFDVS--VWEFFWPLLYGARLV-MARPdghKDAAYLAQLIERTgitTLHF-VPSMLQQ 1773
Cdd:PRK07787 157 LDALAEAWQWTADDVLVHGLPL-FHVHglVLGVLGPLRIGNRFVhTGRP---TPEAYAQALSEGG---TLYFgVPTVWSR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1774 FVqwADADCAcDSLR--RVICSGEA-LPAELQQRFFARFNAQLHNLYGPTEAAIDVTFWAcqpDDHRSFVPIGRPIANTQ 1850
Cdd:PRK07787 230 IA--ADPEAA-RALRgaRLLVSGSAaLPVPVFDRLAALTGHRPVERYGMTETLITLSTRA---DGERRPGWVGLPLAGVE 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1851 LYILDTLGQPVPLGVA--GELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSLEYLGRN--D 1926
Cdd:PRK07787 304 TRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW--------FRTGDVAVVDPDGMHRIVGREstD 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1927 FqVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDpaDLRQQLGQHLAEYMVPGAFVTLD 2006
Cdd:PRK07787 376 L-IKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAAD--ELIDFVAQQLSVHKRPREVRFVD 452
|
490
....*....|....*...
gi 641744967 2007 AFPLTPNGKLDRKALPAP 2024
Cdd:PRK07787 453 ALPRNAMGKVLKKQLLSE 470
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1523-2016 |
5.40e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 182.47 E-value: 5.40e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1523 DFPHDALIHQLvEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLID-LGVKPDDRIAICVERSLDMVIGLLAILKA 1601
Cdd:PRK08314 6 TLPETSLFHNL-EVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1602 GAAYVPLDPGYPAERLAYMLDDA-SPVALLTQ--ANQRALLTGD----------------------VPRILLDTADFSHL 1656
Cdd:PRK08314 85 NAVVVPVNPMNREEELAHYVTDSgARVAIVGSelAPKVAPAVGNlrlrhvivaqysdylpaepeiaVPAWLRAEPPLQAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1657 SEDN---------------PHVPGLDahHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFsF 1721
Cdd:PRK08314 165 APGGvvawkealaaglappPHTAGPD--DLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-F 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1722 DVS--VWEFFWPLLYGARLV-MARPDghKDAAylAQLIERTGITTLHFVPSMLQQF---VQWADADCAcdSLRRVICSGE 1795
Cdd:PRK08314 242 HVTgmVHSMNAPIYAGATVVlMPRWD--REAA--ARLIERYRVTHWTNIPTMVVDFlasPGLAERDLS--SLRYIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1796 ALPAELQQRFFARFNAQLHNLYGPTEAAidvTFWACQPDDHRSFVPIGRPIANTQLYILD-TLGQPVPLGVAGELHIGGV 1874
Cdd:PRK08314 316 AMPEAVAERLKELTGLDYVEGYGLTETM---AQTHSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1875 GVARGYLNRPDLTAERFIPdpfINqpGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEA 1954
Cdd:PRK08314 393 QVFKGYWNRPEATAEAFIE---ID--GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEA 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641744967 1955 VVVAREDSPGDTRLVAYLCPQPG--VTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKL 2016
Cdd:PRK08314 468 CVIATPDPRRGETVKAVVVLRPEarGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1533-2025 |
8.18e-48 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 182.05 E-value: 8.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1533 LVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGY 1612
Cdd:PRK07788 54 LVAHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGF 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1613 PAERLAYMLDDASPVALLTQANQRALLTG---DVPRILLDTADFSHLSEDNPHVPGLD--------------AHHLAYVI 1675
Cdd:PRK07788 134 SGPQLAEVAAREGVKALVYDDEFTDLLSAlppDLGRLRAWGGNPDDDEPSGSTDETLDdliagsstaplpkpPKPGGIVI 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1676 YTSGSTGKPKGVMNSHRALcnrlvwmqntyrLTPDDRVLQKTPF--------------SFDVSVWEFFWPLlyGARLVMA 1741
Cdd:PRK07788 214 LTSGTTGTPKGAPRPEPSP------------LAPLAGLLSRVPFragettllpapmfhATGWAHLTLAMAL--GSTVVLR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1742 RpdgHKDAAYLAQLIERTGITTLHFVPSMLQQFV---QWADADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYG 1818
Cdd:PRK07788 280 R---RFDPEATLEDIAKHKATALVVVPVMLSRILdlgPEVLAKYDTSSLKIIFVSGSALSPELATRALEAFGPVLYNLYG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1819 PTEAAIDVTfwaCQPDDHRsFVP--IGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDltaerfipDPF 1896
Cdd:PRK07788 357 STEVAFATI---ATPEDLA-EAPgtVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRD--------KQI 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1897 INQpgarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQP 1976
Cdd:PRK07788 425 IDG----LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAP 500
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 641744967 1977 GVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPAPD 2025
Cdd:PRK07788 501 GAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2633-3098 |
1.15e-47 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 177.87 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2633 SYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQsa 2712
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVVD-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2713 hlgimngslpvillddgetrpfdnepdtpldarkqgltprhLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQ 2792
Cdd:cd05934 83 -----------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2793 EDVLLGVTSLsFDISILEI-FLP-LLNGARLILATQAQAADAQQLamlIERHAVSFMQATPSTWRMLvelrdFALPPG-- 2868
Cdd:cd05934 122 DDVYLTVLPL-FHINAQAVsVLAaLSVGATLVLLPRFSASRFWSD---VRRYGATVTNYLGAMLSYL-----LAQPPSpd 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2869 -----FKALCGGEALPENLATALLQKVTTLWNLYGPTETT--IWSTLNGlTTPTPYIGHPIANTQIYILDAQGRVVPLGV 2941
Cdd:cd05934 193 drahrLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTETIvgVIGPRDE-PRRPGSIGRPAPGYEVRIVDDDGQELPAGE 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2942 AGEIHIAGA---GVVRGYLGRPDLTAERFitdpfsgapEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIE 3018
Cdd:cd05934 272 PGELVIRGLrgwGFFKGYYNMPEATAEAM---------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3019 TRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALP 3098
Cdd:cd05934 343 RAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
500-963 |
1.21e-47 |
|
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: 178.41 E-value: 1.21e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 500 TYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTqsA 579
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLT--D 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 580 QVAQLNSTLPTVLLDTPAAAACPDTnpVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSR-- 657
Cdd:TIGR01923 79 SLLEEKDFQADSLDRIEAAGRYETS--LSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDNwl 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 658 IAL------NASIVFDAsvknwiqLLSGHTLVlVPDALRADAHQLwryfARHAVDLFDCTPVQLQWLLDAGLgsdPAYQP 731
Cdd:TIGR01923 157 LSLplyhisGLSILFRW-------LIEGATLR-IVDKFNQLLEMI----ANERVTHISLVPTQLNRLLDEGG---HNENL 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 732 AQVLIGGEAISPAVWSRLQSLSDTRFiNVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYIldaqDQPVPIGVtGEL 811
Cdd:TIGR01923 222 RKILLGGSAIPAPLIEEAQQYGLPIY-LSYGMTETCSQVTTATPEMLHARPDVGRPLAGREIKI----KVDNKEGH-GEI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 812 HIGGAGVARGYLHRPDLTAERFIPDPFsadpaariyKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCP 891
Cdd:TIGR01923 296 MVKGANLMKGYLYQGELTPAFEQQGWF---------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHP 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641744967 892 GVQDAVVIAREDSPGDTRLVAYLCARpdAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:TIGR01923 367 GIQEAVVVPKPDAEWGQVPVAYIVSE--SDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1538-2021 |
3.09e-47 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 180.62 E-value: 3.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERL 1617
Cdd:PRK06178 43 ARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHEL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1618 AYMLDDASPVALLTQaNQRALLTGDV--------------------------------PRILL-DTADFSHLSEDNP--- 1661
Cdd:PRK06178 123 SYELNDAGAEVLLAL-DQLAPVVEQVraetslrhvivtsladvlpaeptlplpdslraPRLAAaGAIDLLPALRACTapv 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1662 --HVPGLDAhhLAYVIYTSGSTGKPKGVMNSHRalcnRLVWMQNTY-----RLTPDDRVLQKTPFsfdvsvwefFW---- 1730
Cdd:PRK06178 202 plPPPALDA--LAALNYTGGTTGMPKGCEHTQR----DMVYTAAAAyavavVGGEDSVFLSFLPE---------FWiage 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1731 ------PLLYGARLV-MARpdghKDAAYLAQLIERTGIT-TLHFVPSM--LQQFVQWADADCAcdSLRRVICSG--EALP 1798
Cdd:PRK06178 267 nfgllfPLFSGATLVlLAR----WDAVAFMAAVERYRVTrTVMLVDNAveLMDHPRFAEYDLS--SLRQVRVVSfvKKLN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1799 AELQQRFFARFNAQLHNL-YGPTEAAIDVTFWA-CQPDDHR-SFVPI--GRPIANTQLYILD-TLGQPVPLGVAGELHIG 1872
Cdd:PRK06178 341 PDYRQRWRALTGSVLAEAaWGMTETHTCDTFTAgFQDDDFDlLSQPVfvGLPVPGTEFKICDfETGELLPLGAEGEIVVR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1873 GVGVARGYLNRPDLTAERFIpDPFinqpgarlYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQ 1952
Cdd:PRK06178 421 TPSLLKGYWNKPEATAEALR-DGW--------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVL 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 1953 EAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVtLDAFPLTPNGKLDRKAL 2021
Cdd:PRK06178 492 GSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1545-2021 |
4.42e-47 |
|
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: 176.90 E-value: 4.42e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1545 TAVLFEDQHLTYDALNRRANQLAHHLID-LGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDD 1623
Cdd:cd05958 2 TCLRSPEREWTYRDLLALANRIANVLVGeLGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1624 ASPValltqanqRALLTGDVprilldTAdfshlSEDnphvpgldahhLAYVIYTSGSTGKPKGVMNSHR---ALCNRlvW 1700
Cdd:cd05958 82 ARIT--------VALCAHAL------TA-----SDD-----------ICILAFTSGTTGAPKATMHFHRdplASADR--Y 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1701 MQNTYRLTPDDRVLQKTP--FSFDVSVWEFFwPLLYGARLVM---ARPDGhkdaayLAQLIERTGITTLHFVPSMLQQFV 1775
Cdd:cd05958 130 AVNVLRLREDDRFVGSPPlaFTFGLGGVLLF-PFGVGASGVLleeATPDL------LLSAIARYKPTVLFTAPTAYRAML 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1776 QWADA---DCACdsLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAidVTFWACQPDDHRsfvP--IGRPIANTQ 1850
Cdd:cd05958 203 AHPDAagpDLSS--LRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMF--HIFISARPGDAR---PgaTGKPVPGYE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1851 LYILDTLGQPVPLGVAGELHIGGvgvARGYLNRPDLTAERFIPDPFInqpgarlyKTGDLARWLPDGSLEYLGRNDFQVK 1930
Cdd:cd05958 276 AKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQGGWN--------ITGDTYSRDPDGYFRHQGRSDDMIV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1931 LRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPA---DLRQQLGQHLAEYMVPGAFVTLDA 2007
Cdd:cd05958 345 SGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAKAHIAPYKYPRAIEFVTE 424
|
490
....*....|....
gi 641744967 2008 FPLTPNGKLDRKAL 2021
Cdd:cd05958 425 LPRTATGKLQRFAL 438
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
490-963 |
4.44e-47 |
|
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: 178.72 E-value: 4.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 490 IAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDA 569
Cdd:cd05959 21 TAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDS 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 570 APVALLTQSAQVAQLNS-------TLPTVLLDTPA-------------AAACPDTNPVvqGLHAAHLAYVIYTSGSTGRP 629
Cdd:cd05959 101 RARVVVVSGELAPVLAAaltksehTLVVLIVSGGAgpeagalllaelvAAEAEQLKPA--ATHADDPAFWLYSSGSTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 630 KGVMVAHRNVINLA-TGLHTLLALdHPSRIALNASIVFDA-SVKN--WIQLLSGHTLVLVPDalRADAHQLWRYFARHAV 705
Cdd:cd05959 179 KGVVHLHADIYWTAeLYARNVLGI-REDDVCFSAAKLFFAyGLGNslTFPLSVGATTVLMPE--RPTPAAVFKRIRRYRP 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 706 DLFDCTPVqlqwLLDAGLGSDPAYQPAQVLI-----GGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQP 780
Cdd:cd05959 256 TVFFGVPT----LYAAMLAAPNLPSRDLSSLrlcvsAGEALPAEVGERWKARFGLDILDGIGSTEMLHIFLSNRPGRVRY 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 781 lPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIpdpfsadpaARIYKTGDLARWLPDGN 860
Cdd:cd05959 332 -GTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ---------GEWTRTGDKYVRDDDGF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 861 IDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARP---DAELHPAALRQQLAASLAD 937
Cdd:cd05959 402 YTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPgyeDSEALEEELKEFVKDRLAP 481
|
490 500
....*....|....*....|....*.
gi 641744967 938 YMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05959 482 YKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1537-2021 |
4.96e-47 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 177.85 E-value: 4.96e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1537 QAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAER 1616
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1617 LAYMLDDASPVALLTQANQRALLTGDVPrilldtADFSHLSE-DNPHVPGLDAHHL---AYVIYTSGSTGKPKGVMNSHr 1692
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEAKLIPGIS------VKFAELMNgPKEEAEIQEEFDLdevATIMYTSGTTGKPKGVIQTY- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1693 alcnrlvwmQNTYR----------LTPDDRVLQKTPFsFDVSVWE-FFWPLLYGARLVMARpdgHKDAAYLAQLIERTGI 1761
Cdd:PRK03640 164 ---------GNHWWsavgsalnlgLTEDDCWLAAVPI-FHISGLSiLMRSVIYGMRVVLVE---KFDAEKINKLLQTGGV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1762 TTLHFVPSMLQQFVQWADADCACDSLRRVIC-SGEALPAELQQrffarfnAQLHNL-----YGPTEAAIDVTfwACQPDD 1835
Cdd:PRK03640 231 TIISVVSTMLQRLLERLGEGTYPSSFRCMLLgGGPAPKPLLEQ-------CKEKGIpvyqsYGMTETASQIV--TLSPED 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1836 HRSFV-PIGRPIANTQLYILDTlGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlyKTGDLARWL 1914
Cdd:PRK03640 302 ALTKLgSAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF---------KTGDIGYLD 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1915 PDGSLEYLGRndfqvklRGFRIELG-------EIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCpqPGVTPDPADLRQ 1987
Cdd:PRK03640 372 EEGFLYVLDR-------RSDLIISGgeniypaEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVV--KSGEVTEEELRH 442
|
490 500 510
....*....|....*....|....*....|....
gi 641744967 1988 QLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK03640 443 FCEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2639-3097 |
5.78e-47 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 176.86 E-value: 5.78e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2639 RRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGA----YVPLDPTYPVERLRYMLDDAKP-VALISQSAh 2713
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGrIVLADAGA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2714 lgimngslpVILLDDGETRPFDnePDTPLDAR----KQGLTPRH------LAYVIYTSGSTGKPKGVMVEHANMVNFLCS 2783
Cdd:cd05922 80 ---------ADRLRDALPASPD--PGTVLDADgiraARASAPAHevshedLALLLYTSGSTGSPKLVRLSHQNLLANARS 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2784 MRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLamLIERHAVSFMQATPSTWRMLVEL-RD 2862
Cdd:cd05922 149 IAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWE--DLREHGATGLAGVPSTYAMLTRLgFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2863 FALPPGFKALC-GGEALPENLATALLQKV--TTLWNLYGPTETTIWSTL----NGLTTPTPyIGHPIANTQIYILDAQGR 2935
Cdd:cd05922 227 PAKLPSLRYLTqAGGRLPQETIARLRELLpgAQVYVMYGQTEATRRMTYlppeRILEKPGS-IGLAIPGGEFEILDDDGT 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2936 VVPLGVAGEIHIAGAGVVRGYLGRPdltaeRFITDPfsGAPEARMYkTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELG 3015
Cdd:cd05922 306 PTPPGEPGEIVHRGPNVMKGYWNDP-----PYRRKE--GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPT 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3016 EIETRLARCHGVHDAVVIAREDSPGDkRLVAYLLAQPDtvLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRK 3095
Cdd:cd05922 378 EIEAAARSIGLIIEAAAVGLPDPLGE-KLALFVTAPDK--IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYA 454
|
..
gi 641744967 3096 AL 3097
Cdd:cd05922 455 AL 456
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
477-921 |
9.61e-47 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 179.91 E-value: 9.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 477 QRFEAQAEQTPEAIAVLFED----QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVP 552
Cdd:COG1022 15 DLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 553 MDPAYPAERLAYILDDAAPVALLTQS-AQVAQLNS---TLPT----VLLDTPAAAACPDTNPV----------------- 607
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVEDqEQLDKLLEvrdELPSlrhiVVLDPRGLRDDPRLLSLdellalgrevadpaele 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 608 --VQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSR-------------------IALNASIVF 666
Cdd:COG1022 175 arRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRtlsflplahvfertvsyyaLAAGATVAF 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 667 DASVKNWIQLLSG---HTLVLVP-------DALRADAHQ-------LWRYFARHAVDLFDctpvQLQWLLDAGLGSDPAY 729
Cdd:COG1022 255 AESPDTLAEDLREvkpTFMLAVPrvwekvyAGIQAKAEEagglkrkLFRWALAVGRRYAR----ARLAGKSPSLLLRLKH 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 730 QPAQVLI-----------------GGEAISPAVwsrlqslsdTRF-----INV---YGPTECTvdATACVVDRTQPLP-T 783
Cdd:COG1022 331 ALADKLVfsklrealggrlrfavsGGAALGPEL---------ARFfralgIPVlegYGLTETS--PVITVNRPGDNRIgT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 784 IGKPLANTRlyildaqdqpVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDY 863
Cdd:COG1022 400 VGPPLPGVE----------VKIAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW--------LHTGDIGELDEDGFLRI 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641744967 864 LGRNDFQIKVR-GFRIEAGEIESRLLRCPGVQDAVVIaredspGDTR--LVAYLCarPDAE 921
Cdd:COG1022 462 TGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV------GDGRpfLAALIV--PDFE 514
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
495-963 |
1.81e-46 |
|
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: 177.05 E-value: 1.81e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 495 EDQHLTYRELNRRANQLAHHLIALGVQPDDRVA-LCVE--RSLEMMVGLLGIlkaGAAYVPMDPAYPAERLAYILDDAAP 571
Cdd:cd12119 22 EVHRYTYAEVAERARRLANALRRLGVKPGDRVAtLAWNthRHLELYYAVPGM---GAVLHTINPRLFPEQIAYIINHAED 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 572 VALLTQS---AQVAQLNSTLPTV---LLDTPAAAACPDTNPVV----QGLHAA-----------HLAYVI-YTSGSTGRP 629
Cdd:cd12119 99 RVVFVDRdflPLLEAIAPRLPTVehvVVMTDDAAMPEPAGVGVlayeELLAAEspeydwpdfdeNTAAAIcYTSGTTGNP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 630 KGVMVAHRNVInlatgLHTLlALDHPSRIALNAS-----IVFDASVKNW----IQLLSGHTLVLvPDAlRADAHQLWRYF 700
Cdd:cd12119 179 KGVVYSHRSLV-----LHAM-AALLTDGLGLSESdvvlpVVPMFHVNAWglpyAAAMVGAKLVL-PGP-YLDPASLAELI 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 701 ARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPA-QVLIGGEAISPAVWSRLQSLsDTRFINVYGPTE-CTVDATACVVDRT 778
Cdd:cd12119 251 EREGVTFAAGVPTVWQGLLDHLEANGRDLSSLrRVVIGGSAVPRSLIEAFEER-GVRVIHAWGMTEtSPLGTVARPPSEH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 779 QPLP---------TIGKPLANTRLYILDAQDQPVPI-GVT-GELHIGGAGVARGYLHRPDlTAERFIPDPFsadpaariY 847
Cdd:cd12119 330 SNLSedeqlalraKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDE-ESEALTEDGW--------L 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 848 KTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAAL 927
Cdd:cd12119 401 RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEEL 480
|
490 500 510
....*....|....*....|....*....|....*.
gi 641744967 928 RQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd12119 481 LEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1554-2021 |
4.12e-46 |
|
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: 174.32 E-value: 4.12e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTqa 1633
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1634 nqralltgdvprillDTADfshlsednphvpgldahHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRV 1713
Cdd:cd05907 84 ---------------EDPD-----------------DLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGDRH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1714 LQKTPFS--FDVSVWEFFwPLLYGARLVMARPDghkdaAYLAQLIERTGITTLHFVPSMLQQFV------------QWAD 1779
Cdd:cd05907 132 LSFLPLAhvFERRAGLYV-PLLAGARIYFASSA-----ETLLDDLSEVRPTVFLAVPRVWEKVYaaikvkavpglkRKLF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1780 ADCACDSLRRVICSGEALPAELqQRFFARFNAQLHNLYGPTEAAIDVTFWacQPDDHRsfvpigrpiantqlyiLDTLGQ 1859
Cdd:cd05907 206 DLAVGGRLRFAASGGAPLPAEL-LHFFRALGIPVYEGYGLTETSAVVTLN--PPGDNR----------------IGTVGK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1860 PVP-----LGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSLEYLGR-NDFQVKLRG 1933
Cdd:cd05907 267 PLPgvevrIADDGEILVRGPNVMLGYYKNPEATAEALDADGW--------LHTGDLGEIDEDGFLHITGRkKDLIITSGG 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1934 FRIELGEIEARLMQCPGVQEAVVVaredspGDTR--LVAYLCPQPGVTPDPA-----------------DLRQQLGQHLA 1994
Cdd:cd05907 339 KNISPEPIENALKASPLISQAVVI------GDGRpfLVALIVPDPEALEAWAeehgiaytdvaelaanpAVRAEIEAAVE 412
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 641744967 1995 E--------------YMVPGAFvTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05907 413 AanarlsryeqikkfLLLPEPF-TIENGELTPTLKLKRPVI 452
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1530-2021 |
8.55e-46 |
|
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: 174.62 E-value: 8.55e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFEDQ--HLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVP 1607
Cdd:cd05923 3 VFEMLRRAASRAPDACAIADPARglRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1608 LDPGYPAERLAYML-----------DDASPVALLTQANQRALLTGDVPRILLDTAdFSHLSEDNPHVPGLDahhlAYVIY 1676
Cdd:cd05923 83 INPRLKAAELAELIergemtaaviaVDAQVMDAIFQSGVRVLALSDLVGLGEPES-AGPLIEDPPREPEQP----AFVFY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1677 TSGSTGKPKGVMNSHRALCNRLVWM--QNTYRLTPDDRVLQKTPFSFDVSVWEFF-WPLLYGARLVMARPDghkDAAYLA 1753
Cdd:cd05923 158 TSGTTGLPKGAVIPQRAAESRVLFMstQAGLRHGRHNVVLGLMPLYHVIGFFAVLvAALALDGTYVVVEEF---DPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1754 QLIERTGITTLHFVPSMLQQFVQWAD-ADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTFWACQ 1832
Cdd:cd05923 235 KLIEQERVTSLFATPTHLDALAAAAEfAGLKLSSLRHVTFAGATMPDAVLERVNQHLPGEKVNIYGTTEAMNSLYMRDAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1833 PDDhrsfvpIGRPIANTQLYILDTLGQPV---PLGVAGELHIGGVGVA--RGYLNRPDLTAERFIpdpfinqpgARLYKT 1907
Cdd:cd05923 315 TGT------EMRPGFFSEVRIVRIGGSPDealANGEEGELIVAAAADAafTGYLNQPEATAKKLQ---------DGWYRT 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1908 GDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGvtPDPADLRQ 1987
Cdd:cd05923 380 GDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREG--TLSADELD 457
|
490 500 510
....*....|....*....|....*....|....*.
gi 641744967 1988 Q--LGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05923 458 QfcRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
499-937 |
1.06e-45 |
|
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: 173.17 E-value: 1.06e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQs 578
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 aqvaqlnstlptvlldtpaaaacpdtnpvvqglHAAHLAYVIYTSGSTGRPKGVMVAHRNVI-NLATGLHTLLALDHPSR 657
Cdd:cd05907 85 ---------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILsNALALAERLPATEGDRH 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 658 IA-LNASIVFDASVKNWIQLLSGHTLVLVPDA--LRAD-----------AHQLWR--YFARHAVDlfdcTPVQLQWLLDA 721
Cdd:cd05907 132 LSfLPLAHVFERRAGLYVPLLAGARIYFASSAetLLDDlsevrptvflaVPRVWEkvYAAIKVKA----VPGLKRKLFDL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 722 GLGSDPAYqpaqVLIGGEAISPAVWSRLQSLSDTrFINVYGPTECTvdATACVVDRTQPLP-TIGKPLANTRlyildaqd 800
Cdd:cd05907 208 AVGGRLRF----AASGGAPLPAELLHFFRALGIP-VYEGYGLTETS--AVVTLNPPGDNRIgTVGKPLPGVE-------- 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 801 qpVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLGR-NDFQIKVRGFRIE 879
Cdd:cd05907 273 --VRIADDGEILVRGPNVMLGYYKNPEATAEALDADGW--------LHTGDLGEIDEDGFLHITGRkKDLIITSGGKNIS 342
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 880 AGEIESRLLRCPGVQDAVVIaredspGDTR--LVAYLCARPDAELHPAALRQQLAASLAD 937
Cdd:cd05907 343 PEPIENALKASPLISQAVVI------GDGRpfLVALIVPDPEALEAWAEEHGIAYTDVAE 396
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
1067-1495 |
1.61e-45 |
|
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: 170.83 E-value: 1.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1067 PLPLSFSQQRLWFLAQLDpAASQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQqidpdtlgfSL 1146
Cdd:cd19537 1 DTALSPIEREWWHKYQLS-TGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRR---------SY 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1147 SSHdlrkldeAARTTRVAEL-AEQEARARFDLTQGPLIRGqLLQLDdnthVLLLTQHHIISDGWSIGILARELAALYQAA 1225
Cdd:cd19537 71 SSS-------PPRVQRVDTLdVWKEINRPFDLEREDPIRV-FISPD----TLLVVMSHIICDLTTLQLLLREVSAAYNGK 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1226 LegseanLPPLPVQYADYAVWQRQWLQGEtlndlRDYWRDQLQGAPalleiPTDRPRP-SVQRYAGDQVPFHLDAGQLRR 1304
Cdd:cd19537 139 L------LPPVRREYLDSTAWSRPASPED-----LDFWSEYLSGLP-----LLNLPRRtSSKSYRGTSRVFQLPGSLYRS 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1305 LHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPRQELEGMVGFFVNTLALR--TEPGRCHAVADLLDQVR 1382
Cdd:cd19537 203 LLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRirFPSSSDASAADFLRAVR 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1383 ERALDAYAHqALPFEQVVEILQ-PARSLSYsPIFQVMLS--LNNTPAQALTLPDLTlsaverPQHsTH-----FDLSLSL 1454
Cdd:cd19537 283 RSSQAALAH-AIPWHQLLEHLGlPPDSPNH-PLFDVMVTfhDDRGVSLALPIPGVE------PLY-TWaegakFPLMFEF 353
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 641744967 1455 IETEnglNGGLV----YATDLFDRETILRVVGYVENILMAMADDV 1495
Cdd:cd19537 354 TALS---DDSLLlrleYDTDCFSEEEIDRIESLILAALELLVEGK 395
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
2620-3097 |
2.75e-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: 172.88 E-value: 2.75e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:cd05926 3 APALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALI---------SQSAH--------LGIMNGSLpvILLDDGETRPFDNEPDTPLDARKQGLtPRHLAYVIYTSG 2762
Cdd:cd05926 83 ADLGSKLVLtpkgelgpaSRAASklglaileLALDVGVL--IRAPSAESLSNLLADKKNAKSEGVPL-PDDLALILHTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2763 STGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLsFDISILEIFL--PLLNGARLILATQAqaadaqqlamlie 2840
Cdd:cd05926 160 TTGRPKGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL-FHVHGLVASLlsTLAAGGSVVLPPRF------------- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2841 rHAVSF---MQATPSTWRMLVE-----LRDFALPPGFKAL-------CGGEALPENLATALLQKV-TTLWNLYGPTETTI 2904
Cdd:cd05926 226 -SASTFwpdVRDYNATWYTAVPtihqiLLNRPEPNPESPPpklrfirSCSASLPPAVLEALEATFgAPVLEAYGMTEAAH 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2905 WSTLNglttPTPYIGHPI------ANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapea 2978
Cdd:cd05926 305 QMTSN----PLPPGPRKPgsvgkpVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------ 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2979 rmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEP 3058
Cdd:cd05926 375 --FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVVLREGASVTE 452
|
490 500 510
....*....|....*....|....*....|....*....
gi 641744967 3059 ADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05926 453 EELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1533-2011 |
3.03e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 174.16 E-value: 3.03e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1533 LVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGY 1612
Cdd:PRK06164 15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1613 PAERLAYMLDDASPVALLTQANQRALltgDVPRILLDTADFSHLS----------------------------EDNPHVP 1664
Cdd:PRK06164 95 RSHEVAHILGRGRARWLVVWPGFKGI---DFAAILAAVPPDALPPlraiavvddaadatpapapgarvqlfalPDPAPPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1665 GL-----DAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLV 1739
Cdd:PRK06164 172 AAgeraaDPDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1740 MarpDGHKDAAYLAQLIERTGITtlHFVPS--MLQQFVQWADADCACDSLRRV-----ICSGEALPAELQQRffarfNAQ 1812
Cdd:PRK06164 252 C---EPVFDAARTARALRRHRVT--HTFGNdeMLRRILDTAGERADFPSARLFgfasfAPALGELAALARAR-----GVP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1813 LHNLYGPTEAAIDVTFWACQPDDHRSFVPIGRPI-ANTQLYILDTL-GQPVPLGVAGELHIGGVGVARGYLNRPDLTAER 1890
Cdd:PRK06164 322 LTGLYGSSEVQALVALQPATDPVSVRIEGGGRPAsPEARVRARDPQdGALLPDGESGEIEIRAPSLMRGYLDNPDATARA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1891 FIPDPFinqpgarlYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREdSPGDTRLVA 1970
Cdd:PRK06164 402 LTDDGY--------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT-RDGKTVPVA 472
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 641744967 1971 YLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLT 2011
Cdd:PRK06164 473 FVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVT 513
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1524-2021 |
4.00e-45 |
|
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: 172.80 E-value: 4.00e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1524 FPHDALIHQLVEDQAARTPDTTAvlFED----QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAIL 1599
Cdd:cd05904 1 LPTDLPLDSVSFLFASAHPSRPA--LIDaatgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1600 KAGAAYVPLDPGYPAERLAYMLDDASPVALLTQA-NQRALLTGDVPRILLDTADFSHLSED---------NPHVPGLDAH 1669
Cdd:cd05904 79 SLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAeLAEKLASLALPVVLLDSAEFDSLSFSdllfeadeaEPPVVVIKQD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1670 HLAYVIYTSGSTGKPKGVMNSHR---ALCNRLVWMQNTyRLTPDDRVLQKTPFSfdvSVWEFFWPLLYGARL-----VMA 1741
Cdd:cd05904 159 DVAALLYSSGTTGRSKGVMLTHRnliAMVAQFVAGEGS-NSDSEDVFLCVLPMF---HIYGLSSFALGLLRLgatvvVMP 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1742 RpdghKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADcACD--SLRRVICSGEALPAELQQRFFARF-NAQLHNLYG 1818
Cdd:cd05904 235 R----FDLEELLAAIERYKVTHLPVVPPIVLALVKSPIVD-KYDlsSLRQIMSGAAPLGKELIEAFRAKFpNVDLGQGYG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1819 PTEA-AIDVTFwaCQPDDHRS-FVPIGRPIANTQLYILDT-LGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDP 1895
Cdd:cd05904 310 MTEStGVVAMC--FAPEKDRAkYGSVGRLVPNVEAKIVDPeTGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1896 FInqpgarlyKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQ 1975
Cdd:cd05904 388 WL--------HTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRK 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 641744967 1976 PGVTPDPADLRQQLGQHLAEY----MVpgAFVtlDAFPLTPNGKLDRKAL 2021
Cdd:cd05904 460 PGSSLTEDEIMDFVAKQVAPYkkvrKV--AFV--DAIPKSPSGKILRKEL 505
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1504-2016 |
8.65e-45 |
|
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: 173.92 E-value: 8.65e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1504 ILPDSERRQVMLDFNATEADFPHDA---LIHQLVEDQAARTPDTTAVLFED------QHLTYDALNRRANQLAHHLIDLG 1574
Cdd:cd17634 26 ITPYQKVKNTSFAPGAPSIKWFEDAtlnLAANALDRHLRENGDRTAIIYEGddtsqsRTISYRELHREVCRFAGTLLDLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1575 VKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLT---------------QANQRALL 1639
Cdd:cd17634 106 VKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITadggvragrsvplkkNVDDALNP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1640 TGDVPR--ILLDTA------------DFSHLSEDNP--HVP-GLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVW-M 1701
Cdd:cd17634 186 NVTSVEhvIVLKRTgsdidwqegrdlWWRDLIAKASpeHQPeAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATtM 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLTPDDRVLQKTPFSFDVS-VWEFFWPLLYGARLVM--ARPDgHKDAAYLAQLIERTGITTLHFVPSMLQQfVQWA 1778
Cdd:cd17634 266 KYVFDYGPGDIYWCTADVGWVTGhSYLLYGPLACGATTLLyeGVPN-WPTPARMWQVVDKHGVNILYTAPTAIRA-LMAA 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1779 DADCA----CDSLRRVICSGEALPAELQQRFFARFNAQ---LHNLYGPTEaaidvTFWACQPDdHRSFVPIG-----RPI 1846
Cdd:cd17634 344 GDDAIegtdRSSLRILGSVGEPINPEAYEWYWKKIGKEkcpVVDTWWQTE-----TGGFMITP-LPGAIELKagsatRPV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1847 ANTQLYILDTLGQPVPLGVAGELHIGGV--GVARGYLNRPDltaeRFIPDPFINQPGarLYKTGDLARWLPDGSLEYLGR 1924
Cdd:cd17634 418 FGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFSTFKG--MYFSGDGARRDEDGYYWITGR 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1925 NDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDP---ADLRQQLGQHLAEYMVPGA 2001
Cdd:cd17634 492 SDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPelyAELRNWVRKEIGPLATPDV 571
|
570
....*....|....*
gi 641744967 2002 FVTLDAFPLTPNGKL 2016
Cdd:cd17634 572 VHWVDSLPKTRSGKI 586
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1518-2021 |
1.71e-44 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 171.85 E-value: 1.71e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1518 NATEADFPHDalihqlvedQAARTPDTTAVLfeDQH---LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIG 1594
Cdd:PRK06087 22 DASLADYWQQ---------TARAMPDKIAVV--DNHgasYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTII 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1595 LLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALL--TQANQRAL------LTGDVPR----ILLD-------TADFSH 1655
Cdd:PRK06087 91 YLACLKVGAVSVPLLPSWREAELVWVLNKCQAKMFFapTLFKQTRPvdlilpLQNQLPQlqqiVGVDklapatsSLSLSQ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1656 LSEDNP---HVPGLDAHHLAYVIYTSGSTGKPKGVMNSH-------RALCNRLvwmqntyRLTPDDRVLQKTPFSFDVSv 1725
Cdd:PRK06087 171 IIADYEpltTAITTHGDELAAVLFTSGTEGLPKGVMLTHnnilaseRAYCARL-------NLTWQDVFMMPAPLGHATG- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1726 weFFW----PLLYGARLVMARpdgHKDAAYLAQLIERTGITTLH----FVPSMLQQfVQWADADCAcdSLRRVICSGEAL 1797
Cdd:PRK06087 243 --FLHgvtaPFLIGARSVLLD---IFTPDACLALLEQQRCTCMLgatpFIYDLLNL-LEKQPADLS--ALRFFLCGGTTI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1798 PAELQQRFFARfNAQLHNLYGPTEAAIDVTfwaCQPDD--HRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVG 1875
Cdd:PRK06087 315 PKKVARECQQR-GIKLLSVYGSTESSPHAV---VNLDDplSRFMHTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPN 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1876 VARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAV 1955
Cdd:PRK06087 391 VFMGYLDEPELTARALDEEGW--------YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDAC 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 1956 VVAREDSPGDTRLVAYLCPQPGV-TPDPADLRQQLG-QHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK06087 463 VVAMPDERLGERSCAYVVLKAPHhSLTLEEVVAFFSrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
2631-3097 |
1.81e-44 |
|
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: 168.81 E-value: 1.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2631 SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQ 2710
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2711 SAhlgimngslpvilLDDgetrpfdnepdtpldarkqgltprhLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGI 2790
Cdd:cd05935 81 SE-------------LDD-------------------------LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2791 AQEDVLLGVTSLsFDIS--ILEIFLPLLNGARLILATQAQAADAQQlamLIERHAVSFMQATPStwrMLVELRDfalPPG 2868
Cdd:cd05935 123 TPSDVILACLPL-FHVTgfVGSLNTAVYVGGTYVLMARWDRETALE---LIEKYKVTFWTNIPT---MLVDLLA---TPE 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2869 FKALC---------GGEALPENLATALLQKVTTLWN-LYGPTETTIWSTLNGLTTP-TPYIGHPIANTQIYILDAQ-GRV 2936
Cdd:cd05935 193 FKTRDlsslkvltgGGAPMPPAVAEKLLKLTGLRFVeGYGLTETMSQTHTNPPLRPkLQCLGIP*FGVDARVIDIEtGRE 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2937 VPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDpfSGapeARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGE 3016
Cdd:cd05935 273 LPPNEVGEIVVRGPQIFKGYWNRPEETEESFIEI--KG---RRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAE 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3017 IETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLE--PADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDR 3094
Cdd:cd05935 348 VEAKLYKHPAI*EVCVISVPDERVGEEVKAFIVLRPEYRGKvtEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILW 427
|
...
gi 641744967 3095 KAL 3097
Cdd:cd05935 428 RLL 430
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
2611-3093 |
1.03e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 169.30 E-value: 1.03e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2611 LFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTY 2690
Cdd:PRK07798 8 LFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2691 PVERLRYMLDDAKPVALISQSAHLGIMNGSLP-------VILLDDGETRPFDNEPDTPLDARKQGLTPRHLA-------Y 2756
Cdd:PRK07798 88 VEDELRYLLDDSDAVALVYEREFAPRVAEVLPrlpklrtLVVVEDGSGNDLLPGAVDYEDALAAGSPERDFGerspddlY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2757 VIYTSGSTGKPKGVMVEHANM-------VNFLCS--MRKEPGIAQEdVLLGVTSLSFDISIL-------EIFLPLLNGAR 2820
Cdd:PRK07798 168 LLYTGGTTGMPKGVMWRQEDIfrvllggRDFATGepIEDEEELAKR-AAAGPGMRRFPAPPLmhgagqwAAFAALFSGQT 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2821 LILATQAQAADAQQLAmLIERHAVSFMQ------ATPstwrMLVELR---DFALPPGFKALCGGEALPENLATALLQKV- 2890
Cdd:PRK07798 247 VVLLPDVRFDADEVWR-TIEREKVNVITivgdamARP----LLDALEargPYDLSSLFAIASGGALFSPSVKEALLELLp 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2891 -TTLWNLYGPTET----TIWSTLNGLTTPTPYIGhpiANTQIYILDAQGRVVPLGVAGEIHIAGAGVV-RGYLGRPDLTA 2964
Cdd:PRK07798 322 nVVLTDSIGSSETgfggSGTVAKGAVHTGGPRFT---IGPRTVVLDEDGNPVEPGSGEIGWIARRGHIpLGYYKDPEKTA 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2965 ERFITdpFSGapeARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRL 3044
Cdd:PRK07798 399 ETFPT--IDG---VRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPDERWGQEV 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 641744967 3045 VAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLD 3093
Cdd:PRK07798 474 VAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
2620-3097 |
1.33e-43 |
|
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: 168.32 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKP-VALISQSAH------LGIMNGSLPVILLDDGE-----TRPFDNEPDTPLDARKQGLT-PRHLAYVIYTSGSTGK 2766
Cdd:cd05959 98 EDSRArVVVVSGELApvlaaaLTKSEHTLVVLIVSGGAgpeagALLLAELVAAEAEQLKPAAThADDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2767 PKGVMVEHANMVnFLCSMRKEP--GIAQEDVLLGVTSLSFDISILE-IFLPLLNGARLILATQAQAADAQQLAMLIERHA 2843
Cdd:cd05959 178 PKGVVHLHADIY-WTAELYARNvlGIREDDVCFSAAKLFFAYGLGNsLTFPLSVGATTVLMPERPTPAAVFKRIRRYRPT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2844 VSF--------MQATP-STWRMLVELRdfalppgfKALCGGEALPEnlatallqKVTTLW-NLYGPTettiwsTLNGL-T 2912
Cdd:cd05959 257 VFFgvptlyaaMLAAPnLPSRDLSSLR--------LCVSAGEALPA--------EVGERWkARFGLD------ILDGIgS 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2913 TPTPYI--------------GHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFitdpfsgapEA 2978
Cdd:cd05959 315 TEMLHIflsnrpgrvrygttGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF---------QG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2979 RMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQP---DTV 3055
Cdd:cd05959 386 EWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRPgyeDSE 465
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 641744967 3056 LEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05959 466 ALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
2161-2568 |
1.80e-43 |
|
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: 164.78 E-value: 1.80e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2161 IYPLAPLQEGILfhHLLQEQGDTYLLRSmvAFTHRERLD--AFLSALQQVIDRHDILRTAVCWQDLSQPVQVVWRQAILP 2238
Cdd:cd19545 1 IYPCTPLQEGLM--ALTARQPGAYVGQR--VFELPPDIDlaRLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPIS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2239 INHFepTSPEDVLAQlqahtePRTRRIDLSQaPLFRADIAHDPlQNEWLLALSFHHLISDHMTLALIVGEIRLLLQHQAd 2318
Cdd:cd19545 77 WTES--TSLDEYLEE------DRAAPMGLGG-PLVRLALVEDP-DTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEP- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2319 aLPTPLPYRNFIAQTLSVPNSAHEAYFRDKLADVDEPTAP-FGLLNVQGSGGDIHEARLVLDATLASairqqarhlGVSP 2397
Cdd:cd19545 146 -VPQPPPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAVFPpLPSSRYQPRPDATLEHSISLPSSASS---------GVTL 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2398 GVLFHVAWAQVLAQTSGRDDVVFGSVLLGRLAGAEGADRIMGMFINTLPLRISLADRGA-AEVVERTSHDLMTLLEHEQA 2476
Cdd:cd19545 216 ATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSvEDFLQTVQKDLLDMIPFEHT 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2477 PLALAQRCSGVAPPMPLFSTLLNYRHTQASSTDNTLSDIRVLTSEER---TNYPLTLAVDDRGEGFSLVA----QTLEDI 2549
Cdd:cd19545 296 GLQNIRRLGPDARAACNFQTLLVVQPALPSSTSESLELGIEEESEDLedfSSYGLTLECQLSGSGLRVRArydsSVISEE 375
|
410
....*....|....*....
gi 641744967 2550 DPHRLLNYLMTAISSLVDA 2568
Cdd:cd19545 376 QVERLLDQFEHVLQQLASA 394
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
2615-3097 |
2.12e-43 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 168.77 E-value: 2.12e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2615 QVACTPDAIAVVFGE-ASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVE 2693
Cdd:PRK06087 32 TARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2694 RLRYMLDDAKPVALI------------------SQSAHLGimngslPVILLDDgetrpfdNEPDTPLDARKQGLT----- 2750
Cdd:PRK06087 112 ELVWVLNKCQAKMFFaptlfkqtrpvdlilplqNQLPQLQ------QIVGVDK-------LAPATSSLSLSQIIAdyepl 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2751 ----PRH---LAYVIYTSGSTGKPKGVMVEHANMvnfLCSMR---KEPGIAQEDVLLGVTSLSFDISILE-IFLPLLNGA 2819
Cdd:PRK06087 179 ttaiTTHgdeLAAVLFTSGTEGLPKGVMLTHNNI---LASERaycARLNLTWQDVFMMPAPLGHATGFLHgVTAPFLIGA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2820 RLILATQAQAADAQQlamLIERHAVSF-MQATPSTWRMLVELRdfALPPGFKA----LCGGEALPENLATALLQKVTTLW 2894
Cdd:PRK06087 256 RSVLLDIFTPDACLA---LLEQQRCTCmLGATPFIYDLLNLLE--KQPADLSAlrffLCGGTTIPKKVARECQQRGIKLL 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2895 NLYGPTETTIWSTLNgLTTPTPYIGH----PIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITD 2970
Cdd:PRK06087 331 SVYGSTESSPHAVVN-LDDPLSRFMHtdgyAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEE 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2971 PFsgapearmYKTGDLGRWLPDGTLEYLGRNDfQVKVRGFR-IELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAY-L 3048
Cdd:PRK06087 410 GW--------YYSGDLCRMDEAGYIKITGRKK-DIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYvV 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 641744967 3049 LAQPDTVLEPADLRQRLSE-GVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK06087 481 LKAPHHSLTLEEVVAFFSRkRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
481-963 |
2.57e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 169.07 E-value: 2.57e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 481 AQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAE 560
Cdd:PRK06178 41 AWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREH 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 561 RLAYILDDAAPVALLTQSAQVAQLNSTLPTV----LLDTPAAAACPD--TNPVVQGLHAAH------------------- 615
Cdd:PRK06178 121 ELSYELNDAGAEVLLALDQLAPVVEQVRAETslrhVIVTSLADVLPAepTLPLPDSLRAPRlaaagaidllpalractap 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 616 ----------LAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFdasvknWIQ---------L 676
Cdd:PRK06178 201 vplpppaldaLAALNYTGGTTGMPKGCEHTQRDMVYTAAAAYAVAVVGGEDSVFLSFLPEF------WIAgenfgllfpL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 677 LSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSD---PAYQPAQVLIGGEAISPAVWSRLQSLS 753
Cdd:PRK06178 275 FSGATLVLLA---RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHPRFAEydlSSLRQVRVVSFVKKLNPDYRQRWRALT 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 754 DTRFINV-YGPTEC-TVDA-TACVVD-----RTQPLpTIGKPLANTRLYILDAQD-QPVPIGVTGELHIGGAGVARGYLH 824
Cdd:PRK06178 352 GSVLAEAaWGMTEThTCDTfTAGFQDddfdlLSQPV-FVGLPVPGTEFKICDFETgELLPLGAEGEIVVRTPSLLKGYWN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 825 RPDLTAERFIpDPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDS 904
Cdd:PRK06178 431 KPEATAEALR-DGW--------LHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDP 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 905 PGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVtLDALPLTPNGKLDRKAL 963
Cdd:PRK06178 502 DKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
483-958 |
3.68e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 167.42 E-value: 3.68e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERL 562
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 563 AYILDDAAPVALLTQSAQVAQLNSTLPTVLLDTPAAAACPDTNPVVQGLHA-------------------AHLAYVIYTS 623
Cdd:PRK08316 101 AYILDHSGARAFLVDPALAPTAEAALALLPVDTLILSLVLGGREAPGGWLDfadwaeagsvaepdveladDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 624 GSTGRPKGVMVAHRNVInlATGLHTLLALDH-PSRIALNASIVFD-ASVKNWI--QLLSGHTLVLVPdalRADAHQLWRY 699
Cdd:PRK08316 181 GTESLPKGAMLTHRALI--AEYVSCIVAGDMsADDIPLHALPLYHcAQLDVFLgpYLYVGATNVILD---APDPELILRT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 700 FARHAVDLFDCTPVqlQWLldaGLGSDPAYQPAQvLIG------GEAISP-AVWSRLQS-LSDTRFINVYGPTECTVDAT 771
Cdd:PRK08316 256 IEAERITSFFAPPT--VWI---SLLRHPDFDTRD-LSSlrkgyyGASIMPvEVLKELRErLPGLRFYNCYGQTEIAPLAT 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 772 AcvvdrTQP------LPTIGKPLANTRLYILDAQDQPVPIGVTGELhiggagVAR------GYLHRPDLTAERFIPDPFs 839
Cdd:PRK08316 330 V-----LGPeehlrrPGSAGRPVLNVETRVVDDDGNDVAPGEVGEI------VHRspqlmlGYWDDPEKTAEAFRGGWF- 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 840 adpaariyKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPD 919
Cdd:PRK08316 398 --------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAG 469
|
490 500 510
....*....|....*....|....*....|....*....
gi 641744967 920 AELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKL 958
Cdd:PRK08316 470 ATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1530-1992 |
4.95e-43 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 168.74 E-value: 4.95e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFED----QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAY 1605
Cdd:COG1022 13 LPDLLRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVT 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1606 VPLDPGYPAERLAYMLDDASPVALL--TQANQRALLT--GDVPR----ILLDT-------------------ADFSHLSE 1658
Cdd:COG1022 93 VPIYPTSSAEEVAYILNDSGAKVLFveDQEQLDKLLEvrDELPSlrhiVVLDPrglrddprllsldellalgREVADPAE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1659 DNPHVPGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFS--FDvSVWEFFWpLLYGA 1736
Cdd:COG1022 173 LEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAhvFE-RTVSYYA-LAAGA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1737 RLVMARpdghkDAAYLAQLIERTGITTLHFVP-----------------SMLQQFV---------QWADADCACDS---- 1786
Cdd:COG1022 251 TVAFAE-----SPDTLAEDLREVKPTFMLAVPrvwekvyagiqakaeeaGGLKRKLfrwalavgrRYARARLAGKSpsll 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1787 -----------------------LRRVICSGEALPAELqQRFFARFNAQLHNLYGPTEAAIDVTfwaCQPDDHRSFVPIG 1843
Cdd:COG1022 326 lrlkhaladklvfsklrealggrLRFAVSGGAALGPEL-ARFFRALGIPVLEGYGLTETSPVIT---VNRPGDNRIGTVG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1844 RPIANTQLYILDTlgqpvplgvaGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSLEYLG 1923
Cdd:COG1022 402 PPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW--------LHTGDIGELDEDGFLRITG 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641744967 1924 RNDFQVKLR-GFRIELGEIEARLMQCPGVQEAVVVaredspGDTR--LVAyLcpqpgVTPDPADLRQQLGQH 1992
Cdd:COG1022 464 RKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV------GDGRpfLAA-L-----IVPDFEALGEWAEEN 523
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1536-2020 |
6.32e-43 |
|
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and is homologous to fatty acyl-coenzyme A (CoA) ligases (FACLs). However, FAALs produce only the acyl adenylate and are unable to perform the thioester-forming reaction, while FACLs perform a two-step catalytic reaction; AMP ligation followed by CoA ligation using ATP and CoA as cofactors. FAALs have insertion motifs between the N-terminal and C-terminal subdomains that distinguish them from the FACLs. This insertion motif precludes the binding of CoA, thus preventing CoA ligation. It has been suggested that the acyl adenylates serve as substrates for multifunctional polyketide synthases to permit synthesis of complex lipids such as phthiocerol dimycocerosate, sulfolipids, mycolic acids, and mycobactin.
Pssm-ID: 341254 [Multi-domain] Cd Length: 547 Bit Score: 167.42 E-value: 6.32e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1536 DQAARTPDTTAVLF------EDQHLTYDALNRRANQLAHHLIDLGvKPDDRIAICVERSLDMVIGLLAILKAGAAYVPL- 1608
Cdd:cd05931 1 RRAAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLp 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1609 --DPGYPAERLAYMLDDASPVALLTQANQRALLTGDV---------PRILLDTADFShlSEDNPHVPGLDAHHLAYVIYT 1677
Cdd:cd05931 80 ppTPGRHAERLAAILADAGPRVVLTTAAALAAVRAFAasrpaagtpRLLVVDLLPDT--SAADWPPPSPDPDDIAYLQYT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1678 SGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEF-FWPLLYGARLVMARPdghkdAAYLA--- 1753
Cdd:cd05931 158 SGSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGlLTPLYSGGPSVLMSP-----AAFLRrpl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1754 ---QLIERTGITTlHFVPSM-LQQFVQWADADCACD----SLRRVICSGEALPAELQQRFFARFNAqlHNL--------Y 1817
Cdd:cd05931 233 rwlRLISRYRATI-SAAPNFaYDLCVRRVRDEDLEGldlsSWRVALNGAEPVRPATLRRFAEAFAP--FGFrpeafrpsY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1818 GPTEAAIDVTF-----------------------WACQPDDHRSFVPIGRPIANTQLYILDT-LGQPVPLGVAGELHIGG 1873
Cdd:cd05931 310 GLAEATLFVSGgppgtgpvvlrvdrdalagravaVAADDPAARELVSCGRPLPDQEVRIVDPeTGRELPDGEVGEIWVRG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1874 VGVARGYLNRPDLTAERFIPDPfiNQPGARLYKTGDLARwLPDGSLEYLGRndfqVK----LRGFRIELGEIEARLMQCP 1949
Cdd:cd05931 390 PSVASGYWGRPEATAETFGALA--ATDEGGWLRTGDLGF-LHDGELYITGR----LKdliiVRGRNHYPQDIEATAEEAH 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 1950 GVQE---AVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEY--MVPGAFVTL--DAFPLTPNGKLDRKA 2020
Cdd:cd05931 463 PALRpgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREhgVAPADVVLVrpGSIPRTSSGKIQRRA 540
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
500-963 |
6.52e-43 |
|
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: 164.53 E-value: 6.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 500 TYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQSA 579
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVTDGS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 580 qvaqlnstlptvllDTPAaaacpdtnpvvqglhaahlaYVIYTSGSTGRPKGVMVAHRNVINLATGLHtlLALDHPSRia 659
Cdd:cd05971 88 --------------DDPA--------------------LIIYTSGTTGPPKGALHAHRVLLGHLPGVQ--FPFNLFPR-- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 660 lNASIVFDASVKNWIQLLSGhtlVLVPDAL-----------RADAHQLWRYFARHAVDLFDCTPVQLQWLLDAG-LGSDP 727
Cdd:cd05971 130 -DGDLYWTPADWAWIGGLLD---VLLPSLYfgvpvlahrmtKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGeQLKHA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 728 AYQPAQVLIGGEAISPA--VWSRLQsLSDTrfIN-VYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQPVP 804
Cdd:cd05971 206 QVKLRAIATGGESLGEEllGWAREQ-FGVE--VNeFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 805 IGVTGELhiggaGVAR-------GYLHRPDLTAERFIPDPFsadpaariyKTGDLARWLPDGNIDYLGRNDFQIKVRGFR 877
Cdd:cd05971 283 PGEVGEI-----AVELpdpvaflGYWNNPSATEKKMAGDWL---------LTGDLGRKDSDGYFWYVGRDDDVITSSGYR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 878 IEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARP---DAELHPAALRQQLAASLADYMIPSAFVTLDALPLTP 954
Cdd:cd05971 349 IGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPgetPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTA 428
|
....*....
gi 641744967 955 NGKLDRKAL 963
Cdd:cd05971 429 TGKIRRREL 437
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1530-2021 |
1.61e-42 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 165.24 E-value: 1.61e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFED-----QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAA 1604
Cdd:PRK08008 9 LRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1605 YVPLDPGYPAERLAYMLDDASPVALLTQAN-----QRALLTGDVP--RILL---------DTADFSHLSEDNP----HVP 1664
Cdd:PRK08008 89 MVPINARLLREESAWILQNSQASLLVTSAQfypmyRQIQQEDATPlrHICLtrvalpaddGVSSFTQLKAQQPatlcYAP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1665 GLDAHHLAYVIYTSGSTGKPKGVMNSHralCNRL------VWmQNtyRLTPDDRVLQKTP-FSFDVSVWEFFWPLLYGAR 1737
Cdd:PRK08008 169 PLSTDDTAEILFTSGTTSRPKGVVITH---YNLRfagyysAW-QC--ALRDDDVYLTVMPaFHIDCQCTAAMAAFSAGAT 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1738 LVM-----ARpdghkdaAYLAQLIE-RTGITtlHFVPS-----MLQQFVQWADADCacdsLRRVICSgeaLPAELQQR-- 1804
Cdd:PRK08008 243 FVLlekysAR-------AFWGQVCKyRATIT--ECIPMmirtlMVQPPSANDRQHC----LREVMFY---LNLSDQEKda 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1805 FFARFNAQLHNLYGPTEAAIDVTfwACQPDDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGV---GVARGYL 1881
Cdd:PRK08008 307 FEERFGVRLLTSYGMTETIVGII--GDRPGDKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1882 NRPDLTAERFIPDPFInqpgarlyKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVARED 1961
Cdd:PRK08008 385 LDPKATAKVLEADGWL--------HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKD 456
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1962 SPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK08008 457 SIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
499-963 |
5.92e-42 |
|
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: 161.49 E-value: 5.92e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQS 578
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 AQvaqlnstlptvlldtpaaaacpdtnpvvqglhaAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHpSRI 658
Cdd:cd05935 82 EL---------------------------------DDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTP-SDV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 659 ALNASIVFdaSVKNWIQLLS-----GHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQ 733
Cdd:cd05935 128 ILACLPLF--HVTGFVGSLNtavyvGGTYVLMA---RWDRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 734 VLIGGEA-ISPAVWSRLQSLSDTRFINVYGPTEcTVDATACVVDRTQPLPTIGKPLANTRLYILDAQD-QPVPIGVTGEL 811
Cdd:cd05935 203 VLTGGGApMPPAVAEKLLKLTGLRFVEGYGLTE-TMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIETgRELPPNEVGEI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 812 HIGGAGVARGYLHRPDLTAERFIpdpfsADPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCP 891
Cdd:cd05935 282 VVRGPQIFKGYWNRPEETEESFI-----EIKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHP 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641744967 892 GVQDAVVIAREDSPGDTRLVAYLCARPD--AELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05935 357 AI*EVCVISVPDERVGEEVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
488-966 |
6.16e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 162.47 E-value: 6.16e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 488 EAIAVLFEDQHLTYRELNRRANQLAHhlialGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDP-AYPAERlAYIL 566
Cdd:PRK07787 15 IADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPdSGVAER-RHIL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 567 DDAAPVALLtqsAQVAQLNSTLPTVLLDTPAAAACPDTNPvvqglHAAHLAYVIYTSGSTGRPKGVMVahrnvinlatgl 646
Cdd:PRK07787 89 ADSGAQAWL---GPAPDDPAGLPHVPVRLHARSWHRYPEP-----DPDAPALIVYTSGTTGPPKGVVL------------ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 647 htllaldhpSRIALNASIvfDASVKNW-----------IQLLSGHTLVL-VPDALRADAHqlwryfARHAVDLfdcTPVQ 714
Cdd:PRK07787 149 ---------SRRAIAADL--DALAEAWqwtaddvlvhgLPLFHVHGLVLgVLGPLRIGNR------FVHTGRP---TPEA 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 715 LQWLLDAG-------------LGSDP----AYQPAQVLIGGEAISPA-VWSRLQSLSDTRFINVYGPTEcTVDATACVVD 776
Cdd:PRK07787 209 YAQALSEGgtlyfgvptvwsrIAADPeaarALRGARLLVSGSAALPVpVFDRLAALTGHRPVERYGMTE-TLITLSTRAD 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 777 RTQPLPTIGKPLANTRLYILDAQDQPVPI-GVT-GELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLAR 854
Cdd:PRK07787 288 GERRPGWVGLPLAGVETRLVDEDGGPVPHdGETvGELQVRGPTLFDGYLNRPDATAAAFTADGW--------FRTGDVAV 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 855 WLPDGNIDYLGRN--DFqIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAElhPAALRQQLA 932
Cdd:PRK07787 360 VDPDGMHRIVGREstDL-IKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVA--ADELIDFVA 436
|
490 500 510
....*....|....*....|....*....|....
gi 641744967 933 ASLADYMIPSAFVTLDALPLTPNGKLDRKALPAP 966
Cdd:PRK07787 437 QQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
470-953 |
8.04e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 163.76 E-value: 8.04e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 470 PREMLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLG------- 542
Cdd:PRK06164 7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAcarlgat 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 543 ----------------ILKAGAAYVPMDPAYPAERLAYILDDAAPVALLT--QSAQVAQLNSTLP-------TVLLDTPA 597
Cdd:PRK06164 87 viavntryrshevahiLGRGRARWLVVWPGFKGIDFAAILAAVPPDALPPlrAIAVVDDAADATPapapgarVQLFALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 598 AAACPDTNPVVQGLHAAHLAYViyTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRI--ALNASIVFDASVKnWIQ 675
Cdd:PRK06164 167 PAPPAAAGERAADPDAGALLFT--TSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLlaALPFCGVFGFSTL-LGA 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 676 LLSGHTLVLVP--DALRAdAHQLWRYFARHAV---DLFDctpvqlqWLLDAGlGSDPAYQPAQVLiGGEAISPAvWSRLQ 750
Cdd:PRK06164 244 LAGGAPLVCEPvfDAART-ARALRRHRVTHTFgndEMLR-------RILDTA-GERADFPSARLF-GFASFAPA-LGELA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 751 SLSDTRFI---NVYGPTECTV-----DATACVVDRTQPLPTIGKPLANTRlyILDAQDQPV-PIGVTGELHIGGAGVARG 821
Cdd:PRK06164 313 ALARARGVpltGLYGSSEVQAlvalqPATDPVSVRIEGGGRPASPEARVR--ARDPQDGALlPDGESGEIEIRAPSLMRG 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 822 YLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAR 901
Cdd:PRK06164 391 YLDNPDATARALTDDGY--------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA 462
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 641744967 902 EdSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLT 953
Cdd:PRK06164 463 T-RDGKTVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVT 513
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1103-1391 |
8.44e-42 |
|
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: 160.73 E-value: 8.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1103 LDRPALTTALNGLVARHESLRTRFTSiDGQpaQQIDPDTLGFSLSSHDLRKLDEAARTTRVAELAEQEARARFDLTQGPL 1182
Cdd:cd19535 37 LDPDRLERAWNKLIARHPMLRAVFLD-DGT--QQILPEVPWYGITVHDLRGLSEEEAEAALEELRERLSHRVLDVERGPL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1183 IRGQLLQLDDNTHVLlltqhHI-----ISDGWSIGILARELAALYqaalEGSEANLPPLPVQYADYaVWQRQWLQGETLN 1257
Cdd:cd19535 114 FDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRELAALY----EDPGEPLPPLELSFRDY-LLAEQALRETAYE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1258 DLRDYWR---DQLQGAPAL--LEIPTDRPRPSVQRYAgdqvpFHLDAGQLRRLHALNRQQGTTLFMTLLAAWSVVLSRLS 1332
Cdd:cd19535 184 RARAYWQerlPTLPPAPQLplAKDPEEIKEPRFTRRE-----HRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWS 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641744967 1333 GQDDIVIGTPVANRPR--QELEGMVGFFVNTLALRTEPGRCHAVADLLDQVRERALDAYAH 1391
Cdd:cd19535 259 GQPRFLLNLTLFNRLPlhPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDH 319
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1523-2019 |
1.05e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 164.02 E-value: 1.05e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1523 DFPHDALIHqLVEDQAARTPDTTAVLFEDQHLTY---DALNRRAnqlAHHLIDLGVKPDDRIAICVERSLDMVIGLLAIL 1599
Cdd:PRK05605 28 DYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYaelGKQVRRA---AAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1600 KAGAAYVPLDPGYPAERLAYMLDD-----------ASPVA----------------------LLTQ----------ANQR 1636
Cdd:PRK05605 104 RLGAVVVEHNPLYTAHELEHPFEDhgarvaivwdkVAPTVerlrrttpletivsvnmiaampLLQRlalrlpipalRKAR 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1637 ALLTGDVPrillDTADFSHLSE-------DNPHVPGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLV----WMQNTY 1705
Cdd:PRK05605 184 AALTGPAP----GTVPWETLVDaaiggdgSDVSHPRPTPDDVALILYTSGTTGKPKGAQLTHRNLFANAAqgkaWVPGLG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1706 RltPDDRVLQKTPF----------SFDVSVweffwpllyGARLV-MARPDghkdAAYLAQLIERTGITTLHFVPSMLQQF 1774
Cdd:PRK05605 260 D--GPERVLAALPMfhaygltlclTLAVSI---------GGELVlLPAPD----IDLILDAMKKHPPTWLPGVPPLYEKI 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1775 VQWADA-DCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVtfwACQP-DDHRSFVPIGRPIANTQLY 1852
Cdd:PRK05605 325 AEAAEErGVDLSGVRNAFSGAMALPVSTVELWEKLTGGLLVEGYGLTETSPII---VGNPmSDDRRPGYVGVPFPDTEVR 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1853 ILD--TLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDpfinqpgarLYKTGDLARWLPDGSLEYLGRNDFQVK 1930
Cdd:PRK05605 402 IVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG---------WFRTGDVVVMEEDGFIRIVDRIKELII 472
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1931 LRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPL 2010
Cdd:PRK05605 473 TGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPR 552
|
....*....
gi 641744967 2011 TPNGKLDRK 2019
Cdd:PRK05605 553 DQLGKVRRR 561
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
483-963 |
1.08e-41 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 162.74 E-value: 1.08e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFED-QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAER 561
Cdd:PRK07514 12 AFADRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 562 LAYILDDAAPVALLTQSAQ---VAQLNSTLPTVLLDT----------PAAAACPDTNPVVQgLHAAHLAYVIYTSGSTGR 628
Cdd:PRK07514 92 LDYFIGDAEPALVVCDPANfawLSKIAAAAGAPHVETldadgtgsllEAAAAAPDDFETVP-RGADDLAAILYTSGTTGR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 629 PKGVMVAHRNVINLATGLH---------TLL-ALD----HPSRIALNasivfdasvknwIQLLSGHTLVLVPdalRADAH 694
Cdd:PRK07514 171 SKGAMLSHGNLLSNALTLVdywrftpddVLIhALPifhtHGLFVATN------------VALLAGASMIFLP---KFDPD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 695 QLWRYFARHAVdlFDCTP---VQLqwLLDAGLGSDpAYQPAQVLIGGEAisPAvwsrlqsLSDT----------RFINVY 761
Cdd:PRK07514 236 AVLALMPRATV--MMGVPtfyTRL--LQEPRLTRE-AAAHMRLFISGSA--PL-------LAEThrefqertghAILERY 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 762 GPTEcTVDATACVVDRTQPLPTIGKPLANTRLYILDAQD-QPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsa 840
Cdd:PRK07514 302 GMTE-TNMNTSNPYDGERRAGTVGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF-- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 841 dpaariYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAredSP----GDTrLVAYLCA 916
Cdd:PRK07514 379 ------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIG---VPhpdfGEG-VTAVVVP 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 641744967 917 RPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK07514 449 KPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
480-958 |
1.53e-41 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 163.21 E-value: 1.53e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 480 EAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLI-ALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYP 558
Cdd:PRK08314 17 EVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 559 AERLAYILDDA-APVALLTQS--AQVAQLNSTL---------------------PTVLLDTPAAAACPDTNPVVQ----- 609
Cdd:PRK08314 97 EEELAHYVTDSgARVAIVGSElaPKVAPAVGNLrlrhvivaqysdylpaepeiaVPAWLRAEPPLQALAPGGVVAwkeal 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 610 ------GLHAAH---LAYVIYTSGSTGRPKGVMVAHRNVINLATGlHTLLALDHPSRIAL---------------NASIV 665
Cdd:PRK08314 177 aaglapPPHTAGpddLAVLPYTSGTTGVPKGCMHTHRTVMANAVG-SVLWSNSTPESVVLavlplfhvtgmvhsmNAPIY 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 666 fdasvknwiqllSGHTLVLVPDALRADAHQLwryFARHAVDLFDCTPVQLQWLLdaglgSDPAYQP------AQVLIGGE 739
Cdd:PRK08314 256 ------------AGATVVLMPRWDREAAARL---IERYRVTHWTNIPTMVVDFL-----ASPGLAErdlsslRYIGGGGA 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 740 AISPAVWSRLQSLSDTRFINVYGPTEcTVDATacvvdRTQP-----LPTIGKPLANTRLYILDAQD-QPVPIGVTGELHI 813
Cdd:PRK08314 316 AMPEAVAERLKELTGLDYVEGYGLTE-TMAQT-----HSNPpdrpkLQCLGIPTFGVDARVIDPETlEELPPGEVGEIVV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 814 GGAGVARGYLHRPDLTAERFIpdpfSADpAARIYKTGDLARWLPDGN---IDYLGRndfQIKVRGFRIEAGEIESRLLRC 890
Cdd:PRK08314 390 HGPQVFKGYWNRPEATAEAFI----EID-GKRFFRTGDLGRMDEEGYffiTDRLKR---MINASGFKVWPAEVENLLYKH 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641744967 891 PGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAA------LRQQLAAsladYMIPSAFVTLDALPLTPNGKL 958
Cdd:PRK08314 462 PAIQEACVIATPDPRRGETVKAVVVLRPEARGKTTEeeiiawAREHMAA----YKYPRIVEFVDSLPKSGSGKI 531
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
25-459 |
1.68e-41 |
|
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: 160.96 E-value: 1.68e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 25 VQDIYPLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICWQGLHQPVQVVWRQAPL 104
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 105 TVNTL---TTTSSDTVPAQLRAATDPSNHRLNLSNAPLLSA---TTAHDpvcgEWLLSLSIHHLISDHITQALIIDEIR- 177
Cdd:pfam00668 81 ELEIIdisDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAglfRIAEN----RHHLLLSMHHIIVDGVSLGILLRDLAd 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 178 ----LLLEDRPEALPKPlPYRNFIAQILSVPLSE----HEQYFRNRLADIDTPTA-PFDLVDVQGNGEDITEARLSLDSS 248
Cdd:pfam00668 157 lyqqLLKGEPLPLPPKT-PYKDYAEWLQQYLQSEdyqkDAAYWLEQLEGELPVLQlPKDYARPADRSFKGDRLSFTLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 249 LADALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRlqGNLGADRVMGMFINTLPLRVSLRE-RSVHDVV 327
Cdd:pfam00668 236 TEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGR--PSPDIERMVGMFVNTLPLRIDPKGgKTFSELI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 328 QATSHELMMLLAHEQAPLALAQQCSQVP---PPLPLFSTLFNYrhsQKDASSQFWEGMRQLSG---------RERTNYPI 395
Cdd:pfam00668 314 KRVQEDLLSAEPHQGYPFGDLVNDLRLPrdlSRHPLFDPMFSF---QNYLGQDSQEEEFQLSEldlsvssviEEEAKYDL 390
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 396 TLSVDDLGDGFNLT---------AKTVmgvdpERIVHYMLTAIENLVtsleKTPQQPALSQPILPKSERQQVL 459
Cdd:pfam00668 391 SLTASERGGGLTIKidyntslfdEETI-----ERFAEHFKELLEQAI----AHPSQPLSELDLLSDAEKQKLL 454
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1554-2025 |
1.92e-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: 160.36 E-value: 1.92e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDA-SPVALLTQ 1632
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSeAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1633 AnqralltgdvpriLLDTADfshlsednPHVPgldahhlAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDR 1712
Cdd:cd05969 81 E-------------LYERTD--------PEDP-------TLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1713 V-LQKTPFSFDVSVWEFFWPLLYGARLVMArpDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADCA---CDSLR 1788
Cdd:cd05969 133 YwCTADPGWVTGTVYGIWAPWLNGVTNVVY--EGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARkydLSSLR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1789 RVICSGEALPAELQQRFFARFNAQLHNLYGPTE-AAIDVTFWACQPDDHRSfvpIGRPIANTQLYILDTLGQPVPLGVAG 1867
Cdd:cd05969 211 FIHSVGEPLNPEAIRWGMEVFGVPIHDTWWQTEtGSIMIANYPCMPIKPGS---MGKPLPGVKAAVVDENGNELPPGTKG 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1868 ELHI--GGVGVARGYLNRPdltaERFiPDPFINQpgarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARL 1945
Cdd:cd05969 288 ILALkpGWPSMFRGIWNDE----ERY-KNSFIDG----WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESAL 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1946 MQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPA---DLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALP 2022
Cdd:cd05969 359 MEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRRVLK 438
|
...
gi 641744967 2023 APD 2025
Cdd:cd05969 439 AKE 441
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
497-963 |
3.41e-41 |
|
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: 161.25 E-value: 3.41e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 497 QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLT 576
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFT 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 577 QSAQVAQLNST-LPTVLLDTPAA---------AACPDTNPVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGL 646
Cdd:cd05904 111 TAELAEKLASLaLPVVLLDSAEFdslsfsdllFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 647 HTLLALDHPSRIALNASI----VFDASVKNWIQLLSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAG 722
Cdd:cd05904 191 VAGEGSNSDSEDVFLCVLpmfhIYGLSSFALGLLRLGATVVVMP---RFDLEELLAAIERYKVTHLPVVPPIVLALVKSP 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 723 LGSDpaYQPA---QVLIGGEAISPAVWSR-LQSLSDTRFINVYGPTECTVDATACVVDRTQPLP--TIGKPLANTRLYIL 796
Cdd:cd05904 268 IVDK--YDLSslrQIMSGAAPLGKELIEAfRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAKygSVGRLVPNVEAKIV 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 797 DAQD-QPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQIKVRG 875
Cdd:cd05904 346 DPETgESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW--------LHTGDLCYIDEDGYLFIVDRLKELIKYKG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 876 FRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPN 955
Cdd:cd05904 418 FQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLTEDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPS 497
|
....*...
gi 641744967 956 GKLDRKAL 963
Cdd:cd05904 498 GKILRKEL 505
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
2616-3097 |
3.59e-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: 160.57 E-value: 3.59e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2616 VACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERL 2695
Cdd:cd05920 25 AARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLALPSHRRSEL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2696 RYMLDDAKPVALISqsahlgimngslpvilldDGETRPFDNEPDTPLDARKQgltpRHLAYVIYTSGSTGKPKGVMVEHA 2775
Cdd:cd05920 105 SAFCAHAEAVAYIV------------------PDRHAGFDHRALARELAESI----PEVALFLLSGGTTGTPKLIPRTHN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2776 nmvNFLCSMRKEP---GIAQEDVLLGVTSLS--FDISILEIFLPLLNGARLILATQAQAADAQQlamLIERHAVSFMQAT 2850
Cdd:cd05920 163 ---DYAYNVRASAevcGLDQDTVYLAVLPAAhnFPLACPGVLGTLLAGGRVVLAPDPSPDAAFP---LIEREGVTVTALV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2851 PSTWRMLVELRDF--ALPPGFKAL-CGGEALPENLATALLQKVT-TLWNLYGPTETTIwsTLNGLTTPTPYI----GHPI 2922
Cdd:cd05920 237 PALVSLWLDAAASrrADLSSLRLLqVGGARLSPALARRVPPVLGcTLQQVFGMAEGLL--NYTRLDDPDEVIihtqGRPM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2923 -ANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRN 3001
Cdd:cd05920 315 sPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF--------YRTGDLVRRTPDGYLVVEGRI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3002 DFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQpDTVLEPADLRQRLSE-GVAEYMIPSAFVT 3080
Cdd:cd05920 387 KDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLR-DPPPSAAQLRRFLRErGLAAYKLPDRIEF 465
|
490
....*....|....*..
gi 641744967 3081 LDAFPLTPNGKLDRKAL 3097
Cdd:cd05920 466 VDSLPLTAVGKIDKKAL 482
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
2608-3097 |
3.63e-41 |
|
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: 161.85 E-value: 3.63e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2608 IHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGayVPLD 2687
Cdd:COG1021 27 LGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2688 pTYPVER---LRYMLDDAKPVALISQSAHLGIMNGSL------------PVILLDD-GETRPFDNEPDTPLDARKQGLTP 2751
Cdd:COG1021 105 -ALPAHRraeISHFAEQSEAVAYIIPDRHRGFDYRALarelqaevpslrHVLVVGDaGEFTSLDALLAAPADLSEPRPDP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2752 RHLAYVIYTSGSTGKPKGVMVEHANmvnFLCSMRKEPGIA---QEDVLLGVtsL----SFDISILEIFLPLLNGARLILA 2824
Cdd:COG1021 184 DDVAFFQLSGGTTGLPKLIPRTHDD---YLYSVRASAEICgldADTVYLAA--LpaahNFPLSSPGVLGVLYAGGTVVLA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2825 TQAQAADAQQlamLIERHAVSF-----------MQATP------STWRMLvelrdfalppgfkaLCGGEALPENLATAL- 2886
Cdd:COG1021 259 PDPSPDTAFP---LIERERVTVtalvpplallwLDAAErsrydlSSLRVL--------------QVGGAKLSPELARRVr 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2887 ------LQKVttlwnlYGPTEttiwstlnGLTTPTPyIGHP---IANTQ---------IYILDAQGRVVPLGVAGEIHIA 2948
Cdd:COG1021 322 palgctLQQV------FGMAE--------GLVNYTR-LDDPeevILTTQgrpispddeVRIVDEDGNPVPPGEVGELLTR 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2949 GAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVH 3028
Cdd:COG1021 387 GPYTIRGYYRAPEHNARAFTPDGF--------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVH 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3029 DAVVIAREDSPGDKRLVAYLLAQPDTvLEPADLRQRLSE-GVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:COG1021 459 DAAVVAMPDEYLGERSCAFVVPRGEP-LTLAELRRFLRErGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1075-1494 |
4.74e-41 |
|
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: 157.85 E-value: 4.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1075 QRLWFLAQL-DPAASQAYHlpaALHLTGRLDRPALTTALNGLVARHESLRTRF--TSIDGQPAQQIdpdtlgfslsshdL 1151
Cdd:cd19542 8 QEGMLLSQLrSPGLYFNHF---VFDLDSSVDVERLRNAWRQLVQRHDILRTVFveSSAEGTFLQVV-------------L 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1152 RKLDEAARTTRVAELAEQEARARFD----LTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALE 1227
Cdd:cd19542 72 KSLDPPIEEVETDEDSLDALTRDLLddptLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1228 GSeanlpplPVQYADYAvwqrQWLQGETLNDLRDYWRDQLQGAPALLEiptdrprPSVQRYAGDQVPFHLDAGQLRRLHA 1307
Cdd:cd19542 152 PP-------APPFSDYI----SYLQSQSQEESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1308 LNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANR--PRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQVRERA 1385
Cdd:cd19542 214 FCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQY 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1386 LDAYAHQALPFEQVVEILQPARSlsySPIFQVMLSLNNTPAQALTLPDLTLSAVERPQHSTH-FDLSLSLIETENGLNGG 1464
Cdd:cd19542 294 LRSLPHQHLSLREIQRALGLWPS---GTLFNTLVSYQNFEASPESELSGSSVFELSAAEDPTeYPVAVEVEPSGDSLKVS 370
|
410 420 430
....*....|....*....|....*....|
gi 641744967 1465 LVYATDLFDRETILRVVGYVENILMAMADD 1494
Cdd:cd19542 371 LAYSTSVLSEEQAEELLEQFDDILEALLAN 400
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
616-963 |
6.47e-41 |
|
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: 155.18 E-value: 6.47e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 616 LAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSR--IALNASIVFDASVKnWIQLLSGHTLVLvPDALRADA 693
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSwlLSLPLYHVGGLAIL-VRSLLAGAELVL-LERNQALA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 694 HQLWRYFARHAvdlfDCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAISPAVWSRLQSLsDTRFINVYGPTECTVDATAC 773
Cdd:cd17630 80 EDLAPPGVTHV----SLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 774 VVDRTQpLPTIGKPLANTRLYILDaqdqpvpigvTGELHIGGAGVARGYLHRPdltaerfIPDPFSADPaarIYKTGDLA 853
Cdd:cd17630 155 RPDGFG-RGGVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQ-------LVPEFNEDG---WFTTKDLG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 854 RWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLcaRPDAELHPAALRQQLAA 933
Cdd:cd17630 214 ELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVI--VGRGPADPAELRAWLKD 291
|
330 340 350
....*....|....*....|....*....|
gi 641744967 934 SLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd17630 292 KLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
482-963 |
7.25e-41 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 159.74 E-value: 7.25e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 482 QAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAER 561
Cdd:PRK03640 11 RAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 562 LAYILDDAAPVALLTQSAQVAQLNSTLPtVLLDTPAAAACPDTNPvVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRN--- 638
Cdd:PRK03640 91 LLWQLDDAEVKCLITDDDFEAKLIPGIS-VKFAELMNGPKEEAEI-QEEFDLDEVATIMYTSGTTGKPKGVIQTYGNhww 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 639 -----VINLatGLH------TLLALDHPSRIalnaSIVFDasvknwiQLLSGHTLVLVPdalRADAHQLWRYFARHAVDL 707
Cdd:PRK03640 169 savgsALNL--GLTeddcwlAAVPIFHISGL----SILMR-------SVIYGMRVVLVE---KFDAEKINKLLQTGGVTI 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 708 FDCTPVQLQWLLdAGLGSDPaYQPA--QVLIGGEAISPAVwsrLQSLSDTRF--INVYGPTE-----CTVDATacvvDRT 778
Cdd:PRK03640 233 ISVVSTMLQRLL-ERLGEGT-YPSSfrCMLLGGGPAPKPL---LEQCKEKGIpvYQSYGMTEtasqiVTLSPE----DAL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 779 QPLPTIGKPLANTRLYILDaQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariyKTGDLARWLPD 858
Cdd:PRK03640 304 TKLGSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF---------KTGDIGYLDEE 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 859 GNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCArpDAELHPAALRQQLAASLADY 938
Cdd:PRK03640 374 GFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKY 451
|
490 500
....*....|....*....|....*
gi 641744967 939 MIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK03640 452 KVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
2581-3097 |
8.20e-41 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 160.99 E-value: 8.20e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2581 PVLPDSERQQMlvdfnaTDADIPRHALIHELFEAQVACTPDAIAVV-----FGEAS-LSYDELNRRANRLAHHLISFGVR 2654
Cdd:PRK13295 5 AVLLPPRRAAS------IAAGHWHDRTINDDLDACVASCPDKTAVTavrlgTGAPRrFTYRELAALVDRVAVGLARLGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2655 PDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQSA-----HLGIMNG---SLP---- 2722
Cdd:PRK13295 79 RGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAESKVLVVPKTfrgfdHAAMARRlrpELPalrh 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2723 VILLD-DGE--------TRPFDNEPDTP--LDARKQGltPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIA 2791
Cdd:PRK13295 159 VVVVGgDGAdsfealliTPAWEQEPDAPaiLARLRPG--PDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLG 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2792 QEDVLLGVTSLS----FDISILeifLPLLNGARLILATQAQAADAQQlamLIERHAVSF-MQATPSTWRML--VELRDFA 2864
Cdd:PRK13295 237 ADDVILMASPMAhqtgFMYGLM---MPVMLGATAVLQDIWDPARAAE---LIRTEGVTFtMASTPFLTDLTraVKESGRP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2865 LPPGFKALCGGEALPENLA----TALLQKVTTLWnlyGPTETTIwSTLNGLTTPTPYI----GHPIANTQIYILDAQGRV 2936
Cdd:PRK13295 311 VSSLRTFLCAGAPIPGALVerarAALGAKIVSAW---GMTENGA-VTLTKLDDPDERAsttdGCPLPGVEVRVVDADGAP 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2937 VPLGVAGEIHIAGAGVVRGYLGRPDLTAerfitDPFSGapearMYKTGDLGRWLPDGTLEYLGRNDfQVKVRGFR-IELG 3015
Cdd:PRK13295 387 LPAGQIGRLQVRGCSNFGGYLKRPQLNG-----TDADG-----WFDTGDLARIDADGYIRISGRSK-DVIIRGGEnIPVV 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3016 EIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRL-SEGVAEYMIPSAFVTLDAFPLTPNGKLDR 3094
Cdd:PRK13295 456 EIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQK 535
|
...
gi 641744967 3095 KAL 3097
Cdd:PRK13295 536 FRL 538
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
2631-3097 |
1.70e-40 |
|
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: 157.76 E-value: 1.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2631 SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQ 2710
Cdd:cd05907 5 PITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFVE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2711 sahlgimngslpvillddgetrpfdnepdtpldarkqglTPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGI 2790
Cdd:cd05907 85 ---------------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2791 AQEDVLLGVTSLSfdiSILE----IFLPLLNGARLILatqaQAADAQQLAMLIERHAVSFMQAtPSTWRMLVELRDFALP 2866
Cdd:cd05907 126 TEGDRHLSFLPLA---HVFErragLYVPLLAGARIYF----ASSAETLLDDLSEVRPTVFLAV-PRVWEKVYAAIKVKAV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2867 PGFK--------------ALCGGEALPENLATALLQKVTTLWNLYGPTETTIWSTLNGLTTPTP-YIGHPIANTQIYIld 2931
Cdd:cd05907 198 PGLKrklfdlavggrlrfAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIgTVGKPLPGVEVRI-- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2932 aqgrvvplGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGR-NDFQVKVRGF 3010
Cdd:cd05907 276 --------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW--------LHTGDLGEIDEDGFLHITGRkKDLIITSGGK 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3011 RIELGEIETRLARCHGVHDAVVIaredspGDKR--LVA------------------------YLLAQPDTVLEPADLRQR 3064
Cdd:cd05907 340 NISPEPIENALKASPLISQAVVI------GDGRpfLVAlivpdpealeawaeehgiaytdvaELAANPAVRAEIEAAVEA 413
|
490 500 510
....*....|....*....|....*....|....*....
gi 641744967 3065 LSEGVAEYMIPSAFVTL------DAFPLTPNGKLDRKAL 3097
Cdd:cd05907 414 ANARLSRYEQIKKFLLLpepftiENGELTPTLKLKRPVI 452
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1554-2021 |
1.96e-40 |
|
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: 156.35 E-value: 1.96e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPvalltqa 1633
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1634 nqralltgdvprilldtadfshlsednphvpGLDAhhLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRV 1713
Cdd:cd05912 75 -------------------------------KLDD--IATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNW 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1714 LQKTPFsFDVS-VWEFFWPLLYGARLVMARpdgHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADCAcDSLRRVIC 1792
Cdd:cd05912 122 LCALPL-FHISgLSILMRSVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYP-NNLRCILL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1793 SGEALPAEL----QQRffarfNAQLHNLYGPTEAAID-VTFwacQPDD-HRSFVPIGRPIANTQLYILDTLGQPvplGVA 1866
Cdd:cd05912 197 GGGPAPKPLleqcKEK-----GIPVYQSYGMTETCSQiVTL---SPEDaLNKIGSAGKPLFPVELKIEDDGQPP---YEV 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1867 GELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlyKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLM 1946
Cdd:cd05912 266 GEILLKGPNVTKGYLNRPDATEESFENGWF---------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLL 336
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 1947 QCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPdpADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05912 337 SHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISE--EELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1538-2021 |
2.29e-40 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 158.50 E-value: 2.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLFED-QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAER 1616
Cdd:PRK07514 12 AFADRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1617 LAYMLDDASP-VALLTQANQRAL--------------LTGDVPRILLDTAdfSHLSEDNPHVPgLDAHHLAYVIYTSGST 1681
Cdd:PRK07514 92 LDYFIGDAEPaLVVCDPANFAWLskiaaaagaphvetLDADGTGSLLEAA--AAAPDDFETVP-RGADDLAAILYTSGTT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1682 GKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPF--------SFDVSvweffwpLLYGARLV-MARpdghKDAAYL 1752
Cdd:PRK07514 169 GRSKGAMLSHGNLLSNALTLVDYWRFTPDDVLIHALPIfhthglfvATNVA-------LLAGASMIfLPK----FDPDAV 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1753 AQLIERTgiTTLHFVPS----MLQQfvQWADADcACDSLRRVIcSGEA-LPAELQQRFFARFNAQLHNLYGPTEAAIDVT 1827
Cdd:PRK07514 238 LALMPRA--TVMMGVPTfytrLLQE--PRLTRE-AAAHMRLFI-SGSApLLAETHREFQERTGHAILERYGMTETNMNTS 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1828 fwacQP-DDHRSFVPIGRPIANTQLYILD-TLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlY 1905
Cdd:PRK07514 312 ----NPyDGERRAGTVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF--------F 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1906 KTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQE-AVV-VAREDSpGDTrLVAYLCPQPGVTPDPA 1983
Cdd:PRK07514 380 ITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVEsAVIgVPHPDF-GEG-VTAVVVPKPGAALDEA 457
|
490 500 510
....*....|....*....|....*....|....*...
gi 641744967 1984 DLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK07514 458 AILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
2633-3097 |
2.44e-40 |
|
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: 158.95 E-value: 2.44e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2633 SYDELNRRANRLAHHLISFGVRPDERVAIcvergLDM-----VVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVAL 2707
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVAT-----LAWnthrhLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2708 ISQSAHLGI---MNGSLP----VILLDDGETRPFDNEPDTP----LDARKQGLTP-----RHLAYVI-YTSGSTGKPKGV 2770
Cdd:cd12119 102 FVDRDFLPLleaIAPRLPtvehVVVMTDDAAMPEPAGVGVLayeeLLAAESPEYDwpdfdENTAAAIcYTSGTTGNPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2771 MVEHANMV--NFLCSMRKEPGIAQEDVLLGVTSLsFDISILEI-FLPLLNGARLILatQAQAADAQQLAMLIERHAVSFM 2847
Cdd:cd12119 182 VYSHRSLVlhAMAALLTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVL--PGPYLDPASLAELIEREGVTFA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2848 QATPSTWRML---VELRDFALPPGFKALCGGEALPENLATALLQKVTTLWNLYGPTETTIWSTLNGLTT---PTPY---- 2917
Cdd:cd12119 259 AGVPTVWQGLldhLEANGRDLSSLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARPPSehsNLSEdeql 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2918 -----IGHPIANTQIYILDAQGRVVPL-GVA-GEIHIAGAGVVRGYLGRPDlTAERFITDPFsgapearmYKTGDLGRWL 2990
Cdd:cd12119 339 alrakQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDE-ESEALTEDGW--------LRTGDVATID 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2991 PDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVA 3070
Cdd:cd12119 410 EDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLEFLADKVA 489
|
490 500
....*....|....*....|....*..
gi 641744967 3071 EYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd12119 490 KWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
487-966 |
3.51e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 158.61 E-value: 3.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVAL----CVERSLEMMVGLLgilkAGAAYVPMDPAYPAERL 562
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALlslnRPEVLMAIGAAQL----AGLRRTALHPLGSLDDH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 563 AYILDDAAP--------------VALLTQSAQVAQLNSTLPT-VLLDTPAAAACPDTNPVVQGLHAAHLAYVIYTSGSTG 627
Cdd:PRK06188 102 AYVLEDAGIstlivdpapfveraLALLARVPSLKHVLTLGPVpDGVDLLAAAAKFGPAPLVAAALPPDIAGLAYTGGTTG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 628 RPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWIQLLSGHTLVLVPdalRADAHQLWRYFARHAVDL 707
Cdd:PRK06188 182 KPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAFFLPTLLRGGTVIVLA---KFDPAEVLRAIEEQRITA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 708 FDCTPVQLQWLLDAGLGSDPAYQPAQ-VLIGGEAISPAvwsRLQSLSDTR---FINVYGPTECTVdaTACVV-----DRT 778
Cdd:PRK06188 259 TFLVPTMIYALLDHPDLRTRDLSSLEtVYYGASPMSPV---RLAEAIERFgpiFAQYYGQTEAPM--VITYLrkrdhDPD 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 779 QP--LPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFipdpfsadpAARIYKTGDLARWL 856
Cdd:PRK06188 334 DPkrLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF---------RDGWLHTGDVARED 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 857 PDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLA 936
Cdd:PRK06188 405 EDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERKG 484
|
490 500 510
....*....|....*....|....*....|
gi 641744967 937 DYMIPSAFVTLDALPLTPNGKLDRKALPAP 966
Cdd:PRK06188 485 SVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
2616-3096 |
4.66e-40 |
|
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: 158.56 E-value: 4.66e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2616 VACTPDAIAVVF------GEASLSYDELNRRANRLAHHLISFGvRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPT 2689
Cdd:cd05931 3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2690 YP---VERLRYMLDDAKPVALISQSAHLGIMNGSLPVILLDDGETRPF-DNEPDTPLDA-RKQGLTPRHLAYVIYTSGST 2764
Cdd:cd05931 82 TPgrhAERLAAILADAGPRVVLTTAAALAAVRAFAASRPAAGTPRLLVvDLLPDTSAADwPPPSPDPDDIAYLQYTSGST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2765 GKPKGVMVEHANMVNFLCSMRKEPGIAQEDVllGVTSLSF--DIS-ILEIFLPLLNGARLILAtqaqaadaqqlamlier 2841
Cdd:cd05931 162 GTPKGVVVTHRNLLANVRQIRRAYGLDPGDV--VVSWLPLyhDMGlIGGLLTPLYSGGPSVLM----------------- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2842 HAVSFMQAtPSTW-RMLVELR-------DFALppgfkALCGGEALPENLATALLQKVTTLWN------------------ 2895
Cdd:cd05931 223 SPAAFLRR-PLRWlRLISRYRatisaapNFAY-----DLCVRRVRDEDLEGLDLSSWRVALNgaepvrpatlrrfaeafa 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2896 -----------LYGPTETTIWSTLNGLTTPTPYI---------------------------GHPIANTQIYILDAQG-RV 2936
Cdd:cd05931 297 pfgfrpeafrpSYGLAEATLFVSGGPPGTGPVVLrvdrdalagravavaaddpaarelvscGRPLPDQEVRIVDPETgRE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2937 VPLGVAGEIHIAGAGVVRGYLGRPDLTAERFitDPFSGAPEARMYKTGDLGRwLPDGTLEYLGRndfqVK----VRGFRI 3012
Cdd:cd05931 377 LPDGEVGEIWVRGPSVASGYWGRPEATAETF--GALAATDEGGWLRTGDLGF-LHDGELYITGR----LKdliiVRGRNH 449
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3013 ELGEIETRLARCHGV---HDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEY--MIPSAFVTL--DAFP 3085
Cdd:cd05931 450 YPQDIEATAEEAHPAlrpGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREhgVAPADVVLVrpGSIP 529
|
570
....*....|.
gi 641744967 3086 LTPNGKLDRKA 3096
Cdd:cd05931 530 RTSSGKIQRRA 540
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
480-967 |
6.72e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 158.17 E-value: 6.72e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 480 EAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPA 559
Cdd:PRK07788 56 AHAARRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 560 ERL----------AYILDDAAPVALLTQSAQVAQLNSTLPTVLLDTPAAAACPDTNPVVQGLHAA-------HLAYVIYT 622
Cdd:PRK07788 136 PQLaevaaregvkALVYDDEFTDLLSALPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAplpkppkPGGIVILT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 623 SGSTGRPKGVMVAHrnvinlATGLHTLLA-LDH-PSR----IALNASIVFDASVKNW-IQLLSGHTLVLvpdALRADAHQ 695
Cdd:PRK07788 216 SGTTGTPKGAPRPE------PSPLAPLAGlLSRvPFRagetTLLPAPMFHATGWAHLtLAMALGSTVVL---RRRFDPEA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 696 LWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQ---VLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATA 772
Cdd:PRK07788 287 TLEDIAKHKATALVVVPVMLSRILDLGPEVLAKYDTSSlkiIFVSGSALSPELATRALEAFGPVLYNLYGSTEVAFATIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 773 CVVDRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYlhrpdlTAERfipDPFSADPaarIYKTGDL 852
Cdd:PRK07788 367 TPEDLAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR---DKQIIDG---LLSSGDV 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 853 ARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLA 932
Cdd:PRK07788 435 GYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIKDYVR 514
|
490 500 510
....*....|....*....|....*....|....*
gi 641744967 933 ASLADYMIPSAFVTLDALPLTPNGKLDRKALPAPD 967
Cdd:PRK07788 515 DNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1549-2016 |
7.41e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 156.99 E-value: 7.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1549 FEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVA 1628
Cdd:PRK08276 7 PSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1629 LLTQANQR-------ALLTGDVPRILLDTAD------FSHLSEDNPHVPGLDAHHLAYVIYTSGSTGKPKGVMNS----- 1690
Cdd:PRK08276 87 LIVSAALAdtaaelaAELPAGVPLLLVVAGPvpgfrsYEEALAAQPDTPIADETAGADMLYSSGTTGRPKGIKRPlpgld 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1691 -HRALCNRLVWMQNTYRLTPDDRVLQKTPF------SFDVSVweffwpLLYGARLV-MARPDGHKdaaYLAqLIERTGIT 1762
Cdd:PRK08276 167 pDEAPGMMLALLGFGMYGGPDSVYLSPAPLyhtaplRFGMSA------LALGGTVVvMEKFDAEE---ALA-LIERYRVT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1763 TLHFVPSMLQQFVQWADA-----DCAcdSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEaAIDVTFwaCQPDD-- 1835
Cdd:PRK08276 237 HSQLVPTMFVRMLKLPEEvraryDVS--SLRVAIHAAAPCPVEVKRAMIDWWGPIIHEYYASSE-GGGVTV--ITSEDwl 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1836 -HRSFVpiGRPIAnTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAErfipdpfiNQPGARLYKTGDLArWL 1914
Cdd:PRK08276 312 aHPGSV--GKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAA--------ARNPHGWVTVGDVG-YL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1915 -PDGSLeYL-GRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPA---DLRQQL 1989
Cdd:PRK08276 380 dEDGYL-YLtDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADGADAGDAlaaELIAWL 458
|
490 500
....*....|....*....|....*..
