|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2-2129 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1571.70 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2 SDLRKRLESLTPEQRDMVLKKLKnkRENHYLSNggrHVIPR-HEERGSYPLSSIQKQIWFMSQLNPELPIYNEHlIKINL 80
Cdd:PRK12467 7 LRIARRFITLPLEKRRLYLEKMQ--EEGVSFAN---LPIPQvRSAFERIPLSYAQERQWFLWQLDPDSAAYNIP-TALRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 81 SGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVITKSEP-TIQFLSLRGISGEEQQEILSEYCRKEANYPYRLEQE 159
Cdd:PRK12467 81 RGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSlTIPLDDLANEQGRARESQIEAYINEEVARPFDLANG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 160 NLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYSQNGEInpeqSQEELTIQYHDYALWQEKLLTSENL 239
Cdd:PRK12467 161 PLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYSQGREP----SLPALPIQYADYAIWQRSWLEAGER 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 240 EKGLEYWKEKLEGDLPMLSIGG----ITQEGTGvGSEYNFKIPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQET 315
Cdd:PRK12467 237 ERQLAYWQEQLGGEHTVLELPTdrprPAVPSYR-GARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 316 DLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVIEYLQQVHETTIQALENQDVPFEKVVEVLNPNRDVRANPFY 395
Cdd:PRK12467 316 DIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLF 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 396 QLLFVMQEPPTQFS------LPGIKVEYELIPTEVARFPLTLSIIEGEEMIGRVL-YRTSILSEYEVQSFVQRLLQVADE 468
Cdd:PRK12467 396 QVMFNHQNTATGGRdregaqLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFtYATDLFEATTIERLATHWRNLLEA 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 469 IVQSPHQRIYDLNLLTSKERSESAYLYNQSGcKPFPTEPIHVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWL 548
Cdd:PRK12467 476 IVAEPRRRLGELPLLDAEERARELVRWNAPA-TEYAPDCVHQLIEAQARQHPERPALVFGEQVLSYAELNRQANRLAHVL 554
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 549 QKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITHSEYKTSYE-GYEVPILYI 627
Cdd:PRK12467 555 IAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPvPAGLRSLCL 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 628 DQLDDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTT 707
Cdd:PRK12467 635 DEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQLAADDSMLMVSTFAFDLGVTE 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 708 IYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKA-LSSESGTKLFPRKGLILGGEASEWSWIKEIYRN 786
Cdd:PRK12467 715 LFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQAlLQASRVALPRPQRALVCGGEALQVDLLARVRAL 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 787 IPaSCKLFNHYGPSETTIGVAVYEVTKKGLSNQFSttPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNR 866
Cdd:PRK12467 795 GP-GARLINHYGPTETTVGVSTYELSDEERDFGNV--PIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRR 871
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 867 EELTAERFMEDPFITD-SRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNE 945
Cdd:PRK12467 872 PALTAERFVPDPFGADgGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQPGDAG 951
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 946 EQLVAYYV-------SKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEIQVSNWNEIEIQPMNRL 1018
Cdd:PRK12467 952 LQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDASAVQATFVAPQTEL 1031
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1019 EEKMKDVWEKILERPVPSIDDSFFKLGGHSLLATRLVSMIRKEFKVELSIKEFFEKPSIRELSTHLLQLEAVsthfALSN 1098
Cdd:PRK12467 1032 EKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAVAAQQQG----AQPA 1107
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1099 ISEAEKEKGIPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNiDPVQVVL 1178
Cdd:PRK12467 1108 LPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQEDG-RTRQVIH 1186
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1179 KDLKCTINILDFD-ENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAI 1257
Cdd:PRK12467 1187 PVGSLTLEEPLLLaADKDEAQLKVYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDELVAL 1266
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1258 YHQIISNMPIQL-EQPVyQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEK 1336
Cdd:PRK12467 1267 YAAYSQGQSLQLpALPI-QYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPA 1345
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1337 HAVLIKEICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQ 1416
Cdd:PRK12467 1346 LAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASFQQLLQQ 1425
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1417 VNNQILGALENQDISFERIVQELNPERSLSYNPIYQVAFTLQNDEQGKNGNYGGLSVEEFEIEWRTSKVDLTLIIGQSKR 1496
Cdd:PRK12467 1426 VKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQAQLPGLSVESLSWESQTAQFDLTLDTYESSE 1505
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1497 GFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENPNMEISRIQLVD---QQHDLLVKKAESQPRSIKDCIQYSFENWVR 1573
Cdd:PRK12467 1506 GLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDeaeRRQILEGWNATHTGYPLARLVHQLIEDQAA 1585
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1574 SSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDF 1653
Cdd:PRK12467 1586 ATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAY 1665
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1654 ILKDASVGAIVTQTSLEEKLSKSD-LPYLCTDQSQD-----SEDYSLLTKDksyPEDIAYIIYTSGTTGTPNGVMVKHSS 1727
Cdd:PRK12467 1666 MIEDSGIELLLTQSHLQARLPLPDgLRSLVLDQEDDwlegySDSNPAVNLA---PQNLAYVIYTSGSTGRPKGAGNRHGA 1742
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1728 VMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDS 1807
Cdd:PRK12467 1743 LVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSMLQQ 1822
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1808 ILPED-----IPSLQTVSTGGERCPIKVAKRWSL---DRNFYNVYGPTETTIATT-WYRVSSPECVQDSVPIGTPVPNTE 1878
Cdd:PRK12467 1823 LLQMDeqvehPLSLRRVVCGGEALEVEALRPWLErlpDTGLFNLYGPTETAVDVThWTCRRKDLEGRDSVPIGQPIANLS 1902
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1879 VFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPF-REEEILYKTGDIGKVLHDGNLEHLGRLDHQIKV 1957
Cdd:PRK12467 1903 TYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKI 1982
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1958 RGFRIELGEIESLLNLQTGVKEAIVQPLgDNQNYHTLVAYVVPHGEWEEKKIIEE----------LRSKLPEHMVPSIFV 2027
Cdd:PRK12467 1983 RGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVPTDPGLVDDDEAQvalrailknhLKASLPEYMVPAHLV 2061
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2028 QMEELPRLNNKKVDRHSLPtAVHIFRQQKVIQKPVTEEEVVVAECWAETLNLPidNIGLNSNFFELGGHSLTATQLVARi 2107
Cdd:PRK12467 2062 FLARMPLTPNGKLDRKALP-APDASELQQAYVAPQSELEQRLAAIWQDVLGLE--QVGLHDNFFELGGDSIISIQVVSR- 2137
|
2170 2180
....*....|....*....|..
gi 497785100 2108 SELFEIELPIKAIFEYPTIQAI 2129
Cdd:PRK12467 2138 ARQAGIRFTPKDLFQHQTVQSL 2159
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
32-2129 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1217.32 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 32 LSNGGRHV--IPRHEERGSYPLSSIQKQIWFMSQLNPELPIYNehlIK--INLSGKVNIEALKKSFEQIVNRHQILRMRV 107
Cdd:PRK05691 657 LAGGGAAQaaIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYN---IPggLHLRGELDEAALRASFQRLVERHESLRTRF 733
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 108 KQtEDSI--EQVITKSEPTIQFLSLRGISGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILS 185
Cdd:PRK05691 734 YE-RDGValQRIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVA 812
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 186 DGWSASILLSELERFYNMYSQNGEINpeqsQEELTIQYHDYALWQEKLLTSENLEKGLEYWKEKLEGDLPMLSI-----G 260
Cdd:PRK05691 813 DGWSLNILLDEFSRLYAAACQGQTAE----LAPLPLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELatdhpR 888
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 261 GITQEGTGvgSEYNFKIPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFIN 340
Cdd:PRK05691 889 SARQAHSA--ARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFIN 966
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 341 TVVIRTKAEQNLSVIEYLQQVHETTIQALENQDVPFEKVVEVLNpnrDVRANPFYQLLFVMQE--PPTQFSLPGIKVEyE 418
Cdd:PRK05691 967 TQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALP---QAREQGLFQVMFNHQQrdLSALRRLPGLLAE-E 1042
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 419 LiP--TEVARFPLTLSiiEGEEMIGRVL----YRTSILSEYEVQSFVQRLLQVADEIVQSPHQRIYDLNLLTSKERSESA 492
Cdd:PRK05691 1043 L-PwhSREAKFDLQLH--SEEDRNGRLTlsfdYAAELFDAATIERLAEHFLALLEQVCEDPQRALGDVQLLDAAERAQLA 1119
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 493 YlYNQSGCKPfPTEPIHVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIA 572
Cdd:PRK05691 1120 Q-WGQAPCAP-AQAWLPELLNEQARQTPERIALVWDGGSLDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVG 1197
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 573 MLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITHSEYKTSYEGYE-VPILYIDQLDdflLDEREDNL-NVDCDSSQ 650
Cdd:PRK05691 1198 LLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEgVSAIALDSLH---LDSWPSQApGLHLHGDN 1274
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 651 LAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDryLLLQS--LAYDFCLTTIYTSLLSGGTLFFLLKEDAID 728
Cdd:PRK05691 1275 LAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSD--VLMQKapISFDVSVWECFWPLITGCRLVLAGPGEHRD 1352
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 729 PAKVEEIVQGKAIDWYKITPSHLKALSSESG----TKLfprKGLILGGEASEWSWIKEIYRNIPAsCKLFNHYGPSETTI 804
Cdd:PRK05691 1353 PQRIAELVQQYGVTTLHFVPPLLQLFIDEPLaaacTSL---RRLFSGGEALPAELRNRVLQRLPQ-VQLHNRYGPTETAI 1428
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 805 GVAVYEVTKKglSNQFSttPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITD-S 883
Cdd:PRK05691 1429 NVTHWQCQAE--DGERS--PIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDgA 1504
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 884 RMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYVSKK--EVLDK 961
Cdd:PRK05691 1505 RLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAVLVREGAAGAQLVGYYTGEAgqEAEAE 1584
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 962 DLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEIQvsnWNEIE-IQPMNRLEEKMKDVWEKILERPVPSIDDS 1040
Cdd:PRK05691 1585 RLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPV---WQQREhVEPRTELQQQIAAIWREVLGLPRVGLRDD 1661
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1041 FFKLGGHSLLATRLVSMIRKEFKVELSIKEFFEKPSIRELSTHLLQLEAVSTHFALSNISEAEKEKGIPLSDAQKRMWFL 1120
Cdd:PRK05691 1662 FFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVARIQAAGERNSQGAIARVDRSQPVPLSYSQQRMWFL 1741
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1121 YRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFrESKNIDPVQVVLKDLKCTINILDF---DENRSEQ 1197
Cdd:PRK05691 1742 WQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRTTF-PSVDGVPVQQVAEDSGLRMDWQDFsalPADARQQ 1820
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1198 DIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMPIQLEQPVYQYA 1277
Cdd:PRK05691 1821 RLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYL 1900
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1278 DYVNWQQNRYTEEQINQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAvlikeiceeAKVTPY---- 1353
Cdd:PRK05691 1901 DYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPADRPRPPVQSHRGELYRFDLSPELA---------ARVRAFnaqr 1971
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1354 --TIFLTF---FNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGALENQ 1428
Cdd:PRK05691 1972 glTLFMTMtatLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQ 2051
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1429 DISFERIVQELNPERSLSYNPIYQVAFTLQNDEQGKNGNYGGLSVEEFEIEWRTSKVDLTLIIGQSKRGFEMVMEYNTDL 1508
Cdd:PRK05691 2052 DLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSRQLAGMTVEYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDL 2131
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1509 FRQQSIEQMLSDYIKIISQVIENPNMEISRIQLVD---QQHDLLVKKAESQPRSIKDCIQYSFENWVRSSPNHIALRFLD 1585
Cdd:PRK05691 2132 FDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAaaeQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAG 2211
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1586 RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVT 1665
Cdd:PRK05691 2212 QTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLS 2291
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1666 QTSLEEKLskSDLP-----YLCTDQSQDSEDYSLLTKDK-SYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEF 1739
Cdd:PRK05691 2292 DRALFEAL--GELPagvarWCLEDDAAALAAYSDAPLPFlSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF 2369
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1740 NITQETKVGQFATISFDASLWQILMALLAGA-------------TLCVVSREEQLS----TKALVKRFRDWNVTLADLPP 1802
Cdd:PRK05691 2370 GMRADDCELHFYSINFDAASERLLVPLLCGArvvlraqgqwgaeEICQLIREQQVSilgfTPSYGSQLAQWLAGQGEQLP 2449
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1803 VVLdsilpedipslqtVSTGGERCP------IKVAKRWSLdrnFYNVYGPTETTIATTWYRVssPECVQD---SVPIGTP 1873
Cdd:PRK05691 2450 VRM-------------CITGGEALTgehlqrIRQAFAPQL---FFNAYGPTETVVMPLACLA--PEQLEEgaaSVPIGRV 2511
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1874 VPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEE-ILYKTGDIGKVLHDGNLEHLGRLD 1952
Cdd:PRK05691 2512 VGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADGgRLYRTGDLVRLRADGLVEYVGRID 2591
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1953 HQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLgDNQNYHTLVAYVVPHGEWEEKKIIEELR--------SKLPEHMVPS 2024
Cdd:PRK05691 2592 HQVKIRGFRIELGEIESRLLEHPAVREAVVLAL-DTPSGKQLAGYLVSAVAGQDDEAQAALRealkahlkQQLPDYMVPA 2670
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2025 IFVQMEELPRLNNKKVDRHSLPTA-VHIFRQQkvIQKPVTEEEVVVAECWAETLNlpIDNIGLNSNFFELGGHSLTATQL 2103
Cdd:PRK05691 2671 HLILLDSLPLTANGKLDRRALPAPdPELNRQA--YQAPRSELEQQLAQIWREVLN--VERVGLGDNFFELGGDSILSIQV 2746
|
2170 2180
....*....|....*....|....*.
gi 497785100 2104 VARISELfEIELPIKAIFEYPTIQAI 2129
Cdd:PRK05691 2747 VSRARQL-GIHFSPRDLFQHQTVQTL 2771
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-2129 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1211.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 40 IPRHEERGSYPLSSIQKQIWFMSQLNPELPIYNEHLiKINLSGkVNIEALKKSFEQIVNRHQILRMR-VKQTE-DSIEQV 117
Cdd:PRK12316 1548 LPAGEIADIYPLSPMQQGMLFHSLYEQEAGDYINQL-RVDVQG-LDPDRFRAAWQATVDRHEILRSGfLWQDGlEQPLQV 1625
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 118 ITKsEPTIQFLSLRGISGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSE- 196
Cdd:PRK12316 1626 IHK-QVELPFAELDWRGREDLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEv 1704
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 197 LERFynmysqNGEINPEqsqeeLTIQYHDYALWqeklLTSENLEKGLEYWKEKL-EGDLPMLSIGGIT--QEGTGVGSEY 273
Cdd:PRK12316 1705 LQRY------AGQPVAA-----PGGRYRDYIAW----LQRQDAAASEAFWKEQLaALEEPTRLAQAARteDGQVGYGDHQ 1769
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 274 NFKIPNiLTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGR--NIRETRNVIGPFINTVVIRTKAEQN 351
Cdd:PRK12316 1770 QLLDPA-QTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRpaELPGIEQQIGLFINTLPVIAAPRPD 1848
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 352 LSVIEYLQQVHETTIQALENQDVPFEKVV-------EVLNPNRDVRANpfyqllFVMQEPPTQFSLPGIKVEyELIPTEV 424
Cdd:PRK12316 1849 QSVADWLQEVQALNLALREHEHTPLYDIQrwagqggEALFDSLLVFEN------YPVAEALKQGAPAGLVFG-RVSNHEQ 1921
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 425 ARFPLTLSIIEGEEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSPHQRIYDLNLLTSKERSESAYLYNQSGcKPFP 504
Cdd:PRK12316 1922 TNYPLTLAVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTP-EAYP 2000
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 505 TEP-IHVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAY 583
Cdd:PRK12316 2001 RGPgVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAY 2080
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 584 LPLDVESPKERIEIITQDSKLKAIITHSEYKTSYE-GYEVPILYIDQLDDfLLDEREDNLNVDCDSSQLAYGIYTSGSTG 662
Cdd:PRK12316 2081 VPLDPNYPAERLAYMLEDSGAALLLTQRHLLERLPlPAGVARLPLDRDAE-WADYPDTAPAVQLAGENLAYVIYTSGSTG 2159
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 663 IPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLffLLKEDAI-DPAKVEEIVQGKAI 741
Cdd:PRK12316 2160 LPKGVAVSHGALVAHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV--LIRDDELwDPEQLYDEMERHGV 2237
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 742 DWYKITPSHLKALSSES---GTKLFPRKgLILGGEASEWSWIKEIYRNIPAScKLFNHYGPSETTIGVAVYEVTKKGLSN 818
Cdd:PRK12316 2238 TILDFPPVYLQQLAEHAerdGRPPAVRV-YCFGGEAVPAASLRLAWEALRPV-YLFNGYGPTEAVVTPLLWKCRPQDPCG 2315
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 819 QFSTtPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPF-ITDSRMYKTGDIGKILYT 897
Cdd:PRK12316 2316 AAYV-PIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFsASGERLYRTGDLARYRAD 2394
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 898 GEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYV--SKKEVLDKDLQTYLKQKLPPNL 975
Cdd:PRK12316 2395 GVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVpdDAAEDLLAELRAWLAARLPAYM 2474
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 976 VPAYLVKMDTLPRHAHGKIDRKALPEIQVSNWNEIEIQPMNRLEEKMKDVWEKILERPVPSIDDSFFKLGGHSLLATRLV 1055
Cdd:PRK12316 2475 VPAHWVVLERLPLNPNGKLDRKALPKPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVV 2554
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1056 SMIRKEFKVELSIKEFFEKPSIRELSTHLLQLEAVSThfalSNISEAEKEKGIPLSDAQKRMWFLYRMESDSAYYNMPIS 1135
Cdd:PRK12316 2555 SRVRQDLGLEVPLRILFERPTLAAFAASLESGQTSRA----PVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSA 2630
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1136 LKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNiDPVQVVLKDLKCTINILDfDENRSEQDIMNYLTEKSMEPFKLET 1215
Cdd:PRK12316 2631 LHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGE-QTRQVILPNMSLRIVLED-CAGVADAAIRQRVAEEIQRPFDLAR 2708
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1216 GPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMPIQLEQPVYQYADYVNWQQNRYTEEQINQQ 1295
Cdd:PRK12316 2709 GPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWMDSGEGARQ 2788
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1296 LQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAVLIKEICEEAKVTPYTIFLTFFNILLYRYTYQDKILV 1375
Cdd:PRK12316 2789 LDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRV 2868
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1376 GTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGALENQDISFERIVQELNPERSLSYNPIYQVAF 1455
Cdd:PRK12316 2869 GVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMY 2948
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1456 TLQNDEQGKnGNYGGLSVEEFEIEWRTSKVDLTLIIGQSKRGFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENPNME 1535
Cdd:PRK12316 2949 NHQSGERAA-AQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRS 3027
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1536 ISRIQLVD-QQHDLLVK--KAESQPRSIKDCIQYSFENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRG 1612
Cdd:PRK12316 3028 VDELAMLDaEERGQLLEawNATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPD 3107
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1613 DRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQTSLEEKLSKSdLPYLCTDqsQDSEDY 1692
Cdd:PRK12316 3108 VLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQG-VQVLDLD--RGDENY 3184
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1693 SLLTKD-KSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGAT 1771
Cdd:PRK12316 3185 AEANPAiRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGAR 3264
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1772 LCVVSREEQLSTKALVKRFRDwnvTLADLPPVV-------LDSILPEDIPSLQTVSTGGERCPIKVAKRWSLDRNFYNVY 1844
Cdd:PRK12316 3265 VVLAGPEDWRDPALLVELINS---EGVDVLHAYpsmlqafLEEEDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLY 3341
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1845 GPTETTIATTWYRVSSPEcvQDSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPF 1924
Cdd:PRK12316 3342 GPTEATITVTHWQCVEEG--KDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF 3419
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1925 REEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQnyhtLVAYVVPHGEW 2004
Cdd:PRK12316 3420 VPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQ----LVAYVVPEDEA 3495
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2005 EE--KKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSLPtAVHIFRQQKVIQKPVTEEEVVVAECWAETLNLPid 2082
Cdd:PRK12316 3496 GDlrEALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALP-RPDAALLQQDYVAPVNELERRLAAIWADVLKLE-- 3572
|
2090 2100 2110 2120
....*....|....*....|....*....|....*....|....*..
gi 497785100 2083 NIGLNSNFFELGGHSLTATQLVARISELfEIELPIKAIFEYPTIQAI 2129
Cdd:PRK12316 3573 QVGLTDNFFELGGDSIISLQVVSRARQA-GIRFTPKDLFQHQTIQGL 3618
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1108-2135 |
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: 928.11 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1108 IPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNIDPVQVVLKDLK--CTI 1185
Cdd:COG1020 18 LPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAplPVV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1186 NILDFDENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNM 1265
Cdd:COG1020 98 VLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1266 PIQLEQPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAVLIKEIC 1345
Cdd:COG1020 178 PLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALA 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1346 EEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGAL 1425
Cdd:COG1020 258 RRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1426 ENQDISFERIVQELNPERSLSYNPIYQVAFTLQNDEQGKnGNYGGLSVEEFEIEWRTSKVDLTLIIGQSKRGFEMVMEYN 1505
Cdd:COG1020 338 AHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADE-LELPGLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYN 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1506 TDLFRQQSIEQMLSDYIKIISQVIENPNMEISRIQLVD--QQHDLLVKKAESQ-PRSIKDCIQYSFENWVRSSPNHIALR 1582
Cdd:COG1020 417 TDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTaaERQQLLAEWNATAaPYPADATLHELFEAQAARTPDAVAVV 496
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1583 FLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGA 1662
Cdd:COG1020 497 FGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARL 576
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1663 IVTQTSLEEKLSKSDLPYLCTDQSQDSEDYSLLTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNIT 1742
Cdd:COG1020 577 VLTQSALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLG 656
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1743 QETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSIL---PEDIPSLQTV 1819
Cdd:COG1020 657 PGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRALLdaaPEALPSLRLV 736
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1820 STGGERCPIKVAKRW---SLDRNFYNVYGPTETTIATTWYRVSSPECVQDSVPIGTPVPNTEVFILDPDLNPVPMGVIGE 1896
Cdd:COG1020 737 LVGGEALPPELVRRWrarLPGARLVNLYGPTETTVDSTYYEVTPPDADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGE 816
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1897 IYIGGVGVSNGYLNRDDLNEKRFIPHPFREE-EILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQT 1975
Cdd:COG1020 817 LYIGGAGLARGYLNRPELTAERFVADPFGFPgARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHP 896
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1976 GVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIE--ELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSLPTAVHIFR 2053
Cdd:COG1020 897 GVREAVVVAREDAPGDKRLVAYVVPEAGAAAAAALLrlALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAA 976
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2054 QQKVIQKPVTEEEVVvaecWAETLNLPIDNIGLNSNFFELGGHSLTATQLVARISELFEIELPIKAIFEYPTIQAILDFI 2133
Cdd:COG1020 977 AAAAAPPAEEEEEEA----ALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAA 1052
|
..