gi 641744967 1990 GQHLAEYMVPGAFVTLDAFPLTPNGKL 2016
Cdd:PRK08276 459 RGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
499-963 |
1.09e-39 |
|
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: 154.80 E-value: 1.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQS 578
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 AQVAqlnstlptvlldtpaaaacpdtnpvvqglhaahlaYVIYTSGSTGRPKGVMVAHRnvINLATGLHTLLALD-HPSr 657
Cdd:cd05972 81 EDPA-----------------------------------LIYFTSGTTGLPKGVLHTHS--YPLGHIPTAAYWLGlRPD- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 658 ialnaSIVFDASVKNWI---------QLLSGHTlVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLgsdPA 728
Cdd:cd05972 123 -----DIHWNIADPGWAkgawssffgPWLLGAT-VFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDL---SS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 729 YQPAQ---VLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVdatACVVDRTQPL-P-TIGKPLANTRLYILDAQDQPV 803
Cdd:cd05972 194 YKFSHlrlVVSAGEPLNPEVIEWWRAATGLPIRDGYGQTETGL---TVGNFPDMPVkPgSMGRPTPGYDVAIIDDDGREL 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 804 PIGVTGEL--HIGGAGVARGYLHRPDLTAERFIPDpfsadpaarIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAG 881
Cdd:cd05972 271 PPGEEGDIaiKLPPPGLFLGYVGDPEKTEASIRGD---------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPF 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 882 EIESRLLRCPGVQDAVVIAREDsPGDTRLV-AYLCARPDAELHPA---ALRQQLAASLADYMIPS--AFVtlDALPLTPN 955
Cdd:cd05972 342 EVESALLEHPAVAEAAVVGSPD-PVRGEVVkAFVVLTSGYEPSEElaeELQGHVKKVLAPYKYPReiEFV--EELPKTIS 418
|
....*...
gi 641744967 956 GKLDRKAL 963
Cdd:cd05972 419 GKIRRVEL 426
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
483-962 |
3.92e-39 |
|
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: 155.86 E-value: 3.92e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLF------EDQHLTYRELNRRANQLAHHLIALGvQPDDRVALCVERSLEMMVGLLGILKAGAAYVPM--- 553
Cdd:cd05931 3 AAARPDRPAYTFlddeggREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLppp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 554 DPAYPAERLAYILDDAAPVALLTQSAQVAQL---------NSTLPTVLLDTPAAAACPDTNPVVQGLHAahLAYVIYTSG 624
Cdd:cd05931 82 TPGRHAERLAAILADAGPRVVLTTAAALAAVrafaasrpaAGTPRLLVVDLLPDTSAADWPPPSPDPDD--IAYLQYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 625 STGRPKGVMVAHRNVINLATGLHTLLALDHPSRIA--------------LNASIVFDAS---------VKN---WIQLLS 678
Cdd:cd05931 160 STGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVswlplyhdmgliggLLTPLYSGGPsvlmspaafLRRplrWLRLIS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 679 GHTLVL--VPDalradahqlwryFA-RHAVDLF---DCTPVQLQWLLDAGLGSDP-----------AYQPAqvligG--- 738
Cdd:cd05931 240 RYRATIsaAPN------------FAyDLCVRRVrdeDLEGLDLSSWRVALNGAEPvrpatlrrfaeAFAPF-----Gfrp 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 739 EAISPA--------------VWSRLQSLSDTRFINvygptECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQD-QPV 803
Cdd:cd05931 303 EAFRPSyglaeatlfvsggpPGTGPVVLRVDRDAL-----AGRAVAVAADDPAARELVSCGRPLPDQEVRIVDPETgREL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 804 PIGVTGELHIGGAGVARGYLHRPDLTAERFipDPFSADPAARIYKTGDLARwLPDGNIDYLGRNDFQIKVRGFRIEAGEI 883
Cdd:cd05931 378 PDGEVGEIWVRGPSVASGYWGRPEATAETF--GALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDI 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 884 ESRLLRCPGVQD---AVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADY--MIPSAFVTL--DALPLTPNG 956
Cdd:cd05931 455 EATAEEAHPALRpgcVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVAREhgVAPADVVLVrpGSIPRTSSG 534
|
....*.
gi 641744967 957 KLDRKA 962
Cdd:cd05931 535 KIQRRA 540
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
2619-3097 |
5.46e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 155.97 E-value: 5.46e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2619 TPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYM 2698
Cdd:PRK06178 46 RPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2699 LDDAKPVALISQSAHLGIMNG-----------------------SLPV-------ILLDDGETRPFDNEPDTPLDARKQG 2748
Cdd:PRK06178 126 LNDAGAEVLLALDQLAPVVEQvraetslrhvivtsladvlpaepTLPLpdslrapRLAAAGAIDLLPALRACTAPVPLPP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2749 LTPRHLAYVIYTSGSTGKPKGVMVEHANMV-----NFLCSMRkepgIAQEDVLLGVTSLsFDIS--ILEIFLPLLNGARL 2821
Cdd:PRK06178 206 PALDALAALNYTGGTTGMPKGCEHTQRDMVytaaaAYAVAVV----GGEDSVFLSFLPE-FWIAgeNFGLLFPLFSGATL 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2822 ILatqaqaadaqqlamLIERHAVSFMQATP----STWRMLV----ELRDFalpPGFKALcGGEALPENLATALLQKVTT- 2892
Cdd:PRK06178 281 VL--------------LARWDAVAFMAAVEryrvTRTVMLVdnavELMDH---PRFAEY-DLSSLRQVRVVSFVKKLNPd 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2893 ---LWN----------LYGPTETtiwSTLNGLTT------------PTpYIGHPIANTQIYILDAQ-GRVVPLGVAGEIH 2946
Cdd:PRK06178 343 yrqRWRaltgsvlaeaAWGMTET---HTCDTFTAgfqdddfdllsqPV-FVGLPVPGTEFKICDFEtGELLPLGAEGEIV 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2947 IAGAGVVRGYLGRPDLTAERFitdpfsgapEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHG 3026
Cdd:PRK06178 419 VRTPSLLKGYWNKPEATAEAL---------RDGWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPA 489
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641744967 3027 VHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVtLDAFPLTPNGKLDRKAL 3097
Cdd:PRK06178 490 VLGSAVVGRPDPDKGQVPVAFVQLKPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDL 559
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
470-978 |
6.42e-39 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 155.30 E-value: 6.42e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 470 PREMLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAA 549
Cdd:PRK06155 18 PSERTLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 550 YVPMDPAYPAERLAYILDDAAPVALLTQSAQVAQLNSTLPTV-------LLDTPAAAACP---DTNPVVQGLHAA----- 614
Cdd:PRK06155 98 AVPINTALRGPQLEHILRNSGARLLVVEAALLAALEAADPGDlplpavwLLDAPASVSVPagwSTAPLPPLDAPApaaav 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 615 ---HLAYVIYTSGSTGRPKGVMVAHRNV----INLATGLH--------TLLALDHPSriALNAsiVFDAsvknwiqLLSG 679
Cdd:PRK06155 178 qpgDTAAILYTSGTTGPSKGVCCPHAQFywwgRNSAEDLEigaddvlyTTLPLFHTN--ALNA--FFQA-------LLAG 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 680 HTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVliggeAISPAVWSRLQSLSDTRF-- 757
Cdd:PRK06155 247 ATYVLEP---RFSASGFWPAVRRHGATVTYLLGAMVSILLSQPARESDRAHRVRV-----ALGPGVPAALHAAFRERFgv 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 758 --INVYGPTECTVdatACVVDRTQPLP-TIGKPLANTRLYILDAQDQPVPIGVTGELHIGGA---GVARGYLHRPDLTAE 831
Cdd:PRK06155 319 dlLDGYGSTETNF---VIAVTHGSQRPgSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfAFATGYFGMPEKTVE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 832 rfipdpfsadpAAR--IYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTR 909
Cdd:PRK06155 396 -----------AWRnlWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDE 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 910 LVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAPDQTAfATRDYEA 978
Cdd:PRK06155 465 VMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVTA-DTWDREA 532
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
2624-3097 |
6.44e-39 |
|
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: 152.62 E-value: 6.44e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2624 AVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAK 2703
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2704 PVALISQSahlgimngslpvillDDgetrpfdnepdtpldarkqgltprhLAYVIYTSGSTGKPKGVMVEHANMVNFLCS 2783
Cdd:cd05919 83 ARLVVTSA---------------DD-------------------------IAYLLYSSGTTGPPKGVMHAHRDPLLFADA 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2784 MRKEP-GIAQEDVLLGVTSLSFDISI-LEIFLPLLNGARLILATQAQAADAQQLamLIERHAVSFMQATPSTWRMLVELR 2861
Cdd:cd05919 123 MAREAlGLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLNPGWPTAERVLA--TLARFRPTVLYGVPTFYANLLDSC 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2862 DFAlPPGFKAL----CGGEALPENLATALLQkvTTLwnlyGPTETTIWSTLNGLT----TPTPY----IGHPIANTQIYI 2929
Cdd:cd05919 201 AGS-PDALRSLrlcvSAGEALPRGLGERWME--HFG----GPILDGIGATEVGHIflsnRPGAWrlgsTGRPVPGYEIRL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2930 LDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFitdpfsgapEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRG 3009
Cdd:cd05919 274 VDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF---------NGGWYRTGDKFCRDADGWYTHAGRADDMLKVGG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3010 FRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPA---DLRQRLSEGVAEYMIPSAFVTLDAFPL 3086
Cdd:cd05919 345 QWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESlarDIHRHLLERLSAHKVPRRIAFVDELPR 424
|
490
....*....|.
gi 641744967 3087 TPNGKLDRKAL 3097
Cdd:cd05919 425 TATGKLQRFKL 435
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
480-963 |
9.65e-39 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 153.48 E-value: 9.65e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 480 EAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLI-ALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYP 558
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 559 AERLAYILDDAAPVALLTQ------SAQVAQLNSTLPTVLLDTPAAAACPDTNPVVQGLHAAHLaYVIYTSGSTGRPKGV 632
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEktfqnmALSMQKVSYVQRVISITSLKEIEDRKIDNFVEKNESASF-IICYTSGTTGKPKGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 633 MVAHRNVinLATGLHTLLALDHPSRialNASIVFDASVK-NWIQLLSGHTL-----VLVPDalRADAHQLWRYFARHAVD 706
Cdd:PRK06839 168 VLTQENM--FWNALNNTFAIDLTMH---DRSIVLLPLFHiGGIGLFAFPTLfaggvIIVPR--KFEPTKALSMIEKHKVT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 707 LFDCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTEctvdaTACVV------DRTQP 780
Cdd:PRK06839 241 VVMGVPTIHQALINCSKFETTNLQSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTE-----TSPTVfmlseeDARRK 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 781 LPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERfIPDPFsadpaariYKTGDLARWLPDGN 860
Cdd:PRK06839 316 VGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW--------LCTGDLARVDEDGF 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 861 IDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMI 940
Cdd:PRK06839 387 VYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAKYKI 466
|
490 500
....*....|....*....|...
gi 641744967 941 PSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK06839 467 PKEIVFLKELPKNATGKIQKAQL 489
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1551-2024 |
2.80e-38 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 152.55 E-value: 2.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1551 DQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALL 1630
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1631 TQANQRALLTGDVP------------------RILLD-------TADFSHLSEDNPHVPGLDAHHLAYVIYTSGSTGKPK 1685
Cdd:PRK12406 89 AHADLLHGLASALPagvtvlsvptppeiaaayRISPAlltppagAIDWEGWLAQQEPYDGPPVPQPQSMIYTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1686 GVMNSHRALCNRLVWMQN---TYRLTPDDRVL------QKTPFSFDVSVWEFfwpllyGARLV-MARpdghKDAAYLAQL 1755
Cdd:PRK12406 169 GVRRAAPTPEQAAAAEQMralIYGLKPGIRALltgplyHSAPNAYGLRAGRL------GGVLVlQPR----FDPEELLQL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1756 IERTGITTLHFVPSMLQQFVQWADADCA---CDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIdVTFwaCQ 1832
Cdd:PRK12406 239 IERHRITHMHMVPTMFIRLLKLPEEVRAkydVSSLRHVIHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGA-VTF--AT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1833 PDDHRSFvP--IGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVAR-GYLNRPDLTAErfipdpfINQPGarLYKTGD 1909
Cdd:PRK12406 316 SEDALSH-PgtVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE-------IDRGG--FITSGD 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1910 LARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQL 1989
Cdd:PRK12406 386 VGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQPGATLDEADIRAQL 465
|
490 500 510
....*....|....*....|....*....|....*
gi 641744967 1990 GQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPAP 2024
Cdd:PRK12406 466 KARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
472-963 |
2.82e-38 |
|
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: 152.28 E-value: 2.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 472 EMLiqqRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYV 551
Cdd:cd05923 5 EML---RRAASRAPDACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 552 PMDPAYPAERLAY-ILDDAAPVALLTQSAQVAQLNSTLPTVLL----DTPAAAACPDTNPV-VQGLHAAHLAYVIYTSGS 625
Cdd:cd05923 82 LINPRLKAAELAElIERGEMTAAVIAVDAQVMDAIFQSGVRVLalsdLVGLGEPESAGPLIeDPPREPEQPAFVFYTSGT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 626 TGRPKGVMVAHR----NVINLAT------GLHT----LLALDHPS--RIALNASIVFDAsvknwiqllsghTLVLVPDAL 689
Cdd:cd05923 162 TGLPKGAVIPQRaaesRVLFMSTqaglrhGRHNvvlgLMPLYHVIgfFAVLVAALALDG------------TYVVVEEFD 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 690 RADAHQLwryFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLI-GGEAISPAVWSRLQSLSDTRFINVYGPTEctv 768
Cdd:cd05923 230 PADALKL---IEQERVTSLFATPTHLDALAAAAEFAGLKLSSLRHVTfAGATMPDAVLERVNQHLPGEKVNIYGTTE--- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 769 dATACVVDRTQPLPTIGKPLANTRLY---ILDAQDQPVPIGVTGELHIGGAGVA--RGYLHRPDLTAERFipdpfsadpA 843
Cdd:cd05923 304 -AMNSLYMRDARTGTEMRPGFFSEVRivrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKL---------Q 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 844 ARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPdAELH 923
Cdd:cd05923 374 DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPRE-GTLS 452
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 641744967 924 PAALRQ-QLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05923 453 ADELDQfCRASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1538-2021 |
3.02e-38 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 152.54 E-value: 3.02e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLF--EDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAE 1615
Cdd:PRK13391 7 AQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1616 RLAYMLDDASPVALLTQANQR---ALLTGDVP----RILLDTAD-------FSHLSEDNPHVPGLDAHHLAYVIYTSGST 1681
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLdvaRALLKQCPgvrhRLVLDGDGelegfvgYAEAVAGLPATPIADESLGTDMLYSSGTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1682 GKPKGVMN-----------SHRALCNRLvwmqntYRLTPDDRVLQKTPFSFDVsvweffwPLLY--------GARLVMAr 1742
Cdd:PRK13391 167 GRPKGIKRplpeqppdtplPLTAFLQRL------WGFRSDMVYLSPAPLYHSA-------PQRAvmlvirlgGTVIVME- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1743 pdgHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADA-----DCAcdSLRRVICSGEALPAELQQRFFARFNAQLHNLY 1817
Cdd:PRK13391 233 ---HFDAEQYLALIEEYGVTHTQLVPTMFSRMLKLPEEvrdkyDLS--SLEVAIHAAAPCPPQVKEQMIDWWGPIIHEYY 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1818 GPTEAaidVTFWACQPDD---HRSFVpiGRPIANTqLYILDTLGQPVPLGVAGELHIGGvGVARGYLNRPDLTAERFIPD 1894
Cdd:PRK13391 308 AATEG---LGFTACDSEEwlaHPGTV--GRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPD 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1895 PfinqpgaRLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCP 1974
Cdd:PRK13391 381 G-------TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGEEVKAVVQP 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 641744967 1975 QPGVTPDPA---DLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK13391 454 VDGVDPGPAlaaELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
2602-3097 |
3.14e-38 |
|
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: 152.39 E-value: 3.14e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2602 IPRHALIHELFEAQVACTPDAIAVVFGE--ASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKA 2679
Cdd:cd05904 1 LPTDLPLDSVSFLFASAHPSRPALIDAAtgRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2680 GGAYVPLDPTYPVERLRYMLDDAKPVALISQSAHLG-IMNGSLPVILLDDGETRPFDNEPDT----PLDARKQGLTPRHL 2754
Cdd:cd05904 81 GAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAELAEkLASLALPVVLLDSAEFDSLSFSDLLfeadEAEPPVVVIKQDDV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2755 AYVIYTSGSTGKPKGVMVEHANMVNFLCS--MRKEPGIAQEDVLLGVTSLsFDISILEIFL--PLLNGARLILATQAQAA 2830
Cdd:cd05904 161 AALLYSSGTTGRSKGVMLTHRNLIAMVAQfvAGEGSNSDSEDVFLCVLPM-FHIYGLSSFAlgLLRLGATVVVMPRFDLE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2831 DAQQlamLIERHAVSFMQATPStwrMLVELRDFALPPGF------KALCGGEALPENLATALLQKVTT--LWNLYGPTET 2902
Cdd:cd05904 240 ELLA---AIERYKVTHLPVVPP---IVLALVKSPIVDKYdlsslrQIMSGAAPLGKELIEAFRAKFPNvdLGQGYGMTES 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2903 T--IWSTLNGLTTPTPY--IGHPIANTQIYILD-AQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgape 2977
Cdd:cd05904 314 TgvVAMCFAPEKDRAKYgsVGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW----- 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2978 armYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLE 3057
Cdd:cd05904 389 ---LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVRKPGSSLT 465
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 641744967 3058 PADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05904 466 EDEIMDFVAKQVAPYKKVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1538-2021 |
4.63e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 151.58 E-value: 4.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERL 1617
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1618 AYMLDDASPVALLTQANQRALLTGDVPRILLDT---ADFSHLSEdnPHVPGLDAH-----HLAYVIYTSGSTGKPKGVMN 1689
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFDAIVALETPKIVIDAaaqADSRRLAQ--GGLEIPPQAavaptDLVRLMYTSGTTDRPKGVMH 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1690 SHRALCNRLVWMQNTYRLTPDDRVLQKTPF----SFDVSVWEFFWpllYGARLVMARpdgHKDAAYLAQLIERTGITTLH 1765
Cdd:PRK06145 170 SYGNLHWKSIDHVIALGLTASERLLVVGPLyhvgAFDLPGIAVLW---VGGTLRIHR---EFDPEAVLAAIERHRLTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1766 FVPSMLQQFVQWADAD-CACDSLRRVICSGEALPaELQQRFFARF--NAQLHNLYGPTEAAIDVTFWAcQPDDHRSFVPI 1842
Cdd:PRK06145 244 MAPVMLSRVLTVPDRDrFDLDSLAWCIGGGEKTP-ESRIRDFTRVftRARYIDAYGLTETCSGDTLME-AGREIEKIGST 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1843 GRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlyKTGDLARWLPDGSLEYL 1922
Cdd:PRK06145 322 GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF---------RSGDVGYLDEEGFLYLT 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1923 GRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAF 2002
Cdd:PRK06145 393 DRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQL 472
|
490
....*....|....*....
gi 641744967 2003 VTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK06145 473 KVRDELPRNPSGKVLKRVL 491
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
2601-3092 |
6.74e-38 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 152.04 E-value: 6.74e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2601 DIPRHALIHELfEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLIS-FGVRPDERVAICVERGLDMVVGLLGILKA 2679
Cdd:PRK08314 6 TLPETSLFHNL-EVSARRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQeCGVRKGDRVLLYMQNSPQFVIAYYAILRA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2680 GGAYVPLDPTYPVERLRYMLDDAKPVALISQS---------------AHLGIMNGS----------LPVILLDDGETRPF 2734
Cdd:PRK08314 85 NAVVVPVNPMNREEELAHYVTDSGARVAIVGSelapkvapavgnlrlRHVIVAQYSdylpaepeiaVPAWLRAEPPLQAL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2735 DNEPDTPL-DARKQGLTPR-------HLAYVIYTSGSTGKPKGVMVEHAN-MVNFLCSMRKEpGIAQEDVLLGVTSLsFD 2805
Cdd:PRK08314 165 APGGVVAWkEALAAGLAPPphtagpdDLAVLPYTSGTTGVPKGCMHTHRTvMANAVGSVLWS-NSTPESVVLAVLPL-FH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2806 ISILEIFL--PLLNGARLILATQAQAADAQQlamLIERHAVSFMQATPStwrMLVelrDFALPPGFKALC---------G 2874
Cdd:PRK08314 243 VTGMVHSMnaPIYAGATVVLMPRWDREAAAR---LIERYRVTHWTNIPT---MVV---DFLASPGLAERDlsslryiggG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2875 GEALPEnlatALLQKVTTLWNL-----YGPTETTIWSTLNGLTTPTPY-IGHPIANTQIYILDAQ-GRVVPLGVAGEIHI 2947
Cdd:PRK08314 314 GAAMPE----AVAERLKELTGLdyvegYGLTETMAQTHSNPPDRPKLQcLGIPTFGVDARVIDPEtLEELPPGEVGEIVV 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2948 AGAGVVRGYLGRPDLTAERFITdpFSGapeARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGV 3027
Cdd:PRK08314 390 HGPQVFKGYWNRPEATAEAFIE--IDG---KRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAI 464
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 3028 HDAVVIAREDSPGDKRLVAYLLAQPDTV--LEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKL 3092
Cdd:PRK08314 465 QEACVIATPDPRRGETVKAVVVLRPEARgkTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
448-963 |
9.10e-38 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 151.74 E-value: 9.10e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 448 PILPKSERQQvlvdfnATDADFPREMLIQQRFEAQAEQTPEAIAVL------FEDQHLTYRELNRRANQLAHHLIALGVQ 521
Cdd:PRK13295 5 AVLLPPRRAA------SIAAGHWHDRTINDDLDACVASCPDKTAVTavrlgtGAPRRFTYRELAALVDRVAVGLARLGVG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 522 PDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDA-APVALLTQS-------AQVAQLNSTLPTV-- 591
Cdd:PRK13295 79 RGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAeSKVLVVPKTfrgfdhaAMARRLRPELPALrh 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 592 --------------LLDTPAAAACPDTNPVVQGLH--AAHLAYVIYTSGSTGRPKGVMVAHrnvinlatglHTLLALDHP 655
Cdd:PRK13295 159 vvvvggdgadsfeaLLITPAWEQEPDAPAILARLRpgPDDVTQLIYTSGTTGEPKGVMHTA----------NTLMANIVP 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 656 --SRIALNA-SIVFDASVknwiqlLSGHT----LVLVPDALRADA--HQLWRyfARHAVDLFDCTPVQLQ-----WLLD- 720
Cdd:PRK13295 229 yaERLGLGAdDVILMASP------MAHQTgfmyGLMMPVMLGATAvlQDIWD--PARAAELIRTEGVTFTmastpFLTDl 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 721 AGLGSDPAYQPAQV---LIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPL-PTIGKPLANTRLYIL 796
Cdd:PRK13295 301 TRAVKESGRPVSSLrtfLCAGAPIPGALVERARAALGAKIVSAWGMTENGAVTLTKLDDPDERAsTTDGCPLPGVEVRVV 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 797 DAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTaerfipdpfsADPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGF 876
Cdd:PRK13295 381 DADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLN----------GTDADGWFDTGDLARIDADGYIRISGRSKDVIIRGGE 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 877 RIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQL-AASLADYMIPSAFVTLDALPLTPN 955
Cdd:PRK13295 451 NIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAFVVPRPGQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPS 530
|
....*...
gi 641744967 956 GKLDRKAL 963
Cdd:PRK13295 531 GKIQKFRL 538
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
499-963 |
9.57e-38 |
|
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: 148.65 E-value: 9.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPvalltqs 578
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDV------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 aqvaQLNSTlptvlldtpaaaacpdtnpvvqglhaahlAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSR- 657
Cdd:cd05912 75 ----KLDDI-----------------------------ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDDNw 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 658 -IAL------NASIVFDasvknwiQLLSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPaYQ 730
Cdd:cd05912 122 lCALplfhisGLSILMR-------SVIYGMTVYLVD---KFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYP-NN 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 731 PAQVLIGGEAISPAVWSRLQSLsDTRFINVYGPTE-CTVDATACVVDRTQPLPTIGKPLANTRLYIldAQDQPVPIGVtG 809
Cdd:cd05912 191 LRCILLGGGPAPKPLLEQCKEK-GIPVYQSYGMTEtCSQIVTLSPEDALNKIGSAGKPLFPVELKI--EDDGQPPYEV-G 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 810 ELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariyKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLR 889
Cdd:cd05912 267 EILLKGPNVTKGYLNRPDATEESFENGWF---------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLS 337
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641744967 890 CPGVQDAVVIAREDSPGDTRLVAYLCArpDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05912 338 HPAIKEAGVVGIPDDKWGQVPVAFVVS--ERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
2161-2532 |
9.95e-38 |
|
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: 149.00 E-value: 9.95e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2161 IYPLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCWQDLSQPVQVV-------Wr 2233
Cdd:cd19547 1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVrddlappW- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2234 qAILPINHFEPTSPEDVLAQLQAhtEPRTRRIDLSQAPLFRADIAHDPLQNEWLLaLSFHHLISDHMTLALIVGEI-RL- 2311
Cdd:cd19547 80 -ALLDWSGEDPDRRAELLERLLA--DDRAAGLSLADCPLYRLTLVRLGGGRHYLL-WSHHHILLDGWCLSLIWGDVfRVy 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2312 --LLQHQADALPTPLPYRNFIA--QTLSVPNSAHEAYFRDKLADVdEPTaPFGLLNVQGSgGDIHEARLVLDATLASAIR 2387
Cdd:cd19547 156 eeLAHGREPQLSPCRPYRDYVRwiRARTAQSEESERFWREYLRDL-TPS-PFSTAPADRE-GEFDTVVHEFPEQLTRLVN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2388 QQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRLAGAEGADRIMGMFINTLPLRISL-ADRGAAEVVERTSHD 2466
Cdd:cd19547 233 EAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLdPDQTVTGLLETIHRD 312
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641744967 2467 LMTLLEHEQAPLAL------AQRCSGVAppmpLFSTLLNYR-HTQASSTDNTLS-DIRVLTSEERTNYPLTLAV 2532
Cdd:cd19547 313 LATTAAHGHVPLAQikswasGERLSGGR----VFDNLVAFEnYPEDNLPGDDLSiQIIDLHAQEKTEYPIGLIV 382
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
2619-3097 |
1.40e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 149.73 E-value: 1.40e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2619 TPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYM 2698
Cdd:PRK03640 15 TPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2699 LDDAKPVALISQSAHLGIMNGSLPVIL--LDDGETRPFDNEPDTPLDArkqgltprhLAYVIYTSGSTGKPKGVMVEHAN 2776
Cdd:PRK03640 95 LDDAEVKCLITDDDFEAKLIPGISVKFaeLMNGPKEEAEIQEEFDLDE---------VATIMYTSGTTGKPKGVIQTYGN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2777 --------MVNFlcsmrkepGIAQEDVLLGVTSLsFDISILEI-FLPLLNGARLILATQAQAADAQQlamLIERHAVSFM 2847
Cdd:PRK03640 166 hwwsavgsALNL--------GLTEDDCWLAAVPI-FHISGLSIlMRSVIYGMRVVLVEKFDAEKINK---LLQTGGVTII 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2848 QATPSTW-RMLVELRDFALPPGFKA--LCGGEALPENLATAlLQKVTTLWNLYGPTETTiwSTLngLTTPTPYI------ 2918
Cdd:PRK03640 234 SVVSTMLqRLLERLGEGTYPSSFRCmlLGGGPAPKPLLEQC-KEKGIPVYQSYGMTETA--SQI--VTLSPEDAltklgs 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2919 -GHPIANTQIYILDaQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmyKTGDLGRWLPDGTLEY 2997
Cdd:PRK03640 309 aGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF---------KTGDIGYLDEEGFLYV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2998 LGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAqpDTVLEPADLRQRLSEGVAEYMIPSA 3077
Cdd:PRK03640 379 LDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVK--SGEVTEEELRHFCEEKLAKYKVPKR 456
|
490 500
....*....|....*....|
gi 641744967 3078 FVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK03640 457 FYFVEELPRNASGKLLRHEL 476
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1530-2018 |
1.42e-37 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 151.46 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFEDQHL--TYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVP 1607
Cdd:PRK12583 20 IGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1608 LDPGYPAERLAYMLDDASPVALLTQANQR-----ALLTGDVPRIL------LDTADFSHLS-------EDNPHV------ 1663
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICADAFKtsdyhAMLQELLPGLAegqpgaLACERLPELRgvvslapAPPPGFlawhel 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1664 ----------------PGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPF--SFDVsV 1725
Cdd:PRK12583 180 qargetvsrealaerqASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhCFGM-V 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1726 WEFFWPLLYGARLVMarPDGHKDAAYLAQLIERTGITTLHFVPSMlqqFV------QWADADCAcdSLRRVICSGEALPA 1799
Cdd:PRK12583 259 LANLGCMTVGACLVY--PNEAFDPLATLQAVEEERCTALYGVPTM---FIaeldhpQRGNFDLS--SLRTGIMAGAPCPI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1800 ELQQRFFARFN-AQLHNLYGPTEAAiDVTFWACQPDD-HRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVA 1877
Cdd:PRK12583 332 EVMRRVMDEMHmAEVQIAYGMTETS-PVSLQTTAADDlERRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVM 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1878 RGYLNRPDLTAERFIPDPFINqpgarlykTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVV 1957
Cdd:PRK12583 411 KGYWNNPEATAESIDEDGWMH--------TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVF 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641744967 1958 AREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDR 2018
Cdd:PRK12583 483 GVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1554-2021 |
1.88e-37 |
|
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: 148.44 E-value: 1.88e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQA 1633
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1634 NQRALLTGDVprilldtadFSHLSednphvpgldahhlayviyTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRv 1713
Cdd:cd05973 81 ANRHKLDSDP---------FVMMF-------------------TSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDS- 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1714 lqktpfsfdvsvwefFWPL--------LYGA---RLVMARPDGHKDAAYLAQL----IERTGITTLHFVPSMLQQFVQwA 1778
Cdd:cd05973 132 ---------------FWNAadpgwaygLYYAitgPLALGHPTILLEGGFSVEStwrvIERLGVTNLAGSPTAYRLLMA-A 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1779 DADCACD---SLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDV-TFWACQPDDHRSfvPIGRPIANTQLYIL 1854
Cdd:cd05973 196 GAEVPARpkgRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELGMVLaNHHALEHPVHAG--SAGRAMPGWRVAVL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1855 DTLGQPVPLGVAGELHIggvGVAR-------GYLNRPDLTaerfipdpfinqPGARLYKTGDLARWLPDGSLEYLGRNDF 1927
Cdd:cd05973 274 DDDGDELGPGEPGRLAI---DIANsplmwfrGYQLPDTPA------------IDGGYYLTGDTVEFDPDGSFSFIGRADD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1928 QVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDsPGDTRLV-AYLCPQPGVTPDPA---DLRQQLGQHLAEYMVPGAFV 2003
Cdd:cd05973 339 VITMSGYRIGPFDVESALIEHPAVAEAAVIGVPD-PERTEVVkAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPRTIH 417
|
490
....*....|....*...
gi 641744967 2004 TLDAFPLTPNGKLDRKAL 2021
Cdd:cd05973 418 FVDELPKTPSGKIQRFLL 435
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
482-963 |
4.79e-37 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 149.51 E-value: 4.79e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 482 QAEQTPEAIAVLfeDQH---LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYP 558
Cdd:PRK06087 32 TARAMPDKIAVV--DNHgasYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWR 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 559 AERLAYILDDAAPVALLTQS------------AQVAQLNSTLPTVLLD-------TPAAAACPDTNPVVQG---LHAAHL 616
Cdd:PRK06087 110 EAELVWVLNKCQAKMFFAPTlfkqtrpvdlilPLQNQLPQLQQIVGVDklapatsSLSLSQIIADYEPLTTaitTHGDEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 617 AYVIYTSGSTGRPKGVMVAHRNVI----NLATGLHtLLALD---HPSriALNASIVFDASVKnwIQLLSGHTLVLvpdal 689
Cdd:PRK06087 190 AAVLFTSGTEGLPKGVMLTHNNILaserAYCARLN-LTWQDvfmMPA--PLGHATGFLHGVT--APFLIGARSVL----- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 690 radahqLWRYFARHAVDLFD---CTpvqlqWLLDAG---------LGSDPAYQPA-QVLIGGEAISPAVWSRLQSLSDTR 756
Cdd:PRK06087 260 ------LDIFTPDACLALLEqqrCT-----CMLGATpfiydllnlLEKQPADLSAlRFFLCGGTTIPKKVARECQQRGIK 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 757 FINVYGPTECTVDAtacVVDRTQPLP----TIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAER 832
Cdd:PRK06087 329 LLSVYGSTESSPHA---VVNLDDPLSrfmhTDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARA 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 833 FIPDPFsadpaariYKTGDLARWLPDGNIDYLGRNDfQIKVRGFR-IEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLV 911
Cdd:PRK06087 406 LDEEGW--------YYSGDLCRMDEAGYIKITGRKK-DIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDERLGERSC 476
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 912 AYlcARPDAELHPAALRQQLA----ASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK06087 477 AY--VVLKAPHHSLTLEEVVAffsrKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
28-435 |
4.92e-37 |
|
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: 145.90 E-value: 4.92e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 28 IYPLAPLQEGiLFHYQLQEKGDtYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICWQGLHQPVQVVWRQAPLTVN 107
Cdd:cd19545 1 IYPCTPLQEG-LMALTARQPGA-YVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISWT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 108 TltTTSSDTVPAQLRAATdpsnHRLNlsnAPLLSATTAHDPVCGEWLLsLSIHHLISDHITQALIIDEIRLLLEDRPeaL 187
Cdd:cd19545 79 E--STSLDEYLEEDRAAP----MGLG---GPLVRLALVEDPDTERYFV-WTIHHALYDGWSLPLILRQVLAAYQGEP--V 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 188 PKPLPYRNFIAQILSVPLSEHEQYFRNRLADIDTPTAPfdlvdvqgngeditEARLSLDSSLADALRRQARHL------G 261
Cdd:cd19545 147 PQPPPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPAVFP--------------PLPSSRYQPRPDATLEHSISLpssassG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 262 ISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRlqgNL---GADRVMGMFINTLPLRVSL-RERSVHDVVQATSHELMML 337
Cdd:cd19545 213 VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGR---NApvpGIEQIVGPTIATVPLRVRIdPEQSVEDFLQTVQKDLLDM 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 338 LAHEQAPLALAQQCSQVPPPLPLFSTLFN--YRHSQKDASSQFWEGMRQLSGRER-TNYPITLSVDDLGDGFNLTA---K 411
Cdd:cd19545 290 IPFEHTGLQNIRRLGPDARAACNFQTLLVvqPALPSSTSESLELGIEEESEDLEDfSSYGLTLECQLSGSGLRVRArydS 369
|
410 420
....*....|....*....|....*
gi 641744967 412 TVMGVDP-ERIVHYMLTAIENLVTS 435
Cdd:cd19545 370 SVISEEQvERLLDQFEHVLQQLASA 394
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
499-967 |
8.84e-37 |
|
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: 146.49 E-value: 8.84e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDA-APVALLTQ 577
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSeAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 578 SAqvaqLNSTLPtvllDTPAaaacpdtnpvvqglhaahlaYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALdHPSR 657
Cdd:cd05969 81 EL----YERTDP----EDPT--------------------LLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDL-HPDD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 658 I---ALNASIVFDASVKNWIQLLSGHTLVLVPDalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQ- 733
Cdd:cd05969 132 IywcTADPGWVTGTVYGIWAPWLNGVTNVVYEG--RFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDELARKYDLSSl 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 734 --VLIGGEAISPAV--WSrlQSLSDTRFINVYGPTECTVDATA-CVVDRTQPlPTIGKPLANTRLYILDAQDQPVPIGVT 808
Cdd:cd05969 210 rfIHSVGEPLNPEAirWG--MEVFGVPIHDTWWQTETGSIMIAnYPCMPIKP-GSMGKPLPGVKAAVVDENGNELPPGTK 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 809 GELHI--GGAGVARGYLHRPDLTAERFIPDpfsadpaarIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESR 886
Cdd:cd05969 287 GILALkpGWPSMFRGIWNDEERYKNSFIDG---------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 887 LLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAA-------LRQQLAASLAdymiPSAFVTLDALPLTPNGKLD 959
Cdd:cd05969 358 LMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFEPSDELkeeiinfVRQKLGAHVA----PREIEFVDNLPKTRSGKIM 433
|
....*...
gi 641744967 960 RKALPAPD 967
Cdd:cd05969 434 RRVLKAKE 441
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2633-3097 |
1.12e-36 |
|
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: 146.04 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2633 SYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISqsa 2712
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2713 hlgimngslpvillddgetrpfdNEPDTPldarkqgltprhlAYVIYTSGSTGKPKG------VMVEHANMVNFLCSMRK 2786
Cdd:cd05971 85 -----------------------DGSDDP-------------ALIIYTSGTTGPPKGalhahrVLLGHLPGVQFPFNLFP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2787 EPGiaqeDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVELRDFALP 2866
Cdd:cd05971 129 RDG----DLYWTPADWAWIGGLLDVLLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2867 PGFKAL---CGGEALPEN-LATALLQKVTTLWNLYGPTETT-IWSTLNGLTTPTP-YIGHPIANTQIYILDAQGRVVPLG 2940
Cdd:cd05971 205 AQVKLRaiaTGGESLGEElLGWAREQFGVEVNEFYGQTECNlVIGNCSALFPIKPgSMGKPIPGHRVAIVDDNGTPLPPG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2941 VAGEIHIAGAGVVR--GYLGRPDLTAERFITDPFsgapearmyKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIE 3018
Cdd:cd05971 285 EVGEIAVELPDPVAflGYWNNPSATEKKMAGDWL---------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3019 TRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPA---DLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRK 3095
Cdd:cd05971 356 ECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVLNPGETPSDAlarEIQELVKTRLAAHEYPREIEFVNELPRTATGKIRRR 435
|
..
gi 641744967 3096 AL 3097
Cdd:cd05971 436 EL 437
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
2632-3097 |
1.42e-36 |
|
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: 145.56 E-value: 1.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQS 2711
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2712 ahlgimngslpvillDDgetrpfdnepdtpldarkqgltprhLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIA 2791
Cdd:cd05972 81 ---------------ED-------------------------PALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLR 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2792 QEDVLLGVTSLSFDISIL-EIFLPLLNGARLILATQAQAADAQQLAmLIERHAVSFMQATPSTWRMLVELrdfaLPPGFK 2870
Cdd:cd05972 121 PDDIHWNIADPGWAKGAWsSFFGPWLLGATVFVYEGPRFDAERILE-LLERYGVTSFCGPPTAYRMLIKQ----DLSSYK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2871 ------ALCGGEAL-PENLATALLQKVTTLWNLYGPTETTIW-STLNGLTTPTPYIGHPIANTQIYILDAQGRVVPLGVA 2942
Cdd:cd05972 196 fshlrlVVSAGEPLnPEVIEWWRAATGLPIRDGYGQTETGLTvGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2943 GEI--HIAGAGVVRGYLGRPDLTAERFITDpfsgapearMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETR 3020
Cdd:cd05972 276 GDIaiKLPPPGLFLGYVGDPEKTEASIRGD---------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3021 LARCHGVHDAVVIAredSPGDKR---------LVAYLLAQPDTVLEPADL-RQRLSEGVAEYMIpsAFVtlDAFPLTPNG 3090
Cdd:cd05972 347 LLEHPAVAEAAVVG---SPDPVRgevvkafvvLTSGYEPSEELAEELQGHvKKVLAPYKYPREI--EFV--EELPKTISG 419
|
....*..
gi 641744967 3091 KLDRKAL 3097
Cdd:cd05972 420 KIRRVEL 426
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
489-958 |
1.71e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 146.97 E-value: 1.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 489 AIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDD 568
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 569 AAPVALLTQ---SAQVAQLNSTLP---TVLLDTP-----------AAAACPDTNPVVQGLhAAHLAyviYTSGSTGRPKG 631
Cdd:PRK08276 82 SGAKVLIVSaalADTAAELAAELPagvPLLLVVAgpvpgfrsyeeALAAQPDTPIADETA-GADML---YSSGTTGRPKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 632 VMVA--HRNVINLATGLHTLLALDH---PSRIALNASIVFDASVKNWIQ--LLSGHTLVLVPdalRADAHQLWRYFARHA 704
Cdd:PRK08276 158 IKRPlpGLDPDEAPGMMLALLGFGMyggPDSVYLSPAPLYHTAPLRFGMsaLALGGTVVVME---KFDAEEALALIERYR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 705 VDLFDCTPVQLQWLLdaglgsdpayqpaqvliggeAISPAVWSRLqSLSDTRF----------------INVYGPT---- 764
Cdd:PRK08276 235 VTHSQLVPTMFVRML--------------------KLPEEVRARY-DVSSLRVaihaaapcpvevkramIDWWGPIihey 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 765 -ECTVDATACVVDRTQPL--P-TIGKPLAnTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSA 840
Cdd:PRK08276 294 yASSEGGGVTVITSEDWLahPgSVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGWVT 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 841 dpaariykTGDLArWLPDGNIDYL-GRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPD 919
Cdd:PRK08276 373 --------VGDVG-YLDEDGYLYLtDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPADG 443
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 641744967 920 AELHPA---ALRQQLAASLADYMIPSAFVTLDALPLTPNGKL 958
Cdd:PRK08276 444 ADAGDAlaaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
2603-3087 |
2.68e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 147.20 E-value: 2.68e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2603 PRHALIHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGA 2682
Cdd:PRK06164 7 PRADTLASLLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGAT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2683 YVPLDPTYPVERLRYMLDDAKPVALISQSAHLGI-----MNGSLP--------VILLDDGETR-----PFD--NEPDTPL 2742
Cdd:PRK06164 87 VIAVNTRYRSHEVAHILGRGRARWLVVWPGFKGIdfaaiLAAVPPdalpplraIAVVDDAADAtpapaPGArvQLFALPD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2743 DARKQGLTPRH-----LAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLS--FDISILEIFLPl 2815
Cdd:PRK06164 167 PAPPAAAGERAadpdaGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCgvFGFSTLLGALA- 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2816 lNGARLILATQAQAADAQQlamLIERHAVSFMQATPSTWRMLVEL----RDFALPP--GFKALCGGEAlpeNLATALLQK 2889
Cdd:PRK06164 246 -GGAPLVCEPVFDAARTAR---ALRRHRVTHTFGNDEMLRRILDTagerADFPSARlfGFASFAPALG---ELAALARAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2890 VTTLWNLYGPTETTIWSTLNGLTTPTPYI----GHPI-ANTQIYILDAQ-GRVVPLGVAGEIHIAGAGVVRGYLGRPDLT 2963
Cdd:PRK06164 319 GVPLTGLYGSSEVQALVALQPATDPVSVRieggGRPAsPEARVRARDPQdGALLPDGESGEIEIRAPSLMRGYLDNPDAT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2964 AERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREdSPGDKR 3043
Cdd:PRK06164 399 ARALTDDGY--------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGAT-RDGKTV 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 641744967 3044 LVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLT 3087
Cdd:PRK06164 470 PVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVT 513
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
2613-3097 |
3.71e-36 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 145.77 E-value: 3.71e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2613 EAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLI-SFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYP 2691
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIyELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2692 VERLRYMLDDAKPVALISQ------SAHLGIMNGSLPVILLDDgetrpfdnePDTPLDARKQGLTPRH--LAYVI-YTSG 2762
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEktfqnmALSMQKVSYVQRVISITS---------LKEIEDRKIDNFVEKNesASFIIcYTSG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2763 STGKPKGVMVEHANMvnFLCSMRKEPGI--AQEDVLLGVTSLsFDISILEIF-LP-LLNGARLILATQAQAADAQQlamL 2838
Cdd:PRK06839 160 TTGKPKGAVLTQENM--FWNALNNTFAIdlTMHDRSIVLLPL-FHIGGIGLFaFPtLFAGGVIIVPRKFEPTKALS---M 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2839 IERHAVSFMQATPSTWRMLVELRDFAlPPGFKAL----CGGEALPENLATALLQKVTTLWNLYGPTET--TIWSTLNGLT 2912
Cdd:PRK06839 234 IEKHKVTVVMGVPTIHQALINCSKFE-TTNLQSVrwfyNGGAPCPEELMREFIDRGFLFGQGFGMTETspTVFMLSEEDA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2913 TPTP-YIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERfITDPFsgapearmYKTGDLGRWLP 2991
Cdd:PRK06839 313 RRKVgSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW--------LCTGDLARVDE 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2992 DGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAE 3071
Cdd:PRK06839 384 DGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEKDVIEHCRLFLAK 463
|
490 500
....*....|....*....|....*.
gi 641744967 3072 YMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK06839 464 YKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1671-2021 |
3.73e-36 |
|
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: 141.31 E-value: 3.73e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1671 LAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPfSFDVSVWEFFWP-LLYGARLVMARPDghkda 1749
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLP-LYHVGGLAILVRsLLAGAELVLLERN----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1750 AYLAQLIERTGITTLHFVPSMLQQFVQWADADCACDSLRRVICSGEALPAELQQRFFARfNAQLHNLYGPTEAAIDVTFW 1829
Cdd:cd17630 76 QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLERAADR-GIPLYTTYGMTETASQVATK 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1830 ACQPDDHRSfvpIGRPIANTQLYILDTlgqpvplgvaGELHIGGVGVARGYLNRPdltaerfIPDPFINQPgarLYKTGD 1909
Cdd:cd17630 155 RPDGFGRGG---VGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ-------LVPEFNEDG---WFTTKD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1910 LARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGvtPDPADLRQQL 1989
Cdd:cd17630 212 LGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGRGP--ADPAELRAWL 289
|
330 340 350
....*....|....*....|....*....|..
gi 641744967 1990 GQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd17630 290 KDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1667-2021 |
4.76e-36 |
|
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: 145.55 E-value: 4.76e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1667 DAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTP----FSFDVSVWeffWPLLYGARLVMAr 1742
Cdd:cd05909 145 QPDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPffhsFGLTGCLW---LPLLSGIKVVFH- 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1743 PDGhKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADCAcDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEA 1822
Cdd:cd05909 221 PNP-LDYKKIPELIYDKKATILLGTPTFLRGYARAAHPEDF-SSLRLVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTEC 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1823 AIDVTFWACQPDDHRSFVpiGRPIANTQLYILDTLG-QPVPLGVAGELHIGGVGVARGYLNRPDLTAERFipdpfinqpG 1901
Cdd:cd05909 299 SPVISVNTPQSPNKEGTV--GRPLPGMEVKIVSVEThEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF---------G 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1902 ARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQ-CPGVQEAVVVARED-SPGDtRLVAYLCPQpgvT 1979
Cdd:cd05909 368 DGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEiLPEDNEVAVVSVPDgRKGE-KIVLLTTTT---D 443
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 641744967 1980 PDPADLRQQLGQH-LAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05909 444 TDPSSLNDILKNAgISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1537-2021 |
7.14e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 144.95 E-value: 7.14e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1537 QAARTPDTTAV--LFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPA 1614
Cdd:PRK09088 4 HARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1615 ERLAYMLDDASPVALLTQANQRALLTgdvprILLDTADF--SHLSEDNPHVPGLDAHHLAYVIYTSGSTGKPKGVMNSHR 1692
Cdd:PRK09088 84 SELDALLQDAEPRLLLGDDAVAAGRT-----DVEDLAAFiaSADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1693 ALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLY--GARLVmarPDGHKDAAYLAQLIERT-GITTLHFVPS 1769
Cdd:PRK09088 159 NLQQTAHNFGVLGRVDAHSSFLCDAPMFHIIGLITSVRPVLAvgGSILV---SNGFEPKRTLGRLGDPAlGITHYFCVPQ 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1770 MLQQFVQWADADCAcdSLRRV--ICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIdVTFWACQPDDHRSFV-PIGRPI 1846
Cdd:PRK09088 236 MAQAFRAQPGFDAA--ALRHLtaLFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAGT-VFGMSVDCDVIRAKAgAAGIPT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1847 ANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSLEYLGRND 1926
Cdd:PRK09088 313 PTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW--------FRTGDIARRDADGFFWVVDRKK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1927 FQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLD 2006
Cdd:PRK09088 385 DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVD 464
|
490
....*....|....*
gi 641744967 2007 AFPLTPNGKLDRKAL 2021
Cdd:PRK09088 465 ALPRTASGKLQKARL 479
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
496-963 |
7.29e-36 |
|
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: 143.77 E-value: 7.29e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 496 DQHLTYRELNRRANQLAHHLI-ALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAapval 574
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 575 ltqsaqvaqlnstlptvlldTPAAAACPDtnpvvQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHT-LLALD 653
Cdd:cd05958 83 --------------------RITVALCAH-----ALTASDDICILAFTSGTTGAPKATMHFHRDPLASADRYAVnVLRLR 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 654 HPSRI----------ALNASIVFDASVknwiqllsGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQwlldAGL 723
Cdd:cd05958 138 EDDRFvgspplaftfGLGGVLLFPFGV--------GASGVLLE---EATPDLLLSAIARYKPTVLFTAPTAYR----AML 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 724 GSDPAYQP-----AQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPlPTIGKPLANTRLYILDA 798
Cdd:cd05958 203 AHPDAAGPdlsslRKCVSAGEALPAALHRAWKEATGIPIIDGIGSTEMFHIFISARPGDARP-GATGKPVPGYEAKVVDD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 799 QDQPVPIGVTGELHIGGAgvaRGYLHRPDLTAERFIPDPFSAdpaariykTGDLARWLPDGNIDYLGRNDFQIKVRGFRI 878
Cdd:cd05958 282 EGNPVPDGTIGRLAVRGP---TGCRYLADKRQRTYVQGGWNI--------TGDTYSRDPDGYFRHQGRSDDMIVSGGYNI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 879 EAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPA---ALRQQLAASLADYMIPSAFVTLDALPLTPN 955
Cdd:cd05958 351 APPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAKAHIAPYKYPRAIEFVTELPRTAT 430
|
....*...
gi 641744967 956 GKLDRKAL 963
Cdd:cd05958 431 GKLQRFAL 438
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
479-961 |
7.63e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 146.30 E-value: 7.63e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 479 FEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYP 558
Cdd:PRK05605 38 YDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVEHNPLYT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 559 AERLAYILDD-AAPVA--------LLTQSAQVAQLN--------STLPTVL-----LDTPAA--------AACPDTNP-- 606
Cdd:PRK05605 118 AHELEHPFEDhGARVAivwdkvapTVERLRRTTPLEtivsvnmiAAMPLLQrlalrLPIPALrkaraaltGPAPGTVPwe 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 607 -------VVQGLHAAH-------LAYVIYTSGSTGRPKGVMVAHRNVI-NLATGLHTLLAL-DHPSRIaLNASIVFDA-- 668
Cdd:PRK05605 198 tlvdaaiGGDGSDVSHprptpddVALILYTSGTTGKPKGAQLTHRNLFaNAAQGKAWVPGLgDGPERV-LAALPMFHAyg 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 669 -SVKNWIQLLSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLI-GGEAISPAVW 746
Cdd:PRK05605 277 lTLCLTLAVSIGGELVLLP---APDIDLILDAMKKHPPTWLPGVPPLYEKIAEAAEERGVDLSGVRNAFsGAMALPVSTV 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 747 SRLQSLSDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQD--QPVPIGVTGELHIGGAGVARGYLH 824
Cdd:PRK05605 354 ELWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPEDpdETMPDGEEGELLVRGPQVFKGYWN 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 825 RPDLTAERFIPDpfsadpaarIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDS 904
Cdd:PRK05605 434 RPEETAKSFLDG---------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPRE 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 905 PGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRK 961
Cdd:PRK05605 505 DGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1530-2021 |
3.18e-35 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 143.87 E-value: 3.18e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFEDQH--LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVP 1607
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1608 LDPGYPAERLAYMLDDASPVALLTQAN---QRALLTGDVPRILLDTADFSHLSEDNPHVPgLDA---------------H 1669
Cdd:PRK05852 98 LDPALPIAEQRVRSQAAGARVVLIDADgphDRAEPTTRWWPLTVNVGGDSGPSGGTLSVH-LDAateptpatstpeglrP 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1670 HLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDA 1749
Cdd:PRK05852 177 DDAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1750 AYLAQLIERTGITTLHFVPSMLQQFVQWADADCACD---SLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDV 1826
Cdd:PRK05852 257 HTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpaALRFIRSCSAPLTAETAQALQTEFAAPVVCAFGMTEATHQV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1827 T----FWACQPDDHRSFV-PIGRPIAnTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpg 1901
Cdd:PRK05852 337 TttqiEGIGQTENPVVSTgLVGRSTG-AQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL----- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1902 arlyKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPD 1981
Cdd:PRK05852 411 ----RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPT 486
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 641744967 1982 PADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK05852 487 AEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
449-958 |
4.19e-35 |
|
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: 144.26 E-value: 4.19e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 449 ILPKSERQQVLVDFNATDADFPREMLIQQRFEA---QAEQTPEAIAVLFED------QHLTYRELNRRANQLAHHLIALG 519
Cdd:cd17634 26 ITPYQKVKNTSFAPGAPSIKWFEDATLNLAANAldrHLRENGDRTAIIYEGddtsqsRTISYRELHREVCRFAGTLLDLG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 520 VQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQS---------------AQVAQL 584
Cdd:cd17634 106 VKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADggvragrsvplkknvDDALNP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 585 NSTLP-TVLL------------------DTPAAAACPDTNPVvqGLHAAHLAYVIYTSGSTGRPKGVMVAHRN-VINLAT 644
Cdd:cd17634 186 NVTSVeHVIVlkrtgsdidwqegrdlwwRDLIAKASPEHQPE--AMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAAT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 645 GLHTLLALdHPSRIALNASIVFDASVKNWI---QLLSGHTLVL---VPDALRADAhqLWRYFARHAVDLFDCTPVQLQWL 718
Cdd:cd17634 264 TMKYVFDY-GPGDIYWCTADVGWVTGHSYLlygPLACGATTLLyegVPNWPTPAR--MWQVVDKHGVNILYTAPTAIRAL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 719 LDAGLGSDPAYQPA--QVLIG-GEAISPAVWS---RLQSLSDTRFINVYGPTECtvdATACVVDRTQPLPTIG----KPL 788
Cdd:cd17634 341 MAAGDDAIEGTDRSslRILGSvGEPINPEAYEwywKKIGKEKCPVVDTWWQTET---GGFMITPLPGAIELKAgsatRPV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 789 ANTRLYILDAQDQPVPIGVTGELHIGGA--GVARGYLHRPDltaeRFIPDPFSAdpAARIYKTGDLARWLPDGNIDYLGR 866
Cdd:cd17634 418 FGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFEQTYFST--FKGMYFSGDGARRDEDGYYWITGR 491
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 867 NDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHP---AALRQQLAASLADYMIPSA 943
Cdd:cd17634 492 SDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVLNHGVEPSPelyAELRNWVRKEIGPLATPDV 571
|
570
....*....|....*
gi 641744967 944 FVTLDALPLTPNGKL 958
Cdd:cd17634 572 VHWVDSLPKTRSGKI 586
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
2608-3097 |
4.30e-35 |
|
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: 142.65 E-value: 4.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2608 IHELFEAQVACTPDAIAVVFGEAS--LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVP 2685
Cdd:cd05923 3 VFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2686 LDPTYPVERLRYMLDDAKPVALISQSAHL---GIMNGSLPVILLDDgETRPFDNEPDTPLDARKQGlTPRHLAYVIYTSG 2762
Cdd:cd05923 83 INPRLKAAELAELIERGEMTAAVIAVDAQvmdAIFQSGVRVLALSD-LVGLGEPESAGPLIEDPPR-EPEQPAFVFYTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2763 STGKPKGVMVEHANMVNFLCSMRKEPGI--AQEDVLLGVTSLSFDISILEIFL-PLLNGARLILATQAQAADAQQlamLI 2839
Cdd:cd05923 161 TTGLPKGAVIPQRAAESRVLFMSTQAGLrhGRHNVVLGLMPLYHVIGFFAVLVaALALDGTYVVVEEFDPADALK---LI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2840 ERHAVSFMQATPSTWRMLVELRDFAlPPGFKAL----CGGEALPENLATALLQKVTTLW-NLYGPTEttiwsTLNGLTTP 2914
Cdd:cd05923 238 EQERVTSLFATPTHLDALAAAAEFA-GLKLSSLrhvtFAGATMPDAVLERVNQHLPGEKvNIYGTTE-----AMNSLYMR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2915 TPYIG---HPIANTQIYILDAQGRVV---PLGVAGEIHIAGAG--VVRGYLGRPDLTAERfITDpfsgapeaRMYKTGDL 2986
Cdd:cd05923 312 DARTGtemRPGFFSEVRIVRIGGSPDealANGEEGELIVAAAAdaAFTGYLNQPEATAKK-LQD--------GWYRTGDV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2987 GRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLS 3066
Cdd:cd05923 383 GYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQFCRA 462
|
490 500 510
....*....|....*....|....*....|.
gi 641744967 3067 EGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05923 463 SELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1536-2021 |
7.38e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 141.84 E-value: 7.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1536 DQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDdRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAE 1615
Cdd:PRK07638 9 KHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNK-TIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1616 RLAYMLDDASPVALLTQANQRALLTG-DVPRILLDTADFSHLSEDNPHVPGLDAHHLA-YVIYTSGSTGKPKGVMNSHRA 1693
Cdd:PRK07638 88 ELKERLAISNADMIVTERYKLNDLPDeEGRVIEIDEWKRMIEKYLPTYAPIENVQNAPfYMGFTSGSTGKPKAFLRAQQS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1694 lcnrlvWMQN------TYRLTPDDRVLqkTPFSFDVSVWEF--FWPLLYGARLVMAR---PDGHKDAaylaqlIERTGIT 1762
Cdd:PRK07638 168 ------WLHSfdcnvhDFHMKREDSVL--IAGTLVHSLFLYgaISTLYVGQTVHLMRkfiPNQVLDK------LETENIS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1763 TLHFVPSMLQQFVQwadADCACDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIdVTFWACQpDDHRSFVP 1841
Cdd:PRK07638 234 VMYTVPTMLESLYK---ENRVIENKMKIISSGAKWEAEAKEKIKNIFpYAKLYEFYGASELSF-VTALVDE-ESERRPNS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1842 IGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNrpdltaerfipdpfinqpGARLYKTGDLARWLP------ 1915
Cdd:PRK07638 309 VGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYII------------------GGVLARELNADGWMTvrdvgy 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1916 ---DGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPgvtpDPADLRQQLGQH 1992
Cdd:PRK07638 371 edeEGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSA----TKQQLKSFCLQR 446
|
490 500
....*....|....*....|....*....
gi 641744967 1993 LAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK07638 447 LSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1536-2021 |
9.02e-35 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 142.73 E-value: 9.02e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1536 DQAARTPDTTAVLFED----------QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAY 1605
Cdd:PRK09274 14 RAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1606 VPLDPGYPAERLAYMLDDASPVALLTQ--------------ANQRALLTGDvPRILLDTADFSHLSEDNPHVPG----LD 1667
Cdd:PRK09274 94 VLVDPGMGIKNLKQCLAEAQPDAFIGIpkahlarrlfgwgkPSVRRLVTVG-GRLLWGGTTLATLLRDGAAAPFpmadLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1668 AHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTP-FSfdvsvweFFWPLLyGARLVM-----A 1741
Cdd:PRK09274 173 PDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPTFPlFA-------LFGPAL-GMTSVIpdmdpT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1742 RPdGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADA-DCACDSLRRVICSGEALPAELQQRFFARFN--AQLHNLYG 1818
Cdd:PRK09274 245 RP-ATVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEAnGIKLPSLRRVISAGAPVPIAVIERFRAMLPpdAEILTPYG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1819 PTEA---------AIDVTFWAcQPDDHRSfVPIGRPIANTQLYIL-----------DTLgqPVPLGVAGELHIGGVGVAR 1878
Cdd:PRK09274 324 ATEAlpissiesrEILFATRA-ATDNGAG-ICVGRPVDGVEVRIIaisdapipewdDAL--RLATGEIGEIVVAGPMVTR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1879 GYLNRPDLTAERFIPDPfinQPGARlYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVA 1958
Cdd:PRK09274 400 SYYNRPEATRLAKIPDG---QGDVW-HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSALVG 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1959 REdSPGDTRLVayLC--PQPGVTPDPADLRQQLGQHLAEY-MVPG--AFVTLDAFPLTP--NGKLDRKAL 2021
Cdd:PRK09274 476 VG-VPGAQRPV--LCveLEPGVACSKSALYQELRALAAAHpHTAGieRFLIHPSFPVDIrhNAKIFREKL 542
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2597-3053 |
9.26e-35 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 143.70 E-value: 9.26e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2597 ATDADIPRHALIHELFEAQVACTPDAIAVVF----GEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVG 2672
Cdd:COG1022 2 SEFSDVPPADTLPDLLRRRAARFPDRVALREkedgIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2673 LLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALI-SQSAHLGIMN---GSLP----VILLDDGETRPFDN-------- 2736
Cdd:COG1022 82 DLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFvEDQEQLDKLLevrDELPslrhIVVLDPRGLRDDPRllsldell 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2737 ------EPDTPLDARKQGLTPRHLAYVIYTSGSTGKPKGVMVEHANMV-NFLCSMRKEPGIAQEDVLLgvtslsfdisil 2809
Cdd:COG1022 162 algrevADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLsNARALLERLPLGPGDRTLS------------ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2810 eiFLPLLN-GARLIlatqaqaadaqQLAMLIERHAVSF-------------------------------------MQATP 2851
Cdd:COG1022 230 --FLPLAHvFERTV-----------SYYALAAGATVAFaespdtlaedlrevkptfmlavprvwekvyagiqakaEEAGG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2852 STWRML----------VELRDFALPPGFK--------------------------ALCGGEALPENLAT-------ALLQ 2888
Cdd:COG1022 297 LKRKLFrwalavgrryARARLAGKSPSLLlrlkhaladklvfsklrealggrlrfAVSGGAALGPELARffralgiPVLE 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2889 kvttlwnLYGPTETTIWSTLNGLTTPTP-YIGHPIANTQIYIldaqgrvvplGVAGEIHIAGAGVVRGYLGRPDLTAERF 2967
Cdd:COG1022 377 -------GYGLTETSPVITVNRPGDNRIgTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAF 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2968 ITDPFsgapearmYKTGDLGRWLPDGTLEYLGR--------NdfqvkvrGFRIELGEIETRLARCHGVHDAVVIaredsp 3039
Cdd:COG1022 440 DADGW--------LHTGDIGELDEDGFLRITGRkkdlivtsG-------GKNVAPQPIENALKASPLIEQAVVV------ 498
|
570
....*....|....*.
gi 641744967 3040 GDKR--LVAylLAQPD 3053
Cdd:COG1022 499 GDGRpfLAA--LIVPD 512
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1676-2018 |
1.00e-34 |
|
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: 138.18 E-value: 1.00e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1676 YTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPF--SFDvSVWEFFWPLLYGARLVMARPDGHKDAAYLA 1753
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLfhCFG-SVLGVLACLTHGATMVFPSPSFDPLAVLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1754 qlIERTGITTLHFVPSMlqqFV----QWADADCACDSLRRVICSGEALPAELQQRFFARFN-AQLHNLYGPTEAAiDVTF 1828
Cdd:cd05917 88 --IEKEKCTALHGVPTM---FIaeleHPDFDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNmKDVTIAYGMTETS-PVST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1829 wACQPDD--HRSFVPIGRPIANTQLYILDTLGQPVP-LGVAGELHIGGVGVARGYLNRPDLTAERFIPDpfinqpgaRLY 1905
Cdd:cd05917 162 -QTRTDDsiEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD--------GWL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1906 KTGDLARWLPDGSLEYLGR-NDFQVKlRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPAD 1984
Cdd:cd05917 233 HTGDLAVMDEDGYCRIVGRiKDMIIR-GGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEED 311
|
330 340 350
....*....|....*....|....*....|....
gi 641744967 1985 LRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDR 2018
Cdd:cd05917 312 IKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
475-963 |
1.06e-34 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 142.13 E-value: 1.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 475 IQQRFEAQAEQTPEAIAVLFED-----QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAA 549
Cdd:PRK08008 9 LRQMWDDLADVYGHKTALIFESsggvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 550 YVPMDPAYPAERLAYILDDAAPVALLTQSA------QVAQLNSTLPTVLLDTPAAAacPDTNPVV-----QGLHAAHLAY 618
Cdd:PRK08008 89 MVPINARLLREESAWILQNSQASLLVTSAQfypmyrQIQQEDATPLRHICLTRVAL--PADDGVSsftqlKAQQPATLCY 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 619 -----------VIYTSGSTGRPKGVMVAHRNVinLATGLHTLLaldhpsRIALNASIVF---------DASVKNWIQLLS 678
Cdd:PRK08008 167 applstddtaeILFTSGTTSRPKGVVITHYNL--RFAGYYSAW------QCALRDDDVYltvmpafhiDCQCTAAMAAFS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 679 -GHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLdaglgsdpaYQPaqvliggeaisPAVWSRLQSLSD--- 754
Cdd:PRK08008 239 aGATFVLLE---KYSARAFWGQVCKYRATITECIPMMIRTLM---------VQP-----------PSANDRQHCLREvmf 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 755 -------------TRF----INVYGPTECTVDAtacVVDR---TQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIG 814
Cdd:PRK08008 296 ylnlsdqekdafeERFgvrlLTSYGMTETIVGI---IGDRpgdKRRWPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIK 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 815 G-AG--VARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCP 891
Cdd:PRK08008 373 GvPGktIFKEYYLDPKATAKVLEADGW--------LHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHP 444
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641744967 892 GVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK08008 445 KIQDIVVVGIKDSIRDEAIKAFVVLNEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1530-2015 |
1.14e-34 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 142.64 E-value: 1.14e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFEDQHL--TYDALNRRANQLAHHLIDLGVKPDDRIAI----CVErsldMVIGLLAILKAGA 1603
Cdd:PRK08315 18 IGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIwapnVPE----WVLTQFATAKIGA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1604 AYVPLDPGYPAERLAYMLDDASPVALLT-----QANQRALLTGDVPRI------LLDTADFSHLSE----DNPHVPGL-- 1666
Cdd:PRK08315 94 ILVTINPAYRLSELEYALNQSGCKALIAadgfkDSDYVAMLYELAPELatcepgQLQSARLPELRRviflGDEKHPGMln 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1667 ---------DAHHLAY-----------VI---YTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPF---- 1719
Cdd:PRK08315 174 fdellalgrAVDDAELaarqatldpddPIniqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIPVPLyhcf 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1720 -------------SFDVSVWEFFWPLLygarlVMarpdghkdaaylaQLIERTGITTLHFVPSMlqqFV------QWADA 1780
Cdd:PRK08315 254 gmvlgnlacvthgATMVYPGEGFDPLA-----TL-------------AAVEEERCTALYGVPTM---FIaeldhpDFARF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1781 DCAcdSLRRVICSGEALPAELQQRFFARFN-AQLHNLYGPTEA-------AIDvtfwacQPDDHR-SFVpiGRPIANTQL 1851
Cdd:PRK08315 313 DLS--SLRTGIMAGSPCPIEVMKRVIDKMHmSEVTIAYGMTETspvstqtRTD------DPLEKRvTTV--GRALPHLEV 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1852 YILD-TLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFINqpgarlykTGDLARWLPDGSLEYLGRndfqVK 1930
Cdd:PRK08315 383 KIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGWMH--------TGDLAVMDEEGYVNIVGR----IK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1931 ---LRGfrielGE------IEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGA 2001
Cdd:PRK08315 451 dmiIRG-----GEniypreIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRY 525
|
570
....*....|....
gi 641744967 2002 FVTLDAFPLTPNGK 2015
Cdd:PRK08315 526 IRFVDEFPMTVTGK 539
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
2631-3097 |
1.19e-34 |
|
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: 139.40 E-value: 1.19e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2631 SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPValisq 2710
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVK----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2711 sahlgimngslpvilLDDgetrpfdnepdtpldarkqgltprhLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGI 2790
Cdd:cd05912 76 ---------------LDD-------------------------IATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGL 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2791 AQEDVLLGVTSLsFDISILEIFL-PLLNGARLILATQAQAADAQQlamLIERHAVSFMQATPSTWRMLVELRDFALPPGF 2869
Cdd:cd05912 116 TEDDNWLCALPL-FHISGLSILMrSVIYGMTVYLVDKFDAEQVLH---LINSGKVTIISVVPTMLQRLLEILGEGYPNNL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2870 KA-LCGGEALPENLATALLQKVTTLWNLYGPTETTIWS-TLNGLTTPTPY--IGHPIANTQIYILDAQGrvvPLGVAGEI 2945
Cdd:cd05912 192 RCiLLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCSQIvTLSPEDALNKIgsAGKPLFPVELKIEDDGQ---PPYEVGEI 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2946 HIAGAGVVRGYLGRPDLTAERFITDPFsgapearmyKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCH 3025
Cdd:cd05912 269 LLKGPNVTKGYLNRPDATEESFENGWF---------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHP 339
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641744967 3026 GVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEpaDLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05912 340 AIKEAGVVGIPDDKWGQVPVAFVVSERPISEE--ELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
2162-2566 |
2.05e-34 |
|
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: 139.08 E-value: 2.05e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2162 YPLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCwQDLSQPVQVVwrqailpinh 2241
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFC-EEAGRYEQVV---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2242 FEPTSPEDV-LAQLQAHTEPRTRRIDLSQAPLFRA-DIAHDPL---------QNEWLLALSFHHLISDHMTLALIVGEIR 2310
Cdd:cd19066 71 LDKTVRFRIeIIDLRNLADPEARLLELIDQIQQTIyDLERGPLvrvalfrlaDERDVLVVAIHHIIVDGGSFQILFEDIS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2311 LL---LQHQADALPTPL-PYRNFIA----QTLSVPNSAHEAYFRDKLADVDEPtAPFGLLNVQG--SGGDIHEARLVLDA 2380
Cdd:cd19066 151 SVydaAERQKPTLPPPVgSYADYAAwlekQLESEAAQADLAYWTSYLHGLPPP-LPLPKAKRPSqvASYEVLTLEFFLRS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2381 TLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRLagAEGADRIMGMFINTLPLRISLA-DRGAAEV 2459
Cdd:cd19066 230 EETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRP--DEAVEDTIGLFLNLLPLRIDTSpDATFPEL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2460 VERTSHDLMTLLEHEQAPLALAQRCSGVAPPM---PLFSTLLNYRHTQA--SSTDNTLSDIRVLTSEERTNYPLTLAVDD 2534
Cdd:cd19066 308 LKRTKEQSREAIEHQRVPFIELVRHLGVVPEApkhPLFEPVFTFKNNQQqlGKTGGFIFTTPVYTSSEGTVFDLDLEASE 387
|
410 420 430
....*....|....*....|....*....|....*..
gi 641744967 2535 RGEG-----FSLVAQTLEDIDPHRLLNYLMTAISSLV 2566
Cdd:cd19066 388 DPDGdlllrLEYSRGVYDERTIDRFAERYMTALRQLI 424
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1540-2021 |
3.33e-34 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 140.90 E-value: 3.33e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1540 RTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAyvPLDPGYPAERL-- 1617
Cdd:PRK10946 35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSel 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1618 -AYMlDDASPvALLTQANQRALLTGDV-----------PRILL---DTADFS---HLSEDNPHVPGLD--AHHLAYVIYT 1677
Cdd:PRK10946 113 nAYA-SQIEP-ALLIADRQHALFSDDDflntlvaehssLRVVLllnDDGEHSlddAINHPAEDFTATPspADEVAFFQLS 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1678 SGSTGKPKGVMNSHralcnrlvwmqNTY-----------RLTPDDRVLQKTP--FSFDVSVWEFFWPLLYGARLVMArPD 1744
Cdd:PRK10946 191 GGSTGTPKLIPRTH-----------NDYyysvrrsveicGFTPQTRYLCALPaaHNYPMSSPGALGVFLAGGTVVLA-PD 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1745 ghKDAAYLAQLIERTGITTLHFVP---SMLQQFVQWADADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTE 1821
Cdd:PRK10946 259 --PSATLCFPLIEKHQVNVTALVPpavSLWLQAIAEGGSRAQLASLKLLQVGGARLSETLARRIPAELGCQLQQVFGMAE 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1822 AAIDVTfwACQPDDHRSFVPIGRPIA-NTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqp 1900
Cdd:PRK10946 337 GLVNYT--RLDDSDERIFTTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF---- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1901 garlYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLcpqpgVTP 1980
Cdd:PRK10946 411 ----YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFL-----VVK 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 641744967 1981 DP---ADLRQQL-GQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK10946 482 EPlkaVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1552-1957 |
3.43e-34 |
|
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: 139.42 E-value: 3.43e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1552 QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLT 1631
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1632 QAnqralltgdvprilldtadfshlSEDNphvpgldahhLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDD 1711
Cdd:cd17640 84 EN-----------------------DSDD----------LATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1712 RVLQKTP--FSFDVSVWEFFwpLLYGARLVMARPDGHKD--AAYLAQLIE---------RTGITTLHFVPSMLQQFVqwA 1778
Cdd:cd17640 131 RFLSILPiwHSYERSAEYFI--FACGCSQAYTSIRTLKDdlKRVKPHYIVsvprlweslYSGIQKQVSKSSPIKQFL--F 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1779 DADCACDSLRRVICSGEALPAELQqRFFARFNAQLHNLYGPTEAAIDVTfwaCQPDDHRSFVPIGRPIANTQLYILDTLG 1858
Cdd:cd17640 207 LFFLSGGIFKFGISGGGALPPHVD-TFFEAIGIEVLNGYGLTETSPVVS---ARRLKCNVRGSVGRPLPGTEIKIVDPEG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1859 Q-PVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFINqpgarlykTGDLARWLPDGSLEYLGR-NDFQVKLRGFRI 1936
Cdd:cd17640 283 NvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGWFN--------TGDLGWLTCGGELVLTGRaKDTIVLSNGENV 354
|
410 420
....*....|....*....|.
gi 641744967 1937 ELGEIEARLMQCPGVQEAVVV 1957
Cdd:cd17640 355 EPQPIEEALMRSPFIEQIMVV 375
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
480-963 |
3.63e-34 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 140.79 E-value: 3.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 480 EAQAEQTPEAIAVLFEDQH--LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAY 557
Cdd:PRK05852 23 EVAATRLPEAPALVVTADRiaISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 558 P-AERLAYILDDAAPVALLTQSAQVAQLNSTLP-----------------TVLLDTPAAAACPDTNPVVQGLHAAHlAYV 619
Cdd:PRK05852 103 PiAEQRVRSQAAGARVVLIDADGPHDRAEPTTRwwpltvnvggdsgpsggTLSVHLDAATEPTPATSTPEGLRPDD-AMI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 620 IYTSGSTGRPKGVMVAHRNVinlATGLHTLLAL----DHPSRIALNASIVFDASVKNWIQLLSGHTLVLVPDALRADAHQ 695
Cdd:PRK05852 182 MFTGGTTGLPKMVPWTHANI---ASSVRAIITGyrlsPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAHT 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 696 LWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAISPAVWSRLQSLSDT---RFINVYGPTECTVDATA 772
Cdd:PRK05852 259 FWDDIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALRFIRSCSAPLTAETAQALQTEfaaPVVCAFGMTEATHQVTT 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 773 CVVD---RTQ-PLPTIGKPLANT--RLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaari 846
Cdd:PRK05852 339 TQIEgigQTEnPVVSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL-------- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 847 yKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAA 926
Cdd:PRK05852 411 -RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPTAEE 489
|
490 500 510
....*....|....*....|....*....|....*..
gi 641744967 927 LRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK05852 490 LVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
472-941 |
3.83e-34 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 141.55 E-value: 3.83e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 472 EMLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYV 551
Cdd:PRK08279 36 KRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 552 PMDPAYPAERLAYILDDAAPVALLTQSAQVAQLNSTLPTVLLDTP--------------------AAAACPDTNPVV-QG 610
Cdd:PRK08279 116 LLNTQQRGAVLAHSLNLVDAKHLIVGEELVEAFEEARADLARPPRlwvaggdtlddpegyedlaaAAAGAPTTNPASrSG 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 611 LHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIAL-------NASIVFDASVknwiqLLSGHTLV 683
Cdd:PRK08279 196 VTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVLYCclplyhnTGGTVAWSSV-----LAAGATLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 684 LVPdalRADAHQLWRYFARHavdlfDCTPVQ-----LQWLLDaglgsdpayQPAQ--------VLIGGEAISPAVWSRLQ 750
Cdd:PRK08279 271 LRR---KFSASRFWDDVRRY-----RATAFQyigelCRYLLN---------QPPKptdrdhrlRLMIGNGLRPDIWDEFQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 751 slsdTRF-----INVYGPTECTV--------DATACVVdrtqplPTIGK-PLA------NTRLYILDAQD--QPVPIGVT 808
Cdd:PRK08279 334 ----QRFgipriLEFYAASEGNVgfinvfnfDGTVGRV------PLWLAhPYAivkydvDTGEPVRDADGrcIKVKPGEV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 809 GEL--HIGGAGVARGYLhRPDLTAERFIPDPFSadPAARIYKTGDLARwlPDGN-----IDYLGrnD-FQIKvrGFRIEA 880
Cdd:PRK08279 404 GLLigRITDRGPFDGYT-DPEASEKKILRDVFK--KGDAWFNTGDLMR--DDGFghaqfVDRLG--DtFRWK--GENVAT 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 881 GEIESRLLRCPGVQDAVVIAREdSPG-DTRL-VAYLCARPDAELHPAALRQQLAASLADYMIP 941
Cdd:PRK08279 475 TEVENALSGFPGVEEAVVYGVE-VPGtDGRAgMAAIVLADGAEFDLAALAAHLYERLPAYAVP 536
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1531-2021 |
4.30e-34 |
|
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: 141.54 E-value: 4.30e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1531 HQLVEDQAARTPDTTAVLFE------DQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAA 1604
Cdd:cd05966 56 YNCLDRHLKERGDKVAIIWEgdepdqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAV 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1605 YVPLDPGYPAERLAYMLDDASPVALLTqANQraLLTGDVPRILLDTAD--------------FSHLSEDNPHVPG----- 1665
Cdd:cd05966 136 HSVVFAGFSAESLADRINDAQCKLVIT-ADG--GYRGGKVIPLKEIVDealekcpsvekvlvVKRTGGEVPMTEGrdlww 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1666 ---------------LDAHHLAYVIYTSGSTGKPKGVMNSHRALcnrLVW----MQNTYRLTPDDRvlqktpfsfdvsvw 1726
Cdd:cd05966 213 hdlmakqspecepewMDSEDPLFILYTSGSTGKPKGVVHTTGGY---LLYaattFKYVFDYHPDDI-------------- 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1727 efFW-----------------PLLYGARLVM--ARPDgHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADC-ACD- 1785
Cdd:cd05966 276 --YWctadigwitghsyivygPLANGATTVMfeGTPT-YPDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVkKHDl 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1786 -SLRrVICS-GEALPAELQQRFfarfnaqlHNLYGPTEAAIDVTFW-------------ACQPDDHRSfvpIGRPIANTQ 1850
Cdd:cd05966 353 sSLR-VLGSvGEPINPEAWMWY--------YEVIGKERCPIVDTWWqtetggimitplpGATPLKPGS---ATRPFFGIE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1851 LYILDTLGQPVPLGVAGELHIGGV--GVARGYLNRPdltaERFIPDPFINQPGarLYKTGDLARWLPDGSLEYLGRNDFQ 1928
Cdd:cd05966 421 PAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDH----ERYEDTYFSKFPG--YYFTGDGARRDEDGYYWITGRVDDV 494
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1929 VKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPaDLRQQLGQHLAEymVPGAFVTLDAF 2008
Cdd:cd05966 495 INVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSD-ELRKELRKHVRK--EIGPIATPDKI 571
|
570
....*....|....*....
gi 641744967 2009 ------PLTPNGKLDRKAL 2021
Cdd:cd05966 572 qfvpglPKTRSGKIMRRIL 590
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1533-2021 |
8.45e-34 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 139.51 E-value: 8.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1533 LVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAI-CVERS--LDMVIGLLAIlkaGAAYVPLD 1609
Cdd:PRK06155 26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALmCGNRIefLDVFLGCAWL---GAIAVPIN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1610 PGYPAERLAYMLDDASPVALLTQANQ----RALLTGDVPR---ILLDTADFSHLSE--DNPHVPGLDAH---------HL 1671
Cdd:PRK06155 103 TALRGPQLEHILRNSGARLLVVEAALlaalEAADPGDLPLpavWLLDAPASVSVPAgwSTAPLPPLDAPapaaavqpgDT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1672 AYVIYTSGSTGKPKGVMNSHRALcnrLVWMQNTYR---LTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMAR---PDG 1745
Cdd:PRK06155 183 AAILYTSGTTGPSKGVCCPHAQF---YWWGRNSAEdleIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPrfsASG 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1746 HKDAAylaqliERTGITTLHFVPSMLQQFV-QWADADCACDSLRRVIcsGEALPAELQQRFFARFNAQLHNLYGPTEAai 1824
Cdd:PRK06155 260 FWPAV------RRHGATVTYLLGAMVSILLsQPARESDRAHRVRVAL--GPGVPAALHAAFRERFGVDLLDGYGSTET-- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1825 DVTFWACQPDDHRSFvpIGRPIANTQLYILDTLGQPVPLGVAGEL---HIGGVGVARGYLNRPDLTAERFIPDPFinqpg 1901
Cdd:PRK06155 330 NFVIAVTHGSQRPGS--MGRLAPGFEARVVDEHDQELPDGEPGELllrADEPFAFATGYFGMPEKTVEAWRNLWF----- 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1902 arlyKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPD 1981
Cdd:PRK06155 403 ----HTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLRDGTALE 478
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 641744967 1982 PADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK06155 479 PVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1537-2021 |
1.17e-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: 139.34 E-value: 1.17e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1537 QAARTPDTTAVLFED-----QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPG 1611
Cdd:cd05906 18 RAAERGPTKGITYIDadgseEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1612 ----YPAERLAY------MLDdaSPVALLTQANQ---RALLTGD-VPRILLDTADFSHLSEDNPHVPGLDAHHLAYVIYT 1677
Cdd:cd05906 98 ptydEPNARLRKlrhiwqLLG--SPVVLTDAELVaefAGLETLSgLPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLT 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1678 SGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEF-FWPLLYGARLVMARPDghkdaAYLAQ-- 1754
Cdd:cd05906 176 SGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVPLDHVGGLVELhLRAVYLGCQQVHVPTE-----EILADpl 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1755 ----LIERTGITTL---HFVPSMLQQFVQWADADCA-CDSLRRVICSGEALPAELQQRF---FARFNAQ---LHNLYGPT 1820
Cdd:cd05906 251 rwldLIDRYRVTITwapNFAFALLNDLLEEIEDGTWdLSSLRYLVNAGEAVVAKTIRRLlrlLEPYGLPpdaIRPAFGMT 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1821 EAAIDVTFWA-CQPDDHR---SFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPF 1896
Cdd:cd05906 331 ETCSGVIYSRsFPTYDHSqalEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1897 inqpgarlYKTGDLArWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVA---REDSPGDTRLVAYLC 1973
Cdd:cd05906 411 --------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAfavRDPGAETEELAIFFV 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 1974 PQPGVTPDPADLRQQLGQHLA-------EYMVPgafVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05906 482 PEYDLQDALSETLRAIRSVVSrevgvspAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
480-968 |
1.26e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 139.40 E-value: 1.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 480 EAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPA 559
Cdd:PRK06710 31 EQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 560 ERLAYILDDAAPVALLTQSAQVAQLNSTLPTVLLDTPAAAACPDTNPVVQGL-------------------HAAHL---- 616
Cdd:PRK06710 111 RELEYQLHDSGAKVILCLDLVFPRVTNVQSATKIEHVIVTRIADFLPFPKNLlypfvqkkqsnlvvkvsesETIHLwnsv 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 617 ------------------AYVIYTSGSTGRPKGVMVAHRNVI-NLATGLHTLLALDHPSRIALNASIVFD----ASVKNw 673
Cdd:PRK06710 191 ekevntgvevpcdpendlALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVVLGVLPFFHvygmTAVMN- 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 674 IQLLSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAISPA-VWSRLQSL 752
Cdd:PRK06710 270 LSIMQGYKMVLIP---KFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIRACISGSAPLPVeVQEKFETV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 753 SDTRFINVYGPTECT-VDATACVVDRTQPlPTIGKPLANTRLYILDAQD-QPVPIGVTGELHIGGAGVARGYLHRPDLTA 830
Cdd:PRK06710 347 TGGKLVEGYGLTESSpVTHSNFLWEKRVP-GSIGVPWPDTEAMIMSLETgEALPPGEIGEIVVKGPQIMKGYWNKPEETA 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 831 ErfipdpfsadpaarIYKTGdlarWLPDGNIDYLGRNDF---------QIKVRGFRIEAGEIESRLLRCPGVQDAVVIAR 901
Cdd:PRK06710 426 A--------------VLQDG----WLHTGDVGYMDEDGFfyvkdrkkdMIVASGFNVYPREVEEVLYEHEKVQEVVTIGV 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 902 EDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAPDQ 968
Cdd:PRK06710 488 PDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEK 554
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1532-2021 |
1.30e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 139.02 E-value: 1.30e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1532 QLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPG 1611
Cdd:PRK07470 11 HFLRQAARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1612 YPAERLAYMLDDASPVALLTQAN-------QRALLTGDVPRILLDTADFSH----LSEDNPHVPGLDAH----HLAYVIY 1676
Cdd:PRK07470 91 QTPDEVAYLAEASGARAMICHADfpehaaaVRAASPDLTHVVAIGGARAGLdyeaLVARHLGARVANAAvdhdDPCWFFF 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1677 TSGSTGKPKGVMNSHRALC----NRLV-WMQNTyrlTPDDRVLQKTPFSFDVSVWEffwpLLYGARLVMA--RPDGHKDA 1749
Cdd:PRK07470 171 TSGTTGRPKAAVLTHGQMAfvitNHLAdLMPGT---TEQDASLVVAPLSHGAGIHQ----LCQVARGAATvlLPSERFDP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1750 AYLAQLIERTGITTLHFVPSMLQQFVQWADADcACD--SLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVT 1827
Cdd:PRK07470 244 AEVWALVERHRVTNLFTVPTILKMLVEHPAVD-RYDhsSLRYVIYAGAPMYRADQKRALAKLGKVLVQYFGLGEVTGNIT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1828 -----FWACQPDDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpga 1902
Cdd:PRK07470 323 vlppaLHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF------ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1903 rlyKTGDLARWLPDGSLEYLGR-NDFQVKlRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPD 1981
Cdd:PRK07470 397 ---RTGDLGHLDARGFLYITGRaSDMYIS-GGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVD 472
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 641744967 1982 PADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK07470 473 EAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
487-963 |
1.52e-33 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 138.97 E-value: 1.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAyvPMDPAYPAERL---A 563
Cdd:PRK10946 37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSelnA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 564 YIlDDAAPvALLTQSAQ---------VAQLNSTLPTV----------------LLDTPAAAACPDTNPvvqglhAAHLAY 618
Cdd:PRK10946 115 YA-SQIEP-ALLIADRQhalfsdddfLNTLVAEHSSLrvvlllnddgehslddAINHPAEDFTATPSP------ADEVAF 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 619 VIYTSGSTGRPKGVMVAH--------RNVINLATGLHT--LLALDHPSRIALN---ASIVFDAsvknwiqllsGHTLVLV 685
Cdd:PRK10946 187 FQLSGGSTGTPKLIPRTHndyyysvrRSVEICGFTPQTryLCALPAAHNYPMSspgALGVFLA----------GGTVVLA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 686 PDAlraDAHQLWRYFARHAVDLFDCTP--VQLqWLLDAGL-GSDPAYQPAQVL-IGGEAISPAVWSRLQSLSDTRFINVY 761
Cdd:PRK10946 257 PDP---SATLCFPLIEKHQVNVTALVPpaVSL-WLQAIAEgGSRAQLASLKLLqVGGARLSETLARRIPAELGCQLQQVF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 762 GPTECTVDATACVVDRTQPLPTIGKPLA-NTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsa 840
Cdd:PRK10946 333 GMAEGLVNYTRLDDSDERIFTTQGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF-- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 841 dpaariYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARpdA 920
Cdd:PRK10946 411 ------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVK--E 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 641744967 921 ELHPAALRQQL-AASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK10946 483 PLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
499-963 |
1.66e-33 |
|
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: 136.88 E-value: 1.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQS 578
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 AQVAQLnstlptvlldtpaaaacpDTNPVVQglhaahlayvIYTSGSTGRPKGVMVAHRNVinLATGLHTLLALDHPSri 658
Cdd:cd05973 81 ANRHKL------------------DSDPFVM----------MFTSGTTGLPKGVPVPLRAL--AAFGAYLRDAVDLRP-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 659 alnASIVFDASVKNWI---------QLLSGHTLVLVPDALRADAhqLWRYFARHAVDLFDCTPVQLQWLLDAGLGS--DP 727
Cdd:cd05973 129 ---EDSFWNAADPGWAyglyyaitgPLALGHPTILLEGGFSVES--TWRVIERLGVTNLAGSPTAYRLLMAAGAEVpaRP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 728 AYQPAQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTEC-TVDATACVVDRTQPLPTIGKPLANTRLYILD-AQDQPVPi 805
Cdd:cd05973 204 KGRLRRVSSAGEPLTPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVHAGSAGRAMPGWRVAVLDdDGDELGP- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 806 GVTGELHIGGAGVA----RGYLHRPDltaerfipdpfsADPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAG 881
Cdd:cd05973 283 GEPGRLAIDIANSPlmwfRGYQLPDT------------PAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPF 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 882 EIESRLLRCPGVQDAVVIAREDsPGDTRLV-AYLCARPDAELHPA---ALRQQLAASLADYMIPSAFVTLDALPLTPNGK 957
Cdd:cd05973 351 DVESALIEHPAVAEAAVIGVPD-PERTEVVkAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDELPKTPSGK 429
|
....*.
gi 641744967 958 LDRKAL 963
Cdd:cd05973 430 IQRFLL 435
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1529-2023 |
1.77e-33 |
|
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: 139.93 E-value: 1.77e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1529 LIHQLVEDQAARTPDTTAVLFEDQH-----LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGA 1603
Cdd:cd05968 62 IVEQLLDKWLADTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1604 AYVPLDPGYPAERLAYMLDDASPVALLTqanQRALLTGDVPRILLDTADFS--------------HLSEDNPHVPGLD-- 1667
Cdd:cd05968 142 IVVPIFSGFGKEAAATRLQDAEAKALIT---ADGFTRRGREVNLKEEADKAcaqcptvekvvvvrHLGNDFTPAKGRDls 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1668 --------AHHLA--------YVIYTSGSTGKPKGVMNSHRALCNRLVW-MQNTYRLTPDDRVLQKTPFSFDVSVWEFFW 1730
Cdd:cd05968 219 ydeeketaGDGAErtesedplMIIYTSGTTGKPKGTVHVHAGFPLKAAQdMYFQFDLKPGDLLTWFTDLGWMMGPWLIFG 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1731 PLLYGARLVM--ARPDgHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADCACDSLR--RVICS-GEALPAELQQRF 1805
Cdd:cd05968 299 GLILGATMVLydGAPD-HPKADRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSslRVLGStGEPWNPEPWNWL 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1806 FARF---NAQLHNLYGPTEaaIDVTFWACQPddHRSFVPIG--RPIANTQLYILDTLGQPVPlGVAGELHIGG--VGVAR 1878
Cdd:cd05968 378 FETVgkgRNPIINYSGGTE--ISGGILGNVL--IKPIKPSSfnGPVPGMKADVLDESGKPAR-PEVGELVLLApwPGMTR 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1879 GYLNRPDltaeRFIPDPFINQPGARLYktGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVA 1958
Cdd:cd05968 453 GFWRDED----RYLETYWSRFDNVWVH--GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIG 526
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 1959 REDSPGDTRLVAYLCPQPGVTPDPA---DLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPA 2023
Cdd:cd05968 527 VPHPVKGEAIVCFVVLKPGVTPTEAlaeELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
2597-3095 |
2.09e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 138.98 E-value: 2.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2597 ATDADIPRHALIHeLFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGI 2676
Cdd:PRK05605 24 PHDLDYGDTTLVD-LYDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2677 LKAGGAYVPLDPTYPVERLRYMLDD--AK-------------------------PVALISQSAHLGIMNGSLPVILLDDG 2729
Cdd:PRK05605 103 LRLGAVVVEHNPLYTAHELEHPFEDhgARvaivwdkvaptverlrrttpletivSVNMIAAMPLLQRLALRLPIPALRKA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2730 E---------TRPFDNEPDTPLDARKQGL-----TPRHLAYVIYTSGSTGKPKGVMVEHAN-MVNFLCSMRKEPGIA-QE 2793
Cdd:PRK05605 183 RaaltgpapgTVPWETLVDAAIGGDGSDVshprpTPDDVALILYTSGTTGKPKGAQLTHRNlFANAAQGKAWVPGLGdGP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2794 DVLLGVTSL--SFDISILEIFLPLLnGARLILATQAQAADAQQlamLIERHAVSFMQATPSTWRMLVEL---RDFALPPG 2868
Cdd:PRK05605 263 ERVLAALPMfhAYGLTLCLTLAVSI-GGELVLLPAPDIDLILD---AMKKHPPTWLPGVPPLYEKIAEAaeeRGVDLSGV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2869 FKALCGGEALPENLaTALLQKVT--TLWNLYGPTETTIWSTLNGLTTP--TPYIGHPIANTQIYILDAQ--GRVVPLGVA 2942
Cdd:PRK05605 339 RNAFSGAMALPVST-VELWEKLTggLLVEGYGLTETSPIIVGNPMSDDrrPGYVGVPFPDTEVRIVDPEdpDETMPDGEE 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2943 GEIHIAGAGVVRGYLGRPDLTAERFITDpfsgapearMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLA 3022
Cdd:PRK05605 418 GELLVRGPQVFKGYWNRPEETAKSFLDG---------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLR 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 3023 RCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRK 3095
Cdd:PRK05605 489 EHPGVEDAAVVGLPREDGSEEVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1067-1339 |
2.52e-33 |
|
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: 135.84 E-value: 2.52e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1067 PLPLSFSQQrlWFLAQlDPAASQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDTLG-FS 1145
Cdd:cd19534 1 EVPLTPIQR--WFFEQ-NLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEElFR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1146 LSSHDLRKLDEAARttrVAELAEqEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAA 1225
Cdd:cd19534 78 LEVVDLSSLAQAAA---IEALAA-EAQSSLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1226 LEGSEANLPPLPvQYADYAVWQRQWLQGETLNDLRDYWRDQLQGAPAllEIPTDRPrpsvQRYAG-DQVPFHLDAGQLRR 1304
Cdd:cd19534 154 LAGEPIPLPSKT-SFQTWAELLAEYAQSPALLEELAYWRELPAADYW--GLPKDPE----QTYGDaRTVSFTLDEEETEA 226
|
250 260 270
....*....|....*....|....*....|....*.
gi 641744967 1305 L-HALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVI 1339
Cdd:cd19534 227 LlQEANAAYRTEINDLLLAALALAFQDWTGRAPPAI 262
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1538-2024 |
3.14e-33 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 137.97 E-value: 3.14e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERL 1617
Cdd:PRK13382 53 AQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPAL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1618 AYMLDDASPVALLTQANqralLTGDVPRILLDTADFSHLSE--DNPH---VPGLDAHHLA-----------YVIYTSGST 1681
Cdd:PRK13382 133 AEVVTREGVDTVIYDEE----FSATVDRALADCPQATRIVAwtDEDHdltVEVLIAAHAGqrpeptgrkgrVILLTSGTT 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1682 GKPKGVMNSHRAlcnrlvwmqntyrlTPDD--RVLQKTPFSFDVSV---------WEFFWPLLYGA---RLVMARpdgHK 1747
Cdd:PRK13382 209 GTPKGARRSGPG--------------GIGTlkAILDRTPWRAEEPTvivapmfhaWGFSQLVLAASlacTIVTRR---RF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1748 DAAYLAQLIERTGITTLHFVPSMLQQFVQWAD---ADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAI 1824
Cdd:PRK13382 272 DPEATLDLIDRHRATGLAVVPVMFDRIMDLPAevrNRYSGRSLRFAAASGSRMRPDVVIAFMDQFGDVIYNNYNATEAGM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1825 DVTfwaCQPDDHRSFVPI-GRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYlnRPDLTAErfIPDPFINqpgar 1903
Cdd:PRK13382 352 IAT---ATPADLRAAPDTaGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD--FHDGFMA----- 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1904 lykTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPA 1983
Cdd:PRK13382 420 ---SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPE 496
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 641744967 1984 DLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPAP 2024
Cdd:PRK13382 497 TLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1538-2021 |
5.62e-33 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 135.38 E-value: 5.62e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERL 1617
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1618 AymlddaspvALLTQANQRALLTGDVPRILLDTADFSHLSEDNPHVPGLDAHHLAYVIYTSGSTGKPKGVMNSHRA-LCN 1696
Cdd:PRK09029 93 E---------ELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAhLAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1697 R---LVWMQntyrLTPDDRVLQKTPFsFDVS----VWEffWpLLYGARLVMarPDGHKDAAYLAqliertGITTLHFVPS 1769
Cdd:PRK09029 164 AegvLSLMP----FTAQDSWLLSLPL-FHVSgqgiVWR--W-LYAGATLVV--RDKQPLEQALA------GCTHASLVPT 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1770 MLQQFVQWADADCacdSLRRVICSGEALPAELQQRffarfnAQLHNL-----YGPTEAAIDVTfwACQPDDHRSfvpIGR 1844
Cdd:PRK09029 228 QLWRLLDNRSEPL---SLKAVLLGGAAIPVELTEQ------AEQQGIrcwcgYGLTEMASTVC--AKRADGLAG---VGS 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1845 PIANTQLYIldtlgqpvplgVAGELHIGGVGVARGYLNRPDLTaerfipdPFINQPGarLYKTGDLARWLpDGSLEYLGR 1924
Cdd:PRK09029 294 PLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEG--WFATRDRGEWQ-NGELTILGR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1925 NDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLcpQPGVTPDPADLRQQLGQHLAEYMVPGAFVT 2004
Cdd:PRK09029 353 LDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV--ESDSEAAVVNLAEWLQDKLARFQQPVAYYL 430
|
490
....*....|....*..
gi 641744967 2005 LDAFPLTPNGKLDRKAL 2021
Cdd:PRK09029 431 LPPELKNGGIKISRQAL 447
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
483-958 |
6.61e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 136.83 E-value: 6.61e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERL 562
Cdd:PRK07786 27 ALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 563 AYILDDAAPVALLTQS------AQVAQLNSTLPTVL------------LDTPAAAACPDTNPVVQGLHAAhlAYVIYTSG 624
Cdd:PRK07786 107 AFLVSDCGAHVVVTEAalapvaTAVRDIVPLLSTVVvaggssddsvlgYEDLLAEAGPAHAPVDIPNDSP--ALIMYTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 625 STGRPKGVMVAHRNVINLA-TGLHTlLALDHPSRIALNASIVFD-ASVKNWIQ-LLSGHTLVLVPdaLRA-DAHQLWRYF 700
Cdd:PRK07786 185 TTGRPKGAVLTHANLTGQAmTCLRT-NGADINSDVGFVGVPLFHiAGIGSMLPgLLLGAPTVIYP--LGAfDPGQLLDVL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 701 ARHAVDLFDCTPVQLQWLLDAGlGSDPAYQPAQVLIGGEAisPAVWSRLQSLS----DTRFINVYGPTEctVDATACVV- 775
Cdd:PRK07786 262 EAEKVTGIFLVPAQWQAVCAEQ-QARPRDLALRVLSWGAA--PASDTLLRQMAatfpEAQILAAFGQTE--MSPVTCMLl 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 776 --DRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFipdpfsadpAARIYKTGDLA 853
Cdd:PRK07786 337 geDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF---------AGGWFHSGDLV 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 854 RWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPD-AELHPAALRQQLA 932
Cdd:PRK07786 408 RQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDdAALTLEDLAEFLT 487
|
490 500
....*....|....*....|....*.
gi 641744967 933 ASLADYMIPSAFVTLDALPLTPNGKL 958
Cdd:PRK07786 488 DRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2163-2542 |
7.71e-33 |
|
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: 134.51 E-value: 7.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2163 PLAPLQEGILF-HHLLQEQgDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCWQ-DLSQPVQVVWRQAILPIN 2240
Cdd:cd19532 3 PMSFGQSRFWFlQQYLEDP-TTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDpEDGEPMQGVLASSPLRLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2241 HFEPTSPEDVLAQLQAHtepRTRRIDLSQAPLFRA-DIAHDPlqNEWLLALSFHHLISDHMTLALIVGEIRLLLQHQADa 2319
Cdd:cd19532 82 HVQISDEAEVEEEFERL---KNHVYDLESGETMRIvLLSLSP--TEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPL- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2320 LPTPLPYRNF-IAQTLSVPNSAHE---AYFRDKLADVDEPTAPFGLLNVQG----SGGDIHEARLVLDATLASAIRQQAR 2391
Cdd:cd19532 156 LPPPLQYLDFaARQRQDYESGALDedlAYWKSEFSTLPEPLPLLPFAKVKSrpplTRYDTHTAERRLDAALAARIKEASR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2392 HLGVSPgvlFHV---AWAQVLAQTSGRDDVVFGSVLLGRlaGAEGADRIMGMFINTLPLRISLaDRGA--AEVVERTSHD 2466
Cdd:cd19532 236 KLRVTP---FHFylaALQVLLARLLDVDDICIGIADANR--TDEDFMETIGFFLNLLPLRFRR-DPSQtfADVLKETRDK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2467 LMTLLEHEQAPLAL------AQRCSGvapPMPLFSTLLNYRhtQASSTDNTLSDIR---VLTSEERTNYPLTLAVDDRGE 2537
Cdd:cd19532 310 AYAALAHSRVPFDVlldelgVPRSAT---HSPLFQVFINYR--QGVAESRPFGDCElegEEFEDARTPYDLSLDIIDNPD 384
|
....*
gi 641744967 2538 GFSLV 2542
Cdd:cd19532 385 GDCLL 389
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1536-2021 |
7.79e-33 |
|
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: 137.83 E-value: 7.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1536 DQAARTPDTtAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAE 1615
Cdd:cd05967 66 DQIALIYDS-PVTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGFAAK 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1616 RLAYMLDDASPVALLTqAN--------------------------------QRALLTGDVPRIL--LDTADFSHLSEDNP 1661
Cdd:cd05967 145 ELASRIDDAKPKLIVT-AScgiepgkvvpykplldkalelsghkphhvlvlNRPQVPADLTKPGrdLDWSELLAKAEPVD 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1662 HVPgLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVW-MQNTYRLTPDDrvlqktpfsfdvsVW----EFFW------ 1730
Cdd:cd05967 224 CVP-VAATDPLYILYTSGTTGKPKGVVRDNGGHAVALNWsMRNIYGIKPGD-------------VWwaasDVGWvvghsy 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1731 ----PLLYGARLVM--ARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQwADAD------CACDSLRRVICSGEALP 1798
Cdd:cd05967 290 ivygPLLHGATTVLyeGKPVGTPDPGAFWRVIEKYQVNALFTAPTAIRAIRK-EDPDgkyikkYDLSSLRTLFLAGERLD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1799 AELQQRFFARFNAQLHNLYGPTEaaidvTFWA--CQPddhRSFVPI-------GRPIANTQLYILDTLGQPVPLGVAGEL 1869
Cdd:cd05967 369 PPTLEWAENTLGVPVIDHWWQTE-----TGWPitANP---VGLEPLpikagspGKPVPGYQVQVLDEDGEPVGPNELGNI 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1870 HIGGvGVARGYLNRPDLTAERFIPDPFINQPGarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCP 1949
Cdd:cd05967 441 VIKL-PLPPGCLLTLWKNDERFKKLYLSKFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHP 517
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 1950 GVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVP-GAF---VTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05967 518 AVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVALVREQIGPvAAFrlvIFVKRLPKTRSGKILRRTL 593
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
487-957 |
1.39e-32 |
|
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: 135.12 E-value: 1.39e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYIL 566
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 567 DDAAPVALL--TQSAQVAQLNSTLPTVLLDTPAAaacpDTNPVVqglhaahlayVIYTSGSTGRPKGVMVAHRN--VINL 642
Cdd:cd12118 98 RHSEAKVLFvdREFEYEDLLAEGDPDFEWIPPAD----EWDPIA----------LNYTSGTTGRPKGVVYHHRGayLNAL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 643 ATGLHTLLaldHPSRIALNASIVFDAS--VKNWIQLLSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLD 720
Cdd:cd12118 164 ANILEWEM---KQHPVYLWTLPMFHCNgwCFPWTVAAVGGTNVCLR---KVDAKAIYDLIEKHKVTHFCGAPTVLNMLAN 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 721 AG-LGSDPAYQPAQVLIGGEAISPAVWSRLQSLSdTRFINVYGPTECTVDATACVvdrTQP----LPTIGKPLANTR--- 792
Cdd:cd12118 238 APpSDARPLPHRVHVMTAGAPPPAAVLAKMEELG-FDVTHVYGLTETYGPATVCA---WKPewdeLPTEERARLKARqgv 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 793 -------LYILDAQ-DQPVPI-GVT-GELHIGGAGVARGYLHRPDLTAERFipdpfsadpAARIYKTGDLARWLPDGNID 862
Cdd:cd12118 314 ryvgleeVDVLDPEtMKPVPRdGKTiGEIVFRGNIVMKGYLKNPEATAEAF---------RGGWFHSGDLAVIHPDGYIE 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 863 YLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPS 942
Cdd:cd12118 385 IKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEIIAFCREHLAGFMVPK 464
|
490
....*....|....*
gi 641744967 943 AFVTLDaLPLTPNGK 957
Cdd:cd12118 465 TVVFGE-LPKTSTGK 478
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
28-434 |
1.99e-32 |
|
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: 133.21 E-value: 1.99e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 28 IYPLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICWQGLHQPVQVVWR--QAPLT 105
Cdd:cd19547 1 VYPLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDdlAPPWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 106 VNTLTTTSSDTVPAQL-RAATDPSNHRLNLSNAPLLSATTAHDPVCGEWLLsLSIHHLISDHITQALIIDEIRLLLED-- 182
Cdd:cd19547 81 LLDWSGEDPDRRAELLeRLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLL-WSHHHILLDGWCLSLIWGDVFRVYEEla 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 183 --RPEALPKPLPYRNFIAQIL--SVPLSEHEQYFRNRLADIdTPTaPFDLVDVQGNGEDITEARlSLDSSLADALRRQAR 258
Cdd:cd19547 160 hgREPQLSPCRPYRDYVRWIRarTAQSEESERFWREYLRDL-TPS-PFSTAPADREGEFDTVVH-EFPEQLTRLVNEAAR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 259 HLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQGNLGADRVMGMFINTLPLRVSLR-ERSVHDVVQATSHELMML 337
Cdd:cd19547 237 GYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDpDQTVTGLLETIHRDLATT 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 338 LAHEQAPLALAQQCS--------QVPPPLPLFSTLFNYRHSQKDASSQFWEgmrqLSGRERTNYPITLSV---DDLGDGF 406
Cdd:cd19547 317 AAHGHVPLAQIKSWAsgerlsggRVFDNLVAFENYPEDNLPGDDLSIQIID----LHAQEKTEYPIGLIVlplQKLAFHF 392
|
410 420
....*....|....*....|....*...
gi 641744967 407 NLTAKTVMGVDPERIVHYMLTAIENLVT 434
Cdd:cd19547 393 NYDTTHFTRAQVDRFIEVFRLLTEQLCR 420
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
618-959 |
3.22e-32 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 130.97 E-value: 3.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 618 YVIYTSGSTGRPKGVMVAHR-------NVINLATGLHTLLALDHPSRIAlNASIVF--------DASVKNWIQLLSGHTL 682
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEdifrmlmGGADFGTGEFTPSEDAHKAAAA-AAGTVMfpapplmhGTGSWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 683 VLVPDaLRADAHQLWRYFARHAVDLFDCT-PVQLQWLLDAGLGSDPAYQPAQVLI--GGEAISPAVWSRLQ-SLSDTRFI 758
Cdd:cd05924 86 VVLPD-DRFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALRDAGPYDLSSLFAIssGGALLSPEVKQGLLeLVPNITLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 759 NVYGPTEctVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAG-VARGYLHRPDLTAERFipdp 837
Cdd:cd05924 165 DAFGSSE--TGFTGSGHSAGSGPETGPFTRANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKTAETF---- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 838 FSADpAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCAR 917
Cdd:cd05924 239 PEVD-GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAVVQLR 317
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 641744967 918 PDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLD 959
Cdd:cd05924 318 EGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1554-2023 |
6.10e-32 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 135.93 E-value: 6.10e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQA 1633
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1634 NQRALLTgdvPRILLDTAD-FSHLSEDNP---HVPGLDAHhlAYVIYTSGSTGKPKGVMNSH-------RALCnrlvwmQ 1702
Cdd:PRK06060 111 ALRDRFQ---PSRVAEAAElMSEAARVAPggyEPMGGDAL--AYATYTSGTTGPPKAAIHRHadpltfvDAMC------R 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1703 NTYRLTPDDRVLQKTPFSFDV----SVWeffWPLLYGARLVMAR-PDGHKDAAYLAQLIERTgitTLHFVPSMlqqFVQW 1777
Cdd:PRK06060 180 KALRLTPEDTGLCSARMYFAYglgnSVW---FPLATGGSAVINSaPVTPEAAAILSARFGPS---VLYGVPNF---FARV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1778 ADAdCACDSLRRVIC---SGEALPAELQQRFfARFNAQLHNLYGPTEAAIDVTFWACQPDDHRSFVpIGRPIANTQLYIL 1854
Cdd:PRK06060 251 IDS-CSPDSFRSLRCvvsAGEALELGLAERL-MEFFGGIPILDGIGSTEVGQTFVSNRVDEWRLGT-LGRVLPPYEIRVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1855 DTLGQPVPLGVAGELHIGGVGVARGYLNRPDltaerfipdPFINQPGarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGF 1934
Cdd:PRK06060 328 APDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---------SPVANEG--WLDTRDRVCIDSDGWVTYRCRADDTEVIGGV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1935 RIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPA---DLRQQLGQHLAEYMVPGAFVTLDAFPLT 2011
Cdd:PRK06060 397 NVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSvmrDLHRGLLNRLSAFKVPHRFAVVDRLPRT 476
|
490
....*....|..
gi 641744967 2012 PNGKLDRKALPA 2023
Cdd:PRK06060 477 PNGKLVRGALRK 488
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
2620-3097 |
1.19e-31 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 132.31 E-value: 1.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAV-VFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYM 2698
Cdd:PRK07514 16 RDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2699 LDDAKPVALISQSAHLGIMN------GSLPVILLDDGETRPF----DNEPDTPLDARKQgltPRHLAYVIYTSGSTGKPK 2768
Cdd:PRK07514 96 IGDAEPALVVCDPANFAWLSkiaaaaGAPHVETLDADGTGSLleaaAAAPDDFETVPRG---ADDLAAILYTSGTTGRSK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2769 GVMVEHANMVNFLCSMRKEPGIAQEDVLlgvtslsfdISILEIF----------LPLLNGARLILATQAQAADAQQlamL 2838
Cdd:PRK07514 173 GAMLSHGNLLSNALTLVDYWRFTPDDVL---------IHALPIFhthglfvatnVALLAGASMIFLPKFDPDAVLA---L 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2839 IERhAVSFMqATPSTW-RMLVElrdfalpPGF-KALCG-------GEA--LPENLAT-------ALLQKvttlwnlYGPT 2900
Cdd:PRK07514 241 MPR-ATVMM-GVPTFYtRLLQE-------PRLtREAAAhmrlfisGSAplLAETHREfqertghAILER-------YGMT 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2901 ETtiwstlnGLTTPTPY--------IGHPIANTQIYILD-AQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDP 2971
Cdd:PRK07514 305 ET-------NMNTSNPYdgerragtVGFPLPGVSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2972 FsgapearmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQ 3051
Cdd:PRK07514 378 F--------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGVPHPDFGEGVTAVVVPK 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 641744967 3052 PDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK07514 450 PGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLL 495
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
442-960 |
1.59e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 132.97 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 442 QPALSQPILPKSERQQVLVD-FNATDADFPREmliqqrfeaqaeqtpEAIAVLFEDQHLTYRELNRRANQLAHHLIALGV 520
Cdd:PRK12583 3 QPSYYQGGGDKPLLTQTIGDaFDATVARFPDR---------------EALVVRHQALRYTWRQLADAVDRLARGLLALGV 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 521 QPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLT-----QSAQVAQLNSTLPTVLLDT 595
Cdd:PRK12583 68 QPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPGLAEGQ 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 596 PAAAACP-----------------------------------DTNPVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVI 640
Cdd:PRK12583 148 PGALACErlpelrgvvslapapppgflawhelqargetvsreALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNIL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 641 NLATGLHTLLALDHPSRIALNASI--VFDASVKNWIQLLSGHTLVLVPDALRADAhqlwryfARHAVDLFDCTpvqlqwl 718
Cdd:PRK12583 228 NNGYFVAESLGLTEHDRLCVPVPLyhCFGMVLANLGCMTVGACLVYPNEAFDPLA-------TLQAVEEERCT------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 719 ldaGLGSDPAYQPAQV----------------LIGGEAISPAVWSR-LQSLSDTRFINVYGPTECT-VDATACVVDrtqP 780
Cdd:PRK12583 294 ---ALYGVPTMFIAELdhpqrgnfdlsslrtgIMAGAPCPIEVMRRvMDEMHMAEVQIAYGMTETSpVSLQTTAAD---D 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 781 LP----TIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAErfipdpfSADPAARIYkTGDLARWL 856
Cdd:PRK12583 368 LErrveTVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAE-------SIDEDGWMH-TGDLATMD 439
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 857 PDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLA 936
Cdd:PRK12583 440 EQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQVFGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIA 519
|
570 580
....*....|....*....|....
gi 641744967 937 DYMIPSAFVTLDALPLTPNGKLDR 960
Cdd:PRK12583 520 HFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
2608-3097 |
1.65e-31 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 132.70 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2608 IHELFEAQVACTPDAIAVVFGE--ASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVP 2685
Cdd:PRK05852 18 IADLVEVAATRLPEAPALVVTAdrIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVP 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2686 LDPTYPVERL---------RYMLDDAK-------------PVAlISQSAHLGIMNGSLPVILLDDGETrpfdnepdTPLD 2743
Cdd:PRK05852 98 LDPALPIAEQrvrsqaagaRVVLIDADgphdraepttrwwPLT-VNVGGDSGPSGGTLSVHLDAATEP--------TPAT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2744 ARKQGLTPRHlAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLIL 2823
Cdd:PRK05852 169 STPEGLRPDD-AMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVL 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2824 ATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVELRDFALPPG------FKALCGGEALPENLATALLQKVTTLWNLY 2897
Cdd:PRK05852 248 LPARGRFSAHTFWDDIKAVGATWYTAVPTIHQILLERAATEPSGRkpaalrFIRSCSAPLTAETAQALQTEFAAPVVCAF 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2898 GPTETTIWSTlnglTTPTPYIGH---PIANT---------QIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAE 2965
Cdd:PRK05852 328 GMTEATHQVT----TTQIEGIGQtenPVVSTglvgrstgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAA 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2966 RFiTDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLV 3045
Cdd:PRK05852 404 NF-TDGW--------LRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVA 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 641744967 3046 AYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK05852 475 AVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
2611-3100 |
2.04e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 131.27 E-value: 2.04e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2611 LFEAQVACTPD-AIAVVFGEASLSYDELNRRANRLAHhlisfGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPT 2689
Cdd:PRK07787 4 LNPAAVAAAADiADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2690 YPVERLRYMLDDAKPVALIsqsahlgimnGSLPvillDDGETRP-FDNEPDTPLDARKQGLTPRHLAYVIYTSGSTGKPK 2768
Cdd:PRK07787 79 SGVAERRHILADSGAQAWL----------GPAP----DDPAGLPhVPVRLHARSWHRYPEPDPDAPALIVYTSGTTGPPK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2769 GVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLsFDIS--ILEIFLPLLNGARLilatqaqaadaqqlamlieRHAVSF 2846
Cdd:PRK07787 145 GVVLSRRAIAADLDALAEAWQWTADDVLVHGLPL-FHVHglVLGVLGPLRIGNRF-------------------VHTGRP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2847 ---------------MQATPSTWRMLVELRDF--ALPPGFKALCGGEALP----ENLATALLQKVTtlwNLYGPTETTIW 2905
Cdd:PRK07787 205 tpeayaqalseggtlYFGVPTVWSRIAADPEAarALRGARLLVSGSAALPvpvfDRLAALTGHRPV---ERYGMTETLIT 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2906 STLNGLTTPTP-YIGHPIANTQIYILDAQGRVVPLGVA--GEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYK 2982
Cdd:PRK07787 282 LSTRADGERRPgWVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW--------FR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2983 TGDLGRWLPDGTLEYLGRN--DFqVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTvlEPAD 3060
Cdd:PRK07787 354 TGDVAVVDPDGMHRIVGREstDL-IKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDV--AADE 430
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 641744967 3061 LRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAP 3100
Cdd:PRK07787 431 LIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSE 470
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
1534-2035 |
2.46e-31 |
|
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: 133.14 E-value: 2.46e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1534 VEDQAARTPDTTAVLFE------DQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVP 1607
Cdd:TIGR02188 63 VDRHLEARPDKVAIIWEgdepgeVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1608 LDPGYPAERLAYMLDDASPVALLTqANQ-----RAL-LTGDVPRILLDTAD-------FSHLSEDNPH-VPGLD------ 1667
Cdd:TIGR02188 143 VFGGFSAEALADRINDAGAKLVIT-ADEglrggKVIpLKAIVDEALEKCPVsvehvlvVRRTGNPVVPwVEGRDvwwhdl 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1668 --------------AHHLAYVIYTSGSTGKPKGVMNSHRALcnrLVWMQNTYRLTpddrvlqktpfsFDVSVWEFFW--- 1730
Cdd:TIGR02188 222 makasaycepepmdSEDPLFILYTSGSTGKPKGVLHTTGGY---LLYAAMTMKYV------------FDIKDGDIFWcta 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1731 --------------PLLYGARLVM--ARPDgHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADCAC---DSLrRVI 1791
Cdd:TIGR02188 287 dvgwitghsyivygPLANGATTVMfeGVPT-YPDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGDEWVKKhdlSSL-RLL 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1792 CS-GEALPAELQQRFfarfnaqlHNLYGPTEAAIDVTFWACQPDDHR-----SFVPI-----GRPIANTQLYILDTLGQP 1860
Cdd:TIGR02188 365 GSvGEPINPEAWMWY--------YKVVGKERCPIVDTWWQTETGGIMitplpGATPTkpgsaTLPFFGIEPAVVDEEGNP 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1861 VP-LGVAGELHIGGV--GVARGYLNRPdltaERFIPDPFINQPGarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIE 1937
Cdd:TIGR02188 437 VEgPGEGGYLVIKQPwpGMLRTIYGDH----ERFVDTYFSPFPG--YYFTGDGARRDKDGYIWITGRVDDVINVSGHRLG 510
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1938 LGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPaDLRQQLGQHLAEYMVPGA------FVtlDAFPLT 2011
Cdd:TIGR02188 511 TAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDD-ELRKELRKHVRKEIGPIAkpdkirFV--PGLPKT 587
|
570 580
....*....|....*....|....
gi 641744967 2012 PNGKLDRKALpapdqSAVATRDYE 2035
Cdd:TIGR02188 588 RSGKIMRRLL-----RKIAAGEAE 606
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
497-899 |
2.75e-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: 130.56 E-value: 2.75e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 497 QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLT 576
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 577 QSAqvaqlnstlptvlldtpaaaacPDTnpvvqglhaahLAYVIYTSGSTGRPKGVMVAHRNVI----NLATGLHT---- 648
Cdd:cd17640 84 END----------------------SDD-----------LATIIYTSGTTGNPKGVMLTHANLLhqirSLSDIVPPqpgd 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 649 ----LLALDHPSR-------IALNASIVFDA--SVKNWIQLLSGHTLVLVP---DALRADAHQLWRyfarhavdlfDCTP 712
Cdd:cd17640 131 rflsILPIWHSYErsaeyfiFACGCSQAYTSirTLKDDLKRVKPHYIVSVPrlwESLYSGIQKQVS----------KSSP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 713 VQLQWLLDAGLGSdpayQPAQVLIGGEAISPAVwsrlqslsDTRF-------INVYGPTECTVDATAcvvdRTQPLP--- 782
Cdd:cd17640 201 IKQFLFLFFLSGG----IFKFGISGGGALPPHV--------DTFFeaigievLNGYGLTETSPVVSA----RRLKCNvrg 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 783 TIGKPLANTRLYILDAQ-DQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNI 861
Cdd:cd17640 265 SVGRPLPGTEIKIVDPEgNVVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW--------FNTGDLGWLTCGGEL 336
|
410 420 430
....*....|....*....|....*....|....*....
gi 641744967 862 DYLGRNDFQIKVR-GFRIEAGEIESRLLRCPGVQDAVVI 899
Cdd:cd17640 337 VLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1673-2017 |
5.43e-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: 341248 [Multi-domain] Cd Length: 364 Bit Score: 127.50 E-value: 5.43e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1673 YVIYTSGSTGKPKGVMNSH----RALCNRLVWMQNTYrlTPDDRVLQKT------------PFSFDVSVWEFFWPLLYGA 1736
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQedifRMLMGGADFGTGEF--TPSEDAHKAAaaaagtvmfpapPLMHGTGSWTAFGGLLGGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1737 RLVMarPDGHKDAAYLAQLIERTGITTLHFV------PsMLQQFVQWADADCAcdSLRRVICSGEALPAELQQRFFARF- 1809
Cdd:cd05924 85 TVVL--PDDRFDPEEVWRTIEKHKVTSMTIVgdamarP-LIDALRDAGPYDLS--SLFAISSGGALLSPEVKQGLLELVp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1810 NAQLHNLYGPTEAAIDVT-FWACQPDDHRSFVpigrpIANTQLYILDTLGQPVPLGVAGELHIGGVG-VARGYLNRPDLT 1887
Cdd:cd05924 160 NITLVDAFGSSETGFTGSgHSAGSGPETGPFT-----RANPDTVVLDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1888 AERFipdPFINqpGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTR 1967
Cdd:cd05924 235 AETF---PEVD--GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 641744967 1968 LVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLD 2017
Cdd:cd05924 310 VVAVVQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
2632-3101 |
5.60e-31 |
|
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: 129.16 E-value: 5.60e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISqs 2711
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLIT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2712 ahlgimngslpvillddgetrpfdnepdTPLDARKqgLTPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIA 2791
Cdd:cd05969 79 ----------------------------TEELYER--TDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2792 QEDVLLG------VTSLSFDIsileiFLPLLNGARLILATQAQAADAQQLAmlIERHAVSFMQATPSTWRML----VEL- 2860
Cdd:cd05969 129 PDDIYWCtadpgwVTGTVYGI-----WAPWLNGVTNVVYEGRFDAESWYGI--IERVKVTVWYTAPTAIRMLmkegDELa 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2861 RDFALPPGFKALCGGEAL-PENLATALLQKVTTLWNLYGPTETTIWSTLNGLTTPTP--YIGHPIANTQIYILDAQGRVV 2937
Cdd:cd05969 202 RKYDLSSLRFIHSVGEPLnPEAIRWGMEVFGVPIHDTWWQTETGSIMIANYPCMPIKpgSMGKPLPGVKAAVVDENGNEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2938 PLGVAGEIHIAGA--GVVRGYLGRPDLTAERFITDpfsgapearMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELG 3015
Cdd:cd05969 282 PPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDG---------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3016 EIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDtvLEPAD-----LRQRLSEGVAEYMIPSAFVTLDAFPLTPNG 3090
Cdd:cd05969 353 EVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEG--FEPSDelkeeIINFVRQKLGAHVAPREIEFVDNLPKTRSG 430
|
490
....*....|.
gi 641744967 3091 KLDRKALPAPD 3101
Cdd:cd05969 431 KIMRRVLKAKE 441
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
482-963 |
6.52e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 129.93 E-value: 6.52e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 482 QAEQTPEAIAV--LFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPA 559
Cdd:PRK09088 4 HARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 560 ERLAYILDDAAPvALLTQSAQVAQLnSTLPTVLLDTPAAAAC--PDTNPvvqGLHAAHLAYVIYTSGSTGRPKGVMVAHR 637
Cdd:PRK09088 84 SELDALLQDAEP-RLLLGDDAVAAG-RTDVEDLAAFIASADAlePADTP---SIPPERVSLILFTSGTSGQPKGVMLSER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 638 NVINLATGLHTLLALDHPSRIALNAS----IVFDASVKNwiQLLSGHTlVLVPDALRADAHQLWRYFARHAVDLFDCTPv 713
Cdd:PRK09088 159 NLQQTAHNFGVLGRVDAHSSFLCDAPmfhiIGLITSVRP--VLAVGGS-ILVSNGFEPKRTLGRLGDPALGITHYFCVP- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 714 QLQWLLDAGLGSDP-AYQPAQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTEC-TV---DATACVVDRTQPLPTIGKPL 788
Cdd:PRK09088 235 QMAQAFRAQPGFDAaALRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAgTVfgmSVDCDVIRAKAGAAGIPTPT 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 789 ANTRlyILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLGRND 868
Cdd:PRK09088 315 VQTR--VVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW--------FRTGDIARRDADGFFWVVDRKK 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 869 FQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLD 948
Cdd:PRK09088 385 DMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRLVD 464
|
490
....*....|....*
gi 641744967 949 ALPLTPNGKLDRKAL 963
Cdd:PRK09088 465 ALPRTASGKLQKARL 479
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
483-963 |
8.24e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 130.01 E-value: 8.24e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERL 562
Cdd:PRK06145 12 ARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 563 AYILDDAAPVALLTQSAQVAQLNSTLPTVLLDtpaAAACPDTNPVVQGLHAAHLAYV---------IYTSGSTGRPKGVM 633
Cdd:PRK06145 92 AYILGDAGAKLLLVDEEFDAIVALETPKIVID---AAAQADSRRLAQGGLEIPPQAAvaptdlvrlMYTSGTTDRPKGVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 634 VAHRNVinlatglhTLLALDHPSRIALNAS---IVFDASVKNWIQLLSGHTLVLVPDALRA----DAHQLWRYFARHAVD 706
Cdd:PRK06145 169 HSYGNL--------HWKSIDHVIALGLTASerlLVVGPLYHVGAFDLPGIAVLWVGGTLRIhrefDPEAVLAAIERHRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 707 LFDCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAISPAvwSRLQSLSD----TRFINVYGPTE-CTVDATACVVDRTQPL 781
Cdd:PRK06145 241 CAWMAPVMLSRVLTVPDRDRFDLDSLAWCIGGGEKTPE--SRIRDFTRvftrARYIDAYGLTEtCSGDTLMEAGREIEKI 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 782 PTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariyKTGDLARWLPDGNI 861
Cdd:PRK06145 319 GSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF---------RSGDVGYLDEEGFL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 862 DYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIP 941
Cdd:PRK06145 390 YLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVP 469
|
490 500
....*....|....*....|..
gi 641744967 942 SAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK06145 470 RQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1534-1999 |
1.77e-30 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 130.38 E-value: 1.77e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1534 VEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYP 1613
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1614 AERLAYMLDDASPVALLTQANQ-------RALLTGDVPRILLDTADF-------------SHLSEDNPHV-PGLDAHHLA 1672
Cdd:PRK08279 123 GAVLAHSLNLVDAKHLIVGEELveafeeaRADLARPPRLWVAGGDTLddpegyedlaaaaAGAPTTNPASrSGVTAKDTA 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1673 YVIYTSGSTGKPK-GVMNSHRALCNrLVWMQNTYRLTPDDRVLQKTPFSFDV-------SVweffwpLLYGARLVMAR-- 1742
Cdd:PRK08279 203 FYIYTSGTTGLPKaAVMSHMRWLKA-MGGFGGLLRLTPDDVLYCCLPLYHNTggtvawsSV------LAAGATLALRRkf 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1743 ------PDghkdaaylaqlIERTGITTLHFVPSM----LQQFVQWADADcacDSLRRVIcsGEALPAELQQRFFARFN-A 1811
Cdd:PRK08279 276 sasrfwDD-----------VRRYRATAFQYIGELcrylLNQPPKPTDRD---HRLRLMI--GNGLRPDIWDEFQQRFGiP 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1812 QLHNLYGPTEAaiDVTFW-------ACqpddhrSFVPI--GRPIA------NTQLYILDTLG--QPVPLGVAGELhIGGV 1874
Cdd:PRK08279 340 RILEFYAASEG--NVGFInvfnfdgTV------GRVPLwlAHPYAivkydvDTGEPVRDADGrcIKVKPGEVGLL-IGRI 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1875 GVAR---GYlNRPDLTAERFIPDPFinQPGARLYKTGDLARWLPDGSLEYLGR--NDFQVKlrGFRIELGEIEARLMQCP 1949
Cdd:PRK08279 411 TDRGpfdGY-TDPEASEKKILRDVF--KKGDAWFNTGDLMRDDGFGHAQFVDRlgDTFRWK--GENVATTEVENALSGFP 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 641744967 1950 GVQEAVV--VAREDSPGDTRLVAyLCPQPGVTPDPADLRQQLGQHLAEYMVP 1999
Cdd:PRK08279 486 GVEEAVVygVEVPGTDGRAGMAA-IVLADGAEFDLAALAAHLYERLPAYAVP 536
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
467-963 |
2.74e-30 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 129.40 E-value: 2.74e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 467 ADFPREMLIQQ------RFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLI-ALGVQPDDRVALCVERSLEMMVG 539
Cdd:PRK08974 11 ADVPAEINPDRyqslvdMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 540 LLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTqsaqVAQLNSTLPTVLLDTP-------------AAAACPDTNP 606
Cdd:PRK08974 91 LFGILRAGMIVVNVNPLYTPRELEHQLNDSGAKAIVI----VSNFAHTLEKVVFKTPvkhviltrmgdqlSTAKGTLVNF 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 607 VV-------------------QGLHAAH-------------LAYVIYTSGSTGRPKGVMVAHRNVI-NLATGLHTLLALD 653
Cdd:PRK08974 167 VVkyikrlvpkyhlpdaisfrSALHKGRrmqyvkpelvpedLAFLQYTGGTTGVAKGAMLTHRNMLaNLEQAKAAYGPLL 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 654 HPSR----IALNASIVFDASVKNWIQLLSGHTLVLV--PDALRADAHQLWRY--FARHAVD-LF-------DCTPVQLQW 717
Cdd:PRK08974 247 HPGKelvvTALPLYHIFALTVNCLLFIELGGQNLLItnPRDIPGFVKELKKYpfTAITGVNtLFnallnneEFQELDFSS 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 718 L-LDAGlgsdpayqpaqvliGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYIL 796
Cdd:PRK08974 327 LkLSVG--------------GGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 797 DAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAErFIPDPFSAdpaariykTGDLARWLPDGNIDYLGRNDFQIKVRGF 876
Cdd:PRK08974 393 DDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGWLA--------TGDIAVMDEEGFLRIVDRKKDMILVSGF 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 877 RIEAGEIESRLLRCPGVQDAVVIARE-DSPGDTrlVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPN 955
Cdd:PRK08974 464 NVYPNEIEDVVMLHPKVLEVAAVGVPsEVSGEA--VKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNV 541
|
....*...
gi 641744967 956 GKLDRKAL 963
Cdd:PRK08974 542 GKILRREL 549
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
2162-2542 |
2.87e-30 |
|
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: 126.70 E-value: 2.87e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2162 YPLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCWQDlSQPVQVVWRQAILPINH 2241
Cdd:cd19531 2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVD-GEPVQVILPPLPLPLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2242 --FEPTSPEDVLAQLQAHTEPRTRR-IDLSQAPLFRADIahdpLQ---NEWLLALSFHHLISDHMTLALIVGEIRLL--- 2312
Cdd:cd19531 81 vdLSGLPEAEREAEAQRLAREEARRpFDLARGPLLRATL----LRlgeDEHVLLLTMHHIVSDGWSMGVLLRELAALyaa 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2313 -LQHQADALPtPLP--YRNFIA---QTLSVPN-SAHEAYFRDKLADVDEPtapfglLN---------VQGSGGDIHeaRL 2376
Cdd:cd19531 157 fLAGRPSPLP-PLPiqYADYAVwqrEWLQGEVlERQLAYWREQLAGAPPV------LElptdrprpaVQSFRGARV--RF 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2377 VLDATLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGR-LAGAEGadrIMGMFINTLPLRISLA-DR 2454
Cdd:cd19531 228 TLPAELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRnRAELEG---LIGFFVNTLVLRTDLSgDP 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2455 GAAEVVERTSHDLMTLLEHEQAPL-----ALaqrcsgvAPP-----MPLFSTLLNYRHTQASSTDNTLSDIRVLTSEERT 2524
Cdd:cd19531 305 TFRELLARVRETALEAYAHQDLPFeklveAL-------QPErdlsrSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGT 377
|
410
....*....|....*....
gi 641744967 2525 -NYPLTLAVDDRGEGFSLV 2542
Cdd:cd19531 378 aKFDLTLSLTETDGGLRGS 396
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
2611-3097 |
3.02e-30 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 128.72 E-value: 3.02e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2611 LFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAI-CVERG--LDMVVGLLGIlkaGGAYVPLD 2687
Cdd:PRK06155 26 MLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALmCGNRIefLDVFLGCAWL---GAIAVPIN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2688 PTYPVERLRYMLDDAKPVALISQSAHLGIMNG------SLPVILLDDGET-----RPFDNEPDTPLDAR--KQGLTPRHL 2754
Cdd:PRK06155 103 TALRGPQLEHILRNSGARLLVVEAALLAALEAadpgdlPLPAVWLLDAPAsvsvpAGWSTAPLPPLDAPapAAAVQPGDT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2755 AYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLsFDISILEIFLP-LLNGARLILATQAQAADAQ 2833
Cdd:PRK06155 183 AAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTLPL-FHTNALNAFFQaLLAGATYVLEPRFSASGFW 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2834 QLamlIERHA----------VSFMQATPSTWRMLVELRDFALPPGFKALCgGEALPENLATALLQKvttlwnlYGPTETT 2903
Cdd:PRK06155 262 PA---VRRHGatvtyllgamVSILLSQPARESDRAHRVRVALGPGVPAAL-HAAFRERFGVDLLDG-------YGSTETN 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2904 IwstLNGLTTPTP---YIGHPIANTQIYILDAQGRVVPLGVAGEIhiagagVVR---------GYLGRPDLTAErfitdp 2971
Cdd:PRK06155 331 F---VIAVTHGSQrpgSMGRLAPGFEARVVDEHDQELPDGEPGEL------LLRadepfafatGYFGMPEKTVE------ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2972 fsgAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQ 3051
Cdd:PRK06155 396 ---AWRNLWFHTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAAVVLR 472
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 641744967 3052 PDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK06155 473 DGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
499-963 |
3.26e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 129.11 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIAL-GVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQ 577
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 578 S--------------------AQVAQLNSTLPTVLLDT--------------PAAAACPDTNPVVQG-------LHAAHL 616
Cdd:PRK05677 130 AnmahlaekvlpktgvkhvivTEVADMLPPLKRLLINAvvkhvkkmvpayhlPQAVKFNDALAKGAGqpvteanPQADDV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 617 AYVIYTSGSTGRPKGVMVAHRNVI------------NLATGLHTLLA---LDHPSRIALNASIVfdasvknwiqLLSGHT 681
Cdd:PRK05677 210 AVLQYTGGTTGVAKGAMLTHRNLVanmlqcralmgsNLNEGCEILIAplpLYHIYAFTFHCMAM----------MLIGNH 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 682 LVLVPDALRADAH----QLWRYFArhavdlFdctpVQLQWLLDAgLGSDPAYQPAQ------VLIGGEAISPAVWSRLQS 751
Cdd:PRK05677 280 NILISNPRDLPAMvkelGKWKFSG------F----VGLNTLFVA-LCNNEAFRKLDfsalklTLSGGMALQLATAERWKE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 752 LSDTRFINVYGPTECTVDATACVVDRTQpLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAE 831
Cdd:PRK05677 349 VTGCAICEGYGMTETSPVVSVNPSQAIQ-VGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 832 RFIPDPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLV 911
Cdd:PRK05677 428 ILDSDGW--------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIK 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 641744967 912 AYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK05677 500 VFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1552-2021 |
3.26e-30 |
|
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: 127.19 E-value: 3.26e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1552 QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLt 1631
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1632 qanqralltgDVPRilldtadfshlsednphvpgldAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDD 1711
Cdd:cd05910 80 ----------GIPK----------------------ADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1712 RVLQKTPfsfdvsVWEFFWPLLYGARLVMA----RPdGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADA-DCACDS 1786
Cdd:cd05910 128 VDLATFP------LFALFGPALGLTSVIPDmdptRP-ARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQhGITLPS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1787 LRRVICSGEALPAELQQRF--FARFNAQLHNLYGPTEA----AID----VTFWACQPDDHRSfVPIGRPIANTQLYILDT 1856
Cdd:cd05910 201 LRRVLSAGAPVPIALAARLrkMLSDEAEILTPYGATEAlpvsSIGsrelLATTTAATSGGAG-TCVGRPIPGVRVRIIEI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1857 LGQP---------VPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPfinqPGARLYKTGDLARWLPDGSLEYLGRNDF 1927
Cdd:cd05910 280 DDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN----SEGFWHRMGDLGYLDDEGRLWFCGRKAH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1928 QVKLRGFRIELGEIEARLMQCPGVQEAVVVAReDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVP---GAFVT 2004
Cdd:cd05910 356 RVITTGGTLYTEPVERVFNTHPGVRRSALVGV-GKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDYPHTqriGRFLI 434
|
490
....*....|....*....
gi 641744967 2005 LDAFPLTP--NGKLDRKAL 2021
Cdd:cd05910 435 HPSFPVDIrhNAKIFREKL 453
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1549-2018 |
3.39e-30 |
|
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: 127.17 E-value: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1549 FEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVA 1628
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1629 LLTQANqralltgdvprilldtadfshlsEDnphvpgldahhLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLT 1708
Cdd:cd05914 83 IFVSDE-----------------------DD-----------VALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1709 PDDRVLQKTPFSFDVS-VWEFFWPLLYGARLV-MARPDGHK-DAAYLAQLIERTGITTLHFV----------PSMLQQFV 1775
Cdd:cd05914 129 KGDKILSILPLHHIYPlTFTLLLPLLNGAHVVfLDKIPSAKiIALAFAQVTPTLGVPVPLVIekifkmdiipKLTLKKFK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1776 QWADADCACDSLR---------------RVICSGEA-LPAELQQrFFARFNAQLHNLYGPTEAAIDVTFwacQPDDHRSF 1839
Cdd:cd05914 209 FKLAKKINNRKIRklafkkvheafggniKEFVIGGAkINPDVEE-FLRTIGFPYTIGYGMTETAPIISY---SPPNRIRL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1840 VPIGRPIANTQLYILDtlgqPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSL 1919
Cdd:cd05914 285 GSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW--------FHTGDLGKIDAEGYL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1920 EYLGR-NDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDspgdtRLVAYlcpqpgVTPDPADL------------- 1985
Cdd:cd05914 353 YIRGRkKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEK-----KLVAL------AYIDPDFLdvkalkqrniida 421
|
490 500 510
....*....|....*....|....*....|....*....
gi 641744967 1986 -----RQQLGQHLAEY-MVPGAFVTLDAFPLTPNGKLDR 2018
Cdd:cd05914 422 ikwevRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1530-2026 |
3.81e-30 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 129.00 E-value: 3.81e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLD 1609
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1610 PGYPAERLAYMLDDASPVALL--------------TQANQRALLTG-----DVPRILL---------------DTADFSH 1655
Cdd:PRK06710 106 PLYTERELEYQLHDSGAKVILcldlvfprvtnvqsATKIEHVIVTRiadflPFPKNLLypfvqkkqsnlvvkvSESETIH 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1656 L-----SEDNP--HVPGLDAHHLAYVIYTSGSTGKPKGVMNSHRALC-NRLVWMQNTYRLTPDDRVLqktpfsfdVSVWE 1727
Cdd:PRK06710 186 LwnsveKEVNTgvEVPCDPENDLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEGEEVV--------LGVLP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1728 FFWplLYGARLVM--ARPDGHK-------DAAYLAQLIERTGITTLHFVPSMLQQFVQ---WADADCAcdSLRRVICSGE 1795
Cdd:PRK06710 258 FFH--VYGMTAVMnlSIMQGYKmvlipkfDMKMVFEAIKKHKVTLFPGAPTIYIALLNsplLKEYDIS--SIRACISGSA 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1796 ALPAELQQRFFARFNAQLHNLYGPTEAAidvtfwacqPDDHRSF-----VP--IGRPIANTQLYILD-TLGQPVPLGVAG 1867
Cdd:PRK06710 334 PLPVEVQEKFETVTGGKLVEGYGLTESS---------PVTHSNFlwekrVPgsIGVPWPDTEAMIMSlETGEALPPGEIG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1868 ELHIGGVGVARGYLNRPDLTAErFIPDPFINqpgarlykTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQ 1947
Cdd:PRK06710 405 EIVVKGPQIMKGYWNKPEETAA-VLQDGWLH--------TGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYE 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 1948 CPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPAPDQ 2026
Cdd:PRK06710 476 HEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEK 554
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1538-2023 |
4.24e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 128.19 E-value: 4.24e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERL 1617
Cdd:PRK13383 45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1618 AYMLDdASPVALLTQANQ---RALLTGDVPRILLDTADFSHLSEDNPHV--PGldahhlAYVIYTSGSTGKPKGVMNSHR 1692
Cdd:PRK13383 125 AAALR-AHHISTVVADNEfaeRIAGADDAVAVIDPATAGAEESGGRPAVaaPG------RIVLLTSGTTGKPKGVPRAPQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1693 ALCNRLVWMQ--NTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARpdgHKDA-AYLAQliertgiTTLH---- 1765
Cdd:PRK13383 198 LRSAVGVWVTilDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHR---HFDAeAALAQ-------ASLHrada 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1766 --FVPSMLQQFVQWAD---ADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTfwaCQPDDHRSFV 1840
Cdd:PRK13383 268 ftAVPVVLARILELPPrvrARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGAL---ATPADLRDAP 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1841 -PIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNrpdlTAERFIPDPfinqpgarLYKTGDLARWLPDGSL 1919
Cdd:PRK13383 345 eTVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTD----GGGKAVVDG--------MTSTGDMGYLDNAGRL 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1920 EYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVP 1999
Cdd:PRK13383 413 FIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQP 492
|
490 500
....*....|....*....|....
gi 641744967 2000 GAFVTLDAFPLTPNGKLDRKALPA 2023
Cdd:PRK13383 493 RDINIVSSIPRNPTGKVLRKELPG 516
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
483-965 |
4.43e-30 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 127.81 E-value: 4.43e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERL 562
Cdd:PRK13383 45 AARWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 563 AYILDDAAPVALLTQSAQVAQLNSTLPTVLLDTPAAAACPDTN--PVVqglhAAHLAYVIYTSGSTGRPKGVMVAH--RN 638
Cdd:PRK13383 125 AAALRAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGgrPAV----AAPGRIVLLTSGTTGKPKGVPRAPqlRS 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 639 VINLATGLHTLLALDHPSRIALNASIVFDASVKNWIQLLSGHTLVLVPDALraDAHQLWRYFARHAVDLFDCTPVQLQWL 718
Cdd:PRK13383 201 AVGVWVTILDRTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHF--DAEAALAQASLHRADAFTAVPVVLARI 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 719 LDAG---LGSDPAYQPAQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYI 795
Cdd:PRK13383 279 LELPprvRARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGDILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRI 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 796 LDAQDQPVPIGVTGELHIGGAGVARGYLHrpdlTAERFIPDPFSAdpaariykTGDLARWLPDGNIDYLGRNDFQIKVRG 875
Cdd:PRK13383 359 LDRNNRPVGPRVTGRIFVGGELAGTRYTD----GGGKAVVDGMTS--------TGDMGYLDNAGRLFIVGREDDMIISGG 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 876 FRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPN 955
Cdd:PRK13383 427 ENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPT 506
|
490
....*....|
gi 641744967 956 GKLDRKALPA 965
Cdd:PRK13383 507 GKVLRKELPG 516
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1533-2015 |
5.79e-30 |
|
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: 127.03 E-value: 5.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1533 LVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGY 1612
Cdd:cd12118 9 FLERAAAVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRL 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1613 PAERLAYMLDDASPVALL--TQANQRALLTGDVPrilldtadfshlseDNPHVPGLDAHHLAYVIYTSGSTGKPKGVMNS 1690
Cdd:cd12118 89 DAEEIAFILRHSEAKVLFvdREFEYEDLLAEGDP--------------DFEWIPPADEWDPIALNYTSGTTGRPKGVVYH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1691 HR-----ALCNRLVWmqntyRLTPDDRVLQKTPFsFDVSVWEFFW-PLLYGARLVMARpdgHKDAAYLAQLIERTGITtl 1764
Cdd:cd12118 155 HRgaylnALANILEW-----EMKQHPVYLWTLPM-FHCNGWCFPWtVAAVGGTNVCLR---KVDAKAIYDLIEKHKVT-- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1765 HF--VPSMLQQFVQWADADCACDSLR-RVICSGEALPAELQQRFfARFNAQLHNLYGPTEAAIDVTFWACQPD-DH---- 1836
Cdd:cd12118 224 HFcgAPTVLNMLANAPPSDARPLPHRvHVMTAGAPPPAAVLAKM-EELGFDVTHVYGLTETYGPATVCAWKPEwDElpte 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1837 -------RSFVPIgrpIANTQLYILDT-LGQPVPL-GV-AGELHIGGVGVARGYLNRPDLTAERFipdpfinQPGarLYK 1906
Cdd:cd12118 303 erarlkaRQGVRY---VGLEEVDVLDPeTMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF-------RGG--WFH 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1907 TGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLR 1986
Cdd:cd12118 371 SGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVELKEGAKVTEEEII 450
|
490 500
....*....|....*....|....*....
gi 641744967 1987 QQLGQHLAEYMVPGAFVTLDaFPLTPNGK 2015
Cdd:cd12118 451 AFCREHLAGFMVPKTVVFGE-LPKTSTGK 478
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
499-965 |
7.91e-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: 7.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQS 578
Cdd:cd05968 92 LTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITAD 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 AQVAQLNSTLPTVLLDTpAAAACPDTNPVV-------------------------QGLHAAHLA-----YVIYTSGSTGR 628
Cdd:cd05968 172 GFTRRGREVNLKEEADK-ACAQCPTVEKVVvvrhlgndftpakgrdlsydeeketAGDGAERTEsedplMIIYTSGTTGK 250
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 629 PKGVMVAHrnvinlatglhtllaLDHPSRIALNASIVFDasVKN-----WIQ--------------LLSGHTLVL---VP 686
Cdd:cd05968 251 PKGTVHVH---------------AGFPLKAAQDMYFQFD--LKPgdlltWFTdlgwmmgpwlifggLILGATMVLydgAP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 687 DALRADahQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQV-LIG--GEAISPAVWSRL-QSLSDTR--FINV 760
Cdd:cd05968 314 DHPKAD--RLWRMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSSLrVLGstGEPWNPEPWNWLfETVGKGRnpIINY 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 761 YGPTECTVDATACVVDRtqPLPTIG--KPLANTRLYILDAQDQPVPiGVTGELHIGGA--GVARGYLHRPDltaeRFIPD 836
Cdd:cd05968 392 SGGTEISGGILGNVLIK--PIKPSSfnGPVPGMKADVLDESGKPAR-PEVGELVLLAPwpGMTRGFWRDED----RYLET 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 837 PFSADPAARIYktGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCA 916
Cdd:cd05968 465 YWSRFDNVWVH--GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPVKGEAIVCFVVL 542
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 641744967 917 RPDAELHPaALRQQLAASLADYM----IPSAFVTLDALPLTPNGKLDRKALPA 965
Cdd:cd05968 543 KPGVTPTE-ALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
2620-3100 |
7.98e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 127.41 E-value: 7.98e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAI----CVERGLDMVVGLLgilkAGGAYVPLDPTYPVERL 2695
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALlslnRPEVLMAIGAAQL----AGLRRTALHPLGSLDDH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2696 RYMLDDAKPVALISQSAH-------LGIMNGSLPVIL-LDDGETRP-----FDNEPDTPLDARKQgltPRHLAYVIYTSG 2762
Cdd:PRK06188 102 AYVLEDAGISTLIVDPAPfveralaLLARVPSLKHVLtLGPVPDGVdllaaAAKFGPAPLVAAAL---PPDIAGLAYTGG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2763 STGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILeiFLP-LLNGARLILATQAQAADAQQlamLIER 2841
Cdd:PRK06188 179 TTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF--FLPtLLRGGTVIVLAKFDPAEVLR---AIEE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2842 HAVSFMQATPSTWRMLVE---LRDFALPPGFKALCGGEAL-PENLATALLQKVTTLWNLYGPTET--TIwSTL----NGL 2911
Cdd:PRK06188 254 QRITATFLVPTMIYALLDhpdLRTRDLSSLETVYYGASPMsPVRLAEAIERFGPIFAQYYGQTEApmVI-TYLrkrdHDP 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2912 TTPTPYI--GHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDpfsgapearMYKTGDLGRW 2989
Cdd:PRK06188 333 DDPKRLTscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG---------WLHTGDVARE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2990 LPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGV 3069
Cdd:PRK06188 404 DEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVLRPGAAVDAAELQAHVKERK 483
|
490 500 510
....*....|....*....|....*....|.
gi 641744967 3070 AEYMIPSAFVTLDAFPLTPNGKLDRKALPAP 3100
Cdd:PRK06188 484 GSVHAPKQVDFVDSLPLTALGKPDKKALRAR 514
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
2628-3033 |
8.06e-30 |
|
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: 126.32 E-value: 8.06e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2628 GEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVAL 2707
Cdd:cd17640 2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2708 IsqsahlgimngslpvillddgetrpFDNEPDTpldarkqgltprhLAYVIYTSGSTGKPKGVMVEHAN----MVNFLCS 2783
Cdd:cd17640 82 V-------------------------VENDSDD-------------LATIIYTSGTTGNPKGVMLTHANllhqIRSLSDI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2784 MRKEPGiaqedvllgvtslsfDISILeiFLPLLNGA-RL----ILATQAQAADAQQLAML--IERHAVSFMQATPSTWRM 2856
Cdd:cd17640 124 VPPQPG---------------DRFLS--ILPIWHSYeRSaeyfIFACGCSQAYTSIRTLKddLKRVKPHYIVSVPRLWES 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2857 LVE---------------LRDFALPPG-FK-ALCGGEALPENLATALLQKVTTLWNLYGPTETTIWSTLNGLTTPT-PYI 2918
Cdd:cd17640 187 LYSgiqkqvsksspikqfLFLFFLSGGiFKfGISGGGALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVrGSV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2919 GHPIANTQIYILDAQGRVV-PLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEY 2997
Cdd:cd17640 267 GRPLPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW--------FNTGDLGWLTCGGELVL 338
|
410 420 430
....*....|....*....|....*....|....*..
gi 641744967 2998 LGR-NDFQVKVRGFRIELGEIETRLARCHGVHDAVVI 3033
Cdd:cd17640 339 TGRaKDTIVLSNGENVEPQPIEEALMRSPFIEQIMVV 375
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1664-2021 |
9.17e-30 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 130.43 E-value: 9.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1664 PGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPF--SFDVSVWEFFwPLLYGARLVmA 1741
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTVTLWL-PLLEGIKVV-Y 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1742 RPDGhKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADCAC-DSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPT 1820
Cdd:PRK08633 855 HPDP-TDALGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMfASLRLVVAGAEKLKPEVADAFEEKFGIRILEGYGAT 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1821 E----AAI------DVTFWAcQPDDHRSFVpiGRPIANTQLYILD-TLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAE 1889
Cdd:PRK08633 934 EtspvASVnlpdvlAADFKR-QTGSKEGSV--GMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1890 rFIPDPfinqPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQ--CPGVQEAVVVAREDSPGDTR 1967
Cdd:PRK08633 1011 -VIKDI----DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEKKGEK 1085
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 1968 LVAYLCPQPGvtpDPADLRQQLGQ-HLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK08633 1086 LVVLHTCGAE---DVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
2162-2500 |
1.01e-29 |
|
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: 125.17 E-value: 1.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2162 YPLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCWQDLsQPVQVVWRQAILPINH 2241
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEG-EPYQWIDPYTPVPIRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2242 FEPTSPEDVLAQLQAHTEPRTRR-IDLSQAPLFRADIAHDPlQNEWLLALSFHHLISDHMTLALIVGEIRLLLQHQADAL 2320
Cdd:cd19533 81 IDLSGDPDPEGAAQQWMQEDLRKpLPLDNDPLFRHALFTLG-DNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2321 PTP----LPYRNFIAQTLSVPNSAH----EAYFRDKLADVDEPTapfgLLNVQGSGG--DIHEARLVLDATLASAIRQQA 2390
Cdd:cd19533 160 PAPpapfGSFLDLVEEEQAYRQSERferdRAFWTEQFEDLPEPV----SLARRAPGRslAFLRRTAELPPELTRTLLEAA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2391 RHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRLAGAEgadRIM-GMFINTLPLRISLA-DRGAAEVVERTSHDLM 2468
Cdd:cd19533 236 EAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAA---RQTpGMVANTLPLRLTVDpQQTFAELVAQVSRELR 312
|
330 340 350
....*....|....*....|....*....|...
gi 641744967 2469 TLLEHEQAPLALAQRCSGVAPPM-PLFSTLLNY 2500
Cdd:cd19533 313 SLLRHQRYRYEDLRRDLGLTGELhPLFGPTVNY 345
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
496-966 |
1.18e-29 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 126.35 E-value: 1.18e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 496 DQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALL 575
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 576 TQSAQVAQLNSTLP---TVL-LDTPA--------AAACPDTNPVVQGLH---AAHLAY----------VIYTSGSTGRPK 630
Cdd:PRK12406 89 AHADLLHGLASALPagvTVLsVPTPPeiaaayriSPALLTPPAGAIDWEgwlAQQEPYdgppvpqpqsMIYTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 631 GV---------------MVAHrnVINLATGLHTLLA--LDH--PSRIALNASIVfdasvknwiqllsGHTLVLVPdalRA 691
Cdd:PRK12406 169 GVrraaptpeqaaaaeqMRAL--IYGLKPGIRALLTgpLYHsaPNAYGLRAGRL-------------GGVLVLQP---RF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 692 DAHQLWRYFARHAVDLFDCTPVQLQWLLDAglgsdpayqPAQV-----------LIGGEAISPA-VWSRLQSLSDTRFIN 759
Cdd:PRK12406 231 DPEELLQLIERHRITHMHMVPTMFIRLLKL---------PEEVrakydvsslrhVIHAAAPCPAdVKRAMIEWWGPVIYE 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 760 VYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVargylhrPDLTaerfipdpFS 839
Cdd:PRK12406 302 YYGSTESGAVTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGN-------PDFT--------YH 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 840 ADPAARiyKTGDLARWLPDGNIDYLG----------RNDFQIKvRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTR 909
Cdd:PRK12406 367 NKPEKR--AEIDRGGFITSGDVGYLDadgylflcdrKRDMVIS-GGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEA 443
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 910 LVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAP 966
Cdd:PRK12406 444 LMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
2754-3097 |
1.21e-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: 122.44 E-value: 1.21e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2754 LAYVIYTSGSTGKPKGVMVEHANMV-NFLCSMRKEPGIAQEDVLLgvtSL-SFDISILEI-FLPLLNGARLILATQAQAA 2830
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLaSAAGLHSRLGFGGGDSWLL---SLpLYHVGGLAIlVRSLLAGAELVLLERNQAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2831 DAQqlamlIERHAVSFMQATPST-WRMLVELRDFALPPGFKA-LCGGEALPENLATALLQKVTTLWNLYGPTETTiwSTL 2908
Cdd:cd17630 79 AED-----LAPPGVTHVSLVPTQlQRLLDSGQGPAALKSLRAvLLGGAPIPPELLERAADRGIPLYTTYGMTETA--SQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2909 NGLTTPTP---YIGHPIANTQIYILDAqgrvvplgvaGEIHIAGAGVVRGYLGRPdltaerfITDPFsgaPEARMYKTGD 2985
Cdd:cd17630 152 ATKRPDGFgrgGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ-------LVPEF---NEDGWFTTKD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2986 LGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAylLAQPDTVLEPADLRQRL 3065
Cdd:cd17630 212 LGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVA--VIVGRGPADPAELRAWL 289
|
330 340 350
....*....|....*....|....*....|..
gi 641744967 3066 SEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd17630 290 KDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
1069-1481 |
1.34e-29 |
|
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: 124.73 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1069 PLSFSQQRLWFLAQLDPAaSQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSID-GQPAQQIDPD------T 1141
Cdd:cd19547 3 PLAPMQEGMLFRGLFWPD-SDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDlappwaL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1142 LGFSLSSHDlrkldeaarttRVAELAEQ----EARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARE 1217
Cdd:cd19547 82 LDWSGEDPD-----------RRAELLERlladDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1218 LAALYQAALEGSEANLPPLPvQYADYAVWQR-QWLQGEtlnDLRDYWRDQLQG-APA-LLEIPTDRprpsvqryAGD-QV 1293
Cdd:cd19547 151 VFRVYEELAHGREPQLSPCR-PYRDYVRWIRaRTAQSE---ESERFWREYLRDlTPSpFSTAPADR--------EGEfDT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1294 PFHLDAGQLRRLHA-LNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVANRPrQELEG---MVGFFVNTLALRTEPG 1369
Cdd:cd19547 219 VVHEFPEQLTRLVNeAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRP-PELEGsehMVGIFINTIPLRIRLD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1370 RCHAVADLLDQVRERALDAYAHQALPFEQVVEILQPARsLSYSPIFQVMLSLNNTPAQALTLPDLTLSAVE-RPQHSTHF 1448
Cdd:cd19547 298 PDQTVTGLLETIHRDLATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQIIDlHAQEKTEY 376
|
410 420 430
....*....|....*....|....*....|...
gi 641744967 1449 DLSLSLIETENgLNGGLVYATDLFDRETILRVV 1481
Cdd:cd19547 377 PIGLIVLPLQK-LAFHFNYDTTHFTRAQVDRFI 408
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1670-2018 |
2.66e-29 |
|
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: 121.36 E-value: 2.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1670 HLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMarpDGHKDA 1749
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIG---QRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1750 AYLAQLIERTGITTLHFVPSMLQQFVQwadADCACDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIdVTF 1828
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALAR---TLEPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSF-ITY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1829 WAcqPDDHRSFVPIGRPIANTQLYILDTLGqpvplGVAGELHIGGVGVARGYLNRPDLTAERFipdpfinqpgarlYKTG 1908
Cdd:cd17633 154 NF--NQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-------------MSVG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1909 DLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLcpqPGVTPDPADLRQQ 1988
Cdd:cd17633 214 DIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALY---SGDKLTYKQLKRF 290
|
330 340 350
....*....|....*....|....*....|
gi 641744967 1989 LGQHLAEYMVPGAFVTLDAFPLTPNGKLDR 2018
Cdd:cd17633 291 LKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
2622-3097 |
8.17e-29 |
|
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: 122.59 E-value: 8.17e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2622 AIAVVFGEASLSYDELNRRANRLAHHLIS-FGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLD 2700
Cdd:cd05958 1 RTCLRSPEREWTYRDLLALANRIANVLVGeLGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2701 DAKPValisqsahlgimngslpVILLDDGETRPFDnepdtpldarkqgltprhLAYVIYTSGSTGKPKGVMVEHANMV-N 2779
Cdd:cd05958 81 KARIT-----------------VALCAHALTASDD------------------ICILAFTSGTTGAPKATMHFHRDPLaS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2780 FLCSMRKEPGIAQEDVLLGVTSLSFDISI-LEIFLPLLNGARLILATQAQAADAQQlamLIERHAVSFMQATPSTWRMLV 2858
Cdd:cd05958 126 ADRYAVNVLRLREDDRFVGSPPLAFTFGLgGVLLFPFGVGASGVLLEEATPDLLLS---AIARYKPTVLFTAPTAYRAML 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2859 ELRDFA---LPPGFKALCGGEALPENLATALLQKV-TTLWNLYGPTET--TIWSTLNGLTTPTPyIGHPIANTQIYILDA 2932
Cdd:cd05958 203 AHPDAAgpdLSSLRKCVSAGEALPAALHRAWKEATgIPIIDGIGSTEMfhIFISARPGDARPGA-TGKPVPGYEAKVVDD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2933 QGRVVPlgvAGEIhiaGAGVVRGylgrPdlTAERFITDPfsgapEARMY------KTGDLGRWLPDGTLEYLGRNDFQVK 3006
Cdd:cd05958 282 EGNPVP---DGTI---GRLAVRG----P--TGCRYLADK-----RQRTYvqggwnITGDTYSRDPDGYFRHQGRSDDMIV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3007 VRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPA---DLRQRLSEGVAEYMIPSAFVTLDA 3083
Cdd:cd05958 345 SGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRPGVIPGPVlarELQDHAKAHIAPYKYPRAIEFVTE 424
|
490
....*....|....
gi 641744967 3084 FPLTPNGKLDRKAL 3097
Cdd:cd05958 425 LPRTATGKLQRFAL 438
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
496-963 |
8.96e-29 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 124.36 E-value: 8.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 496 DQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALL 575
Cdd:PRK07059 46 GKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQLKDSGAEAIV 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 576 TqsaqVAQLNSTLPTVLLDTPA----AAACPD--------TNPVV---------------------------QGLHAAHL 616
Cdd:PRK07059 126 V----LENFATTVQQVLAKTAVkhvvVASMGDllgfkghiVNFVVrrvkkmvpawslpghvrfndalaegarQTFKPVKL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 617 -----AYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLL--ALDHPSRI-------ALNASIVFDASVKNWIQLLSGHTL 682
Cdd:PRK07059 202 gpddvAFLQYTGGTTGVSKGATLLHRNIVANVLQMEAWLqpAFEKKPRPdqlnfvcALPLYHIFALTVCGLLGMRTGGRN 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 683 VLVPDALraDAHQLWRYFARHAVDLFdctPVqLQWLLDAgLGSDPAYQP---AQVLI---GGEAISPAVWSRLQSLSDTR 756
Cdd:PRK07059 282 ILIPNPR--DIPGFIKELKKYQVHIF---PA-VNTLYNA-LLNNPDFDKldfSKLIVangGGMAVQRPVAERWLEMTGCP 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 757 FINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPD 836
Cdd:PRK07059 355 ITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTAD 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 837 PFsadpaariYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDS-PGDTrlVAYLC 915
Cdd:PRK07059 435 GF--------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEhSGEA--VKLFV 504
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 641744967 916 ARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK07059 505 VKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1543-2023 |
1.03e-28 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 124.62 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1543 DTTAVLFEDQH----LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLA 1618
Cdd:PRK04319 59 DKVALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1619 YMLDDASPVALLTQAN-------------QRALLTGDVPRILLDTADFSHLSE---DNPHVPGLDAHHLAYVIYTSGSTG 1682
Cdd:PRK04319 139 DRLEDSEAKVLITTPAllerkpaddlpslKHVLLVGEDVEEGPGTLDFNALMEqasDEFDIEWTDREDGAILHYTSGSTG 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1683 KPKGVMNSHRALCNRLV---WMQNtyrLTPDDR---------VlqkTPFSFDVsvwefFWPLLYGARLVMARPDGHKDAA 1750
Cdd:PRK04319 219 KPKGVLHVHNAMLQHYQtgkYVLD---LHEDDVywctadpgwV---TGTSYGI-----FAPWLNGATNVIDGGRFSPERW 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1751 YlaQLIERTGITTLHFVPS---MLQQfvqwADADCA----CDSLRRVICSGEALPAE--------LQQRFfarfnaqlHN 1815
Cdd:PRK04319 288 Y--RILEDYKVTVWYTAPTairMLMG----AGDDLVkkydLSSLRHILSVGEPLNPEvvrwgmkvFGLPI--------HD 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1816 LYGPTE-AAIDVTFWACQPDDHRSfvpIGRPIANTQLYILDTLGQPVPLGVAGELHI--GGVGVARGYLNRPDLTAERFI 1892
Cdd:PRK04319 354 NWWMTEtGGIMIANYPAMDIKPGS---MGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFA 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1893 PDpfinqpgarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYL 1972
Cdd:PRK04319 431 GD---------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFV 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 1973 CPQPGVTPDPAdLRQQLGQH----LAEYMVPGAFVTLDAFPLTPNGKLDRKALPA 2023
Cdd:PRK04319 502 ALRPGYEPSEE-LKEEIRGFvkkgLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
621-960 |
1.08e-28 |
|
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: 120.46 E-value: 1.08e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 621 YTSGSTGRPKGVMVAHRNVINLA--TGLHTLLALDHpsRIALNASI--VFDASVKNWIQLLSGHTLVLVPDALRADAhql 696
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGyfIGERLGLTEQD--RLCIPVPLfhCFGSVLGVLACLTHGATMVFPSPSFDPLA--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 697 wryfARHAVDLFDCT-----PVQLQWLLDagLGSDPAYQPAQV---LIGGEAISPAVWSRLQS-LSDTRFINVYGPTECT 767
Cdd:cd05917 84 ----VLEAIEKEKCTalhgvPTMFIAELE--HPDFDKFDLSSLrtgIMAGAPCPPELMKRVIEvMNMKDVTIAYGMTETS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 768 VDATACVVDRTQP--LPTIGKPLANTRLYILDAQDQPVP-IGVTGELHIGGAGVARGYLHRPDLTAERFIPDpfsadpaa 844
Cdd:cd05917 158 PVSTQTRTDDSIEkrVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 845 RIYKTGDLARWLPDGNIDYLGRndfqIK---VRGFR-IEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDA 920
Cdd:cd05917 230 GWLHTGDLAVMDEDGYCRIVGR----IKdmiIRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGA 305
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 641744967 921 ELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDR 960
Cdd:cd05917 306 ELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
64-405 |
1.78e-28 |
|
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: 121.41 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 64 RLDAFLDVLQQVIARHDILRTAICWQ-GLHQPVQVVWRQAPLTVNTLTTTSSDTVPAQLRAAtdpSNHRLNLSNAPLLSA 142
Cdd:cd19532 37 DVARLERAVRAVGQRHEALRTCFFTDpEDGEPMQGVLASSPLRLEHVQISDEAEVEEEFERL---KNHVYDLESGETMRI 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 143 TtahdpvcgewLLSLS---------IHHLISDHITQALIIDEIRLLLEDRPEaLPKPLPYRNFIAQ----ILSVPLSEHE 209
Cdd:cd19532 114 V----------LLSLSptehylifgYHHIAMDGVSFQIFLRDLERAYNGQPL-LPPPLQYLDFAARqrqdYESGALDEDL 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 210 QYFRNRLADIDTPTAPFDLVDVQG----NGEDITEARLSLDSSLADALRRQARHLGISSsvlFHV---AWAQVLALTSGR 282
Cdd:cd19532 183 AYWKSEFSTLPEPLPLLPFAKVKSrpplTRYDTHTAERRLDAALAARIKEASRKLRVTP---FHFylaALQVLLARLLDV 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 283 DDVVFGSVLSGRlqGNLGADRVMGMFINTLPLRVSL-RERSVHDVVQATSHELMMLLAHEQAPL-ALAQQCsQVP---PP 357
Cdd:cd19532 260 DDICIGIADANR--TDEDFMETIGFFLNLLPLRFRRdPSQTFADVLKETRDKAYAALAHSRVPFdVLLDEL-GVPrsaTH 336
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 641744967 358 LPLFSTLFNYRhsQKDASSQFWEGMrQLSGRE----RTNYPITLSVDDLGDG 405
Cdd:cd19532 337 SPLFQVFINYR--QGVAESRPFGDC-ELEGEEfedaRTPYDLSLDIIDNPDG 385
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1521-2021 |
2.01e-28 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 124.30 E-value: 2.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1521 EADFPHDalIHQLVEDQAARTPDTTAVLF--------EDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMV 1592
Cdd:PRK07529 20 ARDLPAS--TYELLSRAAARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETH 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1593 IGLLAILKAGAAyVPLDPGYPAERLAYMLDDASPVALLTQA-------------------NQRALLTGDVPRILLDTADF 1653
Cdd:PRK07529 98 FALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAKVLVTLGpfpgtdiwqkvaevlaalpELRTVVEVDLARYLPGPKRL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1654 S-HLSEDNPHVPGLD--------------------AHHLAYVIYTSGSTGKPKGVMNSHRALCNRlVWMQNTY-RLTPDD 1711
Cdd:PRK07529 177 AvPLIRRKAHARILDfdaelarqpgdrlfsgrpigPDDVAAYFHTGGTTGMPKLAQHTHGNEVAN-AWLGALLlGLGPGD 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1712 RVLQKTP-FSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLA---QLIERTGITTLHFVPSMLQQFVQWADADCACDSL 1787
Cdd:PRK07529 256 TVFCGLPlFHVNALLVTGLAPLARGAHVVLATPQGYRGPGVIAnfwKIVERYRINFLSGVPTVYAALLQVPVDGHDISSL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1788 RRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVtfwACQP-DDHRSFVPIGRPIANTQLYI--LDTLG---QPV 1861
Cdd:PRK07529 336 RYALCGAAPLPVEVFRRFEAATGVRIVEGYGLTEATCVS---SVNPpDGERRIGSVGLRLPYQRVRVviLDDAGrylRDC 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1862 PLGVAGELHIGGVGVARGYLNrPDLTAERFIPDPFINqpgarlykTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEI 1941
Cdd:PRK07529 413 AVDEVGVLCIAGPNVFSGYLE-AAHNKGLWLEDGWLN--------TGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAI 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1942 EARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAE-YMVPGAFVTLDAFPLTPNGKLDRKA 2020
Cdd:PRK07529 484 EEALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPA 563
|
.
gi 641744967 2021 L 2021
Cdd:PRK07529 564 L 564
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
483-963 |
2.23e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 122.84 E-value: 2.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERL 562
Cdd:PRK07470 17 ARRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 563 AYILDDAAPVALLTQSA---QVAQLNSTLPTVLLDTPAAAAcpDTNPVVQGLHAAHL--------------AYVIYTSGS 625
Cdd:PRK07470 97 AYLAEASGARAMICHADfpeHAAAVRAASPDLTHVVAIGGA--RAGLDYEALVARHLgarvanaavdhddpCWFFFTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 626 TGRPKGVMVAHRNVINLATGlHtlLALDHPSRIALNASIVF-----DASVKNWIQLLSGHTLVLVPdALRADAHQLWRYF 700
Cdd:PRK07470 175 TGRPKAAVLTHGQMAFVITN-H--LADLMPGTTEQDASLVVaplshGAGIHQLCQVARGAATVLLP-SERFDPAEVWALV 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 701 ARHAVDLFDCTPVQLQWLLDaglgsDPAYQPAQ------VLIGGEAISPAVWSR-LQSLSDTrFINVYGPTECTVDATAC 773
Cdd:PRK07470 251 ERHRVTNLFTVPTILKMLVE-----HPAVDRYDhsslryVIYAGAPMYRADQKRaLAKLGKV-LVQYFGLGEVTGNITVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 774 ------VVDRTQP-LPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaari 846
Cdd:PRK07470 325 ppalhdAEDGPDArIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-------- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 847 yKTGDLARWLPDGNIDYLGR-NDFQIKvRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPA 925
Cdd:PRK07470 397 -RTGDLGHLDARGFLYITGRaSDMYIS-GGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDEA 474
|
490 500 510
....*....|....*....|....*....|....*...
gi 641744967 926 ALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK07470 475 ELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
2622-3092 |
2.38e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 122.32 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2622 AIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDD 2701
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2702 AKPVALISQSAHL-------GIMNGSLPVILLDDGETRPF-------DNEPDTPLDARKQGltprhlAYVIYTSGSTGKP 2767
Cdd:PRK08276 82 SGAKVLIVSAALAdtaaelaAELPAGVPLLLVVAGPVPGFrsyeealAAQPDTPIADETAG------ADMLYSSGTTGRP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2768 KGVmvehanmvnflcsMRKEPGIAQEDVLLG-VTSLSFDISILE--IFL---PLLNGARLILATQAQAADAQQLAM---- 2837
Cdd:PRK08276 156 KGI-------------KRPLPGLDPDEAPGMmLALLGFGMYGGPdsVYLspaPLYHTAPLRFGMSALALGGTVVVMekfd 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2838 ------LIERHAVSFMQATPSTW-RMLvelrdfALPPGFK----------ALCGGEALPENLATALLQkvttlWnlYGPT 2900
Cdd:PRK08276 223 aeealaLIERYRVTHSQLVPTMFvRML------KLPEEVRarydvsslrvAIHAAAPCPVEVKRAMID-----W--WGPI 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2901 --ETTIWSTLNGLTTPTP--YIGHP-----IANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFItdp 2971
Cdd:PRK08276 290 ihEYYASSEGGGVTVITSedWLAHPgsvgkAVLGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN--- 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2972 fsgapEARMYKTGDLGrWL-PDGTLeYL-GRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAyll 3049
Cdd:PRK08276 367 -----PHGWVTVGDVG-YLdEDGYL-YLtDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKA--- 436
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 3050 aqpdtVLEPAD---------------LRQRLsegvAEYMIPSAFVTLDAFPLTPNGKL 3092
Cdd:PRK08276 437 -----VVQPADgadagdalaaeliawLRGRL----AHYKCPRSIDFEDELPRTPTGKL 485
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
2619-3092 |
2.41e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 122.73 E-value: 2.41e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2619 TPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYM 2698
Cdd:PRK08316 24 YPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2699 LDDAKPVALISQSAHLGI------MNGSLPVILLD-------DGETRPFD----NEPDTPLDARkqgLTPRHLAYVIYTS 2761
Cdd:PRK08316 104 LDHSGARAFLVDPALAPTaeaalaLLPVDTLILSLvlggreaPGGWLDFAdwaeAGSVAEPDVE---LADDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2762 GSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLsFDISILEIFL-P-LLNGARLILATQAQAADAQQlamLI 2839
Cdd:PRK08316 181 GTESLPKGAMLTHRALIAEYVSCIVAGDMSADDIPLHALPL-YHCAQLDVFLgPyLYVGATNVILDAPDPELILR---TI 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2840 ERHAVSFMQATPSTWRMLVELRDFA---LPPGFKALCGGEALPENLATALLQKVTTL--WNLYGPTETTIWSTLNG---- 2910
Cdd:PRK08316 257 EAERITSFFAPPTVWISLLRHPDFDtrdLSSLRKGYYGASIMPVEVLKELRERLPGLrfYNCYGQTEIAPLATVLGpeeh 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2911 LTTPTPyIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmyKTGDLGRWL 2990
Cdd:PRK08316 337 LRRPGS-AGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF---------HSGDLGVMD 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2991 PDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADL----RQRLs 3066
Cdd:PRK08316 407 EEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDELiahcRARL- 485
|
490 500
....*....|....*....|....*.
gi 641744967 3067 egvAEYMIPSAFVTLDAFPLTPNGKL 3092
Cdd:PRK08316 486 ---AGFKVPKRVIFVDELPRNPSGKI 508
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
494-921 |
3.45e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 121.40 E-value: 3.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 494 FEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVA 573
Cdd:cd05914 3 YGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 574 LLTqsaqvaqlnstlptvlldtpaaaacpdTNPvvqglhaAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALD 653
Cdd:cd05914 83 IFV---------------------------SDE-------DDVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLG 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 654 HPSRIA--LNASIVFDASVKNWIQLLSGHTLVLV--PDALRADAHQlwryFARHAVDLFDCTPVQLQ------------- 716
Cdd:cd05914 129 KGDKILsiLPLHHIYPLTFTLLLPLLNGAHVVFLdkIPSAKIIALA----FAQVTPTLGVPVPLVIEkifkmdiipkltl 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 717 ----WLLDAGLGSDPAYQPA-------------QVLIGGEAISPAVWSRLQSLSDTrFINVYGPTECTVDATACVVDRTQ 779
Cdd:cd05914 205 kkfkFKLAKKINNRKIRKLAfkkvheafggnikEFVIGGAKINPDVEEFLRTIGFP-YTIGYGMTETAPIISYSPPNRIR 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 780 pLPTIGKPLANTRLYIldaqDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDG 859
Cdd:cd05914 284 -LGSAGKVIDGVEVRI----DSPDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW--------FHTGDLGKIDAEG 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 860 NIDYLGR-NDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDspgdtRLVAYLCARPDAE 921
Cdd:cd05914 351 YLYIRGRkKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEK-----KLVALAYIDPDFL 408
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
2620-3097 |
3.84e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 122.07 E-value: 3.84e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:PRK07470 21 PDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALISQSA---HLGIMNGSLP----VILLDDGE-TRPFDNEPDTPLDARKQGLTPRH--LAYVIYTSGSTGKPKG 2769
Cdd:PRK07470 101 EASGARAMICHADfpeHAAAVRAASPdlthVVAIGGARaGLDYEALVARHLGARVANAAVDHddPCWFFFTSGTTGRPKA 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2770 VMVEHANM----VNFLCSMRkePGIAQEDVLLGVTSLSFDISILEIfLPLLNGARLILATQAQAADAQQLAmLIERHAVS 2845
Cdd:PRK07470 181 AVLTHGQMafviTNHLADLM--PGTTEQDASLVVAPLSHGAGIHQL-CQVARGAATVLLPSERFDPAEVWA-LVERHRVT 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2846 FMQATPSTWRMLVE-----------LRD--FALPPGFKAlcggealPENLATALLQKVttLWNLYGPTETTiwstlNGLT 2912
Cdd:PRK07470 257 NLFTVPTILKMLVEhpavdrydhssLRYviYAGAPMYRA-------DQKRALAKLGKV--LVQYFGLGEVT-----GNIT 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2913 TPTPYI--------------GHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapea 2978
Cdd:PRK07470 323 VLPPALhdaedgpdarigtcGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF------ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2979 rmyKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEP 3058
Cdd:PRK07470 397 ---RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARDGAPVDE 473
|
490 500 510
....*....|....*....|....*....|....*....
gi 641744967 3059 ADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK07470 474 AELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMV 512
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
2747-3097 |
8.31e-28 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 124.27 E-value: 8.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2747 QGLTPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSL--SFDISIlEIFLPLLNGARLILA 2824
Cdd:PRK08633 777 PTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTV-TLWLPLLEGIKVVYH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2825 TQAQAADAQQLamLIERHAVSFMQATPSTWRMLveLRDF-ALPPGFKAL----CGGEALPENLATALLQKV-TTLWNLYG 2898
Cdd:PRK08633 856 PDPTDALGIAK--LVAKHRATILLGTPTFLRLY--LRNKkLHPLMFASLrlvvAGAEKLKPEVADAFEEKFgIRILEGYG 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2899 PTETTIWSTLN------GLTTPTPY-----IGHPIANTQIYILDAQ-GRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAEr 2966
Cdd:PRK08633 932 ATETSPVASVNlpdvlaADFKRQTGskegsVGMPLPGVAVRIVDPEtFEELPPGEDGLILIGGPQVMKGYLGDPEKTAE- 1010
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2967 FITDpfsgAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGvHDAVVIAREDSPGDKR--L 3044
Cdd:PRK08633 1011 VIKD----IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKALG-GEEVVFAVTAVPDEKKgeK 1085
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 641744967 3045 VAYLLAQPDTvlEPADLRQRLSE-GVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK08633 1086 LVVLHTCGAE--DVEELKRAIKEsGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
1088-1399 |
9.52e-28 |
|
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: 118.55 E-value: 9.52e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1088 SQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDTLGFSLSSHDLrkLDEAarttrvaeLA 1167
Cdd:cd19545 19 PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESPISWTESTS--LDEY--------LE 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1168 EQEARaRFDLTQgPLIRGQLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQaaleGSEanlPPLPVQYADYAvwq 1247
Cdd:cd19545 89 EDRAA-PMGLGG-PLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQ----GEP---VPQPPPFSRFV--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1248 rQWLQGETLNDLRDYWRDQLQGAPALL--EIPTDRPRPSVQRYAgdqvpfhldagQLRRLHALNRQQGTTLFMTLLAAWS 1325
Cdd:cd19545 157 -KYLRQLDDEAAAEFWRSYLAGLDPAVfpPLPSSRYQPRPDATL-----------EHSISLPSSASSGVTLATVLRAAWA 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 1326 VVLSRLSGQDDIVIGTPVANR--PRQELEGMVGFFVNTLALRTepgRCHA---VADLLDQVRERALDayahqALPFEQV 1399
Cdd:cd19545 225 LVLSRYTGSDDVVFGVTLSGRnaPVPGIEQIVGPTIATVPLRV---RIDPeqsVEDFLQTVQKDLLD-----MIPFEHT 295
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
1531-2128 |
1.16e-27 |
|
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: 123.27 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1531 HQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDP 1610
Cdd:COG3319 4 AAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1611 GYPAERLAYMLDDASPVALLTQANQRALLTGDVPRILLDTADFSHLSEDNPHVPGLDAHH----LAYVIYTSGSTGKPKG 1686
Cdd:COG3319 84 LALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAaaaaLAAAAGLGGGGGGAGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1687 VMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDGHKDAAYLAQLIERTGITTLHF 1766
Cdd:COG3319 164 LVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1767 VPSMLQQFVQWADADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTFWACQPDDHRSfVPIGRPI 1846
Cdd:COG3319 244 LAALLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGAL-GPIGGGP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1847 ANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFINQPGARLYKTGDLARWLPDGSLEYLGRND 1926
Cdd:COG3319 323 GLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLR 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1927 FQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLcPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLD 2006
Cdd:COG3319 403 LQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAV-VAAAALAAAALLLLLLLLLLPPPLPPALLLLLL 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2007 AFPLTPNGKLDRKALPAPDqsAVATRDYEAPQGEVETALAAVWQDLLGLTRVGRHDHFFALGGHSLLIVSLIERLRRAGL 2086
Cdd:COG3319 482 LLLLLLLAALLLAAAAPAA--AAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLL 559
|
570 580 590 600
....*....|....*....|....*....|....*....|..
gi 641744967 2087 ALDVRGVFSTPVLSDMAQAILAHQDKPAVVVPPNRIPADSTA 2128
Cdd:COG3319 560 RLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPLRAGGSG 601
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
2608-3094 |
1.41e-27 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 121.03 E-value: 1.41e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2608 IHELFEAQVACTPDAIAVVFGEASL--SYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVP 2685
Cdd:PRK12583 20 IGDAFDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2686 LDPTYPVERLRYMLDDAKPVALIS-----QSAHLGIMNGSLP--------------------VILLDDGETRPFDNEPD- 2739
Cdd:PRK12583 100 INPAYRASELEYALGQSGVRWVICadafkTSDYHAMLQELLPglaegqpgalacerlpelrgVVSLAPAPPPGFLAWHEl 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2740 ---------TPLDARKQGLTPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSL--SFDIsI 2808
Cdd:PRK12583 180 qargetvsrEALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhCFGM-V 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2809 LEIFLPLLNGARLILATQAQAADAQQLAmlIERHAVSFMQATPSTWRMLVELRDF------ALPPGFKAlcGGEALPEnl 2882
Cdd:PRK12583 259 LANLGCMTVGACLVYPNEAFDPLATLQA--VEEERCTALYGVPTMFIAELDHPQRgnfdlsSLRTGIMA--GAPCPIE-- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2883 ataLLQKVTTLWNL------YGPTETTIWSTLNGLTTPTPY----IGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGV 2952
Cdd:PRK12583 333 ---VMRRVMDEMHMaevqiaYGMTETSPVSLQTTAADDLERrvetVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2953 VRGYLGRPDLTAERFITDPFsgapearMYkTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVV 3032
Cdd:PRK12583 410 MKGYWNNPEATAESIDEDGW-------MH-TGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVADVQV 481
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641744967 3033 IAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDR 3094
Cdd:PRK12583 482 FGVPDEKYGEEIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1674-2018 |
1.57e-27 |
|
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: 116.60 E-value: 1.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1674 VIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFsFDVSVWEFFWPLLY--GARLVMARpdghKDAAY 1751
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLNMLPL-FHIAGLNLALATFHagGANVVMEK----FDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1752 LAQLIERTGITTLHFVPSMLQQFVQWADADCA-CDSLRRVicSGEALPaELQQRFFARFNAQLHNLYGPTEAAIDVTFwa 1830
Cdd:cd17637 80 ALELIEEEKVTLMGSFPPILSNLLDAAEKSGVdLSSLRHV--LGLDAP-ETIQRFEETTGATFWSLYGQTETSGLVTL-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1831 cQPDDHRSfVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFipdpfinqpgaR--LYKTG 1908
Cdd:cd17637 155 -SPYRERP-GSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-----------RngWHHTG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1909 DLARWLPDGSLEYLGRNDFQ--VKLRGFRIELGEIEARLMQCPGVQEAVVVAREDsPGDTRLVAYLCP-QPGVTPDPADL 1985
Cdd:cd17637 222 DLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPD-PKWGEGIKAVCVlKPGATLTADEL 300
|
330 340 350
....*....|....*....|....*....|...