gi 497785100 2134 VE 2135
Cdd:COG1020 1053 AA 1054
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
40-1319 |
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: 838.74 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 40 IPRHEERGSYPLSSIQKQIWFMSQLNPELPIYNEHLIkINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVI- 118
Cdd:COG1020 9 LPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALA-LLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIq 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 119 TKSEPTIQFLSLRGISGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELE 198
Cdd:COG1020 88 PVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELL 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 199 RFYNMYSQNgeinPEQSQEELTIQYHDYALWQEKLLTSENLEKGLEYWKEKLEGDLPMLSI---GGITQEGTGVGSEYNF 275
Cdd:COG1020 168 RLYLAAYAG----APLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELptdRPRPAVQSYRGARVSF 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 276 KIPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVI 355
Cdd:COG1020 244 RLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFA 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 356 EYLQQVHETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLFVMQE-PPTQFSLPGIKVEYELIPTEVARFPLTLSII 434
Cdd:COG1020 324 ELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNaPADELELPGLTLEPLELDSGTAKFDLTLTVV 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 435 E-GEEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSPHQRIYDLNLLTSKERSESAYLYNQSGcKPFPTE-PIHVQF 512
Cdd:COG1020 404 EtGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATA-APYPADaTLHELF 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 513 EGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPK 592
Cdd:COG1020 483 EAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPA 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 593 ERIEIITQDSKLKAIITHSEYKTSYEGYEVPILYIDQLDdfLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHR 672
Cdd:COG1020 563 ERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDALA--LAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHR 640
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 673 NLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLK 752
Cdd:COG1020 641 ALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLR 720
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 753 ALSSESGTKLFPRKGLILGGEASEWSWIKEIYRNIPAsCKLFNHYGPSETTIGVAVYEVTKKGLSNqfSTTPIGSSLSNN 832
Cdd:COG1020 721 ALLDAAPEALPSLRLVLVGGEALPPELVRRWRARLPG-ARLVNLYGPTETTVDSTYYEVTPPDADG--GSVPIGRPIANT 797
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 833 RIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPF-ITDSRMYKTGDIGKILYTGEIQFLGRLDGQVK 911
Cdd:COG1020 798 RVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFgFPGARLYRTGDLARWLPDGNLEFLGRADDQVK 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 912 IRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYV---SKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPR 988
Cdd:COG1020 878 IRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVvpeAGAAAAAALLRLALALLLPPYMVPAAVVLLLPLPL 957
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 989 HAHGKIDRKALPEIQVSNwNEIEIQPMNRLEEKMKDVWEKILERPVPSIDDSFFKLGGHSLLATRLVSMIRKEFKVELSI 1068
Cdd:COG1020 958 TGNGKLDRLALPAPAAAA-AAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLL 1036
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1069 KEFFEkpsiRELSTHLLQLEAVSTHFALSNISEAEKEKGIPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFT 1148
Cdd:COG1020 1037 LLLFL----AAAAAAAAAAAAAAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALL 1112
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1149 ESIQEVNKRHDSLRTVFRESKNIDPVQVVLKDLKCTINILDFDENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNP 1228
Cdd:COG1020 1113 LLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLL 1192
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1229 NEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMPIQLEQPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAPS 1308
Cdd:COG1020 1193 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALL 1272
|
1290
....*....|.
gi 497785100 1309 LLELPLDKPRP 1319
Cdd:COG1020 1273 LLALALLLPAL 1283
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
4-1337 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 784.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 4 LRKRLESLTPEQRDMVLKKLKNKRENHYLSN--GGRHVIPRHeergsyPLSSIQKQIWFMSQLNPELPIYNEHLIkINLS 81
Cdd:PRK12316 9 LARRFIELPLEKRRVFLATLRGEGVDFSLFPipAGVSSAERD------RLSYAQQRMWFLWQLEPQSGAYNLPSA-VRLN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 82 GKVNIEALKKSFEQIVNRHQILRMR-VKQTEDSIEQVITKSEPTIQFLSLRGISGEEQQEILSEYCRKEANYPYRLEQEN 160
Cdd:PRK12316 82 GPLDRQALERAFASLVQRHETLRTVfPRGADDSLAQVPLDRPLEVEFEDCSGLPEAEQEARLRDEAQRESLQPFDLCEGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 161 LIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYSQNGEinPEQsqEELTIQYHDYALWQEKLLTSENLE 240
Cdd:PRK12316 162 LLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAE--PGL--PALPIQYADYALWQRSWLEAGEQE 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 241 KGLEYWKEKLEGDLPMLSIGgITQEGTGV----GSEYNFKIPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETD 316
Cdd:PRK12316 238 RQLEYWRAQLGEEHPVLELP-TDHPRPAVpsyrGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTD 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 317 LAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVIEYLQQVHETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQ 396
Cdd:PRK12316 317 IRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQ 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 397 LLFVMQ----EPPTQFSLPGIKVEYELIPTEVARFPLTLSIIE-GEEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQ 471
Cdd:PRK12316 397 VMYNHQplvaDIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEkGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVE 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 472 SPHQRIYDLNLLTSKERSESAYLYNQSGCKpFPTEP-IHVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQK 550
Cdd:PRK12316 477 NPQARVDELPMLDAEERGQLVEGWNATAAE-YPLQRgVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIE 555
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 551 QGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIIT--HSEYKTSYEGyEVPILYID 628
Cdd:PRK12316 556 RGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSqsHLGRKLPLAA-GVQVLDLD 634
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 629 QLDDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTI 708
Cdd:PRK12316 635 RPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEF 714
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 709 YTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSESG-TKLFPRKGLILGGEASEWSWIKEIYRNI 787
Cdd:PRK12316 715 FWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDEDvASCTSLRRIVCSGEALPADAQEQVFAKL 794
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 788 PaSCKLFNHYGPSETTIGVAVYEVTKKGLSnqfsTTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNRE 867
Cdd:PRK12316 795 P-QAGLYNLYGPTEAAIDVTHWTCVEEGGD----SVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRP 869
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 868 ELTAERFMEDPFITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTkvrNEEQ 947
Cdd:PRK12316 870 GLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAV---DGKQ 946
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 948 LVAYYVSKKE--VLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEIQVSNWNEIEIQPMNRLEEKMKDV 1025
Cdd:PRK12316 947 LVGYVVLESEggDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEASVAQQGYVAPRNALERTLAAI 1026
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1026 WEKILERPVPSIDDSFFKLGGHSLLATRLVSMIRKEfKVELSIKEFFEKPSIRelsthllQLEAVSTHFALSNISEAEKE 1105
Cdd:PRK12316 1027 WQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIR-------SLALVAKAGQATAADQGPAS 1098
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1106 KGIPLSDAQKrmWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESkniDPVQVVLKDLKCTI 1185
Cdd:PRK12316 1099 GEVALAPVQR--WFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREE---DGGWQQAYAAPQAG 1173
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1186 NILDFDENRSEQDIMNyLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNM 1265
Cdd:PRK12316 1174 EVLWQRQAASEEELLA-LCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADL 1252
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497785100 1266 PIQLeqpvyqyADYVNW--QQNRYTEEQInQQLQYWKEQLSGAPSllELPLDKPRPSMQSYNGSLIRMKLPEKH 1337
Cdd:PRK12316 1253 PART-------SSYQAWarRLHEHAGARA-EELDYWQAQLEDAPH--ELPCENPDGALENRHERKLELRLDAER 1316
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1069-2129 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 774.52 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1069 KEFFEKP-SIRELSTHLLQLEAVSthFALSNI----SEAEKEkgiPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLD 1143
Cdd:PRK12316 11 RRFIELPlEKRRVFLATLRGEGVD--FSLFPIpagvSSAERD---RLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1144 YRAFTESIQEVNKRHDSLRTVFRESKNiDPVQVVLKDLKCTINILDF---DENRSEQDIMNYLTEKSMEPFKLETGPLIR 1220
Cdd:PRK12316 86 RQALERAFASLVQRHETLRTVFPRGAD-DSLAQVPLDRPLEVEFEDCsglPEAEQEARLRDEAQRESLQPFDLCEGPLLR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1221 VHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMPIQLEQPVYQYADYVNWQQnRYTE--EQiNQQLQY 1298
Cdd:PRK12316 165 VRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYATGAEPGLPALPIQYADYALWQR-SWLEagEQ-ERQLEY 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1299 WKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAVLIKEICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTP 1378
Cdd:PRK12316 243 WRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1379 IANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGALENQDISFERIVQELNPERSLSYNPIYQVAFTLQ 1458
Cdd:PRK12316 323 IANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNHQ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1459 ND--EQGKNGNYGGLSVEEFEIEWRTSKVDLTLIIGQSKRGFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENPNMEI 1536
Cdd:PRK12316 403 PLvaDIEALDTVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARV 482
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1537 SRIQLVD-QQHDLLVKKAESQPRS--IKDCIQYSFENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGD 1613
Cdd:PRK12316 483 DELPMLDaEERGQLVEGWNATAAEypLQRGVHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDV 562
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1614 RVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQTSLEEKLS-KSDLPYLCTDQ-SQDSED 1691
Cdd:PRK12316 563 LVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPlAAGVQVLDLDRpAAWLEG 642
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1692 YSLLTKDKS-YPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGA 1770
Cdd:PRK12316 643 YSEENPGTElNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVGDTVLQKTPFSFDVSVWEFFWPLMSGA 722
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1771 TLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSILPE----DIPSLQTVSTGGERCPIKV-----AKRWSldRNFY 1841
Cdd:PRK12316 723 RLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFLQDedvaSCTSLRRIVCSGEALPADAqeqvfAKLPQ--AGLY 800
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1842 NVYGPTETTI-ATTWYRVSSpecVQDSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFI 1920
Cdd:PRK12316 801 NLYGPTEAAIdVTHWTCVEE---GGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFV 877
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1921 PHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQnyhtLVAYVVP 2000
Cdd:PRK12316 878 PSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDGKQ----LVGYVVL 953
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2001 H--GEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSLPtAVHIFRQQKVIQKPVTEEEVVVAECWAETLN 2078
Cdd:PRK12316 954 EseGGDWREALKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALP-APEASVAQQGYVAPRNALERTLAAIWQDVLG 1032
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|.
gi 497785100 2079 lpIDNIGLNSNFFELGGHSLTATQLVARISELfEIELPIKAIFEYPTIQAI 2129
Cdd:PRK12316 1033 --VERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQTIRSL 1080
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
40-1322 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 765.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 40 IPRHEERGSYPLSSIQKQIWFMSQLNPELPIYNehlI--KINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQV 117
Cdd:PRK12467 1108 LPDVDRDQPLPLSYAQERQWFLWQLEPGSAAYH---IpqALRLKGPLDIEALERSFDALVARHESLRTTFVQEDGRTRQV 1184
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 118 ITKSEPTIQFLSLRGISGEEQQEILSeYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSEL 197
Cdd:PRK12467 1185 IHPVGSLTLEEPLLLAADKDEAQLKV-YVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSMQVLVDEL 1263
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 198 ERFYNMYSQNGEInpeqSQEELTIQYHDYALWQEKLLTSENLEKGLEYWKEKLEGDLPMLSIGG---ITQEGTGVGSEYN 274
Cdd:PRK12467 1264 VALYAAYSQGQSL----QLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTdrpRPAVQSHRGARLA 1339
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 275 FKIPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSV 354
Cdd:PRK12467 1340 FELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQASF 1419
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 355 IEYLQQVHETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLFVMQEPPTQF--SLPGIKVEYELIPTEVARFPLTLS 432
Cdd:PRK12467 1420 QQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAqaQLPGLSVESLSWESQTAQFDLTLD 1499
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 433 IIEGEEMIGRVL-YRTSILSEYEVQSFVQRLLQVADEIVQSPHQRIYDLNLLTSKERSESAYLYNQSGCKPFPTEPIHVQ 511
Cdd:PRK12467 1500 TYESSEGLQASLtYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLVHQL 1579
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESP 591
Cdd:PRK12467 1580 IEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYP 1659
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 592 KERIEIITQDSKLKAIITHSEYKTSYE-GYEVPILYIDQLDDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVE 670
Cdd:PRK12467 1660 RERLAYMIEDSGIELLLTQSHLQARLPlPDGLRSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNR 1739
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 671 HRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSH 750
Cdd:PRK12467 1740 HGALVNRLCATQEAYQLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPPGAHRDPEQLIQLIERQQVTTLHFVPSM 1819
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 751 LKALSSESGTKLFPRK--GLILGGEASEWSWIKEIYRNIPAScKLFNHYGPSETTIGVAVYEVTKKGLSNQFSTtPIGSS 828
Cdd:PRK12467 1820 LQQLLQMDEQVEHPLSlrRVVCGGEALEVEALRPWLERLPDT-GLFNLYGPTETAVDVTHWTCRRKDLEGRDSV-PIGQP 1897
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 829 LSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPF-ITDSRMYKTGDIGKILYTGEIQFLGRLD 907
Cdd:PRK12467 1898 IANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFgTVGSRLYRTGDLARYRADGVIEYLGRID 1977
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 908 GQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYVSK-KEVLDKD---------LQTYLKQKLPPNLVP 977
Cdd:PRK12467 1978 HQVKIRGFRIELGEIEARLREQGGVREAVVIAQDGANGKQLVAYVVPTdPGLVDDDeaqvalraiLKNHLKASLPEYMVP 2057
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 978 AYLVKMDTLPRHAHGKIDRKALPEIQVSNWNEIEIQPMNRLEEKMKDVWEKILERPVPSIDDSFFKLGGHSLLATRLVSM 1057
Cdd:PRK12467 2058 AHLVFLARMPLTPNGKLDRKALPAPDASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSR 2137
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1058 IRKEfKVELSIKEFFEKPSIRELSThllqleAVSTHFALSNISEAEKEKGIPLSDAQkRMWFlyrmESDSA---YYNMPI 1134
Cdd:PRK12467 2138 ARQA-GIRFTPKDLFQHQTVQSLAA------VAQEGDGTVSIDQGPVTGDLPLLPIQ-QMFF----ADDIPerhHWNQSV 2205
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1135 SLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRE-----SKNIDPVQVVLKDLKCTINILDFDENRSeqdimnyLTEKSME 1209
Cdd:PRK12467 2206 LLEPREALDAELLEAALQALLVHHDALRLGFVQedggwSAMHRAPEQERRPLLWQVVVADKEELEA-------LCEQAQR 2278
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1210 PFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMPIQLEQPVYQYADYVNWQQNRYTE 1289
Cdd:PRK12467 2279 SLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVDGVSWRILLEDLQTAYRQLQGGQPVKLPAKTSAFKAWAERLQTYAAS 2358
|
1290 1300 1310
....*....|....*....|....*....|...
gi 497785100 1290 EQINQQLQYWKEQLSGAPSllELPLDKPRPSMQ 1322
Cdd:PRK12467 2359 AALADELGYWQAQLQGAST--ELPCDHPQGGLQ 2389
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
519-2122 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 738.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIAL------SDHERSYTYLQTNNRANQIARWLQKQGigkedfigiqlQPCAKAII----------AMLGVLKAG-- 580
Cdd:PRK05691 22 TPDRLALrfladdPGEGVVLSYRDLDLRARTIAAALQARA-----------SFGDRAVLlfpsgpdyvaAFFGCLYAGvi 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 581 --GAYLPldvESPK----ERIEIITQDSKLKAIITHSEYKTSYEGYEV-------PILYIDQLDDFLLDE-REDNLNVDc 646
Cdd:PRK05691 91 avPAYPP---ESARrhhqERLLSIIADAEPRLLLTVADLRDSLLQMEElaaanapELLCVDTLDPALAEAwQEPALQPD- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 647 dssQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLG--NKPKDRYLLLQSLAYDF-----CLTTIYTS----LLSG 715
Cdd:PRK05691 167 ---DIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGidLNPDDVIVSWLPLYHDMgliggLLQPIFSGvpcvLMSP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 716 GtlFFLLKedaidPAKVEEivqgkAIDWYKIT----PSHLKALSSE--SGTKLfprKGLILGGEASEWSWIKEI------ 783
Cdd:PRK05691 244 A--YFLER-----PLRWLE-----AISEYGGTisggPDFAYRLCSErvSESAL---ERLDLSRWRVAYSGSEPIrqdsle 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 784 -YRNIPASC-----KLFNHYGPSETTI---------GVAVYEVTKKGLSNQFSTTPIGSSL-------SNNRIYILD-DK 840
Cdd:PRK05691 309 rFAEKFAACgfdpdSFFASYGLAEATLfvsggrrgqGIPALELDAEALARNRAEPGTGSVLmscgrsqPGHAVLIVDpQS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 841 LRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEdpfiTDSRMY-KTGDIGkILYTGEIQFLGRLDGQVKIRGIRVEP 919
Cdd:PRK05691 389 LEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE----HDGRTWlRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYP 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 920 EEIQSQLLSHPSITE----AIVTVTKVRNEEQLVAYYVSK---KEVLDKDLQTYLKQKLP------PNLVpaYLVKMDTL 986
Cdd:PRK05691 464 QDIEKTVEREVEVVRkgrvAAFAVNHQGEEGIGIAAEISRsvqKILPPQALIKSIRQAVAeacqeaPSVV--LLLNPGAL 541
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 987 PRHAHGKIDRKA---------------LPEIQVSNWNEIEIQPmNRLEEKMKDVWEKILERPVPSIDDSFFKLGGHSLLA 1051
Cdd:PRK05691 542 PKTSSGKLQRSAcrlrladgsldsyalFPALQAVEAAQTAASG-DELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIAA 620
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1052 TRLVSMIRKEFKVELSIKEFFEKPSIRELSTHLLQLEAVSTHfALSNISEAEKEKGIPLSDAQKRMWFLYRMESDSAYYN 1131
Cdd:PRK05691 621 TQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGA-AQAAIARLPRGQALPQSLAQNRLWLLWQLDPQSAAYN 699
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1132 MPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNIdPVQVVLKDLKCTINILDFD---ENRSEQDIMNYLTEKSM 1208
Cdd:PRK05691 700 IPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGV-ALQRIDAQGEFALQRIDLSdlpEAEREARAAQIREEEAR 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1209 EPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMPIQLEQPVYQYADYVNWQQNRYT 1288
Cdd:PRK05691 779 QPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLA 858
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1289 EEQINQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAVLIKEICEEAKVTPYTIFLTFFNILLYRYT 1368
Cdd:PRK05691 859 QGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYS 938
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1369 YQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGALENQDISFERIVQELNPERSlsyN 1448
Cdd:PRK05691 939 GQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQARE---Q 1015
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1449 PIYQVAFTLQNDEQGKNGNYGGLSVEEFEIEWRTSKVDLTLIIGQSKRG-FEMVMEYNTDLFRQQSIEQMLSDYIKIISQ 1527
Cdd:PRK05691 1016 GLFQVMFNHQQRDLSALRRLPGLLAEELPWHSREAKFDLQLHSEEDRNGrLTLSFDYAAELFDAATIERLAEHFLALLEQ 1095
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1528 VIENPNMEISRIQLVD-----QQHDLLVKKAESQPRSIKDCIqysfENWVRSSPNHIALRFLDRSYTYDEVNKRANKIAN 1602
Cdd:PRK05691 1096 VCEDPQRALGDVQLLDaaeraQLAQWGQAPCAPAQAWLPELL----NEQARQTPERIALVWDGGSLDYAELHAQANRLAH 1171
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1603 QLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQTSLEEKLSKSD-LPYL 1681
Cdd:PRK05691 1172 YLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLLERLPQAEgVSAI 1251
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1682 CTDQsqdsedyslLTKDkSYP----------EDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFA 1751
Cdd:PRK05691 1252 ALDS---------LHLD-SWPsqapglhlhgDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALDDSDVLMQKA 1321
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1752 TISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVT-LADLPP---VVLDSILPEDIPSLQTVSTGGERCP 1827
Cdd:PRK05691 1322 PISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTtLHFVPPllqLFIDEPLAAACTSLRRLFSGGEALP 1401
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1828 IKVAKRwSLDR----NFYNVYGPTETTIATTWYRVSSPEcvQDSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVG 1903
Cdd:PRK05691 1402 AELRNR-VLQRlpqvQLHNRYGPTETAINVTHWQCQAED--GERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAG 1478
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1904 VSNGYLNRDDLNEKRFIPHPFREE-EILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIV 1982
Cdd:PRK05691 1479 LARGYLGRPALTAERFVPDPLGEDgARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGVAQAAV 1558
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1983 QpLGDNQNYHTLVAYVVPHGEWEEKKI--IEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSLPTAVHifrQQKVIQK 2060
Cdd:PRK05691 1559 L-VREGAAGAQLVGYYTGEAGQEAEAErlKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVW---QQREHVE 1634
|
1690 1700 1710 1720 1730 1740
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497785100 2061 PVTEEEVVVAECWAETLNLPidNIGLNSNFFELGGHSLTATQLVARISELFEIELPIKAIFE 2122
Cdd:PRK05691 1635 PRTELQQQIAAIWREVLGLP--RVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFE 1694
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
50-1375 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 708.65 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 50 PLSSIQKQIWFMSQLNPELPIYNEHLIkINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVITKSEPTIQFLS 129
Cdd:PRK12316 2604 PLSHAQQRQWFLWQLEPESAAYHLPSA-LHLRGVLDQAALEQAFDALVLRHETLRTRFVEVGEQTRQVILPNMSLRIVLE 2682
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 130 LRGISGEEQQEilsEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYSQNGE 209
Cdd:PRK12316 2683 DCAGVADAAIR---QRVAEEIQRPFDLARGPLLRVRLLALDGQEHVLVITQHHIVSDGWSMQVMVDELVQAYAGARRGEQ 2759
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 210 InpeqSQEELTIQYHDYALWQEKLLTSENLEKGLEYWKEKLEGDLPMLSIGGITQEG---TGVGSEYNFKIPNILTDKLR 286
Cdd:PRK12316 2760 P----TLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPalqSHRGARLDVALDVALSRELL 2835
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 287 KLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVIEYLQQVHETTI 366
Cdd:PRK12316 2836 ALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQVDAQLAFRDLLGQVKEQAL 2915
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 367 QALENQDVPFEKVVEVLNPNRDVRANPFYQLLFVMQEPP-TQFSLPGIKVEYELIPTEVARFPLTLSIIEGEEMIGRVL- 444
Cdd:PRK12316 2916 GAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGErAAAQLPGLHIESFAWDGAATQFDLALDTWESAEGLGASLt 2995
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 445 YRTSILSEYEVQSFVQRLLQVADEIVQSPHQRIYDLNLLTSKERSESAYLYNQSGCKPFPTEPIHVQFEGQVLNTPNSIA 524
Cdd:PRK12316 2996 YATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERGVHRLFEEQVERTPDAVA 3075
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 525 LSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKL 604
Cdd:PRK12316 3076 LAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGA 3155
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 605 KAIITHSEYKTSYEGyEVPILYIDQLDDfllDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTK 684
Cdd:PRK12316 3156 QLLLSQSHLRLPLAQ-GVQVLDLDRGDE---NYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQA 3231
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 685 LGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHL-KALSSESGTKLF 763
Cdd:PRK12316 3232 YGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEGVDVLHAYPSMLqAFLEEEDAHRCT 3311
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 764 PRKGLILGGEAsewsWIKEIYRNIPASCKLFNHYGPSETTIGVAVYEVTKKGLsnqfSTTPIGSSLSNNRIYILDDKLRP 843
Cdd:PRK12316 3312 SLKRIVCGGEA----LPADLQQQVFAGLPLYNLYGPTEATITVTHWQCVEEGK----DAVPIGRPIANRACYILDGSLEP 3383
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 844 VPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQ 923
Cdd:PRK12316 3384 VPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIE 3463
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 924 SQLLSHPSITEAIVTVTkvrNEEQLVAYYVSKKEV--LDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPE 1001
Cdd:PRK12316 3464 ARLLEHPWVREAVVLAV---DGRQLVAYVVPEDEAgdLREALKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPR 3540
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1002 IQVSNWNEIEIQPMNRLEEKMKDVWEKILERPVPSIDDSFFKLGGHSLLATRLVSMIRKEfKVELSIKEFFEKPSIRELS 1081
Cdd:PRK12316 3541 PDAALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRARQA-GIRFTPKDLFQHQTIQGLA 3619
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1082 T-------HLLQLEAVSTHFALSNISEAEKEKGIPlsdaQKRMWFLYRMesdsayynmpisLKIIGDLDYRAFTESIQEV 1154
Cdd:PRK12316 3620 RvarvgggVAVDQGPVSGETLLLPIQQQFFEEPVP----ERHHWNQSLL------------LKPREALDAAALEAALQAL 3683
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1155 NKRHDSLRTVFRESKNIDPVQVVLKDLKctiNILDFDENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLL 1234
Cdd:PRK12316 3684 VEHHDALRLRFVEDAGGWTAEHLPVELG---GALLWRAELDDAEELERLGEEAQRSLDLADGPLLRALLATLADGSQRLL 3760
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1235 IVQHHIISDGWSLRIMMDELFAIYHQIISNMPIQLEQPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAPSllELPL 1314
Cdd:PRK12316 3761 LVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGVSS--ELPC 3838
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 1315 DKPRPSMQSYNGSLIRMKLpekHAVLIKEICEEAKVTPYT----IFLTFFNILLYRYTYQDKILV 1375
Cdd:PRK12316 3839 DHPQGALQNRHAASVQTRL---DRELTRRLLQQAPAAYRTqvndLLLTALARVVCRWTGEASALV 3900
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
40-1375 |
6.71e-180 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 613.71 E-value: 6.71e-180
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 40 IPRHEERGSYPLSSIQKQIWFMSQLNPELPIYNEHLIKiNLSGKVNIEALKKSFEQIVNRHQILRMrvkqTEDSI----- 114
Cdd:PRK05691 1720 IARVDRSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMA-RLSGVLDVDRFEAALQALILRHETLRT----TFPSVdgvpv 1794
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 115 EQVITKSEPTIQFLSLRGISGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILL 194
Cdd:PRK05691 1795 QQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPFDLERGPLLRACLVKAAEREHYFVLTLHHIVTEGWAMDIFA 1874
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 195 SELERFYNMYSQNgeinPEQSQEELTIQYHDYALWQEKLLTSENLEKGLEYWKEKLEGDLPMLSIGG-----ITQegTGV 269
Cdd:PRK05691 1875 RELGALYEAFLDD----RESPLEPLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELPAdrprpPVQ--SHR 1948
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 270 GSEYNFKIPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRnIR-ETRNVIGPFINTVVIRTKA 348
Cdd:PRK05691 1949 GELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANR-IRpESEGLIGAFLNTQVLRCQL 2027
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 349 EQNLSVIEYLQQVHETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLFVMQEPPTQFS--LPGIKVEYELIPTEVAR 426
Cdd:PRK05691 2028 DGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQRWEFQQSrqLAGMTVEYLVNDARATK 2107
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 427 FPLTLSIIEGEEMIGRVL-YRTSILSEYEVQSFVQRLLQVADEIVQSPHQRIYDLNLLTSKERSESAYLYNQSGCKPFPT 505
Cdd:PRK05691 2108 FDLNLEVTDLDGRLGCCLtYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARLD 2187
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 506 EPIHVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLP 585
Cdd:PRK05691 2188 QTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVP 2267
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 586 LDVESPKERIEIITQDSKLKAIITHSEYKTSYEgyEVPI------LYIDQ--LDDFLLDEReDNLNVdcdSSQLAYGIYT 657
Cdd:PRK05691 2268 LDPEYPLERLHYMIEDSGIGLLLSDRALFEALG--ELPAgvarwcLEDDAaaLAAYSDAPL-PFLSL---PQHQAYLIYT 2341
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 658 SGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFfLLKEDAIDPAKVEEIVQ 737
Cdd:PRK05691 2342 SGSTGKPKGVVVSHGEIAMHCQAVIERFGMRADDCELHFYSINFDAASERLLVPLLCGARVV-LRAQGQWGAEEICQLIR 2420
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 738 GKAIDWYKITPSHLKALSSESGTK--LFPRKGLILGGEA---SEWSWIKEIYRniPASckLFNHYGPSETTIgVAVYEVT 812
Cdd:PRK05691 2421 EQQVSILGFTPSYGSQLAQWLAGQgeQLPVRMCITGGEAltgEHLQRIRQAFA--PQL--FFNAYGPTETVV-MPLACLA 2495
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 813 KKGLSNQFSTTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDS-RMYKTGDI 891
Cdd:PRK05691 2496 PEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADGgRLYRTGDL 2575
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 892 GKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYVSKKEVLDKD--------L 963
Cdd:PRK05691 2576 VRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEaqaalreaL 2655
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 964 QTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEIQVSNWNEIEIQPMNRLEEKMKDVWEKILERPVPSIDDSFFK 1043
Cdd:PRK05691 2656 KAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDPELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFE 2735
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1044 LGGHSLLATRLVSMIRkEFKVELSIKEFFEKPSIRELSthllqleAVSTHFALSNISEAEKEKGIPLSDAQKrmWFLYRM 1123
Cdd:PRK05691 2736 LGGDSILSIQVVSRAR-QLGIHFSPRDLFQHQTVQTLA-------AVATHSEAAQAEQGPLQGASGLTPIQH--WFFDSP 2805
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1124 ESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESK---NIDPVQVVLKDLKCTINILDFDENRSeqdim 1200
Cdd:PRK05691 2806 VPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQADgrwQAEYRAVTAQELLWQVTVADFAECAA----- 2880
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1201 nyLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMPIQLEQPVYQYADYV 1280
Cdd:PRK05691 2881 --LFADAQRSLDLQQGPLLRALLVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWA 2958
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1281 NWQQNRYTEEQINQQLQYWKEQLSGAPSllELPLDKPRPSMQSYNGSLIRMKL-PEKHAVLIKEICEEAKVTPYTIFLTF 1359
Cdd:PRK05691 2959 ARLQAYAGSESLREELGWWQAQLGGPRA--ELPCDRPQGGNLNRHAQTVSVRLdAERTRQLLQQAPAAYRTQVNDLLLTA 3036
|
1370
....*....|....*.