gi 641744967 1986 RQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDR 2018
Cdd:cd17637 301 IEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1538-2021 |
2.08e-27 |
|
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: 119.02 E-value: 2.08e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICverSLDMVIGLLAILKAGAAYVPldpgyPAERL 1617
Cdd:cd05929 2 EARDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIY---LINSILTVFAAAAAWKCGAC-----PAYKS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1618 AYMLDDASPVALLTQANQRALLTGDVPRILLDTADFSHLSEDNPHVPGLDAHHLAYVIYTSGSTGKPKGVM--------- 1688
Cdd:cd05929 74 SRAPRAEACAIIEIKAAALVCGLFTGGGALDGLEDYEAAEGGSPETPIEDEAAGWKMLYSGGTTGRPKGIKrglpggppd 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1689 NSHRALCNRLVWMqntyrlTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARpdgHKDAAYLAQLIERTGITTLHFVP 1768
Cdd:cd05929 154 NDTLMAAALGFGP------GADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLME---KFDPEEFLRLIERYRVTFAQFVP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1769 SMLQQFVQWADA-----DCAcdSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEA----AIDVTFWACQPDDhrsf 1839
Cdd:cd05929 225 TMFVRLLKLPEAvrnayDLS--SLKRVIHAAAPCPPWVKEQWIDWGGPIIWEYYGGTEGqgltIINGEEWLTHPGS---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1840 vpIGRPIANtQLYILDTLGQPVPLGVAGELHIGGvGVARGYLNRPDLTAERfipdpfINQPGARlyKTGDLARWLPDGSL 1919
Cdd:cd05929 299 --VGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTNDPEKTAAA------RNEGGWS--TLGDVGYLDEDGYL 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1920 EYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPA---DLRQQLGQHLAEY 1996
Cdd:cd05929 367 YLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTAlaeELIAFLRDRLSRY 446
|
490 500
....*....|....*....|....*
gi 641744967 1997 MVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05929 447 KCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
483-963 |
2.31e-27 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 118.82 E-value: 2.31e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERL 562
Cdd:PRK09029 13 AQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 563 AYILDDAAPVALLTQSAQVAQLNSTLPTVLLDTPAAAACPDtnpvvqglhAAHLAYVIYTSGSTGRPKGVMVAHRNVINL 642
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQ---------PQRLATMTLTSGSTGLPKAAVHTAQAHLAS 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 643 ATGLHTL------------LALDHPSRIAlnasIVfdasvknWIQLLSGHTLVLvpdalrADAHQLWRyfarhavDLFDC 710
Cdd:PRK09029 164 AEGVLSLmpftaqdswllsLPLFHVSGQG----IV-------WRWLYAGATLVV------RDKQPLEQ-------ALAGC 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 711 T-----PVQLQWLLDaglgsDPAYQPA--QVLIGGEAISPAVWSRLQSLSDTRFINvYGPTEctVDATACVVdRTQPLPT 783
Cdd:PRK09029 220 ThaslvPTQLWRLLD-----NRSEPLSlkAVLLGGAAIPVELTEQAEQQGIRCWCG-YGLTE--MASTVCAK-RADGLAG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 784 IGKPLANTRLYIldaqdqpvpigVTGELHIGGAGVARGYLHRPDLTaerfipdPFSADPAAriYKTGDLARWLpDGNIDY 863
Cdd:PRK09029 291 VGSPLPGREVKL-----------VDGEIWLRGASLALGYWRQGQLV-------PLVNDEGW--FATRDRGEWQ-NGELTI 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 864 LGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLcaRPDAELHPAALRQQLAASLADYMIPSA 943
Cdd:PRK09029 350 LGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV--ESDSEAAVVNLAEWLQDKLARFQQPVA 427
|
490 500
....*....|....*....|
gi 641744967 944 FVTLDALPLTPNGKLDRKAL 963
Cdd:PRK09029 428 YYLLPPELKNGGIKISRQAL 447
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
490-965 |
4.21e-27 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 119.61 E-value: 4.21e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 490 IAVLFEDQH----LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYI 565
Cdd:PRK04319 61 VALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDR 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 566 LDDAAPVALLTQSAQ-----VAQLnSTLPTVLL------------DTPAAAACPDTNPVVQGLHAAHLAYVIYTSGSTGR 628
Cdd:PRK04319 141 LEDSEAKVLITTPALlerkpADDL-PSLKHVLLvgedveegpgtlDFNALMEQASDEFDIEWTDREDGAILHYTSGSTGK 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 629 PKGVMVAHRNVI-NLATGLHtllALD-HPSRI---ALNASIVFDASVKNWIQLLSGHTLVLvpDALRADAHQLWRYFARH 703
Cdd:PRK04319 220 PKGVLHVHNAMLqHYQTGKY---VLDlHEDDVywcTADPGWVTGTSYGIFAPWLNGATNVI--DGGRFSPERWYRILEDY 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 704 AVDLFDCTPVQLQWLLDAglGSDPAYQ---PA--QVLIGGEAISP-AVWSRLQSLsDTRFINVYGPTEctvdaTACVVDR 777
Cdd:PRK04319 295 KVTVWYTAPTAIRMLMGA--GDDLVKKydlSSlrHILSVGEPLNPeVVRWGMKVF-GLPIHDNWWMTE-----TGGIMIA 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 778 TQPLPTI-----GKPLANTRLYILDAQDQPVPIGVTGELHI--GGAGVARGYLHRPDLTAERFIPDpfsadpaarIYKTG 850
Cdd:PRK04319 367 NYPAMDIkpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAGD---------WYVSG 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 851 DLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAElhPA-ALRQ 929
Cdd:PRK04319 438 DSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGYE--PSeELKE 515
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 641744967 930 QLAA----SLADYMIPSAFVTLDALPLTPNGKLDRKALPA 965
Cdd:PRK04319 516 EIRGfvkkGLGAHAAPREIEFKDKLPKTRSGKIMRRVLKA 555
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
473-963 |
5.11e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 118.34 E-value: 5.11e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 473 MLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDdRVALCVERSLEMMVGLLGILKAGAAYVP 552
Cdd:PRK07638 1 MGITKEYKKHASLQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNK-TIAILLENRIEFLQLFAGAAMAGWTCVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 553 MDPAYPAERLAYILDDAAPVALLTQSAQVAQL-NSTLPTVLLDT---PAAAACPDTNPVVQGLHAAHlaYVIYTSGSTGR 628
Cdd:PRK07638 80 LDIKWKQDELKERLAISNADMIVTERYKLNDLpDEEGRVIEIDEwkrMIEKYLPTYAPIENVQNAPF--YMGFTSGSTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 629 PKGVMVAHRnvinlaTGLHTllaldhpsrialnasivFDASVKNWiqLLSGHTLVLVPDALRadaHQLWRYFARHAvdLF 708
Cdd:PRK07638 158 PKAFLRAQQ------SWLHS-----------------FDCNVHDF--HMKREDSVLIAGTLV---HSLFLYGAIST--LY 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 709 DCTPVQLQwlldaglgsdPAYQPAQVL--IGGEAI----------------------------SPAVWS-----RLQSL- 752
Cdd:PRK07638 208 VGQTVHLM----------RKFIPNQVLdkLETENIsvmytvptmleslykenrvienkmkiisSGAKWEaeakeKIKNIf 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 753 SDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHrpdltaER 832
Cdd:PRK07638 278 PYAKLYEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYII------GG 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 833 FIPDPFSADPAARIYKTGDLARwlpDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVA 912
Cdd:PRK07638 352 VLARELNADGWMTVRDVGYEDE---EGFIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVA 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 641744967 913 YLCARPDAELHPAALRQQLAAsladYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK07638 429 IIKGSATKQQLKSFCLQRLSS----FKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
2631-3097 |
7.07e-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: 117.82 E-value: 7.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2631 SLSYDELNRRANRLAHhLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDA--KPV--- 2705
Cdd:cd05909 7 SLTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAgiKTVlts 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2706 -ALISQSAHLGIMNGSLP--VILLDD----------------GETRPfdnepdtPLDARKQGLTPRH---LAYVIYTSGS 2763
Cdd:cd05909 86 kQFIEKLKLHHLFDVEYDarIVYLEDlrakiskadkckaflaGKFPP-------KWLLRIFGVAPVQpddPAVILFTSGS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2764 TGKPKGVMVEHANMVNFL--CSMRKEPgiAQEDVLLGVTSL--SFDISIlEIFLPLLNGARLILATQAQAADAQQLamLI 2839
Cdd:cd05909 159 EGLPKGVVLSHKNLLANVeqITAIFDP--NPEDVVFGALPFfhSFGLTG-CLWLPLLSGIKVVFHPNPLDYKKIPE--LI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2840 ERHAVSFMQATPSTWRMLVElrdFALPPGFKAL----CGGEALPENLATALLQKV-TTLWNLYGPTETtiwSTLNGLTTP 2914
Cdd:cd05909 234 YDKKATILLGTPTFLRGYAR---AAHPEDFSSLrlvvAGAEKLKDTLRQEFQEKFgIRILEGYGTTEC---SPVISVNTP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2915 TP-----YIGHPIANTQIYILDAQGRV-VPLGVAGEIHIAGAGVVRGYLGRPDLTAErfitdpfsgAPEARMYKTGDLGR 2988
Cdd:cd05909 308 QSpnkegTVGRPLPGMEVKIVSVETHEeVPIGEGGLLLVRGPNVMLGYLNEPELTSF---------AFGDGWYDTGDIGK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2989 WLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLA---RCHGVHDAVVIAREdSPGDKRLVAYLlaqpDTVLEPADLRQRL 3065
Cdd:cd05909 379 IDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSeilPEDNEVAVVSVPDG-RKGEKIVLLTT----TTDTDPSSLNDIL 453
|
490 500 510
....*....|....*....|....*....|...
gi 641744967 3066 SE-GVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05909 454 KNaGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
29-440 |
7.14e-27 |
|
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: 116.74 E-value: 7.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 29 YPLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICwQGLHQPVQVVWRQapltvnt 108
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFC-EEAGRYEQVVLDK------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 109 ltTTSSDTVPAQLRAATDPSNHRLNLSNAPLLSAT-TAHDPVC---------GEWLLSLSIHHLISDHIT-QALIIDEIR 177
Cdd:cd19066 74 --TVRFRIEIIDLRNLADPEARLLELIDQIQQTIYdLERGPLVrvalfrladERDVLVVAIHHIIVDGGSfQILFEDISS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 178 L---LLEDRPEALPKPLPYRNFIAQILSVPLSEHEQ----YFRNRLADIdTPTAPF--DLVDVQGNGEDITEARLSLDSS 248
Cdd:cd19066 152 VydaAERQKPTLPPPVGSYADYAAWLEKQLESEAAQadlaYWTSYLHGL-PPPLPLpkAKRPSQVASYEVLTLEFFLRSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 249 LADALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLqgNLGADRVMGMFINTLPLRVSL-RERSVHDVV 327
Cdd:cd19066 231 ETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRP--DEAVEDTIGLFLNLLPLRIDTsPDATFPELL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 328 QATSHELMMLLAHEQAPLALAQQCSQVPPPL---PLFSTLFNYR--HSQKDASSQFWEGMRQLSGRERTNYPITLSV-DD 401
Cdd:cd19066 309 KRTKEQSREAIEHQRVPFIELVRHLGVVPEApkhPLFEPVFTFKnnQQQLGKTGGFIFTTPVYTSSEGTVFDLDLEAsED 388
|
410 420 430
....*....|....*....|....*....|....*....
gi 641744967 402 LGDGFNLTAKTVMGVDPERIVHYMLTAIENLVTSLEKTP 440
Cdd:cd19066 389 PDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
2608-3102 |
8.13e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 118.60 E-value: 8.13e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2608 IHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLD 2687
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2688 PTYPVERLRYMLDDAKPVALI------SQSAHLGIMNGSLPVILLDDGETRPFDNEPDTPLDARKQG------------- 2748
Cdd:PRK06710 106 PLYTERELEYQLHDSGAKVILcldlvfPRVTNVQSATKIEHVIVTRIADFLPFPKNLLYPFVQKKQSnlvvkvsesetih 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2749 ----------------LTPRH-LAYVIYTSGSTGKPKGVMVEHANMV-NFLCSMRKEPGIAQ-EDVLLGVTSLSFDISIL 2809
Cdd:PRK06710 186 lwnsvekevntgvevpCDPENdLALLQYTGGTTGFPKGVMLTHKNLVsNTLMGVQWLYNCKEgEEVVLGVLPFFHVYGMT 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2810 EIF-LPLLNGARLILATQAQAADAQQLamlIERHAVSFMQATPSTWRMLVE---LRDFALPPGFKALCGGEALPENLATA 2885
Cdd:PRK06710 266 AVMnLSIMQGYKMVLIPKFDMKMVFEA---IKKHKVTLFPGAPTIYIALLNsplLKEYDISSIRACISGSAPLPVEVQEK 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2886 LlQKVT--TLWNLYGPTETTIWSTLNGL---TTPTPyIGHPIANTQIYILDAQ-GRVVPLGVAGEIHIAGAGVVRGYLGR 2959
Cdd:PRK06710 343 F-ETVTggKLVEGYGLTESSPVTHSNFLwekRVPGS-IGVPWPDTEAMIMSLEtGEALPPGEIGEIVVKGPQIMKGYWNK 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2960 PDLTAErFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSP 3039
Cdd:PRK06710 421 PEETAA-VLQDGW--------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPY 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 3040 GDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAPDQ 3102
Cdd:PRK06710 492 RGETVKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEEK 554
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2630-3097 |
8.65e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 116.79 E-value: 8.65e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2630 ASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALIs 2709
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFI- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2710 qsahlGImngslpvillddgetrPFDNEPdtpldarkqgltprhlAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPG 2789
Cdd:cd05910 80 -----GI----------------PKADEP----------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2790 IAQEDVLLGVTSLsfdisiLEIFLPLLNGARLILATQAQAADAQQLAML---IERHAVSFMQATPSTWRMLV---ELRDF 2863
Cdd:cd05910 123 IRPGEVDLATFPL------FALFGPALGLTSVIPDMDPTRPARADPQKLvgaIRQYGVSIVFGSPALLERVArycAQHGI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2864 ALPPGFKALCGGEALPENLATAL---LQKVTTLWNLYGPTETTIWSTLNG---LTTPTPY--------IGHPIANTQIYI 2929
Cdd:cd05910 197 TLPSLRRVLSAGAPVPIALAARLrkmLSDEAEILTPYGATEALPVSSIGSrelLATTTAAtsggagtcVGRPIPGVRVRI 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2930 LDA---------QGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSGApearMYKTGDLGRWLPDGTLEYLGR 3000
Cdd:cd05910 277 IEIddepiaewdDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGF----WHRMGDLGYLDDEGRLWFCGR 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3001 NDFQVKVRGFRIELGEIEtrlaRCHGVHDAV---VIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEY---MI 3074
Cdd:cd05910 353 KAHRVITTGGTLYTEPVE----RVFNTHPGVrrsALVGVGKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDYphtQR 428
|
490 500
....*....|....*....|....*
gi 641744967 3075 PSAFVTLDAFPLTP--NGKLDRKAL 3097
Cdd:cd05910 429 IGRFLIHPSFPVDIrhNAKIFREKL 453
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
471-957 |
9.93e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 118.37 E-value: 9.93e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 471 REMLIQQRFEAQAEQTPEAIAVLFEDQHL--TYRELNRRANQLAHHLIALGVQPDDRVAL----CVERSLEMmvglLGIL 544
Cdd:PRK08315 14 LEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIwapnVPEWVLTQ----FATA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 545 KAGAAYVPMDPAYPAERLAYILDDAAPVALLT--------------------QSAQVAQLNS-TLP----TVLLDTPAAA 599
Cdd:PRK08315 90 KIGAILVTINPAYRLSELEYALNQSGCKALIAadgfkdsdyvamlyelapelATCEPGQLQSaRLPelrrVIFLGDEKHP 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 600 ACPDTNPVVQ-GLHAAHLAY-----------VI---YTSGSTGRPKGVMVAHRNVINlaTGLHT--LLALDHPSRIALNa 662
Cdd:PRK08315 170 GMLNFDELLAlGRAVDDAELaarqatldpddPIniqYTSGTTGFPKGATLTHRNILN--NGYFIgeAMKLTEEDRLCIP- 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 663 siV-----FDASVKNWIQLLSGHTLVLVPDA------LRADAHQlwRYFARHAV-------------DLFDctpvqlqwl 718
Cdd:PRK08315 247 --VplyhcFGMVLGNLACVTHGATMVYPGEGfdplatLAAVEEE--RCTALYGVptmfiaeldhpdfARFD--------- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 719 ldagLGSdpayqpaqvLIGG-EAISP---AVWSRLQSLSDTRFIN-VYGPTECTVDATACVVD-----RTQplpTIGKPL 788
Cdd:PRK08315 314 ----LSS---------LRTGiMAGSPcpiEVMKRVIDKMHMSEVTiAYGMTETSPVSTQTRTDdplekRVT---TVGRAL 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 789 ANTRLYILDAQD-QPVPIGVTGELHIGGAGVARGYLHRPDLTAErfipdpfsADPAARIYKTGDLARWLPDGNIDYLGRn 867
Cdd:PRK08315 378 PHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPEKTAE--------AIDADGWMHTGDLAVMDEEGYVNIVGR- 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 868 dfqIK---VRGfrieaGE------IESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADY 938
Cdd:PRK08315 449 ---IKdmiIRG-----GEniypreIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFCRGKIAHY 520
|
570
....*....|....*....
gi 641744967 939 MIPSAFVTLDALPLTPNGK 957
Cdd:PRK08315 521 KIPRYIRFVDEFPMTVTGK 539
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
500-958 |
1.15e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 117.89 E-value: 1.15e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 500 TYRELNRRANQLAHHLIALGVQPDDRVALCV---ERSLEMMVGLLGilkAGAAYVPMDPAYPAERLAYILDDAAPVAL-- 574
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAYYGVSG---SGAVCHTINPRLFPEQIAYIVNHAEDRYVlf 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 575 -LTQSAQVAQLNSTLPTV---LLDTPAAAACPDTNPVV--QGLHAAH-------------LAYVIYTSGSTGRPKGVMVA 635
Cdd:PRK07008 118 dLTFLPLVDALAPQCPNVkgwVAMTDAAHLPAGSTPLLcyETLVGAQdgdydwprfdenqASSLCYTSGTTGNPKGALYS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 636 HRnvinlATGLHTLLALdHPSRIALNAS-----IVFDASVKNW----IQLLSGHTLVLVPDALraDAHQLWRYFARHAVD 706
Cdd:PRK07008 198 HR-----STVLHAYGAA-LPDAMGLSARdavlpVVPMFHVNAWglpySAPLTGAKLVLPGPDL--DGKSLYELIEAERVT 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 707 LFDCTPVQLQWLLD----AGLGSDPAyqpAQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACVV------- 775
Cdd:PRK07008 270 FSAGVPTVWLGLLNhmreAGLRFSTL---RRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLCKLkwkhsql 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 776 ---DRTQPLPTIGKPLANTRLYILDAQDQPVPI-GVT-GELHIGGAGVARGYLHRpdltaerfipdpfSADPAAR-IYKT 849
Cdd:PRK07008 347 pldEQRKLLEKQGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRG-------------DASPLVDgWFPT 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 850 GDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQ 929
Cdd:PRK07008 414 GDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLA 493
|
490 500
....*....|....*....|....*....
gi 641744967 930 QLAASLADYMIPSAFVTLDALPLTPNGKL 958
Cdd:PRK07008 494 FYEGKVAKWWIPDDVVFVDAIPHTATGKL 522
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1555-2016 |
1.54e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 117.50 E-value: 1.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1555 TYDALNRRANQLAHHLIDLGVKPDDRIAICV---ERSLDMVIGllaILKAGAAYVPLDPGYPAERLAYMLDDASPVALLT 1631
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAwngYRHLEAYYG---VSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1632 QANQRALLTGDVPR-------ILLdtADFSHLSEDN-PHV---------------PGLDAHHLAYVIYTSGSTGKPKGVM 1688
Cdd:PRK07008 118 DLTFLPLVDALAPQcpnvkgwVAM--TDAAHLPAGStPLLcyetlvgaqdgdydwPRFDENQASSLCYTSGTTGNPKGAL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1689 NSHRA--LCNRLVWMQNTYRLTPDDRVLQKTPFsFDVSVWEFFWPL-LYGARLVMARPDghKDAAYLAQLIERTGITTLH 1765
Cdd:PRK07008 196 YSHRStvLHAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGLPYSApLTGAKLVLPGPD--LDGKSLYELIEAERVTFSA 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1766 FVPS---MLQQFVQWADADCAcdSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTF----WACQ--PDD- 1835
Cdd:PRK07008 273 GVPTvwlGLLNHMREAGLRFS--TLRRTVIGGSACPPAMIRTFEDEYGVEVIHAWGMTEMSPLGTLcklkWKHSqlPLDe 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1836 -HRSFVPIGRPIANTQLYILDTLGQPVPL-GVA-GELHIGGVGVARGYLNRPDltaerfipDPFINQpgarLYKTGDLAR 1912
Cdd:PRK07008 351 qRKLLEKQGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRGDA--------SPLVDG----WFPTGDVAT 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1913 WLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGvtpdpADL-RQQLGQ 1991
Cdd:PRK07008 419 IDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVVVKRPG-----AEVtREELLA 493
|
490 500
....*....|....*....|....*....
gi 641744967 1992 H----LAEYMVPGAFVTLDAFPLTPNGKL 2016
Cdd:PRK07008 494 FyegkVAKWWIPDDVVFVDAIPHTATGKL 522
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1674-2017 |
1.86e-26 |
|
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: 113.17 E-value: 1.86e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1674 VIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFsFDVSVWEFFWPLLY--GARLVMARpdghKDAAY 1751
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPL-FHIGTLMFTLATFHagGTNVFVRR----VDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1752 LAQLIERTGITTLHFVPSMLQQFVQwADADCACD--SLRRVICSGE--ALPAELQQRFFARFNAqlhnlYGPTEAAIDVT 1827
Cdd:cd17636 80 VLELIEAERCTHAFLLPPTIDQIVE-LNADGLYDlsSLRSSPAAPEwnDMATVDTSPWGRKPGG-----YGQTEVMGLAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1828 FWACQPDDHRSFvpiGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFipdpfinqpGARLYKT 1907
Cdd:cd17636 154 FAALGGGAIGGA---GRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT---------RGGWHHT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1908 GDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQ 1987
Cdd:cd17636 222 NDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIE 301
|
330 340 350
....*....|....*....|....*....|
gi 641744967 1988 QLGQHLAEYMVPGAFVTLDAFPLTPNGKLD 2017
Cdd:cd17636 302 HCRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
2620-3101 |
2.03e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 117.34 E-value: 2.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:PRK07788 63 PDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALISQSAHLGIM------NGSLPVILLDDGETRPFDNEPDTpLD-------ARKQGLTPRHLAYVIYTSGSTGK 2766
Cdd:PRK07788 143 AREGVKALVYDDEFTDLLsalppdLGRLRAWGGNPDDDEPSGSTDET-LDdliagssTAPLPKPPKPGGIVILTSGTTGT 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2767 PKGVMvehanmvnflcsmRKEPGIAQEDVLL---------GVTSLSFDI------SILEIFLPLlnGARLILATQAQAAD 2831
Cdd:PRK07788 222 PKGAP-------------RPEPSPLAPLAGLlsrvpfragETTLLPAPMfhatgwAHLTLAMAL--GSTVVLRRRFDPEA 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2832 AQQlamLIERHAVSFMQATPSTWRMLVELRDFALP-PGFKAL----CGGEALPENLATALLQKV-TTLWNLYGPTE---T 2902
Cdd:PRK07788 287 TLE---DIAKHKATALVVVPVMLSRILDLGPEVLAkYDTSSLkiifVSGSALSPELATRALEAFgPVLYNLYGSTEvafA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2903 TIWSTLNGLTTPTPyIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYlgrpdltaerfiTDPFSGAPEARMYK 2982
Cdd:PRK07788 364 TIATPEDLAEAPGT-VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGY------------TDGRDKQIIDGLLS 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2983 TGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLR 3062
Cdd:PRK07788 431 SGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEDAIK 510
|
490 500 510
....*....|....*....|....*....|....*....
gi 641744967 3063 QRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAPD 3101
Cdd:PRK07788 511 DYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREMD 549
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
475-866 |
2.17e-26 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 116.92 E-value: 2.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 475 IQQRFEAQAEQTPEAIAVLFED----------QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGIL 544
Cdd:PRK09274 8 IARHLPRAAQERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 545 KAGAAYVPMDPAYPAERLAYILDDAAPVALLTQ-SAQVAQL----------------------NSTLPTVLLDTPAAA-A 600
Cdd:PRK09274 88 KAGAVPVLVDPGMGIKNLKQCLAEAQPDAFIGIpKAHLARRlfgwgkpsvrrlvtvggrllwgGTTLATLLRDGAAAPfP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 601 CPDTNPvvqglhaAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSR------------IAL-NASIVFD 667
Cdd:PRK09274 168 MADLAP-------DDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIdlptfplfalfgPALgMTSVIPD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 668 AsvknwiqllsghtlvlvpDALR---ADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSD---PAYQpaQVLIGGEAI 741
Cdd:PRK09274 241 M------------------DPTRpatVDPAKLFAAIERYGVTNLFGSPALLERLGRYGEANGiklPSLR--RVISAGAPV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 742 SPAVWSRLQSL--SDTRFINVYGPTEC--------------TVDATA-----CVvdrtqplptiGKPLANTRLYILD--- 797
Cdd:PRK09274 301 PIAVIERFRAMlpPDAEILTPYGATEAlpissiesreilfaTRAATDngagiCV----------GRPVDGVEVRIIAisd 370
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 798 ------AQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPdpfsaDPAARIY-KTGDLARWLPDGNIDYLGR 866
Cdd:PRK09274 371 apipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIP-----DGQGDVWhRMGDLGYLDAQGRLWFCGR 441
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
2600-3097 |
4.33e-26 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 116.27 E-value: 4.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2600 ADIP--RHALIHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGIL 2677
Cdd:PRK07059 15 AEIDasQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2678 KAGGAYVPLDPTYPVERLRYMLDD--AKPVALISQSAH------------------LGIMNG------------------ 2719
Cdd:PRK07059 95 RAGYVVVNVNPLYTPRELEHQLKDsgAEAIVVLENFATtvqqvlaktavkhvvvasMGDLLGfkghivnfvvrrvkkmvp 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2720 --SLPVIL-----LDDGETRPFdnepdtpldaRKQGLTPRHLAYVIYTSGSTGKPKGVMVEHANMV-NFLCS-------M 2784
Cdd:PRK07059 175 awSLPGHVrfndaLAEGARQTF----------KPVKLGPDDVAFLQYTGGTTGVSKGATLLHRNIVaNVLQMeawlqpaF 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2785 RKEPGIaqeDVLLGVTSLS-FDISILEI--FLPLLNGARLILATQAQAADAQQLAMliERHAVSFMQATPSTWRMLVELR 2861
Cdd:PRK07059 245 EKKPRP---DQLNFVCALPlYHIFALTVcgLLGMRTGGRNILIPNPRDIPGFIKEL--KKYQVHIFPAVNTLYNALLNNP 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2862 DFA---LPPGFKALCGGEALPENLATALLQKV-TTLWNLYGPTETTIWSTLNGLTTP--TPYIGHPIANTQIYILDAQGR 2935
Cdd:PRK07059 320 DFDkldFSKLIVANGGGMAVQRPVAERWLEMTgCPITEGYGLSETSPVATCNPVDATefSGTIGLPLPSTEVSIRDDDGN 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2936 VVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELG 3015
Cdd:PRK07059 400 DLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF--------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPN 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3016 EIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQpDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRK 3095
Cdd:PRK07059 472 EIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVVKK-DPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRR 550
|
..
gi 641744967 3096 AL 3097
Cdd:PRK07059 551 EL 552
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
472-966 |
6.30e-26 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 115.63 E-value: 6.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 472 EMLIQQRFEAQAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYV 551
Cdd:PRK13382 42 GMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADIL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 552 PMDPAYPAERLAYILDDAAPVALLTQSaqvaQLNSTLPTVLLDTPAAA---ACPDT--NPVVQGLHAAHLA--------- 617
Cdd:PRK13382 122 LLNTSFAGPALAEVVTREGVDTVIYDE----EFSATVDRALADCPQATrivAWTDEdhDLTVEVLIAAHAGqrpeptgrk 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 618 --YVIYTSGSTGRPKGvmvAHRNVINLATGLHTLLaldhpSRIALNAS--IVFDASV-KNWiqllsGHTLVLVPDALRAD 692
Cdd:PRK13382 198 grVILLTSGTTGTPKG---ARRSGPGGIGTLKAIL-----DRTPWRAEepTVIVAPMfHAW-----GFSQLVLAASLACT 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 693 AHQLWRYFARHAVDLFD--------CTPVQLQWLLDAglgsdpayqPAQVL------------IGGEAISPAVWSRLQSL 752
Cdd:PRK13382 265 IVTRRRFDPEATLDLIDrhratglaVVPVMFDRIMDL---------PAEVRnrysgrslrfaaASGSRMRPDVVIAFMDQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 753 SDTRFINVYGPTECTVDATACVVD-RTQPlPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYlhRPDLTAE 831
Cdd:PRK13382 336 FGDVIYNNYNATEAGMIATATPADlRAAP-DTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKD 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 832 rfIPDPFSAdpaariykTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLV 911
Cdd:PRK13382 413 --FHDGFMA--------SGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLA 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 912 AYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAP 966
Cdd:PRK13382 483 AFVVLKPGASATPETLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
483-963 |
6.54e-26 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 116.21 E-value: 6.54e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLF--------EDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAyVPMD 554
Cdd:PRK07529 35 AARHPDAPALSFlldadpldRPETWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPIN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 555 PAYPAERLAYILDDAAPVALLT----------QSAQ--VAQLNSTLPTVLLDTPAAAACPDTNPVVQGLHAAHLAYVIY- 621
Cdd:PRK07529 114 PLLEPEQIAELLRAAGAKVLVTlgpfpgtdiwQKVAevLAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAHARILDFd 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 622 ---------------------------TSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRI--ALNASIVFDASVKN 672
Cdd:PRK07529 194 aelarqpgdrlfsgrpigpddvaayfhTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVfcGLPLFHVNALLVTG 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 673 WIQLLSGHTLVL-VPDALRADA--HQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAISPAVWSRL 749
Cdd:PRK07529 274 LAPLARGAHVVLaTPQGYRGPGviANFWKIVERYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRF 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 750 QSLSDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYI--LDAQD---QPVPIGVTGELHIGGAGVARGYL- 823
Cdd:PRK07529 354 EAATGVRIVEGYGLTEATCVSSVNPPDGERRIGSVGLRLPYQRVRVviLDDAGrylRDCAVDEVGVLCIAGPNVFSGYLe 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 824 --HRPDLTAERfipdpfsadpaaRIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAR 901
Cdd:PRK07529 434 aaHNKGLWLED------------GWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGR 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 902 EDSPGDTRLVAYLCARPDAELHPAALRQQLAASLAD-YMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK07529 502 PDAHAGELPVAYVQLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPAL 564
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1554-2023 |
6.57e-26 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 115.46 E-value: 6.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQA 1633
Cdd:PLN02246 51 YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1634 NQRALLTG-----DVPRILLDTA-----DFSHLSE-DNPHVPGLDAHHLAYVI--YTSGSTGKPKGVMNSHRALCNRlVW 1700
Cdd:PLN02246 131 CYVDKLKGlaeddGVTVVTIDDPpegclHFSELTQaDENELPEVEISPDDVVAlpYSSGTTGLPKGVMLTHKGLVTS-VA 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1701 MQ------NTYrLTPDDRVLQKTP----FSFDvSVweffwpLLYGAR-----LVMARpdghKDAAYLAQLIERTGITTLH 1765
Cdd:PLN02246 210 QQvdgenpNLY-FHSDDVILCVLPmfhiYSLN-SV------LLCGLRvgaaiLIMPK----FEIGALLELIQRHKVTIAP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1766 FVPSMLQQFVQWADADCACDSLRRVICSGEA-LPAELQQRFFARF-NAQLHNLYGPTEA----AIDVTFwACQPDDHRSF 1839
Cdd:PLN02246 278 FVPPIVLAIAKSPVVEKYDLSSIRMVLSGAApLGKELEDAFRAKLpNAVLGQGYGMTEAgpvlAMCLAF-AKEPFPVKSG 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1840 vPIGRPIANTQLYILDT-LGQPVPLGVAGELHIGGVGVARGYLNRPDLTAErfipdpfinqpgarlykTGDLARWLPDGS 1918
Cdd:PLN02246 357 -SCGTVVRNAELKIVDPeTGASLPRNQPGEICIRGPQIMKGYLNDPEATAN-----------------TIDKDGWLHTGD 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1919 LEYLGRND--FQV-------KLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQL 1989
Cdd:PLN02246 419 IGYIDDDDelFIVdrlkeliKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFV 498
|
490 500 510
....*....|....*....|....*....|....
gi 641744967 1990 GQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPA 2023
Cdd:PLN02246 499 AKQVVFYKRIHKVFFVDSIPKAPSGKILRKDLRA 532
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2759-3094 |
6.65e-26 |
|
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: 111.99 E-value: 6.65e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2759 YTSGSTGKPKGVMVEHANMVN--FLCSMRKepGIAQEDVLLGVTSLsFDI--SILEIFLPLLNGARLILATQAQAADAQQ 2834
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNngYFIGERL--GLTEQDRLCIPVPL-FHCfgSVLGVLACLTHGATMVFPSPSFDPLAVL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2835 LAmlIERHAVSFMQATPSTWRMLVELRDFALPPgFKALCGGEALPENLATALLQKVTTLWNL------YGPTETTIWSTL 2908
Cdd:cd05917 86 EA--IEKEKCTALHGVPTMFIAELEHPDFDKFD-LSSLRTGIMAGAPCPPELMKRVIEVMNMkdvtiaYGMTETSPVSTQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2909 NGLTTPTPY----IGHPIANTQIYILDAQGRVVP-LGVAGEIHIAGAGVVRGYLGRPDLTAERFITDpfsgapeaRMYKT 2983
Cdd:cd05917 163 TRTDDSIEKrvntVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD--------GWLHT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2984 GDLGRWLPDGTLEYLGRndfqVK---VRGFR-IELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPA 3059
Cdd:cd05917 235 GDLAVMDEDGYCRIVGR----IKdmiIRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRLKEGAELTEE 310
|
330 340 350
....*....|....*....|....*....|....*
gi 641744967 3060 DLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDR 3094
Cdd:cd05917 311 DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1554-2021 |
7.45e-26 |
|
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: 113.82 E-value: 7.45e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQA 1633
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1634 NQRAlltgDVPRILLdtadfshlsednphvpgldahhlayviYTSGSTGKPKGVMNSHRAL----CNRLVWMQntyrLTP 1709
Cdd:cd05974 81 NTHA----DDPMLLY---------------------------FTSGTTSKPKLVEHTHRSYpvghLSTMYWIG----LKP 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1710 DDRVLQKTPFSFDVSVWE-FFWPLLYGArLVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQwADADCACDSLR 1788
Cdd:cd05974 126 GDVHWNISSPGWAKHAWScFFAPWNAGA-TVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQ-QDLASFDVKLR 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1789 RVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTFWACQPDDHRSfvpIGRPIANTQLYILDTLGQPVPLGVAGe 1868
Cdd:cd05974 204 EVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTETTALVGNSPGQPVKAGS---MGRPLPGYRVALLDPDGAPATEGEVA- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1869 LHIGG---VGVARGYLNRPDLTAERFipdpfinqpGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARL 1945
Cdd:cd05974 280 LDLGDtrpVGLMKGYAGDPDKTAHAM---------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1946 MQCPGVQEAVVVAredSPGDTRLV---AYLCPQPGVTPDPaDLRQQLGQHLAEYMVPGAFVTLDAF---PLTPNGKLDRK 2019
Cdd:cd05974 351 IEHPAVAEAAVVP---SPDPVRLSvpkAFIVLRAGYEPSP-ETALEIFRFSRERLAPYKRIRRLEFaelPKTISGKIRRV 426
|
..
gi 641744967 2020 AL 2021
Cdd:cd05974 427 EL 428
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
482-963 |
7.97e-26 |
|
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: 115.74 E-value: 7.97e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 482 QAEQTPEAIAVLFE------DQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDP 555
Cdd:cd05966 62 HLKERGDKVAIIWEgdepdqSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 556 AYPAERLAYILDDAAPVALLTQSA---------------QVAQLNSTLPTVL----LDTPAA-------------AACPD 603
Cdd:cd05966 142 GFSAESLADRINDAQCKLVITADGgyrggkviplkeivdEALEKCPSVEKVLvvkrTGGEVPmtegrdlwwhdlmAKQSP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 604 TNPVVQgLHAAHLAYVIYTSGSTGRPKGVMvaHrnvinlATGLHTLLAldhpsriALNASIVFD----------ASVkNW 673
Cdd:cd05966 222 ECEPEW-MDSEDPLFILYTSGSTGKPKGVV--H------TTGGYLLYA-------ATTFKYVFDyhpddiywctADI-GW 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 674 IqllSGHT-LVLVPDALRA------------DAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQV-LIG-- 737
Cdd:cd05966 285 I---TGHSyIVYGPLANGAttvmfegtptypDPGRYWDIVEKHKVTIFYTAPTAIRALMKFGDEWVKKHDLSSLrVLGsv 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 738 GEAISPAVWsrlqslsdTRFINVYGPTECTVdatacvVD---RTQ-------PLP--TIGKPLANTRLY------ILDAQ 799
Cdd:cd05966 362 GEPINPEAW--------MWYYEVIGKERCPI------VDtwwQTEtggimitPLPgaTPLKPGSATRPFfgiepaILDEE 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 800 DQPVPIGVTGELHIGGA--GVARGyLHRPDltaERFIPDPFSADPAarIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFR 877
Cdd:cd05966 428 GNEVEGEVEGYLVIKRPwpGMART-IYGDH---ERYEDTYFSKFPG--YYFTGDGARRDEDGYYWITGRVDDVINVSGHR 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 878 IEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPA---ALRQQLAASLADYMIPSAFVTLDALPLTP 954
Cdd:cd05966 502 LGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTLKDGEEPSDElrkELRKHVRKEIGPIATPDKIQFVPGLPKTR 581
|
....*....
gi 641744967 955 NGKLDRKAL 963
Cdd:cd05966 582 SGKIMRRIL 590
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1534-2016 |
1.21e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 114.87 E-value: 1.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1534 VEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYP 1613
Cdd:PRK07786 23 LARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLT 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1614 AERLAYMLDDASPVALLTQANQRALLTG---DVPRILL------DTADFS-----HLSEDNPHVPGLDAHH--LAYVIYT 1677
Cdd:PRK07786 103 PPEIAFLVSDCGAHVVVTEAALAPVATAvrdIVPLLSTvvvaggSSDDSVlgyedLLAEAGPAHAPVDIPNdsPALIMYT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1678 SGSTGKPKGVMNSHRALCNRLVWMQNTYRL-TPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMaRPDGHKDAAYLAQLI 1756
Cdd:PRK07786 183 SGTTGRPKGAVLTHANLTGQAMTCLRTNGAdINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVI-YPLGAFDPGQLLDVL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1757 ERTGITTLHFVPsmlqqfVQWaDADCACDSLR------RVICSGEAlPAE--LQQRFFARF-NAQLHNLYGPTEAAiDVT 1827
Cdd:PRK07786 262 EAEKVTGIFLVP------AQW-QAVCAEQQARprdlalRVLSWGAA-PASdtLLRQMAATFpEAQILAAFGQTEMS-PVT 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1828 FWACQPDDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlyKT 1907
Cdd:PRK07786 333 CMLLGEDAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF---------HS 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1908 GDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTP-DPADLR 1986
Cdd:PRK07786 404 GDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAAVRNDDAAlTLEDLA 483
|
490 500 510
....*....|....*....|....*....|
gi 641744967 1987 QQLGQHLAEYMVPGAFVTLDAFPLTPNGKL 2016
Cdd:PRK07786 484 EFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
2620-3097 |
1.44e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 113.72 E-value: 1.44e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPdERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:PRK07638 15 PNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKN-KTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALISQSAHLG-IMNGSLPVILLDDGEtRPFDNEPDTPLDARKQGLTPrhlAYVIYTSGSTGKPKG-VMVEHANM 2777
Cdd:PRK07638 94 AISNADMIVTERYKLNdLPDEEGRVIEIDEWK-RMIEKYLPTYAPIENVQNAP---FYMGFTSGSTGKPKAfLRAQQSWL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2778 VNFLCSMRkEPGIAQEDVLL--G--VTSLSFDISILEIFLpllnGARLILATQAQAADAQQLamlIERHAVSFMQATPST 2853
Cdd:PRK07638 170 HSFDCNVH-DFHMKREDSVLiaGtlVHSLFLYGAISTLYV----GQTVHLMRKFIPNQVLDK---LETENISVMYTVPTM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2854 WRMLVELRDFALPPgFKALCGGEALP----ENLATALLQkvTTLWNLYGPTETTIWSTL--NGLTTPTPYIGHPIANTQI 2927
Cdd:PRK07638 242 LESLYKENRVIENK-MKIISSGAKWEaeakEKIKNIFPY--AKLYEFYGASELSFVTALvdEESERRPNSVGRPFHNVQV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2928 YILDAQGRVVPLGVAGEIHIAG----AGVVRGYLGRPDLTAERFITdpfsgapearmykTGDLGRWLPDGTLEYLGRNDF 3003
Cdd:PRK07638 319 RICNEAGEEVQKGEIGTVYVKSpqffMGYIIGGVLARELNADGWMT-------------VRDVGYEDEEGFIYIVGREKN 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3004 QVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTvlepADLRQRLSEGVAEYMIPSAFVTLDA 3083
Cdd:PRK07638 386 MILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEKPVAIIKGSATK----QQLKSFCLQRLSSFKIPKEWHFVDE 461
|
490
....*....|....
gi 641744967 3084 FPLTPNGKLDRKAL 3097
Cdd:PRK07638 462 IPYTNSGKIARMEA 475
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
484-963 |
1.62e-25 |
|
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: 115.11 E-value: 1.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 484 EQTPEAIAVLFE------DQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAY 557
Cdd:cd05967 62 AGRGDQIALIYDspvtgtERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGAIHSVVFGGF 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 558 PAERLAYILDDAAPVALLTQSAQV----------------AQLNSTLPTVLL----DTPAAAACPDTN------------ 605
Cdd:cd05967 142 AAKELASRIDDAKPKLIVTASCGIepgkvvpykplldkalELSGHKPHHVLVlnrpQVPADLTKPGRDldwsellakaep 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 606 -PVVQgLHAAHLAYVIYTSGSTGRPKGV-------MVA----HRNVINLATGlhtllaldhpsrialnaSIVFDASVKNW 673
Cdd:cd05967 222 vDCVP-VAATDPLYILYTSGTTGKPKGVvrdngghAVAlnwsMRNIYGIKPG-----------------DVWWAASDVGW 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 674 I---------QLLSGHTLVLV---PDALrADAHQLWRYFARHAVDLFDCTPVQLQWL----LDAGLGSDPAYQPAQVL-I 736
Cdd:cd05967 284 VvghsyivygPLLHGATTVLYegkPVGT-PDPGAFWRVIEKYQVNALFTAPTAIRAIrkedPDGKYIKKYDLSSLRTLfL 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 737 GGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATA---CVVDRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHI 813
Cdd:cd05967 363 AGERLDPPTLEWAENTLGVPVIDHWWQTETGWPITAnpvGLEPLPIKAGSPGKPVPGYQVQVLDEDGEPVGPNELGNIVI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 814 GGAgVARGYLHRPDLTAERFIPDPFSADPAarIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGV 893
Cdd:cd05967 443 KLP-LPPGCLLTLWKNDERFKKLYLSKFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAV 519
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641744967 894 QDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIP-SAF---VTLDALPLTPNGKLDRKAL 963
Cdd:cd05967 520 AECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVALVREQIGPvAAFrlvIFVKRLPKTRSGKILRRTL 593
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
30-370 |
1.68e-25 |
|
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: 112.47 E-value: 1.68e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 30 PLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICWQGLHQPVQVV--WRQAPLTVN 107
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEIlpPGPAPLEVR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 108 TLTTTSSDTVPAQLRAATDPSNHRLNLSNAPLLSATT-AHDPvcGEWLLSLSIHHLISDHITQALIIDEIRLLLEDRPEA 186
Cdd:cd19539 83 DLSDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLgRFDP--DDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 187 LPKPLP-----YRNFIA---QILSVP-LSEHEQYFRNRLADIDTPTAPFDLVDVQGNGEDITEARLSLDSSLADALRRQA 257
Cdd:cd19539 161 PAAPLPelrqqYKEYAAwqrEALAAPrAAELLDFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 258 RHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRlqGNLGADRVMGMFINTLPLRVSLRER-SVHDVVQATSHELMM 336
Cdd:cd19539 241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGR--NHPRFESTVGFFVNLLPLRVDVSDCaTFRDLIARVRKALVD 318
|
330 340 350
....*....|....*....|....*....|....*..
gi 641744967 337 LLAHEQAPLA-LAQQCSQVPPPL--PLFSTLFNYRHS 370
Cdd:cd19539 319 AQRHQELPFQqLVAELPVDRDAGrhPLVQIVFQVTNA 355
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
491-965 |
1.80e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 114.01 E-value: 1.80e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 491 AVLFEDQHLTYRELNRRANQLAHHLIALgvQPDDR---VALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILD 567
Cdd:PRK07867 21 GLYFEDSFTSWREHIRGSAARAAALRAR--LDPTRpphVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDIA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 568 DAAPVALLTQSAQVAQLNSTLPTV-LLDTPAA------AACPDTNPVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVI 640
Cdd:PRK07867 99 HADCQLVLTESAHAELLDGLDPGVrVINVDSPawadelAAHRDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 641 NLATGLHTLLALDhPSRIALNASIVF--DASVKNWIQLLSGHTLVlvpdALRA--DAHQLWRYFARHAVDLFDCTPVQLQ 716
Cdd:PRK07867 179 SAGVMLAQRFGLG-PDDVCYVSMPLFhsNAVMAGWAVALAAGASI----ALRRkfSASGFLPDVRRYGATYANYVGKPLS 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 717 WLLDAGLGSDPAYQPAQVLIGGEAISPAVwSRLQSLSDTRFINVYGPTEctvdaTACVVDRTQPLPT--IGKPLANTRly 794
Cdd:PRK07867 254 YVLATPERPDDADNPLRIVYGNEGAPGDI-ARFARRFGCVVVDGFGSTE-----GGVAITRTPDTPPgaLGPLPPGVA-- 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 795 ILDAQD-QPVPIGV------------TGEL-HIGGAGVARGYLHRPDLTAERFipdpfsadpAARIYKTGDLARWLPDGN 860
Cdd:PRK07867 326 IVDPDTgTECPPAEdadgrllnadeaIGELvNTAGPGGFEGYYNDPEADAERM---------RGGVYWSGDLAYRDADGY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 861 IDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAAS--LADY 938
Cdd:PRK07867 397 AYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAQpdLGPK 476
|
490 500
....*....|....*....|....*..
gi 641744967 939 MIPSAFVTLDALPLTPNGKLDRKALPA 965
Cdd:PRK07867 477 QWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2632-3097 |
1.89e-25 |
|
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: 112.61 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQS 2711
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2712 AHLGimngslpviLLDDGetrPFdnepdtpldarkqgltprhlaYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIA 2791
Cdd:cd05973 81 ANRH---------KLDSD---PF---------------------VMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2792 QEDVLLGVTSLSFDISIL-EIFLPLLNGARLILATQAQAADAQQLamLIERHAVSFMQATPSTWRMLVEL-RDFALPPGF 2869
Cdd:cd05973 128 PEDSFWNAADPGWAYGLYyAITGPLALGHPTILLEGGFSVESTWR--VIERLGVTNLAGSPTAYRLLMAAgAEVPARPKG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2870 K---ALCGGEAL-PENLATALLQKVTTLWNLYGPTET-TIWSTLNGLTTPTPY--IGHPIANTQIYILDAQGRVVPLGVA 2942
Cdd:cd05973 206 RlrrVSSAGEPLtPEVIRWFDAALGVPIHDHYGQTELgMVLANHHALEHPVHAgsAGRAMPGWRVAVLDDDGDELGPGEP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2943 GEIHIAGAGV----VRGYLGRPDltaerfitdpfsGAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIE 3018
Cdd:cd05973 286 GRLAIDIANSplmwFRGYQLPDT------------PAIDGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVE 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3019 TRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPA---DLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRK 3095
Cdd:cd05973 354 SALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTPAladELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRF 433
|
..
gi 641744967 3096 AL 3097
Cdd:cd05973 434 LL 435
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
497-963 |
1.95e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 112.94 E-value: 1.95e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 497 QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLT 576
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 577 QSaqvaqlnstlptvLLDTPAAaacpdtnpvvqglhaahlayVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPS 656
Cdd:cd05910 81 IP-------------KADEPAA--------------------ILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 657 R-------IALnasivFDASVknwiqllsGHTLVLVP-DALR---ADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGS 725
Cdd:cd05910 128 VdlatfplFAL-----FGPAL--------GLTSVIPDmDPTRparADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQH 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 726 D-PAYQPAQVLIGGEAISPAVWSRLQSL--SDTRFINVYGPTEC---TVDATACVVDRTQPLPT------IGKPLANTRL 793
Cdd:cd05910 195 GiTLPSLRRVLSAGAPVPIALAARLRKMlsDEAEILTPYGATEAlpvSSIGSRELLATTTAATSggagtcVGRPIPGVRV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 794 YILDAQDQP---------VPIGVTGELHIGGAGVARGYLHRPDLTAERFIPdpfsaDPAARI-YKTGDLARWLPDGNIDY 863
Cdd:cd05910 275 RIIEIDDEPiaewddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKID-----DNSEGFwHRMGDLGYLDDEGRLWF 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 864 LGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAReDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADY---MI 940
Cdd:cd05910 350 CGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV-GKPGCQLPVLCVEPLPGTITPRARLEQELRALAKDYphtQR 428
|
490 500
....*....|....*....|....*
gi 641744967 941 PSAFVTLDALPLTP--NGKLDRKAL 963
Cdd:cd05910 429 IGRFLIHPSFPVDIrhNAKIFREKL 453
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
29-409 |
2.47e-25 |
|
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: 112.06 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 29 YPLAPLQEGILFHYQLQEKGDTYllNSLLAFdsqtRLDAFLDV------LQQVIARHDILRTAICWQGlHQPVQVVWRQA 102
Cdd:cd19531 2 LPLSFAQQRLWFLDQLEPGSAAY--NIPGAL----RLRGPLDVaaleraLNELVARHEALRTTFVEVD-GEPVQVILPPL 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 103 PLTVNT--LTTTSSDTVPAQLRA-ATDPSNHRLNLSNAPLLSAT---TAHDpvcgEWLLSLSIHHLISDHITQALIIDEI 176
Cdd:cd19531 75 PLPLPVvdLSGLPEAEREAEAQRlAREEARRPFDLARGPLLRATllrLGED----EHVLLLTMHHIVSDGWSMGVLLREL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 177 RLL----LEDRPEALPkPLP--YRNFIA---QILSVP-LSEHEQYFRNRLADIDTPTA-PFDLV--DVQ-GNGEditEAR 242
Cdd:cd19531 151 AALyaafLAGRPSPLP-PLPiqYADYAVwqrEWLQGEvLERQLAYWREQLAGAPPVLElPTDRPrpAVQsFRGA---RVR 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 243 LSLDSSLADALRRQARHLGISssvLFHV---AWAQVLALTSGRDDVVFGSVLSGRLQGNLgaDRVMGMFINTLPLRVSLR 319
Cdd:cd19531 227 FTLPAELTAALRALARREGAT---LFMTllaAFQVLLHRYSGQDDIVVGTPVAGRNRAEL--EGLIGFFVNTLVLRTDLS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 320 ER-SVHDVVQATSHELMMLLAHEQAPL-----ALaqqcsQVPPPL---PLFSTLFNYRHSQKDASSQFWEGMRQLSGRER 390
Cdd:cd19531 302 GDpTFRELLARVRETALEAYAHQDLPFeklveAL-----QPERDLsrsPLFQVMFVLQNAPAAALELPGLTVEPLEVDSG 376
|
410 420
....*....|....*....|
gi 641744967 391 T-NYPITLSVDDLGDGFNLT 409
Cdd:cd19531 377 TaKFDLTLSLTETDGGLRGS 396
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
499-963 |
2.83e-25 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 113.76 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIA-LGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVAL--- 574
Cdd:PRK12492 50 LSYAELERHSAAFAAYLQQhTDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQFKDSGARALvyl 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 575 -----LTQS------------AQVAQLNSTLPTVLLDT--------------PAAAACPDT---------NPVVQGLHaa 614
Cdd:PRK12492 130 nmfgkLVQEvlpdtgieylieAKMGDLLPAAKGWLVNTvvdkvkkmvpayhlPQAVPFKQAlrqgrglslKPVPVGLD-- 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 615 HLAYVIYTSGSTGRPKGVMVAHRN-VINLATGL----------HTLLALDHPSRIA-LNASIVFDASVKNWIQLLSGHTL 682
Cdd:PRK12492 208 DIAVLQYTGGTTGLAKGAMLTHGNlVANMLQVRaclsqlgpdgQPLMKEGQEVMIApLPLYHIYAFTANCMCMMVSGNHN 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 683 VLV--PDALRADAHQL--WRYFARHAVD-LFdctpvqlqwlldAGLGSDPAYQPAQVLI------GGEAISPAVWSRLQS 751
Cdd:PRK12492 288 VLItnPRDIPGFIKELgkWRFSALLGLNtLF------------VALMDHPGFKDLDFSAlkltnsGGTALVKATAERWEQ 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 752 LSDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAE 831
Cdd:PRK12492 356 LTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAE 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 832 rfipdpfsADPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLV 911
Cdd:PRK12492 436 --------ALDAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVK 507
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 641744967 912 AYLCARpDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK12492 508 LFVVAR-DPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1536-2021 |
2.94e-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: 113.39 E-value: 2.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1536 DQAARTPDTTAvlFEDQH----LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPG 1611
Cdd:cd17642 25 KRYASVPGTIA--FTDAHtgvnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1612 YPAERLAYMLDDASPVALLTQAN--QRAL-LTGDVPR----ILLDT-ADFSHLSEDN-----PHVPGLDAHH-------- 1670
Cdd:cd17642 103 YNERELDHSLNISKPTIVFCSKKglQKVLnVQKKLKIiktiIILDSkEDYKGYQCLYtfitqNLPPGFNEYDfkppsfdr 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1671 ---LAYVIYTSGSTGKPKGVMNSHRALCNRLV-WMQNTY--RLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMArpd 1744
Cdd:cd17642 183 deqVALIMNSSGSTGLPKGVQLTHKNIVARFShARDPIFgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLM--- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1745 gHK-DAAYLAQLIERTGITTLHFVPSMLQQFVQWADAD-CACDSLRRVICSGEALPAELQQRFFARFNAQ-LHNLYGPTE 1821
Cdd:cd17642 260 -YKfEEELFLRSLQDYKVQSALLVPTLFAFFAKSTLVDkYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPgIRQGYGLTE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1822 --AAIDVTfwaCQPDDHRSFVPIGRPIANTQLYILDTlGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFINq 1899
Cdd:cd17642 339 ttSAILIT---PEGDDKPGAVGKVVPFFYAKVVDLDT-GKTLGPNERGELCVKGPMIMKGYVNNPEATKALIDKDGWLH- 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1900 pgarlykTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVT 1979
Cdd:cd17642 414 -------SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEAGKT 486
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 641744967 1980 PDPADLRQQL-GQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd17642 487 MTEKEVMDYVaSQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
2607-3092 |
2.99e-25 |
|
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: 113.83 E-value: 2.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2607 LIHELFEAQVACTPDAIAVVFGEA------SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAG 2680
Cdd:cd17634 54 LAANALDRHLRENGDRTAIIYEGDdtsqsrTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2681 GAYVPLDPTYPVERLRYMLDDAKPVALISQSAHL--GIMNGSLPV--------------ILLDDGETRPFDNEPDTPLDA 2744
Cdd:cd17634 134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVraGRSVPLKKNvddalnpnvtsvehVIVLKRTGSDIDWQEGRDLWW 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2745 RKQ--GLTPRHLA---------YVIYTSGSTGKPKGVMVEHAN-MVNFLCSMRKEPGIAQEDVLLGVTSLSFDI--SILe 2810
Cdd:cd17634 214 RDLiaKASPEHQPeamnaedplFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGDIYWCTADVGWVTghSYL- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2811 IFLPLLNGARLILATQAQAADAQQLAM-LIERHAVSFMQATPSTWRMLVELRDFALP----PGFKALCG-GEAL-PENLA 2883
Cdd:cd17634 293 LYGPLACGATTLLYEGVPNWPTPARMWqVVDKHGVNILYTAPTAIRALMAAGDDAIEgtdrSSLRILGSvGEPInPEAYE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2884 TA---LLQKVTTLWNLYGPTET-----TIWSTLNGLTTPTPYIghPIANTQIYILDAQGRVVPLGVAGEIHIAGA--GVV 2953
Cdd:cd17634 373 WYwkkIGKEKCPVVDTWWQTETggfmiTPLPGAIELKAGSATR--PVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQT 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2954 RGYLGRPDLTAERFITDpFSGapearMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVI 3033
Cdd:cd17634 451 RTLFGDHERFEQTYFST-FKG-----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVV 524
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 3034 AREDSPGDKRLVAYLLAQPDtVLEPADLRQRLSEGVAEYM----IPSAFVTLDAFPLTPNGKL 3092
Cdd:cd17634 525 GIPHAIKGQAPYAYVVLNHG-VEPSPELYAELRNWVRKEIgplaTPDVVHWVDSLPKTRSGKI 586
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
2609-3193 |
3.27e-25 |
|
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: 115.19 E-value: 3.27e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2609 HELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDP 2688
Cdd:COG3319 4 AAAAAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2689 TYPVERLRYMLDDAKPVALISQSAHLGIMNGSLPVILLDDGETRPFDNEPDTPLDARKQGLTPRHLAYVIYTSGSTGKPK 2768
Cdd:COG3319 84 LALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2769 GVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQ 2848
Cdd:COG3319 164 LVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLL 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2849 ATPSTWRMLVELRDFALPPGFKALCGGEA-----LPENLATALLQKVTTLWNLYGPTETTIWSTLNGLTTPTPYIGHPIA 2923
Cdd:COG3319 244 LAALLLLLALALLLLLALLLLLGLLALLLallllLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPG 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2924 NTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSGAPEARMYKTGDLGRWLPDGTLEYLGRNDF 3003
Cdd:COG3319 324 LLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRL 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3004 QVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDkRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDA 3083
Cdd:COG3319 404 QRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAA-AALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLL 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3084 FPLTPNGKLDRKALPAPDQSAMATRgyEAPQGDLEHALAQIWQTLLGVERVGRHDHFFELGGHSLLAVQLNARIRAEFLT 3163
Cdd:COG3319 483 LLLLLLAALLLAAAAPAAAAAAAAA--PAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLR 560
|
570 580 590
....*....|....*....|....*....|
gi 641744967 3164 DIPIVAIFQHPQLSALAEVILAAQIHAAWG 3193
Cdd:COG3319 561 LLLLLALLLAPTLAALAAALAAAAAAAALS 590
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
495-963 |
3.45e-25 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 113.15 E-value: 3.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 495 EDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPA----YPAERLAYI----- 565
Cdd:cd05906 36 SEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVPptydEPNARLRKLrhiwq 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 566 -LDDaaPVaLLTQSAQVAQLN-----STLPTVLLDTPAAAACPDTNPVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNV 639
Cdd:cd05906 116 lLGS--PV-VLTDAELVAEFAgletlSGLPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNI 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 640 INLATGLHTL------------LALDHPsrialnASIVFD--ASVKNWIQLLSGHTLVLVPDALR----ADAHQLWRYFA 701
Cdd:cd05906 193 LARSAGKIQHngltpqdvflnwVPLDHV------GGLVELhlRAVYLGCQQVHVPTEEILADPLRwldlIDRYRVTITWA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 702 -----RHAVDLFdCTPVQLQWLLDAGLgsdpayqpaQVLIGGEAISPAVWSRLQS------LSDTRFINVYGPTECTVDA 770
Cdd:cd05906 267 pnfafALLNDLL-EEIEDGTWDLSSLR---------YLVNAGEAVVAKTIRRLLRllepygLPPDAIRPAFGMTETCSGV 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 771 TACVVDRTQPLPT------IGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaa 844
Cdd:cd05906 337 IYSRSFPTYDHSQalefvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW------ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 845 riYKTGDLArWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQD--AVVIAREDSPGDTRLVAYLCArPDAEL 922
Cdd:cd05906 411 --FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPsfTAAFAVRDPGAETEELAIFFV-PEYDL 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 641744967 923 HPA------ALRQQLAASL---ADYMIPsafVTLDALPLTPNGKLDRKAL 963
Cdd:cd05906 487 QDAlsetlrAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
2619-3097 |
4.25e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 112.29 E-value: 4.25e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2619 TPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYM 2698
Cdd:PRK06145 15 TPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2699 LDDAKPVALISQSAHLGIMNGSLPVILLD-----DGETRPFDNEPDTPLDARKqgltPRHLAYVIYTSGSTGKPKGVMVE 2773
Cdd:PRK06145 95 LGDAGAKLLLVDEEFDAIVALETPKIVIDaaaqaDSRRLAQGGLEIPPQAAVA----PTDLVRLMYTSGTTDRPKGVMHS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2774 HANMVNFLCSMRKEPGIAQEDVLLGVTSL----SFDISILEIflpLLNGARLILATQAQAADAQQLamlIERHAVSFMQA 2849
Cdd:PRK06145 171 YGNLHWKSIDHVIALGLTASERLLVVGPLyhvgAFDLPGIAV---LWVGGTLRIHREFDPEAVLAA---IERHRLTCAWM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2850 TP-STWRML-VELRD-FALPPGFKALCGGEALPENLATALLQKVTT--LWNLYGPTETTIWSTLNGLTTPTPYIG---HP 2921
Cdd:PRK06145 245 APvMLSRVLtVPDRDrFDLDSLAWCIGGGEKTPESRIRDFTRVFTRarYIDAYGLTETCSGDTLMEAGREIEKIGstgRA 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2922 IANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmyKTGDLGRWLPDGTLEYLGRN 3001
Cdd:PRK06145 325 LAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF---------RSGDVGYLDEEGFLYLTDRK 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3002 DFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTL 3081
Cdd:PRK06145 396 KDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVLNPGATLTLEALDRHCRQRLASFKVPRQLKVR 475
|
490
....*....|....*.
gi 641744967 3082 DAFPLTPNGKLDRKAL 3097
Cdd:PRK06145 476 DELPRNPSGKVLKRVL 491
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1674-2016 |
4.69e-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: 109.13 E-value: 4.69e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1674 VIYTSGSTGKPKGVMNSHR-ALCNRLVWMQNTyRLTPDDRVLQKTPF--SFDVSVwEFFWPLLYGARLVmarPDGHKDAA 1750
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRqTLRAAAAWADCA-DLTEDDRYLIINPFfhTFGYKA-GIVACLLTGATVV---PVAVFDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1751 YLAQLIERTGITTLHFVPSMLQQFVQWADADCA-CDSLRRVICSGEALPAELQQRFFAR--FNAQLhNLYGPTEAaidVT 1827
Cdd:cd17638 80 AILEAIERERITVLPGPPTLFQSLLDHPGRKKFdLSSLRAAVTGAATVPVELVRRMRSElgFETVL-TAYGLTEA---GV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1828 FWACQPDDHRSFVP--IGRPIANTQLYILDtlgqpvplgvAGELHIGGVGVARGYLNRPDLTAERFIPDPFINqpgarly 1905
Cdd:cd17638 156 ATMCRPGDDAETVAttCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGWLH------- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1906 kTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADL 1985
Cdd:cd17638 219 -TGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDV 297
|
330 340 350
....*....|....*....|....*....|.
gi 641744967 1986 RQQLGQHLAEYMVPGAFVTLDAFPLTPNGKL 2016
Cdd:cd17638 298 IAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1671-2021 |
5.46e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 109.49 E-value: 5.46e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1671 LAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTP-FSFDVSVWEFFWPLLYGARLVMARPDGHKDA 1749
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPlFHVNGSVVTLLTPLASGAHVVLAGPAGYRNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1750 AY---LAQLIERTGITTLHFVPSMLQQFVQW-ADADCAcdSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAID 1825
Cdd:cd05944 84 GLfdnFWKLVERYRITSLSTVPTVYAALLQVpVNADIS--SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1826 VTfwACQPDDHRSFVPIGRPIANTQLYI--LDTLGQ---PVPLGVAGELHIGGVGVARGYLNRpDLTAERFIPDPFINqp 1900
Cdd:cd05944 162 VA--VNPPDGPKRPGSVGLRLPYARVRIkvLDGVGRllrDCAPDEVGEICVAGPGVFGGYLYT-EGNKNAFVADGWLN-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1901 garlykTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTP 1980
Cdd:cd05944 237 ------TGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVV 310
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 641744967 1981 DPADLRQQLGQHLAEY-MVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05944 311 EEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
2618-3097 |
5.74e-25 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 112.39 E-value: 5.74e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2618 CTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGgaYVPLDPTYPVER--L 2695
Cdd:PRK10946 35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLG--VAPVNALFSHQRseL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2696 RYMLDDAKPVALISQSAH-----------LGIMNGSLPVILL-DDGETRPFDNEPDTPLDARKQGLTPR-HLAYVIYTSG 2762
Cdd:PRK10946 113 NAYASQIEPALLIADRQHalfsdddflntLVAEHSSLRVVLLlNDDGEHSLDDAINHPAEDFTATPSPAdEVAFFQLSGG 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2763 STGKPKGVMVEHANM----------------VNFLCS-------MRKEPGIaqedvlLGVtslsfdisileiflpLLNGA 2819
Cdd:PRK10946 193 STGTPKLIPRTHNDYyysvrrsveicgftpqTRYLCAlpaahnyPMSSPGA------LGV---------------FLAGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2820 RLILATQAQAADAQQlamLIERHAVSFMQATP---STWrmlveLRDFALPPGFKAL-------CGGEALPENLATAL--- 2886
Cdd:PRK10946 252 TVVLAPDPSATLCFP---LIEKHQVNVTALVPpavSLW-----LQAIAEGGSRAQLaslkllqVGGARLSETLARRIpae 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2887 ----LQKVttlwnlYGPTETTIWSTlnGLTTPTPYI----GHPIA-NTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYL 2957
Cdd:PRK10946 324 lgcqLQQV------FGMAEGLVNYT--RLDDSDERIfttqGRPMSpDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYY 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2958 GRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIARED 3037
Cdd:PRK10946 396 KSPQHNASAFDANGF--------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMED 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641744967 3038 SPGDKRLVAYLLAQPDtvLEPADLRQRLSE-GVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK10946 468 ELMGEKSCAFLVVKEP--LKAVQLRRFLREqGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
2624-3097 |
5.79e-25 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 112.08 E-value: 5.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2624 AVVF----GEAS-LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYM 2698
Cdd:PRK08008 25 ALIFessgGVVRrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2699 LDDAKPVALISQSAHLGIMNGSLP--------VILLDDGE---------TRPFDNEPDTPLDARKqgLTPRHLAYVIYTS 2761
Cdd:PRK08008 105 LQNSQASLLVTSAQFYPMYRQIQQedatplrhICLTRVALpaddgvssfTQLKAQQPATLCYAPP--LSTDDTAEILFTS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2762 GSTGKPKGVMVEHANMV------NFLCSMRKEpgiaqeDVLLGVTSlSFDISI-LEIFLPLLN-GARLILA--------- 2824
Cdd:PRK08008 183 GTTSRPKGVVITHYNLRfagyysAWQCALRDD------DVYLTVMP-AFHIDCqCTAAMAAFSaGATFVLLekysarafw 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2825 ---TQAQAADAQQLAMLIErhavSFMQATPSTWRMLVELRD--FALPpgfkalcggeaLPENLATALLQKV-TTLWNLYG 2898
Cdd:PRK08008 256 gqvCKYRATITECIPMMIR----TLMVQPPSANDRQHCLREvmFYLN-----------LSDQEKDAFEERFgVRLLTSYG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2899 PTETTIWstLNGlTTPT-----PYIGHPIANTQIYILDAQGRVVPLGVAGEIHI---AGAGVVRGYLGRPDLTAERFitd 2970
Cdd:PRK08008 321 MTETIVG--IIG-DRPGdkrrwPSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAKVL--- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2971 pfsgAPEARMYkTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLA 3050
Cdd:PRK08008 395 ----EADGWLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVL 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 641744967 3051 QPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK08008 470 NEGETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
499-963 |
8.59e-25 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 112.28 E-value: 8.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIA-LGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLT- 576
Cdd:PRK08751 51 ITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVi 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 577 -----------QSAQVAQLNSTLPTVLLDTPAAAA-----------CPD-------------------TNPVVQgLHAAH 615
Cdd:PRK08751 131 dnfgttvqqviADTPVKQVITTGLGDMLGFPKAALvnfvvkyvkklVPEyringairfrealalgrkhSMPTLQ-IEPDD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 616 LAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDhpSRIALNASIVFDASVKNWIQLLSGHTLVLV---------- 685
Cdd:PRK08751 210 IAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGT--GKLEEGCEVVITALPLYHIFALTANGLVFMkiggcnhlis 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 686 -PDALRADAHQL--WRYFARHAVD-LFDctpvqlqwlldaGLGSDPAYQPAQ------VLIGGEAISPAVWSRLQSLSDT 755
Cdd:PRK08751 288 nPRDMPGFVKELkkTRFTAFTGVNtLFN------------GLLNTPGFDQIDfsslkmTLGGGMAVQRSVAERWKQVTGL 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 756 RFINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIP 835
Cdd:PRK08751 356 TLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDA 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 836 DPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDtRLVAYLC 915
Cdd:PRK08751 436 DGW--------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSG-EIVKVVI 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 641744967 916 ARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK08751 507 VKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
480-963 |
1.04e-24 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 111.82 E-value: 1.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 480 EAQAEQTPEAIAVLFEDQH-----LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMD 554
Cdd:cd05970 24 DAMAKEYPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPAT 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 555 PAYPAERLAYILDDA---APVAL----LTQSAQVAQLNSTLPTVLL----DTPAA-----AACPDTNPVVQGLHAA---- 614
Cdd:cd05970 104 HQLTAKDIVYRIESAdikMIVAIaednIPEEIEKAAPECPSKPKLVwvgdPVPEGwidfrKLIKNASPDFERPTANsypc 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 615 --HLAYVIYTSGSTGRPKgvMVAHRNVINLAtglHTLLA-----LDHPSRIALNASIVFDASV--KNWIQLLSGhTLVLV 685
Cdd:cd05970 184 geDILLVYFSSGTTGMPK--MVEHDFTYPLG---HIVTAkywqnVREGGLHLTVADTGWGKAVwgKIYGQWIAG-AAVFV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 686 PDALRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTE 765
Cdd:cd05970 258 YDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 766 CTVdaTACVVDRTQPLP-TIGKPLANTRLYILDAQDQPVPIGVTGELHIGGA-----GVARGYLHRPDLTAERFIPDpfs 839
Cdd:cd05970 338 TTL--TIATFPWMEPKPgSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVWHDG--- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 840 adpaarIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPD 919
Cdd:cd05970 413 ------YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAKG 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 641744967 920 AElhPA-ALRQQLAASL----ADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05970 487 YE--PSeELKKELQDHVkkvtAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
482-963 |
1.11e-24 |
|
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: 112.34 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 482 QAEQTPEAIAVLFE------DQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDP 555
Cdd:TIGR02188 66 HLEARPDKVAIIWEgdepgeVRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLACARIGAIHSVVFG 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 556 AYPAERLAYILDDAAPVALLTQSAQVAQlNSTLPTVLLDTPAAAACPDT-----------NPV---VQG----------- 610
Cdd:TIGR02188 146 GFSAEALADRINDAGAKLVITADEGLRG-GKVIPLKAIVDEALEKCPVSvehvlvvrrtgNPVvpwVEGrdvwwhdlmak 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 611 ---------LHAAHLAYVIYTSGSTGRPKGVMvaHrnvinlATGLHTLLAldhpsriALNASIVFD----------ASVk 671
Cdd:TIGR02188 225 asaycepepMDSEDPLFILYTSGSTGKPKGVL--H------TTGGYLLYA-------AMTMKYVFDikdgdifwctADV- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 672 NWIqllSGHT-LVLVPDALRA------------DAHQLWRYFARHAVDLFDCTPVQLQWLLDAG--------------LG 724
Cdd:TIGR02188 289 GWI---TGHSyIVYGPLANGAttvmfegvptypDPGRFWEIIEKHKVTIFYTAPTAIRALMRLGdewvkkhdlsslrlLG 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 725 SdpayqpaqVligGEAISPAVWSrlqslsdtRFINVYGPTECT-VDA-----TACVVdrTQPLP--TIGKPLANTRLY-- 794
Cdd:TIGR02188 366 S--------V---GEPINPEAWM--------WYYKVVGKERCPiVDTwwqteTGGIM--ITPLPgaTPTKPGSATLPFfg 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 795 ----ILDAQDQPVPI-GVTGELHIGGA--GVARGYLHRPdltaERFIPDPFSadPAARIYKTGDLARWLPDGNIDYLGRN 867
Cdd:TIGR02188 425 iepaVVDEEGNPVEGpGEGGYLVIKQPwpGMLRTIYGDH----ERFVDTYFS--PFPGYYFTGDGARRDKDGYIWITGRV 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 868 DFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHP---AALRQQLAASLADYMIPSAF 944
Cdd:TIGR02188 499 DDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPDDelrKELRKHVRKEIGPIAKPDKI 578
|
570
....*....|....*....
gi 641744967 945 VTLDALPLTPNGKLDRKAL 963
Cdd:TIGR02188 579 RFVPGLPKTRSGKIMRRLL 597
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
483-963 |
2.84e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 110.17 E-value: 2.84e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLF--EDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAE 560
Cdd:PRK13391 7 AQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 561 RLAYILDDAAPVALLTQSAQ---VAQLNSTLPTVLLD---------------TPAAAACPDTNPVVQGLHAAHLayviYT 622
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKldvARALLKQCPGVRHRlvldgdgelegfvgyAEAVAGLPATPIADESLGTDML----YS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 623 SGSTGRPKGVM--VAHRNV---INLATGLHTLLALDHPSrIALNASIVFDASVKNW---IQLLSGHTLVLVpdalRADAH 694
Cdd:PRK13391 163 SGTTGRPKGIKrpLPEQPPdtpLPLTAFLQRLWGFRSDM-VYLSPAPLYHSAPQRAvmlVIRLGGTVIVME----HFDAE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 695 QLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPA--QVLIGGEAISPAVWSRlqslsdtRFINVYGPT-----ECT 767
Cdd:PRK13391 238 QYLALIEEYGVTHTQLVPTMFSRMLKLPEEVRDKYDLSslEVAIHAAAPCPPQVKE-------QMIDWWGPIiheyyAAT 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 768 VDATACVVDRTQPLP---TIGKPLANTrLYILDAQDQPVPIGVTGELHIGGaGVARGYLHRPDLTAErfipdpfSADPAA 844
Cdd:PRK13391 311 EGLGFTACDSEEWLAhpgTVGRAMFGD-LHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAE-------ARHPDG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 845 RIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIA--REDSPGDTRLVAYLC--ARPDA 920
Cdd:PRK13391 382 TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGvpNEDLGEEVKAVVQPVdgVDPGP 461
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 641744967 921 ELhPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK13391 462 AL-AAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1674-2018 |
3.66e-24 |
|
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: 106.58 E-value: 3.66e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1674 VIYTSGSTGKPKGVMNSHRALCNRLV-WMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPdgHKDAAYL 1752
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDiLQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTGGE--NTTYKSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1753 AQLIERTGITTLHFVPSMLQQFV-QWADADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEaaidVTFWAC 1831
Cdd:cd17635 84 FKILTTNAVTTTCLVPTLLSKLVsELKSANATVPSLRLIGYGGSRAIAADVRFIEATGLTNTAQVYGLSE----TGTALC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1832 QP--DDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlyKTGD 1909
Cdd:cd17635 160 LPtdDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV---------NTGD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1910 LARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPA-DLRQQ 1988
Cdd:cd17635 231 LGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIrALKHT 310
|
330 340 350
....*....|....*....|....*....|
gi 641744967 1989 LGQHLAEYMVPGAFVTLDAFPLTPNGKLDR 2018
Cdd:cd17635 311 IRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
483-963 |
4.64e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 109.65 E-value: 4.64e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERL 562
Cdd:PRK08162 28 AEVYPDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASI 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 563 AYILDDAAPVALLTQS--AQVAQlnstlptvlldtPAAAACPDTNPVV---------QGLHAAHLAY------------- 618
Cdd:PRK08162 108 AFMLRHGEAKVLIVDTefAEVAR------------EALALLPGPKPLVidvddpeypGGRFIGALDYeaflasgdpdfaw 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 619 -----------VIYTSGSTGRPKGVMVAHR--------NVINLATGLHTL----LALDH------PSRIALNASI-VFda 668
Cdd:PRK08162 176 tlpadewdaiaLNYTSGTTGNPKGVVYHHRgaylnalsNILAWGMPKHPVylwtLPMFHcngwcfPWTVAARAGTnVC-- 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 669 svknwiqllsghtlvlvpdaLR-ADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAY-QPAQVLIGGEAISPAVW 746
Cdd:PRK08162 254 --------------------LRkVDPKLIFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIdHPVHAMVAGAAPPAAVI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 747 SRLQSLSdTRFINVYGPTECTVDATACVvdrTQP----LPTIGKPLANTR----------LYILDAQD-QPVPI-GVT-G 809
Cdd:PRK08162 314 AKMEEIG-FDLTHVYGLTETYGPATVCA---WQPewdaLPLDERAQLKARqgvryplqegVTVLDPDTmQPVPAdGETiG 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 810 ELHIGGAGVARGYLHRPDLTAERFipdpfsadpAARIYKTGDLARWLPDGNIdylgrndfQIKVR--------GFRIEAG 881
Cdd:PRK08162 390 EIMFRGNIVMKGYLKNPKATEEAF---------AGGWFHTGDLAVLHPDGYI--------KIKDRskdiiisgGENISSI 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 882 EIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAfVTLDALPLTPNGKLDRK 961
Cdd:PRK08162 453 EVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKA-VVFGELPKTSTGKIQKF 531
|
..
gi 641744967 962 AL 963
Cdd:PRK08162 532 VL 533
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
619-959 |
5.02e-24 |
|
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: 106.23 E-value: 5.02e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 619 VIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSrIALNASIVFDASVKNWI--QLLSGHTLVLVPdalRADAHQL 696
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGT-VFLNSGPLFHIGTLMFTlaTFHAGGTNVFVR---RVDAEEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 697 WRYFARHAVDL-FDCTPVQLQWL-LDAGLGSDpayqpaqvLIGGEAISPA-VWSRLQSLSDTRFINV---YGPTECTVDA 770
Cdd:cd17636 81 LELIEAERCTHaFLLPPTIDQIVeLNADGLYD--------LSSLRSSPAApEWNDMATVDTSPWGRKpggYGQTEVMGLA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 771 TACVVDRtQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFipdpfsadpAARIYKTG 850
Cdd:cd17636 153 TFAALGG-GAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT---------RGGWHHTN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 851 DLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQ 930
Cdd:cd17636 223 DLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEH 302
|
330 340
....*....|....*....|....*....
gi 641744967 931 LAASLADYMIPSAFVTLDALPLTPNGKLD 959
Cdd:cd17636 303 CRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
2616-3097 |
5.09e-24 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 109.40 E-value: 5.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2616 VACTPDAIAVVFGE--ASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVE 2693
Cdd:PRK13391 7 AQTTPDKPAVIMAStgEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2694 RLRYMLDDAKPVALISQSAHLGIM--------NGSLPVILLDDGETRPFDN-------EPDTPLDARKQGltprhlAYVI 2758
Cdd:PRK13391 87 EAAYIVDDSGARALITSAAKLDVArallkqcpGVRHRLVLDGDGELEGFVGyaeavagLPATPIADESLG------TDML 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2759 YTSGSTGKPKGVMVEHAnmvnflcsmrkEPGIAQEDVLLGVTSLSFDISILEIFL---PLLNGARLILATQAQAADAQQL 2835
Cdd:PRK13391 161 YSSGTTGRPKGIKRPLP-----------EQPPDTPLPLTAFLQRLWGFRSDMVYLspaPLYHSAPQRAVMLVIRLGGTVI 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2836 AM----------LIERHAVSFMQATPSTW-RMLV---ELRD-FALPPGFKALCGGEALPENLATALLQKV-TTLWNLYGP 2899
Cdd:PRK13391 230 VMehfdaeqylaLIEEYGVTHTQLVPTMFsRMLKlpeEVRDkYDLSSLEVAIHAAAPCPPQVKEQMIDWWgPIIHEYYAA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2900 TE---TTIWSTLNGLTTPTPyIGHPIANTqIYILDAQGRVVPLGVAGEIHIAGAGVVRgYLGRPDLTAErfitdpfSGAP 2976
Cdd:PRK13391 310 TEglgFTACDSEEWLAHPGT-VGRAMFGD-LHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAE-------ARHP 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2977 EARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIA--REDSPGDKRLVAYLL--AQP 3052
Cdd:PRK13391 380 DGTWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGvpNEDLGEEVKAVVQPVdgVDP 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 641744967 3053 DTVLEpADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK13391 460 GPALA-AELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
495-963 |
8.96e-24 |
|
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: 108.19 E-value: 8.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 495 EDQH---LTYRELnRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAP 571
Cdd:cd05909 1 EDTLgtsLTYRKL-LTGAIALARKLAKMTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 572 VALLTQSAQVAQLNST-LPTVLLD--------------------TPAAAACPDTNPVVQ-GLH---AAHLAYVIYTSGST 626
Cdd:cd05909 80 KTVLTSKQFIEKLKLHhLFDVEYDarivyledlrakiskadkckAFLAGKFPPKWLLRIfGVApvqPDDPAVILFTSGSE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 627 GRPKGVMVAHRNVINLATGLHTLLALDhPSRIALNASIVFDA---SVKNWIQLLSGHTLVLVPDALraDAHQLWRYFARH 703
Cdd:cd05909 160 GLPKGVVLSHKNLLANVEQITAIFDPN-PEDVVFGALPFFHSfglTGCLWLPLLSGIKVVFHPNPL--DYKKIPELIYDK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 704 AVDLFDCTPVqlqwLLDAGLGSDPAYQPAQ---VLIGGEAISPAVWSRLQSLSDTRFINVYGPTECtvdatACVVDRTQP 780
Cdd:cd05909 237 KATILLGTPT----FLRGYARAAHPEDFSSlrlVVAGAEKLKDTLRQEFQEKFGIRILEGYGTTEC-----SPVISVNTP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 781 LP-----TIGKPLANTRLYILDAQD-QPVPIGVTGELHIGGAGVARGYLHRPDLTAERFipdpfsadpAARIYKTGDLAR 854
Cdd:cd05909 308 QSpnkegTVGRPLPGMEVKIVSVEThEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF---------GDGWYDTGDIGK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 855 WLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLL-RCPG-VQDAVVIAREDSPGDtRLVAyLCARPDAElhPAALRQQL- 931
Cdd:cd05909 379 IDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSeILPEdNEVAVVSVPDGRKGE-KIVL-LTTTTDTD--PSSLNDILk 454
|
490 500 510
....*....|....*....|....*....|..
gi 641744967 932 AASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05909 455 NAGISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
2599-3091 |
1.41e-23 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 108.36 E-value: 1.41e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2599 DADIP-RHALIHELFEAQVACTPDAIAVVFGEASL--SYDELNRRANRLAHHLISFGVRPDERVAI----CVErgldMVV 2671
Cdd:PRK08315 8 PTDVPlLEQTIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIwapnVPE----WVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2672 GLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALIS-----QSAHLGIMNGSLP--------------------VILL 2726
Cdd:PRK08315 84 TQFATAKIGAILVTINPAYRLSELEYALNQSGCKALIAadgfkDSDYVAMLYELAPelatcepgqlqsarlpelrrVIFL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2727 DDGETRPFDN----------EPDTPLDARKQGLTPRHLAYVIYTSGSTGKPKGVMVEHANMVN--FLCSMRKepGIAQED 2794
Cdd:PRK08315 164 GDEKHPGMLNfdellalgraVDDAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNngYFIGEAM--KLTEED 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2795 -----------------VLLGVTSLSFDISILEIFLPLlngarLILATQAQaadaqqlamliER----HAVSFMqatpst 2853
Cdd:PRK08315 242 rlcipvplyhcfgmvlgNLACVTHGATMVYPGEGFDPL-----ATLAAVEE-----------ERctalYGVPTM------ 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2854 wrMLVEL--RDFA------LPPGFKAlcgGEALPEnlatALLQKVTTLWNL------YGPTETTIWSTLNGLTTP----T 2915
Cdd:PRK08315 300 --FIAELdhPDFArfdlssLRTGIMA---GSPCPI----EVMKRVIDKMHMsevtiaYGMTETSPVSTQTRTDDPlekrV 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2916 PYIGHPIANTQIYILD-AQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearMYkTGDLGRWLPDGT 2994
Cdd:PRK08315 371 TTVGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDADGW-------MH-TGDLAVMDEEGY 442
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2995 LEYLGRndfqVK---VRGfrielG------EIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRL 3065
Cdd:PRK08315 443 VNIVGR----IKdmiIRG-----GeniyprEIEEFLYTHPKIQDVQVVGVPDEKYGEEVCAWIILRPGATLTEEDVRDFC 513
|
570 580
....*....|....*....|....*.
gi 641744967 3066 SEGVAEYMIPSAFVTLDAFPLTPNGK 3091
Cdd:PRK08315 514 RGKIAHYKIPRYIRFVDEFPMTVTGK 539
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1090-1399 |
1.53e-23 |
|
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: 106.37 E-value: 1.53e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1090 AYHLPAALHLTGR--LDRpaLTTALNGLVARHESLRTRFTSiDG--QPAQQIdpdtlgfslsshdLRK-------LDEAA 1158
Cdd:cd19544 23 PYLLRSLLAFDSRarLDA--FLAALQQVIDRHDILRTAILW-EGlsEPVQVV-------------WRQaelpveeLTLDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1159 RTTRVAELAE--QEARARFDLTQGPLIRGQLLQLDDN-THVLLLTQHHIISDGWSIGILARELAALyqaaLEGSEANLPP 1235
Cdd:cd19544 87 GDDALAQLRArfDPRRYRLDLRQAPLLRAHVAEDPANgRWLLLLLFHHLISDHTSLELLLEEIQAI----LAGRAAALPP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1236 lPVQYADYAVwqrQWLQGETLNDLRDYWRDQLQG-----AP-ALLEIPTDRPRPSVQRYAgdqvpfhLDAGQLRRLHALN 1309
Cdd:cd19544 163 -PVPYRNFVA---QARLGASQAEHEAFFREMLGDvdeptAPfGLLDVQGDGSDITEARLA-------LDAELAQRLRAQA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1310 RQQGT---TLFMtllAAWSVVLSRLSGQDDIVIGTPVANRpRQELEG---MVGFFVNTLALRTEPGRChAVADLLDQVRE 1383
Cdd:cd19544 232 RRLGVspaSLFH---LAWALVLARCSGRDDVVFGTVLSGR-MQGGAGadrALGMFINTLPLRVRLGGR-SVREAVRQTHA 306
|
330
....*....|....*...
gi 641744967 1384 R--ALdayahqaLPFEQV 1399
Cdd:cd19544 307 RlaEL-------LRHEHA 317
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1528-2023 |
1.58e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 107.84 E-value: 1.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1528 ALIHQLVEDqaartpDTTAVLFEDQHLTYDALNRRANQLAHHLIDLgvKPDDR---IAICVERSLDMVIGLLAILKAGAA 1604
Cdd:PRK07867 9 ELLLPLAED------DDRGLYFEDSFTSWREHIRGSAARAAALRAR--LDPTRpphVGVLLDNTPEFSLLLGAAALSGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1605 YVPLDPGYPAERLAYMLDDASPVALLTQANQRALLTGD---VPRILLDTADFSHLSEDNPHVP----GLDAHHLAYVIYT 1677
Cdd:PRK07867 81 PVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGLdpgVRVINVDSPAWADELAAHRDAEppfrVADPDDLFMLIFT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1678 SGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLY-GARLVMAR--------PDghkd 1748
Cdd:PRK07867 161 SGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVALAaGASIALRRkfsasgflPD---- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1749 aaylaqlIERTGITTLHFVPSMLQQFVQWADADCACDSLRRVICSGEALPAELQqRFFARFNAQLHNLYGPTEAAIDVTF 1828
Cdd:PRK07867 237 -------VRRYGATYANYVGKPLSYVLATPERPDDADNPLRIVYGNEGAPGDIA-RFARRFGCVVVDGFGSTEGGVAITR 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1829 WACQPDDhrsfvPIGRPIANTQLYILDTlGQPVPLGVA------------GEL-HIGGVGVARGYLNRPDLTAERFipdp 1895
Cdd:PRK07867 309 TPDTPPG-----ALGPLPPGVAIVDPDT-GTECPPAEDadgrllnadeaiGELvNTAGPGGFEGYYNDPEADAERM---- 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1896 finqPGARlYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQ 1975
Cdd:PRK07867 379 ----RGGV-YWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLA 453
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 641744967 1976 PGVTPDPADLRQQLGQH--LAEYMVPGAFVTLDAFPLTPNGKLDRKALPA 2023
Cdd:PRK07867 454 PGAKFDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1533-2021 |
2.02e-23 |
|
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: 107.58 E-value: 2.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1533 LVEDQAARTPDTTAVLFEDQH-----LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVP 1607
Cdd:cd05970 22 VVDAMAKEYPDKLALVWCDDAgeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIP 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1608 LDPGYPAERLAYMLDDASPVALLTQANQ------------------RALLTGDVP-------RILLDTADFSHLSEDNPH 1662
Cdd:cd05970 102 ATHQLTAKDIVYRIESADIKMIVAIAEDnipeeiekaapecpskpkLVWVGDPVPegwidfrKLIKNASPDFERPTANSY 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1663 VPGLDahhLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVW-EFFWPLLYGARlVMA 1741
Cdd:cd05970 182 PCGED---ILLVYFSSGTTGMPKMVEHDFTYPLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAA-VFV 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1742 RPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTE 1821
Cdd:cd05970 258 YDYDKFDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTGIKLMEGFGQTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1822 AAIDVTFWACQPDDHRSfvpIGRPIANTQLYILDTLGQPVPLGVAGELHIG-----GVGVARGYLNRPDLTAERFipdpf 1896
Cdd:cd05970 338 TTLTIATFPWMEPKPGS---MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgkPVGLFGGYYKDAEKTAEVW----- 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1897 inQPGarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQP 1976
Cdd:cd05970 410 --HDG--YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVLAK 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 641744967 1977 GVTPDPAdLRQQLGQHL----AEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05970 486 GYEPSEE-LKKELQDHVkkvtAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
1555-2021 |
2.27e-23 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 107.53 E-value: 2.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1555 TYDALNRRANQLAHHLIDLGVKPDDRIAIC---VERSLDMVIGLLAIlkaGAAYVPLDPGYPAERLAYMLDDASPVALLT 1631
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1632 QANQRALLTGDVPRI-----LLDTADFSHLSEdnPHVPGL-------------------DAHHLAYVIYTSGSTGKPKGV 1687
Cdd:PRK06018 118 DLTFVPILEKIADKLpsverYVVLTDAAHMPQ--TTLKNAvayeewiaeadgdfawktfDENTAAGMCYTSGTTGDPKGV 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1688 MNSHRA--LCNRLVWMQNTYRLTPDDRVLQKTPFsFDVSVW--EFFWPLLyGARLVMarPDGHKDAAYLAQLIERTGITT 1763
Cdd:PRK06018 196 LYSHRSnvLHALMANNGDALGTSAADTMLPVVPL-FHANSWgiAFSAPSM-GTKLVM--PGAKLDGASVYELLDTEKVTF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1764 LHFVPSMLQQFVQWADADCA-CDSLRRVICSGEALPAELQqRFFARFNAQLHNLYGPTEAAIDVTFWACQP------DDH 1836
Cdd:PRK06018 272 TAGVPTVWLMLLQYMEKEGLkLPHLKMVVCGGSAMPRSMI-KAFEDMGVEVRHAWGMTEMSPLGTLAALKPpfsklpGDA 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1837 RSFVPI--GRPIANTQLYILDTLGQPVPL-GVA-GELHIGGVGVARGYLNRPD--LTAERFipdpfinqpgarlYKTGDL 1910
Cdd:PRK06018 351 RLDVLQkqGYPPFGVEMKITDDAGKELPWdGKTfGRLKVRGPAVAAAYYRVDGeiLDDDGF-------------FDTGDV 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1911 ARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLG 1990
Cdd:PRK06018 418 ATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILKYMD 497
|
490 500 510
....*....|....*....|....*....|.
gi 641744967 1991 QHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK06018 498 GKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1554-2021 |
2.55e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 107.54 E-value: 2.55e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDL-GVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQ 1632
Cdd:PRK05677 50 LTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDSGAKALVCL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1633 ANQRALLTGDVPR------ILLDTADF-------------SHLSEDNP--HVPG--------------------LDAHHL 1671
Cdd:PRK05677 130 ANMAHLAEKVLPKtgvkhvIVTEVADMlpplkrllinavvKHVKKMVPayHLPQavkfndalakgagqpvteanPQADDV 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1672 AYVIYTSGSTGKPKGVMNSHRAL-CNRLVWMQNTYRLTPDDRVLQKTP--------FSFDVSVWeffwpLLYGARLVMar 1742
Cdd:PRK05677 210 AVLQYTGGTTGVAKGAMLTHRNLvANMLQCRALMGSNLNEGCEILIAPlplyhiyaFTFHCMAM-----MLIGNHNIL-- 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1743 pdghkdaaylaqliertgITTLHFVPSMLQQFVQWA-----------DADCACDSLRRV--------ICSGEALPAELQQ 1803
Cdd:PRK05677 283 ------------------ISNPRDLPAMVKELGKWKfsgfvglntlfVALCNNEAFRKLdfsalkltLSGGMALQLATAE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1804 RFFARFNAQLHNLYGPTEAAIDVTFwacQPDDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNR 1883
Cdd:PRK05677 345 RWKEVTGCAICEGYGMTETSPVVSV---NPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQR 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1884 PDLTAERFIPDPFInqpgarlyKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSP 1963
Cdd:PRK05677 422 PEATDEILDSDGWL--------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEK 493
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 1964 GDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK05677 494 SGEAIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1554-2021 |
3.16e-23 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 107.24 E-value: 3.16e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLID-LGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDP-GYPAERLAYMLDDASPVALLT 1631
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPsSSLGEIKKRVVDCSVGLAFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1632 QANQRALLTGDVPRILL-DTADFSHLSEDNPHV-------------PGLDAHHLAYVIYTSGSTGKPKGVMNSHR---AL 1694
Cdd:PLN02574 147 PENVEKLSPLGVPVIGVpENYDFDSKRIEFPKFyelikedfdfvpkPVIKQDDVAAIMYSSGTTGASKGVVLTHRnliAM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1695 CNRLVWMQNT-YRLTPDDRV-LQKTPFSFDVSVWEFFWPLL-YGARLVMARpdgHKDAAYLAQLIERTGITTLHFVPSML 1771
Cdd:PLN02574 227 VELFVRFEASqYEYPGSDNVyLAALPMFHIYGLSLFVVGLLsLGSTIVVMR---RFDASDMVKVIDRFKVTHFPVVPPIL 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1772 QQFVQWADADCA--CDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIdVTFWACQPDDHRSFVPIGRPIAN 1848
Cdd:PLN02574 304 MALTKKAKGVCGevLKSLKQVSCGAAPLSGKFIQDFVQTLpHVDFIQGYGMTESTA-VGTRGFNTEKLSKYSSVGLLAPN 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1849 TQLYILD-TLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFInqpgarlyKTGDLARWLPDGSLEYLGRNDF 1927
Cdd:PLN02574 383 MQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGWL--------RTGDIAYFDEDGYLYIVDRLKE 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1928 QVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDA 2007
Cdd:PLN02574 455 IIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFVQS 534
|
490
....*....|....
gi 641744967 2008 FPLTPNGKLDRKAL 2021
Cdd:PLN02574 535 IPKSPAGKILRREL 548
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
2606-3000 |
4.42e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 106.95 E-value: 4.42e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2606 ALIHELFEAQvactPDAIAVVF--------GEA-SLSYDELNRRANRLAHHLISFGVrPDERVAICVERGLDMVVGLLGI 2676
Cdd:PRK05850 5 SLLRERASLQ----PDDAAFTFidyeqdpaGVAeTLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2677 LKAGGAYVPLD-PTYPV--ERLRYMLDDAKPVALISQSAhlgIMNGSLPVILLDDGETRPFDNEPDTP-LDA-RKQGLTP 2751
Cdd:PRK05850 80 LQAGLIAVPLSvPQGGAhdERVSAVLRDTSPSVVLTTSA---VVDDVTEYVAPQPGQSAPPVIEVDLLdLDSpRGSDARP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2752 RHL---AYVIYTSGSTGKPKGVMVEHAN-MVNFLCSMR----KEPGIAQEDVLLgVTSLSF--DIS-ILEIFLPLLNGAR 2820
Cdd:PRK05850 157 RDLpstAYLQYTSGSTRTPAGVMVSHRNvIANFEQLMSdyfgDTGGVPPPDTTV-VSWLPFyhDMGlVLGVCAPILGGCP 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2821 LILATqaqaadaqqlamlierhAVSFMQaTPSTW-RMLVE-LRDFALPPGFK-ALCGGEALPENLATALLQKVTTL---- 2893
Cdd:PRK05850 236 AVLTS-----------------PVAFLQ-RPARWmQLLASnPHAFSAAPNFAfELAVRKTSDDDMAGLDLGGVLGIisgs 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2894 -----------------WNL--------YGPTETTIW-STLNGLTTP-----------------------TPYIGHPIAN 2924
Cdd:PRK05850 298 ervhpatlkrfadrfapFNLretairpsYGLAEATVYvATREPGQPPesvrfdyeklsaghakrcetgggTPLVSYGSPR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2925 TQIY-ILDAQGRV-VPLGVAGEIHIAGAGVVRGYLGRPDLTAERF---ITDPFSGAPEARMYKTGDLGrWLPDGTLEYLG 2999
Cdd:PRK05850 378 SPTVrIVDPDTCIeCPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPGTPEGPWLRTGDLG-FISEGELFIVG 456
|
.
gi 641744967 3000 R 3000
Cdd:PRK05850 457 R 457
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
780-1056 |
4.45e-23 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 102.52 E-value: 4.45e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 780 PLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFSADPaariYKTGDLARWLPDG 859
Cdd:COG3433 16 PPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQP----GRQADDLRLLLRR 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 860 NIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCA--RPDAELHPAALRQQLAASLAD 937
Cdd:COG3433 92 GLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGavAALDGLAAAAALAALDKVPPD 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 938 YMIPSAFVTLDALPLTPNGKLDRKALPAPDQTAFATRDYEAP---QGGIETALAALWQELLGL--DRVGRHDQFFALGGH 1012
Cdd:COG3433 172 VVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPaleTALTEEELRADVAELLGVdpEEIDPDDNLFDLGLD 251
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 641744967 1013 SLLAVQLLNRMNKAGMDVALATLFAHPTLCDLAAAVTATAHDAP 1056
Cdd:COG3433 252 SIRLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1532-2021 |
5.46e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 106.64 E-value: 5.46e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1532 QLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPG 1611
Cdd:PRK07059 27 DLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1612 YPAERLAYMLDDASPVALLTQAN-----QRALLTGDVPRILL----DTADF----------------------------S 1654
Cdd:PRK07059 107 YTPRELEHQLKDSGAEAIVVLENfattvQQVLAKTAVKHVVVasmgDLLGFkghivnfvvrrvkkmvpawslpghvrfnD 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1655 HLSED-----NPhvPGLDAHHLAYVIYTSGSTGKPKGVMNSHR-ALCNRL---VWMQNTYRLTPDDRVLQ---KTPFS-- 1720
Cdd:PRK07059 187 ALAEGarqtfKP--VKLGPDDVAFLQYTGGTTGVSKGATLLHRnIVANVLqmeAWLQPAFEKKPRPDQLNfvcALPLYhi 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1721 FDVSVWEFFWPLLYGARLVMARPdghKDAAYLAQLIERTGITTLHFVPSMLQQFVQWAD-ADCACDSLRRVICSGEALPA 1799
Cdd:PRK07059 265 FALTVCGLLGMRTGGRNILIPNP---RDIPGFIKELKKYQVHIFPAVNTLYNALLNNPDfDKLDFSKLIVANGGGMAVQR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1800 ELQQRFFARFNAQLHNLYGPTEAAIDVTfwaCQPDDHRSFV-PIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVAR 1878
Cdd:PRK07059 342 PVAERWLEMTGCPITEGYGLSETSPVAT---CNPVDATEFSgTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMA 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1879 GYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVA 1958
Cdd:PRK07059 419 GYWNRPDETAKVMTADGF--------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVG 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 1959 REDSPGDTRLVAYLcpqpgVTPDPADLRQQLGQHLAE----YMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK07059 491 VPDEHSGEAVKLFV-----VKKDPALTEEDVKAFCKErltnYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
2757-3094 |
5.59e-23 |
|
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: 103.12 E-value: 5.59e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2757 VIYTSGSTGKPKGVMVEHANMVnfLCSMRKEP--GIAQEDVLLGVTSLsFDISILEIFLPLLN--GARLILATQAQAADA 2832
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLI--AANLQLIHamGLTEADVYLNMLPL-FHIAGLNLALATFHagGANVVMEKFDPAEAL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2833 QqlamLIERHAVSFMQATPSTWRMLVELRDfALPPGFKAL--CGGEALPENLAtaLLQKVT--TLWNLYGPTETTiwstl 2908
Cdd:cd17637 82 E----LIEEEKVTLMGSFPPILSNLLDAAE-KSGVDLSSLrhVLGLDAPETIQ--RFEETTgaTFWSLYGQTETS----- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2909 nGLTTPTPY------IGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDpfsgapearMYK 2982
Cdd:cd17637 150 -GLVTLSPYrerpgsAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG---------WHH 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2983 TGDLGRWLPDGTLEYLGRNDFQ--VKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPAD 3060
Cdd:cd17637 220 TGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPGATLTADE 299
|
330 340 350
....*....|....*....|....*....|....
gi 641744967 3061 LRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDR 3094
Cdd:cd17637 300 LIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
619-960 |
6.02e-23 |
|
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: 103.12 E-value: 6.02e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 619 VIYTSGSTGRPKGVMVAHRNVI------NLATGLH------TLLALDHPSriALNASI-VFDASVKNwiqllsghtlVLV 685
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIaanlqlIHAMGLTeadvylNMLPLFHIA--GLNLALaTFHAGGAN----------VVM 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 686 PdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAisPAVWSRLQSLSDTRFINVYGPTE 765
Cdd:cd17637 73 E---KFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDA--PETIQRFEETTGATFWSLYGQTE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 766 ctvdaTACVVD----RTQPlPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFipdpfsad 841
Cdd:cd17637 148 -----TSGLVTlspyRERP-GSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTF-------- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 842 paaR--IYKTGDLARWLPDGNIDYLGRNDFQ--IKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDsPGDTRLVAYLCA- 916
Cdd:cd17637 214 ---RngWHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPD-PKWGEGIKAVCVl 289
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 641744967 917 RPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDR 960
Cdd:cd17637 290 KPGATLTADELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
2625-3097 |
6.27e-23 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 106.22 E-value: 6.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2625 VVFGEA----SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLD 2700
Cdd:PLN02330 45 VAFVEAvtgkAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2701 DAKPVALISQSAHLGIMNG-SLPVILLDDGETRPFDNEPDTPLDARKQGLTPRH-------LAYVIYTSGSTGKPKGVMV 2772
Cdd:PLN02330 125 AAGAKLIVTNDTNYGKVKGlGLPVIVLGEEKIEGAVNWKELLEAADRAGDTSDNeeilqtdLCALPFSSGTTGISKGVML 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2773 EHANMVNFLCS--MRKEPGIAQEDVLLGVTSLSFDISILEI-FLPLLNGARLILATQAQAADAQQLAMlieRHAVSFMQA 2849
Cdd:PLN02330 205 THRNLVANLCSslFSVGPEMIGQVVTLGLIPFFHIYGITGIcCATLRNKGKVVVMSRFELRTFLNALI---TQEVSFAPI 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2850 TPSTWRMLVE---LRDFALPP-GFKALCGGEA-LPENLATALLQKV--TTLWNLYGPTETTIWStlngLTTPTPYIGHPI 2922
Cdd:PLN02330 282 VPPIILNLVKnpiVEEFDLSKlKLQAIMTAAApLAPELLTAFEAKFpgVQVQEAYGLTEHSCIT----LTHGDPEKGHGI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2923 A----------NTQIYILDAQ-GRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLP 2991
Cdd:PLN02330 358 AkknsvgfilpNLEVKFIDPDtGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW--------LHTGDIGYIDD 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2992 DGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAE 3071
Cdd:PLN02330 430 DGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAH 509
|
490 500
....*....|....*....|....*.
gi 641744967 3072 YMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PLN02330 510 YKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
2625-3094 |
1.03e-22 |
|
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: 104.45 E-value: 1.03e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2625 VVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKP 2704
Cdd:cd05914 1 LYYGGEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2705 VALisqsahlgimngslpvillddgetrpFDNEPDtpldarkqgltprHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSM 2784
Cdd:cd05914 81 KAI--------------------------FVSDED-------------DVALINYTSGTTGNSKGVMLTYRNIVSNVDGV 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2785 RKEPGIAQEDVLLGVTSLSFDISILEIFL-PLLNGA-----------RLILATQAQAADAQQLAMLIERHAVSFMQATPS 2852
Cdd:cd05914 122 KEVVLLGKGDKILSILPLHHIYPLTFTLLlPLLNGAhvvfldkipsaKIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2853 T------WRMLVELRDF------------ALPPGFKALC-GGEALPENLATALLQKVTTLWNLYGPTET------TIWST 2907
Cdd:cd05914 202 LtlkkfkFKLAKKINNRkirklafkkvheAFGGNIKEFViGGAKINPDVEEFLRTIGFPYTIGYGMTETapiisySPPNR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2908 LNGLTTptpyiGHPIANTQIYILDAQgrvvPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLG 2987
Cdd:cd05914 282 IRLGSA-----GKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW--------FHTGDLG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2988 RWLPDGTLEYLGR-NDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREdspgdKRLVAYLLAQPDTVLEPADLRQRLS 3066
Cdd:cd05914 345 KIDAEGYLYIRGRkKEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQE-----KKLVALAYIDPDFLDVKALKQRNII 419
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 641744967 3067 EGVAEYMIPSAFVTLDA-------------FPLTPNGKLDR 3094
Cdd:cd05914 420 DAIKWEVRDKVNQKVPNykkiskvkivkeeFEKTPKGKIKR 460
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1552-1977 |
1.05e-22 |
|
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: 104.99 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1552 QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGA----AYVPLdpGYPAerLAYMLDDASPV 1627
Cdd:cd17639 4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIpivtVYATL--GEDA--LIHSLNETECS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1628 ALLTQANqralltgdvprilldtadfshlSEDnphvpgldahhLAYVIYTSGSTGKPKGVMNSHR-------ALCNRLVw 1700
Cdd:cd17639 80 AIFTDGK----------------------PDD-----------LACIMYTSGSTGNPKGVMLTHGnlvagiaGLGDRVP- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1701 mqntYRLTPDDRVLQKTP----FSFDVSVWEFFWpllyGARL-----------VMARPDGhkDA---------------- 1749
Cdd:cd17639 126 ----ELLGPDDRYLAYLPlahiFELAAENVCLYR----GGTIgygsprtltdkSKRGCKG--DLtefkptlmvgvpaiwd 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1750 ----AYLAQLIERTGI--TTLHFVPSMLQQFVQWADADCACDSL-----R-------RVICSGEALPAELQQRFFARFNA 1811
Cdd:cd17639 196 tirkGVLAKLNPMGGLkrTLFWTAYQSKLKALKEGPGTPLLDELvfkkvRaalggrlRYMLSGGAPLSADTQEFLNIVLC 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1812 QLHNLYGPTE--AAIDVTFWACQPDDHrsfvpIGRPIANTQLYILDT--LG----QPVPlgvAGELHIGGVGVARGYLNR 1883
Cdd:cd17639 276 PVIQGYGLTEtcAGGTVQDPGDLETGR-----VGPPLPCCEIKLVDWeeGGystdKPPP---RGEILIRGPNVFKGYYKN 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1884 PDLTAERFIPDpfinqpgaRLYKTGDLARWLPDGSLEYLGRNDFQVKLR-GFRIELGEIEARLMQCPGVQEAVVVAredS 1962
Cdd:cd17639 348 PEKTKEAFDGD--------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYA---D 416
|
490
....*....|....*
gi 641744967 1963 PGDTRLVAYLCPQPG 1977
Cdd:cd17639 417 PDKSYPVAIVVPNEK 431
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
615-960 |
1.42e-22 |
|
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: 101.71 E-value: 1.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 615 HLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWIQLL-SGHTLVLVPdalRADA 693
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALyLGGTFIGQR---KFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 694 HQLWRYFARHAVDLFDCTPVQLQWLLDAGlgsDPAYQPAQVLIGGEAISPAVWSRLQSLS-DTRFINVYGPTECTVdATA 772
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALARTL---EPESKIKSIFSSGQKLFESTKKKLKNIFpKANLIEFYGTSELSF-ITY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 773 CVVDRTQPLPTIGKPLANTRLYILDAQDqpvpiGVTGELHIGGAGVARGYLHRPDLTAERFipdpfsadpaariYKTGDL 852
Cdd:cd17633 154 NFNQESRPPNSVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW-------------MSVGDI 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 853 ARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARpdaELHPAALRQQLA 932
Cdd:cd17633 216 GYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGD---KLTYKQLKRFLK 292
|
330 340
....*....|....*....|....*...
gi 641744967 933 ASLADYMIPSAFVTLDALPLTPNGKLDR 960
Cdd:cd17633 293 QKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2756-3093 |
1.52e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 102.46 E-value: 1.52e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2756 YVIYTSGSTGKPKGVMVEH----------ANMVNFLCSMRKEPGIAQED----VLLGVTSLSFDISILEIFLPLLNGARL 2821
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQedifrmlmggADFGTGEFTPSEDAHKAAAAaagtVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2822 ILATQAQAADAQQLamLIERHAVSFMQ------ATPstwrMLVELRD---FALPPGFKALCGGEALPENLATALLQKV-- 2890
Cdd:cd05924 87 VLPDDRFDPEEVWR--TIEKHKVTSMTivgdamARP----LIDALRDagpYDLSSLFAISSGGALLSPEVKQGLLELVpn 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2891 TTLWNLYGPTETTiwSTLNGLTTPTPYIGHP--IANTQIYILDAQGRVVPLGVAGEIHIAGAGVV-RGYLGRPDLTAERF 2967
Cdd:cd05924 161 ITLVDAFGSSETG--FTGSGHSAGSGPETGPftRANPDTVVLDDDGRVVPPGSGGVGWIARRGHIpLGYYGDEAKTAETF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2968 ITdpfsgAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAY 3047
Cdd:cd05924 239 PE-----VDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQEVVAV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 641744967 3048 LLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLD 3093
Cdd:cd05924 314 VQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1537-2016 |
1.58e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 104.71 E-value: 1.58e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1537 QAARTPDTTAVLFED--QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPA 1614
Cdd:PRK13390 6 HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1615 ERLAYMLDDASPVALLTQANQRALLT---GDVP-RILLDT-----ADF-SHLSEDNPhvPGLDAHHLAYVIYTSGSTGKP 1684
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAALDGLAAkvgADLPlRLSFGGeidgfGSFeAALAGAGP--RLTEQPCGAVMLYSSGTTGFP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1685 KGVMNShraLCNRLVwmqntyrLTPDDRVLQKTPFSFDVSVWEFFW---------PLLY-------GARLVMARpdgHKD 1748
Cdd:PRK13390 164 KGIQPD---LPGRDV-------DAPGDPIVAIARAFYDISESDIYYssapiyhaaPLRWcsmvhalGGTVVLAK---RFD 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1749 AAYLAQLIERTGITTLHFVPSMLQQFVQW-ADADCACD--SLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEA--- 1822
Cdd:PRK13390 231 AQATLGHVERYRITVTQMVPTMFVRLLKLdADVRTRYDvsSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAhgm 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1823 -AIDVTFWACQPDDhrsfvpIGRPIANTqLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAErfipdpfINQPG 1901
Cdd:PRK13390 311 tFIDSPDWLAHPGS------VGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA-------AQHPA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1902 ARLYKT-GDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTP 1980
Cdd:PRK13390 377 HPFWTTvGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRG 456
|
490 500 510
....*....|....*....|....*....|....*....
gi 641744967 1981 DPADLRQQLG---QHLAEYMVPGAFVTLDAFPLTPNGKL 2016
Cdd:PRK13390 457 SDELARELIDytrSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
619-958 |
2.09e-22 |
|
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: 101.42 E-value: 2.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 619 VIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVK-NWIQ-LLSGHTlvLVPDALrADAHQL 696
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKaGIVAcLLTGAT--VVPVAV-FDVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 697 WRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAISPAVW-SRLQS-LSDTRFINVYGPTECTVdATACV 774
Cdd:cd17638 82 LEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELvRRMRSeLGFETVLTAYGLTEAGV-ATMCR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 775 V--DRTQPLPTIGKPLANTRLYILDAqdqpvpigvtGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDL 852
Cdd:cd17638 161 PgdDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW--------LHTGDV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 853 ARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLA 932
Cdd:cd17638 223 GELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAWCR 302
|
330 340
....*....|....*....|....*.
gi 641744967 933 ASLADYMIPSAFVTLDALPLTPNGKL 958
Cdd:cd17638 303 ERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
499-963 |
2.32e-22 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 104.54 E-value: 2.32e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLI-ALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQ 577
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 578 SAQVAQLNST-LPTVLL------DTPAAAACP-------DTNPVVQGLHAAH-LAYVIYTSGSTGRPKGVMVAHRNVINL 642
Cdd:PLN02574 147 PENVEKLSPLgVPVIGVpenydfDSKRIEFPKfyelikeDFDFVPKPVIKQDdVAAIMYSSGTTGASKGVVLTHRNLIAM 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 643 atgLHTLLALDHPSRIALNASIVFDASVKNW---------IQLLS-GHTLVLVPdalRADAHQLWRYFARHAVDLFDCTP 712
Cdd:PLN02574 227 ---VELFVRFEASQYEYPGSDNVYLAALPMFhiyglslfvVGLLSlGSTIVVMR---RFDASDMVKVIDRFKVTHFPVVP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 713 VQLQWLLDA--GLGSDPAYQPAQVLIGGEAIS-PAVWSRLQSLSDTRFINVYGPTECTVDATACV-VDRTQPLPTIGKPL 788
Cdd:PLN02574 301 PILMALTKKakGVCGEVLKSLKQVSCGAAPLSgKFIQDFVQTLPHVDFIQGYGMTESTAVGTRGFnTEKLSKYSSVGLLA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 789 ANTRLYILDAQDQP-VPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLGRN 867
Cdd:PLN02574 381 PNMQAKVVDWSTGClLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW--------LRTGDIAYFDEDGYLYIVDRL 452
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 868 DFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTL 947
Cdd:PLN02574 453 KEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRKVVFV 532
|
490
....*....|....*.
gi 641744967 948 DALPLTPNGKLDRKAL 963
Cdd:PLN02574 533 QSIPKSPAGKILRREL 548
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
496-941 |
2.81e-22 |
|
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: 103.20 E-value: 2.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 496 DQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALL 575
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 576 tqsaqvaqlnstlptvlldtpaaaacpdtnpvvqglhaAHLAYVIYTSGSTGRPKGVMVAHRNVINLATG---------- 645
Cdd:cd05940 81 --------------------------------------VDAALYIYTSGTTGLPKAAIISHRRAWRGGAFfagsggalps 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 646 --LHTLLALDHPsrialNASIVFDASVknwiqLLSGHTLVLvpdALRADAHQLWRYFARHavdlfDCTPVQ-----LQWL 718
Cdd:cd05940 123 dvLYTCLPLYHS-----TALIVGWSAC-----LASGATLVI---RKKFSASNFWDDIRKY-----QATIFQyigelCRYL 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 719 LDaglgsdpayQPAQV--------LIGGEAISPAVWSRLQslsdTRFiNV------YGPTECT-----VDATACVVDRTQ 779
Cdd:cd05940 185 LN---------QPPKPterkhkvrMIFGNGLRPDIWEEFK----ERF-GVpriaefYAATEGNsgfinFFGKPGAIGRNP 250
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 780 PLPTIGKPLANTRlYILDAQD---------QPVPIGVTGEL--HIGGAGVARGYLhRPDLTAERFIPDPFSADPAAriYK 848
Cdd:cd05940 251 SLLRKVAPLALVK-YDLESGEpirdaegrcIKVPRGEPGLLisRINPLEPFDGYT-DPAATEKKILRDVFKKGDAW--FN 326
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 849 TGDLARWLPDGNIDYLGR--NDFQIKvrGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRL-VAYLCARPDAELHPA 925
Cdd:cd05940 327 TGDLMRLDGEGFWYFVDRlgDTFRWK--GENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAgMAAIVLQPNEEFDLS 404
|
490
....*....|....*.
gi 641744967 926 ALRQQLAASLADYMIP 941
Cdd:cd05940 405 ALAAHLEKNLPGYARP 420
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
2624-3100 |
3.91e-22 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 103.24 E-value: 3.91e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2624 AVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAK 2703
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2704 PVALIsqsAHLGIMNG-------SLPVILL--------------DDGETRPFDNEPDTPLDARK--QGLTPRHLAYVIYT 2760
Cdd:PRK12406 84 ARVLI---AHADLLHGlasalpaGVTVLSVptppeiaaayrispALLTPPAGAIDWEGWLAQQEpyDGPPVPQPQSMIYT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2761 SGSTGKPKGVmvehanmvnflcsmRKEPG-----IAQEDVLLGVTSLSFDISILeIFLPLLN-------------GARLI 2822
Cdd:PRK12406 161 SGTTGHPKGV--------------RRAAPtpeqaAAAEQMRALIYGLKPGIRAL-LTGPLYHsapnayglragrlGGVLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2823 LATQAQAADAQQlamLIERHAVSFMQATPStwrMLVELRDfaLPPGFKA----------LCGGEALPENLATALLQkvtt 2892
Cdd:PRK12406 226 LQPRFDPEELLQ---LIERHRITHMHMVPT---MFIRLLK--LPEEVRAkydvsslrhvIHAAAPCPADVKRAMIE---- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2893 lW------NLYGPTET---TIWSTLNGLTTPTPyIGHPIANTQIYILDAQGRVVPLGVAGEI--HIAGAGVVRgYLGRPD 2961
Cdd:PRK12406 294 -WwgpviyEYYGSTESgavTFATSEDALSHPGT-VGKAAPGAELRFVDEDGRPLPQGEIGEIysRIAGNPDFT-YHNKPE 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2962 LTAE----RFITdpfsgapearmykTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIARED 3037
Cdd:PRK12406 371 KRAEidrgGFIT-------------SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPD 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 3038 SPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAP 3100
Cdd:PRK12406 438 AEFGEALMAVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
2611-3100 |
4.57e-22 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 103.30 E-value: 4.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2611 LFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTY 2690
Cdd:PRK13382 48 GFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSF 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2691 PVERLRYMLDDAKPVALISQSAHLGimngSLPVILLDDGETRPFDNEPDTPLDARKQGL-----------TPRHLAYVIY 2759
Cdd:PRK13382 128 AGPALAEVVTREGVDTVIYDEEFSA----TVDRALADCPQATRIVAWTDEDHDLTVEVLiaahagqrpepTGRKGRVILL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2760 TSGSTGKPKGVMVEHANMVNFLCS-MRKEPGIAQEDVLLgVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQlamL 2838
Cdd:PRK13382 204 TSGTTGTPKGARRSGPGGIGTLKAiLDRTPWRAEEPTVI-VAPMFHAWGFSQLVLAASLACTIVTRRRFDPEATLD---L 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2839 IERHAVSFMQATPSTWRMLVELRDFALPP----GFK-ALCGGEALPENLATALLQKV-TTLWNLYGPTETTIWSTLN--G 2910
Cdd:PRK13382 280 IDRHRATGLAVVPVMFDRIMDLPAEVRNRysgrSLRfAAASGSRMRPDVVIAFMDQFgDVIYNNYNATEAGMIATATpaD 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2911 LTTPTPYIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYL-GRPDLTAERFITdpfsgapearmykTGDLGRW 2989
Cdd:PRK13382 360 LRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTsGSTKDFHDGFMA-------------SGDVGYL 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2990 LPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGV 3069
Cdd:PRK13382 427 DENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETLKQHVRDNL 506
|
490 500 510
....*....|....*....|....*....|.
gi 641744967 3070 AEYMIPSAFVTLDAFPLTPNGKLDRKALPAP 3100
Cdd:PRK13382 507 ANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
2163-2509 |
4.65e-22 |
|
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: 102.07 E-value: 4.65e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2163 PLAPLQEGILFHHllqeQGDTYLLRSMVAFTHRER----LDAFLSALQQVIDRHDILRTAVCWQDLSQPVQVVWRQAILP 2238
Cdd:cd19539 3 PLSFAQERLWFID----QGEDGGPAYNIPGAWRLTgpldVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2239 INHF-EPTSPEDVLAQLQAH-TEPRTRRIDLSQAPLFRADIAHDPlQNEWLLALSFHHLISDHMTLALIVGEIRLLLQHQ 2316
Cdd:cd19539 79 LEVRdLSDPDSDRERRLEELlRERESRGFDLDEEPPIRAVLGRFD-PDDHVLVLVAHHTAFDAWSLDVFARDLAALYAAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2317 ADALPTPLP-----YRNFIA---QTLSVPNSAHE-AYFRDKLADVDEPTAPFGLLNVQGSGGDIHEARLVLDATLASAIR 2387
Cdd:cd19539 158 RKGPAAPLPelrqqYKEYAAwqrEALAAPRAAELlDFWRRRLRGAEPTALPTDRPRPAGFPYPGADLRFELDAELVAALR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2388 QQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRlaGAEGADRIMGMFINTLPLRISLADRGA-AEVVERTSHD 2466
Cdd:cd19539 238 ELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGR--NHPRFESTVGFFVNLLPLRVDVSDCATfRDLIARVRKA 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 641744967 2467 LMTLLEHEQAPlaLAQRCSGVAPPM-----PLFSTLLNYRHTQASSTD 2509
Cdd:cd19539 316 LVDAQRHQELP--FQQLVAELPVDRdagrhPLVQIVFQVTNAPAGELE 361
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
2609-3134 |
4.71e-22 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 104.27 E-value: 4.71e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2609 HELFEAQVACTPDAIAVVF---GEA-----SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLG----- 2675
Cdd:PRK07529 28 YELLSRAAARHPDAPALSFlldADPldrpeTWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGgeaag 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2676 ----------------ILKAGGA--YVPLDPTyP-------VERLRYMLDDAKPVALISQSAHLGIMNGSLPVILLDDGE 2730
Cdd:PRK07529 108 ianpinpllepeqiaeLLRAAGAkvLVTLGPF-PgtdiwqkVAEVLAALPELRTVVEVDLARYLPGPKRLAVPLIRRKAH 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2731 TRPFD------NEPDTPLDARKQgLTPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLsF 2804
Cdd:PRK07529 187 ARILDfdaelaRQPGDRLFSGRP-IGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPL-F 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2805 DI--SILEIFLPLLNGARLILATQA---QAADAQQLAMLIERHAVSFMQATPSTWRMLVelrdfALPPGFK-------AL 2872
Cdd:PRK07529 265 HVnaLLVTGLAPLARGAHVVLATPQgyrGPGVIANFWKIVERYRINFLSGVPTVYAALL-----QVPVDGHdisslryAL 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2873 CGGEALPENLATAlLQKVT--TLWNLYGPTETTIWSTLNGLTTP--TPYIGHPIANTQ--IYILDAQGRVV---PLGVAG 2943
Cdd:PRK07529 340 CGAAPLPVEVFRR-FEAATgvRIVEGYGLTEATCVSSVNPPDGErrIGSVGLRLPYQRvrVVILDDAGRYLrdcAVDEVG 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2944 EIHIAGAGVVRGYLgRPDLTAERFItdpfsgapEARMYKTGDLGRWLPDGTLEYLGRndfqVK---VR-GFRIELGEIET 3019
Cdd:PRK07529 419 VLCIAGPNVFSGYL-EAAHNKGLWL--------EDGWLNTGDLGRIDADGYFWLTGR----AKdliIRgGHNIDPAAIEE 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3020 RLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAE-YMIPSAFVTLDAFPLTPNGKLDRKALp 3098
Cdd:PRK07529 486 ALLRHPAVALAAAVGRPDAHAGELPVAYVQLKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGKIFKPAL- 564
|
570 580 590
....*....|....*....|....*....|....*.
gi 641744967 3099 apdQSAMATRGYEApqgdlehALAQIWQTLLGVERV 3134
Cdd:PRK07529 565 ---RRDAIRRVLRA-------ALRDAGVEAEVVDVV 590
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
486-957 |
5.50e-22 |
|
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: 103.89 E-value: 5.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 486 TPEAIAVLF-----EDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPA- 559
Cdd:cd05943 81 DADDPAAIYaaedgERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGVp 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 560 ---ERLAYIlddaAPVALLT------------QSAQVAQLNSTLPT----VLLDTPAAAACPDTNPVVQGLH-------- 612
Cdd:cd05943 161 gvlDRFGQI----EPKVLFAvdaytyngkrhdVREKVAELVKGLPSllavVVVPYTVAAGQPDLSKIAKALTledflatg 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 613 -----------AAHLAYVIYTSGSTGRPKGVMvaHRnvinlATGlhTLLalDHPSRIALNASI-----VFDASVKNWIQ- 675
Cdd:cd05943 237 aagelefeplpFDHPLYILYSSGTTGLPKCIV--HG-----AGG--TLL--QHLKEHILHCDLrpgdrLFYYTTCGWMMw 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 676 ------LLSGHTLVLV---PdaLRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLgsdpayQPA---------QVLIG 737
Cdd:cd05943 306 nwlvsgLAVGATIVLYdgsP--FYPDTNALWDLADEEGITVFGTSAKYLDALEKAGL------KPAethdlsslrTILST 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 738 G------------EAISPAVWsrLQSLSdtrfinvyGPTectvDATACVV--DRTQPL--PTIGKPLANTRLYILDAQDQ 801
Cdd:cd05943 378 GsplkpesfdyvyDHIKPDVL--LASIS--------GGT----DIISCFVggNPLLPVyrGEIQCRGLGMAVEAFDEEGK 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 802 PVpIGVTGELHIggagvARGYLHRP-----DLTAERFIPDPFSADPAarIYKTGDLARWLPDGNIDYLGRNDFQIKVRGF 876
Cdd:cd05943 444 PV-WGEKGELVC-----TKPFPSMPvgfwnDPDGSRYRAAYFAKYPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGV 515
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 877 RIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPA---ALRQQLAASLADYMIPSAFVTLDALPLT 953
Cdd:cd05943 516 RIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDElrkRIRSTIRSALSPRHVPAKIIAVPDIPRT 595
|
....
gi 641744967 954 PNGK 957
Cdd:cd05943 596 LSGK 599
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
483-852 |
5.81e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 103.48 E-value: 5.81e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEAIAVLFED---------QHLTYRELNRRANQLAHHLIALGVqPDDRVALCVERSLEMMVGLLGILKAGAAYVPM 553
Cdd:PRK05850 11 ASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAGLIAVPL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 554 DPAYPA---ERLAYILDDAAPVALLTQSA---------QVAQLNSTLPTVLLDTPAAAACPDTNPVVQGLHAAhlAYVIY 621
Cdd:PRK05850 90 SVPQGGahdERVSAVLRDTSPSVVLTTSAvvddvteyvAPQPGQSAPPVIEVDLLDLDSPRGSDARPRDLPST--AYLQY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 622 TSGSTGRPKGVMVAHRNVI-NLATGLHTLLAlDHPSRIALNASIVfdasvkNW--------------IQLLSGHTLVLV- 685
Cdd:PRK05850 168 TSGSTRTPAGVMVSHRNVIaNFEQLMSDYFG-DTGGVPPPDTTVV------SWlpfyhdmglvlgvcAPILGGCPAVLTs 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 686 PDA-LRADA---HQLWRYfaRHAvdlFDCTPvQLQWLLDAGLGSD---PAYQPAQVLI---GGEAISPAVWSRLQ----- 750
Cdd:PRK05850 241 PVAfLQRPArwmQLLASN--PHA---FSAAP-NFAFELAVRKTSDddmAGLDLGGVLGiisGSERVHPATLKRFAdrfap 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 751 -SLSDTRFINVYGPTECTV------------------------DATACVVDRTQPLPTIGKPLANTrLYILDAQDQ-PVP 804
Cdd:PRK05850 315 fNLRETAIRPSYGLAEATVyvatrepgqppesvrfdyeklsagHAKRCETGGGTPLVSYGSPRSPT-VRIVDPDTCiECP 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 641744967 805 IGVTGELHIGGAGVARGYLHRPDLTAERF---IPDPFSADPAARIYKTGDL 852
Cdd:PRK05850 394 AGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPGTPEGPWLRTGDL 444
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
2620-3000 |
7.00e-22 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 103.05 E-value: 7.00e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEA----------SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPT 2689
Cdd:PRK09274 20 PDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLVDPG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2690 YPVERLRYMLDDAKPVALISQ-SAHLG---------------------IMNGSLPVILLDDGETRPFDnEPDTPLDArkq 2747
Cdd:PRK09274 100 MGIKNLKQCLAEAQPDAFIGIpKAHLArrlfgwgkpsvrrlvtvggrlLWGGTTLATLLRDGAAAPFP-MADLAPDD--- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2748 gltprhLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDV-------------LLGVTSLsfdisileifLP 2814
Cdd:PRK09274 176 ------MAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIdlptfplfalfgpALGMTSV----------IP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2815 --------LLNGARLILAtqaqaadaqqlamlIERHAVSFMQATPSTWRMLV---ELRDFALPPGFKALCGGEALP---- 2879
Cdd:PRK09274 240 dmdptrpaTVDPAKLFAA--------------IERYGVTNLFGSPALLERLGrygEANGIKLPSLRRVISAGAPVPiavi 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2880 ENLaTALLQKVTTLWNLYGPTE----TTIWST--LNGLTTPTPY-----IGHPIANTQIYILD---------AQGRVVPL 2939
Cdd:PRK09274 306 ERF-RAMLPPDAEILTPYGATEalpiSSIESReiLFATRAATDNgagicVGRPVDGVEVRIIAisdapipewDDALRLAT 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641744967 2940 GVAGEIHIAGAGVVRGYLGRPDLTAERFITDPfSGAPEARMyktGDLGRWLPDGTLEYLGR 3000
Cdd:PRK09274 385 GEIGEIVVAGPMVTRSYYNRPEATRLAKIPDG-QGDVWHRM---GDLGYLDAQGRLWFCGR 441
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
2619-3097 |
7.23e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 102.19 E-value: 7.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2619 TPDAIAVV--FGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLR 2696
Cdd:PRK09088 8 QPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2697 YMLDDAKPvALISQSAHLGimNGSLPVILLDDgetrpFDNEPDTPLDARKQGLTPRHLAYVIYTSGSTGKPKGVMVEHAN 2776
Cdd:PRK09088 88 ALLQDAEP-RLLLGDDAVA--AGRTDVEDLAA-----FIASADALEPADTPSIPPERVSLILFTSGTSGQPKGVMLSERN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2777 M----VNFLCSMRkepgIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPs 2852
Cdd:PRK09088 160 LqqtaHNFGVLGR----VDAHSSFLCDAPMFHIIGLITSVRPVLAVGGSILVSNGFEPKRTLGRLGDPALGITHYFCVP- 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2853 twRMLVELRDfalPPGFKA---------LCGGEALPENLATALLQKVTTLWNLYGPTETtiwSTLNGLTTPTPYI----- 2918
Cdd:PRK09088 235 --QMAQAFRA---QPGFDAaalrhltalFTGGAPHAAEDILGWLDDGIPMVDGFGMSEA---GTVFGMSVDCDVIrakag 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2919 --GHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLE 2996
Cdd:PRK09088 307 aaGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW--------FRTGDIARRDADGFFW 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2997 YLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPS 3076
Cdd:PRK09088 379 VVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWGEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPK 458
|
490 500
....*....|....*....|.
gi 641744967 3077 AFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK09088 459 HLRLVDALPRTASGKLQKARL 479
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
616-963 |
7.88e-22 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 104.62 E-value: 7.88e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 616 LAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIaLNASIVFDA---SVKNWIQLLSGHTLVLVPDALraD 692
Cdd:PRK08633 784 TATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVI-LSSLPFFHSfglTVTLWLPLLEGIKVVYHPDPT--D 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 693 AHQLWRYFARHAVDLFDCTPVQLQwlldaglgsdpAYQ------PAQ------VLIGGEAISPAVWSRLQSLSDTRFINV 760
Cdd:PRK08633 861 ALGIAKLVAKHRATILLGTPTFLR-----------LYLrnkklhPLMfaslrlVVAGAEKLKPEVADAFEEKFGIRILEG 929
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 761 YGPTECTVDATACVVDRTQP---------LPTIGKPLANTRLYILDAQD-QPVPIGVTGELHIGGAGVARGYLHRPDLTA 830
Cdd:PRK08633 930 YGATETSPVASVNLPDVLAAdfkrqtgskEGSVGMPLPGVAVRIVDPETfEELPPGEDGLILIGGPQVMKGYLGDPEKTA 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 831 ErFIPDPfsadPAARIYKTGDLARWLPDGNI---DYLGRndFQiKVRGFRIEAGEIESRLLRCPGVQDAVVIAR--EDSP 905
Cdd:PRK08633 1010 E-VIKDI----DGIGWYVTGDKGHLDEDGFLtitDRYSR--FA-KIGGEMVPLGAVEEELAKALGGEEVVFAVTavPDEK 1081
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 906 GDTRLVAyLCARPDAElhPAALRQQLAAS-LADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK08633 1082 KGEKLVV-LHTCGAED--VEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
2753-3094 |
8.92e-22 |
|
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: 99.02 E-value: 8.92e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2753 HLAYVIYTSGSTGKPKGVM-VEHANMVNFLCSmRKEPGIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAAD 2831
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYrSERSWIESFVCN-EDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQRKFNPKS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2832 AQQlamLIERHAVSFMQATPSTWRMLVeLRDFALPPGFKALCGGEALPENLATALLQ--KVTTLWNLYGPTETT-IWSTL 2908
Cdd:cd17633 80 WIR---KINQYNATVIYLVPTMLQALA-RTLEPESKIKSIFSSGQKLFESTKKKLKNifPKANLIEFYGTSELSfITYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2909 NGLTTPTPYIGHPIANTQIYILDAQGRVVplgvaGEIHIAGAGVVRGYLGRPDLTAERFITdpfsgapearmykTGDLGR 2988
Cdd:cd17633 156 NQESRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSEMVFSGYVRGGFSNPDGWMS-------------VGDIGY 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2989 WLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAylLAQPDTVLEPaDLRQRLSEG 3068
Cdd:cd17633 218 VDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA--LYSGDKLTYK-QLKRFLKQK 294
|
330 340
....*....|....*....|....*.
gi 641744967 3069 VAEYMIPSAFVTLDAFPLTPNGKLDR 3094
Cdd:cd17633 295 LSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
483-965 |
9.05e-22 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 103.57 E-value: 9.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 483 AEQTPEA----IAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYP 558
Cdd:PRK06060 11 AEQASEAgwydRPAFYAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELH 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 559 AERLAYILDDAAPVALLTQSA---QVAQLNSTLPTVLLDTPAAAACPDTNPVvqGLHAAhlAYVIYTSGSTGRPKGVMVA 635
Cdd:PRK06060 91 RDDHALAARNTEPALVVTSDAlrdRFQPSRVAEAAELMSEAARVAPGGYEPM--GGDAL--AYATYTSGTTGPPKAAIHR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 636 HRNVINLATGLHTLLALDHPSRIAL-NASIVFDASVKN--WIQLLSGHTLVLVPDALRADAHQLWRyfARHAVDLFDCTP 712
Cdd:PRK06060 167 HADPLTFVDAMCRKALRLTPEDTGLcSARMYFAYGLGNsvWFPLATGGSAVINSAPVTPEAAAILS--ARFGPSVLYGVP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 713 VQLQWLLDAgLGSDPAYQPAQVLIGGEAISPAVWSRL-QSLSDTRFINVYGPTECTVDATACVVDRTQPlPTIGKPLANT 791
Cdd:PRK06060 245 NFFARVIDS-CSPDSFRSLRCVVSAGEALELGLAERLmEFFGGIPILDGIGSTEVGQTFVSNRVDEWRL-GTLGRVLPPY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 792 RLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPD--LTAERFIpdpfsadpaariyKTGDLARWLPDGNIDYLGRNDF 869
Cdd:PRK06060 323 EIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWL-------------DTRDRVCIDSDGWVTYRCRADD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 870 QIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALR---QQLAASLADYMIPSAFVT 946
Cdd:PRK06060 390 TEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMRdlhRGLLNRLSAFKVPHRFAV 469
|
490
....*....|....*....
gi 641744967 947 LDALPLTPNGKLDRKALPA 965
Cdd:PRK06060 470 VDRLPRTPNGKLVRGALRK 488
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
2164-2397 |
1.69e-21 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 96.26 E-value: 1.69e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2164 LAPLQEGILFhhlLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCWQDlSQPVQVVWRQAILPINHFE 2243
Cdd:COG4908 1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED-GEPVQRIDPDADLPLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2244 PTS--PEDVLAQLQAH-TEPRTRRIDLSQAPLFRADIAHDpLQNEWLLALSFHHLISDHMTLALIVGEI----RLLLQHQ 2316
Cdd:COG4908 77 LSAlpEPEREAELEELvAEEASRPFDLARGPLLRAALIRL-GEDEHVLLLTIHHIISDGWSLGILLRELaalyAALLEGE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2317 ADALPT-PLPYRNFIA---QTLSVPN-SAHEAYFRDKLADVDEPTA-PFGLLNVQGSGGDIHEARLVLDATLASAIRQQA 2390
Cdd:COG4908 156 PPPLPElPIQYADYAAwqrAWLQSEAlEKQLEYWRQQLAGAPPVLElPTDRPRPAVQTFRGATLSFTLPAELTEALKALA 235
|
....*..
gi 641744967 2391 RHLGVSP 2397
Cdd:COG4908 236 KAHGATV 242
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
2620-3097 |
3.13e-21 |
|
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: 100.14 E-value: 3.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRyML 2699
Cdd:cd05929 6 LDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRAEAC-AI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALisqsahlgimngslPVILLDDGETRPFDNEPDTPLDARKQGLTPRHLAY--VIYTSGSTGKPKGVMVEH--- 2774
Cdd:cd05929 85 IEIKAAAL--------------VCGLFTGGGALDGLEDYEAAEGGSPETPIEDEAAGwkMLYSGGTTGRPKGIKRGLpgg 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2775 --ANMVNFLCSMRKEPGiaQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQlamLIERHAVSFMQATPS 2852
Cdd:cd05929 151 ppDNDTLMAAALGFGPG--ADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLR---LIERYRVTFAQFVPT 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2853 TW-RMLV---ELR---DFAlppGFKALCGGEA-----LPENLATALLQKVttlWNLYGPTE---TTIWSTLNGLTTPTPy 2917
Cdd:cd05929 226 MFvRLLKlpeAVRnayDLS---SLKRVIHAAApcppwVKEQWIDWGGPII---WEYYGGTEgqgLTIINGEEWLTHPGS- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2918 IGHPIANtQIYILDAQGRVVPLGVAGEIHIAGAGVVRgYLGRPDLTAERFITDPFSgapearmyKTGDLGRWLPDGTLEY 2997
Cdd:cd05929 299 VGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWS--------TLGDVGYLDEDGYLYL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2998 LGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPAD-------LRQRLSegva 3070
Cdd:cd05929 369 TDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTALaeeliafLRDRLS---- 444
|
490 500
....*....|....*....|....*..
gi 641744967 3071 EYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05929 445 RYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
2620-3099 |
3.63e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 100.46 E-value: 3.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALISQSAHLGIMNGSLPVILLDDGETrpfdnepdtpLDARKQGLTPRHLA---YVIYTSGSTGKPKGVMVehan 2776
Cdd:PRK13383 129 RAHHISTVVADNEFAERIAGADDAVAVIDPAT----------AGAEESGGRPAVAApgrIVLLTSGTTGKPKGVPR---- 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2777 mvnflcSMRKEPGIAQEDVLLGVTSLSFDiSILEIFLPLLNGARLILATQAQAADAQqlaMLIERH--------AVSFMQ 2848
Cdd:PRK13383 195 ------APQLRSAVGVWVTILDRTRLRTG-SRISVAMPMFHGLGLGMLMLTIALGGT---VLTHRHfdaeaalaQASLHR 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2849 ATPSTWRMLVELRDFALPPGFKA----------LCGGEALPENLATALLQKV-TTLWNLYGPTETTIwstlNGLTTPTPY 2917
Cdd:PRK13383 265 ADAFTAVPVVLARILELPPRVRArnplpqlrvvMSSGDRLDPTLGQRFMDTYgDILYNGYGSTEVGI----GALATPADL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2918 ------IGHPIANTQIYILDAQGRVVPLGVAGEIHIAGagvvrgylgrpDLTAERFiTDPFSGAPEARMYKTGDLGRWLP 2991
Cdd:PRK13383 341 rdapetVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGG-----------ELAGTRY-TDGGGKAVVDGMTSTGDMGYLDN 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2992 DGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAE 3071
Cdd:PRK13383 409 AGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPGSGVDAAQLRDYLKDRVSR 488
|
490 500
....*....|....*....|....*...
gi 641744967 3072 YMIPSAFVTLDAFPLTPNGKLDRKALPA 3099
Cdd:PRK13383 489 FEQPRDINIVSSIPRNPTGKVLRKELPG 516
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
2618-3094 |
5.33e-21 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 100.26 E-value: 5.33e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2618 CTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRY 2697
Cdd:PLN02860 19 LRGNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2698 MLDDAKPVALIS----QSAHLGIMNGSLPV----ILLDDGETR--PFDNEPDTPLDARKQGLTPRHLAY---------VI 2758
Cdd:PLN02860 99 AMLLVRPVMLVTdetcSSWYEELQNDRLPSlmwqVFLESPSSSvfIFLNSFLTTEMLKQRALGTTELDYawapddavlIC 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2759 YTSGSTGKPKGVMVEHANMVnfLCSMRKEP--GIAQEDVLLGVTSL------SFDISIL-----EIFLPLLNgARLILAT 2825
Cdd:PLN02860 179 FTSGTTGRPKGVTISHSALI--VQSLAKIAivGYGEDDVYLHTAPLchigglSSALAMLmvgacHVLLPKFD-AKAALQA 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2826 qaqaadaqqlamlIERHAVSFMQATPSTWRMLVEL-RDFALPPGF----KALCGGEALPENL--ATALLQKVTTLWNLYG 2898
Cdd:PLN02860 256 -------------IKQHNVTSMITVPAMMADLISLtRKSMTWKVFpsvrKILNGGGSLSSRLlpDAKKLFPNAKLFSAYG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2899 PTETTiwSTLNGLTTPTPYIGHPIANTQIYILDAQGRV--------------VPLGVA-------GEIHIAGAGVVRGYL 2957
Cdd:PLN02860 323 MTEAC--SSLTFMTLHDPTLESPKQTLQTVNQTKSSSVhqpqgvcvgkpaphVELKIGldessrvGRILTRGPHVMLGYW 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2958 GRPDLTAERFITDPFsgapearmYKTGDLGrWLPD-GTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIARE 3036
Cdd:PLN02860 401 GQNSETASVLSNDGW--------LDTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVP 471
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641744967 3037 DSPGDKRLVAYL--------------LAQPDTVLEPADLRQRLSE-GVAEYMIPSAFVTL-DAFPLTPNGKLDR 3094
Cdd:PLN02860 472 DSRLTEMVVACVrlrdgwiwsdnekeNAKKNLTLSSETLRHHCREkNLSRFKIPKLFVQWrKPFPLTTTGKIRR 545
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
482-958 |
7.57e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 99.31 E-value: 7.57e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 482 QAEQTPEAIAVLFED--QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPA 559
Cdd:PRK13390 6 HAQIAPDRPAVIVAEtgEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 560 ERLAYILDDAAPVALLTQSAQ---VAQLNSTLPTVL-----------LDTPAAAACPDTNPVVQGlhaahlAYVIYTSGS 625
Cdd:PRK13390 86 PEADYIVGDSGARVLVASAALdglAAKVGADLPLRLsfggeidgfgsFEAALAGAGPRLTEQPCG------AVMLYSSGT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 626 TGRPKGVM--VAHRNV-------INLATGLHTLLALDhpsrIALNASIVFDASVKNWIQLLS--GHTLVLvpdALRADAH 694
Cdd:PRK13390 160 TGFPKGIQpdLPGRDVdapgdpiVAIARAFYDISESD----IYYSSAPIYHAAPLRWCSMVHalGGTVVL---AKRFDAQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 695 QLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDATACV 774
Cdd:PRK13390 233 ATLGHVERYRITVTQMVPTMFVRLLKLDADVRTRYDVSSLRAVIHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHGMTF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 775 VDRTQPLP---TIGKPLANTrLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAErfipdpfSADPAARIYKT-G 850
Cdd:PRK13390 313 IDSPDWLAhpgSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA-------AQHPAHPFWTTvG 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 851 DLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSP-GD-TRLVAYLCA--RPDAELhPAA 926
Cdd:PRK13390 385 DLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEmGEqVKAVIQLVEgiRGSDEL-ARE 463
|
490 500 510
....*....|....*....|....*....|..
gi 641744967 927 LRQQLAASLADYMIPSAFVTLDALPLTPNGKL 958
Cdd:PRK13390 464 LIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
497-935 |
8.35e-21 |
|
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: 99.08 E-value: 8.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 497 QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLT 576
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 577 -----QSAQVAQLNSTLPTVLLDTPAAAACPDTNPVVQGLH----------AAHLAYVIYTSGSTGRPKGVM-------- 633
Cdd:cd05932 85 gklddWKAMAPGVPEGLISISLPPPSAANCQYQWDDLIAQHppleerptrfPEQLATLIYTSGTTGQPKGVMltfgsfaw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 634 VAHRNVINLATG----LHTLLALDH-PSRIALNAS-------IVFDASVKNWIQLLSGH--TLVL-VPdalradahQLWR 698
Cdd:cd05932 165 AAQAGIEHIGTEendrMLSYLPLAHvTERVFVEGGslyggvlVAFAESLDTFVEDVQRArpTLFFsVP--------RLWT 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 699 YFaRHAVdlFDCTPVQ-LQWLLD-------------AGLGSDpayqPAQVLIGGEA-ISPAV--WSRLQSLSdtrFINVY 761
Cdd:cd05932 237 KF-QQGV--QDKIPQQkLNLLLKipvvnslvkrkvlKGLGLD----QCRLAGCGSApVPPALleWYRSLGLN---ILEAY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 762 GPTECTVDATACVVDRTQpLPTIGKPLantrlyildaQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsad 841
Cdd:cd05932 307 GMTENFAYSHLNYPGRDK-IGTVGNAG----------PGVEVRISEDGEILVRSPALMMGYYKDPEATAEAFTADGF--- 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 842 paariYKTGDLARWLPDGNIDYLGRNDFQIKV-RGFRIEAGEIESRLLRCPGVQDAVVIARedspGDTRLVAyLCArPDA 920
Cdd:cd05932 373 -----LRTGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGS----GLPAPLA-LVV-LSE 441
|
490
....*....|....*...
gi 641744967 921 ELHPAAL---RQQLAASL 935
Cdd:cd05932 442 EARLRADafaRAELEASL 459
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
497-903 |
1.03e-20 |
|
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: 98.83 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 497 QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGaayVPMDPAYP---AERLAYILDDAAPVA 573
Cdd:cd17639 4 KYMSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTVYAtlgEDALIHSLNETECSA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 574 LLTQSaqvaqlnstlptvlldtpaaaaCPDTnpvvqglhaahLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLaLD 653
Cdd:cd17639 81 IFTDG----------------------KPDD-----------LACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRV-PE 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 654 HPSR----IA-LNASIVFDASVKNwIQLLSG------HTLVLVPDALR---ADAHQL-----------W-RYfaRHAV-- 705
Cdd:cd17639 127 LLGPddryLAyLPLAHIFELAAEN-VCLYRGgtigygSPRTLTDKSKRgckGDLTEFkptlmvgvpaiWdTI--RKGVla 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 706 ----------DLFD--------------CTPV---QLQWLLDAGLGSDPAYqpaqVLIGGEAISPavwsrlqslsDT-RF 757
Cdd:cd17639 204 klnpmgglkrTLFWtayqsklkalkegpGTPLldeLVFKKVRAALGGRLRY----MLSGGAPLSA----------DTqEF 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 758 INV--------YGPTEcTVdATACVVDRTQPLP-TIGKPLANTRLYILDAQ------DQPVPigvTGELHIGGAGVARGY 822
Cdd:cd17639 270 LNIvlcpviqgYGLTE-TC-AGGTVQDPGDLETgRVGPPLPCCEIKLVDWEeggystDKPPP---RGEILIRGPNVFKGY 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 823 LHRPDLTAERFIPDpfsadpaaRIYKTGDLARWLPDGNIDYLGRNDFQIKVR-GFRIEAGEIESRLLRCPGVQDAVVIAR 901
Cdd:cd17639 345 YKNPEKTKEAFDGD--------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYAD 416
|
..
gi 641744967 902 ED 903
Cdd:cd17639 417 PD 418
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1525-2021 |
1.17e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 99.36 E-value: 1.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1525 PHDALIHqLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLI-DLGVKPDDRIAICVERSLDMVIGLLAILKAGA 1603
Cdd:PRK08974 21 RYQSLVD-MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALFGILRAGM 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1604 AYVPLDPGYPAERLAYMLDDASPVALLTQAN--------------QRALLT--GD--------------------VPRIL 1647
Cdd:PRK08974 100 IVVNVNPLYTPRELEHQLNDSGAKAIVIVSNfahtlekvvfktpvKHVILTrmGDqlstakgtlvnfvvkyikrlVPKYH 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1648 LDTA----DFSHLSEDNPHV-PGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYR-LTPDDRVLQKTPFS- 1720
Cdd:PRK08974 180 LPDAisfrSALHKGRRMQYVkPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLANLEQAKAAYGpLLHPGKELVVTALPl 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1721 ---FDVSVWEFFWPLLYGARLVMARPdghKDAAYLAQLIER------TGITTLHfvpSMLQQFVQWADADCAcdSLRRVI 1791
Cdd:PRK08974 260 yhiFALTVNCLLFIELGGQNLLITNP---RDIPGFVKELKKypftaiTGVNTLF---NALLNNEEFQELDFS--SLKLSV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1792 CSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTfwaCQPDDHRSFV-PIGRPIANTQLYILDTLGQPVPLGVAGELH 1870
Cdd:PRK08974 332 GGGMAVQQAVAERWVKLTGQYLLEGYGLTECSPLVS---VNPYDLDYYSgSIGLPVPSTEIKLVDDDGNEVPPGEPGELW 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1871 IGGVGVARGYLNRPDLTAErFIPDPFInqpgarlyKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPG 1950
Cdd:PRK08974 409 VKGPQVMLGYWQRPEATDE-VIKDGWL--------ATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPK 479
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641744967 1951 VQEAVVVARE-DSPGDTRLVAYLCPQPGVTPDpaDLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK08974 480 VLEVAAVGVPsEVSGEAVKIFVVKKDPSLTEE--ELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
2752-3094 |
1.63e-20 |
|
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: 95.79 E-value: 1.63e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2752 RHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEP-GIAQEDVLLGVTSLSFDISILEIFLPLL-NGARLILATQAQA 2829
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTFFAVPDILQKEGlNWVVGDVTYLPLPATHIGGLWWILTCLIhGGLCVTGGENTTY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2830 ADAQQLamlIERHAVSFMQATPSTWRMLVELRDFALPPGFKALC---GGE-ALPENLATALLQKVTTLWNLYGPTETTIW 2905
Cdd:cd17635 81 KSLFKI---LTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLigyGGSrAIAADVRFIEATGLTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2906 STL---NGLTTPTPyIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmyK 2982
Cdd:cd17635 158 LCLptdDDSIEINA-VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV---------N 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2983 TGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQP-DTVLEPADL 3061
Cdd:cd17635 228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAeLDENAIRAL 307
|
330 340 350
....*....|....*....|....*....|...
gi 641744967 3062 RQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDR 3094
Cdd:cd17635 308 KHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
2630-3097 |
1.86e-20 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 98.68 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2630 ASLSYDELNRRANRLAHHLISF-GVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDD--AKPVA 2706
Cdd:PRK05677 48 KTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQFNDsgAKALV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2707 LISQSAHLgiMNGSLP------VILLDDGETRPFD-------------------NEPD----TPLDARKQGLT------- 2750
Cdd:PRK05677 128 CLANMAHL--AEKVLPktgvkhVIVTEVADMLPPLkrllinavvkhvkkmvpayHLPQavkfNDALAKGAGQPvteanpq 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2751 PRHLAYVIYTSGSTGKPKGVMVEHANMVnflcsmrkePGIAQEDVLLGVtSLSFDISILEIFLPLLNGARLILATQAQaa 2830
Cdd:PRK05677 206 ADDVAVLQYTGGTTGVAKGAMLTHRNLV---------ANMLQCRALMGS-NLNEGCEILIAPLPLYHIYAFTFHCMAM-- 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2831 daqqlaMLIERHAV--SFMQATPStwrMLVELRDF------ALPPGFKALCGGE--------ALPENLA--TALLQKVTT 2892
Cdd:PRK05677 274 ------MLIGNHNIliSNPRDLPA---MVKELGKWkfsgfvGLNTLFVALCNNEafrkldfsALKLTLSggMALQLATAE 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2893 LWNL---------YGPTETTIWSTLNGLTTPTP-YIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDL 2962
Cdd:PRK05677 345 RWKEvtgcaicegYGMTETSPVVSVNPSQAIQVgTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEA 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2963 TAERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDK 3042
Cdd:PRK05677 425 TDEILDSDGW--------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGE 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 3043 RLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK05677 497 AIKVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
2757-3093 |
2.41e-20 |
|
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: 95.06 E-value: 2.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2757 VIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLsFDISILEIFLP--LLNGARLILATQAQAADAQq 2834
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPL-FHIGTLMFTLAtfHAGGTNVFVRRVDAEEVLE- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2835 lamLIERHAVSFMQATPSTWRMLVELRDfALPPGFKALCGGEALPE--NLATALlqkvTTLWN----LYGPTETTIWSTL 2908
Cdd:cd17636 83 ---LIEAERCTHAFLLPPTIDQIVELNA-DGLYDLSSLRSSPAAPEwnDMATVD----TSPWGrkpgGYGQTEVMGLATF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2909 NGLTTPTPYI-GHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFitdpfsgapEARMYKTGDLG 2987
Cdd:cd17636 155 AALGGGAIGGaGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT---------RGGWHHTNDLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2988 RWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSE 3067
Cdd:cd17636 226 RREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVLKPGASVTEAELIEHCRA 305
|
330 340
....*....|....*....|....*.
gi 641744967 3068 GVAEYMIPSAFVTLDAFPLTPNGKLD 3093
Cdd:cd17636 306 RIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
467-936 |
2.72e-20 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 98.41 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 467 ADFPREMLiqQRFEAQAEQTPEAIAVLFED-----QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLL 541
Cdd:PRK08180 35 GDYPRRLT--DRLVHWAQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLAL 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 542 GILKAGAAYVPMDPAYPA-----ERLAYIL----------DDAAPVA-------------LLTQSAQVAQLNSTLPTvLL 593
Cdd:PRK08180 113 AAMYAGVPYAPVSPAYSLvsqdfGKLRHVLelltpglvfaDDGAAFAralaavvpadvevVAVRGAVPGRAATPFAA-LL 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 594 DTPAAAAcpdtnpvVQGLHAA----HLAYVIYTSGSTGRPKGVMVAHRNV-INLATGLHTL--LALDHPSRI-------- 658
Cdd:PRK08180 192 ATPPTAA-------VDAAHAAvgpdTIAKFLFTSGSTGLPKAVINTHRMLcANQQMLAQTFpfLAEEPPVLVdwlpwnht 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 659 ---ALNASIV------------------FDASVKNwIQLLSGHTLVLVP-------DALRADAHQLWRYFARhaVDLFdc 710
Cdd:PRK08180 265 fggNHNLGIVlynggtlyiddgkptpggFDETLRN-LREISPTVYFNVPkgwemlvPALERDAALRRRFFSR--LKLL-- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 711 tpvqlqwlldaglgsdpAYqpaqvliGGEAISPAVWSRLQSLS------DTRFINVYGPTECTVDATACvvdrTQPLPT- 783
Cdd:PRK08180 340 -----------------FY-------AGAALSQDVWDRLDRVAeatcgeRIRMMTGLGMTETAPSATFT----TGPLSRa 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 784 --IGKPLANTRLYIldaqdqpVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWL----P 857
Cdd:PRK08180 392 gnIGLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY--------YRSGDAVRFVdpadP 456
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 858 DGNIDYLGR--NDFQIkVRGFRIEAGEIESRLLR--CPGVQDAVVIA--RE--------DSPGDTRLVAYLCARPDAE-L 922
Cdd:PRK08180 457 ERGLMFDGRiaEDFKL-SSGTWVSVGPLRARAVSagAPLVQDVVITGhdRDeigllvfpNLDACRRLAGLLADASLAEvL 535
|
570
....*....|....
gi 641744967 923 HPAALRQQLAASLA 936
Cdd:PRK08180 536 AHPAVRAAFRERLA 549
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1533-1924 |
2.78e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 98.09 E-value: 2.78e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1533 LVEDQAARTPDTTAVLFED---------QHLTYDALNRRANQLAHHLIDLGVkPDDRIAICVERSLDMVIGLLAILKAGA 1603
Cdd:PRK05850 6 LLRERASLQPDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHGS-TGDRAVILAPQGLEYIVAFLGALQAGL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1604 AYVPLD---PGYPAERLAYMLDDASPVALLTQAN--------QRALLTGDVPRIL-LDTADFShlSEDNPHVPGLDAHHL 1671
Cdd:PRK05850 85 IAVPLSvpqGGAHDERVSAVLRDTSPSVVLTTSAvvddvteyVAPQPGQSAPPVIeVDLLDLD--SPRGSDARPRDLPST 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1672 AYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTY------RLTPDDRVLQKTPFSFDVS-VWEFFWPLLYGARLVMARPD 1744
Cdd:PRK05850 163 AYLQYTSGSTRTPAGVMVSHRNVIANFEQLMSDYfgdtggVPPPDTTVVSWLPFYHDMGlVLGVCAPILGGCPAVLTSPV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1745 G--HKDAAYLAQLIERTGittlhfVPSMLQQFV------QWADADCACDSLRRV--ICSG-EAL-PAELqQRF---FARF 1809
Cdd:PRK05850 243 AflQRPARWMQLLASNPH------AFSAAPNFAfelavrKTSDDDMAGLDLGGVlgIISGsERVhPATL-KRFadrFAPF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1810 NAQLHNL---YGPTEAAIDVT------------FWA----------CQPDDHRSFVPIGRPIANTqLYILD--TLGQpVP 1862
Cdd:PRK05850 316 NLRETAIrpsYGLAEATVYVAtrepgqppesvrFDYeklsaghakrCETGGGTPLVSYGSPRSPT-VRIVDpdTCIE-CP 393
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 1863 LGVAGELHIGGVGVARGYLNRPDLTAERF---IPDPFINQPGARLYKTGDLArWLPDGSLEYLGR 1924
Cdd:PRK05850 394 AGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSPGTPEGPWLRTGDLG-FISEGELFIVGR 457
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1566-2018 |
3.02e-20 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 97.95 E-value: 3.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1566 LAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQANQRA----LLTG 1641
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSSwyeeLQND 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1642 DVP----RILLDT-------ADFSHLSEDNPHVPGLDAHHLAY---------VIYTSGSTGKPKGVMNSHRALCnrlvwM 1701
Cdd:PLN02860 125 RLPslmwQVFLESpsssvfiFLNSFLTTEMLKQRALGTTELDYawapddavlICFTSGTTGRPKGVTISHSALI-----V 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLT-----PDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMArPDGHKDAAYlaQLIERTGITTLHFVPSMLQQFVQ 1776
Cdd:PLN02860 200 QSLAKIAivgygEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLL-PKFDAKAAL--QAIKQHNVTSMITVPAMMADLIS 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1777 WA---DADCACDSLRRVICSGEALPAELQQRFFARF-NAQLHNLYGPTEAAIDVTFWA-----CQPDDHRSFVPIGRPIA 1847
Cdd:PLN02860 277 LTrksMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFpNAKLFSAYGMTEACSSLTFMTlhdptLESPKQTLQTVNQTKSS 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1848 NTQLYILDTLGQPVP-----LGVAGELHIG-----GVGVARGYLNRPDLTAERFIPDPFINqpgarlykTGDLArWLPD- 1916
Cdd:PLN02860 357 SVHQPQGVCVGKPAPhvelkIGLDESSRVGriltrGPHVMLGYWGQNSETASVLSNDGWLD--------TGDIG-WIDKa 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1917 GSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLG------ 1990
Cdd:PLN02860 428 GNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLRDGWIWSDNEKENAKKnltlss 507
|
490 500 510
....*....|....*....|....*....|....*...
gi 641744967 1991 ---------QHLAEYMVPGAFVTL-DAFPLTPNGKLDR 2018
Cdd:PLN02860 508 etlrhhcreKNLSRFKIPKLFVQWrKPFPLTTTGKIRR 545
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
470-937 |
3.49e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 98.19 E-value: 3.49e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 470 PREMLIQQRFEAQAEQTPEAIAVLFEDQH------LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGI 543
Cdd:PRK12582 46 PYPRSIPHLLAKWAAEAPDRPWLAQREPGhgqwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 544 LKAGAAYVPMDPAYPA-----ERLAYILDDAAPVALLTQSAQ-----VAQLNSTLPTVLLDTPAA-----------AACP 602
Cdd:PRK12582 126 MQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPRVVFAQSGApfaraLAALDLLDVTVVHVTGPGegiasiafadlAATP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 603 DTNPVVQ---GLHAAHLAYVIYTSGSTGRPKGVMVAHR---NVINLATGLHTLLALDHPSrIALN---------ASIVFD 667
Cdd:PRK12582 206 PTAAVAAaiaAITPDTVAKYLFTSGSTGMPKAVINTQRmmcANIAMQEQLRPREPDPPPP-VSLDwmpwnhtmgGNANFN 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 668 ASvknwiqLLSGHTLVLvpDALRADAHQlwryFARHAVDLFDCTPV------QLQWLLDAGLGSDPAYQPA------QVL 735
Cdd:PRK12582 285 GL------LWGGGTLYI--DDGKPLPGM----FEETIRNLREISPTvygnvpAGYAMLAEAMEKDDALRRSffknlrLMA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 736 IGGEAISPAVWSRLQSLSDTR------FINVYGPTEcTVDATACVVDRTQPLPTIGKPLANTRLYIldaqdqpVPIGVTG 809
Cdd:PRK12582 353 YGGATLSDDLYERMQALAVRTtghripFYTGYGATE-TAPTTTGTHWDTERVGLIGLPLPGVELKL-------APVGDKY 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 810 ELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWL----PDGNIDYLGR--NDFQIKVrGFRIEAGEI 883
Cdd:PRK12582 425 EVRVKGPNVTPGYHKDPELTAAAFDEEGF--------YRLGDAARFVdpddPEKGLIFDGRvaEDFKLST-GTWVSVGTL 495
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 884 ESRLLRC--PGVQDAVViAREDSPGDTRLV-------AYLCARPDAELHPAALRQQLAASLAD 937
Cdd:PRK12582 496 RPDAVAAcsPVIHDAVV-AGQDRAFIGLLAwpnpaacRQLAGDPDAAPEDVVKHPAVLAILRE 557
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2632-3044 |
4.06e-20 |
|
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: 96.10 E-value: 4.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPV-ALISQ 2710
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVyAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2711 SAHlgimngslpvillddgetrpfdnePDTPLdarkqgltprhLAYviYTSGSTGKPKGVMVEHANM-VNFLCSMRkEPG 2789
Cdd:cd05974 81 NTH------------------------ADDPM-----------LLY--FTSGTTSKPKLVEHTHRSYpVGHLSTMY-WIG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2790 IAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVE--LRDFALPP 2867
Cdd:cd05974 123 LKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQqdLASFDVKL 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2868 gfKALCG-GEAL-PEnlataLLQKVTTLWNL-----YGPTETTIW-STLNGLTTPTPYIGHPIANTQIYILDAQGRVVPL 2939
Cdd:cd05974 203 --REVVGaGEPLnPE-----VIEQVRRAWGLtirdgYGQTETTALvGNSPGQPVKAGSMGRPLPGYRVALLDPDGAPATE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2940 G----VAGEIHiaGAGVVRGYLGRPDLTAerfitdpfsGAPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELG 3015
Cdd:cd05974 276 GevalDLGDTR--PVGLMKGYAGDPDKTA---------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPF 344
|
410 420
....*....|....*....|....*....
gi 641744967 3016 EIETRLARCHGVHDAVVIAredSPGDKRL 3044
Cdd:cd05974 345 ELESVLIEHPAVAEAAVVP---SPDPVRL 370
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1525-2001 |
4.77e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 97.81 E-value: 4.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1525 PHDALIHQLVEDQAARTPDTTAVLFEDQH------LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAI 1598
Cdd:PRK12582 46 PYPRSIPHLLAKWAAEAPDRPWLAQREPGhgqwrkVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1599 LKAGAAYVPLDPGYPA-----ERLAYMLDDASPVALLTQAN---QRALLT---GDVPRILLDTA----DFSHLSE--DNP 1661
Cdd:PRK12582 126 MQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPRVVFAQSGapfARALAAldlLDVTVVHVTGPgegiASIAFADlaATP 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1662 HVPGLDAHH-------LAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVlqktPFSFDVSVWEF------ 1728
Cdd:PRK12582 206 PTAAVAAAIaaitpdtVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPP----PVSLDWMPWNHtmggna 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1729 -FWPLLY-GARLVM--ARPdghkdaayLAQLIERTgITTLH--------FVP---SMLQQFVQWADADCAC--DSLRRVI 1791
Cdd:PRK12582 282 nFNGLLWgGGTLYIddGKP--------LPGMFEET-IRNLReisptvygNVPagyAMLAEAMEKDDALRRSffKNLRLMA 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1792 CSGEALPAELQQRFFARFNAQ------LHNLYGPTEAA--IDVTFWacqpdDHRSFVPIGRPIANTQLYIldtlgqpVPL 1863
Cdd:PRK12582 353 YGGATLSDDLYERMQALAVRTtghripFYTGYGATETAptTTGTHW-----DTERVGLIGLPLPGVELKL-------APV 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1864 GVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWL----PDGSLEYLGR--NDFqvKL-RGFRI 1936
Cdd:PRK12582 421 GDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF--------YRLGDAARFVdpddPEKGLIFDGRvaEDF--KLsTGTWV 490
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1937 ELGEIEARLMQ-CPGVQEAVVVAREDSPGDTRLV-------AYLCPQPGVTPDP--------ADLRQQLGQHLAEymVPG 2000
Cdd:PRK12582 491 SVGTLRPDAVAaCSPVIHDAVVAGQDRAFIGLLAwpnpaacRQLAGDPDAAPEDvvkhpavlAILREGLSAHNAE--AGG 568
|
.
gi 641744967 2001 A 2001
Cdd:PRK12582 569 S 569
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
2632-3097 |
6.41e-20 |
|
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: 96.58 E-value: 6.41e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLD--PTYP--------VERLRYMLDd 2701
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTvpPTYDepnarlrkLRHIWQLLG- 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2702 aKPVALISQSAHLGIMnGSLPVILLDDGETRPFDNEPDTPLDARKQGLTPRHLAYVIYTSGSTGKPKGVMVEHANMVNFL 2781
Cdd:cd05906 119 -SPVVLTDAELVAEFA-GLETLSGLPGIRVLSIEELLDTAADHDLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2782 CSMRKEPGIAQEDVLLG------VTSLSFdISILEIFLpllnGARLILATQAQAADAQQLAM-LIERHAVSFMQATPSTW 2854
Cdd:cd05906 197 AGKIQHNGLTPQDVFLNwvpldhVGGLVE-LHLRAVYL----GCQQVHVPTEEILADPLRWLdLIDRYRVTITWAPNFAF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2855 RMLVEL------RDFALPPGFKALCGGEALPENLATALLQ-------KVTTLWNLYGPTET---TIWS---TLNGLTTPT 2915
Cdd:cd05906 272 ALLNDLleeiedGTWDLSSLRYLVNAGEAVVAKTIRRLLRllepyglPPDAIRPAFGMTETcsgVIYSrsfPTYDHSQAL 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2916 PY--IGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGrWLPDG 2993
Cdd:cd05906 352 EFvsLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW--------FRTGDLG-FLDNG 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2994 TLEYLGRNDFQVKVRGFRIELGEIETRLARCHGV---HDAVVIAREDSPGDKRLVAYLL---AQPDTVLEPAD-LRQRLS 3066
Cdd:cd05906 423 NLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVepsFTAAFAVRDPGAETEELAIFFVpeyDLQDALSETLRaIRSVVS 502
|
490 500 510
....*....|....*....|....*....|....
gi 641744967 3067 E--GVA-EYMIPsafVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05906 503 RevGVSpAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
31-258 |
9.81e-20 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 91.25 E-value: 9.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 31 LAPLQEGILFhyqLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICWQGlHQPVQVVWRQAPLTVNTLT 110
Cdd:COG4908 1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEED-GEPVQRIDPDADLPLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 111 TTS---SDTVPAQLRAATDPSNHRLNLSNAPLLSAT---TAHDpvcgEWLLSLSIHHLISDHITQALIIDEI----RLLL 180
Cdd:COG4908 77 LSAlpePEREAELEELVAEEASRPFDLARGPLLRAAlirLGED----EHVLLLTIHHIISDGWSLGILLRELaalyAALL 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 181 EDRPEALP-KPLPYRNFIA----QILSVPLSEHEQYFRNRLADIDTPTA-PFDLVDVQGNGEDITEARLSLDSSLADALR 254
Cdd:COG4908 153 EGEPPPLPeLPIQYADYAAwqraWLQSEALEKQLEYWRQQLAGAPPVLElPTDRPRPAVQTFRGATLSFTLPAELTEALK 232
|
....
gi 641744967 255 RQAR 258
Cdd:COG4908 233 ALAK 236
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1519-2021 |
1.16e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 96.10 E-value: 1.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1519 ATEADFPHDALIHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLI-DLGVKPDDRIAICVERSLDMVIGLLA 1597
Cdd:PRK08751 16 AAEIDLEQFRTVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1598 ILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQAN-----QRALLTGDVPRI----LLDTADFSH------------- 1655
Cdd:PRK08751 96 VLRAGLTVVNVNPLYTPRELKHQLIDSGASVLVVIDNfgttvQQVIADTPVKQVittgLGDMLGFPKaalvnfvvkyvkk 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1656 ----------------LSEDNPH-VPGLDAHH--LAYVIYTSGSTGKPKGVMNSHRALCNRLV----WMQNTYRLTP-DD 1711
Cdd:PRK08751 176 lvpeyringairfreaLALGRKHsMPTLQIEPddIAFLQYTGGTTGVAKGAMLTHRNLVANMQqahqWLAGTGKLEEgCE 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1712 RVLQKTPFS--FDVSVWEFFWPLLYGARLVMARPdghKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADAD-CACDSLR 1788
Cdd:PRK08751 256 VVITALPLYhiFALTANGLVFMKIGGCNHLISNP---RDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDqIDFSSLK 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1789 RVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTFWACQPDDHRSfvPIGRPIANTQLYILDTLGQPVPLGVAGE 1868
Cdd:PRK08751 333 MTLGGGMAVQRSVAERWKQVTGLTLVEAYGLTETSPAACINPLTLKEYNG--SIGLPIPSTDACIKDDAGTVLAIGEIGE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1869 LHIGGVGVARGYLNRPDLTAERFIPDPFINqpgarlykTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQC 1948
Cdd:PRK08751 411 LCIKGPQVMKGYWKRPEETAKVMDADGWLH--------TGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 1949 PGVQE--AVVVAREDSpGDTRLVAYLCPQPGVTPDpaDLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK08751 483 PGVLEvaAVGVPDEKS-GEIVKVVIVKKDPALTAE--DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
2607-3099 |
1.27e-19 |
|
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: 96.41 E-value: 1.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2607 LIHELFEAQVACTPDAIAVVF-GE----ASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGG 2681
Cdd:cd05968 62 IVEQLLDKWLADTRTRPALRWeGEdgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2682 AYVPLDPTYPVERLRYMLDDAKPVALISQSahlGIMNGSLPVILLDDGET------------------RPFDNEPDTPL- 2742
Cdd:cd05968 142 IVVPIFSGFGKEAAATRLQDAEAKALITAD---GFTRRGREVNLKEEADKacaqcptvekvvvvrhlgNDFTPAKGRDLs 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2743 --------DARKQGLTPRHLAYVIYTSGSTGKPKGVMVEHANM-------VNFLCSMRkepgiaQEDVLLGVTSLSFDIS 2807
Cdd:cd05968 219 ydeeketaGDGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFplkaaqdMYFQFDLK------PGDLLTWFTDLGWMMG 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2808 ILEIFLPLLNGARLILATQAQAADAQQLAM-LIERHAVSFMQATPSTWRMLVELRDFALPPGFKA---LCGGEALPENL- 2882
Cdd:cd05968 293 PWLIFGGLILGATMVLYDGAPDHPKADRLWrMVEDHEITHLGLSPTLIRALKPRGDAPVNAHDLSslrVLGSTGEPWNPe 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2883 ------ATALLQKVTTLwNLYGPTETTIWSTLNGLTTPTPYIGH--PIANTQIYILDAQGRVVPlGVAGEIHIAGA--GV 2952
Cdd:cd05968 373 pwnwlfETVGKGRNPII-NYSGGTEISGGILGNVLIKPIKPSSFngPVPGMKADVLDESGKPAR-PEVGELVLLAPwpGM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2953 VRGYLGRPDltaeRFITDPFSGAPEARMYktGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVV 3032
Cdd:cd05968 451 TRGFWRDED----RYLETYWSRFDNVWVH--GDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAA 524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641744967 3033 IAREDSPGDKRLVAYLLAQPDtVLEPADLRQRLSEGVAEYM----IPSAFVTLDAFPLTPNGKLDRKALPA 3099
Cdd:cd05968 525 IGVPHPVKGEAIVCFVVLKPG-VTPTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMRRVIRA 594
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
499-960 |
1.52e-19 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 95.84 E-value: 1.52e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMD-PAYPAERLAYI------LDDAAP 571
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYIaqlrgmLASAQP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 572 VALLT---------QSAQVAQLNSTLPTVLLDTPAAAACPDTNPVvqglhAAHLAYVIYTSGSTGRPKGVMVAHRNVI-N 641
Cdd:PRK09192 130 AAIITpdellpwvnEATHGNPLLHVLSHAWFKALPEADVALPRPT-----PDDIAYLQYSSGSTRFPRGVIITHRALMaN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 642 LATGLHTLLALDHPSRIAlnasivfdasvkNWIQLLsgHTLVLVPDALRADAHQL------WRYFARHAvdlfdctpvqL 715
Cdd:PRK09192 205 LRAISHDGLKVRPGDRCV------------SWLPFY--HDMGLVGFLLTPVATQLsvdylpTRDFARRP----------L 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 716 QWL--------------------------------LD------AGLGSDPAyqPAQVLIG-GEAISPAvwsrlqSLSDTR 756
Cdd:PRK09192 261 QWLdlisrnrgtisysppfgyelcarrvnskdlaeLDlscwrvAGIGADMI--RPDVLHQfAEAFAPA------GFDDKA 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 757 FINVYGPTECT----------------VDATAC--------VVDRTQPLPTI---GKPLANTRLYILDAQDQPVPIGVTG 809
Cdd:PRK09192 333 FMPSYGLAEATlavsfsplgsgivveeVDRDRLeyqgkavaPGAETRRVRTFvncGKALPGHEIEIRNEAGMPLPERVVG 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 810 ELHIGGAGVARGYLHRPDlTAERFIPDPFsadpaariYKTGDLArWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLR 889
Cdd:PRK09192 413 HICVRGPSLMSGYFRDEE-SQDVLAADGW--------LDTGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQ 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 890 CPGVQ--DAVVIAREDSPGDTRLVAYLCARPDAELHpAALRQQLAASLadYMIP--SAFVTL---DALPLTPNGKLDR 960
Cdd:PRK09192 483 EPELRsgDAAAFSIAQENGEKIVLLVQCRISDEERR-GQLIHALAALV--RSEFgvEAAVELvppHSLPRTSSGKLSR 557
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
617-963 |
1.84e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 93.19 E-value: 1.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 617 AYVIYTSGSTGRPKGVMVAHRNVINLATGLHT--------LLALDhPSRIA----LNASIVfdASVKNWIQLLSGHtlvL 684
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADATHDrlggpgqwLLALP-AHHIAglqvLVRSVI--AGSEPVELDVSAG---F 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 685 VPDALRADAHQL---WRYFArhavdlfdCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAISPAVWSRLQSLsDTRFINVY 761
Cdd:PRK07824 112 DPTALPRAVAELgggRRYTS--------LVPMQLAKALDDPAATAALAELDAVLVGGGPAPAPVLDAAAAA-GINVVRTY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 762 GPTECtvdATACVVDrtqplptiGKPLANTRLYILDaqdqpvpigvtGELHIGGAGVARGYLHRPDltaerfiPDPFsAD 841
Cdd:PRK07824 183 GMSET---SGGCVYD--------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPF-AE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 842 PAAriYKTGDLARwLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAE 921
Cdd:PRK07824 233 PGW--FRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPA 309
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 641744967 922 LHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK07824 310 PTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1540-2015 |
2.11e-19 |
|
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: 95.80 E-value: 2.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1540 RTPDTTAVLF-----EDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPA 1614
Cdd:cd05943 80 ADADDPAAIYaaedgERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWSSCSPDFGV 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1615 ERLAYMLDDASPVALLT-----------------QANQRALLTGD----VPRILLD-------TADFSHLSEDNPHVPG- 1665
Cdd:cd05943 160 PGVLDRFGQIEPKVLFAvdaytyngkrhdvrekvAELVKGLPSLLavvvVPYTVAAgqpdlskIAKALTLEDFLATGAAg 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1666 ------LDAHHLAYVIYTSGSTGKPKGVMNSH----------RALCNRLvwmqntyrlTPDDRVlqktpFSFDVSVWeFF 1729
Cdd:cd05943 240 elefepLPFDHPLYILYSSGTTGLPKCIVHGAggtllqhlkeHILHCDL---------RPGDRL-----FYYTTCGW-MM 304
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1730 W-----PLLYGARLVMArpDG---HKDAAYLAQLIERTGITTLHFVPSMLQ-----QFVQWADADCacDSLRRVICSGEA 1796
Cdd:cd05943 305 WnwlvsGLAVGATIVLY--DGspfYPDTNALWDLADEEGITVFGTSAKYLDalekaGLKPAETHDL--SSLRTILSTGSP 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1797 LPAElQQRFF---ARFNAQLHNLYGPTEaaIDVTFWACQPDdhrsfVPIGR-----PIANTQLYILDTLGQPVPlGVAGE 1868
Cdd:cd05943 381 LKPE-SFDYVydhIKPDVLLASISGGTD--IISCFVGGNPL-----LPVYRgeiqcRGLGMAVEAFDEEGKPVW-GEKGE 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1869 LHIggvgvARGYLNRP-----DLTAERFIPDPFINQPGarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEA 1943
Cdd:cd05943 452 LVC-----TKPFPSMPvgfwnDPDGSRYRAAYFAKYPG--VWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYR 524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 1944 RLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPAdLRQQLGQHLAEYM----VPGAFVTLDAFPLTPNGK 2015
Cdd:cd05943 525 VVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDE-LRKRIRSTIRSALsprhVPAKIIAVPDIPRTLSGK 599
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
2599-3097 |
2.16e-19 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 95.27 E-value: 2.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2599 DADIPRHALIHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISF-GVRPDERVAICVERGLDMVVGLLGIL 2677
Cdd:PRK12492 17 TIDLAAYKSVVEVFERSCKKFADRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2678 KAGGAYVPLDPTYPVERLRYMLDDAKPVALIsqsaHLGIMNGSLPVILLDDG-----ETRPFDNEP-------DTPLDAR 2745
Cdd:PRK12492 97 RAGLIVVNTNPLYTAREMRHQFKDSGARALV----YLNMFGKLVQEVLPDTGieyliEAKMGDLLPaakgwlvNTVVDKV 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2746 KQGLTPRHL----------------------------AYVIYTSGSTGKPKGVMVEH----ANMVNFLCSMRKEPGIAQE 2793
Cdd:PRK12492 173 KKMVPAYHLpqavpfkqalrqgrglslkpvpvglddiAVLQYTGGTTGLAKGAMLTHgnlvANMLQVRACLSQLGPDGQP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2794 DVLLGVTSLSFDISILEIFLPLLNGARLILATQAQaadaqqlaMLIE--RHAVSFMQATpSTWR---------MLVELRD 2862
Cdd:PRK12492 253 LMKEGQEVMIAPLPLYHIYAFTANCMCMMVSGNHN--------VLITnpRDIPGFIKEL-GKWRfsallglntLFVALMD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2863 FalpPGFKAL---------CGGEALPEnlATA-LLQKVT--TLWNLYGPTETTIWSTLNglttptPY--------IGHPI 2922
Cdd:PRK12492 324 H---PGFKDLdfsalkltnSGGTALVK--ATAeRWEQLTgcTIVEGYGLTETSPVASTN------PYgelarlgtVGIPV 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2923 ANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRND 3002
Cdd:PRK12492 393 PGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGW--------FKTGDIAVIDPDGFVRIVDRKK 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3003 FQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQpDTVLEPADLRQRLSEGVAEYMIPSAFVTLD 3082
Cdd:PRK12492 465 DLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVAR-DPGLSVEELKAYCKENFTGYKVPKHIVLRD 543
|
570
....*....|....*
gi 641744967 3083 AFPLTPNGKLDRKAL 3097
Cdd:PRK12492 544 SLPMTPVGKILRREL 558
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
2633-3097 |
2.26e-19 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 95.20 E-value: 2.26e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2633 SYDELNRRANRLAHHLISFGVRPDERVAIC---VERGLDMVVGLLGIlkaGGAYVPLDPTYPVERLRYMLDDAKPVALIS 2709
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2710 QSAHLGIMN---GSLP----VILLDDGETRPfdnepDTPL---------------DARKQGLTPRHLAYVIYTSGSTGKP 2767
Cdd:PRK06018 118 DLTFVPILEkiaDKLPsverYVVLTDAAHMP-----QTTLknavayeewiaeadgDFAWKTFDENTAAGMCYTSGTTGDP 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2768 KGVMVEH-ANMVNFLCSMRKEP-GIAQEDVLLGVTSL----SFDISileiFLPLLNGARLILATQAQAADAQQLamLIER 2841
Cdd:PRK06018 193 KGVLYSHrSNVLHALMANNGDAlGTSAADTMLPVVPLfhanSWGIA----FSAPSMGTKLVMPGAKLDGASVYE--LLDT 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2842 HAVSFMQATPSTWRMLV---ELRDFALPPGFKALCGGEALPENLATALLQKVTTLWNLYGPTETTIWSTLNGLTTPTPYI 2918
Cdd:PRK06018 267 EKVTFTAGVPTVWLMLLqymEKEGLKLPHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTLAALKPPFSKL 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2919 ------------GHPIANTQIYILDAQGRVVPL-GVA-GEIHIAGAGVVRGYLGrpdltAERFITDpfsgapEARMYKTG 2984
Cdd:PRK06018 347 pgdarldvlqkqGYPPFGVEMKITDDAGKELPWdGKTfGRLKVRGPAVAAAYYR-----VDGEILD------DDGFFDTG 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2985 DLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETrLARCH-GVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQ 3063
Cdd:PRK06018 416 DVATIDAYGYMRITDRSKDVIKSGGEWISSIDLEN-LAVGHpKVAEAAVIGVYHPKWDERPLLIVQLKPGETATREEILK 494
|
490 500 510
....*....|....*....|....*....|....
gi 641744967 3064 RLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK06018 495 YMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
2617-3091 |
2.30e-19 |
|
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: 94.67 E-value: 2.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2617 ACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLR 2696
Cdd:cd12118 15 AVYPDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2697 YMLDDAKPVALISQSAHLGIMngslpviLLDDGETRPfdnEPDTPLDARkQGLTprhlayVIYTSGSTGKPKGVMVEH-- 2774
Cdd:cd12118 95 FILRHSEAKVLFVDREFEYED-------LLAEGDPDF---EWIPPADEW-DPIA------LNYTSGTTGRPKGVVYHHrg 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2775 ------ANMVNFlcSMRKEP------------------GIAQedvlLGVTSlsfdisileIFLPLLNgARLILAtqaqaa 2830
Cdd:cd12118 158 aylnalANILEW--EMKQHPvylwtlpmfhcngwcfpwTVAA----VGGTN---------VCLRKVD-AKAIYD------ 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2831 daqqlamLIERHAVSFMQATPSTWRMLVELRDFA---LPPGFKALCGGEALPEnlatALLQKVTTLW----NLYGPTETT 2903
Cdd:cd12118 216 -------LIEKHKVTHFCGAPTVLNMLANAPPSDarpLPHRVHVMTAGAPPPA----AVLAKMEELGfdvtHVYGLTETY 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2904 ------IWS-TLNGLTTPTPYI-----GHP-IANTQIYILDAQG-RVVPL-GV-AGEIHIAGAGVVRGYLGRPDLTAERF 2967
Cdd:cd12118 285 gpatvcAWKpEWDELPTEERARlkarqGVRyVGLEEVDVLDPETmKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2968 itdpfsgapEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAY 3047
Cdd:cd12118 365 ---------RGGWFHSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAF 435
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 641744967 3048 LLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDaFPLTPNGK 3091
Cdd:cd12118 436 VELKEGAKVTEEEIIAFCREHLAGFMVPKTVVFGE-LPKTSTGK 478
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
2595-3097 |
2.46e-19 |
|
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: 95.46 E-value: 2.46e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2595 FNATDadipRHALihelfeaqvACTPDAIAVVF------GEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLD 2668
Cdd:cd05967 53 YNALD----RHVE---------AGRGDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2669 MVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQSAhlGI-----------------MNGSLP--VILLDDG 2729
Cdd:cd05967 120 AAIAMLACARIGAIHSVVFGGFAAKELASRIDDAKPKLIVTASC--GIepgkvvpykplldkaleLSGHKPhhVLVLNRP 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2730 ETRPFDNEPDTPLD-------ARKQGLTP---RHLAYVIYTSGSTGKPKGVMVE---HANMVNFlcSMRKEPGIAQEDVL 2796
Cdd:cd05967 198 QVPADLTKPGRDLDwsellakAEPVDCVPvaaTDPLYILYTSGTTGKPKGVVRDnggHAVALNW--SMRNIYGIKPGDVW 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2797 LGVTSLSFDISILEI-FLPLLNGARLILATQAQAADAQQLAM--LIERHAVSFMQATPSTWRML-------VELRDFALP 2866
Cdd:cd05967 276 WAASDVGWVVGHSYIvYGPLLHGATTVLYEGKPVGTPDPGAFwrVIEKYQVNALFTAPTAIRAIrkedpdgKYIKKYDLS 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2867 pGFKAL-CGGEAL-PENLATAllQKVTTL------WNlygpTET-----TIWSTLNGLTTPTPYIGHPIANTQIYILDAQ 2933
Cdd:cd05967 356 -SLRTLfLAGERLdPPTLEWA--ENTLGVpvidhwWQ----TETgwpitANPVGLEPLPIKAGSPGKPVPGYQVQVLDED 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2934 GRVVPLGVAGEIHIAGA---GVVRGYLGRPdltaERFITDPFSGAPEarMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGF 3010
Cdd:cd05967 429 GEPVGPNELGNIVIKLPlppGCLLTLWKND----ERFKKLYLSKFPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVAGH 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3011 RIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIP-SAF---VTLDAFPL 3086
Cdd:cd05967 503 RLSTGEMEESVLSHPAVAECAVVGVRDELKGQVPLGLVVLKEGVKITAEELEKELVALVREQIGPvAAFrlvIFVKRLPK 582
|
570
....*....|.
gi 641744967 3087 TPNGKLDRKAL 3097
Cdd:cd05967 583 TRSGKILRRTL 593
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1551-1999 |
7.19e-19 |
|
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: 92.80 E-value: 7.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1551 DQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAayvpldpgypaerlaymlddaspVALL 1630
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA-----------------------VAAL 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1631 TQANQRalltGDVPRILLDTADFSHLSEDnphvpgldahhLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPD 1710
Cdd:cd05940 58 INYNLR----GESLAHCLNVSSAKHLVVD-----------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1711 DRVLQKTP-FSFDVSVWEFFWPLLYGARLVMAR--------PDGHKDAAYLAQLIERTgITTLHFVPsmlqqfvqwadad 1781
Cdd:cd05940 123 DVLYTCLPlYHSTALIVGWSACLASGATLVIRKkfsasnfwDDIRKYQATIFQYIGEL-CRYLLNQP------------- 188
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1782 cACDSLR----RVICsGEALPAELQQRFFARFN-AQLHNLYGPTEAAIDVTFWACQPDD---HRSFVPIGRPIANTQlYI 1853
Cdd:cd05940 189 -PKPTERkhkvRMIF-GNGLRPDIWEEFKERFGvPRIAEFYAATEGNSGFINFFGKPGAigrNPSLLRKVAPLALVK-YD 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1854 LDTlGQP----------VPLGVAGEL--HIGGVGVARGYLNrPDLTAERFIPDPFinQPGARLYKTGDLARWLPDGSLEY 1921
Cdd:cd05940 266 LES-GEPirdaegrcikVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVF--KKGDAWFNTGDLMRLDGEGFWYF 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 1922 LGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRL-VAYLCPQPGVTPDPADLRQQLGQHLAEYMVP 1999
Cdd:cd05940 342 VDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDGRAgMAAIVLQPNEEFDLSALAAHLEKNLPGYARP 420
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1542-2045 |
8.02e-19 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 93.55 E-value: 8.02e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1542 PDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYML 1621
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1622 DDASPVAL--------LTQANQRALLTGDV---PRILL------------DTADFSHLSEDNPHVPGL--------DAHH 1670
Cdd:PLN03102 108 RHAKPKILfvdrsfepLAREVLHLLSSEDSnlnLPVIFiheidfpkrpssEELDYECLIQRGEPTPSLvarmfriqDEHD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1671 LAYVIYTSGSTGKPKGVMNSHR-----ALCNRLVWMQNTYRLtpddrVLQKTPFsFDVSVWEFFWPL-LYGARLVMARpd 1744
Cdd:PLN03102 188 PISLNYTSGTTADPKGVVISHRgaylsTLSAIIGWEMGTCPV-----YLWTLPM-FHCNGWTFTWGTaARGGTSVCMR-- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1745 gHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADCACDSLR-RVICSGEALPAELQQRfFARFNAQLHNLYGPTEAA 1823
Cdd:PLN03102 260 -HVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRSGPvHVLTGGSPPPAALVKK-VQRLGFQVMHAYGLTEAT 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1824 IDVTFwaCQPDDHRSFVPIGRPIANTQLYILDTLG------------QPVPLG--VAGELHIGGVGVARGYLNRPDLTAE 1889
Cdd:PLN03102 338 GPVLF--CEWQDEWNRLPENQQMELKARQGVSILGladvdvknketqESVPRDgkTMGEIVIKGSSIMKGYLKNPKATSE 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1890 RFiPDPFINqpgarlykTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLV 1969
Cdd:PLN03102 416 AF-KHGWLN--------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETPC 486
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1970 AYLCPQPGVTPDPA----------DLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDR-------KALPAPDQSAVATR 2032
Cdd:PLN03102 487 AFVVLEKGETTKEDrvdklvtrerDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKpklrdiaKGLVVEDEDNVIKK 566
|
570
....*....|...