gi 497785100 1360 FNILLYRYTYQDKILV 1375
Cdd:PRK05691 3037 LARVLCRWSGQPSVLV 3052
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1065-2130 |
7.15e-179 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 610.81 E-value: 7.15e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1065 ELSI-----KEFFEKPSIRELS-THLLQLEAVSTH-------------FALSNISEA----------EKEKGIPLSDAQK 1115
Cdd:PRK12316 4031 ELSLdwtfsREMFEEATIQRLAdDYAAELTALVEHccdaerhgvtpsdFPLAGLDQArldalplplgEIEDIYPLSPMQQ 4110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1116 RMWFLYRMESDSAYYNMPISLKIIGdLDYRAFTESIQEVNKRHDSLRTVFRESKNID-PVQVVLKDLKCTINILDFDENR 1194
Cdd:PRK12316 4111 GMLFHSLYEQEAGDYINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVWQGELGrPLQVVHKQVSLPFAELDWRGRA 4189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1195 SEQDIMNYLTEKSME-PFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIisnmpiQLEQPV 1273
Cdd:PRK12316 4190 DLQAALDALAAAERErGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGEVLERYSGR------PPAQPG 4263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1274 YQYADYVNW--QQNRYTEEQinqqlqYWKEQLSG--APSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAVLiKEICEEAK 1349
Cdd:PRK12316 4264 GRYRDYIAWlqRQDAAASEA------FWREQLAAldEPTRLAQAIARADLRSANGYGEHVRELDATATARL-REFARTQR 4336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1350 VTPYTIFLTFFNILLYRYTYQDKILVGTPIANR--NIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGALEN 1427
Cdd:PRK12316 4337 VTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRpaELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREH 4416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1428 QDISFErivqELNPERSLSYNPIYQVAFTLQN---DEQGKNGNYGGLSVEEFEIEWRTS-KVDLTLIIGQSkrgFEMVME 1503
Cdd:PRK12316 4417 EHTPLY----EIQRWAGQGGEALFDSLLVFENypvSEALQQGAPGGLRFGEVTNHEQTNyPLTLAVGLGET---LSLQFS 4489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1504 YNTDLFRQQSIEQMLSDYIKIISQVIENPNMEISRIQLVD---QQHDLLVKKAESQPRSIKDCIQYSFENWVRSSPNHIA 1580
Cdd:PRK12316 4490 YDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEkaeQQRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVA 4569
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1581 LRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASV 1660
Cdd:PRK12316 4570 VVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGA 4649
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1661 GAIVTQTSLEEKLSKSD-LPYLCTDQSQDSEDYSLLT-KDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDE 1738
Cdd:PRK12316 4650 ALLLTQSHLLQRLPIPDgLASLALDRDEDWEGFPAHDpAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGER 4729
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1739 FNITQETKVGQFATISFDASLWQILMALLAGAtlCVVSREEQL----STKALVKRFRdwnVTLADLPPVVLDSILPE--- 1811
Cdd:PRK12316 4730 YELTPDDRVLQFMSFSFDGSHEGLYHPLINGA--SVVIRDDSLwdpeRLYAEIHEHR---VTVLVFPPVYLQQLAEHaer 4804
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1812 --DIPSLQTVSTGGERCPIKVAKRW--SL-DRNFYNVYGPTETTI-ATTWYRVSSPECVQDSVPIGTPVPNTEVFILDPD 1885
Cdd:PRK12316 4805 dgEPPSLRVYCFGGEAVAQASYDLAwrALkPVYLFNGYGPTETTVtVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQ 4884
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1886 LNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREE-EILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIEL 1964
Cdd:PRK12316 4885 LNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPgGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIEL 4964
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1965 GEIESLLNLQTGVKEAIV----QPLGDNqnyhtLVAYVVPHGEWEEKKIIEE----------LRSKLPEHMVPSIFVQME 2030
Cdd:PRK12316 4965 GEIEARLREHPAVREAVViaqeGAVGKQ-----LVGYVVPQDPALADADEAQaelrdelkaaLRERLPEYMVPAHLVFLA 5039
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2031 ELPRLNNKKVDRHSLPtAVHIFRQQKVIQKPVTEEEVVVAECWAETLNLPidNIGLNSNFFELGGHSLTATQLVARISEL 2110
Cdd:PRK12316 5040 RMPLTPNGKLDRKALP-QPDASLLQQAYVAPRSELEQQVAAIWAEVLQLE--RVGLDDNFFELGGHSLLAIQVTSRIQLE 5116
|
1130 1140
....*....|....*....|
gi 497785100 2111 FEIELPIKAIFEYPTIQAIL 2130
Cdd:PRK12316 5117 LGLELPLRELFQTPTLAAFV 5136
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1576-2045 |
2.72e-178 |
|
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: 550.21 E-value: 2.72e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQtsleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISAT 1735
Cdd:cd05930 81 EDSGAKLVLTD-----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1736 IDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPP----VVLDSILPE 1811
Cdd:cd05930 126 QEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPsllrLLLQELELA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1812 DIPSLQTVSTGGERCPIKVAKRWSL---DRNFYNVYGPTETTIATTWYRVSSPECVQDSVPIGTPVPNTEVFILDPDLNP 1888
Cdd:cd05930 206 ALPSLRLVLVGGEALPPDLVRRWREllpGARLVNLYGPTEATVDATYYRVPPDDEEDGRVPIGRPIPNTRVYVLDENLRP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1889 VPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIE 1968
Cdd:cd05930 286 VPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIE 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497785100 1969 SLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKII--EELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05930 366 AALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDEEElrAHLAERLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
1108-1532 |
1.38e-166 |
|
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: 517.68 E-value: 1.38e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1108 IPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFREsknID--PVQVVLKDLKCTI 1185
Cdd:cd19531 2 LPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVE---VDgePVQVILPPLPLPL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1186 NILDF---DENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQII 1262
Cdd:cd19531 79 PVVDLsglPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1263 SNMPIQLEQPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAVLIK 1342
Cdd:cd19531 159 AGRPSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELTAALR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1343 EICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQIL 1422
Cdd:cd19531 239 ALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVRETAL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1423 GALENQDISFERIVQELNPERSLSYNPIYQVAFTLQNDEQGkNGNYGGLSVEEFEIEWRTSKVDLTLIIGQSKRGFEMVM 1502
Cdd:cd19531 319 EAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAA-ALELPGLTVEPLEVDSGTAKFDLTLSLTETDGGLRGSL 397
|
410 420 430
....*....|....*....|....*....|
gi 497785100 1503 EYNTDLFRQQSIEQMLSDYIKIISQVIENP 1532
Cdd:cd19531 398 EYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
520-999 |
1.35e-165 |
|
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: 515.54 E-value: 1.35e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIIThseyktsyegyevpilyidqlddfllderednlnvdcDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIY 679
Cdd:cd05930 81 EDSGAKLVLT-------------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 680 AIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSESG 759
Cdd:cd05930 124 WMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 760 TKLFPR-KGLILGGEASEWSWIKEIYRNIPaSCKLFNHYGPSETTIGVAVYEVTKKGLSNqfSTTPIGSSLSNNRIYILD 838
Cdd:cd05930 204 LAALPSlRLVLVGGEALPPDLVRRWRELLP-GARLVNLYGPTEATVDATYYRVPPDDEED--GRVPIGRPIPNTRVYVLD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 839 DKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVE 918
Cdd:cd05930 281 ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 919 PEEIQSQLLSHPSITEAIVTV-TKVRNEEQLVAYYVSKK--EVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKID 995
Cdd:cd05930 361 LGEIEAALLAHPGVREAAVVArEDGDGEKRLVAYVVPDEggELDEEELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVD 440
|
....
gi 497785100 996 RKAL 999
Cdd:cd05930 441 RKAL 444
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
40-1092 |
4.02e-161 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 556.11 E-value: 4.02e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 40 IPRHEERGSYPLSSIQKQIWFMSQLNPELPIYNEHLiKINLSGkVNIEALKKSFEQIVNRHQILR---MRVKQTEDSIEQ 116
Cdd:PRK12316 4094 LPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQM-RVDVQG-LDVERFRAAWQAALDRHDVLRsgfVWQGELGRPLQV 4171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 117 VITKSEPTIQFLSLRGisGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSE 196
Cdd:PRK12316 4172 VHKQVSLPFAELDWRG--RADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNHHILMDGWSNSQLLGE 4249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 197 LERFYNMYSqngeinPEQSqeelTIQYHDYALWqeklLTSENLEKGLEYWKEKL-EGDLPMLSIGGITQEGTGVGSEYNF 275
Cdd:PRK12316 4250 VLERYSGRP------PAQP----GGRYRDYIAW----LQRQDAAASEAFWREQLaALDEPTRLAQAIARADLRSANGYGE 4315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 276 KIPNI---LTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGR--NIRETRNVIGPFINTVVIRTKAEQ 350
Cdd:PRK12316 4316 HVRELdatATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRpaELPGIEGQIGLFINTLPVIATPRA 4395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 351 NLSVIEYLQQVHETTIQALENQDVPFEKvvevLNPNRDVRANPFYQLLFVMQEPPT----QFSLPGIKVEYELIPTEVAR 426
Cdd:PRK12316 4396 QQSVVEWLQQVQRQNLALREHEHTPLYE----IQRWAGQGGEALFDSLLVFENYPVsealQQGAPGGLRFGEVTNHEQTN 4471
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 427 FPLTLSIIEGEEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSPHQRIYDLNLLTSKERSESAYLYNQSGCKpFPTE 506
Cdd:PRK12316 4472 YPLTLAVGLGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAG-YPAT 4550
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 507 P-IHVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLP 585
Cdd:PRK12316 4551 RcVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVP 4630
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 586 LDVESPKERIEIITQDSKLKAIITHSEYKTsyegyEVPI------LYIDQLDDFLlDEREDNLNVDCDSSQLAYGIYTSG 659
Cdd:PRK12316 4631 LDPEYPRERLAYMMEDSGAALLLTQSHLLQ-----RLPIpdglasLALDRDEDWE-GFPAHDPAVRLHPDNLAYVIYTSG 4704
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 660 STGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLffLLKEDAI-DPAKVEEIVQG 738
Cdd:PRK12316 4705 STGRPKGVAVSHGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASV--VIRDDSLwDPERLYAEIHE 4782
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 739 KAIDWYKITPSHLKALS--SESGTKLFPRKGLILGGEASEWSWIKEIYRNIPAScKLFNHYGPSETTIGVAVYEvTKKGL 816
Cdd:PRK12316 4783 HRVTVLVFPPVYLQQLAehAERDGEPPSLRVYCFGGEAVAQASYDLAWRALKPV-YLFNGYGPTETTVTVLLWK-ARDGD 4860
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 817 SNQFSTTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPF-ITDSRMYKTGDIGKIL 895
Cdd:PRK12316 4861 ACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYR 4940
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 896 YTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYV-SKKEVLDKD---------LQT 965
Cdd:PRK12316 4941 ADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVpQDPALADADeaqaelrdeLKA 5020
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 966 YLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEIQVSNWNEIEIQPMNRLEEKMKDVWEKILERPVPSIDDSFFKLG 1045
Cdd:PRK12316 5021 ALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELG 5100
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....*..
gi 497785100 1046 GHSLLATRLVSMIRKEFKVELSIKEFFEKPSIRELSTHLLQLEAVST 1092
Cdd:PRK12316 5101 GHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDD 5147
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1109-2126 |
6.09e-161 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 555.16 E-value: 6.09e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1109 PLSDAQKRMWFLYRMESDSAYYNMPISLKIIGdLDYRAFTESIQEVNKRHDSLRTVFRESKNID-PVQVVLKDLKCTINI 1187
Cdd:PRK12467 2648 PLSPMQQGMLFHTLYEGGAGDYINQMRVDVEG-LDVERFRTAWQAVIDRHEILRSGFLWDGELEePLQVVYKQARLPFSR 2726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1188 LDF-DENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYhqiiSNMP 1266
Cdd:PRK12467 2727 LDWrDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRY----FGQP 2802
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1267 iqLEQPVYQYADYVNWQQNRYTEEQinqqLQYWKEQLS--GAPSLLELPLdKPRPSMQSYNGSLIRMKLPEKHAVLIKEI 1344
Cdd:PRK12467 2803 --PPAREGRYRDYIAWLQAQDAEAS----EAFWKEQLAalEEPTRLARAL-YPAPAEAVAGHGAHYLHLDATQTRQLIEF 2875
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1345 CEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANR--NIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQIL 1422
Cdd:PRK12467 2876 ARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRpaQLRGAEQQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNL 2955
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1423 GALENQ-----DIS----------FERIVQELNperslsynpiYQVAFTLQndeQGKNGN--YGGLSVEEfeiewrTSKV 1485
Cdd:PRK12467 2956 ALREFEhtplaDIQrwagqggealFDSILVFEN----------YPISEALK---QGAPSGlrFGAVSSRE------QTNY 3016
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1486 DLTLIIGQskrGFEMVMEYNTD--LFRQQSIEQMLSDYIKIISQVIENPNMEISRIQLVDQQHDLLVKKAESQPRSIK-- 1561
Cdd:PRK12467 3017 PLTLAVGL---GDTLELEFSYDrqHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYps 3093
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1562 -DCIQYSFENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYV 1640
Cdd:PRK12467 3094 eRLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYV 3173
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1641 PIDSELPLNRRDFILKDASVGAIVTQTSLEEKlsksdLPYLCTDQSQDSEDYSLLTKDKSYP------EDIAYIIYTSGT 1714
Cdd:PRK12467 3174 PLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQ-----LPAPAGDTALTLDRLDLNGYSENNPstrvmgENLAYVIYTSGS 3248
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1715 TGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGAtlCVVSREEQLSTKA-LVKRFRDW 1793
Cdd:PRK12467 3249 TGKPKGVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGG--CLVVRDNDLWDPEeLWQAIHAH 3326
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1794 NVTLADLPPVVLDSIL----PEDIPSLQTVSTGGERCP---IKVAKRWSLDRNFYNVYGPTETTIATT-WYRVSSPECVQ 1865
Cdd:PRK12467 3327 RISIACFPPAYLQQFAedagGADCASLDIYVFGGEAVPpaaFEQVKRKLKPRGLTNGYGPTEAVVTVTlWKCGGDAVCEA 3406
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1866 DSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREE-EILYKTGDIGKVLHDGN 1944
Cdd:PRK12467 3407 PYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSgGRLYRTGDLARYRADGV 3486
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1945 LEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLgDNQNYHTLVAYVVPH--GEWEEKKIIEELRSKLPEHMV 2022
Cdd:PRK12467 3487 IEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAdpQGDWRETLRDHLAASLPDYMV 3565
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2023 PSIFVQMEELPRLNNKKVDRHSLPTAVhiFRQQKVIQKPVTEEEVVVAECWAETLNLPidNIGLNSNFFELGGHSLTATQ 2102
Cdd:PRK12467 3566 PAQLLVLAAMPLGPNGKVDRKALPDPD--AKGSREYVAPRSEVEQQLAAIWADVLGVE--QVGVTDNFFELGGDSLLALQ 3641
|
1050 1060
....*....|....*....|....
gi 497785100 2103 LVARISELFEIELPIKAIFEYPTI 2126
Cdd:PRK12467 3642 VLSRIRQSLGLKLSLRDLMSAPTI 3665
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
49-1286 |
1.91e-157 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 544.37 E-value: 1.91e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 49 YPLSSIQKQIWFMSQLNPELPIYNEHLIkINLSGkVNIEALKKSFEQIVNRHQILRMR-VKQTEDSIE-QVITKsEPTIQ 126
Cdd:PRK12467 2647 YPLSPMQQGMLFHTLYEGGAGDYINQMR-VDVEG-LDVERFRTAWQAVIDRHEILRSGfLWDGELEEPlQVVYK-QARLP 2723
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 127 FLSLRGISGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNmysq 206
Cdd:PRK12467 2724 FSRLDWRDRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLLGEVLQRYF---- 2799
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 207 nGEINPEQSQeeltiQYHDYALWqeklLTSENLEKGLEYWKEKLeGDL--PMLSIGGITQ---EGTGVGSEYNFKIPNIL 281
Cdd:PRK12467 2800 -GQPPPAREG-----RYRDYIAW----LQAQDAEASEAFWKEQL-AALeePTRLARALYPapaEAVAGHGAHYLHLDATQ 2868
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 282 TDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGR--NIRETRNVIGPFINTV-VIRT-KAEQNLSviEY 357
Cdd:PRK12467 2869 TRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRpaQLRGAEQQLGLFINTLpVIASpRAEQTVS--DW 2946
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 358 LQQVHETTIQALENQDVP-FE------KVVEVLNPNRDVRAN-PFYQLLfvMQEPPTQFSLPGIKVEyeliptEVARFPL 429
Cdd:PRK12467 2947 LQQVQAQNLALREFEHTPlADiqrwagQGGEALFDSILVFENyPISEAL--KQGAPSGLRFGAVSSR------EQTNYPL 3018
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 430 TLSIIEGEEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSPHQRIYDLNLLTSKERSESAYLYNQSGCKPFPTEPIH 509
Cdd:PRK12467 3019 TLAVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERLVH 3098
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 510 VQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVE 589
Cdd:PRK12467 3099 QLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPE 3178
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 590 SPKERIEIITQDSKLKAIITHSEYKTsyegyEVPILYIDQ---LDDFLLD-EREDNLNVDCDSSQLAYGIYTSGSTGIPK 665
Cdd:PRK12467 3179 YPRERLAYMIEDSGVKLLLTQAHLLE-----QLPAPAGDTaltLDRLDLNgYSENNPSTRVMGENLAYVIYTSGSTGKPK 3253
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 666 GVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLfFLLKEDAIDPAKVEEIVQGKAIDWYK 745
Cdd:PRK12467 3254 GVGVRHGALANHLCWIAEAYELDANDRVLLFMSFSFDGAQERFLWTLICGGCL-VVRDNDLWDPEELWQAIHAHRISIAC 3332
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 746 ITPSHLKALSSESGTKLFPR-KGLILGGEASEWSWIKEIYRNIPASCkLFNHYGPSETTIGVAVYEVTKKGLSnQFSTTP 824
Cdd:PRK12467 3333 FPPAYLQQFAEDAGGADCASlDIYVFGGEAVPPAAFEQVKRKLKPRG-LTNGYGPTEAVVTVTLWKCGGDAVC-EAPYAP 3410
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 825 IGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITD-SRMYKTGDIGKILYTGEIQFL 903
Cdd:PRK12467 3411 IGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSgGRLYRTGDLARYRADGVIEYL 3490
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 904 GRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYVSKKEVLD--KDLQTYLKQKLPPNLVPAYLV 981
Cdd:PRK12467 3491 GRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDwrETLRDHLAASLPDYMVPAQLL 3570
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 982 KMDTLPRHAHGKIDRKALPEIQVSNWNEIeIQPMNRLEEKMKDVWEKILERPVPSIDDSFFKLGGHSLLATRLVSMIRKE 1061
Cdd:PRK12467 3571 VLAAMPLGPNGKVDRKALPDPDAKGSREY-VAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQS 3649
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1062 FKVELSIKEFFEKPSIRELSTHlLQLEAVSTHfalsniseaekekgiPLSDAQKRmwflyrmesdsayynmpislkiigd 1141
Cdd:PRK12467 3650 LGLKLSLRDLMSAPTIAELAGY-SPLGDVPVN---------------LLLDLNRL------------------------- 3688
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1142 ldyrafTESIQEVNKRHDSLRTVFREskniDPVQVVLKDlkctinildfdenrseqdimnylteksmepfkletgplirv 1221
Cdd:PRK12467 3689 ------ETGFPALFCRHEGLGTVFDY----EPLAVILEG----------------------------------------- 3717
|
1210 1220 1230 1240 1250 1260
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 1222 hlvksnpNEHVLLIVQHHIISDGWSlrimmdelfaiyhqiisnmPIQLEQPVYQYADYVNWQQNR 1286
Cdd:PRK12467 3718 -------DRHVLGLTCRHLLDDGWQ-------------------DTSLQAMAVQYADYILWQQAK 3756
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1576-2046 |
5.58e-156 |
|
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: 488.69 E-value: 5.58e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQtsleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISAT 1735
Cdd:cd17652 81 ADARPALLLTT-----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1736 IDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSILPEDIPS 1815
Cdd:cd17652 126 IAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDDLPD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1816 LQTVSTGGERCPIKVAKRWSLDRNFYNVYGPTETTIATTWYRVSSPEcvqDSVPIGTPVPNTEVFILDPDLNPVPMGVIG 1895
Cdd:cd17652 206 LRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGG---GVPPIGRPVPGTRVYVLDARLRPVPPGVPG 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1896 EIYIGGVGVSNGYLNRDDLNEKRFIPHPFREE-EILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQ 1974
Cdd:cd17652 283 ELYIAGAGLARGYLNRPGLTAERFVADPFGAPgSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEH 362
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 1975 TGVKEAIV----QPLGDNQnyhtLVAYVVPHGEWEEKKII--EELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSLP 2046
Cdd:cd17652 363 PGVAEAVVvvrdDRPGDKR----LVAYVVPAPGAAPTAAElrAHLAERLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
512-1001 |
1.76e-155 |
|
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: 489.53 E-value: 1.76e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESP 591
Cdd:cd17655 3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 592 KERIEIITQDSKLKAIITHSEYKtSYEGYEVPILYIDqlDDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEH 671
Cdd:cd17655 83 EERIQYILEDSGADILLTQSHLQ-PPIAFIGLIDLLD--EDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 672 RNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHL 751
Cdd:cd17655 160 RGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 752 KALSSESGTKLFPRKGLILGGEASEWSWIKEIYRNIPASCKLFNHYGPSETTIGVAVYEVTKKglSNQFSTTPIGSSLSN 831
Cdd:cd17655 240 KLLDAADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPE--TDQQVSVPIGKPLGN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 832 NRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKILYTGEIQFLGRLDGQVK 911
Cdd:cd17655 318 TRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVK 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 912 IRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQ-LVAYYVSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHA 990
Cdd:cd17655 398 IRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNyLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTP 477
|
490
....*....|.
gi 497785100 991 HGKIDRKALPE 1001
Cdd:cd17655 478 NGKVDRKALPE 488
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1065-2128 |
2.43e-155 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 538.00 E-value: 2.43e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1065 ELSI-----KEFFEKPSI--------RELST---HLLQLEAVS---THFALSNISEA----------EKEKGIPLSDAQK 1115
Cdd:PRK12316 1485 ELSLhwsfsREMFAEATVqrladdyaRELQAlieHCCDERNRGvtpSDFPLAGLSQAqldalplpagEIADIYPLSPMQQ 1564
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1116 RMWF--LYRMESdSAYYNmpiSLKI-IGDLDYRAFTESIQEVNKRHDSLRTVFRESKNID-PVQVVLKDLKCTINILDFD 1191
Cdd:PRK12316 1565 GMLFhsLYEQEA-GDYIN---QLRVdVQGLDPDRFRAAWQATVDRHEILRSGFLWQDGLEqPLQVIHKQVELPFAELDWR 1640
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1192 ENRSEQDIMNYLTEKSMEP-FKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYhqiiSNMPIQle 1270
Cdd:PRK12316 1641 GREDLGQALDALAQAERQKgFDLTRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRY----AGQPVA-- 1714
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1271 QPVYQYADYVNW--QQNRYTEEqinqqlQYWKEQLSG--APSLLELPLDKPRPsmQSYNGSLIRMKLPEKHAVLiKEICE 1346
Cdd:PRK12316 1715 APGGRYRDYIAWlqRQDAAASE------AFWKEQLAAleEPTRLAQAARTEDG--QVGYGDHQQLLDPAQTRAL-AEFAR 1785
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1347 EAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNiQELEGI---LGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILG 1423
Cdd:PRK12316 1786 AQKVTLNTLVQAAWLLLLQRYTGQETVAFGATVAGRP-AELPGIeqqIGLFINTLPVIAAPRPDQSVADWLQEVQALNLA 1864
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1424 ALENQDISFERIVQELNPERSLSYNPI-----YQVAFTLqndeqgKNGNYGGLSVEEFEIEWRTSkVDLTLIIGQskrGF 1498
Cdd:PRK12316 1865 LREHEHTPLYDIQRWAGQGGEALFDSLlvfenYPVAEAL------KQGAPAGLVFGRVSNHEQTN-YPLTLAVTL---GE 1934
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1499 EMVMEYNTDL--FRQQSIEQMLSDYIKIISQVIENPNMEISRIQLVD-QQHDLLV----KKAESQPRSIKdcIQYSFENW 1571
Cdd:PRK12316 1935 TLSLQYSYDRghFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDaGERQRILadwdRTPEAYPRGPG--VHQRIAEQ 2012
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1572 VRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRR 1651
Cdd:PRK12316 2013 AARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERL 2092
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1652 DFILKDASVGAIVTQTSLEEKLS-KSDLPYLCTDQSQDSEDY-SLLTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVM 1729
Cdd:PRK12316 2093 AYMLEDSGAALLLTQRHLLERLPlPAGVARLPLDRDAEWADYpDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALV 2172
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1730 NLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLcVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSIL 1809
Cdd:PRK12316 2173 AHCQAAGERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARV-LIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLA 2251
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1810 PE-----DIPSLQTVSTGGERCPIKVAKRW--SLDRNF-YNVYGPTETTIATT-WYRVSSPECVQDSVPIGTPVPNTEVF 1880
Cdd:PRK12316 2252 EHaerdgRPPAVRVYCFGGEAVPAASLRLAweALRPVYlFNGYGPTEAVVTPLlWKCRPQDPCGAAYVPIGRALGNRRAY 2331
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1881 ILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREE-EILYKTGDIGKVLHDGNLEHLGRLDHQIKVRG 1959
Cdd:PRK12316 2332 ILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASgERLYRTGDLARYRADGVVEYLGRIDHQVKIRG 2411
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1960 FRIELGEIESLLNLQTGVKEAIVQPLgDNQNYHTLVAYVVPH--GEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNN 2037
Cdd:PRK12316 2412 FRIELGEIEARLQAHPAVREAVVVAQ-DGASGKQLVAYVVPDdaAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPN 2490
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2038 KKVDRHSLPtAVHIFRQQKVIQKPVTEEEVVVAECWAETLNLpiDNIGLNSNFFELGGHSLTATQLVARISELFEIELPI 2117
Cdd:PRK12316 2491 GKLDRKALP-KPDVSQLRQAYVAPQEGLEQRLAAIWQAVLKV--EQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPL 2567
|
1130
....*....|.
gi 497785100 2118 KAIFEYPTIQA 2128
Cdd:PRK12316 2568 RILFERPTLAA 2578
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1568-2046 |
1.24e-154 |
|
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: 487.22 E-value: 1.24e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELP 1647
Cdd:cd17655 3 FEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 LNRRDFILKDASVGAIVTQTSLEEKLSKSDLPYLCTDQSQDSEDYSLLTKDkSYPEDIAYIIYTSGTTGTPNGVMVKHSS 1727
Cdd:cd17655 83 EERIQYILEDSGADILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPV-SKSDDLAYVIYTSGSTGKPKGVMIEHRG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1728 VMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDS 1807
Cdd:cd17655 162 VVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHLKL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1808 ILPEDI---PSLQTVSTGGERCPIKVAKRWS----LDRNFYNVYGPTETTIATTWYRVSSPECVQDSVPIGTPVPNTEVF 1880
Cdd:cd17655 242 LDAADDsegLSLKHLIVGGEALSTELAKKIIelfgTNPTITNAYGPTETTVDASIYQYEPETDQQVSVPIGKPLGNTRIY 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1881 ILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGF 1960
Cdd:cd17655 322 ILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGY 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1961 RIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKV 2040
Cdd:cd17655 402 RIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKV 481
|
....*.
gi 497785100 2041 DRHSLP 2046
Cdd:cd17655 482 DRKALP 487
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1589-1982 |
4.21e-153 |
|
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: 479.45 E-value: 4.21e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKM-GIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQT 1667
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1668 SLEEKLSKSDLPYLCTDQSQDSEDYSLLTKD----KSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQ 1743
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPAPPppdaPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1744 ETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWN-VTLADLPPVVLDSILPEDIP---SLQTV 1819
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAALLAALIAEHpVTVLNLTPSLLALLAAALPPalaSLRLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1820 STGGERCPIKVAKRWSL---DRNFYNVYGPTETTIATTWYRVS-SPECVQDSVPIGTPVPNTEVFILDPDLNPVPMGVIG 1895
Cdd:TIGR01733 241 ILGGEALTPALVDRWRArgpGARLINLYGPTETTVWSTATLVDpDDAPRESPVPIGRPLANTRLYVLDDDLRPVPVGVVG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1896 EIYIGGVGVSNGYLNRDDLNEKRFIPHPFR--EEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNL 1973
Cdd:TIGR01733 321 ELYIGGPGVARGYLNRPELTAERFVPDPFAggDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLR 400
|
....*....
gi 497785100 1974 QTGVKEAIV 1982
Cdd:TIGR01733 401 HPGVREAVV 409
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1568-2045 |
4.27e-149 |
|
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: 471.30 E-value: 4.27e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELP 1647
Cdd:cd12117 3 FEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 LNRRDFILKDASVGAIVTQTSLEEKLSKSDLPYLCTDQSQDSEDYSLLTKDKsyPEDIAYIIYTSGTTGTPNGVMVKHSS 1727
Cdd:cd12117 83 AERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNPAVPVS--PDDLAYVMYTSGSTGRPKGVAVTHRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1728 VMNLISATiDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVT----------- 1796
Cdd:cd12117 161 VVRLVKNT-NYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTvlwltaalfnq 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1797 LADLPPVVLDSilpedipsLQTVSTGGERCPIKVAKRWsLDRN----FYNVYGPTETTIATTWYRVSSPECVQDSVPIGT 1872
Cdd:cd12117 240 LADEDPECFAG--------LRELLTGGEVVSPPHVRRV-LAACpglrLVNGYGPTENTTFTTSHVVTELDEVAGSIPIGR 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1873 PVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLD 1952
Cdd:cd12117 311 PIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFLGRID 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1953 HQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEEL 2032
Cdd:cd12117 391 DQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVVLDEL 470
|
490
....*....|...
gi 497785100 2033 PRLNNKKVDRHSL 2045
Cdd:cd12117 471 PLTANGKVDRRAL 483
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1568-2046 |
3.00e-144 |
|
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: 458.35 E-value: 3.00e-144
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELP 1647
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 LNRRDFILKDASVGAIVTQTSLEEKLSKSDLPYLCTDQSQDSEDYSLLTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSS 1727
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMPHRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1728 VMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDS 1807
Cdd:cd17651 161 LANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1808 ILPE------DIPSLQTVSTGGERCPIKVA-KRWSLDRNF---YNVYGPTETTIATTWYRVSSPECVQDSVPIGTPVPNT 1877
Cdd:cd17651 241 LAEHgrplgvRLAALRYLLTGGEQLVLTEDlREFCAGLPGlrlHNHYGPTETHVVTALSLPGDPAAWPAPPPIGRPIDNT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1878 EVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKV 1957
Cdd:cd17651 321 RVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRADDQVKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1958 RGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKII--EELRSKLPEHMVPSIFVQMEELPRL 2035
Cdd:cd17651 401 RGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDAAElrAALATHLPEYMVPSAFVLLDALPLT 480
|
490
....*....|.
gi 497785100 2036 NNKKVDRHSLP 2046
Cdd:cd17651 481 PNGKLDRRALP 491
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1107-2129 |
1.19e-140 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 474.53 E-value: 1.19e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1107 GIPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNIdPVQVVlkDLKCTIN 1186
Cdd:PRK10252 7 HLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGE-VWQWV--DPALTFP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1187 ILDFDENRSEQD----IMNYLTEKSMEPFKLETG-PLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQI 1261
Cdd:PRK10252 84 LPEIIDLRTQPDphaaAQALMQADLQQDLRVDSGkPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAW 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1262 ISNMPIQlEQPVYQYADYVNWQQnRYTEEQINQQ-LQYWKEQLSGAPSLLELPlDKPRPSmQSYNGSLIRMKLPEKHAVL 1340
Cdd:PRK10252 164 LRGEPTP-ASPFTPFADVVEEYQ-RYRASEAWQRdAAFWAEQRRQLPPPASLS-PAPLPG-RSASADILRLKLEFTDGAF 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1341 IKEICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQ 1420
Cdd:PRK10252 240 RQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQ 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1421 ILGALENQDISFERIVQELN---PERSLsYNPIYQV-AFTLQNDEQGKNGNYGGLSveefeiewrTSKV-DLTLII-GQS 1494
Cdd:PRK10252 320 LKKMRRHQRYDAEQIVRDSGraaGDEPL-FGPVLNIkVFDYQLDFPGVQAQTHTLA---------TGPVnDLELALfPDE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1495 KRGFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENPNMEISRIQLV-DQQHDLLVK---KAESQPRSIKDCIqysFEN 1570
Cdd:PRK10252 390 HGGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILlPGEYAQLAQvnaTAVEIPETTLSAL---VAQ 466
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1571 WVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNR 1650
Cdd:PRK10252 467 QAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDR 546
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1651 RDFILKDASVGAIVTQTSLEEKLS-KSDLPYLCTDQSQDSEDYSLLTKDKsyPEDIAYIIYTSGTTGTPNGVMVKHSSVM 1729
Cdd:PRK10252 547 LKMMLEDARPSLLITTADQLPRFAdVPDLTSLCYNAPLAPQGAAPLQLSQ--PHHTAYIIFTSGSTGRPKGVMVGQTAIV 624
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1730 NLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSIL 1809
Cdd:PRK10252 625 NRLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAFV 704
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1810 ----PEDIP----SLQTVSTGGERCPIKVAKRWSLDRN--FYNVYGPTETTIATTWYRVSSPECVQ---DSVPIGTPVPN 1876
Cdd:PRK10252 705 asltPEGARqscaSLRQVFCSGEALPADLCREWQQLTGapLHNLYGPTEAAVDVSWYPAFGEELAAvrgSSVPIGYPVWN 784
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1877 TEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIK 1956
Cdd:PRK10252 785 TGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDDQLK 864
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1957 VRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHT------LVAYVVPHGEWEEKKI--IEELRSKLPEHMVPSIFVQ 2028
Cdd:PRK10252 865 IRGQRIELGEIDRAMQALPDVEQAVTHACVINQAAATggdarqLVGYLVSQSGLPLDTSalQAQLRERLPPHMVPVVLLQ 944
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2029 MEELPRLNNKKVDRHSLPTAVHifrQQKVIQK-PVTEEEVVVAECWAETLNLPIDNIglNSNFFELGGHSLTATQLVARI 2107
Cdd:PRK10252 945 LDQLPLSANGKLDRKALPLPEL---KAQVPGRaPKTGTETIIAAAFSSLLGCDVVDA--DADFFALGGHSLLAMKLAAQL 1019
|
1050 1060
....*....|....*....|..
gi 497785100 2108 SELFEIELPIKAIFEYPTIQAI 2129
Cdd:PRK10252 1020 SRQFARQVTPGQVMVASTVAKL 1041
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1563-2046 |
9.75e-140 |
|
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: 444.57 E-value: 9.75e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1563 CIQYSFENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPI 1642
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1643 DSELPLNRRDFILKDASVGAIVTQtsleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVM 1722
Cdd:cd17644 81 DPNYPQERLTYILEDAQISVLLTQ-----------------------------------PENLAYVIYTSGSTGKPKGVM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1723 VKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPP 1802
Cdd:cd17644 126 IEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1803 VVL----DSILPEDIP---SLQTVSTGGERC-PIKV---AKRWSLDRNFYNVYGPTETTIATTWYRVSSPECVQ-DSVPI 1870
Cdd:cd17644 206 AYWhllvLELLLSTIDlpsSLRLVIVGGEAVqPELVrqwQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNiTSVPI 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1871 GTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFR--EEEILYKTGDIGKVLHDGNLEHL 1948
Cdd:cd17644 286 GRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDGNIEYL 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1949 GRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKII--EELRSKLPEHMVPSIF 2026
Cdd:cd17644 366 GRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEESPSTVElrQFLKAKLPDYMIPSAF 445
|
490 500
....*....|....*....|
gi 497785100 2027 VQMEELPRLNNKKVDRHSLP 2046
Cdd:cd17644 446 VVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1568-2045 |
2.66e-136 |
|
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: 435.55 E-value: 2.66e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELP 1647
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 LNRRDFILKDASVGAIVTQTSLEEKLSKSDLPYLCTDQSQDSEDySLLTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSS 1727
Cdd:cd17646 84 ADRLAYMLADAGPAVVLTTADLAARLPAGGDVALLGDEALAAPP-ATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVTHAG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1728 VMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLcVVSREEQLSTKA-LVKRFRDWNVTLADLPPVVLD 1806
Cdd:cd17646 163 IVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARL-VVARPGGHRDPAyLAALIREHGVTTCHFVPSMLR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1807 SIL----PEDIPSLQTVSTGGERCPIKVAKRWS--LDRNFYNVYGPTETTIATTWYRVSSPEcVQDSVPIGTPVPNTEVF 1880
Cdd:cd17646 242 VFLaepaAGSCASLRRVFCSGEALPPELAARFLalPGAELHNLYGPTEAAIDVTHWPVRGPA-ETPSVPIGRPVPNTRLY 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1881 ILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGF 1960
Cdd:cd17646 321 VLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGF 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1961 RIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIE---ELRSKLPEHMVPSIFVQMEELPRLNN 2037
Cdd:cd17646 401 RVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVPAAGAAGPDTAAlraHLAERLPEYMVPAAFVVLDALPLTAN 480
|
....*...
gi 497785100 2038 KKVDRHSL 2045
Cdd:cd17646 481 GKLDRAAL 488
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
512-999 |
7.24e-136 |
|
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: 434.32 E-value: 7.24e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESP 591
Cdd:cd12117 3 FEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 592 KERIEIITQDSKLKAIITHSEYKTSYEGYEVPILYIDQLDDflldEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEH 671
Cdd:cd12117 83 AERLAFMLADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDA----GPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 672 RNL------SNYIyaiqtklGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYK 745
Cdd:cd12117 159 RGVvrlvknTNYV-------TLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 746 ITPS---HLKALSSESGTKLfpRKgLILGGEASEWSWIKEIYRNIPAScKLFNHYGPSETTIGVAVYEVTKkgLSNQFST 822
Cdd:cd12117 232 LTAAlfnQLADEDPECFAGL--RE-LLTGGEVVSPPHVRRVLAACPGL-RLVNGYGPTENTTFTTSHVVTE--LDEVAGS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 823 TPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKILYTGEIQF 902
Cdd:cd12117 306 IPIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEF 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 903 LGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRN-EEQLVAYYVSKKEVLDKDLQTYLKQKLPPNLVPAYLV 981
Cdd:cd12117 386 LGRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGgDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFV 465
|
490
....*....|....*...
gi 497785100 982 KMDTLPRHAHGKIDRKAL 999
Cdd:cd12117 466 VLDELPLTANGKVDRRAL 483
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
50-1084 |
1.05e-133 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 454.50 E-value: 1.05e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 50 PLSSIQKQIWFMSQLNPELPIYN-EHLIKINlsGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVITKSePTIQFL 128
Cdd:PRK10252 9 PLVAAQPGIWMAEKLSPLPSAWSvAHYVELT--GELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPA-LTFPLP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 129 SLRGISGE-EQQEILSEYCRKEANYPYRLEQEN-LIRMSIIELSESSYsVLFSR-HHILSDGWSASILLSELERFYNMYs 205
Cdd:PRK10252 86 EIIDLRTQpDPHAAAQALMQADLQQDLRVDSGKpLVFHQLIQLGDNRW-YWYQRyHHLLVDGFSFPAITRRIAAIYCAW- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 206 QNGEINPEQSQEELTIQYHDYALWQEklltSENLEKGLEYWKEKLEGDLPMLSIGGitQEGTGVGSEynfkiPNILTDKL 285
Cdd:PRK10252 164 LRGEPTPASPFTPFADVVEEYQRYRA----SEAWQRDAAFWAEQRRQLPPPASLSP--APLPGRSAS-----ADILRLKL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 286 --------RKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVIEY 357
Cdd:PRK10252 233 eftdgafrQLAAQASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPEL 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 358 LQQVHETTIQALENQDVPFEKVVEVLNPNRDVRanPFYQLLFVMQEPPTQFSLPGIKVEYELIPT-EVARFPLTLSIIEG 436
Cdd:PRK10252 313 ATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDE--PLFGPVLNIKVFDYQLDFPGVQAQTHTLATgPVNDLELALFPDEH 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 437 EEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSPHQRIYDLNLLTSKERSESAYLyNQSGcKPFPTEPIHVQFEGQV 516
Cdd:PRK10252 391 GGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQV-NATA-VEIPETTLSALVAQQA 468
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 517 LNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIE 596
Cdd:PRK10252 469 AKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLK 548
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 597 IITQDSKLKAIITHSEYKTSYEGyeVPILYIDQLDDFLLDEREDNLNVDcDSSQLAYGIYTSGSTGIPKGVLVEHRNLSN 676
Cdd:PRK10252 549 MMLEDARPSLLITTADQLPRFAD--VPDLTSLCYNAPLAPQGAAPLQLS-QPHHTAYIIFTSGSTGRPKGVMVGQTAIVN 625
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 677 YIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEeivqgKAIDWYKIT-----PSHL 751
Cdd:PRK10252 626 RLLWMQNHYPLTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQ-----QFFAEYGVTtthfvPSML 700
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 752 KALSSESGTKLFPRKGLIL-----GGEASEWSWIKEIYRNIPAscKLFNHYGPSETTIGVAVYEVTKKGLSNQFSTT-PI 825
Cdd:PRK10252 701 AAFVASLTPEGARQSCASLrqvfcSGEALPADLCREWQQLTGA--PLHNLYGPTEAAVDVSWYPAFGEELAAVRGSSvPI 778
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 826 GSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKILYTGEIQFLGR 905
Cdd:PRK10252 779 GYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGR 858
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 906 LDGQVKIRGIRVEPEEIQSQLLSHPSITEAiVTVTKVRN--------EEQLVAYYVSKKEV-LDKD-LQTYLKQKLPPNL 975
Cdd:PRK10252 859 SDDQLKIRGQRIELGEIDRAMQALPDVEQA-VTHACVINqaaatggdARQLVGYLVSQSGLpLDTSaLQAQLRERLPPHM 937
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 976 VPAYLVKMDTLPRHAHGKIDRKALPEIQVSNwNEIEIQPMNRLEEKMKDVWEKILERPVPSIDDSFFKLGGHSLLATRLV 1055
Cdd:PRK10252 938 VPVVLLQLDQLPLSANGKLDRKALPLPELKA-QVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLA 1016
|
1050 1060
....*....|....*....|....*....
gi 497785100 1056 SMIRKEFKVELSIKEFFEKPSIRELSTHL 1084
Cdd:PRK10252 1017 AQLSRQFARQVTPGQVMVASTVAKLATLL 1045
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1576-2045 |
8.86e-133 |
|
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: 425.17 E-value: 8.86e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQTSLEEKLSkSDLPYLCTDQSQDSEDYSLLTKDKSyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISAT 1735
Cdd:cd12116 81 EDAEPALVLTDDALPDRLP-AGLPVLLLALAAAAAAPAAPRTPVS-PDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1736 IDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPV----VLDSiLPE 1811
Cdd:cd12116 159 RERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPAtwrmLLDA-GWQ 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1812 DIPSLqTVSTGGERCPIKVAKRW-SLDRNFYNVYGPTETTIATTWYRVSSPEcvqDSVPIGTPVPNTEVFILDPDLNPVP 1890
Cdd:cd12116 238 GRAGL-TALCGGEALPPDLAARLlSRVGSLWNLYGPTETTIWSTAARVTAAA---GPIPIGRPLANTQVYVLDAALRPVP 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1891 MGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREE-EILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIES 1969
Cdd:cd12116 314 PGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPgSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEA 393
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 1970 LLNLQTGVKEAIVQPLGDNQNYHtLVAYVVPHGEWEEKKII--EELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd12116 394 ALAAHPGVAQAAVVVREDGGDRR-LVAYVVLKAGAAPDAAAlrAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
512-1000 |
7.78e-128 |
|
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: 411.74 E-value: 7.78e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESP 591
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 592 KERIEIITQDSKLKAIITHSEYKTSYEGYEVPILYIDQLDDFLLDEreDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEH 671
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPALAGELAVELVAVTLLDQPGAAAGAD--AEPDPALDADDLAYVIYTSGSTGRPKGVVMPH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 672 RNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHL 751
Cdd:cd17651 159 RSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 752 KALSSE---SGTKLFPRKGLILGGEA-SEWSWIKEIYRNIPAScKLFNHYGPSETTigVAVYEVTKKGLSNQFSTTPIGS 827
Cdd:cd17651 239 RALAEHgrpLGVRLAALRYLLTGGEQlVLTEDLREFCAGLPGL-RLHNHYGPTETH--VVTALSLPGDPAAWPAPPPIGR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 828 SLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKILYTGEIQFLGRLD 907
Cdd:cd17651 316 PIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFLGRAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 908 GQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTK-VRNEEQLVAYYVSKKEVLD--KDLQTYLKQKLPPNLVPAYLVKMD 984
Cdd:cd17651 396 DQVKIRGFRIELGEIEAALARHPGVREAVVLAREdRPGEKRLVAYVVGDPEAPVdaAELRAALATHLPEYMVPSAFVLLD 475
|
490
....*....|....*.