gi 641744967 2033 DYEAPQGEVETAL 2045
Cdd:PLN03102 567 VHQRPVEHFSSRL 579
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2754-3097 |
8.62e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 91.00 E-value: 8.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2754 LAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLsFDI--SILEIFLPLLNGARLILATQAQAAD 2831
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPL-FHVngSVVTLLTPLASGAHVVLAGPAGYRN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2832 AQQLA---MLIERHAVSFMQATPSTWRMLVELRDFALPPGFK-ALCGGEALPENLATALLQKV-TTLWNLYGPTETTIWS 2906
Cdd:cd05944 83 PGLFDnfwKLVERYRITSLSTVPTVYAALLQVPVNADISSLRfAMSGAAPLPVELRARFEDATgLPVVEGYGLTEATCLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2907 TLNGLTTPTPyIGH-----PIANTQIYILDAQGRVV-PLGV--AGEIHIAGAGVVRGYLgRPDLTAERFITDPFsgapea 2978
Cdd:cd05944 163 AVNPPDGPKR-PGSvglrlPYARVRIKVLDGVGRLLrDCAPdeVGEICVAGPGVFGGYL-YTEGNKNAFVADGW------ 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2979 rmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEP 3058
Cdd:cd05944 235 --LNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEE 312
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 641744967 3059 ADLRQRLSEGVAEY-MIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05944 313 EELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
619-960 |
9.42e-19 |
|
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: 90.78 E-value: 9.42e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 619 VIYTSGSTGRPKGVMVAHR-----------NVINLATG--LHTLLALDHPSRIALNASIVFDA-------------SVKN 672
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKtffavpdilqkEGLNWVVGdvTYLPLPATHIGGLWWILTCLIHGglcvtggenttykSLFK 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 673 WIQLLSGHTLVLVPDAlradahqlWRYFARHAVDLFDCTPvQLQWlldaglgsdpayqpaqVLIGGEAISPAVWSRLQSL 752
Cdd:cd17635 86 ILTTNAVTTTCLVPTL--------LSKLVSELKSANATVP-SLRL----------------IGYGGSRAIAADVRFIEAT 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 753 SDTRFINVYGPTECTvdaTACVVDRTQPLPTI---GKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLT 829
Cdd:cd17635 141 GLTNTAQVYGLSETG---TALCLPTDDDSIEInavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERT 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 830 AERFIPDPFsadpaariyKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTR 909
Cdd:cd17635 218 AEVLIDGWV---------NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGEL 288
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 641744967 910 LVAYLCARP-DAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDR 960
Cdd:cd17635 289 VGLAVVASAeLDENAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1530-2023 |
9.73e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 93.17 E-value: 9.73e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1530 IHQLVEDQAarTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGvKPDDR--IAICVERSLDMVIGLLAILKAGAAYVP 1607
Cdd:PRK13388 5 IAQLLRDRA--GDDTIAVRYGDRTWTWREVLAEAAARAAALIALA-DPDRPlhVGVLLGNTPEMLFWLAAAALGGYVLVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1608 LDPGYPAERLAYMLDDASPVALLTQANQRALLTG----DVPRILLDTADFSHL----SEDNPHVPgLDAHHLAYVIYTSG 1679
Cdd:PRK13388 82 LNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGldlpGVRVLDVDTPAYAELvaaaGALTPHRE-VDAMDPFMLIFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1680 STGKPKGVMNSH-------RALCNRlvwmqntYRLTPDDRVLQKTPFSFDVSVWEFFWPLL-YGARlvMARPDGHKDAAY 1751
Cdd:PRK13388 161 TTGAPKAVRCSHgrlafagRALTER-------FGLTRDDVCYVSMPLFHSNAVMAGWAPAVaSGAA--VALPAKFSASGF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1752 LAQlIERTGITTLHFVPSMLQQFVQWADADCACDSLRRVICSGEALPaELQQRFFARFNAQLHNLYGPTEAAIDVTfwac 1831
Cdd:PRK13388 232 LDD-VRRYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEASP-RDIAEFSRRFGCQVEDGYGSSEGAVIVV---- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1832 qPDDHRSFVPIGRPIANTQLYILDTLgqpVPLGVA---------------GEL-HIGGVGVARGYLNRPDLTAERFipdp 1895
Cdd:PRK13388 306 -REPGTPPGSIGRGAPGVAIYNPETL---TECAVArfdahgallnadeaiGELvNTAGAGFFEGYYNNPEATAERM---- 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1896 finqpgaR--LYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLC 1973
Cdd:PRK13388 378 -------RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALV 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 641744967 1974 PQPGVTPDPADLRQQLG--QHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPA 2023
Cdd:PRK13388 451 LRDGATFDPDAFAAFLAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1840-2114 |
1.01e-18 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 89.81 E-value: 1.01e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1840 VPIGRPIANTQLYILDTLGQPVPLGVAGelhiGGVGVARGYLNRPDLTAERFIPDPFINQPGARLYKTGDLARWLPDGSL 1919
Cdd:COG3433 18 PVIPPAIVQARALLLIVDLQGYFGGFGG----EGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1920 EYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQ--PGVTPDPADLRQQLGQHLAEYM 1997
Cdd:COG3433 94 GPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAvaALDGLAAAAALAALDKVPPDVV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1998 VPGAFVTLDAFPLTPNGKLDRKALPAPDQSAVATRDYEAPQGE---VETALAAVWQDLLGLT--RVGRHDHFFALGGHSL 2072
Cdd:COG3433 174 AASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALEtalTEEELRADVAELLGVDpeEIDPDDNLFDLGLDSI 253
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 641744967 2073 LIVSLIERLRRAGLALDVRGVFSTPVLSDMAQAILAHQDKPA 2114
Cdd:COG3433 254 RLMQLVERWRKAGLDVSFADLAEHPTLAAWWALLAAAQAAAA 295
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
503-963 |
1.08e-18 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 92.44 E-value: 1.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 503 ELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPaERLAYILDDAAPVALLTQSAQVA 582
Cdd:cd05929 22 VYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAP-RAEACAIIEIKAAALVCGLFTGG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 583 QLNSTLPTvllDTPAAAACPDT--NPVVQGlhaahlAYVIYTSGSTGRPKGVMVAHR-NVINLATGLHTLLALDHPS-RI 658
Cdd:cd05929 101 GALDGLED---YEAAEGGSPETpiEDEAAG------WKMLYSGGTTGRPKGIKRGLPgGPPDNDTLMAAALGFGPGAdSV 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 659 ALNASIVFDASVKNW--IQLLSGHTLVLVPdalRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPA--QV 734
Cdd:cd05929 172 YLSPAPLYHAAPFRWsmTALFMGGTLVLME---KFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPEAVRNAYDLSslKR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 735 LIGGEA-ISPAVWSRLQSLSDTRFINVYGPTECTvdaTACVVDRTQPLP---TIGKPLANtRLYILDAQDQPVPIGVTGE 810
Cdd:cd05929 249 VIHAAApCPPWVKEQWIDWGGPIIWEYYGGTEGQ---GLTIINGEEWLThpgSVGRAVLG-KVHILDEDGNEVPPGEIGE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 811 LHIGGAGvARGYLHRPDLTAERFIPDPFSAdpaariykTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRC 890
Cdd:cd05929 325 VYFANGP-GFEYTNDPEKTAAARNEGGWST--------LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAH 395
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 891 PGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPA---ALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05929 396 PKVLDAAVVGVPDEELGQRVHAVVQPAPGADAGTAlaeELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
29-345 |
1.49e-18 |
|
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: 91.28 E-value: 1.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 29 YPLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICWQGLhQPVQVV--WRQAPLTV 106
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEG-EPYQWIdpYTPVPIRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 107 ntlTTTSSDTVP--AQLRAATDPSNHRLNLSNAPLLSAT--TAHDpvcGEWLLSLSIHHLISDHITQAL----IIDEIRL 178
Cdd:cd19533 81 ---IDLSGDPDPegAAQQWMQEDLRKPLPLDNDPLFRHAlfTLGD---NRHFWYQRVHHIVMDGFSFALfgqrVAEIYTA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 179 LLEDRPealPKPLPYRNFIAQILS-VPLSEHEQYFRNRLADIDTPTAPFDLVDVQGNGE----DITEARLSLDSSLADAL 253
Cdd:cd19533 155 LLKGRP---APPAPFGSFLDLVEEeQAYRQSERFERDRAFWTEQFEDLPEPVSLARRAPgrslAFLRRTAELPPELTRTL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 254 RRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLqgNLGADRVMGMFINTLPLRVSLR-ERSVHDVVQATSH 332
Cdd:cd19533 232 LEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRL--GAAARQTPGMVANTLPLRLTVDpQQTFAELVAQVSR 309
|
330
....*....|...
gi 641744967 333 ELMMLLAHEQAPL 345
Cdd:cd19533 310 ELRSLLRHQRYRY 322
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
2597-3097 |
1.79e-18 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 92.25 E-value: 1.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2597 ATDADIPRHALIHELFEAQVACTPDAIAVV-FGEaSLSYDELNRRANRLAHHLIS-FGVRPDERVAICVERGLDMVVGLL 2674
Cdd:PRK08751 16 AAEIDLEQFRTVAEVFATSVAKFADRPAYHsFGK-TITYREADQLVEQFAAYLLGeLQLKKGDRVALMMPNCLQYPIATF 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2675 GILKAGGAYVPLDPTYPVERLRYMLDDAKPVAL------------------ISQ--SAHLGIMNGSLPVILLDDGETRPF 2734
Cdd:PRK08751 95 GVLRAGLTVVNVNPLYTPRELKHQLIDSGASVLvvidnfgttvqqviadtpVKQviTTGLGDMLGFPKAALVNFVVKYVK 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2735 DNEPDTPL-------DARKQG---------LTPRHLAYVIYTSGSTGKPKGVMVEHANMVnflCSMRKE------PGIAQ 2792
Cdd:PRK08751 175 KLVPEYRIngairfrEALALGrkhsmptlqIEPDDIAFLQYTGGTTGVAKGAMLTHRNLV---ANMQQAhqwlagTGKLE 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2793 EDVLLGVTSLSfdisILEIFLPLLNGarLILatqaqaadaqqlaMLIE--RHAVSFMQATPSTWRMLVELRDFALP---- 2866
Cdd:PRK08751 252 EGCEVVITALP----LYHIFALTANG--LVF-------------MKIGgcNHLISNPRDMPGFVKELKKTRFTAFTgvnt 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2867 --------PGFK---------ALCGGEALPENLATALlQKVT--TLWNLYGPTETTIWSTLNGLTTP--TPYIGHPIANT 2925
Cdd:PRK08751 313 lfngllntPGFDqidfsslkmTLGGGMAVQRSVAERW-KQVTglTLVEAYGLTETSPAACINPLTLKeyNGSIGLPIPST 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2926 QIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDFQV 3005
Cdd:PRK08751 392 DACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW--------LHTGDIARMDEQGFVYIVDRKKDMI 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3006 KVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKrLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFP 3085
Cdd:PRK08751 464 LVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSGE-IVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELP 542
|
570
....*....|..
gi 641744967 3086 LTPNGKLDRKAL 3097
Cdd:PRK08751 543 KTNVGKILRREL 554
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
2601-3097 |
2.14e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 92.04 E-value: 2.14e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2601 DIPRHALIHELFEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLIS-FGVRPDERVAICVERGLDMVVGLLGILKA 2679
Cdd:PRK08974 18 NPDRYQSLVDMFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNgLGLKKGDRVALMMPNLLQYPIALFGILRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2680 GGAYVPLDPTYPVERLRYMLDD--AKPVALISQSAHL---GIMNGSLP-VILLDDGETRPFD------------------ 2735
Cdd:PRK08974 98 GMIVVNVNPLYTPRELEHQLNDsgAKAIVIVSNFAHTlekVVFKTPVKhVILTRMGDQLSTAkgtlvnfvvkyikrlvpk 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2736 -NEPD--TPLDARKQG---------LTPRHLAYVIYTSGSTGKPKGVMVEHANMV-NFL-CSMRKEPGIaQEDVLLGVTS 2801
Cdd:PRK08974 178 yHLPDaiSFRSALHKGrrmqyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNMLaNLEqAKAAYGPLL-HPGKELVVTA 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2802 LSfdisILEIFLPLLN-------GARLILATQAQAADAQQLAMliERHAVSFMQATPSTWRMLVELRDFAlPPGFKAL-- 2872
Cdd:PRK08974 257 LP----LYHIFALTVNcllfielGGQNLLITNPRDIPGFVKEL--KKYPFTAITGVNTLFNALLNNEEFQ-ELDFSSLkl 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2873 --CGGEALPENLATALlQKVT--TLWNLYGPTETTiwstlnGLTTPTPY--------IGHPIANTQIYILDAQGRVVPLG 2940
Cdd:PRK08974 330 svGGGMAVQQAVAERW-VKLTgqYLLEGYGLTECS------PLVSVNPYdldyysgsIGLPVPSTEIKLVDDDGNEVPPG 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2941 VAGEIHIAGAGVVRGYLGRPDLTAErFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETR 3020
Cdd:PRK08974 403 EPGELWVKGPQVMLGYWQRPEATDE-VIKDGW--------LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDV 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 3021 LARCHGVHDAVVIARE-DSPGDkrLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK08974 474 VMLHPKVLEVAAVGVPsEVSGE--AVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
499-933 |
2.15e-18 |
|
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: 91.09 E-value: 2.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPmdpaypaerlayilddaaPVALLTQs 578
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIP------------------ATTLLTP- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 aqvAQLNSTLptvllDTPAAAACPdtnpVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRN--VINLAT----GLHtllal 652
Cdd:cd05974 62 ---DDLRDRV-----DRGGAVYAA----VDENTHADDPMLLYFTSGTTSKPKLVEHTHRSypVGHLSTmywiGLK----- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 653 dhPSRIALNASIVFDA--SVKNWIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSdPAYQ 730
Cdd:cd05974 125 --PGDVHWNISSPGWAkhAWSCFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLAS-FDVK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 731 PAQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTEctvdaTACVVDRT--QPLPT--IGKPLANTRLYILDAQDQPVPIG 806
Cdd:cd05974 202 LREVVGAGEPLNPEVIEQVRRAWGLTIRDGYGQTE-----TTALVGNSpgQPVKAgsMGRPLPGYRVALLDPDGAPATEG 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 807 VTGeLHIGG---AGVARGYLHRPDLTAERFipdpfsadpAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEI 883
Cdd:cd05974 277 EVA-LDLGDtrpVGLMKGYAGDPDKTAHAM---------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFEL 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 884 ESRLLRCPGVQDAVVIAredSPGDTRLV---AYLCARPDAELHPAA-------LRQQLAA 933
Cdd:cd05974 347 ESVLIEHPAVAEAAVVP---SPDPVRLSvpkAFIVLRAGYEPSPETaleifrfSRERLAP 403
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1523-1743 |
2.63e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 92.10 E-value: 2.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1523 DFPHDALIHQLVEDQAARTPDTTAVLFED---------QHLTYDALNRRANQLAHHLIDLGvKPDDRIAICVERSLDMVI 1593
Cdd:PRK07769 16 RFPPNTNLVRHVERWAKVRGDKLAYRFLDfsterdgvaRDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1594 GLLAILKAGAAYVPL-DPGYP--AERLAYMLDDASPVALLTQANQ--------RALLTGDVPRIL-LDTADFSHLSEDNP 1661
Cdd:PRK07769 95 AFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSaegvrkffRARPAKERPRVIaVDAVPDEVGATWVP 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1662 HVPGLDAhhLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMA 1741
Cdd:PRK07769 175 PEANEDT--IAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFM 252
|
..
gi 641744967 1742 RP 1743
Cdd:PRK07769 253 SP 254
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
499-962 |
3.25e-18 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 91.73 E-value: 3.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALgVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPM-DPAYP--AERLAYILDDAAPVALL 575
Cdd:PRK12476 69 LTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 576 TQSA---QVAQLNSTLPT------VLLDTPAAAACPDTNPVvqGLHAAHLAYVIYTSGSTGRPKGVMVAHRNV-INLatg 645
Cdd:PRK12476 148 TTTAaaeAVEGFLRNLPRlrrprvIAIDAIPDSAGESFVPV--ELDTDDVSHLQYTSGSTRPPVGVEITHRAVgTNL--- 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 646 LHTLLALDHPSRIALNAS------------IVFDASVKNWIQLLSGHTLVLVP----DALRADAHQlWRYFArhAVDLFd 709
Cdd:PRK12476 223 VQMILSIDLLDRNTHGVSwlplyhdmglsmIGFPAVYGGHSTLMSPTAFVRRPqrwiKALSEGSRT-GRVVT--AAPNF- 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 710 ctpvQLQWLLDAGL---GSDPAYQPAQVLIGGEAISPAVWSRLQS------LSDTRFINVYGPTECTV-------DATAC 773
Cdd:PRK12476 299 ----AYEWAAQRGLpaeGDDIDLSNVVLIIGSEPVSIDAVTTFNKafapygLPRTAFKPSYGIAEATLfvatiapDAEPS 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 774 VV--DRTQ-------PLP----------TIGKPLANTRLYILDA-QDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERF 833
Cdd:PRK12476 375 VVylDREQlgagravRVAadapnavahvSCGQVARSQWAVIVDPdTGAELPDGEVGEIWLHGDNIGRGYWGRPEETERTF 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 834 -------IPDPFSAD---PAARIYKTGDLARWLpDGNIDYLGRNDFQIKVRGFR-----IEAGEIE-SRLLR-------- 889
Cdd:PRK12476 455 gaklqsrLAEGSHADgaaDDGTWLRTGDLGVYL-DGELYITGRIADLIVIDGRNhypqdIEATVAEaSPMVRrgyvtaft 533
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641744967 890 CPGVQ-DAVVIAREDSPGDTRLVaylcARPDAELHPAALRQQLAASLADYMipsaFVTLDALPLTPNGKLDRKA 962
Cdd:PRK12476 534 VPAEDnERLVIVAERAAGTSRAD----PAPAIDAIRAAVSRRHGLAVADVR----LVPAGAIPRTTSGKLARRA 599
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
499-898 |
4.62e-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: 90.74 E-value: 4.62e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGV--QPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDA-APVALL 575
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAeISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 576 TQSAQVAQLNstlptVLLDTPAAAACPDTNPvvqglHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTL------ 649
Cdd:cd05927 86 DAGVKVYSLE-----EFEKLGKKNKVPPPPP-----KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKIleilnk 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 650 ----------LALDHP-SRIALNASIVFDASVKNW----------IQLLSGHTLVLVP-------DALRADAHQ---LWR 698
Cdd:cd05927 156 inptdvyisyLPLAHIfERVVEALFLYHGAKIGFYsgdirlllddIKALKPTVFPGVPrvlnriyDKIFNKVQAkgpLKR 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 699 YFARHAVDLfdctpvQLQWLLDAGLGSDP-----AYQPAQVLIGGE---------AISPAVWSRLQSLSDTRFINVYGPT 764
Cdd:cd05927 236 KLFNFALNY------KLAELRSGVVRASPfwdklVFNKIKQALGGNvrlmltgsaPLSPEVLEFLRVALGCPVLEGYGQT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 765 ECTVDATACVVDRTQPlPTIGKPLANT--RL-------YilDAQDqPVPigvTGELHIGGAGVARGYLHRPDLTAERFIP 835
Cdd:cd05927 310 ECTAGATLTLPGDTSV-GHVGGPLPCAevKLvdvpemnY--DAKD-PNP---RGEVCIRGPNVFSGYYKDPEKTAEALDE 382
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 836 DPFsadpaariYKTGDLARWLPDGNIDYLGR--NDFQIkVRGFRIEAGEIESRLLRCPGVQDAVV 898
Cdd:cd05927 383 DGW--------LHTGDIGEWLPNGTLKIIDRkkNIFKL-SQGEYVAPEKIENIYARSPFVAQIFV 438
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
2628-3000 |
5.72e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 90.94 E-value: 5.72e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2628 GEA-SLSYDELNRRANRLAHHLISFGvRPDERVAICVERGLDMVVGLLGILKAGGAYVPL-DPTYP--VERLRYMLDDAK 2703
Cdd:PRK07769 51 GVArDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCT 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2704 PVA-LISQSAHLGIMN--GSLP------VILLDD-----GET-RPFDNEPDTpldarkqgltprhLAYVIYTSGSTGKPK 2768
Cdd:PRK07769 130 PSAiLTTTDSAEGVRKffRARPakerprVIAVDAvpdevGATwVPPEANEDT-------------IAYLQYTSGSTRIPA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2769 GVMVEH----ANMVNFLCSMRKEPGIAqedvllGVTSLSF--DISILEIFLPLLNGarlilatqaqaadaqqlamlierH 2842
Cdd:PRK07769 197 GVQITHlnlpTNVLQVIDALEGQEGDR------GVSWLPFfhDMGLITVLLPALLG-----------------------H 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2843 AVSFMqaTPSTW-----RMLVEL--------RDFALPPGFK-ALCGGEALP-------------------ENLATALLQK 2889
Cdd:PRK07769 248 YITFM--SPAAFvrrpgRWIRELarkpggtgGTFSAAPNFAfEHAAARGLPkdgeppldlsnvkgllngsEPVSPASMRK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2890 VTTLWNLYGPTETTI-------WSTLNGLTTPT---PYIGH------------------PIANTQI-----------YIL 2930
Cdd:PRK07769 326 FNEAFAPYGLPPTAIkpsygmaEATLFVSTTPMdeePTVIYvdrdelnagrfvevpadaPNAVAQVsagkvgvsewaVIV 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2931 DA-QGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERF---ITDPFS-----GAPE-ARMYKTGDLGRWLpDGTLEYLGR 3000
Cdd:PRK07769 406 DPeTASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqniLKSRLSeshaeGAPDdALWVRTGDYGVYF-DGELYITGR 484
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
616-963 |
6.04e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 88.69 E-value: 6.04e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 616 LAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRI--ALNASIVFDASVKNWIQLLSG-HTLVLVPDALRAD 692
Cdd:cd05944 4 VAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLlcGLPLFHVNGSVVTLLTPLASGaHVVLAGPAGYRNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 693 A--HQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAyQPAQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVDA 770
Cdd:cd05944 84 GlfDNFWKLVERYRITSLSTVPTVYAALLQVPVNADIS-SLRFAMSGAAPLPVELRARFEDATGLPVVEGYGLTEATCLV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 771 TACVVDRTQPLPTIGKPL--ANTRLYILDAQDQPV-PIGV--TGELHIGGAGVARGYLHRPDltaerfipdPFSADPAAR 845
Cdd:cd05944 163 AVNPPDGPKRPGSVGLRLpyARVRIKVLDGVGRLLrDCAPdeVGEICVAGPGVFGGYLYTEG---------NKNAFVADG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 846 IYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPA 925
Cdd:cd05944 234 WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQLKPGAVVEEE 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 641744967 926 ALRQQLAASLADY-MIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05944 314 ELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1522-2033 |
6.05e-18 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 90.45 E-value: 6.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1522 ADFPhdALIHQLVEDQAARTPDTTAVLFED--QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAIL 1599
Cdd:PRK05857 10 PQLP--STVLDRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1600 KAGAAYVPLDPGYPAERLAYMLDDASPVALLTQ------ANQRALLTGDVPRILLDTADFSHLSEDNPHV------PGLD 1667
Cdd:PRK05857 88 KLGAIAVMADGNLPIAAIERFCQITDPAAALVApgskmaSSAVPEALHSIPVIAVDIAAVTRESEHSLDAaslagnADQG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1668 AHHLAYVIYTSGSTGKPKGVMNSHRAL-----------CNRLVWMQNTYRLTPddrvlqkTPFSFDVSVWEFFWPLLYGA 1736
Cdd:PRK05857 168 SEDPLAMIFTSGTTGEPKAVLLANRTFfavpdilqkegLNWVTWVVGETTYSP-------LPATHIGGLWWILTCLMHGG 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1737 RLVMarpdGHKDAAYLAQLIERTGITTLHFVPSMLQQFV-QWADADCACDSLRRVICSG-EALPAELqqRFFARFNAQLH 1814
Cdd:PRK05857 241 LCVT----GGENTTSLLEILTTNAVATTCLVPTLLSKLVsELKSANATVPSLRLVGYGGsRAIAADV--RFIEATGVRTA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1815 NLYGPTEAAIDVTfwaCQPDDHRSFVPI-----GRPIANTQLYILDTLG-QPVPLGVA-----GELHIGGVGVARGYLNR 1883
Cdd:PRK05857 315 QVYGLSETGCTAL---CLPTDDGSIVKIeagavGRPYPGVDVYLAATDGiGPTAPGAGpsasfGTLWIKSPANMLGYWNN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1884 PDLTAERFIpDPFINqpgarlykTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDsP 1963
Cdd:PRK05857 392 PERTAEVLI-DGWVN--------TGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD-E 461
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1964 GDTRLVAyLCPQPGVTPDPA---DLRQQLGQHL---AEYMV-PGAFVTLDAFPLTPNGKLDRKALPAP---DQSAVATRD 2033
Cdd:PRK05857 462 EFGALVG-LAVVASAELDESaarALKHTIAARFrreSEPMArPSTIVIVTDIPRTQSGKVMRASLAAAataDKARVVVRG 540
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1940-2015 |
7.54e-18 |
|
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: 80.28 E-value: 7.54e-18
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 1940 EIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGK 2015
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
2627-3099 |
9.63e-18 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 90.48 E-value: 9.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2627 FGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTypVERLRYMLDDAkpva 2706
Cdd:PRK06060 26 YAADVVTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPE--LHRDDHALAAR---- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2707 liSQSAHLGIMNGSL-----------PVILLDDG-ETRPFDNEPdtpldarkqgLTPRHLAYVIYTSGSTGKPKGVMVEH 2774
Cdd:PRK06060 100 --NTEPALVVTSDALrdrfqpsrvaeAAELMSEAaRVAPGGYEP----------MGGDALAYATYTSGTTGPPKAAIHRH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2775 ANMVNFLCSM-RKEPGIAQEDVLLGVTSLSFDISI-LEIFLPLLNGARLILatQAQAADAQQLAMLIERHAVSFMQATPS 2852
Cdd:PRK06060 168 ADPLTFVDAMcRKALRLTPEDTGLCSARMYFAYGLgNSVWFPLATGGSAVI--NSAPVTPEAAAILSARFGPSVLYGVPN 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2853 TWRMLVelrDFALPPGFKAL-C---GGEALPENLATALLQKVTTLWNLYGPTETTIWSTL--NGLTTPTP-YIGHPIANT 2925
Cdd:PRK06060 246 FFARVI---DSCSPDSFRSLrCvvsAGEALELGLAERLMEFFGGIPILDGIGSTEVGQTFvsNRVDEWRLgTLGRVLPPY 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2926 QIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPD--LTAERFItdpfsgapearmyKTGDLGRWLPDGTLEYLGRNDF 3003
Cdd:PRK06060 323 EIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPDspVANEGWL-------------DTRDRVCIDSDGWVTYRCRADD 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3004 QVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPA---DLRQRLSEGVAEYMIPSAFVT 3080
Cdd:PRK06060 390 TEVIGGVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSvmrDLHRGLLNRLSAFKVPHRFAV 469
|
490
....*....|....*....
gi 641744967 3081 LDAFPLTPNGKLDRKALPA 3099
Cdd:PRK06060 470 VDRLPRTPNGKLVRGALRK 488
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
2614-3092 |
1.05e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 89.68 E-value: 1.05e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2614 AQVActPDAIAVVFGEA--SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYP 2691
Cdd:PRK13390 7 AQIA--PDRPAVIVAETgeQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2692 VERLRYMLDDAKPVALISQSAHLGIM---NGSLPVILLDDGETRPFDNEPDTpLDARKQGLTPRHL-AYVIYTSGSTGKP 2767
Cdd:PRK13390 85 APEADYIVGDSGARVLVASAALDGLAakvGADLPLRLSFGGEIDGFGSFEAA-LAGAGPRLTEQPCgAVMLYSSGTTGFP 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2768 KGVmveHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIF--LPL-------LNGARLILATQAQAADAQQLaml 2838
Cdd:PRK13390 164 KGI---QPDLPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPIYhaAPLrwcsmvhALGGTVVLAKRFDAQATLGH--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2839 IERHAVSFMQATPSTWRMLVELRD-----FALPPGFKALCGGEALPENLATALLQKV-TTLWNLYGPTET---TIWSTLN 2909
Cdd:PRK13390 238 VERYRITVTQMVPTMFVRLLKLDAdvrtrYDVSSLRAVIHAAAPCPVDVKHAMIDWLgPIVYEYYSSTEAhgmTFIDSPD 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2910 GLTTPTPyIGHPIANTqIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAErfitdpfSGAPEARMYKT-GDLGR 2988
Cdd:PRK13390 318 WLAHPGS-VGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAA-------AQHPAHPFWTTvGDLGS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2989 WLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSP-GDK-RLVAYLLAQPDTVLEPA-DLRQRL 3065
Cdd:PRK13390 389 VDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEmGEQvKAVIQLVEGIRGSDELArELIDYT 468
|
490 500
....*....|....*....|....*..
gi 641744967 3066 SEGVAEYMIPSAFVTLDAFPLTPNGKL 3092
Cdd:PRK13390 469 RSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
2757-3092 |
1.40e-17 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 86.79 E-value: 1.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2757 VIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVT----SLSFDISILeifLPLLNGARLIlatQAQAADA 2832
Cdd:cd17638 5 IMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINpffhTFGYKAGIV---ACLLTGATVV---PVAVFDV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2833 QQLAMLIERHAVSFMQATPSTWRMLV---ELRDFALPPGFKALCGGEALPENLATALLQKVT--TLWNLYGPTET---TI 2904
Cdd:cd17638 79 DAILEAIERERITVLPGPPTLFQSLLdhpGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGfeTVLTAYGLTEAgvaTM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2905 WSTLNGLTTPTPYIGHPIANTQIYILDaqgrvvplgvAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTG 2984
Cdd:cd17638 159 CRPGDDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGW--------LHTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2985 DLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQR 3064
Cdd:cd17638 221 DVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVTLTEEDVIAW 300
|
330 340
....*....|....*....|....*...
gi 641744967 3065 LSEGVAEYMIPSAFVTLDAFPLTPNGKL 3092
Cdd:cd17638 301 CRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
439-963 |
1.47e-17 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 89.27 E-value: 1.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 439 TPQQPALSQPILPKSERQQVLVDFNATDADFpremlIQQRFEAQAEQTPEAIAVlfEDQHLTYRELNRRANQLAHHLIAL 518
Cdd:PLN02330 3 MEIQKQEDNEHIFRSRYPSVPVPDKLTLPDF-----VLQDAELYADKVAFVEAV--TGKAVTYGEVVRDTRRFAKALRSL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 519 GVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQSAQVAQLNST-LPTVLLDTP- 596
Cdd:PLN02330 76 GLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGLgLPVIVLGEEk 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 597 ------------AAAACPDTNpVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVI-NLATGLH----------TLLALD 653
Cdd:PLN02330 156 iegavnwkelleAADRAGDTS-DNEEILQTDLCALPFSSGTTGISKGVMLTHRNLVaNLCSSLFsvgpemigqvVTLGLI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 654 HPSRIALNASIVFdASVKNwiqllSGHTLVLVPDALRADAHQLWRYFARHA---------------VDLFDCTPVQLQWL 718
Cdd:PLN02330 235 PFFHIYGITGICC-ATLRN-----KGKVVVMSRFELRTFLNALITQEVSFApivppiilnlvknpiVEEFDLSKLKLQAI 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 719 LDAGLGSDPayqpaQVLIGGEAISPAVwsRLQSlsdtrfinVYGPTECT-VDATACVVDRTQPLP---TIGKPLANTRLY 794
Cdd:PLN02330 309 MTAAAPLAP-----ELLTAFEAKFPGV--QVQE--------AYGLTEHScITLTHGDPEKGHGIAkknSVGFILPNLEVK 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 795 ILDAQD-QPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQIKV 873
Cdd:PLN02330 374 FIDPDTgRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW--------LHTGDIGYIDDDGDIFIVDRIKELIKY 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 874 RGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLT 953
Cdd:PLN02330 446 KGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKS 525
|
570
....*....|
gi 641744967 954 PNGKLDRKAL 963
Cdd:PLN02330 526 LSGKIMRRLL 535
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
499-958 |
1.67e-17 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 89.44 E-value: 1.67e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAH-HLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPvALLTQ 577
Cdd:cd17632 68 ITYAELWERVGAVAAaHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEP-RLLAV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 578 S------AQVAQLNSTLP-------------------------------TVLLDTPAAAACPDTNP---VVQGLHAAHLA 617
Cdd:cd17632 147 SaehldlAVEAVLEGGTPprlvvfdhrpevdahraalesarerlaavgiPVTTLTLIAVRGRDLPPaplFRPEPDDDPLA 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 618 YVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWI--QLLSGHTLVLVPdalRADAHQ 695
Cdd:cd17632 227 LLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLNFMPMSHIAGRISLygTLARGGTAYFAA---ASDMST 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 696 LWRYFA-----------RHAVDLFDCTPVQLQWLLDAglGSDPAYQPAQV----------------LIGGEAISPAVWSR 748
Cdd:cd17632 304 LFDDLAlvrptelflvpRVCDMLFQRYQAELDRRSVA--GADAETLAERVkaelrervlggrllaaVCGSAPLSAEMKAF 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 749 LQSLSDTRFINVYGPTEctvdATACVVD-RTQPLPTIGKPLANTRLYILDAQDQPVPigvTGELHIGGAGVARGYLHRPD 827
Cdd:cd17632 382 MESLLDLDLHDGYGSTE----AGAVILDgVIVRPPVLDYKLVDVPELGYFRTDRPHP---RGELLVKTDTLFPGYYKRPE 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 828 LTAERFIPDPFsadpaariYKTGD-LARWLPDgNIDYLGRNDFQIK------VRGFRIEAGEIESRLLRCPGVQD----- 895
Cdd:cd17632 455 VTAEVFDEDGF--------YRTGDvMAELGPD-RLVYVDRRNNVLKlsqgefVTVARLEAVFAASPLVRQIFVYGnsera 525
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 896 ---AVVIaredsPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVtLDALPLTP-NGKL 958
Cdd:cd17632 526 yllAVVV-----PTQDALAGEDTARLRAALAESLQRIAREAGLQSYEIPRDFL-IETEPFTIaNGLL 586
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1676-2023 |
1.70e-17 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 89.13 E-value: 1.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1676 YTSGSTGKPKGVMNSHR-----ALCNRLVWMqntyrlTPDDRVLQKTPFSFDVSVWEFFWPL--LYGARLVMArpdgHKD 1748
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRgaylmALSNALIWG------MNEGAVYLWTLPMFHCNGWCFTWTLaaLCGTNICLR----QVT 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1749 AAYLAQLIERTGITTLHFVPSMLQQFVQWADADCACDSLR--RVICSGEALPAEL-----QQRFFARFNAQLHNLYGPTE 1821
Cdd:PLN02479 272 AKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETILPLPRvvHVMTAGAAPPPSVlfamsEKGFRVTHTYGLSETYGPST 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1822 AAIDVTFWACQPDDHRSFVPIG---RPIANTQLYILDT-LGQPVPL--GVAGELHIGGVGVARGYLNRPDLTAERFipdp 1895
Cdd:PLN02479 352 VCAWKPEWDSLPPEEQARLNARqgvRYIGLEGLDVVDTkTMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAF---- 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1896 finQPGarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQ 1975
Cdd:PLN02479 428 ---ANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPCAFVTLK 502
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 641744967 1976 PGV-TPDPADLRQQLGQ----HLAEYMVPGAfVTLDAFPLTPNGKLDRKALPA 2023
Cdd:PLN02479 503 PGVdKSDEAALAEDIMKfcreRLPAYWVPKS-VVFGPLPKTATGKIQKHVLRA 554
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
480-936 |
2.41e-17 |
|
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: 88.64 E-value: 2.41e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 480 EAQAEQTPEAIAVLFED-----QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMD 554
Cdd:cd05921 2 AHWARQAPDRTWLAEREgnggwRRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 555 PAYPA-----ERLAYILD----------DAAP------------VALLTQSAQVAQLNSTLPTVLLDTPAAAACPDTNPV 607
Cdd:cd05921 82 PAYSLmsqdlAKLKHLFEllkpglvfaqDAAPfaralaaifplgTPLVVSRNAVAGRGAISFAELAATPPTAAVDAAFAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 608 VQglhAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLAL--DHPSRIA--LNASIVFDASVKNWIQLLSGHTLV 683
Cdd:cd05921 162 VG---PDTVAKFLFTSGSTGLPKAVINTQRMLCANQAMLEQTYPFfgEEPPVLVdwLPWNHTFGGNHNFNLVLYNGGTLY 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 684 LvpDALRADAHQlwryFARHAVDLFDCTP-----VQLQW-LLDAGLGSDPA-----YQPAQVLI-GGEAISPAVWSRLQS 751
Cdd:cd05921 239 I--DDGKPMPGG----FEETLRNLREISPtvyfnVPAGWeMLVAALEKDEAlrrrfFKRLKLMFyAGAGLSQDVWDRLQA 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 752 LSDT------RFINVYGPTECTVDATACVVDRTQPlPTIGKPLANTRLYIldaqdqpVPIGVTGELHIGGAGVARGYLHR 825
Cdd:cd05921 313 LAVAtvgeriPMMAGLGATETAPTATFTHWPTERS-GLIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 826 PDLTAERFIPDPFsadpaariYKTGDLARWL----PDGNIDYLGR--NDFQIKvRGFRIEAGEIESRLLRC--PGVQDAV 897
Cdd:cd05921 385 PELTAQAFDEEGF--------YCLGDAAKLAdpddPAKGLVFDGRvaEDFKLA-SGTWVSVGPLRARAVAAcaPLVHDAV 455
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 641744967 898 VIA--RE--------DSPGDTRLVAYLCARPDAELHPAALRQQLAASLA 936
Cdd:cd05921 456 VAGedRAevgalvfpDLLACRRLVGLQEASDAEVLRHAKVRAAFRDRLA 504
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
2602-3092 |
2.56e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 88.68 E-value: 2.56e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2602 IPRHALIHelfeaqvactPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGG 2681
Cdd:PRK07786 23 LARHALMQ----------PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2682 AYVPLDPTYPVERLRYMLDDAKPVALISQSAHLGIMNG------SLPVILLDDGETRPF----------DNEPDTPLDAR 2745
Cdd:PRK07786 93 IAVPVNFRLTPPEIAFLVSDCGAHVVVTEAALAPVATAvrdivpLLSTVVVAGGSSDDSvlgyedllaeAGPAHAPVDIP 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2746 KQglTPrhlAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLP-LLNGARLILA 2824
Cdd:PRK07786 173 ND--SP---ALIMYTSGTTGRPKGAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPgLLLGAPTVIY 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2825 TQAQAADAQQLAMLiERHAVSFMQATPSTWRML-----VELRDFALppgfKALCGGEA-LPENLATALLQKVTTLWNL-- 2896
Cdd:PRK07786 248 PLGAFDPGQLLDVL-EAEKVTGIFLVPAQWQAVcaeqqARPRDLAL----RVLSWGAApASDTLLRQMAATFPEAQILaa 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2897 YGPTETT-IWSTLNG--LTTPTPYIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFitdpfs 2973
Cdd:PRK07786 323 FGQTEMSpVTCMLLGedAIRKLGSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF------ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2974 gapEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYL-LAQP 3052
Cdd:PRK07786 397 ---AGGWFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKWGEVPVAVAaVRND 473
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 641744967 3053 DTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKL 3092
Cdd:PRK07786 474 DAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
2612-2785 |
2.63e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 88.78 E-value: 2.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2612 FEAQVACTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYP 2691
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2692 VERLRYMLDDAKPVALI----------SQSAHLGIMngslPVILLDDGETRPF-----------DNEPDTPLDARkQGLT 2750
Cdd:PRK08279 123 GAVLAHSLNLVDAKHLIvgeelveafeEARADLARP----PRLWVAGGDTLDDpegyedlaaaaAGAPTTNPASR-SGVT 197
|
170 180 190
....*....|....*....|....*....|....*
gi 641744967 2751 PRHLAYVIYTSGSTGKPKGVMVEHAnmvNFLCSMR 2785
Cdd:PRK08279 198 AKDTAFYIYTSGTTGLPKAAVMSHM---RWLKAMG 229
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
2899-3187 |
3.27e-17 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 85.19 E-value: 3.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2899 PTETTIWSTLNGLTTPTPYIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFSGAPea 2978
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2979 rmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIARED--SPGDKRLVAYLLAQPDTVL 3056
Cdd:COG3433 79 --GRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAAlrGAGVGLLLIVGAVAALDGL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3057 EPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPAPDQSAMATRGYEAP---QGDLEHALAQIWQTLLGV-- 3131
Cdd:COG3433 157 AAAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPaleTALTEEELRADVAELLGVdp 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 3132 ERVGRHDHFFELGGHSLLAVQLNARIRAEFLtDIPIVAIFQHPQLSALAEVILAAQ 3187
Cdd:COG3433 237 EEIDPDDNLFDLGLDSIRLMQLVERWRKAGL-DVSFADLAEHPTLAAWWALLAAAQ 291
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
2757-3097 |
3.91e-17 |
|
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: 87.91 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2757 VIYTSGSTGKPKgvMVEHAN---MVNFLCSMRKEPGIAQEDVLLGVTSLSFDISIL-EIFLPLLNGARLILATQAQAADA 2832
Cdd:cd05928 179 IYFTSGTTGSPK--MAEHSHsslGLGLKVNGRYWLDLTASDIMWNTSDTGWIKSAWsSLFEPWIQGACVFVHHLPRFDPL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2833 QQLAMLIERHAVSFMQAtPSTWRMLVE--LRDFALPPGFKALCGGEAL-PENLATALLQKVTTLWNLYGPTETT-IWSTL 2908
Cdd:cd05928 257 VILKTLSSYPITTFCGA-PTVYRMLVQqdLSSYKFPSLQHCVTGGEPLnPEVLEKWKAQTGLDIYEGYGQTETGlICANF 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2909 NGLTTPTPYIGHPIANTQIYILDAQGRVVPLGVAGEIHI-----AGAGVVRGYLGRPDLTAERFITDpfsgapearMYKT 2983
Cdd:cd05928 336 KGMKIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGD---------FYLT 406
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2984 GDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYL-LAQPDTVLEPADLR 3062
Cdd:cd05928 407 GDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVvLAPQFLSHDPEQLT 486
|
330 340 350
....*....|....*....|....*....|....*....
gi 641744967 3063 QRLSEGV----AEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05928 487 KELQQHVksvtAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
487-960 |
4.43e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 87.93 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYIL 566
Cdd:PLN02860 21 GNAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAM 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 567 DDAAPVALLT----QSAQVAQLNSTLPT----VLLDTPAAAACPDTNPVV-------QGLHAAHLAY---------VIYT 622
Cdd:PLN02860 101 LLVRPVMLVTdetcSSWYEELQNDRLPSlmwqVFLESPSSSVFIFLNSFLttemlkqRALGTTELDYawapddavlICFT 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 623 SGSTGRPKGVMVAHRNVI--NLA----TG-------LHTlLALDH----PSRIAL-------------NASIVFDASVKN 672
Cdd:PLN02860 181 SGTTGRPKGVTISHSALIvqSLAkiaiVGygeddvyLHT-APLCHigglSSALAMlmvgachvllpkfDAKAALQAIKQH 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 673 WIQllsghTLVLVPdALRADahqLWRYFARHAVDlfDCTPvQLQWLLDAGLGSDPAYQPAQVLIGGEAISPAVWSRLQSL 752
Cdd:PLN02860 260 NVT-----SMITVP-AMMAD---LISLTRKSMTW--KVFP-SVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAC 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 753 SDTRFINVYGPTECTVDATACVVDRTQPLPT-------IGKPLANTRLYIldAQDQPVPigvTGELHIGGAGVARGYLHR 825
Cdd:PLN02860 328 SSLTFMTLHDPTLESPKQTLQTVNQTKSSSVhqpqgvcVGKPAPHVELKI--GLDESSR---VGRILTRGPHVMLGYWGQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 826 PDLTAERFIPDPFSAdpaariykTGDLArWLPD-GNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDS 904
Cdd:PLN02860 403 NSETASVLSNDGWLD--------TGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDS 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641744967 905 PGDTRLVAylCAR-------PDAELHPAALRQQLAAS----------LADYMIPSAFVTL-DALPLTPNGKLDR 960
Cdd:PLN02860 474 RLTEMVVA--CVRlrdgwiwSDNEKENAKKNLTLSSEtlrhhcreknLSRFKIPKLFVQWrKPFPLTTTGKIRR 545
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
1551-2023 |
4.77e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 86.63 E-value: 4.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1551 DQHLTYDALNRRANQLAHHLIdLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALL 1630
Cdd:PRK08308 6 DEEYSKSDFDLRLQRYEEMEQ-FQEAAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1631 TQanqrallTGDVPRILLDTADfshlsednPHVPGLdahhlayVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPD 1710
Cdd:PRK08308 85 YG-------ESDFTKLEAVNYL--------AEEPSL-------LQYSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1711 DRVLQKTPFSFDvsvweffWPLLYGARLVMARPD-----GHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADcacD 1785
Cdd:PRK08308 143 ETPIVACPVTHS-------YGLICGVLAALTRGSkpviiTNKNPKFALNILRNTPQHILYAVPLMLHILGRLLPGT---F 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1786 SLRRVICSGEALPAELQQRFFARFNaQLHNLYGPTEAAidvtfwaCqpddhrsfVPIgrpiaNTQLYILDTLGQPVPlgv 1865
Cdd:PRK08308 213 QFHAVMTSGTPLPEAWFYKLRERTT-YMMQQYGCSEAG-------C--------VSI-----CPDMKSHLDLGNPLP--- 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1866 agelHiggVGVARGylnrpdltAERFIPDPFINQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARL 1945
Cdd:PRK08308 269 ----H---VSVSAG--------SDENAPEEIVVKMGDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVM 333
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 1946 MQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVtpDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALPA 2023
Cdd:PRK08308 334 LRLPGVQEAVVYRGKDPVAGERVKAKVISHEEI--DPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLEL 409
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
2631-3097 |
4.84e-17 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 87.59 E-value: 4.84e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2631 SLSYDELNRRANRLAHHLI-SFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALIS 2709
Cdd:PLN02574 66 SISYSELQPLVKSMAAGLYhVMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIKKRVVDCSVGLAFT 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2710 QSAHLGIMNG-SLPVILLDDG---ETRPFDNEPDTPLDARKQGLTPRHL------AYVIYTSGSTGKPKGVMVEHANM-- 2777
Cdd:PLN02574 146 SPENVEKLSPlGVPVIGVPENydfDSKRIEFPKFYELIKEDFDFVPKPVikqddvAAIMYSSGTTGASKGVVLTHRNLia 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2778 -----VNFLCSMRKEPGiaQEDVLLGVTSLsFDISILEIF-LPLLNGARLILATQAQAADAQQLamLIERHAVSFMQATP 2851
Cdd:PLN02574 226 mvelfVRFEASQYEYPG--SDNVYLAALPM-FHIYGLSLFvVGLLSLGSTIVVMRRFDASDMVK--VIDRFKVTHFPVVP 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2852 StwrMLVELRDFALPPG---FKAL----CGGEALPENLATALLQKV--TTLWNLYGPTETTIWSTlNGLTTPT----PYI 2918
Cdd:PLN02574 301 P---ILMALTKKAKGVCgevLKSLkqvsCGAAPLSGKFIQDFVQTLphVDFIQGYGMTESTAVGT-RGFNTEKlskySSV 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2919 GHPIANTQIYILD-AQGRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEY 2997
Cdd:PLN02574 377 GLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW--------LRTGDIAYFDEDGYLYI 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2998 LGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSA 3077
Cdd:PLN02574 449 VDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQEAVINYVAKQVAPYKKVRK 528
|
490 500
....*....|....*....|
gi 641744967 3078 FVTLDAFPLTPNGKLDRKAL 3097
Cdd:PLN02574 529 VVFVQSIPKSPAGKILRREL 548
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1554-2018 |
5.12e-17 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 87.75 E-value: 5.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLD-PGYPAERLAY------MLDDASP 1626
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMGFGGRESYiaqlrgMLASAQP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1627 VALLTQANQRALL----TGDVPRILLDTADFSHLSEDNPHVPGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWM- 1701
Cdd:PRK09192 130 AAIITPDELLPWVneatHGNPLLHVLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLRAIs 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1702 QNTYRLTPDDRVLQKTPFSFDVSVWEFFW-PL-------LYGARLVMARPdghkdAAYLaQLIERTGiTTLHFVPS---- 1769
Cdd:PRK09192 210 HDGLKVRPGDRCVSWLPFYHDMGLVGFLLtPVatqlsvdYLPTRDFARRP-----LQWL-DLISRNR-GTISYSPPfgye 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1770 MLQQFVQWAD-ADCACDSLRRVICSGEALPAELQQRFFARFnAQLH-------NLYGPTEAAIDVTF------------- 1828
Cdd:PRK09192 283 LCARRVNSKDlAELDLSCWRVAGIGADMIRPDVLHQFAEAF-APAGfddkafmPSYGLAEATLAVSFsplgsgivveevd 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1829 ------------WACQPDDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDlTAERFIPDPF 1896
Cdd:PRK09192 362 rdrleyqgkavaPGAETRRVRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGW 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1897 INqpgarlykTGDLArWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQ--EAVVVAREDSPGDTRLVAYLCP 1974
Cdd:PRK09192 441 LD--------TGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIVLLVQCR 511
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 641744967 1975 qpgvTPDPADlRQQLGQHLAE--YMVPGAFVTLD-----AFPLTPNGKLDR 2018
Cdd:PRK09192 512 ----ISDEER-RGQLIHALAAlvRSEFGVEAAVElvpphSLPRTSSGKLSR 557
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1542-2021 |
5.50e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 87.31 E-value: 5.50e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1542 PDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYML 1621
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1622 DDASPVALLT-----QANQRALLTGDVPRIL-----------------LDTADFshLSEDNPHVPGL------DAHHLAy 1673
Cdd:PRK08162 112 RHGEAKVLIVdtefaEVAREALALLPGPKPLvidvddpeypggrfigaLDYEAF--LASGDPDFAWTlpadewDAIALN- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1674 viYTSGSTGKPKGVMNSHR-----ALCNRLVWmqntyRLTPDDRVLQKTPFsFDVSVWEFFWPLLYGA------RLVmar 1742
Cdd:PRK08162 189 --YTSGTTGNPKGVVYHHRgaylnALSNILAW-----GMPKHPVYLWTLPM-FHCNGWCFPWTVAARAgtnvclRKV--- 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1743 pdghkDAAYLAQLIERTGITtlHF-----VPSMLqqfvqwADADcacDSLRRVI-------CSGEALPAELQQRfFARFN 1810
Cdd:PRK08162 258 -----DPKLIFDLIREHGVT--HYcgapiVLSAL------INAP---AEWRAGIdhpvhamVAGAAPPAAVIAK-MEEIG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1811 AQLHNLYGPTEAAIDVTFWACQPDDHRsfVPIG-----------RPIANTQLYILDT-LGQPVPLG--VAGELHIGGVGV 1876
Cdd:PRK08162 321 FDLTHVYGLTETYGPATVCAWQPEWDA--LPLDeraqlkarqgvRYPLQEGVTVLDPdTMQPVPADgeTIGEIMFRGNIV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1877 ARGYLNRPDLTAERFipdpfinQPGarLYKTGDLARWLPDGsleYLgrndfQVKLR--------GFRIELGEIEARLMQC 1948
Cdd:PRK08162 399 MKGYLKNPKATEEAF-------AGG--WFHTGDLAVLHPDG---YI-----KIKDRskdiiisgGENISSIEVEDVLYRH 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 1949 PGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAfVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK08162 462 PAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKA-VVFGELPKTSTGKIQKFVL 533
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
2631-3063 |
5.72e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 87.79 E-value: 5.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2631 SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPV-----ERLRYMLDDAKPV 2705
Cdd:PRK12582 80 KVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSLmshdhAKLKHLFDLVKPR 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2706 ALISQS--------AHLGIMNGSLPVI--LLDDGETRPFDNEPDTP----LDARKQGLTPRHLAYVIYTSGSTGKPKGVM 2771
Cdd:PRK12582 160 VVFAQSgapfaralAALDLLDVTVVHVtgPGEGIASIAFADLAATPptaaVAAAIAAITPDTVAKYLFTSGSTGMPKAVI 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2772 VEHANMvnflCSMRKEPgiaqedvlLGVTSLSFD--ISILEIFLP--------------LLNGARLILATQAQAADAQQL 2835
Cdd:PRK12582 240 NTQRMM----CANIAMQ--------EQLRPREPDppPPVSLDWMPwnhtmggnanfnglLWGGGTLYIDDGKPLPGMFEE 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2836 AM--LIERHAVSFMQAtPSTWRMLVEL--RDFALPPG-FKAL----CGGEALPENLAT---ALLQKVT----TLWNLYGP 2899
Cdd:PRK12582 308 TIrnLREISPTVYGNV-PAGYAMLAEAmeKDDALRRSfFKNLrlmaYGGATLSDDLYErmqALAVRTTghriPFYTGYGA 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2900 TET------TIWSTLN-GLttptpyIGHPIANTQIyildaqgRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPF 2972
Cdd:PRK12582 387 TETaptttgTHWDTERvGL------IGLPLPGVEL-------KLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2973 sgapearmYKTGDLGRWL----PDGTLEYLGR--NDFQ------VKVRGFRIELgeietrLARCHGV-HDAVViaredsP 3039
Cdd:PRK12582 454 --------YRLGDAARFVdpddPEKGLIFDGRvaEDFKlstgtwVSVGTLRPDA------VAACSPViHDAVV------A 513
|
490 500
....*....|....*....|....
gi 641744967 3040 GDKRLVAYLLAQPDtvlePADLRQ 3063
Cdd:PRK12582 514 GQDRAFIGLLAWPN----PAACRQ 533
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1674-2021 |
5.99e-17 |
|
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: 87.14 E-value: 5.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1674 VIYTSGSTGKPKGVMNSHRAL------CNRLvWMQntyrLTPDDRVLQKTPFSFDVSVW-EFFWPLLYGArLVMARPDGH 1746
Cdd:cd05928 179 IYFTSGTTGSPKMAEHSHSSLglglkvNGRY-WLD----LTASDIMWNTSDTGWIKSAWsSLFEPWIQGA-CVFVHHLPR 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1747 KDAAYLAQLIERTGITTLHFVPSMLQQFVQWADADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAA-ID 1825
Cdd:cd05928 253 FDPLVILKTLSSYPITTFCGAPTVYRMLVQQDLSSYKFPSLQHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGlIC 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1826 VTFWA--CQPDDhrsfvpIGRPIANTQLYILDTLGQPVPLGVAGELHI-----GGVGVARGYLNRPDLTAERFIPDpfin 1898
Cdd:cd05928 333 ANFKGmkIKPGS------MGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGD---- 402
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1899 qpgarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAredSPGDTR---LVAYLCPQ 1975
Cdd:cd05928 403 -----FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVS---SPDPIRgevVKAFVVLA 474
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 641744967 1976 PGV-TPDPADLRQQLGQHL----AEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05928 475 PQFlSHDPEQLTKELQQHVksvtAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
2618-3124 |
7.30e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 87.38 E-value: 7.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2618 CTPDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRY 2697
Cdd:PLN03102 26 CYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2698 MLDDAKP---------VALISQSAHLGIMNGS---LPVILLD--DGETRPFDNEPDTPLDARKQGLTPRHLAYVI----- 2758
Cdd:PLN03102 106 ILRHAKPkilfvdrsfEPLAREVLHLLSSEDSnlnLPVIFIHeiDFPKRPSSEELDYECLIQRGEPTPSLVARMFriqde 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2759 -------YTSGSTGKPKGVMVEHANMvnFLCSMrkepgiaqeDVLLGVTSLSFDISI--LEIF------LPLLNGARLIL 2823
Cdd:PLN03102 186 hdpislnYTSGTTADPKGVVISHRGA--YLSTL---------SAIIGWEMGTCPVYLwtLPMFhcngwtFTWGTAARGGT 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2824 ATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVELRDFALPPG---FKALCGGEALPenlaTALLQKVTTL----WNL 2896
Cdd:PLN03102 255 SVCMRHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSPRsgpVHVLTGGSPPP----AALVKKVQRLgfqvMHA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2897 YGPTETT----------IWSTLNglttptpyighpiANTQIYILDAQGrVVPLGVA--------------------GEIH 2946
Cdd:PLN03102 331 YGLTEATgpvlfcewqdEWNRLP-------------ENQQMELKARQG-VSILGLAdvdvknketqesvprdgktmGEIV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2947 IAGAGVVRGYLGRPDLTAERFitdpfsgapEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHG 3026
Cdd:PLN03102 397 IKGSSIMKGYLKNPKATSEAF---------KHGWLNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPK 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3027 VHDAVVIAREDSPGDKRLVAYLLAQ----------PDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDR-- 3094
Cdd:PLN03102 468 VLETAVVAMPHPTWGETPCAFVVLEkgettkedrvDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKpk 547
|
570 580 590
....*....|....*....|....*....|....*
gi 641744967 3095 -----KALPAPDQSAMATRGYEAPqgdLEHALAQI 3124
Cdd:PLN03102 548 lrdiaKGLVVEDEDNVIKKVHQRP---VEHFSSRL 579
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
2617-3097 |
7.93e-17 |
|
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: 86.81 E-value: 7.93e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2617 ACTPDAIAVV--FGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVER 2694
Cdd:cd17642 28 ASVPGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2695 LRYMLDDAKP-VALISQSAHLGIMN--GSLP----VILLDDGE-------TRPFDNEPDTPLDARKQGLTP-----RHLA 2755
Cdd:cd17642 108 LDHSLNISKPtIVFCSKKGLQKVLNvqKKLKiiktIIILDSKEdykgyqcLYTFITQNLPPGFNEYDFKPPsfdrdEQVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2756 YVIYTSGSTGKPKGVMVEHANMVNFLCSMRkEP----GIAQEDVLLGVTSLSFDISILEIFLPLLNGARLILATQAQAAD 2831
Cdd:cd17642 188 LIMNSSGSTGLPKGVQLTHKNIVARFSHAR-DPifgnQIIPDTAILTVIPFHHGFGMFTTLGYLICGFRVVLMYKFEEEL 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2832 AQQLamlIERHAVSFMQATPSTWRMLVE---LRDFALPPGFKALCGGEALPENLATALLQ--KVTTLWNLYGPTETT--I 2904
Cdd:cd17642 267 FLRS---LQDYKVQSALLVPTLFAFFAKstlVDKYDLSNLHEIASGGAPLSKEVGEAVAKrfKLPGIRQGYGLTETTsaI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2905 WSTLNGLTTPtpyighpiantqiyilDAQGRVVP--------------LGV--AGEIHIAGAGVVRGYLGRPDLTAERFI 2968
Cdd:cd17642 344 LITPEGDDKP----------------GAVGKVVPffyakvvdldtgktLGPneRGELCVKGPMIMKGYVNNPEATKALID 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2969 TDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYL 3048
Cdd:cd17642 408 KDGW--------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVV 479
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 3049 LAQP----------DTVLEPADLRQRLSEGVaeymipsafVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd17642 480 VLEAgktmtekevmDYVASQVSTAKRLRGGV---------KFVDEVPKGLTGKIDRRKI 529
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
2631-3105 |
9.16e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 86.87 E-value: 9.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2631 SLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQ 2710
Cdd:PRK04319 73 KYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKVLITT 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2711 SAHLG-IMNGSLP----VILLDDGEtrpfDNEPDT-PLDARKQG---------LTPRHLAYVIYTSGSTGKPKGVMVEHA 2775
Cdd:PRK04319 153 PALLErKPADDLPslkhVLLVGEDV----EEGPGTlDFNALMEQasdefdiewTDREDGAILHYTSGSTGKPKGVLHVHN 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2776 NMVN----------------FLCSmrKEPGiaqedvllGVTSLSFDisileIFLPLLNGARLILATQAQAADAQQLamLI 2839
Cdd:PRK04319 229 AMLQhyqtgkyvldlheddvYWCT--ADPG--------WVTGTSYG-----IFAPWLNGATNVIDGGRFSPERWYR--IL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2840 ERHAVSFMQATPSTWRMLV----EL-RDFALPPGFKALCGGEAL-PEnlATALLQKVTTLwnlygPTETTIWSTLNG--- 2910
Cdd:PRK04319 292 EDYKVTVWYTAPTAIRMLMgagdDLvKKYDLSSLRHILSVGEPLnPE--VVRWGMKVFGL-----PIHDNWWMTETGgim 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2911 -LTTPTPYI-----GHPIANTQIYILDAQGRVVPLGVAGEIHIAgAG---VVRGYLGRPDLTAERFITDpfsgapearMY 2981
Cdd:PRK04319 365 iANYPAMDIkpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAIK-KGwpsMMRGIWNNPEKYESYFAGD---------WY 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2982 KTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTvlEPAD- 3060
Cdd:PRK04319 435 VSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKPDPVRGEIIKAFVALRPGY--EPSEe 512
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3061 --------LRQRLSEGVAeymiPSAFVTLDAFPLTPNGKLDR---KA----LPAPDQSAM 3105
Cdd:PRK04319 513 lkeeirgfVKKGLGAHAA----PREIEFKDKLPKTRSGKIMRrvlKAwelgLPEGDLSTM 568
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
1543-2021 |
9.78e-17 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 86.76 E-value: 9.78e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1543 DTTAVLFED---QHLTYDALNRRANQLAHHLID-LGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLA 1618
Cdd:PRK05620 25 DTTVTTWGGaeqEQTTFAAIGARAAALAHALHDeLGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1619 YMLDDASP---VALLTQANQRALLTGDVPR----ILLDTADFSH-LSEDNPHV------------------PGLDAHHLA 1672
Cdd:PRK05620 105 HIINHAEDeviVADPRLAEQLGEILKECPCvravVFIGPSDADSaAAHMPEGIkvysyealldgrstvydwPELDETTAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1673 YVIYTSGSTGKPKGVMNSHRALcnrlvWMQNTYRLTPDD-RVLQKTPFSFDVSVWEFF-W--PL---LYGARLVMarPDG 1745
Cdd:PRK05620 185 AICYSTGTTGAPKGVVYSHRSL-----YLQSLSLRTTDSlAVTHGESFLCCVPIYHVLsWgvPLaafMSGTPLVF--PGP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1746 HKDAAYLAQLIERTGITTLHFVPSM-LQQFVQWADADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAI 1824
Cdd:PRK05620 258 DLSAPTLAKIIATAMPRVAHGVPTLwIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERYGVDVVHVWGMTETSP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1825 DVTFwACQP--------DDHRsfVPIGRPIANTQLYILDTlGQPVPLG--VAGELHIGGVGVARGYLNRP---------- 1884
Cdd:PRK05620 338 VGTV-ARPPsgvsgearWAYR--VSQGRFPASLEYRIVND-GQVMESTdrNEGEIQVRGNWVTASYYHSPteegggaast 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1885 ------DLTAERFIPDPFInqpgarlyKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVA 1958
Cdd:PRK05620 414 frgedvEDANDRFTADGWL--------RTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIG 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 1959 REDSPGDTRLVAYLCPQPGVTPDPA---DLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK05620 486 YPDDKWGERPLAVTVLAPGIEPTREtaeRLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
2599-3099 |
1.16e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 86.57 E-value: 1.16e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2599 DADIPRHALIHE-LFE--AQVACTPDAIAVVFGEaSLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLG 2675
Cdd:PLN02246 16 DIYIPNHLPLHDyCFErlSEFSDRPCLIDGATGR-VYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLG 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2676 ILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQSAH------LGIMNGsLPVILLDDGE---------TRPFDNEPDT 2740
Cdd:PLN02246 95 ASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQSCYvdklkgLAEDDG-VTVVTIDDPPegclhfselTQADENELPE 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2741 PldarkqGLTPRHLAYVIYTSGSTGKPKGVMVEHANMVNflcsmrkepGIAQ-------------EDVLLGVTSLsFDI- 2806
Cdd:PLN02246 174 V------EISPDDVVALPYSSGTTGLPKGVMLTHKGLVT---------SVAQqvdgenpnlyfhsDDVILCVLPM-FHIy 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2807 ---SILeiFLPLLNGARLILATQAQAADAQQlamLIERHAVSFMQATP-----------------STWRMLvelrdfalp 2866
Cdd:PLN02246 238 slnSVL--LCGLRVGAAILIMPKFEIGALLE---LIQRHKVTIAPFVPpivlaiakspvvekydlSSIRMV--------- 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2867 pgfkaLCGGEALPENLATALLQKV--TTLWNLYGPTE--TTIWSTLNGLTTPTPY----IGHPIANTQIYILDAQ-GRVV 2937
Cdd:PLN02246 304 -----LSGAAPLGKELEDAFRAKLpnAVLGQGYGMTEagPVLAMCLAFAKEPFPVksgsCGTVVRNAELKIVDPEtGASL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2938 PLGVAGEIHIAGAGVVRGYLGRPDLTAErfitdpfsgapearmykTGDLGRWLPDGTLEYLGRND--FQV-------KVR 3008
Cdd:PLN02246 379 PRNQPGEICIRGPQIMKGYLNDPEATAN-----------------TIDKDGWLHTGDIGYIDDDDelFIVdrlkeliKYK 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3009 GFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEY-MIPSAFVTlDAFPLT 3087
Cdd:PLN02246 442 GFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYkRIHKVFFV-DSIPKA 520
|
570
....*....|..
gi 641744967 3088 PNGKLDRKALPA 3099
Cdd:PLN02246 521 PSGKILRKDLRA 532
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
2632-2995 |
1.52e-16 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 86.12 E-value: 1.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVR--PDERVAI----CVErgldMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAK-P 2704
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIysinRPE----WIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEiS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2705 VALISqsahlgimnGSLPVILLDD----GETRPFDNEPDTPLDarkqgltprhLAYVIYTSGSTGKPKGVMVEHANMVNF 2780
Cdd:cd05927 82 IVFCD---------AGVKVYSLEEfeklGKKNKVPPPPPKPED----------LATICYTSGTTGNPKGVMLTHGNIVSN 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2781 LCSMRKEPGIA----QEDVLLGVTSLS--FDISILEIFlpLLNGA---------RLILATQAQAADAQQLAM--LIER-H 2842
Cdd:cd05927 143 VAGVFKILEILnkinPTDVYISYLPLAhiFERVVEALF--LYHGAkigfysgdiRLLLDDIKALKPTVFPGVprVLNRiY 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2843 A--VSFMQATPSTWRMLVelrDFAL-------------PPGF---------KALCGGE-------ALP------ENLATA 2885
Cdd:cd05927 221 DkiFNKVQAKGPLKRKLF---NFALnyklaelrsgvvrASPFwdklvfnkiKQALGGNvrlmltgSAPlspevlEFLRVA 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2886 LlqKVTTLWNlYGPTETTIWSTLN--GLTTPTpYIGHPIANTQI----------YILDAQGRvvplgvaGEIHIAGAGVV 2953
Cdd:cd05927 298 L--GCPVLEG-YGQTECTAGATLTlpGDTSVG-HVGGPLPCAEVklvdvpemnyDAKDPNPR-------GEVCIRGPNVF 366
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 641744967 2954 RGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTL 2995
Cdd:cd05927 367 SGYYKDPEKTAEALDEDGW--------LHTGDIGEWLPNGTL 400
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1543-2021 |
1.71e-16 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 86.49 E-value: 1.71e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1543 DTTAVLFE------DQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAER 1616
Cdd:PLN02654 104 DKIAIYWEgnepgfDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAES 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1617 LAYMLDDASPVALLT----QANQRALLTGDVPRILLDTADFSHLS---------------EDNPHVPG------------ 1665
Cdd:PLN02654 184 LAQRIVDCKPKVVITcnavKRGPKTINLKDIVDAALDESAKNGVSvgicltyenqlamkrEDTKWQEGrdvwwqdvvpny 263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1666 --------LDAHHLAYVIYTSGSTGKPKGVMNSHRALcnrLVWMQNTYRltpddrvlqktpFSFDVSVWEFFW------- 1730
Cdd:PLN02654 264 ptkcevewVDAEDPLFLLYTSGSTGKPKGVLHTTGGY---MVYTATTFK------------YAFDYKPTDVYWctadcgw 328
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1731 ----------PLLYGAR-LVMARPDGHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWAD---ADCACDSLRRVICSGEA 1796
Cdd:PLN02654 329 itghsyvtygPMLNGATvLVFEGAPNYPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDeyvTRHSRKSLRVLGSVGEP 408
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1797 LPAELQQRFFarfnaqlhNLYGPTEAAIDVTFW-------------ACQPDDHRSFVpigRPIANTQLYILDTLGQPVPL 1863
Cdd:PLN02654 409 INPSAWRWFF--------NVVGDSRCPISDTWWqtetggfmitplpGAWPQKPGSAT---FPFFGVQPVIVDEKGKEIEG 477
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1864 GVAGELHIGGV--GVARGYLNrpdlTAERFIPDPFinQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEI 1941
Cdd:PLN02654 478 ECSGYLCVKKSwpGAFRTLYG----DHERYETTYF--KPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEV 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1942 EARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVtPDPADLRQQLGQHLAEYMvpGAFVTLDA------FPLTPNGK 2015
Cdd:PLN02654 552 ESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGV-PYSEELRKSLILTVRNQI--GAFAAPDKihwapgLPKTRSGK 628
|
....*.
gi 641744967 2016 LDRKAL 2021
Cdd:PLN02654 629 IMRRIL 634
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
499-965 |
2.09e-16 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 85.42 E-value: 2.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQS 578
Cdd:PLN02246 51 YTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAKQAKASGAKLIITQS 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 AQVAQL-----NSTLPTVLLDTPA---------AAACPDTNPVVQgLHAAHLAYVIYTSGSTGRPKGVMVAHRNVI---- 640
Cdd:PLN02246 131 CYVDKLkglaeDDGVTVVTIDDPPegclhfselTQADENELPEVE-ISPDDVVALPYSSGTTGLPKGVMLTHKGLVtsva 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 641 --------NLatGLHT------LLALDHpsrI-ALNaSIVFDAsvknwiqLLSGHTLVLVPdalRADAHQLWRYFARHAV 705
Cdd:PLN02246 210 qqvdgenpNL--YFHSddvilcVLPMFH---IySLN-SVLLCG-------LRVGAAILIMP---KFEIGALLELIQRHKV 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 706 DLFDCTPvqlqwlldaglgsdpayqPAQVLIggeAISPAVWSR-LQS--------------LSDT---RFINV-----YG 762
Cdd:PLN02246 274 TIAPFVP------------------PIVLAI---AKSPVVEKYdLSSirmvlsgaaplgkeLEDAfraKLPNAvlgqgYG 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 763 PTECTVDATACVVDRTQPLPTigKPLA------NTRLYILD-------AQDQPvpigvtGELHIGGAGVARGYLHRPDLT 829
Cdd:PLN02246 333 MTEAGPVLAMCLAFAKEPFPV--KSGScgtvvrNAELKIVDpetgaslPRNQP------GEICIRGPQIMKGYLNDPEAT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 830 AErfipdpfsadpaariykTGDLARWLPDGNIDYLGRND--F-------QIKVRGFRIEAGEIESRLLRCPGVQDAVVIA 900
Cdd:PLN02246 405 AN-----------------TIDKDGWLHTGDIGYIDDDDelFivdrlkeLIKYKGFQVAPAELEALLISHPSIADAAVVP 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 901 REDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADY-MIPSAFVTlDALPLTPNGKLDRKALPA 965
Cdd:PLN02246 468 MKDEVAGEVPVAFVVRSNGSEITEDEIKQFVAKQVVFYkRIHKVFFV-DSIPKAPSGKILRKDLRA 532
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1536-1995 |
3.11e-16 |
|
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: 85.20 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1536 DQAARTPDTTAVLFEDQHLTYDALNRRANQLAH-HLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPA 1614
Cdd:cd17632 50 TDPATGRTTLRLLPRFETITYAELWERVGAVAAaHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASA 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1615 ERLAYMLDDASP------VALLTQANQRALLTGDVPRILLdtadFSHLSEDNPH-------------------------- 1662
Cdd:cd17632 130 AQLAPILAETEPrllavsAEHLDLAVEAVLEGGTPPRLVV----FDHRPEVDAHraalesarerlaavgipvttltliav 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1663 -----------VPGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKtpfsfdvsvwefFWP 1731
Cdd:cd17632 206 rgrdlppaplfRPEPDDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLN------------FMP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1732 LLY-GARLVMARPDGHKDAAY------LAQLIERTGI---TTLHFVP---SMLQQ---------FVQWADADCACDSLR- 1788
Cdd:cd17632 274 MSHiAGRISLYGTLARGGTAYfaaasdMSTLFDDLALvrpTELFLVPrvcDMLFQryqaeldrrSVAGADAETLAERVKa 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1789 ---------RV---ICSGEALPAELQQRFFARFNAQLHNLYGPTEAAIDVTfwacqpdDHRSFVPigrPIANTQLYILDT 1856
Cdd:cd17632 354 elrervlggRLlaaVCGSAPLSAEMKAFMESLLDLDLHDGYGSTEAGAVIL-------DGVIVRP---PVLDYKLVDVPE 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1857 LG-----QPVPlgvAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGD-LARWLPDgSLEYLGRNDFQVK 1930
Cdd:cd17632 424 LGyfrtdRPHP---RGELLVKTDTLFPGYYKRPEVTAEVFDEDGF--------YRTGDvMAELGPD-RLVYVDRRNNVLK 491
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 1931 L-RGFRIELGEIEARLMQCPGVQEAVVVAredSPGDTRLVAYLCPQPGVTP--DPADLRQQLGQHLAE 1995
Cdd:cd17632 492 LsQGEFVTVARLEAVFAASPLVRQIFVYG---NSERAYLLAVVVPTQDALAgeDTARLRAALAESLQR 556
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
2619-3097 |
3.11e-16 |
|
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: 85.24 E-value: 3.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2619 TPDAIAVVF-----GEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPL------- 2686
Cdd:cd05970 30 YPDKLALVWcddagEERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPAthqltak 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2687 DPTYPVERLrymldDAKPVALISQSAHLGIMNGSLPVILLDDGETRPFDNEPDTPLDARKQ------GLTPRH------- 2753
Cdd:cd05970 110 DIVYRIESA-----DIKMIVAIAEDNIPEEIEKAAPECPSKPKLVWVGDPVPEGWIDFRKLiknaspDFERPTansypcg 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2754 --LAYVIYTSGSTGKPKgvMVEHANM--VNFLCSMRKEPGIAQEDVLLGVTSLSFDISIL-EIFLPLLNGARLILATQAQ 2828
Cdd:cd05970 185 edILLVYFSSGTTGMPK--MVEHDFTypLGHIVTAKYWQNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFVYDYDK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2829 AADAQqlaML--IERHAVSFMQATPSTWRMLV--ELRDFALPPGFKALCGGEALPENLATALLQKV-TTLWNLYGPTETT 2903
Cdd:cd05970 263 FDPKA---LLekLSKYGVTTFCAPPTIYRFLIreDLSRYDLSSLRYCTTAGEALNPEVFNTFKEKTgIKLMEGFGQTETT 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2904 IW-STLNGLTTPTPYIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGA-----GVVRGYLGRPDLTAERFitdpFSGape 2977
Cdd:cd05970 340 LTiATFPWMEPKPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEVW----HDG--- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2978 arMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARchgvHDAVV-IAREDSPGDKR-------LVAYLL 3049
Cdd:cd05970 413 --YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQ----HPAVLeCAVTGVPDPIRgqvvkatIVLAKG 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 641744967 3050 AQPDTVLEpADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05970 487 YEPSEELK-KELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
1677-1993 |
3.25e-16 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 84.05 E-value: 3.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1677 TSGSTGKPKGVMNSHRALcnrLVWMQNTYR------LTPDDRVLqkTPFSFDVSVWefFWPLLYGARLV--MARPDGHKD 1748
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDL---DRWAELFARslraagVRPGDRVQ--NAFGYGLFTG--GLGLHYGAERLgaTVIPAGGGN 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1749 AAYLAQLIERTGITTLHFVPSMLQQFVQWADA---DCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAAID 1825
Cdd:COG1541 164 TERQLRLMQDFGPTVLVGTPSYLLYLAEVAEEegiDPRDLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEVGPG 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1826 VtFWACQ-------PDDHRsFVPIGRPiantqlyilDTlGQPVPLGVAGELHIGGvgvargylnrpdLTAERFipdPFIN 1898
Cdd:COG1541 244 V-AYECEaqdglhiWEDHF-LVEIIDP---------ET-GEPVPEGEEGELVVTT------------LTKEAM---PLIR 296
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1899 qpgarlYKTGDLARWLPDGS--------LEY-LGRNDFQVKLRGFRIELGEIEARLMQCPGVQEA--VVVAREDspGDTR 1967
Cdd:COG1541 297 ------YRTGDLTRLLPEPCpcgrthprIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEyqIVVDREG--GLDE 368
|
330 340
....*....|....*....|....*.
gi 641744967 1968 LVAYLCPQPGVtpDPADLRQQLGQHL 1993
Cdd:COG1541 369 LTVRVELAPGA--SLEALAEAIAAAL 392
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1543-2021 |
4.43e-16 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 84.81 E-value: 4.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1543 DTTAVLFE------DQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAER 1616
Cdd:PRK00174 82 DKVAIIWEgddpgdSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVVFGGFSAEA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1617 LAYMLDDASPVALLT-------------QAN-QRALLTGD-------VPRILLDTA-----DF------SHLSEDNPHVP 1664
Cdd:PRK00174 162 LADRIIDAGAKLVITadegvrggkpiplKANvDEALANCPsvekvivVRRTGGDVDwvegrDLwwhelvAGASDECEPEP 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1665 gLDAHHLAYVIYTSGSTGKPKGVMNSHRALcnrLVWMQNTYRLTpddrvlqktpfsFDVSVWEFFW-------------- 1730
Cdd:PRK00174 242 -MDAEDPLFILYTSGSTGKPKGVLHTTGGY---LVYAAMTMKYV------------FDYKDGDVYWctadvgwvtghsyi 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1731 ---PLLYGARLVM--ARPDgHKDAAYLAQLIERTGITTLHFVPSMLQQFVQWADA-----DCAcdSLRrVICS-GEALPA 1799
Cdd:PRK00174 306 vygPLANGATTLMfeGVPN-YPDPGRFWEVIDKHKVTIFYTAPTAIRALMKEGDEhpkkyDLS--SLR-LLGSvGEPINP 381
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1800 ELQQRFfarfnaqlHNLYGPTEAAIDVTFW--------------AcqpddhrsfVPI-----GRPIANTQLYILDTLGQP 1860
Cdd:PRK00174 382 EAWEWY--------YKVVGGERCPIVDTWWqtetggimitplpgA---------TPLkpgsaTRPLPGIQPAVVDEEGNP 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1861 VPLGVAGELHIGGV--GVARGYLNRPdltaERFIPDPFINQPGarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIEL 1938
Cdd:PRK00174 445 LEGGEGGNLVIKDPwpGMMRTIYGDH----ERFVKTYFSTFKG--MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGT 518
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1939 GEIEARLMQCPGVQEAVVVARedsPGDTR---LVAYLCPQPGVTPDPAdLRQQLGQHLAEYMVPGA------FVtlDAFP 2009
Cdd:PRK00174 519 AEIESALVAHPKVAEAAVVGR---PDDIKgqgIYAFVTLKGGEEPSDE-LRKELRNWVRKEIGPIAkpdviqFA--PGLP 592
|
570
....*....|..
gi 641744967 2010 LTPNGKLDRKAL 2021
Cdd:PRK00174 593 KTRSGKIMRRIL 604
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
882-957 |
5.28e-16 |
|
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: 74.89 E-value: 5.28e-16
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 882 EIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGK 957
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1554-1976 |
5.76e-16 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 84.19 E-value: 5.76e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVK--PDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLT 1631
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKpaPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1632 QAnqralltgDVPRILLDtaDFSHLSEDN--PHVPGlDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLV----WMQNTY 1705
Cdd:cd05927 86 DA--------GVKVYSLE--EFEKLGKKNkvPPPPP-KPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAgvfkILEILN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1706 RLTPDDRVLQKTPFS--FDVSVWEFFwpLLYGARLvmarpdG--HKDAAYLA---------------QLIER--TGITTL 1764
Cdd:cd05927 155 KINPTDVYISYLPLAhiFERVVEALF--LYHGAKI------GfySGDIRLLLddikalkptvfpgvpRVLNRiyDKIFNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1765 HFVPSMLQQFVqwadADCACDS----LR--------------------------RVICSGEA-LPAELQQRFFARFNAQL 1813
Cdd:cd05927 227 VQAKGPLKRKL----FNFALNYklaeLRsgvvraspfwdklvfnkikqalggnvRLMLTGSApLSPEVLEFLRVALGCPV 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1814 HNLYGPTE--AAIDVTFwacqPDDHrSFVPIGRPIANTQLYILDtlgqpVP-LGV-------AGELHIGGVGVARGYLNR 1883
Cdd:cd05927 303 LEGYGQTEctAGATLTL----PGDT-SVGHVGGPLPCAEVKLVD-----VPeMNYdakdpnpRGEVCIRGPNVFSGYYKD 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1884 PDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSLEYLGR--NDFqvKL-RGFRIELGEIEARLMQCPGVQEAVVVare 1960
Cdd:cd05927 373 PEKTAEALDEDGW--------LHTGDIGEWLPNGTLKIIDRkkNIF--KLsQGEYVAPEKIENIYARSPFVAQIFVY--- 439
|
490
....*....|....*....
gi 641744967 1961 dspGD---TRLVAYLCPQP 1976
Cdd:cd05927 440 ---GDslkSFLVAIVVPDP 455
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
475-965 |
5.83e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 84.31 E-value: 5.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 475 IQQRFEAQAEQTpeAIAVLFEDQHLTYRELNRRANQLAHHLIALGvQPDDR--VALCVERSLEMMVGLLGILKAGAAYVP 552
Cdd:PRK13388 5 IAQLLRDRAGDD--TIAVRYGDRTWTWREVLAEAAARAAALIALA-DPDRPlhVGVLLGNTPEMLFWLAAAALGGYVLVG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 553 MDPAYPAERLAYILDDAAPVALLTQSAQVAQLN----STLPTVLLDTPA----AAACPDTNPVVQgLHAAHLAYVIYTSG 624
Cdd:PRK13388 82 LNTTRRGAALAADIRRADCQLLVTDAEHRPLLDgldlPGVRVLDVDTPAyaelVAAAGALTPHRE-VDAMDPFMLIFTSG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 625 STGRPKGVMVAHRNVINLATGLHTLLALdHPSRIALNASIVF--DASVKNW-IQLLSGHTLVLVPdalRADAHQLWRYFA 701
Cdd:PRK13388 161 TTGAPKAVRCSHGRLAFAGRALTERFGL-TRDDVCYVSMPLFhsNAVMAGWaPAVASGAAVALPA---KFSASGFLDDVR 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 702 RHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAiSPAVWSRLQSLSDTRFINVYGPTEctvDATACVVDRTQPL 781
Cdd:PRK13388 237 RYGATYFNYVGKPLAYILATPERPDDADNPLRVAFGNEA-SPRDIAEFSRRFGCQVEDGYGSSE---GAVIVVREPGTPP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 782 PTIGKPLANTRLYILDA-QDQPV-----------PIGVTGEL-HIGGAGVARGYLHRPDLTAERFipdpfsadpAARIYK 848
Cdd:PRK13388 313 GSIGRGAPGVAIYNPETlTECAVarfdahgallnADEAIGELvNTAGAGFFEGYYNNPEATAERM---------RHGMYW 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 849 TGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALR 928
Cdd:PRK13388 384 SGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVLRDGATFDPDAFA 463
|
490 500 510
....*....|....*....|....*....|....*....
gi 641744967 929 QQLAAS--LADYMIPSAFVTLDALPLTPNGKLDRKALPA 965
Cdd:PRK13388 464 AFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1842-2021 |
7.02e-16 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 84.10 E-value: 7.02e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1842 IGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSLEY 1921
Cdd:PRK12492 388 VGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEALDAEGW--------FKTGDIAVIDPDGFVRI 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1922 LGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQ-PGVTPDpaDLRQQLGQHLAEYMVPG 2000
Cdd:PRK12492 460 VDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVVARdPGLSVE--ELKAYCKENFTGYKVPK 537
|
170 180
....*....|....*....|.
gi 641744967 2001 AFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK12492 538 HIVLRDSLPMTPVGKILRREL 558
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1549-1957 |
8.24e-16 |
|
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: 83.25 E-value: 8.24e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1549 FEDQHLTYDALNRRANQLAHHLID-LGVKPDDRIAICVERSLDMVIGLLAILKAGAAyvpldpgyPAeRLAYMLDDASPV 1627
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA--------PA-FINYNLSGDPLI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1628 ALLTQANQRALL-TGDVPRILldtadfshlsednphvpgldahhlayvIYTSGSTGKPKGVMNSHRaLCNRLVW-MQNTY 1705
Cdd:cd05937 72 HCLKLSGSRFVIvDPDDPAIL---------------------------IYTSGTTGLPKAAAISWR-RTLVTSNlLSHDL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1706 RLTPDDRVLQKTP-FSFDVSVWEFFWPLLYGARLVMAR--------PDGHKDAAYLAQLIERTGITTLHFVPSMLqqfvq 1776
Cdd:cd05937 124 NLKNGDRTYTCMPlYHGTAAFLGACNCLMSGGTLALSRkfsasqfwKDVRDSGATIIQYVGELCRYLLSTPPSPY----- 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1777 wadadcacDSLRRVICS-GEALPAELQQRFFARFN-AQLHNLYGPTEAAIdvTFWACQPDD-------HRSfvPIGRPIA 1847
Cdd:cd05937 199 --------DRDHKVRVAwGNGLRPDIWERFRERFNvPEIGEFYAATEGVF--ALTNHNVGDfgagaigHHG--LIRRWKF 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1848 NTQLYI----LDTlGQP-----------VPLGVAGE----LHIGGVGVARGYLNRPDLTAERFIPDPFinQPGARLYKTG 1908
Cdd:cd05937 267 ENQVVLvkmdPET-DDPirdpktgfcvrAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVF--RKGDIYFRTG 343
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 641744967 1909 DLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVV 1957
Cdd:cd05937 344 DLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVY 392
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1668-1958 |
1.00e-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: 83.31 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1668 AHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWEF-FWPLLYGA-------RLV 1739
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFhLAPLIAGMnqylmptRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1740 MARPdghkdAAYLAQLIER--TGITTLHFVPS-MLQQFVQWADADCACDSLRRVICSGEALPAELQQRFFARFNA----- 1811
Cdd:cd05908 185 IRRP-----ILWLKKASEHkaTIVSSPNFGYKyFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKyglkr 259
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1812 -QLHNLYGPTEAAIDVTFWACQPD------DHR-------------------SFVPIGRPIANTQLYILDTLGQPVPLGV 1865
Cdd:cd05908 260 nAILPVYGLAEASVGASLPKAQSPfktitlGRRhvthgepepevdkkdseclTFVEVGKPIDETDIRICDEDNKILPDGY 339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1866 AGELHIGGVGVARGYLNRPDLTAERFIPDPFInqpgarlyKTGDLArWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARL 1945
Cdd:cd05908 340 IGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL--------KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIA 410
|
330
....*....|...
gi 641744967 1946 MQCPGVQEAVVVA 1958
Cdd:cd05908 411 EELEGVELGRVVA 423
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
494-963 |
1.27e-15 |
|
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: 82.87 E-value: 1.27e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 494 FEDQHLTYRELNRRANQLAHHLI-ALGVQPDDRVALCVERSLEMMVGLLGILKAGAAyvpmdPAYpaerLAYILDDAAPV 572
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHdDLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA-----PAF----INYNLSGDPLI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 573 ALLTQSaqvaqlNSTLPTVLLDTPAAaacpdtnpvvqglhaahlayVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLAL 652
Cdd:cd05937 72 HCLKLS------GSRFVIVDPDDPAI--------------------LIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 653 DHPSRI--------ALNASIVFDASvknwiqLLSGHTLVLVPdalRADAHQLWRyfarhAVDLFDCTPVQ-----LQWLL 719
Cdd:cd05937 126 KNGDRTytcmplyhGTAAFLGACNC------LMSGGTLALSR---KFSASQFWK-----DVRDSGATIIQyvgelCRYLL 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 720 DAGLGSDPAYQPAQVLIGgEAISPAVWSRLQSlsdtRFiNV------YGPTECTV--------DATACVVDRTQPL---- 781
Cdd:cd05937 192 STPPSPYDRDHKVRVAWG-NGLRPDIWERFRE----RF-NVpeigefYAATEGVFaltnhnvgDFGAGAIGHHGLIrrwk 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 782 ----PTIGKPLANTRLYILDAQD---QPVPIGVTGE----LHIGGAGVARGYLHRPDLTAERFIPDPFSADPAarIYKTG 850
Cdd:cd05937 266 fenqVVLVKMDPETDDPIRDPKTgfcVRAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVFRKGDI--YFRTG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 851 DLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAALRQQ 930
Cdd:cd05937 344 DLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAITLEESSAVPTEFTKS 423
|
490 500 510
....*....|....*....|....*....|....*...
gi 641744967 931 LAASLADYMIPSAFVTL-----DALPLTPNGKLDRKAL 963
Cdd:cd05937 424 LLASLARKNLPSYAVPLflrltEEVATTDNHKQQKGVL 461
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
2633-3070 |
1.38e-15 |
|
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: 83.25 E-value: 1.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2633 SYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPV-----ERLRYMLDDAKPVAL 2707
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLmsqdlAKLKHLFELLKPGLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2708 ISQSAHL------GIMNGSLPVI----LLDDGETRPFDNEPDTP----LDARKQGLTPRHLAYVIYTSGSTGKPKGVMVE 2773
Cdd:cd05921 107 FAQDAAPfaralaAIFPLGTPLVvsrnAVAGRGAISFAELAATPptaaVDAAFAAVGPDTVAKFLFTSGSTGLPKAVINT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2774 HANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISI---LEIFLPLLNGARLILATQAQAADAQQLAM--LIERHAVSFMQ 2848
Cdd:cd05921 187 QRMLCANQAMLEQTYPFFGEEPPVLVDWLPWNHTFggnHNFNLVLYNGGTLYIDDGKPMPGGFEETLrnLREISPTVYFN 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2849 AtPSTWRMLVEL--RDFALPPGF----KALC-GGEALPENLATAlLQKVT--------TLWNLYGPTETTIWSTL-NGLT 2912
Cdd:cd05921 267 V-PAGWEMLVAAleKDEALRRRFfkrlKLMFyAGAGLSQDVWDR-LQALAvatvgeriPMMAGLGATETAPTATFtHWPT 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2913 TPTPYIGHPIANTQIyildaqgRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWL-- 2990
Cdd:cd05921 345 ERSGLIGLPAPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF--------YCLGDAAKLAdp 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2991 --PDGTLEYLGR--NDFQVKvRGFRIELGEIETRL-ARCHG-VHDAVVIA--RE--------DSPGDKRLVAYLLAQPDT 3054
Cdd:cd05921 410 ddPAKGLVFDGRvaEDFKLA-SGTWVSVGPLRARAvAACAPlVHDAVVAGedRAevgalvfpDLLACRRLVGLQEASDAE 488
|
490
....*....|....*.
gi 641744967 3055 VLEPADLRQRLSEGVA 3070
Cdd:cd05921 489 VLRHAKVRAAFRDRLA 504
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
2751-3029 |
1.50e-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: 82.54 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2751 PRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFL-PLLNGARLILATQAQA 2829
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLaPLIAGMNQYLMPTRLF 184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2830 ADAQQLAML-IERHAVSFMQATPSTWRMLVE------LRDFALPPGFKALCGGEALPENLATALLQ-------KVTTLWN 2895
Cdd:cd05908 185 IRRPILWLKkASEHKATIVSSPNFGYKYFLKtlkpekANDWDLSSIRMILNGAEPIDYELCHEFLDhmskyglKRNAILP 264
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2896 LYGPTETTIWSTLNGLTTP--TPYIGH---------------------------PIANTQIYILDAQGRVVPLGVAGEIH 2946
Cdd:cd05908 265 VYGLAEASVGASLPKAQSPfkTITLGRrhvthgepepevdkkdsecltfvevgkPIDETDIRICDEDNKILPDGYIGHIQ 344
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2947 IAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGrWLPDGTLEYLGRNDFQVKVRGFRIELGEIET------- 3019
Cdd:cd05908 345 IRGKNVTPGYYNNPEATAKVFTDDGW--------LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERiaeeleg 415
|
330
....*....|....
gi 641744967 3020 ----RLARChGVHD 3029
Cdd:cd05908 416 velgRVVAC-GVNN 428
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
621-965 |
1.77e-15 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 82.97 E-value: 1.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 621 YTSGSTGRPKGVMVAHRNVInlatglhtLLALDHPSRIALNASIVF---------DASVKNW-IQLLSGHTLVLvpdaLR 690
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGAY--------LMALSNALIWGMNEGAVYlwtlpmfhcNGWCFTWtLAALCGTNICL----RQ 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 691 ADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSD--PAYQPAQVLIGGEAISPAVWSRLqSLSDTRFINVYGPTECTV 768
Cdd:PLN02479 270 VTAKAIYSAIANYGVTHFCAAPVVLNTIVNAPKSETilPLPRVVHVMTAGAAPPPSVLFAM-SEKGFRVTHTYGLSETYG 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 769 DATACVvdrTQP----LPTIGKPLANTR----------LYILDAQD-QPVPI-GVT-GELHIGGAGVARGYLHRPDLTAE 831
Cdd:PLN02479 349 PSTVCA---WKPewdsLPPEEQARLNARqgvryiglegLDVVDTKTmKPVPAdGKTmGEIVMRGNMVMKGYLKNPKANEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 832 RFipdpfsadpAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLV 911
Cdd:PLN02479 426 AF---------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDERWGESPC 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 912 AYLCARPDAELH-PAALRQQLAA----SLADYMIPSAfVTLDALPLTPNGKLDRKALPA 965
Cdd:PLN02479 497 AFVTLKPGVDKSdEAALAEDIMKfcreRLPAYWVPKS-VVFGPLPKTATGKIQKHVLRA 554
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
496-963 |
1.81e-15 |
|
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: 82.09 E-value: 1.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 496 DQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALL 575
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 576 TQsaqvaqlnstlptvlLDTPAAAACPDTNPVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALdHP 655
Cdd:cd05939 81 FN---------------LLDPLLTQSSTEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGM-RP 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 656 SRIALN--------ASIVFDASVknwiqLLSGHTLVLVPdalRADAHQLWRYFARHavdlfDCTPVQL-----QWLLDAG 722
Cdd:cd05939 145 EDVVYDclplyhsaGGIMGVGQA-----LLHGSTVVIRK---KFSASNFWDDCVKY-----NCTIVQYigeicRYLLAQP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 723 LgsDPAYQPAQV-LIGGEAISPAVWSRLQSlsdtRFiNV------YGPTECT-----VDAT--ACVVdrtqpLPTIGKPL 788
Cdd:cd05939 212 P--SEEEQKHNVrLAVGNGLRPQIWEQFVR----RF-GIpqigefYGATEGNsslvnIDNHvgACGF-----NSRILPSV 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 789 ANTRLYILDAqdqpvpigVTGELHIGGAGVA------------------------RGYLHRPDlTAERFIPDPF-SADPA 843
Cdd:cd05939 280 YPIRLIKVDE--------DTGELIRDSDGLCipcqpgepgllvgkiiqndplrrfDGYVNEGA-TNKKIARDVFkKGDSA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 844 ariYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELH 923
Cdd:cd05939 351 ---FLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGVEVPGVEGRAGMAAIVDPERKVD 427
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 641744967 924 PAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05939 428 LDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
496-970 |
2.10e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 81.62 E-value: 2.10e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 496 DQHLTYRELNRRANQLAHHLIaLGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYP---AERLAyilDDAAPV 572
Cdd:PRK08308 6 DEEYSKSDFDLRLQRYEEMEQ-FQEAAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPkeaAIRMA---KRAGCH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 573 ALLTQSAQvaqlnstlpTVLLDTPAAAACPDTnpVVQglhaahlayviYTSGSTGRPKGVmvaHRNVINLATGLHTLLAL 652
Cdd:PRK08308 82 GLLYGESD---------FTKLEAVNYLAEEPS--LLQ-----------YSSGTTGEPKLI---RRSWTEIDREIEAYNEA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 653 dhPSRIALNASIVFdASVKNWIQLLSGhtlVLVpdALRADA--HQLWRYFARHAVDLFDCTPVQLqwlldagLGSDPA-- 728
Cdd:PRK08308 137 --LNCEQDETPIVA-CPVTHSYGLICG---VLA--ALTRGSkpVIITNKNPKFALNILRNTPQHI-------LYAVPLml 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 729 YQPAQVLIGGEAIS---------PAVW-SRLQSLSdTRFINVYGPTEctvdaTACVV---DRTQPLpTIGKPLANTRLYI 795
Cdd:PRK08308 202 HILGRLLPGTFQFHavmtsgtplPEAWfYKLRERT-TYMMQQYGCSE-----AGCVSicpDMKSHL-DLGNPLPHVSVSA 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 796 LDAQDQPVPIGVTgelhiggagvargylhrpdlTAERfipdpfsadpaaRIYkTGDLARWLPDGNIDYLGRNDFQIKVRG 875
Cdd:PRK08308 275 GSDENAPEEIVVK--------------------MGDK------------EIF-TKDLGYKSERGTLHFMGRMDDVINVSG 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 876 FRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCArpDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPN 955
Cdd:PRK08308 322 LNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVIS--HEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNAN 399
|
490
....*....|....*
gi 641744967 956 GKLDRKALPAPDQTA 970
Cdd:PRK08308 400 GKVSRKLLELGEVTA 414
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
500-963 |
2.44e-15 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 82.11 E-value: 2.44e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 500 TYRELNRRANQLAHHLIALGVQPDDRVALC---VERSLEMMVGLLGIlkaGAAYVPMDPAYPAERLAYILDDAAPVALLT 576
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 577 QSAQV---AQLNSTLPTV-----LLDtpaAAACPDT---NPVV--QGLHAAH------------LAYVIYTSGSTGRPKG 631
Cdd:PRK06018 118 DLTFVpilEKIADKLPSVeryvvLTD---AAHMPQTtlkNAVAyeEWIAEADgdfawktfdentAAGMCYTSGTTGDPKG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 632 VMVAHR-NVinlatgLHTLLALDHPSRIALNASIV------FDASvkNWIQLLS----GHTLVLvPDAlRADAHQLWRYF 700
Cdd:PRK06018 195 VLYSHRsNV------LHALMANNGDALGTSAADTMlpvvplFHAN--SWGIAFSapsmGTKLVM-PGA-KLDGASVYELL 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 701 ARHAVDLFDCTPVQLQWLLDAgLGSDPAYQP--AQVLIGGEAISPAVWSRLQSLsDTRFINVYGPTEctvdatacvvdrT 778
Cdd:PRK06018 265 DTEKVTFTAGVPTVWLMLLQY-MEKEGLKLPhlKMVVCGGSAMPRSMIKAFEDM-GVEVRHAWGMTE------------M 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 779 QPLPTIGK---PLANT----RLYILDAQDQPvPIGV------------------TGELHIGGAGVARGYLHrpdltAERF 833
Cdd:PRK06018 331 SPLGTLAAlkpPFSKLpgdaRLDVLQKQGYP-PFGVemkitddagkelpwdgktFGRLKVRGPAVAAAYYR-----VDGE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 834 IPDpfsadpAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAY 913
Cdd:PRK06018 405 ILD------DDGFFDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLI 478
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 641744967 914 LCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:PRK06018 479 VQLKPGETATREEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1539-2020 |
3.07e-15 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 82.10 E-value: 3.07e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1539 ARTPDTTAVlfedqHLTYDALNRRANQLAHHLIDLgVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLD----PGYpA 1614
Cdd:PRK12476 59 SHSAAGCAV-----ELTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFapelPGH-A 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1615 ERLAYMLDDASPVALLTQANQ--------RALLTGDVPRILLDTADFSHLSEDNPHVPgLDAHHLAYVIYTSGSTGKPKG 1686
Cdd:PRK12476 132 ERLDTALRDAEPTVVLTTTAAaeavegflRNLPRLRRPRVIAIDAIPDSAGESFVPVE-LDTDDVSHLQYTSGSTRPPVG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1687 VMNSHRALCNRLVWM-QNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLVMARPDG--HKDAAYLAQLIErtGITT 1763
Cdd:PRK12476 211 VEITHRAVGTNLVQMiLSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMSPTAfvRRPQRWIKALSE--GSRT 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1764 LHFVPSMLQQFVQWA-----DADCACDSLRRV--ICSGEALPAELQQRF---FARFN---AQLHNLYGPTEAAIDVTFWA 1830
Cdd:PRK12476 289 GRVVTAAPNFAYEWAaqrglPAEGDDIDLSNVvlIIGSEPVSIDAVTTFnkaFAPYGlprTAFKPSYGIAEATLFVATIA 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1831 CQ---------------------PDDHRSFVP---IGRPIANTQLYILD-TLGQPVPLGVAGELHIGGVGVARGYLNRPD 1885
Cdd:PRK12476 369 PDaepsvvyldreqlgagravrvAADAPNAVAhvsCGQVARSQWAVIVDpDTGAELPDGEVGEIWLHGDNIGRGYWGRPE 448
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1886 LTAErfipdPFINQPGARL---------------YKTGDLARWLpDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQC-- 1948
Cdd:PRK12476 449 ETER-----TFGAKLQSRLaegshadgaaddgtwLRTGDLGVYL-DGELYITGRIADLIVIDGRNHYPQDIEATVAEAsp 522
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1949 ------------PGV--QEAVVVArEDSPGDTRLVaylcPQPGVTPDPADLRQQLGQHLAEYMvpgaFVTLDAFPLTPNG 2014
Cdd:PRK12476 523 mvrrgyvtaftvPAEdnERLVIVA-ERAAGTSRAD----PAPAIDAIRAAVSRRHGLAVADVR----LVPAGAIPRTTSG 593
|
....*.
gi 641744967 2015 KLDRKA 2020
Cdd:PRK12476 594 KLARRA 599
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1552-1957 |
3.23e-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: 81.75 E-value: 3.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1552 QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLT 1631
Cdd:cd05932 5 VEFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1632 -----QANQRALLTGDVPRILL---DTADFSHLSED-----NPHV--PGLDAHHLAYVIYTSGSTGKPKGVMNSHRAL-- 1694
Cdd:cd05932 85 gklddWKAMAPGVPEGLISISLpppSAANCQYQWDDliaqhPPLEerPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFaw 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1695 -CNRLVwmqNTYRLTPDDRVLQKTPFSFDVSVWEFFWPLLYGARLV--------------MARPDGHKDAAYLAQL---- 1755
Cdd:cd05932 165 aAQAGI---EHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVafaesldtfvedvqRARPTLFFSVPRLWTKfqqg 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1756 -IERTGITTLH------FVPSMLQQFVQwadADCACDSLRRVICSGEALPAELQQrFFARFNAQLHNLYGPTEAAIDVTF 1828
Cdd:cd05932 242 vQDKIPQQKLNlllkipVVNSLVKRKVL---KGLGLDQCRLAGCGSAPVPPALLE-WYRSLGLNILEAYGMTENFAYSHL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1829 waCQPDDHRsfvpIGrpiantqlyildTLGQPVP-----LGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFInqpgar 1903
Cdd:cd05932 318 --NYPGRDK----IG------------TVGNAGPgvevrISEDGEILVRSPALMMGYYKDPEATAEAFTADGFL------ 373
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 1904 lyKTGDLARWLPDGSLEYLGR-NDFQVKLRGFRIELGEIEARLMQCPGVQEAVVV 1957
Cdd:cd05932 374 --RTGDKGELDADGNLTITGRvKDIFKTSKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
485-958 |
3.49e-15 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 82.15 E-value: 3.49e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 485 QTPEAIAVLF--EDQH---LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPA 559
Cdd:PRK03584 96 RRDDRPAIIFrgEDGPrreLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATASLGAIWSSCSPDFGV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 560 ----ERLAYIlddaAPVALLT------------QSAQVAQLNSTLPTV--------LLDTPAAAACPDTNP---VVQGLH 612
Cdd:PRK03584 176 qgvlDRFGQI----EPKVLIAvdgyryggkafdRRAKVAELRAALPSLehvvvvpyLGPAAAAAALPGALLwedFLAPAE 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 613 AAHLA----------YVIYTSGSTGRPKGVMVAHRNVInL----ATGLHTLLaldHPSrialnaSIVFDASVKNWIQ--- 675
Cdd:PRK03584 252 AAELEfepvpfdhplWILYSSGTTGLPKCIVHGHGGIL-LehlkELGLHCDL---GPG------DRFFWYTTCGWMMwnw 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 676 ----LLSGHTLVLV------PDALRadahqLWRYFARHAVDLFDCTPVQLQWLLDAGLgsdpayQPAQ---------VLI 736
Cdd:PRK03584 322 lvsgLLVGATLVLYdgspfyPDPNV-----LWDLAAEEGVTVFGTSAKYLDACEKAGL------VPGEthdlsalrtIGS 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 737 GG------------EAISPAVWsrLQSLSdtrfinvyGPTectvDATACVV--DRTQPL-------PTIGkplanTRLYI 795
Cdd:PRK03584 391 TGsplppegfdwvyEHVKADVW--LASIS--------GGT----DICSCFVggNPLLPVyrgeiqcRGLG-----MAVEA 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 796 LDAQDQPVpIGVTGELhiggagVAR--------GYLHRPDltAERFIPDPFSADPAarIYKTGDLARWLPDGNIDYLGRN 867
Cdd:PRK03584 452 WDEDGRPV-VGEVGEL------VCTkpfpsmplGFWNDPD--GSRYRDAYFDTFPG--VWRHGDWIEITEHGGVVIYGRS 520
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 868 DFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPA---ALRQQLAASLADYMIPSAF 944
Cdd:PRK03584 521 DATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDAlraRIRTTIRTNLSPRHVPDKI 600
|
570
....*....|....
gi 641744967 945 VTLDALPLTPNGKL 958
Cdd:PRK03584 601 IAVPDIPRTLSGKK 614
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
468-866 |
3.61e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 82.08 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 468 DFPREMLIQQRFEAQAEQTPEAIAVLFED---------QHLTYRELNRRANQLAHHLIALGvQPDDRVALCVERSLEMMV 538
Cdd:PRK07769 16 RFPPNTNLVRHVERWAKVRGDKLAYRFLDfsterdgvaRDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 539 GLLGILKAGAAYVPM-DPAYP--AERLAYILDDAAPVALLTQSAQ---VAQLNSTLPTVllDTP---AAAACPDT----- 604
Cdd:PRK07769 95 AFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSaegVRKFFRARPAK--ERPrviAVDAVPDEvgatw 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 605 NPVVqgLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSR----------IALnASIVFDASVKNWI 674
Cdd:PRK07769 173 VPPE--ANEDTIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRgvswlpffhdMGL-ITVLLPALLGHYI 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 675 QLLSGHTLVLVP----DALRADAHQLWRYFARHAVDLFDCT-----PVQLQWLLD----AGL--GSDPAyQPAQVLIGGE 739
Cdd:PRK07769 250 TFMSPAAFVRRPgrwiRELARKPGGTGGTFSAAPNFAFEHAaarglPKDGEPPLDlsnvKGLlnGSEPV-SPASMRKFNE 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 740 AISPavwsrlQSLSDTRFINVYGPTECT-------VDATACV--VDRTQ-----------------PLPTIGKPLANTRL 793
Cdd:PRK07769 329 AFAP------YGLPPTAIKPSYGMAEATlfvsttpMDEEPTViyVDRDElnagrfvevpadapnavAQVSAGKVGVSEWA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 794 YILDA-QDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERF-------IPDPFS--ADPAARIYKTGDLARWLpDGNIDY 863
Cdd:PRK07769 403 VIVDPeTASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrLSESHAegAPDDALWVRTGDYGVYF-DGELYI 481
|
...
gi 641744967 864 LGR 866
Cdd:PRK07769 482 TGR 484
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
2163-2463 |
3.97e-15 |
|
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: 80.93 E-value: 3.97e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2163 PLAPLQEGILFHHLLQEQGDTYLLRsmVAFTHRERLD--AFLSALQQVIDRHDILRTaVCWQDLSQPVQVVW--RQAILP 2238
Cdd:cd19540 3 PLSFAQQRLWFLNRLDGPSAAYNIP--LALRLTGALDvdALRAALADVVARHESLRT-VFPEDDGGPYQVVLpaAEARPD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2239 INHfEPTSPEDVLAQLQAHTeprTRRIDLSQAPLFRAD-IAHDPlqNEWLLALSFHHLISDHMTLALIVGEI------RL 2311
Cdd:cd19540 80 LTV-VDVTEDELAARLAEAA---RRGFDLTAELPLRARlFRLGP--DEHVLVLVVHHIAADGWSMAPLARDLatayaaRR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2312 llqhqADALP--TPLP--YRNFiaqTL---------SVPNS---AHEAYFRDKLADVDEPTA-------PfgllNVQGSG 2368
Cdd:cd19540 154 -----AGRAPdwAPLPvqYADY---ALwqrellgdeDDPDSlaaRQLAYWRETLAGLPEELElptdrprP----AVASYR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2369 GDIHEARLvlDATLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRlaGAEGADRIMGMFINTLPLR 2448
Cdd:cd19540 222 GGTVEFTI--DAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGR--GDEALDDLVGMFVNTLVLR 297
|
330
....*....|....*.
gi 641744967 2449 ISLA-DRGAAEVVERT 2463
Cdd:cd19540 298 TDVSgDPTFAELLARV 313
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1538-1956 |
6.41e-15 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 81.08 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1538 AARTPDTTAVLFED-----QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGY 1612
Cdd:PRK08180 49 AQEAPDRVFLAERGadggwRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAY 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1613 PA-----ERLAYMLDDASPVALLTQANQR------ALLTGDVPRILL-------DTADFSHLSEDNPHvPGLDAHH---- 1670
Cdd:PRK08180 129 SLvsqdfGKLRHVLELLTPGLVFADDGAAfaralaAVVPADVEVVAVrgavpgrAATPFAALLATPPT-AAVDAAHaavg 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1671 ---LAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYrltpddRVLQKTPfsfDVSVWEFFWPLLYGARLVMARPDGHK 1747
Cdd:PRK08180 208 pdtIAKFLFTSGSTGLPKAVINTHRMLCANQQMLAQTF------PFLAEEP---PVLVDWLPWNHTFGGNHNLGIVLYNG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1748 DAAYL------AQLIERT------GITTLHF-VPSMLQQFVQWADADcacdslrrvicsgealpAELQQRFFAR----FN 1810
Cdd:PRK08180 279 GTLYIddgkptPGGFDETlrnlreISPTVYFnVPKGWEMLVPALERD-----------------AALRRRFFSRlkllFY 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1811 A----------QLHNL--------------YGPTEAAIDVTFwaCQPDDHRSFVpIGRPIANTQLYIldtlgqpVPLGVA 1866
Cdd:PRK08180 342 AgaalsqdvwdRLDRVaeatcgerirmmtgLGMTETAPSATF--TTGPLSRAGN-IGLPAPGCEVKL-------VPVGGK 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1867 GELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWL----PDGSLEYLGR--NDFqvKL-RGFRIELG 1939
Cdd:PRK08180 412 LEVRVKGPNVTPGYWRAPELTAEAFDEEGY--------YRSGDAVRFVdpadPERGLMFDGRiaEDF--KLsSGTWVSVG 481
|
490
....*....|....*....
gi 641744967 1940 EIEARL-MQC-PGVQEAVV 1956
Cdd:PRK08180 482 PLRARAvSAGaPLVQDVVI 500
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1525-2021 |
6.41e-15 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 80.79 E-value: 6.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1525 PHDALIHQLVEDQAARTPDTTAVL--FEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAG 1602
Cdd:PLN02330 25 PDKLTLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1603 AAYVPLDPGYPAERLAYMLDDASPVALLTQANQRALLTG-DVPRI---------------LLDTADFSHLSEDNPHVPGL 1666
Cdd:PLN02330 105 GVFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKVKGlGLPVIvlgeekiegavnwkeLLEAADRAGDTSDNEEILQT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1667 DahhLAYVIYTSGSTGKPKGVMNSHRALCNRLVwmQNTYRLTPDD----RVLQKTPFSFDVSVWEFFWPLLY--GARLVM 1740
Cdd:PLN02330 185 D---LCALPFSSGTTGISKGVMLTHRNLVANLC--SSLFSVGPEMigqvVTLGLIPFFHIYGITGICCATLRnkGKVVVM 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1741 ARPDGHkdaAYLAQLIERTgITTLHFVPSMLQQFVQ---WADADCACDSLRRVICSGEALPAELQQRFFARF-NAQLHNL 1816
Cdd:PLN02330 260 SRFELR---TFLNALITQE-VSFAPIVPPIILNLVKnpiVEEFDLSKLKLQAIMTAAAPLAPELLTAFEAKFpGVQVQEA 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1817 YGPTEAAIdVTFWACQPDDHRSFV---PIGRPIANTQLYILD-TLGQPVPLGVAGELHIGGVGVARGYLNRPDLTAERFI 1892
Cdd:PLN02330 336 YGLTEHSC-ITLTHGDPEKGHGIAkknSVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTID 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1893 PDPFINqpgarlykTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYL 1972
Cdd:PLN02330 415 EDGWLH--------TGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACV 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 641744967 1973 CPQPGVTPDPADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:PLN02330 487 VINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLL 535
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
2632-3031 |
7.14e-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: 80.59 E-value: 7.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALI--- 2708
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFvgk 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2709 -----SQSAHLGimnGSLPVILLDDGETRPFDNEPDTpLDARKQGL--TPRH----LAYVIYTSGSTGKPKGVMVEHANM 2777
Cdd:cd05932 87 lddwkAMAPGVP---EGLISISLPPPSAANCQYQWDD-LIAQHPPLeeRPTRfpeqLATLIYTSGTTGQPKGVMLTFGSF 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2778 VNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFL-PLLNGARLILATQAQAADAQqlamlIERHAVSFMQATPSTWRM 2856
Cdd:cd05932 163 AWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGgSLYGGVLVAFAESLDTFVED-----VQRARPTLFFSVPRLWTK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2857 -------------------------LVE---LRDFALPPGFKALCGGEALPENLATALLQKVTTLWNLYGPTETTIWSTL 2908
Cdd:cd05932 238 fqqgvqdkipqqklnlllkipvvnsLVKrkvLKGLGLDQCRLAGCGSAPVPPALLEWYRSLGLNILEAYGMTENFAYSHL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2909 N-GLTTPTPYIGHPIANTQIYILDaqgrvvplgvAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLG 2987
Cdd:cd05932 318 NyPGRDKIGTVGNAGPGVEVRISE----------DGEILVRSPALMMGYYKDPEATAEAFTADGF--------LRTGDKG 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 641744967 2988 RWLPDGTLEYLGRNDFQVKV-RGFRIELGEIETRLArchgVHDAV 3031
Cdd:cd05932 380 ELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLA----EHDRV 420
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
485-963 |
7.31e-15 |
|
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: 80.65 E-value: 7.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 485 QTPEAIAvlFEDQH----LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAE 560
Cdd:cd17642 29 SVPGTIA--FTDAHtgvnYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNER 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 561 RLAYILDDAAPVALLTQSA---QVAQLNSTLPTV----LLDTP---AAAACPD---TNPVVQGLHAAH-----------L 616
Cdd:cd17642 107 ELDHSLNISKPTIVFCSKKglqKVLNVQKKLKIIktiiILDSKedyKGYQCLYtfiTQNLPPGFNEYDfkppsfdrdeqV 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 617 AYVIYTSGSTGRPKGVMVAHRNV---------------INLATGLHTLLALDHP-------------SRIALNASivFDA 668
Cdd:cd17642 187 ALIMNSSGSTGLPKGVQLTHKNIvarfshardpifgnqIIPDTAILTVIPFHHGfgmfttlgylicgFRVVLMYK--FEE 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 669 svKNWIQLLSGH---TLVLVPdalradahQLWRYFARHA-VDLFDCTPVQlqwlldaglgsdpayqpaQVLIGGEAISPA 744
Cdd:cd17642 265 --ELFLRSLQDYkvqSALLVP--------TLFAFFAKSTlVDKYDLSNLH------------------EIASGGAPLSKE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 745 VWSRLQSLSDTRFINV-YGPTECTvdATACVVDRTQPLP-TIGKPLANTRLYILDAqDQPVPIGV--TGELHIGGAGVAR 820
Cdd:cd17642 317 VGEAVAKRFKLPGIRQgYGLTETT--SAILITPEGDDKPgAVGKVVPFFYAKVVDL-DTGKTLGPneRGELCVKGPMIMK 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 821 GYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIA 900
Cdd:cd17642 394 GYVNNPEATKALIDKDGW--------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAG 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 901 REDspgdtrlvaylcarPDAELHPAAL----------RQQLAASLADYMIPS-----AFVTLDALPLTPNGKLDRKAL 963
Cdd:cd17642 466 IPD--------------EDAGELPAAVvvleagktmtEKEVMDYVASQVSTAkrlrgGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
2621-3099 |
7.41e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 80.84 E-value: 7.41e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2621 DAIAVVFGEASLSYDELNRRANRLAHHLISFGvRPDER--VAICVERGLDMVVGLLGILKAGGAYVPLDPTypvERLRYM 2698
Cdd:PRK13388 16 DTIAVRYGDRTWTWREVLAEAAARAAALIALA-DPDRPlhVGVLLGNTPEMLFWLAAAALGGYVLVGLNTT---RRGAAL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2699 LDDAKPV---ALISQSAHLGIMNG----SLPVILLDDGETRPFDNEPDTPLDARKqgLTPRHLAYVIYTSGSTGKPKGVM 2771
Cdd:PRK13388 92 AADIRRAdcqLLVTDAEHRPLLDGldlpGVRVLDVDTPAYAELVAAAGALTPHRE--VDAMDPFMLIFTSGTTGAPKAVR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2772 VEHANMVNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLPLL-NGARLILATQAQAADAQQLamlIERHAVSFMQ-- 2848
Cdd:PRK13388 170 CSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVMAGWAPAVaSGAAVALPAKFSASGFLDD---VRRYGATYFNyv 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2849 --------ATPStwrmLVELRDFALPPGFkalcGGEALPENLATALLQKVTTLWNLYGPTETTIWSTLNGlTTPTPYIGH 2920
Cdd:PRK13388 247 gkplayilATPE----RPDDADNPLRVAF----GNEASPRDIAEFSRRFGCQVEDGYGSSEGAVIVVREP-GTPPGSIGR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2921 PIANTQIY-----------ILDAQGRVV-PLGVAGEI-HIAGAGVVRGYLGRPDLTAERFitdpfsgapeaR--MYKTGD 2985
Cdd:PRK13388 318 GAPGVAIYnpetltecavaRFDAHGALLnADEAIGELvNTAGAGFFEGYYNNPEATAERM-----------RhgMYWSGD 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2986 LGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDS-PGDKRLVAYLLAQPDTvLEPADLRQR 3064
Cdd:PRK13388 387 LAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDErVGDQVMAALVLRDGAT-FDPDAFAAF 465
|
490 500 510
....*....|....*....|....*....|....*..
gi 641744967 3065 LS--EGVAEYMIPSAFVTLDAFPLTPNGKLDRKALPA 3099
Cdd:PRK13388 466 LAaqPDLGTKAWPRYVRIAADLPSTATNKVLKRELIA 502
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
2620-3097 |
9.93e-15 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 79.92 E-value: 9.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:PRK09029 17 PQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAkpvalisQSAHLGIMNGSLPVILLDDGETRPFDNEPDTPLDARKqgltprhLAYVIYTSGSTGKPKGVmVEHANmvN 2779
Cdd:PRK09029 97 PSL-------TLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQR-------LATMTLTSGSTGLPKAA-VHTAQ--A 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2780 FLCSMRkepGI-------AQEDVLLgvtSLS-FDISILEIFLP-LLNGARLILatqaqAADAQQLAMLierHAVSFMQAT 2850
Cdd:PRK09029 160 HLASAE---GVlslmpftAQDSWLL---SLPlFHVSGQGIVWRwLYAGATLVV-----RDKQPLEQAL---AGCTHASLV 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2851 PST-WRMLVELrdfALPPGFKA-LCGGEALPENLATALLQKVTTLWNLYGPTETTiwSTL-----NGLttptPYIGHPIA 2923
Cdd:PRK09029 226 PTQlWRLLDNR---SEPLSLKAvLLGGAAIPVELTEQAEQQGIRCWCGYGLTEMA--STVcakraDGL----AGVGSPLP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2924 NTQIYIldaqgrvvplgVAGEIHIAGAGVVRGYLGRPDLTAerfITDpfsgapEARMYKTGDLGRWLpDGTLEYLGRNDF 3003
Cdd:PRK09029 297 GREVKL-----------VDGEIWLRGASLALGYWRQGQLVP---LVN------DEGWFATRDRGEWQ-NGELTILGRLDN 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3004 QVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLlaQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDA 3083
Cdd:PRK09029 356 LFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADAEFGQRPVAVV--ESDSEAAVVNLAEWLQDKLARFQQPVAYYLLPP 433
|
490
....*....|....
gi 641744967 3084 FPLTPNGKLDRKAL 3097
Cdd:PRK09029 434 ELKNGGIKISRQAL 447
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
2621-3099 |
1.02e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 80.11 E-value: 1.02e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2621 DAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDER-VAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:PRK07867 18 DDRGLYFEDSFTSWREHIRGSAARAAALRARLDPTRPPhVGVLLDNTPEFSLLLGAAALSGIVPVGLNPTRRGAALARDI 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALISQSAHLGIMNGSLPVILLDDGETRPFDNEPDTPLDA--RKQGLTPRHLAYVIYTSGSTGKPKGVMVEHANM 2777
Cdd:PRK07867 98 AHADCQLVLTESAHAELLDGLDPGVRVINVDSPAWADELAAHRDAepPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKV 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2778 VNFLCSMRKEPGIAQEDVLLGVTSLSFDISILEIFLP-LLNGARLILATQAQAADAQQLamlIERH----------AVSF 2846
Cdd:PRK07867 178 ASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVMAGWAVaLAAGASIALRRKFSASGFLPD---VRRYgatyanyvgkPLSY 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2847 MQATPstwrmlvELRDFALPPgFKALCGGEALPENLATALLQKVTTLWNLYGPTETTIwSTLNGLTTPTPYIGHPIANTQ 2926
Cdd:PRK07867 255 VLATP-------ERPDDADNP-LRIVYGNEGAPGDIARFARRFGCVVVDGFGSTEGGV-AITRTPDTPPGALGPLPPGVA 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2927 IY-----------ILDAQGRVVPLGVAGE-IHIAGAGVVRGYLGRPDLTAERFitdpfsgapEARMYKTGDLGRWLPDGT 2994
Cdd:PRK07867 326 IVdpdtgtecppaEDADGRLLNADEAIGElVNTAGPGGFEGYYNDPEADAERM---------RGGVYWSGDLAYRDADGY 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2995 LEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSE--GVAEY 3072
Cdd:PRK07867 397 AYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVGDQVMAALVLAPGAKFDPDAFAEFLAAqpDLGPK 476
|
490 500
....*....|....*....|....*..
gi 641744967 3073 MIPSAFVTLDAFPLTPNGKLDRKALPA 3099
Cdd:PRK07867 477 QWPSYVRVCAELPRTATFKVLKRQLSA 503
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
2163-2449 |
1.05e-14 |
|
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: 79.62 E-value: 1.05e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2163 PLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTaVCWQDLSQPVQVVW--RQAILPIN 2240
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRT-VFPEEDGVPYQLILeeDEATPKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2241 HFEpTSPEDVLAQLQAHTEprtRRIDLSQAPLFRADIaHDPLQNEWLLALSFHHLISDHMTLALIVGEI-----RLLLQH 2315
Cdd:cd19538 82 IKE-VDEEELESEINEAVR---YPFDLSEEPPFRATL-FELGENEHVLLLLLHHIAADGWSLAPLTRDLskayrARCKGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2316 QADALPTPLPYRNFIA------QTLSVPNSAHE---AYFRDKLADVDE----PTAPFGLLNVQGSGGDIheaRLVLDATL 2382
Cdd:cd19538 157 APELAPLPVQYADYALwqqellGDESDPDSLIArqlAYWKKQLAGLPDeielPTDYPRPAESSYEGGTL---TFEIDSEL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 2383 ASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRlaGAEGADRIMGMFINTLPLRI 2449
Cdd:cd19538 234 HQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGR--NDDSLEDLVGFFVNTLVLRT 298
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
2633-3092 |
1.06e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 80.14 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2633 SYDELNRRANRLAHHLISFGVRPDERVAICVERG---LDMVVGLLGilkAGGAYVPLDPTYPVERLRYMLDDAKPVALIS 2709
Cdd:PRK07008 41 TYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGyrhLEAYYGVSG---SGAVCHTINPRLFPEQIAYIVNHAEDRYVLF 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2710 QSAHLGIMNGSLP-------VILLDDGETRPFDNEP----DTPLDARKQG-----LTPRHLAYVIYTSGSTGKPKGVMVE 2773
Cdd:PRK07008 118 DLTFLPLVDALAPqcpnvkgWVAMTDAAHLPAGSTPllcyETLVGAQDGDydwprFDENQASSLCYTSGTTGNPKGALYS 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2774 HANMV--NFLCSMRKEPGIAQEDVLLGVTSLsFDISILEI-FLPLLNGARLILATQAQAADAQQLamLIERHAVSFMQAT 2850
Cdd:PRK07008 198 HRSTVlhAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGLpYSAPLTGAKLVLPGPDLDGKSLYE--LIEAERVTFSAGV 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2851 PSTWRML---VELRDFALPPGFKALCGGEALPENLATALLQ----KVTTLWnlyGPTETTIWSTLNGLTTPTPYI----- 2918
Cdd:PRK07008 275 PTVWLGLlnhMREAGLRFSTLRRTVIGGSACPPAMIRTFEDeygvEVIHAW---GMTEMSPLGTLCKLKWKHSQLpldeq 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2919 -------GHPIANTQIYILDAQGRVVPL-GVA-GEIHIAGAGVVRGYLGRPDltaerfitDPFSgapeARMYKTGDLGRW 2989
Cdd:PRK07008 352 rkllekqGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRGDA--------SPLV----DGWFPTGDVATI 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2990 LPDGTLEYLGRNDFQVKVRGFRIELGEIETrLARCH-GVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEG 3068
Cdd:PRK07008 420 DADGFMQITDRSKDVIKSGGEWISSIDIEN-VAVAHpAVAEAACIACAHPKWDERPLLVVVKRPGAEVTREELLAFYEGK 498
|
490 500
....*....|....*....|....
gi 641744967 3069 VAEYMIPSAFVTLDAFPLTPNGKL 3092
Cdd:PRK07008 499 VAKWWIPDDVVFVDAIPHTATGKL 522
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
497-918 |
1.35e-14 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 80.16 E-value: 1.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 497 QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLT 576
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 577 ----QSAQVAQLNSTLPTVL------------LDTPAAAACPDTNPVVQGLHAAH---------------LAYVIYTSGS 625
Cdd:cd17641 90 edeeQVDKLLEIADRIPSVRyviycdprgmrkYDDPRLISFEDVVALGRALDRRDpglyerevaagkgedVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 626 TGRPKGVMVAHRNVINLATGLhtlLALDHPSRIALNASIVFDAsvknWI--QLLS------------------------- 678
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAY---LAADPLGPGDEYVSVLPLP----WIgeQMYSvgqalvcgfivnfpeepetmmedlr 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 679 --GHTLVLVP-----------DALRADAHQLWRYFARHAVDL--------FDCTPVQLQWLLDAGLGSDPAYQPAQVLIG 737
Cdd:cd17641 243 eiGPTFVLLPprvwegiaadvRARMMDATPFKRFMFELGMKLglraldrgKRGRPVSLWLRLASWLADALLFRPLRDRLG 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 738 ----------GEAISPAVWSRLQSLS-DTRfiNVYGPTECtvdATACVVDRTQPLP--TIGKPLANTRlyildaqdqpVP 804
Cdd:cd17641 323 fsrlrsaatgGAALGPDTFRFFHAIGvPLK--QLYGQTEL---AGAYTVHRDGDVDpdTVGVPFPGTE----------VR 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 805 IGVTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLGR-NDFQIKVRGFRIEAGEI 883
Cdd:cd17641 388 IDEVGEILVRSPGVFVGYYKNPEATAEDFDEDGW--------LHTGDAGYFKENGHLVVIDRaKDVGTTSDGTRFSPQFI 459
|
490 500 510
....*....|....*....|....*....|....*
gi 641744967 884 ESRLLRCPGVQDAVVIARedspGDTRLVAYLCARP 918
Cdd:cd17641 460 ENKLKFSPYIAEAVVLGA----GRPYLTAFICIDY 490
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
487-884 |
1.53e-14 |
|
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: 79.45 E-value: 1.53e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 487 PEAIAVLFEDQ---HLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGaaYVPMdpaypaerla 563
Cdd:cd05908 1 PEGIIFILGDKkekFVSYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGG--MIAV---------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 564 yilddaaPVALLTQSAQVAQLNSTLPTvlLDTPAAAacpdTNPVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVInla 643
Cdd:cd05908 69 -------PVSIGSNEEHKLKLNKVWNT--LKNPYLI----TEEEVLCELADELAFIQFSSGSTGDPKGVMLTHENLV--- 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 644 tglHTLLALDHPSRIALNASIVFDASVKNWIQLLSGHTL--------VLVPDALRADAHQLWRYFA-RHAVDLFDCTPVQ 714
Cdd:cd05908 133 ---HNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLApliagmnqYLMPTRLFIRRPILWLKKAsEHKATIVSSPNFG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 715 LQWLLDAgLGSDPAYQ-----PAQVLIGGEAISPAVWSRLQS------LSDTRFINVYGPTECTVDAT------------ 771
Cdd:cd05908 210 YKYFLKT-LKPEKANDwdlssIRMILNGAEPIDYELCHEFLDhmskygLKRNAILPVYGLAEASVGASlpkaqspfktit 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 772 -----------ACVVDRTQP----LPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAERFIPD 836
Cdd:cd05908 289 lgrrhvthgepEPEVDKKDSecltFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDD 368
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 641744967 837 PFsadpaariYKTGDLArWLPDGNIDYLGRNDFQIKVRGFRIEAGEIE 884
Cdd:cd05908 369 GW--------LKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIE 407
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
490-963 |
3.51e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 78.64 E-value: 3.51e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 490 IAVLFE------DQHLTYRELNRRANQLAHHLIALGVQPDDRVALcverslemmvgllgilkagaaYVPMDP--AY---- 557
Cdd:PRK00174 84 VAIIWEgddpgdSRKITYRELHREVCRFANALKSLGVKKGDRVAI---------------------YMPMIPeaAVamla 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 558 ---------------PAERLAYILDDAAPVALLTQSAQV---------------AQLNSTLPTVL--------------- 592
Cdd:PRK00174 143 carigavhsvvfggfSAEALADRIIDAGAKLVITADEGVrggkpiplkanvdeaLANCPSVEKVIvvrrtggdvdwvegr 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 593 ------LDTPAAAACPdtnPVVqgLHAAHLAYVIYTSGSTGRPKGVMvaHrnvinlATGLHTLLAldhpsriALNASIVF 666
Cdd:PRK00174 223 dlwwheLVAGASDECE---PEP--MDAEDPLFILYTSGSTGKPKGVL--H------TTGGYLVYA-------AMTMKYVF 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 667 D----------ASVkNWIqllSGHT-LVLVPDALRA------------DAHQLWRYFARHAVDLFDCTPVQLQWLLdaGL 723
Cdd:PRK00174 283 DykdgdvywctADV-GWV---TGHSyIVYGPLANGAttlmfegvpnypDPGRFWEVIDKHKVTIFYTAPTAIRALM--KE 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 724 GSDPayqPAQV------LIG--GEAISPAVWsrlqslsdTRFINVYGPTECTVdatacvVD---RTQ-------PLP--T 783
Cdd:PRK00174 357 GDEH---PKKYdlsslrLLGsvGEPINPEAW--------EWYYKVVGGERCPI------VDtwwQTEtggimitPLPgaT 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 784 IGKPLANTR-LY-----ILDAQDQPVPIGVTGELHIGGA--GVARGYLHRPdltaERFIPDPFSADPAarIYKTGDLARW 855
Cdd:PRK00174 420 PLKPGSATRpLPgiqpaVVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDH----ERFVKTYFSTFKG--MYFTGDGARR 493
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 856 LPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIARedsPGDTR---LVAY--LCA--RPDAELHpAALR 928
Cdd:PRK00174 494 DEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGR---PDDIKgqgIYAFvtLKGgeEPSDELR-KELR 569
|
570 580 590 600
....*....|....*....|....*....|....*....|.
gi 641744967 929 QQLA------ASLADYMipsaFVtlDALPLTPNGKLDRKAL 963
Cdd:PRK00174 570 NWVRkeigpiAKPDVIQ----FA--PGLPKTRSGKIMRRIL 604
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
494-900 |
3.94e-14 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 78.62 E-value: 3.94e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 494 FEDQHL------TYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILD 567
Cdd:PLN02387 96 FEKLHLgeyewiTYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLN 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 568 DAAPVALLTQSAQ---VAQLNSTLPTV-----------LLDTPAAAACP-------------DTNPVVQGL-HAAHLAYV 619
Cdd:PLN02387 176 ETEVTTVICDSKQlkkLIDISSQLETVkrviymddegvDSDSSLSGSSNwtvssfseveklgKENPVDPDLpSPNDIAVI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 620 IYTSGSTGRPKGVMVAHRNVINLATGLHTL-------------LALDHPSRIAlnASIVFdASVKNWIQLLSGHTL---- 682
Cdd:PLN02387 256 MYTSGSTGLPKGVMMTHGNIVATVAGVMTVvpklgkndvylayLPLAHILELA--AESVM-AAVGAAIGYGSPLTLtdts 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 683 ------------VLVPDALRADAHQLWRYF--ARHAVD--------LFD------CTPVQLQWL----LDAGLGSDPAYQ 730
Cdd:PLN02387 333 nkikkgtkgdasALKPTLMTAVPAILDRVRdgVRKKVDakgglakkLFDiaykrrLAAIEGSWFgawgLEKLLWDALVFK 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 731 PAQVLIGGeaispavwsRLQSL--------SDT-RFINV---------YGPTECTVDATACVVDRTQpLPTIGKPLANTR 792
Cdd:PLN02387 413 KIRAVLGG---------RIRFMlsggaplsGDTqRFINIclgapigqgYGLTETCAGATFSEWDDTS-VGRVGPPLPCCY 482
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 793 LYILD-------AQDQPVPigvTGELHIGGAGVARGYLHRPDLTAERFIPDpfsaDPAARIYKTGDLARWLPDGNIDYLG 865
Cdd:PLN02387 483 VKLVSweeggylISDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVD----ERGMRWFYTGDIGQFHPDGCLEIID 555
|
490 500 510
....*....|....*....|....*....|....*.
gi 641744967 866 RNDFQIKVR-GFRIEAGEIESRLLRCPGVQDAVVIA 900
Cdd:PLN02387 556 RKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMVHA 591
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1843-2021 |
6.84e-14 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 76.24 E-value: 6.84e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1843 GRPIANTQLYILDtlgqpvplgvaGELHIGGVGVARGYLNRPDltaerfiPDPFInQPGarLYKTGDLARwLPDGSLEYL 1922
Cdd:PRK07824 195 GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPFA-EPG--WFRTDDLGA-LDDGVLTVL 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1923 GRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPADLRQQLGQHLAEYMVPGAF 2002
Cdd:PRK07824 253 GRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDGGPAPTLEALRAHVARTLDRTAAPREL 332
|
170
....*....|....*....
gi 641744967 2003 VTLDAFPLTPNGKLDRKAL 2021
Cdd:PRK07824 333 HVVDELPRRGIGKVDRRAL 351
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
500-963 |
1.08e-13 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 76.74 E-value: 1.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 500 TYRELNRRANQLAHHLI-ALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQS 578
Cdd:cd05928 43 SFRELGSLSRKAANVLSgACGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSD 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 AQVAQLNS------TLPTVLLDTPAA------------AACPDTNPVVQGLHAAHLAYviYTSGSTGRPKgvMVAHRNV- 639
Cdd:cd05928 123 ELAPEVDSvasecpSLKTKLLVSEKSrdgwlnfkellnEASTEHHCVETGSQEPMAIY--FTSGTTGSPK--MAEHSHSs 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 640 --INLATGLHTLLALDhPSRIALNAS----IVFDAS--VKNWIQllsGHTlVLVPDALRADAHQLWRYFARHAVDLFDCT 711
Cdd:cd05928 199 lgLGLKVNGRYWLDLT-ASDIMWNTSdtgwIKSAWSslFEPWIQ---GAC-VFVHHLPRFDPLVILKTLSSYPITTFCGA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 712 PVQLQWLLDAGLGSdpaYQ-PA--QVLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVdatACVVDRTQPLP--TIGK 786
Cdd:cd05928 274 PTVYRMLVQQDLSS---YKfPSlqHCVTGGEPLNPEVLEKWKAQTGLDIYEGYGQTETGL---ICANFKGMKIKpgSMGK 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 787 PLANTRLYILDAQDQPVPIGVTGELHI-----GGAGVARGYLHRPDLTAERFIPDpfsadpaarIYKTGDLARWLPDGNI 861
Cdd:cd05928 348 ASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVDNPEKTAATIRGD---------FYLTGDRGIMDEDGYF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 862 DYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAredSPGDTR---LVAYLCARPDAELH-----PAALRQQLAA 933
Cdd:cd05928 419 WFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVS---SPDPIRgevVKAFVVLAPQFLSHdpeqlTKELQQHVKS 495
|
490 500 510
....*....|....*....|....*....|
gi 641744967 934 SLADYMIPSAFVTLDALPLTPNGKLDRKAL 963
Cdd:cd05928 496 VTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
30-368 |
1.28e-13 |
|
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: 76.14 E-value: 1.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 30 PLAPLQEGILFHYQLQEkgDTYLLNSLLAF--DSQTRLDAFLDVLQQVIARHDILRTAICwQGLHQPVQVVWRQAPLTVN 107
Cdd:cd20483 3 PMSTFQRRLWFLHNFLE--DKTFLNLLLVChiKGKPDVNLLQKALSELVRRHEVLRTAYF-EGDDFGEQQVLDDPSFHLI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 108 TLTTTSSDTVPAQL-RAATDPSNHRLNLSNAPLLSATTAHDPVcGEWLLSLSIHHLISDHITQALIIDEI----RLLLED 182
Cdd:cd20483 80 VIDLSEAADPEAALdQLVRNLRRQELDIEEGEVIRGWLVKLPD-EEFALVLASHHIAWDRGSSKSIFEQFtalyDALRAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 183 RPEALPKPLPYrNFI-------AQILSVPLSEHEQYFRNRLADIDTPTA--PFDLVD---VQGNGEDITEArlSLDSSLA 250
Cdd:cd20483 159 RDLATVPPPPV-QYIdftlwhnALLQSPLVQPLLDFWKEKLEGIPDASKllPFAKAErppVKDYERSTVEA--TLDKELL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 251 DALRRQARHLGISSsvlFHVAWAQVLALTS---GRDDVVFGSVLSGRlqGNLGADRVMGMFINTLPLRVSLR-ERSVHDV 326
Cdd:cd20483 236 ARMKRICAQHAVTP---FMFLLAAFRAFLYrytEDEDLTIGMVDGDR--PHPDFDDLVGFFVNMLPIRCRMDcDMSFDDL 310
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 641744967 327 VQATSHELMMLLAHEQAPLALAQQCSQVPPPL---PLFSTLFNYR 368
Cdd:cd20483 311 LESTKTTCLEAYEHSAVPFDYIVDALDVPRSTshfPIGQIAVNYQ 355
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
1555-1994 |
2.54e-13 |
|
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: 75.93 E-value: 2.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1555 TYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPA-----ERLAYMLDDASPVAL 1629
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLmsqdlAKLKHLFELLKPGLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1630 LTQAN---QRAL---LTGDVPRI----LLDTADFSHLSEDNPHVPGLDAHHL---------AYVIYTSGSTGKPKGVMNS 1690
Cdd:cd05921 107 FAQDAapfARALaaiFPLGTPLVvsrnAVAGRGAISFAELAATPPTAAVDAAfaavgpdtvAKFLFTSGSTGLPKAVINT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1691 HRALCNRLVWMQNTY-RLTPDDRV-LQKTPFSFDVSVWEFFWPLLY-GARLVM--ARPDGHKDAAYLAQLIERTgiTTLH 1765
Cdd:cd05921 187 QRMLCANQAMLEQTYpFFGEEPPVlVDWLPWNHTFGGNHNFNLVLYnGGTLYIddGKPMPGGFEETLRNLREIS--PTVY 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1766 F-VPSMLQQFVQWADADCAC-----DSLRRVICSGEALPAELQQRFFA----------RFNAQlhnlYGPTEAAIDVTFw 1829
Cdd:cd05921 265 FnVPAGWEMLVAALEKDEALrrrffKRLKLMFYAGAGLSQDVWDRLQAlavatvgeriPMMAG----LGATETAPTATF- 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1830 aCQPDDHRSFVpIGRPIANTQLYIldtlgqpVPLGVAGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGD 1909
Cdd:cd05921 340 -THWPTERSGL-IGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF--------YCLGD 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1910 LARWL----PDGSLEYLGR--NDFqvKLR-GFRIELGEIEARLM-QCPGVQEAVVVAREDSPGDTRLV---AYLCPQ--P 1976
Cdd:cd05921 403 AAKLAdpddPAKGLVFDGRvaEDF--KLAsGTWVSVGPLRARAVaACAPLVHDAVVAGEDRAEVGALVfpdLLACRRlvG 480
|
490 500
....*....|....*....|....
gi 641744967 1977 GVTPDPAD------LRQQLGQHLA 1994
Cdd:cd05921 481 LQEASDAEvlrhakVRAAFRDRLA 504
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
2633-3099 |
2.91e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 74.69 E-value: 2.91e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2633 SYDELNRRANRLAHHLIsFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQSA 2712
Cdd:PRK08308 10 SKSDFDLRLQRYEEMEQ-FQEAAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLLYGES 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2713 HLGImngslpvillddGETRPFDNEPDTPLDarkqgltprhlayviYTSGSTGKPKGVM-----VE---HANMVNFLCSM 2784
Cdd:PRK08308 89 DFTK------------LEAVNYLAEEPSLLQ---------------YSSGTTGEPKLIRrswteIDreiEAYNEALNCEQ 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2785 RKEPGIA--------------------QEDVLLGVTSLSFDISIL-EIFLPLLNGARLILatqaqaadaqqlamlierHA 2843
Cdd:PRK08308 142 DETPIVAcpvthsyglicgvlaaltrgSKPVIITNKNPKFALNILrNTPQHILYAVPLML------------------HI 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2844 VSfmqatpstwRMLVELRDFalppgFKALCGGEALPENLATALLQKVTTLWNLYGPTETTIWSTLNGLTTPTPyIGHPIA 2923
Cdd:PRK08308 204 LG---------RLLPGTFQF-----HAVMTSGTPLPEAWFYKLRERTTYMMQQYGCSEAGCVSICPDMKSHLD-LGNPLP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2924 NTQIYILDAQGRvvplgvAGEIhiagagVVRgylgrpdlTAERFItdpfsgapearmyKTGDLGRWLPDGTLEYLGRNDF 3003
Cdd:PRK08308 269 HVSVSAGSDENA------PEEI------VVK--------MGDKEI-------------FTKDLGYKSERGTLHFMGRMDD 315
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3004 QVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAqpDTVLEPADLRQRLSEGVAEYMIPSAFVTLDA 3083
Cdd:PRK08308 316 VINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVIS--HEEIDPVQLREWCIQHLAPYQVPHEIESVTE 393
|
490
....*....|....*.
gi 641744967 3084 FPLTPNGKLDRKALPA 3099
Cdd:PRK08308 394 IPKNANGKVSRKLLEL 409
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
1551-2021 |
5.77e-13 |
|
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: 74.38 E-value: 5.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1551 DQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMlddaspvalL 1630
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHC---------I 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1631 TQANQRALLTGDVPRILLDTadfshlSEDNPHVPGLDAHHLAYVIYTSGSTGKPKGVMNSHralcNRLVWMQ----NTYR 1706
Cdd:cd05939 72 TVSKAKALIFNLLDPLLTQS------STEPPSQDDVNFRDKLFYIYTSGTTGLPKAAVIVH----SRYYRIAagayYAFG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1707 LTPDDRVLQKTPFSFD----VSVWEffwPLLYGARLVMARpdghKDAA--YLAQLIeRTGITTLHFVPSMLQQFVqwADA 1780
Cdd:cd05939 142 MRPEDVVYDCLPLYHSaggiMGVGQ---ALLHGSTVVIRK----KFSAsnFWDDCV-KYNCTIVQYIGEICRYLL--AQP 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1781 DCACDSLRRV-ICSGEALPAELQQRFFARFN-AQLHNLYGPTE-----AAIDVTFWACqpddhrSFVPIG----RPIA-- 1847
Cdd:cd05939 212 PSEEEQKHNVrLAVGNGLRPQIWEQFVRRFGiPQIGEFYGATEgnsslVNIDNHVGAC------GFNSRIlpsvYPIRli 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1848 ----NTQLYILDTLGQPVPL--GVAGELhiggVGVAR---------GYLNRPDlTAERFIPDPFinQPGARLYKTGDLAR 1912
Cdd:cd05939 286 kvdeDTGELIRDSDGLCIPCqpGEPGLL----VGKIIqndplrrfdGYVNEGA-TNKKIARDVF--KKGDSAFLSGDVLV 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1913 WLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVV--VAREDSPGDTRLVAYLCPQPGVtpDPADLRQQLG 1990
Cdd:cd05939 359 MDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVygVEVPGVEGRAGMAAIVDPERKV--DLDRFSAVLA 436
|
490 500 510
....*....|....*....|....*....|.
gi 641744967 1991 QHLAEYMVPGAFVTLDAFPLTPNGKLDRKAL 2021
Cdd:cd05939 437 KSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2196-2492 |
6.58e-13 |
|
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: 73.68 E-value: 6.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2196 ERLDAflsALQQVIDRHDILRTAVcwqdLSQPVQVVWRQ---AILPINHFEPTSPEDVLAQLQA------HteprtRRID 2266
Cdd:cd19535 40 DRLER---AWNKLIARHPMLRAVF----LDDGTQQILPEvpwYGITVHDLRGLSEEEAEAALEElrerlsH-----RVLD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2267 LSQAPLFRADIAHDPlQNEWLLALSFHHLISDHMTLALIVGEIRLLLQHQADALPtPLPY--RNFIAQTLSVPNSAHE-- 2342
Cdd:cd19535 108 VERGPLFDIRLSLLP-EGRTRLHLSIDLLVADALSLQILLRELAALYEDPGEPLP-PLELsfRDYLLAEQALRETAYEra 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2343 -AYFRDKLADVdePTAPfGL-LNVQGSggDIHEARLV-----LDATLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGR 2415
Cdd:cd19535 186 rAYWQERLPTL--PPAP-QLpLAKDPE--EIKEPRFTrrehrLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQ 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2416 DDVVFGSVLLGRLAGAEGADRIMGMFINTLPLRISL-ADRGAAEVVERTSHDLMTLLEHEQAP-----LALAQRCSGVAP 2489
Cdd:cd19535 261 PRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGsEGQSFLERARRLQQQLWEDLDHSSYSgvvvvRRLLRRRGGQPV 340
|
...
gi 641744967 2490 PMP 2492
Cdd:cd19535 341 LAP 343
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
467-965 |
1.00e-12 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 73.89 E-value: 1.00e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 467 ADFPREMLiqQRFEAQAEQTPEAIAVLFED--QHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGIL 544
Cdd:PRK05857 10 PQLPSTVL--DRVFEQARQQPEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 545 KAGAAYVPMDPAYPAERLAYILDDAAPVALLTQ------SAQVAQLNSTLPTVLLDTPAAA---AC------PDTNPvvq 609
Cdd:PRK05857 88 KLGAIAVMADGNLPIAAIERFCQITDPAAALVApgskmaSSAVPEALHSIPVIAVDIAAVTresEHsldaasLAGNA--- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 610 GLHAAHLAYVIYTSGSTGRPKGVMVAHRnvinlatglhTLLALdhPSrialnasiVFDASVKNWIQLLSGHTLVLVPDAL 689
Cdd:PRK05857 165 DQGSEDPLAMIFTSGTTGEPKAVLLANR----------TFFAV--PD--------ILQKEGLNWVTWVVGETTYSPLPAT 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 690 RADAhqLWRyfarhavdLFDCtpvqlqwLLDAGL---GSDPAYQPAQVLIGGEA----ISPAVWSRLQS----------- 751
Cdd:PRK05857 225 HIGG--LWW--------ILTC-------LMHGGLcvtGGENTTSLLEILTTNAVattcLVPTLLSKLVSelksanatvps 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 752 ------------LSDTRFI--------NVYGPTE--CTvdaTACVVDRTQPLPTI-----GKPLANTRLYILDAQ--DQP 802
Cdd:PRK05857 288 lrlvgyggsraiAADVRFIeatgvrtaQVYGLSEtgCT---ALCLPTDDGSIVKIeagavGRPYPGVDVYLAATDgiGPT 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 803 VPIGVT----GELHIGGAGVARGYLHRPDLTAERFIPDPFSadpaariykTGDLARWLPDGNIDYLGRNDFQIKVRGFRI 878
Cdd:PRK05857 365 APGAGPsasfGTLWIKSPANMLGYWNNPERTAEVLIDGWVN---------TGDLLERREDGFFYIKGRSSEMIICGGVNI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 879 EAGEIESRLLRCPGVQDAVVIAREDsPGDTRLVAyLCARPDAELHPAA---LRQQLAA-------SLADymiPSAFVTLD 948
Cdd:PRK05857 436 APDEVDRIAEGVSGVREAACYEIPD-EEFGALVG-LAVVASAELDESAaraLKHTIAArfrresePMAR---PSTIVIVT 510
|
570
....*....|....*..
gi 641744967 949 ALPLTPNGKLDRKALPA 965
Cdd:PRK05857 511 DIPRTQSGKVMRASLAA 527
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1540-2016 |
1.58e-12 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 73.68 E-value: 1.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1540 RTPDTTAVLF--EDQH---LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAI--LKA---------GA 1603
Cdd:PRK03584 96 RRDDRPAIIFrgEDGPrreLSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLATasLGAiwsscspdfGV 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1604 AYVpLD-------------PGYP--------AERLAYM---LDDASPVALLTQANQRALLTGDVPRILLDtaDFSHLSED 1659
Cdd:PRK03584 176 QGV-LDrfgqiepkvliavDGYRyggkafdrRAKVAELraaLPSLEHVVVVPYLGPAAAAAALPGALLWE--DFLAPAEA 252
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1660 NPHVPG-LDAHHLAYVIYTSGSTGKPKGVMNSHR-ALCNRLVWMQNTYRLTPDDRVLQKTPFS-----FDVSVweffwpL 1732
Cdd:PRK03584 253 AELEFEpVPFDHPLWILYSSGTTGLPKCIVHGHGgILLEHLKELGLHCDLGPGDRFFWYTTCGwmmwnWLVSG------L 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1733 LYGARLVMArpDG---HKDAAYLAQLIERTGITTL----HFVPSMLQQFVQWADaDCACDSLRRVICSGEALPAELQQRF 1805
Cdd:PRK03584 327 LVGATLVLY--DGspfYPDPNVLWDLAAEEGVTVFgtsaKYLDACEKAGLVPGE-THDLSALRTIGSTGSPLPPEGFDWV 403
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1806 FARFNAQLH--NLYGPTeaaiDVTfwACqpddhrsFVpIGRPIantqlyildtlgQPVplgVAGELHIGGVGVA------ 1877
Cdd:PRK03584 404 YEHVKADVWlaSISGGT----DIC--SC-------FV-GGNPL------------LPV---YRGEIQCRGLGMAveawde 454
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1878 RGylnRPdLTAER---FIPDPFINQP--------GARLYKT-----------GDLARWLPDGSLEYLGRNDFQVKLRGFR 1935
Cdd:PRK03584 455 DG---RP-VVGEVgelVCTKPFPSMPlgfwndpdGSRYRDAyfdtfpgvwrhGDWIEITEHGGVVIYGRSDATLNRGGVR 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1936 IELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVTPDPA---DLRQQLGQHLAEYMVPGAFVTLDAFPLTP 2012
Cdd:PRK03584 531 IGTAEIYRQVEALPEVLDSLVIGQEWPDGDVRMPLFVVLAEGVTLDDAlraRIRTTIRTNLSPRHVPDKIIAVPDIPRTL 610
|
....
gi 641744967 2013 NGKL 2016
Cdd:PRK03584 611 SGKK 614
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
480-965 |
1.75e-12 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 73.44 E-value: 1.75e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 480 EAQAEQtPEAIAVLFE---DQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPA 556
Cdd:PRK10524 64 AKRPEQ-LALIAVSTEtdeERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVVFGG 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 557 YPAERLAYILDDAAPVALLTQSA----------------QVAQLNSTLPTVLLDTPAAAACP-----------------D 603
Cdd:PRK10524 143 FASHSLAARIDDAKPVLIVSADAgsrggkvvpykplldeAIALAQHKPRHVLLVDRGLAPMArvagrdvdyatlraqhlG 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 604 TNPVVQGLHAAHLAYVIYTSGSTGRPKGVmvaHRNvinlaTGLHTllaldhpsrIALNASI-----------VFDASVKN 672
Cdd:PRK10524 223 ARVPVEWLESNEPSYILYTSGTTGKPKGV---QRD-----TGGYA---------VALATSMdtifggkagetFFCASDIG 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 673 WI---------QLLSGHTLVL---VPdaLRADAHQLWRYFARHAVDLFDCTPVQL--------QWLLDAGLGS------- 725
Cdd:PRK10524 286 WVvghsyivyaPLLAGMATIMyegLP--TRPDAGIWWRIVEKYKVNRMFSAPTAIrvlkkqdpALLRKHDLSSlralfla 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 726 -DPAYQPAQVLIGgEAISPAVwsrlqslsdtrfINVYGPTEC---TVDATACVVDRTQPLPTIGKPLANTRLYILDAQD- 800
Cdd:PRK10524 364 gEPLDEPTASWIS-EALGVPV------------IDNYWQTETgwpILAIARGVEDRPTRLGSPGVPMYGYNVKLLNEVTg 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 801 QPVPIGVTGELHIGGAgVARGYLH---RPDltaERFIPDPFSA-DPAarIYKTGDLARWLPDGNIDYLGRNDFQIKVRGF 876
Cdd:PRK10524 431 EPCGPNEKGVLVIEGP-LPPGCMQtvwGDD---DRFVKTYWSLfGRQ--VYSTFDWGIRDADGYYFILGRTDDVINVAGH 504
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 877 RIEAGEIESRLLRCPGVQDAVVIAREDS-----------PGDTRLVAYLCARPDAElhpAALRQQLAASLADYMIPSAFV 945
Cdd:PRK10524 505 RLGTREIEESISSHPAVAEVAVVGVKDAlkgqvavafvvPKDSDSLADREARLALE---KEIMALVDSQLGAVARPARVW 581
|
570 580
....*....|....*....|
gi 641744967 946 TLDALPLTPNGKLDRKALPA 965
Cdd:PRK10524 582 FVSALPKTRSGKLLRRAIQA 601
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
2632-3096 |
2.12e-12 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 72.85 E-value: 2.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFgVRPDERVAICVERGLDMVVGLLGILKAGGAYVPL-DPTYP--VERLRYMLDDAKPVALI 2708
Cdd:PRK12476 69 LTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVVL 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2709 SQSAHLGIMNGSLpvillddgETRPFDNEP-----DTPLDARKQGLTPRHL-----AYVIYTSGSTGKPKGVMVEHANMV 2778
Cdd:PRK12476 148 TTTAAAEAVEGFL--------RNLPRLRRPrviaiDAIPDSAGESFVPVELdtddvSHLQYTSGSTRPPVGVEITHRAVG 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2779 NFLCSMRKEPGIAQEDVlLGVTSLSF--DISILEIFLPLLNGARLILATqaqaadaqqlamlierhAVSFMQaTPSTW-R 2855
Cdd:PRK12476 220 TNLVQMILSIDLLDRNT-HGVSWLPLyhDMGLSMIGFPAVYGGHSTLMS-----------------PTAFVR-RPQRWiK 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2856 MLVE----LRDFALPPGFK-ALCGGEALPENLATALLQKVTTL--------------------WNL--------YGPTET 2902
Cdd:PRK12476 281 ALSEgsrtGRVVTAAPNFAyEWAAQRGLPAEGDDIDLSNVVLIigsepvsidavttfnkafapYGLprtafkpsYGIAEA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2903 TIW-STLN-----------------GLTTPTPY----------IGHPIANTQIYILDA-QGRVVPLGVAGEIHIAGAGVV 2953
Cdd:PRK12476 361 TLFvATIApdaepsvvyldreqlgaGRAVRVAAdapnavahvsCGQVARSQWAVIVDPdTGAELPDGEVGEIWLHGDNIG 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2954 RGYLGRPDLTAERFITDPFS----------GAPEARMYKTGDLGRWLpDGTLEYLGRNDFQVKVRGfrielgeietrlaR 3023
Cdd:PRK12476 441 RGYWGRPEETERTFGAKLQSrlaegshadgAADDGTWLRTGDLGVYL-DGELYITGRIADLIVIDG-------------R 506
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3024 CHGVHDAVVIAREDSP---------------GDKRLVAYLLAQPDTV-LEPADLRQRLSEGVA-EYMIPSA---FVTLDA 3083
Cdd:PRK12476 507 NHYPQDIEATVAEASPmvrrgyvtaftvpaeDNERLVIVAERAAGTSrADPAPAIDAIRAAVSrRHGLAVAdvrLVPAGA 586
|
570
....*....|...
gi 641744967 3084 FPLTPNGKLDRKA 3096
Cdd:PRK12476 587 IPRTTSGKLARRA 599
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
490-963 |
2.40e-12 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 73.01 E-value: 2.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 490 IAVLFE------DQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLA 563
Cdd:PLN02654 106 IAIYWEgnepgfDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 564 YILDDAAPVALLTQSA-----QVAQLNSTLPTVLLDTP----AAAAC----------------------------PD--T 604
Cdd:PLN02654 186 QRIVDCKPKVVITCNAvkrgpKTINLKDIVDAALDESAkngvSVGICltyenqlamkredtkwqegrdvwwqdvvPNypT 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 605 NPVVQGLHAAHLAYVIYTSGSTGRPKGVMvaHRN---VINLATGLHtlLALD-HPSRI---ALNASIVFDASVKNWIQLL 677
Cdd:PLN02654 266 KCEVEWVDAEDPLFLLYTSGSTGKPKGVL--HTTggyMVYTATTFK--YAFDyKPTDVywcTADCGWITGHSYVTYGPML 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 678 SGHTLVLVPDALR-ADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQV-LIG--GEAISPAVWSrlqsls 753
Cdd:PLN02654 342 NGATVLVFEGAPNyPDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSRKSLrVLGsvGEPINPSAWR------ 415
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 754 dtRFINVYGPTECTVDATACVVDR----TQPLP--------TIGKPLANTRLYILDAQDQPVPIGVTGELHIGGA--GVA 819
Cdd:PLN02654 416 --WFFNVVGDSRCPISDTWWQTETggfmITPLPgawpqkpgSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKSwpGAF 493
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 820 RGYLHrpdlTAERFIPDPFSadPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVI 899
Cdd:PLN02654 494 RTLYG----DHERYETTYFK--PFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVV 567
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 900 AREDSPGDTRLVAYLCARpDAELHPAALRQQLAASLADYMipSAFVTLDA------LPLTPNGKLDRKAL 963
Cdd:PLN02654 568 GIEHEVKGQGIYAFVTLV-EGVPYSEELRKSLILTVRNQI--GAFAAPDKihwapgLPKTRSGKIMRRIL 634
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
3112-3187 |
2.86e-12 |
|
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: 64.49 E-value: 2.86e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 3112 APQGDLEHALAQIWQTLLGV--ERVGRHDHFF-ELGGHSLLAVQLNARIRAEFLTDIPIVAIFQHPQLSALAEVILAAQ 3187
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKL 79
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
2755-3097 |
3.55e-12 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 70.84 E-value: 3.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2755 AYVIYTSGSTGKPKGVMVEHANMV--------------NFLCSMrkePG--IAQEDVLL-----GVTSLSFDISilEIFL 2813
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTasadathdrlggpgQWLLAL---PAhhIAGLQVLVrsviaGSEPVELDVS--AGFD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2814 PllngarlilatqaQAADAQQLAMLIERHAVSF--MQATpstwRMLVELRDFALPPGFKA-LCGGEALPENLATALLQKV 2890
Cdd:PRK07824 113 P-------------TALPRAVAELGGGRRYTSLvpMQLA----KALDDPAATAALAELDAvLVGGGPAPAPVLDAAAAAG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2891 TTLWNLYGPTETTiwstlNGLTtptpYIGHPIANTQIYILDaqgrvvplgvaGEIHIAGAGVVRGYLGRPDltaerfiTD 2970
Cdd:PRK07824 176 INVVRTYGMSETS-----GGCV----YDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2971 PFSgapEARMYKTGDLGRwLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLA 3050
Cdd:PRK07824 229 PFA---EPGWFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVG 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 641744967 3051 QPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK07824 305 DGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
1552-1973 |
3.65e-12 |
|
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: 72.07 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1552 QHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLT 1631
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1632 ----QANQRALLTGDVPRI------------------LLDTADFSHLSE--DNPHvPGL--------DAHHLAYVIYTSG 1679
Cdd:cd17641 90 edeeQVDKLLEIADRIPSVryviycdprgmrkyddprLISFEDVVALGRalDRRD-PGLyerevaagKGEDVAVLCTTSG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1680 STGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTP--------FSFDVSVWE------------------------ 1727
Cdd:cd17641 169 TTGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPlpwigeqmYSVGQALVCgfivnfpeepetmmedlreigptf 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1728 -FFWPLLYGARL--VMARpdgHKDAAYLAQLIERTGI--------TTLHFVPSMLQQFVQWADAD----------CACDS 1786
Cdd:cd17641 249 vLLPPRVWEGIAadVRAR---MMDATPFKRFMFELGMklglraldRGKRGRPVSLWLRLASWLADallfrplrdrLGFSR 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1787 LRRVICSGEALPAELQqRFFARFNAQLHNLYGPTEAAIDVTFwacQPDDHRSFVPIGRPIANTQLYILDTlgqpvplgva 1866
Cdd:cd17641 326 LRSAATGGAALGPDTF-RFFHAIGVPLKQLYGQTELAGAYTV---HRDGDVDPDTVGVPFPGTEVRIDEV---------- 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1867 GELHIGGVGVARGYLNRPDLTAERFIPDPFInqpgarlyKTGDLARWLPDGSLEYLGR-NDFQVKLRGFRIELGEIEARL 1945
Cdd:cd17641 392 GEILVRSPGVFVGYYKNPEATAEDFDEDGWL--------HTGDAGYFKENGHLVVIDRaKDVGTTSDGTRFSPQFIENKL 463
|
490 500
....*....|....*....|....*...
gi 641744967 1946 MQCPGVQEAVVVARedspGDTRLVAYLC 1973
Cdd:cd17641 464 KFSPYIAEAVVLGA----GRPYLTAFIC 487
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
712-964 |
4.58e-12 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 71.18 E-value: 4.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 712 PVQLQWLLDAglgsDPAY--QPAQVLIGGeaiSPAvWSRLQSLSDTRFINV---YGPTEctvdaTA---CVVDRTQPLP- 782
Cdd:PRK07445 215 PTQLQRLLQL----RPQWlaQFRTILLGG---APA-WPSLLEQARQLQLRLaptYGMTE-----TAsqiATLKPDDFLAg 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 783 --TIGKPLANTRLYILDAQdqpvpigvTGELHIGGAGVARGYLhrPDLTAerfipdpfsadpAARIYKTGDLARWLPDGN 860
Cdd:PRK07445 282 nnSSGQVLPHAQITIPANQ--------TGNITIQAQSLALGYY--PQILD------------SQGIFETDDLGYLDAQGY 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 861 IDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAylCARPDA-ELHPAALRQQLAASLADYM 939
Cdd:PRK07445 340 LHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTA--IYVPKDpSISLEELKTAIKDQLSPFK 417
|
250 260
....*....|....*....|....*
gi 641744967 940 IPSAFVTLDALPLTPNGKLDRKALP 964
Cdd:PRK07445 418 QPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
3016-3091 |
5.32e-12 |
|
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: 63.72 E-value: 5.32e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 3016 EIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGK 3091
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
2593-3097 |
6.26e-12 |
|
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: 71.51 E-value: 6.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2593 VDFNATDadipRHALIHelfeaqvactPDAIAVVF-GE-----ASLSYDELNRRANRLAHHLISFGVRPDERVAICVERG 2666
Cdd:TIGR02188 58 VSYNCVD----RHLEAR----------PDKVAIIWeGDepgevRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMI 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2667 LDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQSAHL---------GIMNGSL---------------- 2721
Cdd:TIGR02188 124 PEAAIAMLACARIGAIHSVVFGGFSAEALADRINDAGAKLVITADEGLrggkviplkAIVDEALekcpvsvehvlvvrrt 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2722 --PVILLDDGETRPFDNE--------PDTPLDARkqgltprHLAYVIYTSGSTGKPKGVMveHAN---MVNFLCSMRKEP 2788
Cdd:TIGR02188 204 gnPVVPWVEGRDVWWHDLmakasaycEPEPMDSE-------DPLFILYTSGSTGKPKGVL--HTTggyLLYAAMTMKYVF 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2789 GIAQEDVL-----LG-VTSLSFdisilEIFLPLLNGA-RLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVELr 2861
Cdd:TIGR02188 275 DIKDGDIFwctadVGwITGHSY-----IVYGPLANGAtTVMFEGVPTYPDPGRFWEIIEKHKVTIFYTAPTAIRALMRL- 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2862 dfalppgfkalcgGEALPENLATALLQKVTTL--------WNLY----GPTETTI----WSTLNG--LTTPTPYI----- 2918
Cdd:TIGR02188 349 -------------GDEWVKKHDLSSLRLLGSVgepinpeaWMWYykvvGKERCPIvdtwWQTETGgiMITPLPGAtptkp 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2919 ---GHPIANTQIYILDAQGRVVP-LGVAGEIHIAGA--GVVRGYLGRPdltaERFITDPFSGAPEarMYKTGDLGRWLPD 2992
Cdd:TIGR02188 416 gsaTLPFFGIEPAVVDEEGNPVEgPGEGGYLVIKQPwpGMLRTIYGDH----ERFVDTYFSPFPG--YYFTGDGARRDKD 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2993 GTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLL----AQPDTVLEpADLRQRLSEG 3068
Cdd:TIGR02188 490 GYIWITGRVDDVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTlkdgYEPDDELR-KELRKHVRKE 568
|
570 580
....*....|....*....|....*....
gi 641744967 3069 VAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:TIGR02188 569 IGPIAKPDKIRFVPGLPKTRSGKIMRRLL 597
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1667-2017 |
1.68e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 70.76 E-value: 1.68e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1667 DAHHLAYVIYTSGSTGKPKGVMNSHRA-LCNRlvwMQNTYR--LTPDDRVLQKTPF--SFDVSVwEFFWPLLYGARLVMA 1741
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNlLANR---AQVAARidFSPEDKVFNALPVfhSFGLTG-GLVLPLLSGVKVFLY 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1742 RPDGHkdaaY--LAQLIERTGITTLHFVPSMLQQFVQWADA-DCAcdSLRRVICSGEALPAELQQRFFARFNAQLHNLYG 1818
Cdd:PRK06814 867 PSPLH----YriIPELIYDTNATILFGTDTFLNGYARYAHPyDFR--SLRYVFAGAEKVKEETRQTWMEKFGIRILEGYG 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1819 PTEAAIDVtfwACQPDDHRSFVPIGR--PIANTQLyildtlgQPVPlGV--AGELHIGGVGVARGYLnRPDltaerfipD 1894
Cdd:PRK06814 941 VTETAPVI---ALNTPMHNKAGTVGRllPGIEYRL-------EPVP-GIdeGGRLFVRGPNVMLGYL-RAE--------N 1000
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1895 PFINQPGAR-LYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIE---ARLMqcPGVQEAvVVAREDSPGDTRLVa 1970
Cdd:PRK06814 1001 PGVLEPPADgWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEelaAELW--PDALHA-AVSIPDARKGERII- 1076
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 641744967 1971 YLCPQPGVTPDpADLRQQLGQHLAEYMVPGAFVTLDAFPLTPNGKLD 2017
Cdd:PRK06814 1077 LLTTASDATRA-AFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
2632-2779 |
2.20e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 69.65 E-value: 2.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLD-PT-------YpVERLRYMLDDAK 2703
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPlPMgfggresY-IAQLRGMLASAQ 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2704 PVALISQSAHLGIMN---GSLP---VILLDDGETRPfdnEPDTPLdarkQGLTPRHLAYVIYTSGSTGKPKGVMVEH-AN 2776
Cdd:PRK09192 129 PAAIITPDELLPWVNeatHGNPllhVLSHAWFKALP---EADVAL----PRPTPDDIAYLQYSSGSTRFPRGVIITHrAL 201
|
...
gi 641744967 2777 MVN 2779
Cdd:PRK09192 202 MAN 204
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
1529-2023 |
2.45e-11 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 69.59 E-value: 2.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1529 LIHQLVEDQAARTPDTTAVLF------EDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAG 1602
Cdd:PRK10524 54 LCHNAVDRHLAKRPEQLALIAvstetdEERTYTFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1603 AAYVPLDPGYPAERLAYMLDDASPV------------------ALLTQANQRA-------LLTG-------DVPRILLDT 1650
Cdd:PRK10524 134 AIHSVVFGGFASHSLAARIDDAKPVlivsadagsrggkvvpykPLLDEAIALAqhkprhvLLVDrglapmaRVAGRDVDY 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1651 ADFSHLSEDNpHVP--GLDAHHLAYVIYTSGSTGKPKGVmnsHR-------ALCNRlvwMQNTYRLTPDDrvlqkTPFSF 1721
Cdd:PRK10524 214 ATLRAQHLGA-RVPveWLESNEPSYILYTSGTTGKPKGV---QRdtggyavALATS---MDTIFGGKAGE-----TFFCA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1722 -DVSvweffW----------PLLYGARLVM-----ARPdghkDAAYLAQLIERTGITTLHFVPS---MLQQFvqwaDADC 1782
Cdd:PRK10524 282 sDIG-----WvvghsyivyaPLLAGMATIMyeglpTRP----DAGIWWRIVEKYKVNRMFSAPTairVLKKQ----DPAL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1783 A----CDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEaaidvTFW---ACQP--DD--HRSFVPiGRPIANTQL 1851
Cdd:PRK10524 349 LrkhdLSSLRALFLAGEPLDEPTASWISEALGVPVIDNYWQTE-----TGWpilAIARgvEDrpTRLGSP-GVPMYGYNV 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1852 YILDTL-GQPVPLGVAGELHIGGvGVARGYLN---RPDltaERFIPDPF--INQPgarLYKTGDLARWLPDGSLEYLGRN 1925
Cdd:PRK10524 423 KLLNEVtGEPCGPNEKGVLVIEG-PLPPGCMQtvwGDD---DRFVKTYWslFGRQ---VYSTFDWGIRDADGYYFILGRT 495
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1926 DFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCP-QPGVTPDP-------ADLRQQLGQHLAEYM 1997
Cdd:PRK10524 496 DDVINVAGHRLGTREIEESISSHPAVAEVAVVGVKDALKGQVAVAFVVPkDSDSLADRearlaleKEIMALVDSQLGAVA 575
|
570 580
....*....|....*....|....*.
gi 641744967 1998 VPGAFVTLDAFPLTPNGKLDRKALPA 2023
Cdd:PRK10524 576 RPARVWFVSALPKTRSGKLLRRAIQA 601
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
494-963 |
2.81e-11 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified in Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes an uncharacterized subgroup of FACS.
Pssm-ID: 213283 [Multi-domain] Cd Length: 509 Bit Score: 69.00 E-value: 2.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 494 FEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVA 573
Cdd:cd05915 20 GEVHRTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 574 LLTQSA--QVAQLNSTLPTVLLDTPA------------AAACPDTNPVVQGLHAAHLAyVIYTSGSTGRPKGVMVAHRNV 639
Cdd:cd05915 100 LLFDPNllPLVEAIRGELKTVQHFVVmdekapegylayEEALGEEADPVRVPERAACG-MAYTTGTTGLPKGVVYSHRAL 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 640 INLATGLHTLLALDH-PSRIALNASIVFDASVKNWIQLLSGHTLVLVPDALRADAHQLWRYFARHAVDLFDCTPVQLQWL 718
Cdd:cd05915 179 VLHSLAASLVDGTALsEKDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 719 LDAGLGSDPAYQ-PAQVLIGGEAiSPAVWSRLQSLSDTRFINVYGPTECTVDATACV-VDRTQPLPTIGKPLANTR---- 792
Cdd:cd05915 259 ADYLESTGHRLKtLRRLVVGGSA-APRSLIARFERMGVEVRQGYGLTETSPVVVQNFvKSHLESLSEEEKLTLKAKtglp 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 793 -----LYILDAQDQPVP-IGVTGE-LHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLG 865
Cdd:cd05915 338 iplvrLRVADEEGRPVPkDGKALGeVQLKGPWITGGYYGNEEATRSALTPDGF--------FRTGDIAVWDEEGYVEIKD 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 866 RNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARpDAELHPAALRQQLAASLADY-MIPSAF 944
Cdd:cd05915 410 RLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVVPR-GEKPTPEELNEHLLKAGFAKwQLPDAY 488
|
490
....*....|....*....
gi 641744967 945 VTLDALPLTPNGKLDRKAL 963
Cdd:cd05915 489 VFAEEIPRTSAGKFLKRAL 507
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1544-2020 |
2.94e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 69.25 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1544 TTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDD 1623
Cdd:PRK07768 20 VTGEPDAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPRTDLAVWAED 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1624 ASPVALLTQAnqRALLTGD-----VPriLLDTADFSHLS------EDNPHVPGLDAHHLAYVIYTSGSTGKPKGVMNSHR 1692
Cdd:PRK07768 100 TLRVIGMIGA--KAVVVGEpflaaAP--VLEEKGIRVLTvadllaADPIDPVETGEDDLALMQLTSGSTGSPKAVQITHG 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1693 ALCNRLVWMQNTYRLTPD-DRVLQKTPFSFDVSVWEFFW-PLLYGARLVMARP-DGHKDAAYLAQLIERTGITTL---HF 1766
Cdd:PRK07768 176 NLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLTvPMYFGAELVKVTPmDFLRDPLLWAELISKYRGTMTaapNF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1767 VPSMLQQFVQWADADCACD--SLRRVICSGEALPAELQQRFF---ARFN---AQLHNLYGPTEAAIDVTFWAC------- 1831
Cdd:PRK07768 256 AYALLARRLRRQAKPGAFDlsSLRFALNGAEPIDPADVEDLLdagARFGlrpEAILPAYGMAEATLAVSFSPCgaglvvd 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1832 ----------------QPDDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYlnrpdLTAERFIPdp 1895
Cdd:PRK07768 336 evdadllaalrravpaTKGNTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIP-- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1896 fiNQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVA-RED--SPGDTRLVAYl 1972
Cdd:PRK07768 409 --AQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAvRLDagHSREGFAVAV- 485
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 1973 cpQPGVTPDPADLRQQLGQHLAEY-----MVPGAFVTLDA--FPLTPNGKLDRKA 2020
Cdd:PRK07768 486 --ESNAFEDPAEVRRIRHQVAHEVvaevgVRPRNVVVLGPgsIPKTPSGKLRRAN 538
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
498-962 |
4.14e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 68.48 E-value: 4.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 498 HLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAyVPMDPAyPAER--LA-YILDDAAPVAL 574
Cdd:PRK07768 29 RHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGAS-LTMLHQ-PTPRtdLAvWAEDTLRVIGM 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 575 LTQSAQVA-----QLNSTLP----TVLLDTPAAAACPdTNPVVQGLHAahLAYVIYTSGSTGRPKGVMVAHRNVINLATG 645
Cdd:PRK07768 107 IGAKAVVVgepflAAAPVLEekgiRVLTVADLLAADP-IDPVETGEDD--LALMQLTSGSTGSPKAVQITHGNLYANAEA 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 646 LHTLLALDHPSRIALN---------------------ASIV------FDASVKNWIQLLSGH--TLVLVPD-ALRADAHQ 695
Cdd:PRK07768 184 MFVAAEFDVETDVMVSwlplfhdmgmvgfltvpmyfgAELVkvtpmdFLRDPLLWAELISKYrgTMTAAPNfAYALLARR 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 696 LWRYFARHAVDLfdctpVQLQWlldaglgsdpayqpaqVLIGGEAISPAVWSRLQS------LSDTRFINVYG------- 762
Cdd:PRK07768 264 LRRQAKPGAFDL-----SSLRF----------------ALNGAEPIDPADVEDLLDagarfgLRPEAILPAYGmaeatla 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 763 ---------PTECTVDATACVVDR---------TQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYlh 824
Cdd:PRK07768 323 vsfspcgagLVVDEVDADLLAALRravpatkgnTRRLATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 825 rpdLTAERFIPdpfsADPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDS 904
Cdd:PRK07768 401 ---LTMDGFIP----AQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLD 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 905 PGDTR----LVAYLCARPDAElHPAALRQQLAASLADY--MIPSAFVTLDA--LPLTPNGKLDRKA 962
Cdd:PRK07768 474 AGHSRegfaVAVESNAFEDPA-EVRRIRHQVAHEVVAEvgVRPRNVVVLGPgsIPKTPSGKLRRAN 538
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
2632-3072 |
5.48e-11 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 68.37 E-value: 5.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPV-----ERLRYML------- 2699
Cdd:PRK08180 70 LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYSLvsqdfGKLRHVLelltpgl 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 ---DDAKPVAlisqSAHLGIMNGSLPVIL----LDDGETRPFDNEPDTP----LDARKQGLTPRHLAYVIYTSGSTGKPK 2768
Cdd:PRK08180 150 vfaDDGAAFA----RALAAVVPADVEVVAvrgaVPGRAATPFAALLATPptaaVDAAHAAVGPDTIAKFLFTSGSTGLPK 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2769 GVMVEHANmvnfLCS---MRKE--PGIAQEDVLLgVTSL--------SFDISILeiflpLLNGARLILATQAQAADaqql 2835
Cdd:PRK08180 226 AVINTHRM----LCAnqqMLAQtfPFLAEEPPVL-VDWLpwnhtfggNHNLGIV-----LYNGGTLYIDDGKPTPG---- 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2836 amLIERH---------AVSFMqaTPSTWRMLVEL--RDFALPPGF----KALC-GGEALPENLATAlLQKVT-------- 2891
Cdd:PRK08180 292 --GFDETlrnlreispTVYFN--VPKGWEMLVPAleRDAALRRRFfsrlKLLFyAGAALSQDVWDR-LDRVAeatcgeri 366
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2892 TLWNLYGPTETTIWST-LNGLTTPTPYIGHPIANTQIyildaqgRVVPLGVAGEIHIAGAGVVRGYLGRPDLTAERFITD 2970
Cdd:PRK08180 367 RMMTGLGMTETAPSATfTTGPLSRAGNIGLPAPGCEV-------KLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2971 PFsgapearmYKTGDLGRWL----PDGTLEYLGR--NDFQ------VKVRGFRIELgeietrLARCHG-VHDAVVIA--R 3035
Cdd:PRK08180 440 GY--------YRSGDAVRFVdpadPERGLMFDGRiaEDFKlssgtwVSVGPLRARA------VSAGAPlVQDVVITGhdR 505
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 641744967 3036 ED-------SPGDKRLVAYLLAQPD--TVLEPADLRQRLSEGVAEY 3072
Cdd:PRK08180 506 DEigllvfpNLDACRRLAGLLADASlaEVLAHPAVRAAFRERLARL 551
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1549-1958 |
6.14e-11 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 68.60 E-value: 6.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1549 FEDQHL------TYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLD 1622
Cdd:PLN02387 96 FEKLHLgeyewiTYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLN 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1623 DASPVALLTQANQRALLTG-------------------DVPRILLDTAD-----FSH---LSEDNPHVPGL-DAHHLAYV 1674
Cdd:PLN02387 176 ETEVTTVICDSKQLKKLIDissqletvkrviymddegvDSDSSLSGSSNwtvssFSEvekLGKENPVDPDLpSPNDIAVI 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1675 IYTSGSTGKPKGVMNSHRALCNRLVW-MQNTYRLTPDDRVLQKTPFSfdvSVWEFFWPLL---------YGARLVMARPD 1744
Cdd:PLN02387 256 MYTSGSTGLPKGVMMTHGNIVATVAGvMTVVPKLGKNDVYLAYLPLA---HILELAAESVmaavgaaigYGSPLTLTDTS 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1745 -----GHK-DAAYLaqliertGITTLHFVPSMLQQ-----------------------------------FVQWADADCA 1783
Cdd:PLN02387 333 nkikkGTKgDASAL-------KPTLMTAVPAILDRvrdgvrkkvdakgglakklfdiaykrrlaaiegswFGAWGLEKLL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1784 CDSL-------------RRVICSGEALPAElQQRFFAR-FNAQLHNLYGPTEAAIDVTFwaCQPDDhRSFVPIGRPIANT 1849
Cdd:PLN02387 406 WDALvfkkiravlggriRFMLSGGAPLSGD-TQRFINIcLGAPIGQGYGLTETCAGATF--SEWDD-TSVGRVGPPLPCC 481
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1850 QLYILD-------TLGQPVPlgvAGELHIGGVGVARGYLNRPDLTAERFIPDpfinQPGARLYKTGDLARWLPDGSLEYL 1922
Cdd:PLN02387 482 YVKLVSweeggylISDKPMP---RGEIVIGGPSVTLGYFKNQEKTDEVYKVD----ERGMRWFYTGDIGQFHPDGCLEII 554
|
490 500 510
....*....|....*....|....*....|....*..
gi 641744967 1923 GRNDFQVKLR-GFRIELGEIEARLMQCPGVQEAVVVA 1958
Cdd:PLN02387 555 DRKKDIVKLQhGEYVSLGKVEAALSVSPYVDNIMVHA 591
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
2620-3097 |
6.27e-11 |
|
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: 68.36 E-value: 6.27e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVF-GE-----ASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVE 2693
Cdd:cd05966 67 GDKVAIIWeGDepdqsRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2694 RLRYMLDDAKPVALISQSAhlGIMNGSL------------------PVILLDD-GETRPFDNEPDTPLDARKQGLTPRHL 2754
Cdd:cd05966 147 SLADRINDAQCKLVITADG--GYRGGKViplkeivdealekcpsveKVLVVKRtGGEVPMTEGRDLWWHDLMAKQSPECE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2755 A---------YVIYTSGSTGKPKGVMVEHA-NMVNFLCSMRKEPGIAQEDVL-----LG-VTSLSFdisilEIFLPLLNG 2818
Cdd:cd05966 225 PewmdsedplFILYTSGSTGKPKGVVHTTGgYLLYAATTFKYVFDYHPDDIYwctadIGwITGHSY-----IVYGPLANG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2819 AR-LILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVELrdfalppgfkalcgGEALPENLATALLQKVTT----- 2892
Cdd:cd05966 300 ATtVMFEGTPTYPDPGRYWDIVEKHKVTIFYTAPTAIRALMKF--------------GDEWVKKHDLSSLRVLGSvgepi 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2893 -------LWNLYG----PTETTIWSTLNG--LTTPTPYI--------GHPIANTQIYILDAQGRVVPLGVAGEIHIAGA- 2950
Cdd:cd05966 366 npeawmwYYEVIGkercPIVDTWWQTETGgiMITPLPGAtplkpgsaTRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPw 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2951 -GVVRGYLGRPdltaERFITDPFSgaPEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHD 3029
Cdd:cd05966 446 pGMARTIYGDH----ERYEDTYFS--KFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAE 519
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641744967 3030 AVVIAREDSPGDKRLVAYLL----AQPDTVLEpADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:cd05966 520 AAVVGRPHDIKGEAIYAFVTlkdgEEPSDELR-KELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
2600-3109 |
7.29e-11 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 67.73 E-value: 7.29e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2600 ADIPRHALIHELFEAQVacTPDAIAV--VFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGIL 2677
Cdd:PRK05857 10 PQLPSTVLDRVFEQARQ--QPEAIALrrCDGTSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2678 KAGGAYVPLDPTYPVERLRYMLDDAKPVALISQ------SAHLGIMNGSLPVILLDDG-ETRPFDNEPDTPLDARKQGLT 2750
Cdd:PRK05857 88 KLGAIAVMADGNLPIAAIERFCQITDPAAALVApgskmaSSAVPEALHSIPVIAVDIAaVTRESEHSLDAASLAGNADQG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2751 PRHLAYVIYTSGSTGKPKGVMVehANMVNF-LCSMRKEPGIAQEDVLLGVTSLS----FDISIL-EIFLPLLNGARLIla 2824
Cdd:PRK05857 168 SEDPLAMIFTSGTTGEPKAVLL--ANRTFFaVPDILQKEGLNWVTWVVGETTYSplpaTHIGGLwWILTCLMHGGLCV-- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2825 tqAQAADAQQLAMLIERHAVSFMQATPSTWRMLV-ELR--DFALPP-GFKALCGGEALPENLATALLQKVTTLwNLYGPT 2900
Cdd:PRK05857 244 --TGGENTTSLLEILTTNAVATTCLVPTLLSKLVsELKsaNATVPSlRLVGYGGSRAIAADVRFIEATGVRTA-QVYGLS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2901 ETTIwstlNGLTTPTP----------YIGHPIANTQIYILDAQG------RVVPLGVAGEIHIAGAGVVRGYLGRPDLTA 2964
Cdd:PRK05857 321 ETGC----TALCLPTDdgsivkieagAVGRPYPGVDVYLAATDGigptapGAGPSASFGTLWIKSPANMLGYWNNPERTA 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2965 ERFITDpfsgapearMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIE--------TRLARCHGVHD------- 3029
Cdd:PRK05857 397 EVLIDG---------WVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDriaegvsgVREAACYEIPDeefgalv 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3030 --AVVIARE-DSPGDKRLVAYLLAQpdtvlepadlRQRLSEGVAEymiPSAFVTLDAFPLTPNGKLDRKALPAP---DQS 3103
Cdd:PRK05857 468 glAVVASAElDESAARALKHTIAAR----------FRRESEPMAR---PSTIVIVTDIPRTQSGKVMRASLAAAataDKA 534
|
....*.
gi 641744967 3104 AMATRG 3109
Cdd:PRK05857 535 RVVVRG 540
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
978-1050 |
1.15e-10 |
|
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: 59.87 E-value: 1.15e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 978 APQGGIETALAALWQELLGLD--RVGRHDQFFA-LGGHSLLAVQLLNRMNKA-GMDVALATLFAHPTLCDLAAAVTA 1050
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDpeEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLEE 77
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
613-963 |
1.53e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 67.07 E-value: 1.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 613 AAHLAYVIYTSGSTGRPKGVMVAH-RNVINLATGLHTLLALDHPSRIALNASIvfdasvkNWIQ--------LLSGHTLV 683
Cdd:PTZ00237 253 SSHPLYILYTSGTTGNSKAVVRSNgPHLVGLKYYWRSIIEKDIPTVVFSHSSI-------GWVSfhgflygsLSLGNTFV 325
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 684 LVPDALRADAH---QLWRYFARHAVDLFDCTPVQLQWLLDaglgSDP-------AYQPA---QVLIGGEAISPAVWSRLQ 750
Cdd:PTZ00237 326 MFEGGIIKNKHiedDLWNTIEKHKVTHTLTLPKTIRYLIK----TDPeatiirsKYDLSnlkEIWCGGEVIEESIPEYIE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 751 SLSDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGgagvargyLHRPDLTA 830
Cdd:PTZ00237 402 NKLKIKSSRGYGQTEIGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK--------LPMPPSFA 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 831 ERFIPDP------FSADPAarIYKTGDLArwLPDGNiDYLG---RNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAR 901
Cdd:PTZ00237 474 TTFYKNDekfkqlFSKFPG--YYNSGDLG--FKDEN-GYYTivsRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGI 548
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 902 EDSPGDTRLVAYLCARPDAELHPAALRQ---QLAASLADYMIPSAFVT----LDALPLTPNGKLDRKAL 963
Cdd:PTZ00237 549 YDPDCYNVPIGLLVLKQDQSNQSIDLNKlknEINNIITQDIESLAVLRkiiiVNQLPKTKTGKIPRQII 617
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
3119-3178 |
2.35e-10 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 58.34 E-value: 2.35e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641744967 3119 HALAQIWQTLLGV--ERVGRHDHFFELGGHSLLAVQLNARIRAEFLTDIPIVAIFQHPQLSA 3178
Cdd:pfam00550 1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
495-963 |
2.80e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 65.96 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 495 EDQHLTYRELNRRANQLAHHLI-ALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAP-- 571
Cdd:PRK05620 35 EQEQTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDev 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 572 -VALLTQSAQVAQLNSTLPTV---------LLDTPAAAACPDTN-----------------PVVQGLHAAHLAYviyTSG 624
Cdd:PRK05620 115 iVADPRLAEQLGEILKECPCVravvfigpsDADSAAAHMPEGIKvysyealldgrstvydwPELDETTAAAICY---STG 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 625 STGRPKGVMVAHRNVINLATGLHTL--LALDHPSRIALNASIVfdaSVKNW----IQLLSGHTLVL-------------V 685
Cdd:PRK05620 192 TTGAPKGVVYSHRSLYLQSLSLRTTdsLAVTHGESFLCCVPIY---HVLSWgvplAAFMSGTPLVFpgpdlsaptlakiI 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 686 PDALRADAH-------QLWRYFARHAVDlfdctPVQLQwlldaglgsdpayqpaQVLIGGEAISPAvwsrLQSLSDTRF- 757
Cdd:PRK05620 269 ATAMPRVAHgvptlwiQLMVHYLKNPPE-----RMSLQ----------------EIYVGGSAVPPI----LIKAWEERYg 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 758 ---INVYGPTEctvdatacvvdrTQPLPTIGKPLA----NTRLYILDAQDQpVPIGV-----------------TGELHI 813
Cdd:PRK05620 324 vdvVHVWGMTE------------TSPVGTVARPPSgvsgEARWAYRVSQGR-FPASLeyrivndgqvmestdrnEGEIQV 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 814 GGAGVARGYLHRP----DLTAERF-------IPDPFSADPAARiykTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGE 882
Cdd:PRK05620 391 RGNWVTASYYHSPteegGGAASTFrgedvedANDRFTADGWLR---TGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQ 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 883 IESRLLRCPGVQDAVVIAREDSPGDTRLVAYLCARPDAELHPAA---LRQQLAASLADYMIPSAFVTLDALPLTPNGKLD 959
Cdd:PRK05620 468 LENYIMAAPEVVECAVIGYPDDKWGERPLAVTVLAPGIEPTRETaerLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFD 547
|
....