gi 497785100 985 TLPRHAHGKIDRKALP 1000
Cdd:cd17651 476 ALPLTPNGKLDRRALP 491
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1576-2046 |
1.97e-127 |
|
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: 409.07 E-value: 1.97e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQTsleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISAT 1735
Cdd:cd17649 81 EDSGAGLLLTHH----------------------------------PRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1736 IDEFNITQETKVGQFATISFDASLWQILMALLAGAtlCVVSREEQL--STKALVKRFRDWNVTLADLPPV-------VLD 1806
Cdd:cd17649 127 AERYGLTPGDRELQFASFNFDGAHEQLLPPLICGA--CVVLRPDELwaSADELAEMVRELGVTVLDLPPAylqqlaeEAD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1807 SILPEDIPSLQTVSTGGERCPIKVAKRW-SLDRNFYNVYGPTETTIATTWYRVSS-PECVQDSVPIGTPVPNTEVFILDP 1884
Cdd:cd17649 205 RTGDGRPPSLRLYIFGGEALSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKCEAgAARAGASMPIGRPLGGRSAYILDA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1885 DLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREE-EILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIE 1963
Cdd:cd17649 285 DLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPgSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1964 LGEIESLLNLQTGVKEAIVQPLgDNQNYHTLVAYVVPHGEWEEKKIIEELR----SKLPEHMVPSIFVQMEELPRLNNKK 2039
Cdd:cd17649 365 LGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPELRAQLRtalrASLPDYMVPAHLVFLARLPLTPNGK 443
|
....*..
gi 497785100 2040 VDRHSLP 2046
Cdd:cd17649 444 LDRKALP 450
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1576-2045 |
3.22e-127 |
|
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: 408.23 E-value: 3.22e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQtsleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISAT 1735
Cdd:cd17643 81 ADSGPSLLLTD-----------------------------------PDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAT 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1736 IDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPP------VVLDSIL 1809
Cdd:cd17643 126 QRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPsafyqlVEAADRD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1810 PEDIPSLQTVSTGGERCPIKVAKRW----SLDR-NFYNVYGPTETTIATTWYRVSSPECV-QDSVPIGTPVPNTEVFILD 1883
Cdd:cd17643 206 GRDPLALRYVIFGGEALEAAMLRPWagrfGLDRpQLVNMYGITETTVHVTFRPLDAADLPaAAASPIGRPLPGLRVYVLD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1884 PDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREE-EILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRI 1962
Cdd:cd17643 286 ADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPgSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRI 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1963 ELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKII--EELRSKLPEHMVPSIFVQMEELPRLNNKKV 2040
Cdd:cd17643 366 ELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVADDGAAADIAElrALLKELLPDYMVPARYVPLDALPLTVNGKL 445
|
....*
gi 497785100 2041 DRHSL 2045
Cdd:cd17643 446 DRAAL 450
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
533-937 |
1.11e-126 |
|
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: 405.11 E-value: 1.11e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 533 TYLQTNNRANQIARWLQKQ-GIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITHS 611
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 612 EYKTSYEGYEVPILYIDQLDDFLLDER--EDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKP 689
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDApaPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 690 KDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAK-VEEIVQGKAIDWYKITPSHLKALSSESGTKLFPRKGL 768
Cdd:TIGR01733 161 DDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAAlLAALIAEHPVTVLNLTPSLLALLAAALPPALASLRLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 769 ILGGEASEWSWIKEIYRNIPaSCKLFNHYGPSETTIGVAVYEVTKKGLSnQFSTTPIGSSLSNNRIYILDDKLRPVPSGI 848
Cdd:TIGR01733 241 ILGGEALTPALVDRWRARGP-GARLINLYGPTETTVWSTATLVDPDDAP-RESPVPIGRPLANTRLYVLDDDLRPVPVGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 849 PGHIYIAGEQVARGYLNREELTAERFMEDPFITDS--RMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQL 926
Cdd:TIGR01733 319 VGELYIGGPGVARGYLNRPELTAERFVPDPFAGGDgaRLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 398
|
410
....*....|.
gi 497785100 927 LSHPSITEAIV 937
Cdd:TIGR01733 399 LRHPGVREAVV 409
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1567-2045 |
1.46e-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: 402.84 E-value: 1.46e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1567 SFENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSEL 1646
Cdd:cd17653 2 AFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1647 PLNRRDFILKDASVGAIVTQTSleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHS 1726
Cdd:cd17653 82 PSARIQAILRTSGATLLLTTDS---------------------------------PDDLAYIIFTSGSTGIPKGVMVPHR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1727 SVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALvkrfrdwNVTLADLPPVVLD 1806
Cdd:cd17653 129 GVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPSDPFAHVAR-------TVDALMSTPSILS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1807 SILPEDIPSLQTVSTGGERCPIKVAKRWSLDRNFYNVYGPTETTIATTWYRVSsPEcvqDSVPIGTPVPNTEVFILDPDL 1886
Cdd:cd17653 202 TLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTELL-PG---QPVTIGKPIPNSTCYILDADL 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1887 NPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGE 1966
Cdd:cd17653 278 QPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEE 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1967 IES-LLNLQTGVKEAIVQPLGDNqnyhtLVAYVVPHGeWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd17653 358 IEEvVLQSQPEVTQAAAIVVNGR-----LVAFVTPET-VDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1568-2045 |
9.75e-124 |
|
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: 399.61 E-value: 9.75e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELP 1647
Cdd:cd05918 5 IEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 LNRRDFILKDASVGAIVTqtsleeklsksdlpylctdqsqdsedyslltkdkSYPEDIAYIIYTSGTTGTPNGVMVKHSS 1727
Cdd:cd05918 85 LQRLQEILQDTGAKVVLT----------------------------------SSPSDAAYVIFTSGSTGKPKGVVIEHRA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1728 VMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLStkALVKRFRDWNVTLADLPPVVLDS 1807
Cdd:cd05918 131 LSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLTPSVARL 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1808 ILPEDIPSLQTVSTGGERCPIKVAKRWSLDRNFYNVYGPTETTIATTwyrVSSPECVQDSVPIGTPVPNTeVFILDPDlN 1887
Cdd:cd05918 209 LDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAAT---VSPVVPSTDPRNIGRPLGAT-CWVVDPD-N 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1888 P---VPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHP-------FREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKV 1957
Cdd:cd05918 284 HdrlVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1958 RGFRIELGEIES-LLNLQTGVKEAIVQPL--GDNQNYHTLVAYVVPHGEWEEKKIIEE-------------------LRS 2015
Cdd:cd05918 364 RGQRVELGEIEHhLRQSLPGAKEVVVEVVkpKDGSSSPQLVAFVVLDGSSSGSGDGDSlflepsdefralvaelrskLRQ 443
|
490 500 510
....*....|....*....|....*....|
gi 497785100 2016 KLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05918 444 RLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
520-1000 |
1.05e-122 |
|
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: 394.70 E-value: 1.05e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIITHSEyktsyegyevpilyidqlddfllderednlnvdcdssQLAYGIYTSGSTGIPKGVLVEHRNLSNYIY 679
Cdd:cd17652 81 ADARPALLLTTPD-------------------------------------NLAYVIYTSGSTGRPKGVVVTHRGLANLAA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 680 AIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSESg 759
Cdd:cd17652 124 AQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPPDD- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 760 tkLFPRKGLILGGEA------SEWSwikeiyrnipASCKLFNHYGPSETTIGVAVYEVTKKGlsnqfSTTPIGSSLSNNR 833
Cdd:cd17652 203 --LPDLRTLVVAGEAcpaelvDRWA----------PGRRMINAYGPTETTVCATMAGPLPGG-----GVPPIGRPVPGTR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 834 IYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITD-SRMYKTGDIGKILYTGEIQFLGRLDGQVKI 912
Cdd:cd17652 266 VYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPgSRMYRTGDLARWRADGQLEFLGRADDQVKI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 913 RGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEE-QLVAYYVSKKE--VLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRH 989
Cdd:cd17652 346 RGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDkRLVAYVVPAPGaaPTAAELRAHLAERLPGYMVPAAFVVLDALPLT 425
|
490
....*....|.
gi 497785100 990 AHGKIDRKALP 1000
Cdd:cd17652 426 PNGKLDRRALP 436
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
49-473 |
1.58e-122 |
|
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: 394.03 E-value: 1.58e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 49 YPLSSIQKQIWFMSQLNPELPIYNEHLIkINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVITKSEP-TIQF 127
Cdd:cd19531 2 LPLSFAQQRLWFLDQLEPGSAAYNIPGA-LRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPlPLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 128 LSLRGISGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYSQN 207
Cdd:cd19531 81 VDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGEDEHVLLLTMHHIVSDGWSMGVLLRELAALYAAFLAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 208 GEINPEqsqeELTIQYHDYALWQEKLLTSENLEKGLEYWKEKLEGDLPMLsiggitqE----------GTGVGSEYNFKI 277
Cdd:cd19531 161 RPSPLP----PLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVL-------ElptdrprpavQSFRGARVRFTL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 278 PNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVIEY 357
Cdd:cd19531 230 PAELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFREL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 358 LQQVHETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLFVMQ-EPPTQFSLPGIKVEYELIPTEVARFPLTLSIIE- 435
Cdd:cd19531 310 LARVRETALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQnAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTEt 389
|
410 420 430
....*....|....*....|....*....|....*...
gi 497785100 436 GEEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSP 473
Cdd:cd19531 390 DGGLRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
520-999 |
3.86e-121 |
|
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: 390.90 E-value: 3.86e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIIThseyktsyegyevpilyidqlddfllderednlnvdcDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIY 679
Cdd:cd17643 81 ADSGPSLLLT-------------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFA 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 680 AIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSES- 758
Cdd:cd17643 124 ATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAAd 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 759 --GTKLFPRKGLILGGEASEWSWIKEIYRNIPASC-KLFNHYGPSETTIGVAVYEVTKKGLSNQfSTTPIGSSLSNNRIY 835
Cdd:cd17643 204 rdGRDPLALRYVIFGGEALEAAMLRPWAGRFGLDRpQLVNMYGITETTVHVTFRPLDAADLPAA-AASPIGRPLPGLRVY 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 836 ILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITD-SRMYKTGDIGKILYTGEIQFLGRLDGQVKIRG 914
Cdd:cd17643 283 VLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPgSRMYRTGDLARRLPDGELEYLGRADEQVKIRG 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 915 IRVEPEEIQSQLLSHPSITEAIVTV-TKVRNEEQLVAYYVSK--KEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAH 991
Cdd:cd17643 363 FRIELGEIEAALATHPSVRDAAVIVrEDEPGDTRLVAYVVADdgAAADIAELRALLKELLPDYMVPARYVPLDALPLTVN 442
|
....*...
gi 497785100 992 GKIDRKAL 999
Cdd:cd17643 443 GKLDRAAL 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
520-999 |
2.56e-120 |
|
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: 389.34 E-value: 2.56e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIITHSEYKTSYEGYEVPILYIDQLDDFLLDEREDNLnvdcDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIY 679
Cdd:cd12116 81 EDAEPALVLTDDALPDRLPAGLPVLLLALAAAAAAPAAPRTPV----SPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 680 AIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSeSG 759
Cdd:cd12116 157 SMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPATWRMLLD-AG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 760 TKlfPRKGLIL--GGEASEwSWIKEiyRNIPASCKLFNHYGPSETTIGVAVYEVTKKGlsnqfSTTPIGSSLSNNRIYIL 837
Cdd:cd12116 236 WQ--GRAGLTAlcGGEALP-PDLAA--RLLSRVGSLWNLYGPTETTIWSTAARVTAAA-----GPIPIGRPLANTQVYVL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 838 DDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITD-SRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIR 916
Cdd:cd12116 306 DAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPgSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHR 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 917 VEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYVSK-KEVLDKD-LQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKI 994
Cdd:cd12116 386 IELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKaGAAPDAAaLRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
....*
gi 497785100 995 DRKAL 999
Cdd:cd12116 466 DRKAL 470
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1070-2146 |
7.41e-120 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 425.74 E-value: 7.41e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1070 EFFEKPSIRELSTHLLQ-LEAVSTH-------------FALSNISEA----------EKEKGIPLSDAQKRMWFLYRMES 1125
Cdd:PRK05691 3196 ERYDEQTIAELAEAYLAeLQALIAHcladgaggltpsdFPLAQLTQAqldalpvpaaEIEDVYPLTPMQEGLLLHTLLEP 3275
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1126 DSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNIDPVQVVLKDLKCTINILDF---DENRSEQDIMNY 1202
Cdd:PRK05691 3276 GTGLYYMQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPIDYLDWrglPEDGQEQRLQAL 3355
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1203 LTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMPIQLEQPVyQYADYVNW 1282
Cdd:PRK05691 3356 HKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYTALGEGREAQLPVPP-RYRDYIGW 3434
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1283 QQNRyteeQINQQLQYWKEQLSGAPSLLELPLDkpRPSMQSYNGSLIRM-------KLPEKHAVLIKEICEEAKVTPYTI 1355
Cdd:PRK05691 3435 LQRQ----DLAQARQWWQDNLRGFERPTPIPSD--RPFLREHAGDSGGMvvgdcytRLDAADGARLRELAQAHQLTVNTF 3508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1356 FLTFFNILLYRYTYQDKILVGTPIANRNIQ--ELEGILGLFVNTLVIPSTVKGD------RNFKSLLQQVNNQI-----L 1422
Cdd:PRK05691 3509 AQAAWALVLRRYSGDRDVLFGVTVAGRPVSmpQMQRTVGLFINSIALRVQLPAAgqrcsvRQWLQGLLDSNMELreyeyL 3588
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1423 GALENQDISferivqELnPERslsyNPIYQVAFTLQNdeqgkngnygglSVEEFEIEWRTSKVDLTLIIGQSKRGFEMV- 1501
Cdd:PRK05691 3589 PLVAIQECS------EL-PKG----QPLFDSLFVFEN------------APVEVSVLDRAQSLNASSDSGRTHTNFPLTa 3645
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1502 -----------MEYNTDLFRQQSIEQMLSDYIKIISQVIENPNMEISRIQLVD-QQHDLLVKKAESQPRSIKDCIQYS-- 1567
Cdd:PRK05691 3646 vcypgddlglhLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGeQERDFLLDGCNRSERDYPLEQSYVrl 3725
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELP 1647
Cdd:PRK05691 3726 FEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLP 3805
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 LNRRDFILKDASVGAIVTQTS-------LEEKLSKSDLPYLCT-DQSQDSEDYSLLTKDKSYPEDIAYIIYTSGTTGTPN 1719
Cdd:PRK05691 3806 AQRLQRIIELSRTPVLVCSAAcreqaraLLDELGCANRPRLLVwEEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPK 3885
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1720 GVMVKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLAD 1799
Cdd:PRK05691 3886 GVMVEQRGMLNNQLSKVPYLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLE 3965
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1800 LPPVVLDSILPED---IPSLQTVSTGGERCPIKVAKRWsLDR----NFYNVYGPTETTIATTWYRVSSPECVQDSVPIGT 1872
Cdd:PRK05691 3966 SVPSLIQGMLAEDrqaLDGLRWMLPTGEAMPPELARQW-LQRypqiGLVNAYGPAECSDDVAFFRVDLASTRGSYLPIGS 4044
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1873 PVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREE-EILYKTGDIGKVLHDGNLEHLGRL 1951
Cdd:PRK05691 4045 PTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPgERLYRTGDLARRRSDGVLEYVGRI 4124
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1952 DHQIKVRGFRIELGEIESLLNLQTGVKEAIVQpLGDNQNYHTLVAYVVPHGEWEEKKII-----EELRSKLPEHMVPSIF 2026
Cdd:PRK05691 4125 DHQVKIRGYRIELGEIEARLHEQAEVREAAVA-VQEGVNGKHLVGYLVPHQTVLAQGALlerikQRLRAELPDYMVPLHW 4203
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2027 VQMEELPRLNNKKVDRHSLPtAVHIFRQQ-KVIQKPVTEEEVVVAECWAETLNlpIDNIGLNSNFFELGGHSLTATQLVA 2105
Cdd:PRK05691 4204 LWLDRLPLNANGKLDRKALP-ALDIGQLQsQAYLAPRNELEQTLATIWADVLK--VERVGVHDNFFELGGHSLLATQIAS 4280
|
1130 1140 1150 1160
....*....|....*....|....*....|....*....|.
gi 497785100 2106 RISELFEIELPIKAIFEYPTIQAILDFIVemklELGGEELD 2146
Cdd:PRK05691 4281 RVQKALQRNVPLRAMFECSTVEELAEYIE----GLAGSAID 4317
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1575-2046 |
2.46e-118 |
|
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: 384.13 E-value: 2.46e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1575 SPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFI 1654
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1655 LKDASVGAIVTQTSLEEKLSKSDLPYLCTDQSQDSEDYSLLTKDKSyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISA 1734
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINN-SDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1735 TIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSILPE--- 1811
Cdd:cd17656 160 EREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEref 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1812 --DIPS-LQTVSTGGERCPI-KVAKRWSLDRN--FYNVYGPTETTIATTwYRVSSPECVQDSVPIGTPVPNTEVFILDPD 1885
Cdd:cd17656 240 inRFPTcVKHIITAGEQLVItNEFKEMLHEHNvhLHNHYGPSETHVVTT-YTINPEAEIPELPPIGKPISNTWIYILDQE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1886 LNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELG 1965
Cdd:cd17656 319 QQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1966 EIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd17656 399 EIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKAL 478
|
.
gi 497785100 2046 P 2046
Cdd:cd17656 479 P 479
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
520-999 |
1.03e-117 |
|
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: 381.04 E-value: 1.03e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSklkaiithseyktsyegyEVPILYIDQLDdfllderednlnvdcdssqLAYGIYTSGSTGIPKGVLVEHRNLSNYIY 679
Cdd:cd17650 81 EDS------------------GAKLLLTQPED-------------------LAYVIYTSGTTGKPKGVMVEHRNVAHAAH 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 680 AIQTK--LGNKPKdRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSE 757
Cdd:cd17650 124 AWRREyeLDSFPV-RLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAY 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 758 ---SGTKLFPRKGLILGGEASEWSWIKEIYRNIPASCKLFNHYGPSETTIGVAVYEVTKKGLSNQfSTTPIGSSLSNNRI 834
Cdd:cd17650 203 vyrNGLDLSAMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDS-ANVPIGRPLPNTAM 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 835 YILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRG 914
Cdd:cd17650 282 YVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRG 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 915 IRVEPEEIQSQLLSHPSITEAIVTVTKVRN-EEQLVAYYVSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGK 993
Cdd:cd17650 362 FRIELGEIESQLARHPAIDEAVVAVREDKGgEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGK 441
|
....*.
gi 497785100 994 IDRKAL 999
Cdd:cd17650 442 VDRRAL 447
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
512-999 |
1.42e-116 |
|
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: 379.31 E-value: 1.42e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESP 591
Cdd:cd17646 4 VAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 592 KERIEIITQDSKLKAIITHS-EYKTSYEGYEVPILyidqLDDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVE 670
Cdd:cd17646 84 ADRLAYMLADAGPAVVLTTAdLAARLPAGGDVALL----GDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 671 HRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIvqgkaIDWYKIT--- 747
Cdd:cd17646 160 HAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAAL-----IREHGVTtch 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 748 --PSHLKAL----SSESGTKLfprKGLILGGEASEWSWIKEIYRNIPASckLFNHYGPSETTIGVAVYEVTKKGLSnqfS 821
Cdd:cd17646 235 fvPSMLRVFlaepAAGSCASL---RRVFCSGEALPPELAARFLALPGAE--LHNLYGPTEAAIDVTHWPVRGPAET---P 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 822 TTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKILYTGEIQ 901
Cdd:cd17646 307 SVPIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 902 FLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEE-QLVAYYVSKKEVLDKD---LQTYLKQKLPPNLVP 977
Cdd:cd17646 387 FLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAaRLVGYVVPAAGAAGPDtaaLRAHLAERLPEYMVP 466
|
490 500
....*....|....*....|..
gi 497785100 978 AYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd17646 467 AAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1568-2045 |
1.89e-115 |
|
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: 374.35 E-value: 1.89e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELP 1647
Cdd:cd12115 5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 LNRRDFILKDASVGAIVTQtsleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSS 1727
Cdd:cd12115 85 PERLRFILEDAQARLVLTD-----------------------------------PDDLAYVIYTSGSTGRPKGVAIEHRN 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1728 VMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSreeqlSTKALVKRFRDWNVTLADLPPVVLDS 1807
Cdd:cd12115 130 AAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEVTLINTVPSAAAE 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1808 ILPED-IP-SLQTVSTGGERCP----IKVAKRWSLDRnFYNVYGPTETTIATTWYRVssPECVQDSVPIGTPVPNTEVFI 1881
Cdd:cd12115 205 LLRHDaLPaSVRVVNLAGEPLPrdlvQRLYARLQVER-VVNLYGPSEDTTYSTVAPV--PPGASGEVSIGRPLANTQAYV 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1882 LDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFR 1961
Cdd:cd12115 282 LDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFR 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1962 IELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKI--IEELRSKLPEHMVPSIFVQMEELPRLNNKK 2039
Cdd:cd12115 362 IELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLVEdlRRHLGTRLPAYMVPSRFVRLDALPLTPNGK 441
|
....*.
gi 497785100 2040 VDRHSL 2045
Cdd:cd12115 442 IDRSAL 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1568-2046 |
8.71e-115 |
|
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: 372.27 E-value: 8.71e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELP 1647
Cdd:cd17645 4 FEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 LNRRDFILKDASVGAIVTQtsleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSS 1727
Cdd:cd17645 84 GERIAYMLADSSAKILLTN-----------------------------------PDDLAYVIYTSGSTGLPKGVMIEHHN 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1728 VMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDS 1807
Cdd:cd17645 129 LVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGITISFLPTGAAEQ 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1808 ILPEDIPSLQTVSTGGERCPIKVAKRWSLdrnfYNVYGPTETTIATTWYRVSSPEcvqDSVPIGTPVPNTEVFILDPDLN 1887
Cdd:cd17645 209 FMQLDNQSLRVLLTGGDKLKKIERKGYKL----VNNYGPTENTVVATSFEIDKPY---ANIPIGKPIDNTRVYILDEALQ 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1888 PVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEI 1967
Cdd:cd17645 282 LQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEI 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497785100 1968 ESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSLP 2046
Cdd:cd17645 362 EPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
520-1000 |
1.06e-114 |
|
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: 372.47 E-value: 1.06e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIITHseyktsyegyevpilyidqlddfllderednlnvdcDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIY 679
Cdd:cd17649 81 EDSGAGLLLTH------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQ 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 680 AIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSE-- 757
Cdd:cd17649 125 ATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEad 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 758 -SGTKLFPR-KGLILGGEAsewsWIKEIYRNI-PASCKLFNHYGPSETTIGVAVYEVtKKGLSNQFSTTPIGSSLSNNRI 834
Cdd:cd17649 205 rTGDGRPPSlRLYIFGGEA----LSPELLRRWlKAPVRLFNAYGPTEATVTPLVWKC-EAGAARAGASMPIGRPLGGRSA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 835 YILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITD-SRMYKTGDIGKILYTGEIQFLGRLDGQVKIR 913
Cdd:cd17649 280 YILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPgSRLYRTGDLARWRDDGVIEYLGRVDHQVKIR 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 914 GIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYVSKK----EVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRH 989
Cdd:cd17649 360 GFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAaaaqPELRAQLRTALRASLPDYMVPAHLVFLARLPLT 439
|
490
....*....|.