gi 641744967 960 RKAL 963
Cdd:PRK05620 548 KKDL 551
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2163-2501 |
2.80e-10 |
|
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: 65.36 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2163 PLAPLQEGILFHHLLQEQGDTYLLRSMVAFTHRERLDAFLSALQQVIDRHDILRTAVCwQDLSQPVQVVWRQAILPINHF 2242
Cdd:cd20483 3 PMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYF-EGDDFGEQQVLDDPSFHLIVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2243 EPTSPEDVLAQLQAHTEPRTRR-IDLSQAPLFRADIAHDPlQNEWLLALSFHHLISDHMTLALIVGEI----RLLLQHQA 2317
Cdd:cd20483 82 DLSEAADPEAALDQLVRNLRRQeLDIEEGEVIRGWLVKLP-DEEFALVLASHHIAWDRGSSKSIFEQFtalyDALRAGRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2318 DALPTPLPYrNFIAQTL-------SVPNSAHEAYFRDKLADVDEPTA--PFGLLN---VQGSGGDIHEARlvLDATLASA 2385
Cdd:cd20483 161 LATVPPPPV-QYIDFTLwhnallqSPLVQPLLDFWKEKLEGIPDASKllPFAKAErppVKDYERSTVEAT--LDKELLAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2386 IRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVLLGRlaGAEGADRIMGMFINTLPLRISLADRGAAE-VVERTS 2464
Cdd:cd20483 238 MKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDR--PHPDFDDLVGFFVNMLPIRCRMDCDMSFDdLLESTK 315
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 641744967 2465 HDLMTLLEHEQAPL-ALAQRCSgvAPP----MPLFSTLLNYR 2501
Cdd:cd20483 316 TTCLEAYEHSAVPFdYIVDALD--VPRstshFPIGQIAVNYQ 355
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
30-316 |
2.92e-10 |
|
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: 65.36 E-value: 2.92e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 30 PLAPLQEGILFHYQLQEKGDTYllNSLLAFDSQTRLD--AFLDVLQQVIARHDILRTaiCWQGLH-QPVQVVWRQAPLTV 106
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATY--NIPLVIKLKGKLDvqALQQALYDVVERHESLRT--VFPEEDgVPYQLILEEDEATP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 107 N-TLTTTSSDTVPAQLRAATdpsNHRLNLSNAPLLSATTaHDPVCGEWLLSLSIHHLISDHITQALIIDEIRLLLEDR-- 183
Cdd:cd19538 79 KlEIKEVDEEELESEINEAV---RYPFDLSEEPPFRATL-FELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARck 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 184 ---PEALPKPLPYRNFIA---QIL------SVPLSEHEQYFRNRLA----DIDTPTAPFDLVDVQGNGEDITearLSLDS 247
Cdd:cd19538 155 geaPELAPLPVQYADYALwqqELLgdesdpDSLIARQLAYWKKQLAglpdEIELPTDYPRPAESSYEGGTLT---FEIDS 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 248 SLADALRRQARHLGISSSVLFHVAWAQVLA-LTSGrDDVVFGSVLSGRLQGNLGAdrVMGMFINTLPLRV 316
Cdd:cd19538 232 ELHQQLLQLAKDNNVTLFMVLQAGFAALLTrLGAG-TDIPIGSPVAGRNDDSLED--LVGFFVNTLVLRT 298
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
2632-3024 |
2.93e-10 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 65.70 E-value: 2.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISqs 2711
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQNIPIVTVYATLGEDALIHSLNETECSAIFT-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2712 ahlgimngslpvillddgetrpfDNEPDTpldarkqgltprhLAYVIYTSGSTGKPKGVMVEHANMVNFLCSM--RKEPG 2789
Cdd:cd17639 84 -----------------------DGKPDD-------------LACIMYTSGSTGNPKGVMLTHGNLVAGIAGLgdRVPEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2790 IAQEDVLLGVTSLSfdiSILEI---FLPLLNGARL-----------ILATQAQAADAQQLAMLIE--------RHAVSFM 2847
Cdd:cd17639 128 LGPDDRYLAYLPLA---HIFELaaeNVCLYRGGTIgygsprtltdkSKRGCKGDLTEFKPTLMVGvpaiwdtiRKGVLAK 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2848 QATPSTWRMLV-----ELRDFALPPG----------FK------------ALCGGEALP----ENLATALLQKVTTlwnl 2896
Cdd:cd17639 205 LNPMGGLKRTLfwtayQSKLKALKEGpgtplldelvFKkvraalggrlryMLSGGAPLSadtqEFLNIVLCPVIQG---- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2897 YGPTETTIWSTLNGLTTPTP-YIGHPIANTQIYILDaqgrVVPLGVA-------GEIHIAGAGVVRGYLGRPDLTAERFI 2968
Cdd:cd17639 281 YGLTETCAGGTVQDPGDLETgRVGPPLPCCEIKLVD----WEEGGYStdkppprGEILIRGPNVFKGYYKNPEKTKEAFD 356
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 2969 TDpfsgapeaRMYKTGDLGRWLPDGTLEYLGRNDFQVKVR-GFRIELGEIETRLARC 3024
Cdd:cd17639 357 GD--------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSN 405
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
57-411 |
3.38e-10 |
|
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: 65.42 E-value: 3.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 57 LAFDSQTRLD--AFLDVLQQVIARHDILRTAICWQGlHQPVQVVWRQAPLTVNT--LTTTSSDTVPAQLRA-ATDPsnhr 131
Cdd:cd20484 28 LCFRFSSKLDveKFKQACQFVLEQHPILKSVIEEED-GVPFQKIEPSKPLSFQEedISSLKESEIIAYLREkAKEP---- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 132 LNLSNAPLLSATTAHDPVcGEWLLSLSIHHLISDHITQALIIDEI----RLLLEDR-PEALPKPLPYRNFIA---QILSV 203
Cdd:cd20484 103 FVLENGPLMRVHLFSRSE-QEHFVLITIHHIIFDGSSSLTLIHSLldayQALLQGKqPTLASSPASYYDFVAweqDMLAG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 204 PLSE-HEQYFRNRLA----DIDTPTAPFDLVDVQGNGEdiTEARLsLDSSLADALRRQARHLGISSSVLFHVAWAQVLAL 278
Cdd:cd20484 182 AEGEeHRAYWKQQLSgtlpILELPADRPRSSAPSFEGQ--TYTRR-LPSELSNQIKSFARSQSINLSTVFLGIFKLLLHR 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 279 TSGRDDVVFGSVLSGRLQGNLgaDRVMGMFINTLPLRVS-LRERSVHDVVQATSHELMMLLAHEQAPLALAQQCSQVPPP 357
Cdd:cd20484 259 YTGQEDIIVGMPTMGRPEERF--DSLIGYFINMLPIRSRiLGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLNIPRS 336
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 358 L---PLFSTLFNYRHSQKDASSQ-------------FWEGMRQlsgreRTNYPITLSVDDLGDGFNLTAK 411
Cdd:cd20484 337 QansPVFQVAFFYQNFLQSTSLQqflaeyqdvlsieFVEGIHQ-----EGEYELVLEVYEQEDRFTLNIK 401
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2199-2448 |
5.52e-10 |
|
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: 64.64 E-value: 5.52e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2199 DAFLSALQQVIDRHDILRTAVCWQDlSQPVQVVWRQAILPINHfEPTS---PEDVLAQLQAHT-EPrtrrIDLSQAPLFR 2274
Cdd:cd20484 39 EKFKQACQFVLEQHPILKSVIEEED-GVPFQKIEPSKPLSFQE-EDISslkESEIIAYLREKAkEP----FVLENGPLMR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2275 ADIAHDPLQnEWLLALSFHHLISDHMTLALIVGEI----RLLLQHQADALPTPLP-YRNFIA---QTLSVPNS-AHEAYF 2345
Cdd:cd20484 113 VHLFSRSEQ-EHFVLITIHHIIFDGSSSLTLIHSLldayQALLQGKQPTLASSPAsYYDFVAweqDMLAGAEGeEHRAYW 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2346 RDKLADV--------DEPTApfgllNVQGSGGDIHEARLvlDATLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDD 2417
Cdd:cd20484 192 KQQLSGTlpilelpaDRPRS-----SAPSFEGQTYTRRL--PSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQED 264
|
250 260 270
....*....|....*....|....*....|.
gi 641744967 2418 VVFGSVLLGRlaGAEGADRIMGMFINTLPLR 2448
Cdd:cd20484 265 IIVGMPTMGR--PEERFDSLIGYFINMLPIR 293
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
1764-2022 |
6.29e-10 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 64.63 E-value: 6.29e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1764 LHFVPSMLQQF----VQWadadcacdsLRR----VICSGEALPAELQQrffarfnAQLHNL-----YGPTEAAIDVTfwA 1830
Cdd:PRK07445 211 LSLVPTQLQRLlqlrPQW---------LAQfrtiLLGGAPAWPSLLEQ-------ARQLQLrlaptYGMTETASQIA--T 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1831 CQPDD----HRSfvpIGRPIANTQLYILDtlgqpvplGVAGELHIGGVGVARGYlnrpdltaerfIPDPFINQpgaRLYK 1906
Cdd:PRK07445 273 LKPDDflagNNS---SGQVLPHAQITIPA--------NQTGNITIQAQSLALGY-----------YPQILDSQ---GIFE 327
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1907 TGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAYLCPQPGVtPDPADLR 1986
Cdd:PRK07445 328 TDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAIYVPKDPS-ISLEELK 406
|
250 260 270
....*....|....*....|....*....|....*.
gi 641744967 1987 QQLGQHLAEYMVPGAFVTLDAFPLTPNGKLDRKALP 2022
Cdd:PRK07445 407 TAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQ 442
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
2619-3091 |
7.07e-10 |
|
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: 64.98 E-value: 7.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2619 TPDAIAVVFGE----ASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAY----------- 2683
Cdd:cd05943 82 ADDPAAIYAAEdgerTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAIWsscspdfgvpg 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2684 -----VPLDPT--YPVERLRY----------------MLDDAKPVALIS--QSAHLGIMNGSLPVILLDDGETRPFDNEP 2738
Cdd:cd05943 162 vldrfGQIEPKvlFAVDAYTYngkrhdvrekvaelvkGLPSLLAVVVVPytVAAGQPDLSKIAKALTLEDFLATGAAGEL 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2739 D---TPLDarkqgltprHLAYVIYTSGSTGKPK-------GVMVEHANMVNFLCSMRkePGiaqeDVLLGVTSLS----- 2803
Cdd:cd05943 242 EfepLPFD---------HPLYILYSSGTTGLPKcivhgagGTLLQHLKEHILHCDLR--PG----DRLFYYTTCGwmmwn 306
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2804 FDISileiflPLLNGARLILATQAQAADAQQLAM-LIERHAVSFMQATPstwRMLVELRDFALPPgfkalcggeALPENL 2882
Cdd:cd05943 307 WLVS------GLAVGATIVLYDGSPFYPDTNALWdLADEEGITVFGTSA---KYLDALEKAGLKP---------AETHDL 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2883 ATalLQkvttlwnlygptetTIWSTLNGLTTPT-PYIGHPIAN----------TQIYILDAQG-RVVPLGvAGEIHIAGA 2950
Cdd:cd05943 369 SS--LR--------------TILSTGSPLKPESfDYVYDHIKPdvllasisggTDIISCFVGGnPLLPVY-RGEIQCRGL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2951 GV-VRGYL--GRP--DLTAERFITDP-------FSGAPEARMYKT------------GDLGRWLPDGTLEYLGRNDFQVK 3006
Cdd:cd05943 432 GMaVEAFDeeGKPvwGEKGELVCTKPfpsmpvgFWNDPDGSRYRAayfakypgvwahGDWIEITPRGGVVILGRSDGTLN 511
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3007 VRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPA---DLRQRLSEGVAEYMIPSAFVTLDA 3083
Cdd:cd05943 512 PGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREGVELDDElrkRIRSTIRSALSPRHVPAKIIAVPD 591
|
....*...
gi 641744967 3084 FPLTPNGK 3091
Cdd:cd05943 592 IPRTLSGK 599
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
72-340 |
7.81e-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: 64.05 E-value: 7.81e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 72 LQQVIARHDILRTAIcwqgLHQPVQVVWRQAP---LTVNTLTTTSSDTVPAQLRAATDPSNHR-LNLSNAPLLSATTAHD 147
Cdd:cd19535 46 WNKLIARHPMLRAVF----LDDGTQQILPEVPwygITVHDLRGLSEEEAEAALEELRERLSHRvLDVERGPLFDIRLSLL 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 148 PVcGEWLLSLSIHHLISDHITQALIIDEIRLLLEDRPEALPK-PLPYRNFIAQILSVPLSEHEQ---YFRNRLADIdtPT 223
Cdd:cd19535 122 PE-GRTRLHLSIDLLVADALSLQILLRELAALYEDPGEPLPPlELSFRDYLLAEQALRETAYERaraYWQERLPTL--PP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 224 APfDLvDVQGNGEDITEARLS-----LDSSLADALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQGN 298
Cdd:cd19535 199 AP-QL-PLAKDPEEIKEPRFTrrehrLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPRFLLNLTLFNRLPLH 276
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 641744967 299 LGADRVMGMFINTLPLRVSLRE-RSVHDVVQATSHELMMLLAH 340
Cdd:cd19535 277 PDVNDVVGDFTSLLLLEVDGSEgQSFLERARRLQQQLWEDLDH 319
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
2620-3097 |
9.93e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 64.20 E-value: 9.93e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2620 PDAIAVVFGEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML 2699
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2700 DDAKPVALI-----SQSAH--LGIMNGSLP-VILLDDGETRPFDNEPDTPLDARKQGLTPrHLAYVI-----------YT 2760
Cdd:PRK08162 112 RHGEAKVLIvdtefAEVAReaLALLPGPKPlVIDVDDPEYPGGRFIGALDYEAFLASGDP-DFAWTLpadewdaialnYT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2761 SGSTGKPKGVMVEH-----ANMVNFL-CSMRKEPgiaqedVLLGVtslsfdisileifLPLL--NG-------------- 2818
Cdd:PRK08162 191 SGTTGNPKGVVYHHrgaylNALSNILaWGMPKHP------VYLWT-------------LPMFhcNGwcfpwtvaaragtn 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2819 -------ARLILAtqaqaadaqqlamLIERHAVSFMQATPSTWRMLVELRDfALPPGF----KALCGGEALPEnlatALL 2887
Cdd:PRK08162 252 vclrkvdPKLIFD-------------LIREHGVTHYCGAPIVLSALINAPA-EWRAGIdhpvHAMVAGAAPPA----AVI 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2888 QKVTT----LWNLYGPTET----TI------WSTL-------------------NGLTTPTPYIGHPIAntqiyildAQG 2934
Cdd:PRK08162 314 AKMEEigfdLTHVYGLTETygpaTVcawqpeWDALplderaqlkarqgvryplqEGVTVLDPDTMQPVP--------ADG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2935 RVVplgvaGEIHIAGAGVVRGYLGRPDLTAERFitdpfsgapEARMYKTGDLGRWLPDGtleYLgrndfQVKVR------ 3008
Cdd:PRK08162 386 ETI-----GEIMFRGNIVMKGYLKNPKATEEAF---------AGGWFHTGDLAVLHPDG---YI-----KIKDRskdiii 443
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3009 --GFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVAYLLAQPDTVLEPADLRQRLSEGVAEYMIPSAfVTLDAFPL 3086
Cdd:PRK08162 444 sgGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVELKDGASATEEEIIAHCREHLAGFKVPKA-VVFGELPK 522
|
570
....*....|.
gi 641744967 3087 TPNGKLDRKAL 3097
Cdd:PRK08162 523 TSTGKIQKFVL 533
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
2632-2811 |
1.05e-09 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 64.37 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQS 2711
Cdd:PLN02387 107 ITYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDS 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2712 AHLG---IMNGSLP----VILLDDGETRPFDNEPD------------------TPLDARKQglTPRHLAYVIYTSGSTGK 2766
Cdd:PLN02387 187 KQLKkliDISSQLEtvkrVIYMDDEGVDSDSSLSGssnwtvssfseveklgkeNPVDPDLP--SPNDIAVIMYTSGSTGL 264
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 641744967 2767 PKGVMVEHANMVNFLCSMRKE-PGIAQEDVLLGVTSLSfdiSILEI 2811
Cdd:PLN02387 265 PKGVMMTHGNIVATVAGVMTVvPKLGKNDVYLAYLPLA---HILEL 307
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
986-1041 |
3.11e-09 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 55.26 E-value: 3.11e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 986 ALAALWQELLGLD--RVGRHDQFFALGGHSLLAVQLLNRMNKA-GMDVALATLFAHPTL 1041
Cdd:pfam00550 2 RLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTL 60
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
2629-3032 |
3.32e-09 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 62.37 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2629 EASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALI 2708
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2709 sqsahlgimngslpvillddgetrpFDnepdtpldarkqgltprhLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEP 2788
Cdd:cd05940 81 -------------------------VD------------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2789 GIAQEDVLLGVTSLSFDI-SILEIFLPLLNGARLILATQAQAADAQQLamlIERHAVSFMQATPSTWRMLV------ELR 2861
Cdd:cd05940 118 GALPSDVLYTCLPLYHSTaLIVGWSACLASGATLVIRKKFSASNFWDD---IRKYQATIFQYIGELCRYLLnqppkpTER 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2862 DFALppgfKALCGGEALP---ENLATALlqKVTTLWNLYGPTETTIwSTLN--------GLTTPTPYIGHPIA------N 2924
Cdd:cd05940 195 KHKV----RMIFGNGLRPdiwEEFKERF--GVPRIAEFYAATEGNS-GFINffgkpgaiGRNPSLLRKVAPLAlvkydlE 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2925 TQIYILDAQGRV--VPLGVAGEI--HIAGAGVVRGYLGrPDLTAERFITDPFSGAPeaRMYKTGDLGRWLPDGTLEYLGR 3000
Cdd:cd05940 268 SGEPIRDAEGRCikVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVFKKGD--AWFNTGDLMRLDGEGFWYFVDR 344
|
410 420 430
....*....|....*....|....*....|....
gi 641744967 3001 --NDFQVKvrGFRIELGEIETRLARCHGVHDAVV 3032
Cdd:cd05940 345 lgDTFRWK--GENVSTTEVAAVLGAFPGVEEANV 376
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1562-2018 |
5.40e-09 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 61.71 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1562 RANQLAHHLIDLGvkPDDRIAICVERSLDMVIGLLAILKAGAAyVPLDPG------------YPAERLA-----YMLDDA 1624
Cdd:PRK05851 40 RAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAA-VSILPGpvrgaddgrwadATLTRFAgigvrTVLSHG 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1625 SPVALLtQANQRALLTGDVPRIlldtadfSHLSEDNPhVPGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNT 1704
Cdd:PRK05851 117 SHLERL-RAVDSSVTVHDLATA-------AHTNRSAS-LTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNAR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1705 YRLTPD-DRVLQKTPFSFDVSVWEFFWPLLYGARLVMArPDGHKDAA---YLAQLIE-RTGITTL-HFVPSMLQQFVQWA 1778
Cdd:PRK05851 188 VGLDAAtDVGCSWLPLYHDMGLAFLLTAALAGAPLWLA-PTTAFSASpfrWLSWLSDsRATLTAApNFAYNLIGKYARRV 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1779 DaDCACDSLRRVICSGEALPAELQQRF---FARFN---AQLHNLYGPTEAAIDVTFWAC----QPDD--------HRSFV 1840
Cdd:PRK05851 267 S-DVDLGALRVALNGGEPVDCDGFERFataMAPFGfdaGAAAPSYGLAESTCAVTVPVPgiglRVDEvttddgsgARRHA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1841 PIGRPIANTQLYILDTlGQPVPLGV--AGELHIGGVGVARGYLNRPDLTAERFIPdpfinqpgarlykTGDLArWLPDGS 1918
Cdd:PRK05851 346 VLGNPIPGMEVRISPG-DGAAGVAGreIGEIEIRGASMMSGYLGQAPIDPDDWFP-------------TGDLG-YLVDGG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1919 LEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRlvaylcpqPGVT-------PDPADLRQQLGQ 1991
Cdd:PRK05851 411 LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSAR--------PGLViaaefrgPDEAGARSEVVQ 482
|
490 500 510
....*....|....*....|....*....|.
gi 641744967 1992 HLAEY--MVPG--AFVTLDAFPLTPNGKLDR 2018
Cdd:PRK05851 483 RVASEcgVVPSdvVFVAPGSLPRTSSGKLRR 513
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
2036-2110 |
9.36e-09 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 54.47 E-value: 9.36e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 2036 APQGEVETALAAVWQDLLGL--TRVGRHDHFFA-LGGHSLLIVSLIERLRRA-GLALDVRGVFSTPVLSDMAQAILAHQ 2110
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVADLADYLEEKL 79
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
1672-2017 |
1.18e-08 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 60.88 E-value: 1.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1672 AYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPF--SFDVSVwEFFWPLLYGARLVMARPDGHkda 1749
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEVFLYPSPLH--- 443
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1750 aY--LAQLIERTGITTLHFVPSMLQQFVQWADA-DCAcdSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEAA--- 1823
Cdd:PRK08043 444 -YriVPELVYDRNCTVLFGTSTFLGNYARFANPyDFA--RLRYVVAGAEKLQESTKQLWQDKFGLRILEGYGVTECApvv 520
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1824 -IDVTFwACQPDDhrsfvpIGRPIANTQLYILdtlgqPVPlGVA--GELHIGGVGVARGYL--NRPDL----TAErfipd 1894
Cdd:PRK08043 521 sINVPM-AAKPGT------VGRILPGMDARLL-----SVP-GIEqgGRLQLKGPNIMNGYLrvEKPGVlevpTAE----- 582
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1895 pfiNQPG---ARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGDTRLVAY 1971
Cdd:PRK08043 583 ---NARGemeRGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQHATAIKSDASKGEALVLF 659
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 641744967 1972 lcpqpgvTPDPADLRQQLGQH-----LAEYMVPGAFVTLDAFPLTPNGKLD 2017
Cdd:PRK08043 660 -------TTDSELTREKLQQYarehgVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1663-1977 |
1.23e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 60.60 E-value: 1.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1663 VPGLDAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQNTYRLTPDDRVLQKTP----FSFDVSVwefFWPLLYGARL 1738
Cdd:PRK06334 177 VSDKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLPpfhaYGFNSCT---LFPLLSGVPV 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1739 VMA-RPDGHKDaayLAQLIERTGITTLHFVPSMLQQFVQWADADCAC-DSLRRVICSGEALPAELQQRFFARF-NAQLHN 1815
Cdd:PRK06334 254 VFAyNPLYPKK---IVEMIDEAKVTFLGSTPVFFDYILKTAKKQESClPSLRFVVIGGDAFKDSLYQEALKTFpHIQLRQ 330
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1816 LYGPTEAAIDVTFWACQPDDHRSFVpiGRPIANTQLYIL-DTLGQPVPLGVAGELHIGGVGVARGYLNRpdltaerfipD 1894
Cdd:PRK06334 331 GYGTTECSPVITINTVNSPKHESCV--GMPIRGMDVLIVsEETKVPVSSGETGLVLTRGTSLFSGYLGE----------D 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1895 P---FINQPGARLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAvvvaredsPGDTRLVay 1971
Cdd:PRK06334 399 FgqgFVELGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAA--------DHAGPLV-- 468
|
....*.
gi 641744967 1972 LCPQPG 1977
Cdd:PRK06334 469 VCGLPG 474
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
494-640 |
1.33e-08 |
|
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: 60.38 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 494 FEDQHLTYRELNRRANQLAHHLIA-LGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPV 572
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 573 ALLTQSAQVAQLNSTLPTVLLD-------------------TPAAAACPDTnPVVQGLHAA----HLAYVIYTSGSTGRP 629
Cdd:cd05938 81 VLVVAPELQEAVEEVLPALRADgvsvwylshtsntegvislLDKVDAASDE-PVPASLRAHvtikSPALYIYTSGTTGLP 159
|
170
....*....|.
gi 641744967 630 KGVMVAHRNVI 640
Cdd:cd05938 160 KAARISHLRVL 170
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
2748-3099 |
1.87e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 60.21 E-value: 1.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2748 GLTPRHLAYVIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIAQEDVLLGVT----SLSFDISILeifLPLLNGARLIL 2823
Cdd:PRK06334 179 DKDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLppfhAYGFNSCTL---FPLLSGVPVVF 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2824 ATQAQAADAQQLamLIERHAVSFMQATPSTWRMLVEL---RDFALPPGFKALCGGEALPENL--ATALLQKVTTLWNLYG 2898
Cdd:PRK06334 256 AYNPLYPKKIVE--MIDEAKVTFLGSTPVFFDYILKTakkQESCLPSLRFVVIGGDAFKDSLyqEALKTFPHIQLRQGYG 333
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2899 PTETTIWSTLNGLTTP--TPYIGHPIANTQIYILDAQGRV-VPLGVAGEIHIAGAGVVRGYLGrpdltaerfiTDPFSGA 2975
Cdd:PRK06334 334 TTECSPVITINTVNSPkhESCVGMPIRGMDVLIVSEETKVpVSSGETGLVLTRGTSLFSGYLG----------EDFGQGF 403
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2976 PE---ARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDA------VVIAredSPGDKRLVA 3046
Cdd:PRK06334 404 VElggETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFGQNAAdhagplVVCG---LPGEKVRLC 480
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 641744967 3047 YLLAQPDTVLEPADLRQRLSegVAEYMIPSAFVTLDAFPLTPNGKLDRKALPA 3099
Cdd:PRK06334 481 LFTTFPTSISEVNDILKNSK--TSSILKISYHHQVESIPMLGTGKPDYCSLNA 531
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
1532-2024 |
1.89e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 60.50 E-value: 1.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1532 QLVEDQAARTPDTTAVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPG 1611
Cdd:PRK07868 451 RIIAEQARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPPD 530
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1612 ---YPAERLA---YMLDDASPVALLTQANQRALLTG-------DVPrillDTADFSHLSEDNPHV----------PGLdA 1668
Cdd:PRK07868 531 tdlAAAVRLGgvtEIITDPTNLEAARQLPGRVLVLGggesrdlDLP----DDADVIDMEKIDPDAvelpgwyrpnPGL-A 605
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1669 HHLAYVIY-TSGSTGKPKGVMNSHRALcnRLVWMQNTYRLTPDDRVLQKTPFSFDVSvweffwpLLY--------GARLV 1739
Cdd:PRK07868 606 RDLAFIAFsTAGGELVAKQITNYRWAL--SAFGTASAAALDRRDTVYCLTPLHHESG-------LLVslggavvgGSRIA 676
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1740 MARpdgHKDAAYLAQLIERTGITTLHFVPSMLQQFVQwaDADCACD---SLRRVICSGeaLPAELQQRFFARFN-AQLHN 1815
Cdd:PRK07868 677 LSR---GLDPDRFVQEVRQYGVTVVSYTWAMLREVVD--DPAFVLHgnhPVRLFIGSG--MPTGLWERVVEAFApAHVVE 749
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1816 LYGPTEA-AIDVTFWACQPDDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGGVGVARGYLNRP-DLTAErFIP 1893
Cdd:PRK07868 750 FFATTDGqAVLANVSGAKIGSKGRPLPGAGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLARARGPiDPTAS-VKR 828
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1894 DPFinQPGARLYKTGDLARWLPDGSLEYLGRNDFQVK-LRGFrIELGEIEARLMQCPGVQEAVVVArEDSPGDTRLVAYL 1972
Cdd:PRK07868 829 GVF--APADTWISTEYLFRRDDDGDYWLVDRRGSVIRtARGP-VYTEPVTDALGRIGGVDLAVTYG-VEVGGRQLAVAAV 904
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 1973 CPQPGVTPDPADLRQQLGQhLAEYMVPGAFVTLDAFPLT----PN-GKLDRKALPAP 2024
Cdd:PRK07868 905 TLRPGAAITAADLTEALAS-LPVGLGPDIVHVVPEIPLSatyrPTvSALRAAGIPKP 960
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
2632-3043 |
1.99e-08 |
|
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: 60.06 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALI--- 2708
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETSEANILVven 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2709 -SQSAHLGIMNGSLP----VILLDD--GETRP-------F----DNEPDTPLDARKQGLTPRHLAYVIYTSGSTGKPKGV 2770
Cdd:cd05933 89 qKQLQKILQIQDKLPhlkaIIQYKEplKEKEPnlyswdeFmelgRSIPDEQLDAIISSQKPNQCCTLIYTSGTTGMPKGV 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2771 MVEHANMV----NFLCSMRKEPGIAQEDVLLGVTSLSF-DISILEIFLPLLNGARLILATQAQAADAQQLAM-------- 2837
Cdd:cd05933 169 MLSHDNITwtakAASQHMDLRPATVGQESVVSYLPLSHiAAQILDIWLPIKVGGQVYFAQPDALKGTLVKTLrevrptaf 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2838 ---------LIERHAVSFMQATPSTWRMLVELRDFAL------------PPGFKAL-----------------C-----G 2874
Cdd:cd05933 249 mgvprvwekIQEKMKAVGAKSGTLKRKIASWAKGVGLetnlklmggespSPLFYRLakklvfkkvrkalgldrCqkfftG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2875 GEALPENLATALLQKVTTLWNLYGPTETTIWSTLNGLTTPTPY-IGHPIANTQIYIL--DAQGrvvplgvAGEIHIAGAG 2951
Cdd:cd05933 329 AAPISRETLEFFLSLNIPIMELYGMSETSGPHTISNPQAYRLLsCGKALPGCKTKIHnpDADG-------IGEICFWGRH 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2952 VVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDFQVKVRGfrielGE------IETRL-ARC 3024
Cdd:cd05933 402 VFMGYLNMEDKTEEAIDEDGW--------LHSGDLGKLDEDGFLYITGRIKELIITAG-----GEnvppvpIEDAVkKEL 468
|
490
....*....|....*....
gi 641744967 3025 HGVHDAVVIaredspGDKR 3043
Cdd:cd05933 469 PIISNAMLI------GDKR 481
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
30-316 |
2.22e-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: 59.36 E-value: 2.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 30 PLAPLQEGILFHYQLQEKGDTYllNSLLAFdsqtRLDAFLDV------LQQVIARHDILRTaICWQGLHQPVQVV----W 99
Cdd:cd19540 3 PLSFAQQRLWFLNRLDGPSAAY--NIPLAL----RLTGALDVdalraaLADVVARHESLRT-VFPEDDGGPYQVVlpaaE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 100 RQAPLTVntlTTTSSDTVPAQLRAATDpsnHRLNLSNAPLLSAT---TAHDpvcgEWLLSLSIHHLISDHitqaliiDEI 176
Cdd:cd19540 76 ARPDLTV---VDVTEDELAARLAEAAR---RGFDLTAELPLRARlfrLGPD----EHVLVLVVHHIAADG-------WSM 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 177 RLLLED------------RPEALPKPLPYRNFIA---QIL------SVPLSEHEQYFRNRLADIDTPTA-PFDLV--DVQ 232
Cdd:cd19540 139 APLARDlatayaarragrAPDWAPLPVQYADYALwqrELLgdeddpDSLAARQLAYWRETLAGLPEELElPTDRPrpAVA 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 233 GNGEDITEarLSLDSSLADALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSGRLQGNLgaDRVMGMFINTL 312
Cdd:cd19540 219 SYRGGTVE--FTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEAL--DDLVGMFVNTL 294
|
....
gi 641744967 313 PLRV 316
Cdd:cd19540 295 VLRT 298
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1554-2021 |
2.69e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 59.76 E-value: 2.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDASPVALLTQ- 1632
Cdd:PTZ00237 93 LTYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLFDGYSVKSLIDRIETITPKLIITTn 172
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1633 --------------------------------------ANQRALLTGDVPRI--LLDTAD-FSHLSEDN-----PHVPgL 1666
Cdd:PTZ00237 173 ygilndeiitftpnlkeaielstfkpsnvitlfrnditSESDLKKIETIPTIpnTLSWYDeIKKIKENNqspfyEYVP-V 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1667 DAHHLAYVIYTSGSTGKPKGVM--NSHRALCNRLVWmqnTYRLTPDD--RVLQKTPFSFdVSVWEFFWPLL-YGARLVMA 1741
Cdd:PTZ00237 252 ESSHPLYILYTSGTTGNSKAVVrsNGPHLVGLKYYW---RSIIEKDIptVVFSHSSIGW-VSFHGFLYGSLsLGNTFVMF 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1742 RPDGHKDAAY---LAQLIERTGITTLHFVPSMLQQFVQwADADCA-------CDSLRRVICSGEALPAELQQRFFARFNA 1811
Cdd:PTZ00237 328 EGGIIKNKHIeddLWNTIEKHKVTHTLTLPKTIRYLIK-TDPEATiirskydLSNLKEIWCGGEVIEESIPEYIENKLKI 406
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1812 QLHNLYGPTEaaIDVTFWACQPDDHRSFVPIGRPIANTQLYILDTLGQPVPLGVAGELHIGgvgvargyLNRPDLTAERF 1891
Cdd:PTZ00237 407 KSSRGYGQTE--IGITYLYCYGHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFK--------LPMPPSFATTF 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1892 IPDP------FINQPGarLYKTGDLARWLPDGSLEYLGRNDFQVKLRGFRIELGEIEARLMQCPGVQEAVVVAREDSPGD 1965
Cdd:PTZ00237 477 YKNDekfkqlFSKFPG--YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCY 554
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 1966 TRLVAYLC---PQPGVTPDPADLRQQLGQHLAEYMVPGAFVT----LDAFPLTPNGKLDRKAL 2021
Cdd:PTZ00237 555 NVPIGLLVlkqDQSNQSIDLNKLKNEINNIITQDIESLAVLRkiiiVNQLPKTKTGKIPRQII 617
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
2919-3098 |
2.87e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 59.24 E-value: 2.87e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2919 GHPIANTQIYILDAQgrvvplgvAGEIHIAGAGVVRGYLgrPDLTAERfitdpfsgapeaRMYKTGDLGRWLPDGTLEYL 2998
Cdd:PRK07445 286 GQVLPHAQITIPANQ--------TGNITIQAQSLALGYY--PQILDSQ------------GIFETDDLGYLDAQGYLHIL 343
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2999 GRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKRLVA-YLLAQPDTVLEpaDLRQRLSEGVAEYMIPSA 3077
Cdd:PRK07445 344 GRNSQKIITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEVVTAiYVPKDPSISLE--ELKTAIKDQLSPFKQPKH 421
|
170 180
....*....|....*....|.
gi 641744967 3078 FVTLDAFPLTPNGKLDRKALP 3098
Cdd:PRK07445 422 WIPVPQLPRNPQGKINRQQLQ 442
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
503-960 |
3.13e-08 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 59.39 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 503 ELNRRANQLAHHLIALGvqPDDRVALCVERSLEMMVGLLGILKAGAAYV----PMDPAYPAERLAYILDDAAPVA---LL 575
Cdd:PRK05851 36 EVHGRAENVAARLLDRD--RPGAVGLVGEPTVELVAAIQGAWLAGAAVSilpgPVRGADDGRWADATLTRFAGIGvrtVL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 576 TQSAQVAQLNSTLPTVLLDTPAAAACPDTNPVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHP 655
Cdd:PRK05851 114 SHGSHLERLRAVDSSVTVHDLATAAHTNRSASLTPPDSGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 656 SRIA--------------------------LNASIVFDASVKNWIQLL--SGHTLVLVPD---------ALRADAHQLWR 698
Cdd:PRK05851 194 TDVGcswlplyhdmglaflltaalagaplwLAPTTAFSASPFRWLSWLsdSRATLTAAPNfaynligkyARRVSDVDLGA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 699 Y-FARHAVDLFDCTPVQLQWLLDAGLGSDPAyqpaqvliggeAISPAvwsrlqslsdtrfinvYGPTE--CTVDATAC-- 773
Cdd:PRK05851 274 LrVALNGGEPVDCDGFERFATAMAPFGFDAG-----------AAAPS----------------YGLAEstCAVTVPVPgi 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 774 --VVDR--------TQPLPTIGKPLANTRLYIlDAQDQPVPIGV--TGELHIGGAGVARGYLHRPDLTAERFIPdpfsad 841
Cdd:PRK05851 327 glRVDEvttddgsgARRHAVLGNPIPGMEVRI-SPGDGAAGVAGreIGEIEIRGASMMSGYLGQAPIDPDDWFP------ 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 842 paariykTGDLArWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTR---LVAYLCARP 918
Cdd:PRK05851 400 -------TGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARpglVIAAEFRGP 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 641744967 919 DAELHPAALRQQLAASLAdyMIPS--AFVTLDALPLTPNGKLDR 960
Cdd:PRK05851 472 DEAGARSEVVQRVASECG--VVPSdvVFVAPGSLPRTSSGKLRR 513
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
2192-2449 |
3.55e-08 |
|
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: 58.74 E-value: 3.55e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2192 FTHRERLDAFLSALQQVIDRHDILRT-------AVCWQDLSQPVQVVWRQAIlpinhfeptspeDVLAQLQahteprtRR 2264
Cdd:cd19537 32 LSGDVDRDRLASAWNTVLARHRILRSryvprdgGLRRSYSSSPPRVQRVDTL------------DVWKEIN-------RP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2265 IDLSQAPLFRADIAHDplqnewLLALSFHHLISDHMTLALIVGEIRLLLQHqadaLPTPLPYRNFIAQTL--SVPNSAHE 2342
Cdd:cd19537 93 FDLEREDPIRVFISPD------TLLVVMSHIICDLTTLQLLLREVSAAYNG----KLLPPVRREYLDSTAwsRPASPEDL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2343 AYFRDKLADVDEPTAPfGLLNVQGSGGDIHEARLvlDATLASAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGS 2422
Cdd:cd19537 163 DFWSEYLSGLPLLNLP-RRTSSKSYRGTSRVFQL--PGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGA 239
|
250 260
....*....|....*....|....*..
gi 641744967 2423 VLLGRlaGAEGADRIMGMFINTLPLRI 2449
Cdd:cd19537 240 PYLNR--TSEEDMETVGLFLEPLPIRI 264
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
430-649 |
3.67e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 59.22 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 430 ENLVTSLEKT----PQQPALSQPILPKSERQQVlvdfnaTDAD-FPREMliqqrfeaqaeqtpeAIAVLFEDQHLTYREL 504
Cdd:PTZ00216 69 PNFLQRLERIckerGDRRALAYRPVERVEKEVV------KDADgKERTM---------------EVTHFNETRYITYAEL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 505 NRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQSAQVAQL 584
Cdd:PTZ00216 128 WERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECKAIVCNGKNVPNL 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 585 ----------------NSTLPT---------------VLLDTPAAAACPDTNPvvqgLHAAHLAYVIYTSGSTGRPKGVM 633
Cdd:PTZ00216 208 lrlmksggmpnttiiyLDSLPAsvdtegcrlvawtdvVAKGHSAGSHHPLNIP----ENNDDLALIMYTSGTTGDPKGVM 283
|
250
....*....|....*.
gi 641744967 634 VAHRnviNLATGLHTL 649
Cdd:PTZ00216 284 HTHG---SLTAGILAL 296
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
2624-3096 |
3.86e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 59.24 E-value: 3.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2624 AVVFGEAS----LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPL-DPTYPVERLRYM 2698
Cdd:PRK07768 18 GMVTGEPDapvrHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLhQPTPRTDLAVWA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2699 LDDAKPVALISQSAhlgimngslpVILLDdgetrPFD----------------NEPDTPLDARKQGLTPRHLAYVIYTSG 2762
Cdd:PRK07768 98 EDTLRVIGMIGAKA----------VVVGE-----PFLaaapvleekgirvltvADLLAADPIDPVETGEDDLALMQLTSG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2763 STGKPKGVMVEHANMVNFLCSMRKEPGIAQE-DVLLGVTSLSFDISILEIF-LPLLNGARLILATQAQAADAQQLAM-LI 2839
Cdd:PRK07768 163 STGSPKAVQITHGNLYANAEAMFVAAEFDVEtDVMVSWLPLFHDMGMVGFLtVPMYFGAELVKVTPMDFLRDPLLWAeLI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2840 ERHAVSFMQATPSTWRMLVE-LRDFALPPGFK------ALCGGE----ALPENLATALLQ---KVTTLWNLYGPTETTIW 2905
Cdd:PRK07768 243 SKYRGTMTAAPNFAYALLARrLRRQAKPGAFDlsslrfALNGAEpidpADVEDLLDAGARfglRPEAILPAYGMAEATLA 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2906 STL----NGLTTPTP-----------------------YIGHPIANTQIYILDAQGRVVPLGVAGEIHIAGAGVVRGYLg 2958
Cdd:PRK07768 323 VSFspcgAGLVVDEVdadllaalrravpatkgntrrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL- 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2959 rpdltaerfITDPFSGAPEAR-MYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIARED 3037
Cdd:PRK07768 402 ---------TMDGFIPAQDADgWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRL 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 3038 SPGDKRLVAYLLAQPDTVLEPADLRqRLSEGVAEY------MIPSAFVTLDA--FPLTPNGKLDRKA 3096
Cdd:PRK07768 473 DAGHSREGFAVAVESNAFEDPAEVR-RIRHQVAHEvvaevgVRPRNVVVLGPgsIPKTPSGKLRRAN 538
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
617-959 |
4.43e-08 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 59.21 E-value: 4.43e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 617 AYVIYTSGSTGRPKGVMVAHRNVinLATGLHTLLALD-HPSRIALNASIVFDA---SVKNWIQLLSGHTLVLVPDALR-- 690
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNL--LANRAQVAARIDfSPEDKVFNALPVFHSfglTGGLVLPLLSGVKVFLYPSPLHyr 873
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 691 --------ADAHQLWRY------FAR--HAVDLfdctpvqlqwlldaglgsdpaYQPAQVLIGGEAISPA---VWSRLQS 751
Cdd:PRK06814 874 iipeliydTNATILFGTdtflngYARyaHPYDF---------------------RSLRYVFAGAEKVKEEtrqTWMEKFG 932
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 752 LsdtRFINVYGPTEctvdaTACVVDRTQPL----PTIGK--PLANTRLyildaqdQPVP-IGVTGELHIGGAGVARGYLH 824
Cdd:PRK06814 933 I---RILEGYGVTE-----TAPVIALNTPMhnkaGTVGRllPGIEYRL-------EPVPgIDEGGRLFVRGPNVMLGYLR 997
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 825 rpdltAERfipdPFSADPAARI-YKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIE---SRLLrcPGVQDAVViA 900
Cdd:PRK06814 998 -----AEN----PGVLEPPADGwYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEelaAELW--PDALHAAV-S 1065
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 641744967 901 REDSPGDTRLVaYLCARPDAElHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLD 959
Cdd:PRK06814 1066 IPDARKGERII-LLTTASDAT-RAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2190-2463 |
8.01e-08 |
|
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: 57.65 E-value: 8.01e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2190 VAFTHRERLD--AFLSALQQVIDRHDILRtAVCWQDlsqpvQVVWRQAILPINHFEPT------SPEDVLAQLQAHTEPR 2261
Cdd:cd19534 26 VLLRVPQGLDpdALRQALRALVEHHDALR-MRFRRE-----DGGWQQRIRGDVEELFRlevvdlSSLAQAAAIEALAAEA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2262 TRRIDLSQAPLFRADIAHDPlQNEWLLALSFHHLISDHMTLALIVGEIRLLLQHQADALPTPLP----YRNFI---AQTL 2334
Cdd:cd19534 100 QSSLDLEEGPLLAAALFDGT-DGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPIPLPsktsFQTWAellAEYA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2335 SVPNSAHEAYFRDKLadvdEPTAPFGL-LNVQGSGGDIHEARLVLDATLASAIRQQA-RHLGVSPGVLFHVAWAQVLAQT 2412
Cdd:cd19534 179 QSPALLEELAYWREL----PAADYWGLpKDPEQTYGDARTVSFTLDEEETEALLQEAnAAYRTEINDLLLAALALAFQDW 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 641744967 2413 SGRDDVVfgsVLL---GRLAGAEGAD--RIMGMFINTLPLRISLADRGA-AEVVERT 2463
Cdd:cd19534 255 TGRAPPA---IFLeghGREEIDPGLDlsRTVGWFTSMYPVVLDLEASEDlGDTLKRV 308
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
30-330 |
9.86e-08 |
|
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: 57.20 E-value: 9.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 30 PLAPLQEGILFHYQLQEKGDTYLLNSLLAFDSQTRLDAFLDVLQQVIARHDILRTAICwQGLHQPVQVVWRQAPlTVNTL 109
Cdd:cd19537 3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYV-PRDGGLRRSYSSSPP-RVQRV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 110 TTTSsdtvpaqLRAAtdpSNHRLNLSNAPLLSATTAHDpvcgewLLSLSIHHLISDHITQALIIDEI------RLLLEDR 183
Cdd:cd19537 81 DTLD-------VWKE---INRPFDLEREDPIRVFISPD------TLLVVMSHIICDLTTLQLLLREVsaayngKLLPPVR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 184 PEALPKPLPYRnfiaqilsVPLSEHEQYFRNRLADIDTPTAPFDLVDVQGNGEDITearLSLDSSLADALRRQARHLGIS 263
Cdd:cd19537 145 REYLDSTAWSR--------PASPEDLDFWSEYLSGLPLLNLPRRTSSKSYRGTSRV---FQLPGSLYRSLLQFSTSSGIT 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 641744967 264 ssvLFHVAWAQV-LAL--TSGRDDVVFGSVLSGRlqGNLGADRVMGMFINTLPLRVSL---RERSVHDVVQAT 330
Cdd:cd19537 214 ---LHQLALAAVaLALqdLSDRTDIVLGAPYLNR--TSEEDMETVGLFLEPLPIRIRFpssSDASAADFLRAV 281
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
619-882 |
1.30e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 57.72 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 619 VIYTSGSTGRPKGVMVAHRNVINLATGLHTLLALDHPSRIALNASI-------VFD-----------ASVKNW---IQLL 677
Cdd:PLN02614 228 IMYTSGTTGDPKGVMISNESIVTLIAGVIRLLKSANAALTVKDVYLsylplahIFDrvieecfiqhgAAIGFWrgdVKLL 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 678 SGHTLVLVPDALRADAHQLWRYFARHAVDL----------FDC-------------TPVQLQWLLDA--------GLGSD 726
Cdd:PLN02614 308 IEDLGELKPTIFCAVPRVLDRVYSGLQKKLsdggflkkfvFDSafsykfgnmkkgqSHVEASPLCDKlvfnkvkqGLGGN 387
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 727 payqpAQVLIGGEA-ISPAVWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANtrlyiLDAQDQPVP- 804
Cdd:PLN02614 388 -----VRIILSGAApLASHVESFLRVVACCHVLQGYGLTESCAGTFVSLPDELDMLGTVGPPVPN-----VDIRLESVPe 457
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 805 -----IGVT--GELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariyKTGDLARWLPDGNIDYLGRndfqiKVRGFR 877
Cdd:PLN02614 458 meydaLASTprGEICIRGKTLFSGYYKREDLTKEVLIDGWL---------HTGDVGEWQPNGSMKIIDR-----KKNIFK 523
|
....*
gi 641744967 878 IEAGE 882
Cdd:PLN02614 524 LSQGE 528
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
2918-3094 |
1.48e-07 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 57.08 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2918 IGHPIANTQIYIL--DAQGRVVPLGVaGEIHIAGAGVVRGYLGRPDLTAERFitdpfsgapearmYKTGDLGrWLPDGTL 2995
Cdd:PRK05851 347 LGNPIPGMEVRISpgDGAAGVAGREI-GEIEIRGASMMSGYLGQAPIDPDDW-------------FPTGDLG-YLVDGGL 411
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2996 EYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVIAREDSPGDKR---LVAYLLAQPDTVLEPADLRQRLSE--GVa 3070
Cdd:PRK05851 412 VVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARpglVIAAEFRGPDEAGARSEVVQRVASecGV- 490
|
170 180
....*....|....*....|....*.
gi 641744967 3071 eymIPS--AFVTLDAFPLTPNGKLDR 3094
Cdd:PRK05851 491 ---VPSdvVFVAPGSLPRTSSGKLRR 513
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1674-1943 |
2.20e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 56.95 E-value: 2.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1674 VIYTSGSTGKPKGVMNSHRALCN------RLVWMQNTyRLTPDDRVLQKTPFS--FDVSVWEFFwpLLYGARLVMARPDG 1745
Cdd:PLN02614 228 IMYTSGTTGDPKGVMISNESIVTliagviRLLKSANA-ALTVKDVYLSYLPLAhiFDRVIEECF--IQHGAAIGFWRGDV 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1746 H---KDAAYLAQLIERTGITTLHFVPSMLQQ------FVQWADADCA--------------------CDSLR-------- 1788
Cdd:PLN02614 305 KlliEDLGELKPTIFCAVPRVLDRVYSGLQKklsdggFLKKFVFDSAfsykfgnmkkgqshveasplCDKLVfnkvkqgl 384
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1789 ----RVICSGEAlPAELQQRFFARFNAQLHNL--YGPTEAAIDvTFwACQPDDHRSFVPIGRPIANTQLYI-------LD 1855
Cdd:PLN02614 385 ggnvRIILSGAA-PLASHVESFLRVVACCHVLqgYGLTESCAG-TF-VSLPDELDMLGTVGPPVPNVDIRLesvpemeYD 461
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1856 TLGQPVplgvAGELHIGGVGVARGYLNRPDLTAERFIpDPFINqpgarlykTGDLARWLPDGSLEYLGRndfqvKLRGFR 1935
Cdd:PLN02614 462 ALASTP----RGEICIRGKTLFSGYYKREDLTKEVLI-DGWLH--------TGDVGEWQPNGSMKIIDR-----KKNIFK 523
|
....*...
gi 641744967 1936 IELGEIEA 1943
Cdd:PLN02614 524 LSQGEYVA 531
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
2630-3092 |
2.30e-07 |
|
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: 56.69 E-value: 2.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2630 ASLSYDELNRRANRLAH-HLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALI 2708
Cdd:cd17632 66 ETITYAELWERVGAVAAaHDPEQPVRPGDFVAVLGFTSPDYATVDLALTRLGAVSVPLQAGASAAQLAPILAETEPRLLA 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2709 SQSAHLgimngSLPVILLDDGETRP----FDNEPD-------------------------TPLDARKQGLTPRH------ 2753
Cdd:cd17632 146 VSAEHL-----DLAVEAVLEGGTPPrlvvFDHRPEvdahraalesarerlaavgipvttlTLIAVRGRDLPPAPlfrpep 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2754 ----LAYVIYTSGSTGKPKGVMVEHANMVNF-LCSMRKEPGIAQEDVLLGVTSLSF-----------------------D 2805
Cdd:cd17632 221 dddpLALLIYTSGSTGTPKGAMYTERLVATFwLKVSSIQDIRPPASITLNFMPMSHiagrislygtlarggtayfaaasD 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2806 ISILEIFLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQATPSTWRMLVELRDFALPPGFK-ALCGGEALPENLAT 2884
Cdd:cd17632 301 MSTLFDDLALVRPTELFLVPRVCDMLFQRYQAELDRRSVAGADAETLAERVKAELRERVLGGRLLaAVCGSAPLSAEMKA 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2885 ---ALLQkvTTLWNLYGPTETTIwSTLNGLTTPTPYIGHPIANtqiyildaqgrvVP-LGV--------AGEIHIAGAGV 2952
Cdd:cd17632 381 fmeSLLD--LDLHDGYGSTEAGA-VILDGVIVRPPVLDYKLVD------------VPeLGYfrtdrphpRGELLVKTDTL 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2953 VRGYLGRPDLTAERFITDPFsgapearmYKTGD-LGRWLPDgTLEYLGRNDFQVKV-RGFRIELGEIETRLARCHGVHDA 3030
Cdd:cd17632 446 FPGYYKRPEVTAEVFDEDGF--------YRTGDvMAELGPD-RLVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQI 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 3031 VVIAREDSpgdkrlvAYLLA------QPDTVLEPADLRQRLSE---------GVAEYMIPSAFVtLDAFPLTP-NGKL 3092
Cdd:cd17632 517 FVYGNSER-------AYLLAvvvptqDALAGEDTARLRAALAEslqriareaGLQSYEIPRDFL-IETEPFTIaNGLL 586
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
2759-3099 |
3.06e-07 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 56.01 E-value: 3.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2759 YTSGSTGKPKGVMVEH--ANMVNFLCSMrkepgiaqedvLLGVTSLSFDISILEIF----------LPLLNGARLILATQ 2826
Cdd:PLN02479 202 YTSGTTASPKGVVLHHrgAYLMALSNAL-----------IWGMNEGAVYLWTLPMFhcngwcftwtLAALCGTNICLRQV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2827 AQAADAQQlamlIERHAVSFMQATPSTWRMLV----ELRDFALPPGFKALCGGEALPENLATALLQK---VTTLWNL--- 2896
Cdd:PLN02479 271 TAKAIYSA----IANYGVTHFCAAPVVLNTIVnapkSETILPLPRVVHVMTAGAAPPPSVLFAMSEKgfrVTHTYGLset 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2897 YGPTETTIWST-----------------------LNGLTTPTPYIGHPIAntqiyildAQGRVVplgvaGEIHIAGAGVV 2953
Cdd:PLN02479 347 YGPSTVCAWKPewdslppeeqarlnarqgvryigLEGLDVVDTKTMKPVP--------ADGKTM-----GEIVMRGNMVM 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2954 RGYLGRPDLTAERFitdpfsgapEARMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHGVHDAVVI 3033
Cdd:PLN02479 414 KGYLKNPKANEEAF---------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVV 484
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641744967 3034 AREDSPGDKRLVAYLLAQP--DTVLEPA---DLRQRLSEGVAEYMIPSAfVTLDAFPLTPNGKLDRKALPA 3099
Cdd:PLN02479 485 ARPDERWGESPCAFVTLKPgvDKSDEAAlaeDIMKFCRERLPAYWVPKS-VVFGPLPKTATGKIQKHVLRA 554
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
495-721 |
1.14e-06 |
|
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: 54.28 E-value: 1.14e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 495 EDQHLTYRELNRRANQLAHHLI-ALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDD----- 568
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTckvrv 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 569 ---------AAPVALLTQSAQVAQ-LNSTLP--TVLLDTPAAAACPDTNPVVQGLHAAH-LAYVIYTSGSTGRPKGVMVA 635
Cdd:cd05905 91 altveaclkGLPKKLLKSKTAAEIaKKKGWPkiLDFVKIPKSKRSKLKKWGPHPPTRDGdTAYIEYSFSSDGSLSGVAVS 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 636 HRNVINLATGLHTLLALDHPSRIALNASIVFDASVKNWIQL--LSGHTLVLVPDALRADAHQLW-----RYFARhavDLF 708
Cdd:cd05905 171 HSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLWHGCLLsvYSGHHTILIPPELMKTNPLLWlqtlsQYKVR---DAY 247
|
250
....*....|...
gi 641744967 709 dCTPVQLQWLLDA 721
Cdd:cd05905 248 -VKLRTLHWCLKD 259
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
1667-1937 |
1.32e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 54.34 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1667 DAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWMQN-----TYRLtpddrvlqKTPFSF-DVS-VWE---FFWPLLYGA 1736
Cdd:PTZ00342 302 DPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLCKhsifkKYNP--------KTHLSYlPIShIYErviAYLSFMLGG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1737 RLVMARpdghKDAAYLAQLIERTGITTLHFVP----------------------SMLQQ------------FVQWADA-- 1780
Cdd:PTZ00342 374 TINIWS----KDINYFSKDIYNSKGNILAGVPkvfnriytnimteinnlpplkrFLVKKilslrksnnnggFSKFLEGit 449
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1781 -------DCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTEA--AIDVtfwacQPDDHRSFVPIGRPIANTQL 1851
Cdd:PTZ00342 450 hisskikDKVNPNLEVILNGGGKLSPKIAEELSVLLNVNYYQGYGLTETtgPIFV-----QHADDNNTESIGGPISPNTK 524
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1852 YIL---------DTLGQpvplgvaGELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlYKTGDLARWLPDGSLEYL 1922
Cdd:PTZ00342 525 YKVrtwetykatDTLPK-------GELLIKSDSIFSGYFLEKEQTKNAFTEDGY--------FKTGDIVQINKNGSLTFL 589
|
330
....*....|....*.
gi 641744967 1923 GRNDFQVKL-RGFRIE 1937
Cdd:PTZ00342 590 DRSKGLVKLsQGEYIE 605
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1550-1733 |
1.40e-06 |
|
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: 53.89 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1550 EDQHLTYDALNRRANQLAHHLID-LGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYML-----DD 1623
Cdd:cd05905 11 EATTLTWGKLLSRAEKIAAVLQKkVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLgtckvRV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1624 ASPVALLTQANQRALLTGD----------VPRILldtaDFSHLSEDNPHV-------PGLDAHHLAYVIYTSGSTGKPKG 1686
Cdd:cd05905 91 ALTVEACLKGLPKKLLKSKtaaeiakkkgWPKIL----DFVKIPKSKRSKlkkwgphPPTRDGDTAYIEYSFSSDGSLSG 166
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 641744967 1687 VMNSHRALCNRLVWMQNTYRLTPDDRVLQKTPFSFDVSVWefFWPLL 1733
Cdd:cd05905 167 VAVSHSSLLAHCRALKEACELYESRPLVTVLDFKSGLGLW--HGCLL 211
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1531-1694 |
1.88e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 53.83 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1531 HQLVEDQ--AARTPDTTaVLFEDQHLTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAG--AAYV 1606
Cdd:PTZ00216 98 KEVVKDAdgKERTMEVT-HFNETRYITYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSmvAATV 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1607 PLDPGYPAerLAYMLDDASPVALLTQA-NQRALLT----GDVPR---ILLDT--ADF------------------SHLSE 1658
Cdd:PTZ00216 177 YANLGEDA--LAYALRETECKAIVCNGkNVPNLLRlmksGGMPNttiIYLDSlpASVdtegcrlvawtdvvakghSAGSH 254
|
170 180 190
....*....|....*....|....*....|....*.
gi 641744967 1659 DNPHVPGlDAHHLAYVIYTSGSTGKPKGVMNSHRAL 1694
Cdd:PTZ00216 255 HPLNIPE-NNDDLALIMYTSGTTGDPKGVMHTHGSL 289
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
616-919 |
1.91e-06 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 53.56 E-value: 1.91e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 616 LAYVIYTSGSTGRPKGVMVAHRNVINLATGlHTLLALDHPSRIAL------------NASIVFDASVKnwIQLLSGHTLV 683
Cdd:PLN02736 223 VATICYTSGTTGTPKGVVLTHGNLIANVAG-SSLSTKFYPSDVHIsylplahiyervNQIVMLHYGVA--VGFYQGDNLK 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 684 LVPD--ALR----ADAHQLW-------------------RYFA------RHAvdLFDCTPVQLQW------LLDAGLGSD 726
Cdd:PLN02736 300 LMDDlaALRptifCSVPRLYnriydgitnavkesgglkeRLFNaaynakKQA--LENGKNPSPMWdrlvfnKIKAKLGGR 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 727 PAYqpaqVLIGGEAISPAVWSRLQSLSDTRFINVYGPTEctvdaTACVVDRTQP----LPTIGKPLANTRLYILD----- 797
Cdd:PLN02736 378 VRF----MSSGASPLSPDVMEFLRICFGGRVLEGYGMTE-----TSCVISGMDEgdnlSGHVGSPNPACEVKLVDvpemn 448
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 798 --AQDQPVPigvTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLGR--NDFQIkV 873
Cdd:PLN02736 449 ytSEDQPYP---RGEICVRGPIIFKGYYKDEVQTREVIDEDGW--------LHTGDIGLWLPGGRLKIIDRkkNIFKL-A 516
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 641744967 874 RGFRIEAGEIESRLLRCPGVQDAVVIaredspGDT---RLVAYLCARPD 919
Cdd:PLN02736 517 QGEYIAPEKIENVYAKCKFVAQCFVY------GDSlnsSLVAVVVVDPE 559
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
1096-1326 |
2.85e-06 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 52.79 E-value: 2.85e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1096 ALHLTGRLDRPALTTALNGLVARHESLRTRFtsidgqpaqQIDPDTLGFSLSSHDLRKLDEAARTTRVAELAEqearARF 1175
Cdd:PRK09294 27 TAHLRGVLDIDALSDAFDALLRAHPVLAAHL---------EQDSDGGWELVADDLLHPGIVVVDGDAARPLPE----LQL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1176 DLTQGpLIRGQLLQLDDNTHVLLLTqHHIISDGWSIGILARELAALYQAALEGSEAnlPPLPVQYADYAvwqrqwlqGET 1255
Cdd:PRK09294 94 DQGVS-LLALDVVPDDGGARVTLYI-HHSIADAHHSASLLDELWSRYTDVVTTGDP--GPIRPQPAPQS--------LEA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1256 LNDLRDYWRDQLQGAPALL------EIPTDRPRPSVQRYAGDQVPFH----LDAGQLRRLHALNRQQGTTL-----FMTL 1320
Cdd:PRK09294 162 VLAQRGIRRQALSGAERFMpamyayELPPTPTAAVLAKPGLPQAVPVtrcrLSKAQTSSLAAFGRRHRLTVnalvsAAIL 241
|
....*.
gi 641744967 1321 LAAWSV 1326
Cdd:PRK09294 242 LAEWQL 247
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
2165-2535 |
3.00e-06 |
|
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: 52.87 E-value: 3.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2165 APLQEGILFHHLL-QEQGDTYLLRSMVAFTHRERLD--AFLSALQQVIDRHDILRT--AVCWQDLSQpvQVVWRQAILPI 2239
Cdd:cd19546 5 VPATAGQLRTWLLaRLDEETRGRHLSVALRLRGRLDrdALEAALGDVAARHEILRTtfPGDGGDVHQ--RILDADAARPE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2240 NHFEPTSPEDVLAQLQAHTEprtRRIDLSQAPLFRADIAhdPLQN-EWLLALSFHHLISDHMTLALIVGEIRLLLQHQAD 2318
Cdd:cd19546 83 LPVVPATEEELPALLADRAA---HLFDLTRETPWRCTLF--ALSDtEHVLLLVVHRIAADDESLDVLVRDLAAAYGARRE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2319 A-----LPTPLPYRNFIAQTLSVPNSAHE---------AYFRDKLADVDEPTA-PFGLLNVQGSGGDIHEARLVLDATLA 2383
Cdd:cd19546 158 GraperAPLPLQFADYALWERELLAGEDDrdsligdqiAYWRDALAGAPDELElPTDRPRPVLPSRRAGAVPLRLDAEVH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2384 SAIRQQARHLGVSPGVLFHVAWAQVLAQTSGRDDVVFGSVlLGRLAGAEGADRIMGMFINTLPLRISL-ADRGAAEVVER 2462
Cdd:cd19546 238 ARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTV-LPRDDEEGDLEGMVGPFARPLALRTDLsGDPTFRELLGR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2463 TSHDLMTLLEHEQAPLALAQRCSGVAPPM---PLFSTLLNYRHTQASSTDNT----LSDIRVLTSEERTNYPLTLAVDDR 2535
Cdd:cd19546 317 VREAVREARRHQDVPFERLAELLALPPSAdrhPVFQVALDVRDDDNDPWDAPelpgLRTSPVPLGTEAMELDLSLALTER 396
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
3111-3185 |
5.12e-06 |
|
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: 46.86 E-value: 5.12e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 3111 EAPQGDLEHALAQIWQTLLGV---ERVGRHDHFFELGGHSLLAVQLNARIRAEFLTDIPIVAIFQHPQLSALAEVILA 3185
Cdd:smart00823 7 AERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
604-888 |
5.25e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 52.41 E-value: 5.25e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 604 TNPVVQGLHAAHLAYVIYTSGSTGRPKGVMVAHRNVINLATGL--HTLLALDHPS-------------RIALNASIVFDA 668
Cdd:PTZ00342 294 TNYKIQNEDPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVVPLckHSIFKKYNPKthlsylpishiyeRVIAYLSFMLGG 373
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 669 SVKNW---IQLLS-------GHTLVLVPDALR----------ADAHQLWRYFARHAVDL---FDCTPvqLQWLLDAGLG- 724
Cdd:PTZ00342 374 TINIWskdINYFSkdiynskGNILAGVPKVFNriytnimteiNNLPPLKRFLVKKILSLrksNNNGG--FSKFLEGITHi 451
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 725 ----SDPAYQPAQVLI-GGEAISPAVWSRLQSLSDTRFINVYGPTECTvdaTACVVDRTQPLPT--IGKPLANTRLY--- 794
Cdd:PTZ00342 452 sskiKDKVNPNLEVILnGGGKLSPKIAEELSVLLNVNYYQGYGLTETT---GPIFVQHADDNNTesIGGPISPNTKYkvr 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 795 ---ILDAQDQPvPigvTGELHIGGAGVARGYLHRPDLTAERFIPDPFsadpaariYKTGDLARWLPDGNIDYLGRNDFQI 871
Cdd:PTZ00342 529 tweTYKATDTL-P---KGELLIKSDSIFSGYFLEKEQTKNAFTEDGY--------FKTGDIVQINKNGSLTFLDRSKGLV 596
|
330
....*....|....*...
gi 641744967 872 KvrgfrIEAGE-IESRLL 888
Cdd:PTZ00342 597 K-----LSQGEyIETDML 609
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
66-257 |
6.49e-06 |
|
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: 51.48 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 66 DAFLDVLQQVIARHDILRtAICWQGLHQPVQV----VWRQAPLTVNTLtttSSDTVPAQLRAATDPSNHRLNLSNAPLLS 141
Cdd:cd19534 37 DALRQALRALVEHHDALR-MRFRREDGGWQQRirgdVEELFRLEVVDL---SSLAQAAAIEALAAEAQSSLDLEEGPLLA 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 142 A-----TTAHDpvcgewLLSLSIHHLISDHITQALIIDEIRLLLEDRPEALPKPLP----YRNFI---AQILSVPLSEHE 209
Cdd:cd19534 113 AalfdgTDGGD------RLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPIPLPsktsFQTWAellAEYAQSPALLEE 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 641744967 210 QYFRNRLADIDTPTAPFDLVDVQGngeDITEARLSLDSSLADALRRQA 257
Cdd:cd19534 187 LAYWRELPAADYWGLPKDPEQTYG---DARTVSFTLDEEETEALLQEA 231
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
32-318 |
6.58e-06 |
|
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: 51.71 E-value: 6.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 32 APLQEGILFHYQL-QEKGDTYLLNSLLAFDSQTRLD--AFLDVLQQVIARHDILRTAICWQG--LHQPVQVVWRQAPLTv 106
Cdd:cd19546 5 VPATAGQLRTWLLaRLDEETRGRHLSVALRLRGRLDrdALEAALGDVAARHEILRTTFPGDGgdVHQRILDADAARPEL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 107 nTLTTTSSDTVPAQLRAATDpsnHRLNLS-----NAPLLSATTAhdpvcgEWLLSLSIHHLISDHITQALIIDEIRLLLE 181
Cdd:cd19546 84 -PVVPATEEELPALLADRAA---HLFDLTretpwRCTLFALSDT------EHVLLLVVHRIAADDESLDVLVRDLAAAYG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 182 DR-----PEALPKPLPYRNFI---------AQILSVPLSEHEQYFRNRLADI-DTPTAPFDLVDVQGNGEDITEARLSLD 246
Cdd:cd19546 154 ARregraPERAPLPLQFADYAlwerellagEDDRDSLIGDQIAYWRDALAGApDELELPTDRPRPVLPSRRAGAVPLRLD 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641744967 247 SSLADALRRQARHLGISSSVLFHVAWAQVLALTSGRDDVVFGSVLSgRLQGNLGADRVMGMFINTLPLRVSL 318
Cdd:cd19546 234 AEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLP-RDDEEGDLEGMVGPFARPLALRTDL 304
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
1677-1951 |
8.07e-06 |
|
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: 51.09 E-value: 8.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1677 TSGSTGKPKGVMNSHRALCN------RLVWMQNtyrLTPDDRVLQKTPFSFdvsvWEFFWPLLYGAR----LVMARPDGH 1746
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDLDVwaelvaRCLDAAG---VTPGDRVQNAYGYGL----FTGGLGFHYGAErlgaLVIPAGGGN 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1747 KDAayLAQLIERTGITTLHFVPSMLQQFVQWAD---ADCACDSLRRVICSGEALPAELQQRFFARFNAQLHNLYGPTE-- 1821
Cdd:cd05913 159 TER--QLQLIKDFGPTVLCCTPSYALYLAEEAEeegIDPRELSLKVGIFGAEPWTEEMRKRIERRLGIKAYDIYGLTEii 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1822 ---AAID------VTFWacqpDDHrsFVPIgrpiantqlYILDTLGQPVPLGVAGELHIggvgvargylnrPDLTAERFi 1892
Cdd:cd05913 237 gpgVAFEceekdgLHIW----EDH--FIPE---------IIDPETGEPVPPGEVGELVF------------TTLTKEAM- 288
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 1893 pdPFINqpgarlYKTGDLARWLPDGSLE---------YLGRNDFQVKLRGFRIELGEIEARLMQCPGV 1951
Cdd:cd05913 289 --PLIR------YRTRDITRLLPGPCPCgrthrridrITGRSDDMLIIRGVNVFPSQIEDVLLKIPGL 348
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
2738-3093 |
8.10e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 51.89 E-value: 8.10e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2738 PDTPLDARKqgltPRHLAYVIYTSGSTGKPKGVMVEHANMvnfLCSMRKepgiAQEDVLLGVTSLSFDIsiLEIF----- 2812
Cdd:PRK06814 783 PLVYFCNRD----PDDPAVILFTSGSEGTPKGVVLSHRNL---LANRAQ----VAARIDFSPEDKVFNA--LPVFhsfgl 849
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2813 -----LPLLNGARLilatqaqaadaqqlamlierhavsFMQATPSTWRMLVEL-----------RDFAL--------PPG 2868
Cdd:PRK06814 850 tgglvLPLLSGVKV------------------------FLYPSPLHYRIIPELiydtnatilfgTDTFLngyaryahPYD 905
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2869 FKAL----CGGEALPENLATALLQKV-TTLWNLYGPTETtiwSTLNGLTTPTpyigHPIANTQiyildaqGRVVPL---- 2939
Cdd:PRK06814 906 FRSLryvfAGAEKVKEETRQTWMEKFgIRILEGYGVTET---APVIALNTPM----HNKAGTV-------GRLLPGieyr 971
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2940 -----GV--AGEIHIAGAGVVRGYLgRPDltAERFITDPFSGapearMYKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRI 3012
Cdd:PRK06814 972 lepvpGIdeGGRLFVRGPNVMLGYL-RAE--NPGVLEPPADG-----WYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMI 1043
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 3013 ELGEIETRLARCHGVHDAVVIAREDSPGDKRLVayLLAQPDTVLEPADLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKL 3092
Cdd:PRK06814 1044 SLAAVEELAAELWPDALHAAVSIPDARKGERII--LLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKI 1121
|
.
gi 641744967 3093 D 3093
Cdd:PRK06814 1122 D 1122
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
1652-1985 |
8.65e-06 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 51.74 E-value: 8.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1652 DFSHLSEDNPHVPGL-DAHHLAYVIYTSGSTGKPKGVMNSHRALCNRLVWM-----QNTYRLTPDDRVLQKTPFS--FDV 1723
Cdd:PLN02430 202 DFLHMGKENPSETNPpKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlfmeQFEDKMTHDDVYLSFLPLAhiLDR 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1724 SVWEFFWPllYGARLVMArpdgHKDAAYLAQLIERTGITTLHFVPSM-------LQQFVQ-------------------W 1777
Cdd:PLN02430 282 MIEEYFFR--KGASVGYY----HGDLNALRDDLMELKPTLLAGVPRVferihegIQKALQelnprrrlifnalykyklaW 355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1778 ADADCACDS--------------------LRRVICSGEALPAELQQrfFARFN--AQLHNLYGPTEAAIDVTFwaCQPDD 1835
Cdd:PLN02430 356 MNRGYSHKKaspmadflafrkvkaklggrLRLLISGGAPLSTEIEE--FLRVTscAFVVQGYGLTETLGPTTL--GFPDE 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1836 HRSFVPIGRPIANTQLYI-------LDTLGQPVplgvAGELHIGGVGVARGYLNRPDLTAErFIPDPFinqpgarlYKTG 1908
Cdd:PLN02430 432 MCMLGTVGAPAVYNELRLeevpemgYDPLGEPP----RGEICVRGKCLFSGYYKNPELTEE-VMKDGW--------FHTG 498
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1909 DLARWLPDGSLEYLGRNDFQVKL-RGFRIELGEIEARLMQCPGVQEAVVVaredspGDT---RLVAYLCPQPGVTPDPAD 1984
Cdd:PLN02430 499 DIGEILPNGVLKIIDRKKNLIKLsQGEYVALEYLENVYGQNPIVEDIWVY------GDSfksMLVAVVVPNEENTNKWAK 572
|
.
gi 641744967 1985 L 1985
Cdd:PLN02430 573 D 573
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
672-1204 |
1.02e-05 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 51.80 E-value: 1.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 672 NWIQLLSGHTLVLVPDALRADAHQLWryfARHAVDLFDCTPVQLQWLLDAGLGSDPAYQPAQVLIGGEAISPAVWSRLQS 751
Cdd:COG3321 848 DWSALYPGRGRRRVPLPTYPFQREDA---AAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALAAA 924
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 752 LSDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANTRLYILDAQDQPVPIGVTGELHIGGAGVARGYLHRPDLTAE 831
Cdd:COG3321 925 ALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAALAL 1004
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 832 RFIPDPFSADPAARIYKTGDLARWLPDGNIDYLGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDAVVIAREDSPGDTRLV 911
Cdd:COG3321 1005 LAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAAAL 1084
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 912 AYLCARPDAELHPAALRQQLAASLADYMIPSAFVTLDALPLTPNGKLDRKALPAPDQTAFATRDYEAPQGGIETALAALW 991
Cdd:COG3321 1085 ALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAALA 1164
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 992 QELLGLDRVGRHDQFFALGGHSLLAVQLLNRMNKAGMDVALATLFAHPTLCDLAAAVTATAHDAPFTLPVADRTQPLPLS 1071
Cdd:COG3321 1165 AALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAAAA 1244
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1072 FSQQRLWFLAQLDPAASQAYHLPAALHLTGRLDRPALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDTLGFSLSSHDL 1151
Cdd:COG3321 1245 VAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAALAAA 1324
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 641744967 1152 RKLDEAARTTRVAELAEQEARARFDLTQGPLIRGQLLQLDDNTHVLLLTQHHI 1204
Cdd:COG3321 1325 LLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALA 1377
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
2633-3055 |
1.37e-05 |
|
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: 50.88 E-value: 1.37e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2633 SYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQS- 2711
Cdd:cd17641 13 TWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIAEDe 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2712 -------AHLGIMNGSLPVILLDD------------------GETRPFDNEPDTPLDARKQGLTPRHLAYVIYTSGSTGK 2766
Cdd:cd17641 93 eqvdkllEIADRIPSVRYVIYCDPrgmrkyddprlisfedvvALGRALDRRDPGLYEREVAAGKGEDVAVLCTTSGTTGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2767 PKGVMVEHANMvnflcsmrkepgIAQEDVLLGVTSLSFDISILEiFLPLLNGARLILATQAQaadaqqlamLIERHAVSF 2846
Cdd:cd17641 173 PKLAMLSHGNF------------LGHCAAYLAADPLGPGDEYVS-VLPLPWIGEQMYSVGQA---------LVCGFIVNF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2847 ------------------MQATPSTW---------RM----------------------------------LVELRDFAL 2865
Cdd:cd17641 231 peepetmmedlreigptfVLLPPRVWegiaadvraRMmdatpfkrfmfelgmklglraldrgkrgrpvslwLRLASWLAD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2866 PPGFKAL-------------CGGEALPENLATALLQKVTTLWNLYGPTETTIWSTLN-GLTTPTPYIGHPIANTQIYILD 2931
Cdd:cd17641 311 ALLFRPLrdrlgfsrlrsaaTGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHrDGDVDPDTVGVPFPGTEVRIDE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2932 AqgrvvplgvaGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGR-NDFQVKVRGF 3010
Cdd:cd17641 391 V----------GEILVRSPGVFVGYYKNPEATAEDFDEDGW--------LHTGDAGYFKENGHLVVIDRaKDVGTTSDGT 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 641744967 3011 RIELGEIETRLARCHGVHDAVVIARedspGDKRLVAYLLAQPDTV 3055
Cdd:cd17641 453 RFSPQFIENKLKFSPYIAEAVVLGA----GRPYLTAFICIDYAIV 493
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
710-960 |
1.51e-05 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 50.53 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 710 CTPVQLQWLLDAG--LGSDPA-YQPAQVLIGGEAISPAVWSRLQSLSDTRFINVYGPTECTVD-ATACvvdRTQP----- 780
Cdd:COG1541 181 GTPSYLLYLAEVAeeEGIDPRdLSLKKGIFGGEPWSEEMRKEIEERWGIKAYDIYGLTEVGPGvAYEC---EAQDglhiw 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 781 ----LPTIGKPlaNTrlyildaqDQPVPIGVTGELHIGGagvargylhrpdLTAERFipdpfsadPAARiYKTGDLARWL 856
Cdd:COG1541 258 edhfLVEIIDP--ET--------GEPVPEGEEGELVVTT------------LTKEAM--------PLIR-YRTGDLTRLL 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 857 PDGN--------IDY-LGRNDFQIKVRGFRIEAGEIESRLLRCPGVQDA--VVIAREDspGDTRLVAYLCARPDAELhpA 925
Cdd:COG1541 307 PEPCpcgrthprIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEyqIVVDREG--GLDELTVRVELAPGASL--E 382
|
250 260 270
....*....|....*....|....*....|....*...
gi 641744967 926 ALRQQLAASLADYMIPSA---FVTLDALPLTPnGKLDR 960
Cdd:COG1541 383 ALAEAIAAALKAVLGLRAeveLVEPGSLPRSE-GKAKR 419
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
2044-2101 |
1.76e-05 |
|
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: 44.86 E-value: 1.76e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 641744967 2044 ALAAVWQDLLGLT--RVGRHDHFFALGGHSLLIVSLIERLRRA-GLALDVRGVFSTPVLSD 2101
Cdd:pfam00550 2 RLRELLAEVLGVPaeEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLAE 62
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
54-331 |
2.21e-05 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 50.55 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 54 NSLLAFDSQTRLDAFL--DVLQQVIARHDILRTAIC-----WQGLHQPV---QVVWRqapLTVNTLTTTSSDTVPAQlra 123
Cdd:PRK05691 2813 NQALLLEPRQALDPALleQALQALVEHHDALRLRFSqadgrWQAEYRAVtaqELLWQ---VTVADFAECAALFADAQ--- 2886
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 124 atdpsnHRLNLSNAPLLSATTAHDPVCGEWLLsLSIHHLISDHITQALIIDEI----RLLLEDRPEALP-KPLPYRNFIA 198
Cdd:PRK05691 2887 ------RSLDLQQGPLLRALLVDGPQGQQRLL-LAIHHLVVDGVSWRVLLEDLqalyRQLSAGAEPALPaKTSAFRDWAA 2959
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 199 QIL----SVPLSEHEQYFRNRLADIDTpTAPFDLVDVQGNGEDITEARLSLDSSLADALRRQ---ARHLGISSSVLfhVA 271
Cdd:PRK05691 2960 RLQayagSESLREELGWWQAQLGGPRA-ELPCDRPQGGNLNRHAQTVSVRLDAERTRQLLQQapaAYRTQVNDLLL--TA 3036
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 641744967 272 WAQVLALTSGRDDVVFGSVLSGR--LQGNLGADRVMGMFINTLPLRvsLRERSVHDVVQATS 331
Cdd:PRK05691 3037 LARVLCRWSGQPSVLVQLEGHGReaLFDDIDLTRSVGWFTSAYPLR--LTPAPGDDAARGES 3096
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
2631-2823 |
5.33e-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: 5.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2631 SLSYDELNRRANRLAHHLI-SFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYML-----DDAKP 2704
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLgtckvRVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2705 VALISqSAHLGIMNGSLPVILLDDGETRP----FDNEP-DTPLDARKQGLTPR----HLAYVIYTSGSTGKPKGVMVEHA 2775
Cdd:cd05905 94 VEACL-KGLPKKLLKSKTAAEIAKKKGWPkildFVKIPkSKRSKLKKWGPHPPtrdgDTAYIEYSFSSDGSLSGVAVSHS 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 641744967 2776 NMVNFlCSMRKEPGIAQE-DVLLGVTSLSFDIS-ILEIFLPLLNGARLIL 2823
Cdd:cd05905 173 SLLAH-CRALKEACELYEsRPLVTVLDFKSGLGlWHGCLLSVYSGHHTIL 221
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
972-1050 |
7.47e-05 |
|
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: 43.78 E-value: 7.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 972 ATRDYEAPQGGIETALAALWQELLGL---DRVGRHDQFFALGGHSLLAVQLLNRMNKA-GMDVALATLFAHPTLCDLAAA 1047
Cdd:smart00823 2 AALPPAERRRLLLDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAAtGLRLPATLVFDHPTPAALAEH 81
|
...
gi 641744967 1048 VTA 1050
Cdd:smart00823 82 LAA 84
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1554-2005 |
1.30e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 47.91 E-value: 1.30e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1554 LTYDALNRRANQLAHHLIDLGVKPDDRIAICVERSLDMVIGLLAILKAGAAYVPLDPGYPAERLAYMLDDAS-PVALLTQ 1632
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEvSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1633 ANQRALLT---------------GDVPRILLDTAD-----------FSHLSEDNPHVPGLDAHHLAYVIYTSGSTGKPKG 1686
Cdd:PLN02861 158 SKISSILSclpkcssnlktivsfGDVSSEQKEEAEelgvscfsweeFSLMGSLDCELPPKQKTDICTIMYTSGTTGEPKG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1687 VMNSHRALCNRLVWMQNTYRLTpdDRVLQKTPFSFDvsvwefFWPLLYGARLVMARPDGHK---------DAAYLAQLIE 1757
Cdd:PLN02861 238 VILTNRAIIAEVLSTDHLLKVT--DRVATEEDSYFS------YLPLAHVYDQVIETYCISKgasigfwqgDIRYLMEDVQ 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1758 RTGITTLHFVPSM---------------------------------LQQFVQWADADCACDSLR------------RVIC 1792
Cdd:PLN02861 310 ALKPTIFCGVPRVydriytgimqkissggmlrkklfdfaynyklgnLRKGLKQEEASPRLDRLVfdkikeglggrvRLLL 389
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1793 SGEA-LPAELQQrfFARFN--AQLHNLYGPTEaaidvtfwACQPddhrSFVPIGRPIAntqlyILDTLGQPVPLGVA--- 1866
Cdd:PLN02861 390 SGAApLPRHVEE--FLRVTscSVLSQGYGLTE--------SCGG----CFTSIANVFS-----MVGTVGVPMTTIEArle 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1867 ---------------GELHIGGVGVARGYLNRPDLTAERFIPDPFinqpgarlyKTGDLARWLPDGSLEYLGRNDFQVKL 1931
Cdd:PLN02861 451 svpemgydalsdvprGEICLRGNTLFSGYHKRQDLTEEVLIDGWF---------HTGDIGEWQPNGAMKIIDRKKNIFKL 521
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 641744967 1932 -RGFRIELGEIEARLMQCPGVQEAVVVAredSPGDTRLVAYLCPQpgvtpdpadlRQQLGQHLAEYMVPGAFVTL 2005
Cdd:PLN02861 522 sQGEYVAVENLENTYSRCPLIASIWVYG---NSFESFLVAVVVPD----------RQALEDWAANNNKTGDFKSL 583
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
499-963 |
2.29e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 46.76 E-value: 2.29e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 499 LTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDPAYPAERLAYILDDAAPVALLTQS 578
Cdd:PLN02861 78 LTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSIAFVQE 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 579 AQVAQLNSTLP--TVLLDTPAA----------------AACPDTNPVVQ---------GLHAAHLAYVIYTSGSTGRPKG 631
Cdd:PLN02861 158 SKISSILSCLPkcSSNLKTIVSfgdvsseqkeeaeelgVSCFSWEEFSLmgsldcelpPKQKTDICTIMYTSGTTGEPKG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 632 VMVAHRNVI-NLATGLHTLLALDhpsRIA---------LNASIVFD-----------ASVKNW----------IQLLSGH 680
Cdd:PLN02861 238 VILTNRAIIaEVLSTDHLLKVTD---RVAteedsyfsyLPLAHVYDqvietyciskgASIGFWqgdirylmedVQALKPT 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 681 TLVLVP---DALRADAHQLWRYFARHAVDLFDCTPVQLQWLLDAGLGSDPAyQP-----------------AQVLIGGEA 740
Cdd:PLN02861 315 IFCGVPrvyDRIYTGIMQKISSGGMLRKKLFDFAYNYKLGNLRKGLKQEEA-SPrldrlvfdkikeglggrVRLLLSGAA 393
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 741 ISPA-VWSRLQSLSDTRFINVYGPTECTVDATACVVDRTQPLPTIGKPLANtrlyiLDAQDQPVP-IGVT-------GEL 811
Cdd:PLN02861 394 PLPRhVEEFLRVTSCSVLSQGYGLTESCGGCFTSIANVFSMVGTVGVPMTT-----IEARLESVPeMGYDalsdvprGEI 468
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 812 HIGGAGVARGYLHRPDLTAERFIPDPFsadpaariyKTGDLARWLPDGNIDYLGRndfqiKVRGFRIEAGE------IES 885
Cdd:PLN02861 469 CLRGNTLFSGYHKRQDLTEEVLIDGWF---------HTGDIGEWQPNGAMKIIDR-----KKNIFKLSQGEyvavenLEN 534
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 886 RLLRCPGVQD-------------AVVI----ARED------SPGDtrlVAYLCARPDA------ELHPAALRQQLAAS-- 934
Cdd:PLN02861 535 TYSRCPLIASiwvygnsfesflvAVVVpdrqALEDwaannnKTGD---FKSLCKNLKArkyildELNSTGKKLQLRGFem 611
|
570 580 590
....*....|....*....|....*....|
gi 641744967 935 -LADYMIPSAFvTLDALPLTPNGKLDRKAL 963
Cdd:PLN02861 612 lKAIHLEPNPF-DIERDLITPTFKLKRPQL 640
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
1026-1563 |
3.50e-04 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 46.79 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1026 AGMDVALATLFAHPTLCDLAAAVTATAHDAPFTLPVADRTQPLPLSFSQQRLWFLAQLDPAASQAYHLPAALHLTGRLDR 1105
Cdd:COG3321 843 AGVPVDWSALYPGRGRRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAAALAAALLALAAAAAAALALA 922
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1106 PALTTALNGLVARHESLRTRFTSIDGQPAQQIDPDTLGFSLSSHDLRKLDEAARTTRVAELAEQEARARFDLTQGPLIRG 1185
Cdd:COG3321 923 AAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAAAAAL 1002
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1186 QLLQLDDNTHVLLLTQHHIISDGWSIGILARELAALYQAALEGSEANLPPLPVQYADYAVWQRQWLQGETLNDLRDYWRD 1265
Cdd:COG3321 1003 ALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELALAAA 1082
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1266 QLQGAPALLEIPTDRPRPSVQRYAGDQVPFHLDAGQLRRLHALNRQQGTTLFMTLLAAWSVVLSRLSGQDDIVIGTPVAN 1345
Cdd:COG3321 1083 ALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAALAAA 1162
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1346 RPRQELEGMVGFFVNTLALRTEPGRCHAVADLLDQVRERALDAYAHQALPFEQVVEILQPARSLSYSPIFQVMLSLNNTP 1425
Cdd:COG3321 1163 LAAALLAAAALLLALALALAAALAAALAGLAALLLAALLAALLAALLALALAALAAAAAALLAAAAAAAALALLALAAAA 1242
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 1426 AQALTLPDLTLSAVERPQhSTHFDLSLSLIETENGLNGGLVYATDLFDRETILRVVGYVENILMAMADDVTQPVATLPIL 1505
Cdd:COG3321 1243 AAVAALAAAAAALLAALA-ALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAAAAAAAAAAAAAAAAAAL 1321
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 641744967 1506 PDSERRQVMLDFNATEADFPHDALIHQLVEDQAARTPDTTAVLFEDQHLTYDALNRRA 1563
Cdd:COG3321 1322 AAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALA 1379
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
2621-3097 |
5.01e-04 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 45.93 E-value: 5.01e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2621 DAIAVVFGEAS---LSYDELNRRANRLAHHLI-SFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLR 2696
Cdd:PRK05620 25 DTTVTTWGGAEqeqTTFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2697 YMLDDAKPVALISQSA---HLGIMNGSLP-----VILLDDGETRPFDNEP--------DTPLDARKQ-----GLTPRHLA 2755
Cdd:PRK05620 105 HIINHAEDEVIVADPRlaeQLGEILKECPcvravVFIGPSDADSAAAHMPegikvysyEALLDGRSTvydwpELDETTAA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2756 YVIYTSGSTGKPKGVMVEHANMvnFLCSMRkepgiaqedvLLGVTSLSfdISILEIFL-------------PL---LNGA 2819
Cdd:PRK05620 185 AICYSTGTTGAPKGVVYSHRSL--YLQSLS----------LRTTDSLA--VTHGESFLccvpiyhvlswgvPLaafMSGT 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2820 RLILATQAQAADAQQLamLIERHAVSFMQATPSTWRMLVeLRDFALPPGFKAL----CGGEALPENLATALLQK----VT 2891
Cdd:PRK05620 251 PLVFPGPDLSAPTLAK--IIATAMPRVAHGVPTLWIQLM-VHYLKNPPERMSLqeiyVGGSAVPPILIKAWEERygvdVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2892 TLWnlyGPTETTIWSTLNglTTPTPYIGHPIANTQIyildAQGRvVPLGV-----------------AGEIHIAGAGVVR 2954
Cdd:PRK05620 328 HVW---GMTETSPVGTVA--RPPSGVSGEARWAYRV----SQGR-FPASLeyrivndgqvmestdrnEGEIQVRGNWVTA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2955 GYL----GRPDLTAERFITDPFSGAPEARM----YKTGDLGRWLPDGTLEYLGRNDFQVKVRGFRIELGEIETRLARCHG 3026
Cdd:PRK05620 398 SYYhsptEEGGGAASTFRGEDVEDANDRFTadgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPE 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 641744967 3027 VHDAVVIAREDSPGDKRLVAYLLAQPDTvlEPA-----DLRQRLSEGVAEYMIPSAFVTLDAFPLTPNGKLDRKAL 3097
Cdd:PRK05620 478 VVECAVIGYPDDKWGERPLAVTVLAPGI--EPTretaeRLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
2632-2796 |
5.28e-04 |
|
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: 45.49 E-value: 5.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2632 LSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLGILKAGGAYVPLDPTYPVERLRYMLDDAKPVALISQs 2711
Cdd:cd05939 4 WTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFN- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2712 ahlgimngslpviLLDDGETRPFDNEPDTPLdarkQGLTPRhLAYvIYTSGSTGKPKGVMVEHANMVNFLCSMRKEPGIA 2791
Cdd:cd05939 83 -------------LLDPLLTQSSTEPPSQDD----VNFRDK-LFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFGMR 143
|
....*
gi 641744967 2792 QEDVL 2796
Cdd:cd05939 144 PEDVV 148
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
2619-2774 |
7.44e-04 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 45.17 E-value: 7.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2619 TPDAIAVVF-----GEASLSYDELNRRANRLAHHLISFGVRPDERVAICVERGLDMVVGLLG------------------ 2675
Cdd:PRK03584 97 RDDRPAIIFrgedgPRRELSWAELRRQVAALAAALRALGVGPGDRVAAYLPNIPETVVAMLAtaslgaiwsscspdfgvq 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2676 ------------ILKAGGAY----VPLDPTYPVERLRYMLDDAKPVALISQSAHLGIMNGSLPVILLDD----GETRPFD 2735
Cdd:PRK03584 177 gvldrfgqiepkVLIAVDGYryggKAFDRRAKVAELRAALPSLEHVVVVPYLGPAAAAAALPGALLWEDflapAEAAELE 256
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 641744967 2736 NEPdTPLDarkqgltprHLAYVIYTSGSTGKPK-------GVMVEH 2774
Cdd:PRK03584 257 FEP-VPFD---------HPLWILYSSGTTGLPKcivhghgGILLEH 292
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
482-555 |
1.01e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 45.09 E-value: 1.01e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 641744967 482 QAEQTPEAIAVLFEDQHLTYRELNRRANQLAHHLIALGVQPDDRVALCVERSLEMMVGLLGILKAGAAYVPMDP 555
Cdd:PRK07868 456 QARDAPKGEFLLFDGRVHTYEAVNRRINNVVRGLIAVGVRQGDRVGVLMETRPSALVAIAALSRLGAVAVLMPP 529
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
2751-2778 |
1.32e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 44.32 E-value: 1.32e-03
10 20
....*....|....*....|....*...
gi 641744967 2751 PRHLAYVIYTSGSTGKPKGVMVEHANMV 2778
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNLI 247
|
|
| Anticodon_Ia_Cys |
cd07963 |
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA ... |
486-519 |
1.51e-03 |
|
Anticodon-binding domain of cysteinyl tRNA synthetases; This domain is found in cysteinyl tRNA synthetases (CysRS), which belong to the class Ia aminoacyl tRNA synthetases. It lies C-terminal to the catalytic core domain, and recognizes and specifically binds to the tRNA anticodon. CysRS catalyzes the transfer of cysteine to the 3'-end of its tRNA.
Pssm-ID: 153417 [Multi-domain] Cd Length: 156 Bit Score: 41.78 E-value: 1.51e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 641744967 486 TPEAIAVLFEdqhLTyRELNR-------RANQLAHHLIALG 519
Cdd:cd07963 48 TPEALAVLFE---LA-REINRlkkedieKAAALAALLKALG 84
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
2943-3024 |
2.38e-03 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 43.68 E-value: 2.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2943 GEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmyKTGDLGRWLPDGTLEYLGRndfqvKVRGFRIELGE------ 3016
Cdd:PLN02861 466 GEICLRGNTLFSGYHKRQDLTEEVLIDGWF---------HTGDIGEWQPNGAMKIIDR-----KKNIFKLSQGEyvaven 531
|
....*...
gi 641744967 3017 IETRLARC 3024
Cdd:PLN02861 532 LENTYSRC 539
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
2751-3021 |
2.50e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 43.55 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2751 PRHLAYVIYTSGSTGKPKGVMVEHANMVNFL-----CSMRK-----------------EPGIAQEDVLLGVT--SLSFDI 2806
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVvplckHSIFKkynpkthlsylpishiyERVIAYLSFMLGGTinIWSKDI 382
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2807 SILEifLPLLNGARLILATQAQAADAQQLAMLIERHAVSFMQatpstwRMLVElRDFALPPGFKA--------------- 2871
Cdd:PTZ00342 383 NYFS--KDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLK------RFLVK-KILSLRKSNNNggfskflegithiss 453
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2872 -------------LCGGEALPENLATALlqkvTTLWNL-----YGPTETT--IWSTlNGLTTPTPYIGHPIANTQIY--- 2928
Cdd:PTZ00342 454 kikdkvnpnleviLNGGGKLSPKIAEEL----SVLLNVnyyqgYGLTETTgpIFVQ-HADDNNTESIGGPISPNTKYkvr 528
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2929 ---ILDAQGRvVPlgvAGEIHIAGAGVVRGYLGRPDLTAERFITDPFsgapearmYKTGDLGRWLPDGTLEYLGRNDFQV 3005
Cdd:PTZ00342 529 tweTYKATDT-LP---KGELLIKSDSIFSGYFLEKEQTKNAFTEDGY--------FKTGDIVQINKNGSLTFLDRSKGLV 596
|
330
....*....|....*..
gi 641744967 3006 KvrgfrIELGE-IETRL 3021
Cdd:PTZ00342 597 K-----LSQGEyIETDM 608
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
2918-3016 |
2.72e-03 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 43.47 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 641744967 2918 IGHPIANTQIYI-------LDAQGRVVplgvAGEIHIAGAGVVRGYLGRPDLTAERFITDpfsgapearMYKTGDLGRWL 2990
Cdd:PLN02614 441 VGPPVPNVDIRLesvpemeYDALASTP----RGEICIRGKTLFSGYYKREDLTKEVLIDG---------WLHTGDVGEWQ 507
|
90 100
....*....|....*....|....*.
gi 641744967 2991 PDGTLEYLGRndfqvKVRGFRIELGE 3016
Cdd:PLN02614 508 PNGSMKIIDR-----KKNIFKLSQGE 528
|
|
|