gi 497785100 990 AHGKIDRKALP 1000
Cdd:cd17649 440 PNGKLDRKALP 450
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
508-1000 |
1.35e-114 |
|
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: 372.92 E-value: 1.35e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 508 IHVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLD 587
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 588 VESPKERIEIITQDSKLKAIITHSEyktsyegyevpilyidqlddfllderednlnvdcdssQLAYGIYTSGSTGIPKGV 667
Cdd:cd17644 82 PNYPQERLTYILEDAQISVLLTQPE-------------------------------------NLAYVIYTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 668 LVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKIT 747
Cdd:cd17644 125 MIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 748 PSHLKALSSESGTKLFPR----KGLILGGEA---SEWSWIKEIYRNIPascKLFNHYGPSETTIGVAVYEVTKKGlSNQF 820
Cdd:cd17644 205 PAYWHLLVLELLLSTIDLpsslRLVIVGGEAvqpELVRQWQKNVGNFI---QLINVYGPTEATIAATVCRLTQLT-ERNI 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 821 STTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFI--TDSRMYKTGDIGKILYTG 898
Cdd:cd17644 281 TSVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNssESERLYKTGDLARYLPDG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 899 EIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTK-VRNEEQLVAYYVSKKEV--LDKDLQTYLKQKLPPNL 975
Cdd:cd17644 361 NIEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREdQPGNKRLVAYIVPHYEEspSTVELRQFLKAKLPDYM 440
|
490 500
....*....|....*....|....*
gi 497785100 976 VPAYLVKMDTLPRHAHGKIDRKALP 1000
Cdd:cd17644 441 IPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
519-1000 |
2.63e-114 |
|
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: 372.58 E-value: 2.63e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEII 598
Cdd:cd17656 1 TPDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAIITHSEYKTSYEgYEVPILYIDqlDDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYI 678
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLS-FNKSTILLE--DPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 679 YAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSES 758
Cdd:cd17656 158 HFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSER 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 759 GTK-LFPR--KGLILGGEASEWS-WIKEIYRNipASCKLFNHYGPSETTIgVAVYEVTKKGLSNQFSttPIGSSLSNNRI 834
Cdd:cd17656 238 EFInRFPTcvKHIITAGEQLVITnEFKEMLHE--HNVHLHNHYGPSETHV-VTTYTINPEAEIPELP--PIGKPISNTWI 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 835 YILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRG 914
Cdd:cd17656 313 YILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRG 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 915 IRVEPEEIQSQLLSHPSITEAIVTVTKVRN-EEQLVAYYVSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGK 993
Cdd:cd17656 393 YRIELGEIEAQLLNHPGVSEAVVLDKADDKgEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGK 472
|
....*..
gi 497785100 994 IDRKALP 1000
Cdd:cd17656 473 VDRKALP 479
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1576-2045 |
1.08e-113 |
|
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: 369.49 E-value: 1.08e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQtsleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISAT 1735
Cdd:cd17650 81 EDSGAKLLLTQ-----------------------------------PEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1736 IDEFNI-TQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSILPE--- 1811
Cdd:cd17650 126 RREYELdSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYvyr 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1812 ---DIPSLQTVSTGGERCPIKvAKRWSLDR-----NFYNVYGPTETTIATTWYRVS-SPECVQDSVPIGTPVPNTEVFIL 1882
Cdd:cd17650 206 nglDLSAMRLLIVGSDGCKAQ-DFKTLAARfgqgmRIINSYGVTEATIDSTYYEEGrDPLGDSANVPIGRPLPNTAMYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1883 DPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRI 1962
Cdd:cd17650 285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1963 ELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDR 2042
Cdd:cd17650 365 ELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444
|
...
gi 497785100 2043 HSL 2045
Cdd:cd17650 445 RAL 447
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1104-1544 |
5.44e-112 |
|
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: 364.73 E-value: 5.44e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1104 KEKGIPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNIDPVQVVLKDLKC 1183
Cdd:pfam00668 1 VQDEYPLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVILEERPF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1184 TINILDF---DENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQ 1260
Cdd:pfam00668 81 ELEIIDIsdlSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1261 IISNMPIQLeQPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAVL 1340
Cdd:pfam00668 161 LLKGEPLPL-PPKTPYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEEL 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1341 IKEICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQ 1420
Cdd:pfam00668 240 LRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQED 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1421 ILGALENQDISFERIVQELNPERSLSYNPIYQVAFTLQND------EQGKNGNYGGLSVEEFEIEwrTSKVDLTLIIGQS 1494
Cdd:pfam00668 320 LLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYlgqdsqEEEFQLSELDLSVSSVIEE--EAKYDLSLTASER 397
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 497785100 1495 KRGFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENPNMEISRIQLVDQ 1544
Cdd:pfam00668 398 GGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSD 447
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1576-2042 |
1.22e-110 |
|
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: 361.97 E-value: 1.22e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQTSLEEKLSKSDLPYLCTDQSQDSEDysLLTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISAT 1735
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPA--PPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1736 IDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSIL------ 1809
Cdd:cd12114 159 NRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLdvleaa 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1810 PEDIPSLQTVSTGGERCPI----KVAKRWSlDRNFYNVYGPTETTIATTWYRVSSPECVQDSVPIGTPVPNTEVFILDPD 1885
Cdd:cd12114 239 QALLPSLRLVLLSGDWIPLdlpaRLRALAP-DARLISLGGATEASIWSIYHPIDEVPPDWRSIPYGRPLANQRYRVLDPR 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1886 LNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPfrEEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELG 1965
Cdd:cd12114 318 GRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELG 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1966 EIESLLNLQTGVKEAIVQPLGDNqNYHTLVAYVVPHGEWEEKKII---EELRSKLPEHMVPSIFVQMEELPRLNNKKVDR 2042
Cdd:cd12114 396 EIEAALQAHPGVARAVVVVLGDP-GGKRLAAFVVPDNDGTPIAPDalrAFLAQTLPAYMIPSRVIALEALPLTANGKVDR 474
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
49-1112 |
2.44e-110 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 395.31 E-value: 2.44e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 49 YPLSSIQKQIWFMSQLNPELPIYN-EHLIKINlsGKVNIEALKKSFEQIVNRHQILRMR-VKQTEDSIEQVITKSEPT-I 125
Cdd:PRK05691 3258 YPLTPMQEGLLLHTLLEPGTGLYYmQDRYRIN--SALDPERFAQAWQAVVARHEALRASfSWNAGETMLQVIHKPGRTpI 3335
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 126 QFLSLRGISGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSElerFYNMYS 205
Cdd:PRK05691 3336 DYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMND---FFEIYT 3412
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 206 QNGEinPEQSQEELTIQYHDYALWqeklLTSENLEKGLEYWKEKLEG---------DLPMLSIGGITQEGTGVGSEYNfK 276
Cdd:PRK05691 3413 ALGE--GREAQLPVPPRYRDYIGW----LQRQDLAQARQWWQDNLRGferptpipsDRPFLREHAGDSGGMVVGDCYT-R 3485
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 277 IPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIR--ETRNVIGPFINTVVIRTK---AEQN 351
Cdd:PRK05691 3486 LDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRPVSmpQMQRTVGLFINSIALRVQlpaAGQR 3565
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 352 LSVIEYLQQVHETTIQALENQDVPfekVVEVLNPNRDVRANPFYQLLFVMQEPPTQFSL----PGIKVEYELIPTEVaRF 427
Cdd:PRK05691 3566 CSVRQWLQGLLDSNMELREYEYLP---LVAIQECSELPKGQPLFDSLFVFENAPVEVSVldraQSLNASSDSGRTHT-NF 3641
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 428 PLTLSIIEGEEMIGRVLYRTSILSEYEVQSFV---QRLLQVadeIVQSPHQRIYDLNLLTSKERSESAYLYNQSGcKPFP 504
Cdd:PRK05691 3642 PLTAVCYPGDDLGLHLSYDQRYFDAPTVERLLgefKRLLLA---LVQGFHGDLSELPLLGEQERDFLLDGCNRSE-RDYP 3717
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 505 TEPIHV-QFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAY 583
Cdd:PRK05691 3718 LEQSYVrLFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGY 3797
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 584 LPLDVESPKERIEIITQDSKLKAIIThseyktSYEGYEVPILYIDQLDDF----LL--------DEREDNLNVDCDSSQL 651
Cdd:PRK05691 3798 LPLDPGLPAQRLQRIIELSRTPVLVC------SAACREQARALLDELGCAnrprLLvweevqagEVASHNPGIYSGPDNL 3871
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 652 AYGIYTSGSTGIPKGVLVEHRNLSNyiyaiqTKLGNKPkdrYLLLQ---------SLAYDFCLTTIYTSLLSGGTLFFLL 722
Cdd:PRK05691 3872 AYVIYTSGSTGLPKGVMVEQRGMLN------NQLSKVP---YLALSeadviaqtaSQSFDISVWQFLAAPLFGARVEIVP 3942
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 723 KEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSESGTKLFPRKGLILGGEA------SEWSwikEIYRNIpascKLFNH 796
Cdd:PRK05691 3943 NAIAHDPQGLLAHVQAQGITVLESVPSLIQGMLAEDRQALDGLRWMLPTGEAmppelaRQWL---QRYPQI----GLVNA 4015
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 797 YGPSETTIGVAVYEVTKKglSNQFSTTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFME 876
Cdd:PRK05691 4016 YGPAECSDDVAFFRVDLA--STRGSYLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVP 4093
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 877 DPFIT-DSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYVSK 955
Cdd:PRK05691 4094 HPFGApGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVPH 4173
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 956 KEVLDKD-----LQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEIQVSNWNEIEIQ-PMNRLEEKMKDVWEKI 1029
Cdd:PRK05691 4174 QTVLAQGallerIKQRLRAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIGQLQSQAYLaPRNELEQTLATIWADV 4253
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1030 LERPVPSIDDSFFKLGGHSLLATRLVSMIRKEFKVELSIKEFFEKPSIRELSTHLLQLEAvsthfalsniSEAEKEKGIP 1109
Cdd:PRK05691 4254 LKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAG----------SAIDEQKVDR 4323
|
...
gi 497785100 1110 LSD 1112
Cdd:PRK05691 4324 LSD 4326
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
508-999 |
2.53e-110 |
|
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: 359.71 E-value: 2.53e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 508 IHVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLD 587
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 588 VESPKERIEIITQDSKLKAIIThseyktsyegyevpilyidqlddfllderednlnvdcDSSQLAYGIYTSGSTGIPKGV 667
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT-------------------------------------DPDDLAYVIYTSGSTGRPKGV 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 668 LVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFflLKEDAID----------------PAK 731
Cdd:cd12115 124 AIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELFGPLATGGKVV--LADNVLAlpdlpaaaevtlintvPSA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 732 VEEIVQGKAIdwykitPSHLKALSsesgtklfprkgliLGGEASEWSWIKEIYRNIPASCkLFNHYGPSETTIGVAVYEV 811
Cdd:cd12115 202 AAELLRHDAL------PASVRVVN--------------LAGEPLPRDLVQRLYARLQVER-VVNLYGPSEDTTYSTVAPV 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 812 TKKGLSnqfsTTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDSRMYKTGDI 891
Cdd:cd12115 261 PPGASG----EVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDL 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 892 GKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTK-VRNEEQLVAYYVSK--KEVLDKDLQTYLK 968
Cdd:cd12115 337 VRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGdAAGERRLVAYIVAEpgAAGLVEDLRRHLG 416
|
490 500 510
....*....|....*....|....*....|.
gi 497785100 969 QKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd12115 417 TRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
1108-1532 |
6.82e-110 |
|
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: 357.73 E-value: 6.82e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1108 IPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNIdPVQVVLKDLKCTINI 1187
Cdd:cd19538 2 IPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGV-PYQLILEEDEATPKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1188 LDFDENRSEQDimNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMPI 1267
Cdd:cd19538 81 EIKEVDEEELE--SEINEAVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1268 QLEQPVYQYADYVNWQQN-----RYTEEQINQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEK-HAVLI 1341
Cdd:cd19538 159 ELAPLPVQYADYALWQQEllgdeSDPDSLIARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSElHQQLL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1342 KeICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQI 1421
Cdd:cd19538 239 Q-LAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1422 LGALENQDISFERIVQELNPERSLSYNPIYQVAFTLQNDEQGKngnyggLSVEEFEIEWR-----TSKVDLTLIIGQSKR 1496
Cdd:cd19538 318 LEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPS------LDLPGLEAKLElrtvgSAKFDLTFELREQYN 391
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 497785100 1497 -----GFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENP 1532
Cdd:cd19538 392 dgtpnGIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
509-1000 |
1.18e-108 |
|
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: 354.55 E-value: 1.18e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 509 HVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDV 588
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 589 ESPKERIEIITQDSKLKAIIThseyktsyegyevpilyidqlddfllderednlnvdcDSSQLAYGIYTSGSTGIPKGVL 668
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLT-------------------------------------NPDDLAYVIYTSGSTGLPKGVM 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 669 VEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIdwykiTP 748
Cdd:cd17645 124 IEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGI-----TI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 749 SHLKALSSESGTKL--FPRKGLILGGEAsewswIKEIYRNipaSCKLFNHYGPSETTIGVAVYEVTKkglsnQFSTTPIG 826
Cdd:cd17645 199 SFLPTGAAEQFMQLdnQSLRVLLTGGDK-----LKKIERK---GYKLVNNYGPTENTVVATSFEIDK-----PYANIPIG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 827 SSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKILYTGEIQFLGRL 906
Cdd:cd17645 266 KPIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 907 DGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQ-LVAYYVSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDT 985
Cdd:cd17645 346 DQQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKyLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKA 425
|
490
....*....|....*
gi 497785100 986 LPRHAHGKIDRKALP 1000
Cdd:cd17645 426 LPLTANGKVDRKALP 440
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1572-2045 |
1.24e-108 |
|
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: 355.02 E-value: 1.24e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1572 VRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRR 1651
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1652 DFILKDASVGAIVTQtsleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNL 1731
Cdd:cd05945 81 REILDAAKPALLIAD-----------------------------------GDDNAYIIFTSGSTGRPKGVQISHDNLVSF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1732 ISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVT-------LADLPpVV 1804
Cdd:cd05945 126 TNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITvwvstpsFAAMC-LL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1805 LDSILPEDIPSLQTVSTGGERCPIKVAKRWSL---DRNFYNVYGPTETTIATTWYRVSSPECVQ-DSVPIGTPVPNTEVF 1880
Cdd:cd05945 205 SPTFTPESLPSLRHFLFCGEVLPHKTARALQQrfpDARIYNTYGPTEATVAVTYIEVTPEVLDGyDRLPIGYAKPGAKLV 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1881 ILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREeeiLYKTGDIGKVLHDGNLEHLGRLDHQIKVRGF 1960
Cdd:cd05945 285 ILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQR---AYRTGDLVRLEADGLLFYRGRLDFQVKLNGY 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1961 RIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIE---ELRSKLPEHMVPSIFVQMEELPRLNN 2037
Cdd:cd05945 362 RIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGLTKAikaELAERLPPYMIPRRFVYLDELPLNAN 441
|
....*...
gi 497785100 2038 KKVDRHSL 2045
Cdd:cd05945 442 GKIDRKAL 449
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
508-999 |
7.34e-108 |
|
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: 354.16 E-value: 7.34e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 508 IHVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLD 587
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 588 VESPKERIEIITQDSKLKAIITHseyktsyegyevpilyidqlddfllderednlnvdcDSSQLAYGIYTSGSTGIPKGV 667
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTS------------------------------------SPSDAAYVIFTSGSTGKPKGV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 668 LVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDpaKVEEIVQGKAIDWYKIT 747
Cdd:cd05918 125 VIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLN--DLAGFINRLRVTWAFLT 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 748 PSHLKALSSESgtklFPR-KGLILGGEASEWS----WIKeiyrnipaSCKLFNHYGPSETTIGVAVYEVTKkglsnqfST 822
Cdd:cd05918 203 PSVARLLDPED----VPSlRTLVLGGEALTQSdvdtWAD--------RVRLINAYGPAECTIAATVSPVVP-------ST 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 823 TP--IGSSLsNNRIYILD--DKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDP-------FITDSRMYKTGDI 891
Cdd:cd05918 264 DPrnIGRPL-GATCWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDL 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 892 GKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSH-PSITEAIVTVTKVRN---EEQLVAYYVSKKEVLD------- 960
Cdd:cd05918 343 VRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQSlPGAKEVVVEVVKPKDgssSPQLVAFVVLDGSSSGsgdgdsl 422
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 497785100 961 ------------KDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05918 423 flepsdefralvAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
512-999 |
6.72e-106 |
|
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: 346.60 E-value: 6.72e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESP 591
Cdd:cd17653 3 FERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 592 KERIEIITQDSKLKAIIthseyktsyegyevpilYIDQLDDfllderednlnvdcdssqLAYGIYTSGSTGIPKGVLVEH 671
Cdd:cd17653 83 SARIQAILRTSGATLLL-----------------TTDSPDD------------------LAYIIFTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 672 RNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLffLLKEDAIDPAKVeeivqGKAIDWYKITPSHL 751
Cdd:cd17653 128 RGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTL--VLADPSDPFAHV-----ARTVDALMSTPSIL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 752 KALSSESgtklFPR-KGLILGGEA------SEWSWIKEIYrnipascklfNHYGPSETTIGVAVYEVTKKglsnqfSTTP 824
Cdd:cd17653 201 STLSPQD----FPNlKTIFLGGEAvppsllDRWSPGRRLY----------NAYGPTECTISSTMTELLPG------QPVT 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 825 IGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKILYTGEIQFLG 904
Cdd:cd17653 261 IGKPIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 905 RLDGQVKIRGIRVEPEEIQSQ-LLSHPSITEAIVTVTkvrnEEQLVAYYVSkkEVLDKD-LQTYLKQKLPPNLVPAYLVK 982
Cdd:cd17653 341 REDNQVKVRGFRINLEEIEEVvLQSQPEVTQAAAIVV----NGRLVAFVTP--ETVDVDgLRSELAKHLPSYAVPDRIIA 414
|
490
....*....|....*..
gi 497785100 983 MDTLPRHAHGKIDRKAL 999
Cdd:cd17653 415 LDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
520-999 |
1.04e-105 |
|
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: 347.72 E-value: 1.04e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIITHSEYKtsyegYEVPILYIDQLDDFLLDERED-NLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYI 678
Cdd:cd12114 81 ADAGARLVLTDGPDA-----QLDVAVFDVLILDLDALAAPApPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 679 YAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSES 758
Cdd:cd12114 156 LDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 759 GTKLFPRKGL---ILGGEasewsWIKEI----YRNIPASCKLFNHYGPSETTIGVAVYEVTKkgLSNQFSTTPIGSSLSN 831
Cdd:cd12114 236 EAAQALLPSLrlvLLSGD-----WIPLDlparLRALAPDARLISLGGATEASIWSIYHPIDE--VPPDWRSIPYGRPLAN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 832 NRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPfiTDSRMYKTGDIGKILYTGEIQFLGRLDGQVK 911
Cdd:cd12114 309 QRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 912 IRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYVSKKEV---LDKDLQTYLKQKLPPNLVPAYLVKMDTLPR 988
Cdd:cd12114 387 VRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGtpiAPDALRAFLAQTLPAYMIPSRVIALEALPL 466
|
490
....*....|.
gi 497785100 989 HAHGKIDRKAL 999
Cdd:cd12114 467 TANGKVDRAAL 477
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1568-1958 |
2.02e-104 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 341.60 E-value: 2.02e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIAL-RFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSEL 1646
Cdd:pfam00501 1 LERQAARTPDKTALeVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1647 PLNRRDFILKDASVGAIVTQTSLEEKLSKSDLPY-------LCTDQSQDSEDYSLLTKDKSY-----------PEDIAYI 1708
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELLEALGKlevvklvLVLDRDPVLKEEPLPEEAKPAdvppppppppdPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1709 IYTSGTTGTPNGVMVKHSSVMNLISA----TIDEFNITQETKVGQFATISFDASL-WQILMALLAGATLCVVSREEQLST 1783
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSikrvRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1784 KALVKRFRDWNVTLADLPPVVLDSIL------PEDIPSLQTVSTGGERCPIKVAKRWS--LDRNFYNVYGPTETTIATTW 1855
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLeagapkRALLSSLRLVLSGGAPLPPELARRFRelFGGALVNGYGLTETTGVVTT 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1856 yRVSSPECVQDSVPIGTPVPNTEVFILDPD-LNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFreeeilYKTG 1934
Cdd:pfam00501 321 -PLPLDEDLRSLGSVGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDEDGW------YRTG 393
|
410 420
....*....|....*....|....
gi 497785100 1935 DIGKVLHDGNLEHLGRLDHQIKVR 1958
Cdd:pfam00501 394 DLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1576-2046 |
1.39e-103 |
|
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: 340.53 E-value: 1.39e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGD-RVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFI 1654
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRPDdLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1655 LKDASVGAIVTQtsleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISA 1734
Cdd:cd17648 81 LEDTGARVVITN-----------------------------------STDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1735 TIDEFNITQET--KVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSILPED 1812
Cdd:cd17648 126 LSERYFGRDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDLAR 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1813 IPSLQTVSTGGE--RCPIKVAKRWSLDRNFYNVYGPTETTIATTWYRVSSPECVQDSvpIGTPVPNTEVFILDPDLNPVP 1890
Cdd:cd17648 206 LPHLKRVDAAGEefTAPVFEKLRSRFAGLIINAYGPTETTVTNHKRFFPGDQRFDKS--LGRPVRNTKCYVLNDAMKRVP 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1891 MGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEE--------ILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRI 1962
Cdd:cd17648 284 VGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnaRLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRI 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1963 ELGEIESLLNLQTGVKEAIVQPLGDNQNYHT-----LVAYVVPH-GEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLN 2036
Cdd:cd17648 364 EPGEVEAALASYPGVRECAVVAKEDASQAQSriqkyLVGYYLPEpGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTI 443
|
490
....*....|
gi 497785100 2037 NKKVDRHSLP 2046
Cdd:cd17648 444 NGKLDVRALP 453
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
1108-1532 |
3.62e-103 |
|
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: 338.63 E-value: 3.62e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1108 IPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESkniD--PVQVVLkdlkcti 1185
Cdd:cd19540 2 IPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPED---DggPYQVVL------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1186 nilDFDENR--------SEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAI 1257
Cdd:cd19540 72 ---PAAEARpdltvvdvTEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATA 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1258 Y------HQiisnmPIQLEQPVyQYADYVNWQQNRYTEEQ-----INQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNG 1326
Cdd:cd19540 149 YaarragRA-----PDWAPLPV-QYADYALWQRELLGDEDdpdslAARQLAYWRETLAGLPEELELPTDRPRPAVASYRG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1327 SLIRMKLP-EKHAVLiKEICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVK 1405
Cdd:cd19540 223 GTVEFTIDaELHARL-AALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVS 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1406 GDRNFKSLLQQVNNQILGALENQDISFERIVQELNPERSLSYNPIYQVAFTLQNDEQGKnGNYGGLSVEEFEIEWRTSKV 1485
Cdd:cd19540 302 GDPTFAELLARVRETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAAT-LELPGLTVEPVPVDTGVAKF 380
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 497785100 1486 DLTLIIGQSK------RGFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENP 1532
Cdd:cd19540 381 DLSFTLTERRdadgapAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
520-1000 |
1.49e-102 |
|
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: 337.45 E-value: 1.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGK-EDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEII 598
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAIIThseyktsyegyevpilyidqlddfllderednlnvdcDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYI 678
Cdd:cd17648 81 LEDTGARVVIT-------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLR 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 679 YAIQTKLG--NKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSS 756
Cdd:cd17648 124 TSLSERYFgrDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYDL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 757 ESGTKLfprKGLILGGEASEWSWIKEIYRNIPAscKLFNHYGPSETTigvaVYEVTKKGLSNQFSTTPIGSSLSNNRIYI 836
Cdd:cd17648 204 ARLPHL---KRVDAAGEEFTAPVFEKLRSRFAG--LIINAYGPTETT----VTNHKRFFPGDQRFDKSLGRPVRNTKCYV 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 837 LDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITD--------SRMYKTGDIGKILYTGEIQFLGRLDG 908
Cdd:cd17648 275 LNDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEqerargrnARLYKTGDLVRWLPSGELEYLGRNDF 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 909 QVKIRGIRVEPEEIQSQLLSHPSITEAIV------TVTKVRNEEQLVAYYVSKKEVLDK-DLQTYLKQKLPPNLVPAYLV 981
Cdd:cd17648 355 QVKIRGQRIEPGEVEAALASYPGVRECAVvakedaSQAQSRIQKYLVGYYLPEPGHVPEsDLLSFLRAKLPRYMVPARLV 434
|
490
....*....|....*....
gi 497785100 982 KMDTLPRHAHGKIDRKALP 1000
Cdd:cd17648 435 RLEGIPVTINGKLDVRALP 453
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1568-2045 |
1.07e-100 |
|
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: 332.16 E-value: 1.07e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELP 1647
Cdd:COG0318 5 LRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 LNRRDFILKDASVGAIVTqtsleeklsksdlpylctdqsqdsedyslltkdksypediAYIIYTSGTTGTPNGVMVKHSS 1727
Cdd:COG0318 85 AEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVMLTHRN 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1728 VMNLISATIDEFNITQETKVGQFATISFDASL-WQILMALLAGATLCVVSReeqLSTKALVKRFRDWNVTLADLPPVVLD 1806
Cdd:COG0318 125 LLANAAAIAAALGLTPGDVVLVALPLFHVFGLtVGLLAPLLAGATLVLLPR---FDPERVLELIERERVTVLFGVPTMLA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1807 SIL------PEDIPSLQTVSTGGERCPIKVAKRWS--LDRNFYNVYGPTETTIATTwyrvSSPECVQDSVP--IGTPVPN 1876
Cdd:COG0318 202 RLLrhpefaRYDLSSLRLVVSGGAPLPPELLERFEerFGVRIVEGYGLTETSPVVT----VNPEDPGERRPgsVGRPLPG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1877 TEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiPHPFreeeilYKTGDIGKVLHDGNLEHLGRLDHQIK 1956
Cdd:COG0318 278 VEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW------LRTGDLGRLDEDGYLYIVGRKKDMII 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1957 VRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKI--IEELRSKLPEHMVPSIFVQMEELPR 2034
Cdd:COG0318 351 SGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGERVVAFVVLRPGAELDAEelRAFLRERLARYKVPRRVEFVDELPR 430
|
490
....*....|.
gi 497785100 2035 LNNKKVDRHSL 2045
Cdd:COG0318 431 TASGKIDRRAL 441
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
519-999 |
2.88e-96 |
|
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes D-alanyl carrier protein ligase DltA and aliphatic beta-amino acid adenylation enzymes IdnL1 and CmiS6. DltA incorporates D-ala in techoic acids in gram-positive bacteria via a two-step process, starting with adenylation of D-alanine that transfers D-alanine to the D-alanyl carrier protein. IdnL1, a short-chain aliphatic beta-amino acid adenylation enzyme, recognizes 3-aminobutanoic acid, and is involved in the synthesis of the macrolactam antibiotic incednine. CmiS6 is a medium-chain beta-amino acid adenylation enzyme that recognizes 3-aminononanoic acid, and is involved in the synthesis of cremimycin, also a macrolactam antibiotic. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341267 [Multi-domain] Cd Length: 449 Bit Score: 319.19 E-value: 2.88e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEII 598
Cdd:cd05945 4 NPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAIIThseyktsyegyevpilyidqlddfllderednlnvdcDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYI 678
Cdd:cd05945 84 LDAAKPALLIA-------------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSFT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 679 YAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAK-VEEIVQGKAIDWYKiTPS--HLKALS 755
Cdd:cd05945 127 NWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQlFRFLAEHGITVWVS-TPSfaAMCLLS 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 756 SESGTKLFPR-KGLILGGEASEWSWIKEIYRNIPAsCKLFNHYGPSETTIGVAVYEVTKKgLSNQFSTTPIGSSLSNNRI 834
Cdd:cd05945 206 PTFTPESLPSlRHFLFCGEVLPHKTARALQQRFPD-ARIYNTYGPTEATVAVTYIEVTPE-VLDGYDRLPIGYAKPGAKL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 835 YILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPfitDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRG 914
Cdd:cd05945 284 VILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE---GQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNG 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 915 IRVEPEEIQSQLLSHPSITEAIVTVTKVRN-EEQLVAYYVSKKEV---LDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHA 990
Cdd:cd05945 361 YRIELEEIEAALRQVPGVKEAVVVPKYKGEkVTELIAFVVPKPGAeagLTKAIKAELAERLPPYMIPRRFVYLDELPLNA 440
|
....*....
gi 497785100 991 HGKIDRKAL 999
Cdd:cd05945 441 NGKIDRKAL 449
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
46-488 |
2.83e-90 |
|
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: 302.33 E-value: 2.83e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 46 RGSYPLSSIQKQIWFMSQLNPELPIYNEHLIkINLSGKVNIEALKKSFEQIVNRHQILRMR-VKQTEDSIEQVITKSEP- 123
Cdd:pfam00668 2 QDEYPLSPAQKRMWFLEKLEPHSSAYNMPAV-LKLTGELDPERLEKALQELINRHDALRTVfIRQENGEPVQVILEERPf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 124 TIQFLSLRGISGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNM 203
Cdd:pfam00668 81 ELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 204 YSQNGEINPEQSQeeltiQYHDYALWQEKLLTSENLEKGLEYWKEKLEGDLPMLSIGGIT---QEGTGVGSEYNFKIPNI 280
Cdd:pfam00668 161 LLKGEPLPLPPKT-----PYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYarpADRSFKGDRLSFTLDED 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 281 LTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVIEYLQQ 360
Cdd:pfam00668 236 TEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKR 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 361 VHETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLFVMQEPPTQ------FSLPGIKVEYELIPTEVARFPLTLSII 434
Cdd:pfam00668 316 VQEDLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLGQdsqeeeFQLSELDLSVSSVIEEEAKYDLSLTAS 395
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 435 EGEEMIG-RVLYRTSILSEYEVQSFVQRLLQVADEIVQSPHQRIYDLNLLTSKER 488
Cdd:pfam00668 396 ERGGGLTiKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEK 450
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
50-473 |
5.25e-85 |
|
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: 286.08 E-value: 5.25e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 50 PLSSIQKQIWFMSQLNPELPIYNEHLIkINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVI-TKSEPTIQFL 128
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSATYNIPLV-IKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLIlEEDEATPKLE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 129 SLRgISGEEQQEILSEycrkEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYSQNG 208
Cdd:cd19538 82 IKE-VDEEELESEINE----AVRYPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRARCKGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 209 EInpeqSQEELTIQYHDYALWQEKLLTSEN-----LEKGLEYWKEKLEG--DLPMLSIGGITQEGTGV-GSEYNFKIPNI 280
Cdd:cd19538 157 AP----ELAPLPVQYADYALWQQELLGDESdpdslIARQLAYWKKQLAGlpDEIELPTDYPRPAESSYeGGTLTFEIDSE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 281 LTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVIEYLQQ 360
Cdd:cd19538 233 LHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLER 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 361 VHETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLFVMQEPPT-QFSLPGIKVEYELIPTEVARFPLTLSIIEGEE- 438
Cdd:cd19538 313 VKETNLEAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQpSLDLPGLEAKLELRTVGSAKFDLTFELREQYNd 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 497785100 439 -----MIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSP 473
Cdd:cd19538 393 gtpngIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1108-1532 |
2.37e-84 |
|
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: 284.27 E-value: 2.37e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1108 IPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNIDPVQVVL--KDLKCTI 1185
Cdd:cd19539 2 IPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILppGPAPLEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1186 NILDFDENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNM 1265
Cdd:cd19539 82 RDLSDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1266 PIQLEQPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGApSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAVLIKEIC 1345
Cdd:cd19539 162 AAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGA-EPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1346 EEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGAL 1425
Cdd:cd19539 241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1426 ENQDISFERIVQELNPERSLSYNPIYQVAFTLQNDEQGKNGNYGGLSVEEFEIEWRTSKVDLTLIIGQSKRGFEMVMEYN 1505
Cdd:cd19539 321 RHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYA 400
|
410 420
....*....|....*....|....*..
gi 497785100 1506 TDLFRQQSIEQMLSDYIKIISQVIENP 1532
Cdd:cd19539 401 TSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
1299-2147 |
8.88e-84 |
|
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: 304.68 E-value: 8.88e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1299 WKEQLSgAPSLLELPLDKPRPSMQSYNGSLIRMKLPEKhavlikEICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTP 1378
Cdd:TIGR03443 2 WSERLD-NPTLSVLPHDYLRPANNRLVEATYSLQLPSA------EVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1379 IANRNiqelegilglfvNTLVIPSTVKGDRNFKSLLQQVNNQILGALENQDISFERIVQELNPERSLSYNP-IYQVAFTL 1457
Cdd:TIGR03443 75 SNKSG------------RPFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAFQD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1458 QNDEQGKNGNYGglsveefeiewrtSKVDLTLIIGQSKRGFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENPNMEIS 1537
Cdd:TIGR03443 143 APDNQQTTYSTG-------------STTDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIG 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1538 RIQLV-DQQ--------------------HDLLVKKAESQPRsiKDCIQYSFENWVRSSPNhialrfldRSYTYDEVNKR 1596
Cdd:TIGR03443 210 KVSLItPSQksllpdptkdldwsgfrgaiHDIFADNAEKHPD--RTCVVETPSFLDPSSKT--------RSFTYKQINEA 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1597 ANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNR-------------------------- 1650
Cdd:TIGR03443 280 SNILAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsvakpraliviekagtldqlv 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1651 RDFILKDASVGAIVTQTSLEE--KLSKSDLPYLCTDQSQDSEDYslltKDKSY-----PEDIAYIIYTSGTTGTPNGVMV 1723
Cdd:TIGR03443 360 RDYIDKELELRTEIPALALQDdgSLVGGSLEGGETDVLAPYQAL----KDTPTgvvvgPDSNPTLSFTSGSEGIPKGVLG 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1724 KHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPV 1803
Cdd:TIGR03443 436 RHFSLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPA 515
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1804 ---VLDSILPEDIPSLQTVSTGGErcpiKVAKR-----WSLDRNFY--NVYGPTETTIATTWYRVSSP-------ECVQD 1866
Cdd:TIGR03443 516 mgqLLSAQATTPIPSLHHAFFVGD----ILTKRdclrlQTLAENVCivNMYGTTETQRAVSYFEIPSRssdstflKNLKD 591
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1867 SVPIGTPVPNTEVFILDPDLNPVPMGV--IGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEI--------------- 1929
Cdd:TIGR03443 592 VMPAGKGMKNVQLLVVNRNDRTQTCGVgeVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPSHwidldkennkperef 671
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1930 -------LYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHG 2002
Cdd:TIGR03443 672 wlgprdrLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQD 751
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2003 EWEEKKIIEE----------------------------LRSKLPEHMVPSIFVQMEELPrLN-NKKVDRHSLP------- 2046
Cdd:TIGR03443 752 KSDELEEFKSevddeessdpvvkglikyrklikdireyLKKKLPSYAIPTVIVPLKKLP-LNpNGKVDKPALPfpdtaql 830
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2047 TAVHIFRQQKVIQKPVTEEEVVVAECWAETLNLPIDNIGLNSNFFELGGHSLTATQLVARISELFEIELPIKAIFEYPTI 2126
Cdd:TIGR03443 831 AAVAKNRSASAADEEFTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTI 910
|
970 980
....*....|....*....|.
gi 497785100 2127 QAildFIVEMKLELGGEELDS 2147
Cdd:TIGR03443 911 KG---FAKEVDRLKKGEELAD 928
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
512-1001 |
1.95e-83 |
|
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: 282.47 E-value: 1.95e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESP 591
Cdd:COG0318 5 LRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 592 KERIEIITQDSKLKAIIThseyktsyegyevpilyidqlddfllderednlnvdcdssqlAYGIYTSGSTGIPKGVLVEH 671
Cdd:COG0318 85 AEELAYILEDSGARALVT------------------------------------------ALILYTSGTTGRPKGVMLTH 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 672 RNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLT-TIYTSLLSGGTLFFLlkeDAIDPAKVEEIVQGKAIDWYKITPSH 750
Cdd:COG0318 123 RNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTvGLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGVPTM 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 751 LKAL--SSESGTKLFPR-KGLILGGEASEWSWIKEIYRNipASCKLFNHYGPSETTIGVAV----YEVTKKGlsnqfstt 823
Cdd:COG0318 200 LARLlrHPEFARYDLSSlRLVVSGGAPLPPELLERFEER--FGVRIVEGYGLTETSPVVTVnpedPGERRPG-------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 824 PIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFmEDPFitdsrmYKTGDIGKILYTGEIQFL 903
Cdd:COG0318 270 SVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW------LRTGDLGRLDEDGYLYIV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 904 GRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVT-VTKVRNEEQLVAYYVSKK--EVLDKDLQTYLKQKLPPNLVPAYL 980
Cdd:COG0318 343 GRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVgVPDEKWGERVVAFVVLRPgaELDAEELRAFLRERLARYKVPRRV 422
|
490 500
....*....|....*....|.
gi 497785100 981 VKMDTLPRHAHGKIDRKALPE 1001
Cdd:COG0318 423 EFVDELPRTASGKIDRRALRE 443
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
512-913 |
8.88e-83 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 279.20 E-value: 8.88e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHE-RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVES 590
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 591 PKERIEIITQDSKLKAIITHSEYK-------TSYEGYEVPILYIDQLDDF---LLDEREDNLNVD------CDSSQLAYG 654
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKleelleaLGKLEVVKLVLVLDRDPVLkeePLPEEAKPADVPppppppPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 655 IYTSGSTGIPKGVLVEHRNLSNYIYAI----QTKLGNKPKDRYLLLQSLAYDFCLTT-IYTSLLSGGTLFFLLKEDAIDP 729
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIkrvrPRGFGLGPDDRVLSTLPLFHDFGLSLgLLGPLLAGATVVLPPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 730 AKVEEIVQGKAIDWYKITPSHLKALSSESGTKLFPRKGL---ILGGEA---SEWSWIKEIYRnipasCKLFNHYGPSETT 803
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAGAPKRALLSSLrlvLSGGAPlppELARRFRELFG-----GALVNGYGLTETT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 804 iGVAVYEVTKKGLSNQFSTtpIGSSLSNNRIYILDDK-LRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDpfitd 882
Cdd:pfam00501 316 -GVVTTPLPLDEDLRSLGS--VGRPLPGTEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED----- 387
|
410 420 430
....*....|....*....|....*....|.
gi 497785100 883 sRMYKTGDIGKILYTGEIQFLGRLDGQVKIR 913
Cdd:pfam00501 388 -GWYRTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1560-2045 |
7.31e-81 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 276.78 E-value: 7.31e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1560 IKDCIQySFENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAY 1639
Cdd:PRK04813 1 IMDIIE-TIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1640 VPIDSELPLNRRDFIlKDASVGAIVTQTSlEEKLSKSDLPYLCTDQSQDSedyslLTKDKSYPE-------DIAYIIYTS 1712
Cdd:PRK04813 80 IPVDVSSPAERIEMI-IEVAKPSLIIATE-ELPLEILGIPVITLDELKDI-----FATGNPYDFdhavkgdDNYYIIFTS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1713 GTTGTPNGVMVKHSsvmNLISAT---IDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVsreeqlsTKALVKR 1789
Cdd:PRK04813 153 GTTGKPKGVQISHD---NLVSFTnwmLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVAL-------PKDMTAN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1790 FRDWNVTLADLPPVV-------------LDSILPEDIPSLQTVSTGGERCPIKVAKrwSLDRNF-----YNVYGPTETTI 1851
Cdd:PRK04813 223 FKQLFETLPQLPINVwvstpsfadmcllDPSFNEEHLPNLTHFLFCGEELPHKTAK--KLLERFpsatiYNTYGPTEATV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1852 ATTWYRVsSPECVQ--DSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIphpFREEEI 1929
Cdd:PRK04813 301 AVTSIEI-TDEMLDqyKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFF---TFDGQP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1930 LYKTGDIGKvLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVP--HGEWEEK 2007
Cdd:PRK04813 377 AYHTGDAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPkeEDFEREF 455
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 497785100 2008 KIIEELRSKL----PEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK04813 456 ELTKAIKKELkerlMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1108-1532 |
8.07e-81 |
|
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: 273.81 E-value: 8.07e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1108 IPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNIdPVQVVLKDLKCTINI 1187
Cdd:cd20484 2 SPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGV-PFQKIEPSKPLSFQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1188 LDFdENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMPI 1267
Cdd:cd20484 81 EDI-SSLKESEIIAYLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1268 QLEQPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAVLIKEICEE 1347
Cdd:cd20484 160 TLASSPASYYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1348 AKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGALEN 1427
Cdd:cd20484 240 QSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDH 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1428 QDISFERIVQELNPERSLSYNPIYQVAFTLQNDEQGKngnygglSVEEFEIEWRTS-------------KVDLTLIIGQS 1494
Cdd:cd20484 320 AAYPFPAMVRDLNIPRSQANSPVFQVAFFYQNFLQST-------SLQQFLAEYQDVlsiefvegihqegEYELVLEVYEQ 392
|
410 420 430
....*....|....*....|....*....|....*...
gi 497785100 1495 KRGFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENP 1532
Cdd:cd20484 393 EDRFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
263-1105 |
2.66e-80 |
|
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: 293.51 E-value: 2.66e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 263 TQEGTGVGSEYNFKIPNiltdklRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTpiagRNIRETRnvigPFIntv 342
Cdd:TIGR03443 21 PANNRLVEATYSLQLPS------AEVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT----SSNKSGR----PFV--- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 343 vIRTKAEQNLSVIEYLQQVHETTIQALENQDVPFEKVVEVLNP-NRDVRANPFYQLLFVMQEPPTQfslpgikveyelip 421
Cdd:TIGR03443 84 -LRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAaKKLERTPPLFRLAFQDAPDNQQ-------------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 422 TEVARF---PLTLSIIEGEEMIGRVLYRTSIL-SEYEVQSFVQRLLQVADEIVQSPHQRIYDLNLLTSkerSESAYLynq 497
Cdd:TIGR03443 149 TTYSTGsttDLTVFLTPSSPELELSIYYNSLLfSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITP---SQKSLL--- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 498 sgckPFPTE---------PIHVQFEGQ---------VLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFI 559
Cdd:TIGR03443 223 ----PDPTKdldwsgfrgAIHDIFADNaekhpdrtcVVETPSFLDPSSKTRSFTYKQINEASNILAHYLLKTGIKRGDVV 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 560 GIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAII------THSEYKTSYEGYEVPIL-YIDQL-- 630
Cdd:TIGR03443 299 MIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKPRALIviekagTLDQLVRDYIDKELELRtEIPALal 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 631 --DDFLLDEREDNLNVDCDSSQLAY-----GI-----------YTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDR 692
Cdd:TIGR03443 379 qdDGSLVGGSLEGGETDVLAPYQALkdtptGVvvgpdsnptlsFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSENDK 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 693 YLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPakveeivqGKAIDW---YKITPSHLKalssesgtklfPRKGLI 769
Cdd:TIGR03443 459 FTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTP--------GRLAEWmakYGATVTHLT-----------PAMGQL 519
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 770 LGGEASewswikeiyRNIPA------------------------SCKLFNHYGPSETTIGVAVYEVTKKG-----LSNQF 820
Cdd:TIGR03443 520 LSAQAT---------TPIPSlhhaffvgdiltkrdclrlqtlaeNVCIVNMYGTTETQRAVSYFEIPSRSsdstfLKNLK 590
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 821 STTPIGSSLSN------NRiyilDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDS----------- 883
Cdd:TIGR03443 591 DVMPAGKGMKNvqllvvNR----NDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPShwidldkennk 666
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 884 -----------RMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQ-LVAY 951
Cdd:TIGR03443 667 perefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPtLVSY 746
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 952 YV----------SKKEV------------------LDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEIQ 1003
Cdd:TIGR03443 747 IVpqdksdeleeFKSEVddeessdpvvkglikyrkLIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPD 826
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1004 VSNWN--------EIEIQPMNRLEEKMKDVWEKILERPVPSI--DDSFFKLGGHSLLATRLVSMIRKEFKVELSIKEFFE 1073
Cdd:TIGR03443 827 TAQLAavaknrsaSAADEEFTETEREIRDLWLELLPNRPATIspDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFK 906
|
970 980 990
....*....|....*....|....*....|...
gi 497785100 1074 KPSIRELSTHLLQLEAVSTH-FALSNISEAEKE 1105
Cdd:TIGR03443 907 SPTIKGFAKEVDRLKKGEELaDEGDSEIEEEET 939
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1108-1530 |
2.46e-77 |
|
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: 263.74 E-value: 2.46e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1108 IPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNiDPVQVVLKDLKCTINI 1187
Cdd:cd20483 2 RPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDD-FGEQQVLDDPSFHLIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1188 LDF-DENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMP 1266
Cdd:cd20483 81 IDLsEAADPEAALDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAGRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1267 IQ-LEQPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAP---SLLELPLDKPRPSMQsYNGSLIRMKLPEKHAVLIK 1342
Cdd:cd20483 161 LAtVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGIPdasKLLPFAKAERPPVKD-YERSTVEATLDKELLARMK 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1343 EICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQIL 1422
Cdd:cd20483 240 RICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTTCL 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1423 GALENQDISFERIVQELNPERSLSYNPIYQVAFTLQNDEQGKNGNYGGLSVEEFEIEWRTSKVDLTL-IIGQSKRGFEMV 1501
Cdd:cd20483 320 EAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQVHGKFPEYDTGDFKFTDYDHYDIPTACDIALeAEEDPDGGLDLR 399
|
410 420
....*....|....*....|....*....
gi 497785100 1502 MEYNTDLFRQQSIEQMLSDYIKIISQVIE 1530
Cdd:cd20483 400 LEFSTTLYDSADMERFLDNFVTFLTSVIR 428
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1108-1532 |
2.03e-74 |
|
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: 255.41 E-value: 2.03e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1108 IPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESkNIDPVQVVLKDL-KCTIN 1186
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEE-AGRYEQVVLDKTvRFRIE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1187 ILDF-DENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNM 1265
Cdd:cd19066 81 IIDLrNLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1266 PIqLEQPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAVLIKEIC 1345
Cdd:cd19066 161 PT-LPPPVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1346 EEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGAL 1425
Cdd:cd19066 240 RESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQSREAI 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1426 ENQDISFERIVQELNPERSLSYNPIYQVAFTLQNDEQGKnGNYGGLSVEEFEIEWR-TSKVDLTL-IIGQSKRGFEMVME 1503
Cdd:cd19066 320 EHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQL-GKTGGFIFTTPVYTSSeGTVFDLDLeASEDPDGDLLLRLE 398
|
410 420
....*....|....*....|....*....
gi 497785100 1504 YNTDLFRQQSIEQMLSDYIKIISQVIENP 1532
Cdd:cd19066 399 YSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1110-1353 |
5.60e-74 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 246.87 E-value: 5.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1110 LSDAQKRMWFlyrMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNiDPVQVVLKDLKCTINILD 1189
Cdd:COG4908 1 LSPAQKRFLF---LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDG-EPVQRIDPDADLPLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1190 ---FDENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMP 1266
Cdd:COG4908 77 lsaLPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1267 IQLEQPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAVLIKEICE 1346
Cdd:COG4908 157 PPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236
|
....*..
gi 497785100 1347 EAKVTPY 1353
Cdd:COG4908 237 AHGATVN 243
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
50-473 |
3.42e-70 |
|
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: 243.48 E-value: 3.42e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 50 PLSSIQKQIWFMSQLNPELPIYNEHLIkINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVITKSEPTIQFLS 129
Cdd:cd19540 3 PLSFAQQRLWFLNRLDGPSAAYNIPLA-LRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 130 LRGISGEEQQEILSEycrkEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYSQNGE 209
Cdd:cd19540 82 VVDVTEDELAARLAE----AARRGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYAARRAGRA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 210 inPEQsqEELTIQYHDYALWQEKLLTSEN-----LEKGLEYWKEKLEG-----DLPmlsiggiT-----QEGTGVGSEYN 274
Cdd:cd19540 158 --PDW--APLPVQYADYALWQRELLGDEDdpdslAARQLAYWRETLAGlpeelELP-------TdrprpAVASYRGGTVE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 275 FKIPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSV 354
Cdd:cd19540 227 FTIDAELHARLAALAREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTF 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 355 IEYLQQVHETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLFVMQ-EPPTQFSLPGIKVEYELIPTEVARFPLTLSI 433
Cdd:cd19540 307 AELLARVRETDLAAFAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQnTAAATLELPGLTVEPVPVDTGVAKFDLSFTL 386
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 497785100 434 IE-------GEEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSP 473
Cdd:cd19540 387 TErrdadgaPAGLTGELEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
1109-1532 |
6.39e-70 |
|
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: 241.98 E-value: 6.39e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1109 PLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKN-IDPVQVVLKDLKC---T 1184
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEdGEPMQGVLASSPLrleH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1185 INILDFDENRSE-QDIMNYlteksmePFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYhqiis 1263
Cdd:cd19532 83 VQISDEAEVEEEfERLKNH-------VYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAY----- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1264 NMPiQLEQPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAPS---LLELPLDKPRPSMQSYNGSLIRMKLPEKHAVL 1340
Cdd:cd19532 151 NGQ-PLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLPEplpLLPFAKVKSRPPLTRYDTHTAERRLDAALAAR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1341 IKEICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQ 1420
Cdd:cd19532 230 IKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1421 ILGALENQDISFERIVQELNPERSLSYNPIYQVAFtlqNDEQG--KNGNYGGLSVEefEIEWRTSKV--DLTL-IIGQSK 1495
Cdd:cd19532 310 AYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFI---NYRQGvaESRPFGDCELE--GEEFEDARTpyDLSLdIIDNPD 384
|
410 420 430
....*....|....*....|....*....|....*..
gi 497785100 1496 RGFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENP 1532
Cdd:cd19532 385 GDCLLTLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
518-999 |
1.04e-69 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 244.42 E-value: 1.04e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 518 NTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFI---GIQlQPcaKAIIAMLGVLKAGGAYLPLDVESPKER 594
Cdd:PRK04813 14 TQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIivfGHM-SP--EMLATFLGAVKAGHAYIPVDVSSPAER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 595 IEIITQDSKLKAIITHSEYKTSYEGyeVPILYIDQLDDFLLDEREDNLN--VDCDSSqlAYGIYTSGSTGIPKGVLVEHR 672
Cdd:PRK04813 91 IEMIIEVAKPSLIIATEELPLEILG--IPVITLDELKDIFATGNPYDFDhaVKGDDN--YYIIFTSGTTGKPKGVQISHD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 673 NL---SNYIyaiqTKLGNKPKDRYLLLQSLaYDFCLTT--IYTSLLSGGTLFFLLKEDAIDPAKV-EEIVQGKAIDWYKi 746
Cdd:PRK04813 167 NLvsfTNWM----LEDFALPEGPQFLNQAP-YSFDLSVmdLYPTLASGGTLVALPKDMTANFKQLfETLPQLPINVWVS- 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 747 TPS--HLKALSSESGTKLFPR-KGLILGGEASEWSWIKEIYRNIPAScKLFNHYGPSETTIGVAVYEVTKKGLsNQFSTT 823
Cdd:PRK04813 241 TPSfaDMCLLDPSFNEEHLPNlTHFLFCGEELPHKTAKKLLERFPSA-TIYNTYGPTEATVAVTSIEITDEML-DQYKRL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 824 PIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEdpfITDSRMYKTGDIGKIlYTGEIQFL 903
Cdd:PRK04813 319 PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGYL-EDGLLFYQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 904 GRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVtVTKVRNE--EQLVAYYVSKKEVLDKDLQTY------LKQKLPPNL 975
Cdd:PRK04813 395 GRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVV-VPYNKDHkvQYLIAYVVPKEEDFEREFELTkaikkeLKERLMEYM 473
|
490 500
....*....|....*....|....
gi 497785100 976 VPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK04813 474 IPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1109-1532 |
6.31e-69 |
|
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: 239.41 E-value: 6.31e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1109 PLSDAQKRMWF--LYRMESDSayYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNIDPVQVVLKDLKCTIN 1186
Cdd:cd19543 3 PLSPMQEGMLFhsLLDPGSGA--YVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKDRKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1187 ILDF---DENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIIS 1263
Cdd:cd19543 81 ELDLshlSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1264 NMPIQLEqPVYQYADYVNW--QQNRyteeqiNQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLIRMKLPEKHAVLI 1341
Cdd:cd19543 161 GQPPSLP-PVRPYRDYIAWlqRQDK------EAAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1342 KEICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIqELEGI---LGLFVNTLVIPSTVKGDRNFKSLLQQVN 1418
Cdd:cd19543 234 QELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPA-ELPGIetmVGLFINTLPVRVRLDPDQTVLELLKDLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1419 NQILGALENQDISFERIvQelnpERSLSYNPIYQVAFTLQN----DEQGKNGNYGGLSVEEFEIEWRTSkVDLTLIIGQS 1494
Cdd:cd19543 313 AQQLELREHEYVPLYEI-Q----AWSEGKQALFDHLLVFENypvdESLEEEQDEDGLRITDVSAEEQTN-YPLTVVAIPG 386
|
410 420 430
....*....|....*....|....*....|....*...
gi 497785100 1495 KRgFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENP 1532
Cdd:cd19543 387 EE-LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1704-2041 |
2.17e-63 |
|
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: 220.23 E-value: 2.17e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1704 DIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLST 1783
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1784 KALVKRFRdwnVTLADLPPVVLDSIL------PEDIPSLQTVSTGGERCPIKVAKRWS--LDRNFYNVYGPTETTIATTW 1855
Cdd:cd04433 81 LELIEREK---VTILLGVPTLLARLLkapesaGYDLSSLRALVSGGAPLPPELLERFEeaPGIKLVNGYGLTETGGTVAT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1856 YRVSSPECVQDSVpiGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfreEEILYKTGD 1935
Cdd:cd04433 158 GPPDDDARKPGSV--GRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD-------EDGWYRTGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1936 IGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKI--IEEL 2013
Cdd:cd04433 229 LGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDAEelRAHV 308
|
330 340
....*....|....*....|....*...
gi 497785100 2014 RSKLPEHMVPSIFVQMEELPRLNNKKVD 2041
Cdd:cd04433 309 RERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
50-473 |
1.11e-62 |
|
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: 221.48 E-value: 1.11e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 50 PLSSIQKQIWFMSQLNPELPIYNEHLIkINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSI--EQVITKSEPTIqF 127
Cdd:cd19539 3 PLSFAQERLWFIDQGEDGGPAYNIPGA-WRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVprQEILPPGPAPL-E 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 128 LSLRGISGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYSQN 207
Cdd:cd19539 81 VRDLSDPDSDRERRLEELLRERESRGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 208 geinPEQSQEELTIQYHDYALWQEKLLTSENLEKGLEYWKEKLEG--------DLPMLSIGGITqegtgvGSEYNFKIPN 279
Cdd:cd19539 161 ----PAAPLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRGaeptalptDRPRPAGFPYP------GADLRFELDA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 280 ILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVIEYLQ 359
Cdd:cd19539 231 ELVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 360 QVHETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLF-VMQEPPTQFSLPG-IKVEYELIPTEVARFPLTLSIIE-G 436
Cdd:cd19539 311 RVRKALVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFqVTNAPAGELELAGgLSYTEGSDIPDGAKFDLNLTVTEeG 390
|
410 420 430
....*....|....*....|....*....|....*..
gi 497785100 437 EEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSP 473
Cdd:cd19539 391 TGLRGSLGYATSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
49-473 |
1.92e-62 |
|
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: 220.54 E-value: 1.92e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 49 YPLSSIQKQIWFMSQLNPELPIYNEHLIkINLSGKVNIEALKKSFEQIVNRHQILRMR-VKQTEDSIEQVITKS-EPTIQ 126
Cdd:cd19543 2 YPLSPMQEGMLFHSLLDPGSGAYVEQMV-ITLEGPLDPDRFRAAWQAVVDRHPILRTSfVWEGLGEPLQVVLKDrKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 127 FLSLRGISGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYSQ 206
Cdd:cd19543 81 ELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYAALGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 207 NGEINPEQSQeeltiQYHDYALWqeklLTSENLEKGLEYWKEKLEG--DLPMLSIG-GITQEGTGVGSEYNFKIPNILTD 283
Cdd:cd19543 161 GQPPSLPPVR-----PYRDYIAW----LQRQDKEAAEAYWREYLAGfeEPTPLPKElPADADGSYEPGEVSFELSAELTA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 284 KLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRN--IRETRNVIGPFINTVVIRTKAEQNLSVIEYLQQV 361
Cdd:cd19543 232 RLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPaeLPGIETMVGLFINTLPVRVRLDPDQTVLELLKDL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 362 HETTIQALENQDVPFekvVEVlnPNRDVRANPFYQLLFVMQEPPTQFSLPGIKVEYELIPTEVA-----RFPLTLSIIEG 436
Cdd:cd19543 312 QAQQLELREHEYVPL---YEI--QAWSEGKQALFDHLLVFENYPVDESLEEEQDEDGLRITDVSaeeqtNYPLTVVAIPG 386
|
410 420 430
....*....|....*....|....*....|....*..
gi 497785100 437 EEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSP 473
Cdd:cd19543 387 EELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
49-473 |
6.16e-60 |
|
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: 213.42 E-value: 6.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 49 YPLSSIQKQIWFMSQLNPELPIYNEHlIKINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVItkSEPTIQF- 127
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVA-IEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVV--LDKTVRFr 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 128 LSLRGISGEEQQEI-LSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYSQ 206
Cdd:cd19066 79 IEIIDLRNLADPEArLLELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 207 NGEINPEqsqeeLTIQYHDYALWQEKLLTSENLEKGLEYWKEKLEG--DLPMLSIGGIT-QEGTGVGSEYNFKIPNILTD 283
Cdd:cd19066 159 QKPTLPP-----PVGSYADYAAWLEKQLESEAAQADLAYWTSYLHGlpPPLPLPKAKRPsQVASYEVLTLEFFLRSEETK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 284 KLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVIEYLQQVHE 363
Cdd:cd19066 234 RLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 364 TTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLFVMQEPPTQFSLPGIKVEYELI--PTEVARFPLTLSIIEGE--EM 439
Cdd:cd19066 314 QSREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFTTPVytSSEGTVFDLDLEASEDPdgDL 393
|
410 420 430
....*....|....*....|....*....|....
gi 497785100 440 IGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSP 473
Cdd:cd19066 394 LLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
51-297 |
4.45e-59 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 204.12 E-value: 4.45e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 51 LSSIQKQIWFMsqlNPELPIYNEHLIkINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVITKSEP-TIQFLS 129
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAV-LRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADlPLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 130 LRGISGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYSQNGE 209
Cdd:COG4908 77 LSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYAALLEGEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 210 InpeqSQEELTIQYHDYALWQEKLLTSENLEKGLEYWKEKLEGDLPMLSIGGI---TQEGTGVGSEYNFKIPNILTDKLR 286
Cdd:COG4908 157 P----PLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDrprPAVQTFRGATLSFTLPAELTEALK 232
|
250
....*....|.
gi 497785100 287 KLAEEQKVSLY 297
Cdd:COG4908 233 ALAKAHGATVN 243
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1585-2045 |
1.10e-57 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 207.71 E-value: 1.10e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1585 DRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIV 1664
Cdd:cd17654 14 DTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 tqtslEEKLSksdlpylctDQSQDSEDYSLLTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQE 1744
Cdd:cd17654 94 -----QNKEL---------DNAPLSFTPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1745 tKVGQFATI-SFDASLWQILMALLAGATLCV----VSREEQLSTKALVKRFRdwnVTLADLPPVVLDSILPEDIP----- 1814
Cdd:cd17654 160 -DILFLTSPlTFDPSVVEIFLSLSSGATLLIvptsVKVLPSKLADILFKRHR---ITVLQATPTLFRRFGSQSIKstvls 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1815 ---SLQTVSTGGERCPIKVA-KRWSLDRN---FYNVYGPTETTIATTWYRVSSPECvqdSVPIGTPVPNTEVFILDPDLN 1887
Cdd:cd17654 236 atsSLRVLALGGEPFPSLVIlSSWRGKGNrtrIFNIYGITEVSCWALAYKVPEEDS---PVQLGSPLLGTVIEVRDQNGS 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1888 PVPmgviGEIYIGgvGVSNGYLNRDDLNekrfiphpfREEEILYKTGDIGKVlHDGNLEHLGRLDHQIKVRGFRIELGEI 1967
Cdd:cd17654 313 EGT----GQVFLG--GLNRVCILDDEVT---------VPKGTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLI 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 1968 ESLLNLQTGVkEAIVQPLGDNQNyhtLVAYVVPHGEWEEKKIIEELrSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd17654 377 QQVIESCLGV-ESCAVTLSDQQR---LIAFIVGESSSSRIHKELQL-TLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1568-2045 |
3.48e-57 |
|
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: 206.65 E-value: 3.48e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELP 1647
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 LNRRDFILKDASVGAIVTQTSLEEKLSKS-DLPYLCTDQsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHS 1726
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFTDLLAAGaPLGERVALT----------------PEDVAVLQYTSGTTGVPKGAMLTHR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1727 svmNLISATIDEFNITQETKVGQ---------FATISFDASLwqiLMALLAGATLCVVSReeqLSTKALVKRFRDWNVT- 1796
Cdd:cd05936 149 ---NLVANALQIKAWLEDLLEGDdvvlaalplFHVFGLTVAL---LLPLALGATIVLIPR---FRPIGVLKEIRKHRVTi 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1797 ----------LADLPPVvldsiLPEDIPSLQTVSTGGERCPIKVAKRWS--LDRNFYNVYGPTETTIATTwyrVSSPECV 1864
Cdd:cd05936 220 fpgvptmyiaLLNAPEF-----KKRDFSSLRLCISGGAPLPVEVAERFEelTGVPIVEGYGLTETSPVVA---VNPLDGP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1865 QDSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFReeeilykTGDIGKVLHDGN 1944
Cdd:cd05936 292 RKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWLR-------TGDIGYMDEDGY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1945 LEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPH--GEWEEKKIIEELRSKLPEHMV 2022
Cdd:cd05936 365 FFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSGEAVKAFVVLKegASLTEEEIIAFCREQLAGYKV 444
|
490 500
....*....|....*....|...
gi 497785100 2023 PSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05936 445 PRQVEFRDELPKSAVGKILRREL 467
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
1108-1532 |
3.33e-54 |
|
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: 196.93 E-value: 3.33e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1108 IPLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNiDPVQvvlkdlkctiNI 1187
Cdd:cd19546 5 VPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGG-DVHQ----------RI 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1188 LDFDENR--------SEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYH 1259
Cdd:cd19546 74 LDADAARpelpvvpaTEEELPALLADRAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1260 -----QIISNMPIQLeqpvyQYADYVNWQQNRYTEEQ-----INQQLQYWKEQLSGAPSLLELPLDKPRPSMQSYNGSLI 1329
Cdd:cd19546 154 arregRAPERAPLPL-----QFADYALWERELLAGEDdrdslIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1330 RMKLP-EKHAVLIkEICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQ-ELEGILGLFVNTLVIPSTVKGD 1407
Cdd:cd19546 229 PLRLDaEVHARLM-EAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGD 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1408 RNFKSLLQQVNNQILGALENQDISFERIVQELNPERSLSYNPIYQVAFTLQNDEQGKNGNYG--GLSVEEFEIEWRTSKV 1485
Cdd:cd19546 308 PTFRELLGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDAPElpGLRTSPVPLGTEAMEL 387
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 497785100 1486 DLTLIIGQSKR------GFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENP 1532
Cdd:cd19546 388 DLSLALTERRNddgdpdGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
1589-2045 |
7.29e-53 |
|
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: 193.05 E-value: 7.29e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQTS 1668
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1669 LEEKLSKSD-LPYLCTdqsQDSEDYSLLTKDKSypEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKv 1747
Cdd:TIGR01923 81 LEEKDFQADsLDRIEA---AGRYETSLSASFNM--DQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDN- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1748 gqfATIS---FDASLWQILM-ALLAGATLCVVSREEQLSTkaLVKRFRdwnVTLADLPPVVLDSILPEDIP--SLQTVST 1821
Cdd:TIGR01923 155 ---WLLSlplYHISGLSILFrWLIEGATLRIVDKFNQLLE--MIANER---VTHISLVPTQLNRLLDEGGHneNLRKILL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1822 GGERCPIKVAKRwSLDRNF--YNVYGPTET--TIATtwyrvSSPECVQDSVPIGTPVPNTEVFILDPDLNPVpmgviGEI 1897
Cdd:TIGR01923 227 GGSAIPAPLIEE-AQQYGLpiYLSYGMTETcsQVTT-----ATPEMLHARPDVGRPLAGREIKIKVDNKEGH-----GEI 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1898 YIGGVGVSNGYLNRDDLNekrfiphPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGV 1977
Cdd:TIGR01923 296 MVKGANLMKGYLYQGELT-------PAFEQQGWFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPGI 368
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 1978 KEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:TIGR01923 369 QEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1572-2042 |
1.19e-52 |
|
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: 192.44 E-value: 1.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1572 VRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRR 1651
Cdd:cd17631 5 ARRHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1652 DFILKDASVGAIVtqtsleeklsksdlpylctdqsqdsedyslltkdksypEDIAYIIYTSGTTGTPNGVMVKHSSVMNL 1731
Cdd:cd17631 85 AYILADSGAKVLF--------------------------------------DDLALLMYTSGTTGRPKGAMLTHRNLLWN 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1732 ISATIDEFNITQETKVGQFATIS-FDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRdwnVTLADLPPVVLDSIL- 1809
Cdd:cd17631 127 AVNALAALDLGPDDVLLVVAPLFhIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHR---VTSFFLVPTMIQALLq 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1810 -PE----DIPSLQTVSTGGERCPIKVAKRWSlDRN--FYNVYGPTETTIATTWYrvsSPECVQDSV-PIGTPVPNTEVFI 1881
Cdd:cd17631 204 hPRfattDLSSLRAVIYGGAPMPERLLRALQ-ARGvkFVQGYGMTETSPGVTFL---SPEDHRRKLgSAGRPVFFVEVRI 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1882 LDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFReeeilykTGDIGKVLHDGNLEHLGRLDHQIKVRGFR 1961
Cdd:cd17631 280 VDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWFH-------TGDLGRLDEDGYLYIVDRKKDMIISGGEN 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1962 IELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV--PHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKK 2039
Cdd:cd17631 353 VYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEAVVAVVVprPGAELDEDELIAHCRERLARYKIPKSVEFVDALPRNATGK 432
|
...
gi 497785100 2040 VDR 2042
Cdd:cd17631 433 ILK 435
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
50-435 |
1.62e-52 |
|
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: 191.52 E-value: 1.62e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 50 PLSSIQKQIWFMSQLNPELPIYNeHLIKINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIE--QVITkSEPTIQF 127
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFN-VTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFFTDPEDGEpmQGVL-ASSPLRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 128 LSLRgISGEEqqEILSEYcRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMysqn 207
Cdd:cd19532 81 EHVQ-ISDEA--EVEEEF-ERLKNHVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNG---- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 208 geinpeQSQEELTIQYHDYALWQEKLLTSENLEKGLEYWKEKLEGD---LPMLSIggitqegTGVGS-----EYN----- 274
Cdd:cd19532 153 ------QPLLPPPLQYLDFAARQRQDYESGALDEDLAYWKSEFSTLpepLPLLPF-------AKVKSrppltRYDthtae 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 275 FKIPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSV 354
Cdd:cd19532 220 RRLDAALAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTF 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 355 IEYLQQVHETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLF-VMQEPPTQFSLPGIKVEYELIptEVARFP--LTL 431
Cdd:cd19532 300 ADVLKETRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFInYRQGVAESRPFGDCELEGEEF--EDARTPydLSL 377
|
....
gi 497785100 432 SIIE 435
Cdd:cd19532 378 DIID 381
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
519-999 |
2.82e-52 |
|
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: 193.85 E-value: 2.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEII 598
Cdd:TIGR03098 13 LPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLLKAEQVAHI 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAIITHSEY--KTSYEGYEVPILYIDQLDDFLLDEREDNLN------------------VDCDSSQLAYGIYTS 658
Cdd:TIGR03098 93 LADCNVRLLVTSSERldLLHPALPGCHDLRTLIIVGDPAHASEGHPGeepaswpkllalgdadppHPVIDSDMAAILYTS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 659 GSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLF---FLLKEDAIDPAKVEEI 735
Cdd:TIGR03098 173 GSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYGFNQLTTAFYVGATVVlhdYLLPRDVLKALEKHGI 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 736 ----------VQGKAIDWYKITPSHLKALSSeSGTKLfPRkglilggeasewSWIKEIYRNIPAScKLFNHYGPSE---- 801
Cdd:TIGR03098 253 tglaavpplwAQLAQLDWPESAAPSLRYLTN-SGGAM-PR------------ATLSRLRSFLPNA-RLFLMYGLTEafrs 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 802 TTIGVAvyEVTKKGLSnqfsttpIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDP-FI 880
Cdd:TIGR03098 318 TYLPPE--EVDRRPDS-------IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpFP 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 881 TDSRMYKT----GDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVT-VTKVRNEEQLVAYYV-S 954
Cdd:TIGR03098 389 GELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFgVPDPTLGQAIVLVVTpP 468
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 497785100 955 KKEVLDKD-LQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:TIGR03098 469 GGEELDRAaLLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1109-1532 |
3.28e-52 |
|
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: 190.21 E-value: 3.28e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1109 PLSDAQKRMwfLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVF-RESKNIDPVQVVLKDLKCTINI 1187
Cdd:cd19542 3 PCTPMQEGM--LLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTFLQVVLKSLDPPIEE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1188 LDFDEnrseQDIMNYLTEKSMEPFkLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQiisnmpi 1267
Cdd:cd19542 81 VETDE----DSLDALTRDLLDDPT-LFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNG------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1268 QLEQPVYQYADYVNWQQNRYTEEqinqQLQYWKEQLSGAPSLLElpldkprPSMQSYNGSLIRMKLPEKHAVLIKEICEE 1347
Cdd:cd19542 149 QLLPPAPPFSDYISYLQSQSQEE----SLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAKLEAFCAS 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1348 AKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRN--IQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGAL 1425
Cdd:cd19542 218 LGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSL 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1426 ENQDISFERIVQELNPERSLS-YNPIYQV-AFTLQNDEQGKNGNYGGLSVEEFEIEwrtskVDLTLIIGQSKRGFEMVME 1503
Cdd:cd19542 298 PHQHLSLREIQRALGLWPSGTlFNTLVSYqNFEASPESELSGSSVFELSAAEDPTE-----YPVAVEVEPSGDSLKVSLA 372
|
410 420
....*....|....*....|....*....
gi 497785100 1504 YNTDLFRQQSIEQMLSDYIKIISQVIENP 1532
Cdd:cd19542 373 YSTSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
531-999 |
2.07e-51 |
|
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: 189.22 E-value: 2.07e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 531 SYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITH 610
Cdd:cd17654 16 TVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 611 SEyktsyegyevpilyIDQLDDFLLDEREdNLNVDCDSSqLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPK 690
Cdd:cd17654 96 KE--------------LDNAPLSFTPEHR-HFNIRTDEC-LAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITSE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 691 DRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIV-QGKAIDWYKITPSHLKALSSESG-----TKLFP 764
Cdd:cd17654 160 DILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILfKRHRITVLQATPTLFRRFGSQSIkstvlSATSS 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 765 RKGLILGGEASEWSWIKEIYRNIPASCKLFNHYGPSETTIGVAVYEVTKKGlsnqfSTTPIGSSLSNNRIYILDDklrpv 844
Cdd:cd17654 240 LRVLALGGEPFPSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEED-----SPVQLGSPLLGTVIEVRDQ----- 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 845 pSGIPGHIYIAGEQVARGYLNREELTAerfmedPFitdSRMYKTGDIGKIlYTGEIQFLGRLDGQVKIRGIRVEPEEIQS 924
Cdd:cd17654 310 -NGSEGTGQVFLGGLNRVCILDDEVTV------PK---GTMRATGDFVTV-KDGELFFLGRKDSQIKRRGKRINLDLIQQ 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497785100 925 QLLSHPSIteaIVTVTKVRNEEQLVAYYVS--KKEVLDKDLQTYLkqkLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd17654 379 VIESCLGV---ESCAVTLSDQQRLIAFIVGesSSSRIHKELQLTL---LSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
650-995 |
2.21e-51 |
|
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: 185.57 E-value: 2.21e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 650 QLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAidp 729
Cdd:cd04433 1 DPALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKFDP--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 730 akvEEIVQgkAIDWYKIT-----PSHLKAL---SSESGTKLFPRKGLILGGEASEWSWIKEIYRNIPasCKLFNHYGPSE 801
Cdd:cd04433 78 ---EAALE--LIEREKVTillgvPTLLARLlkaPESAGYDLSSLRALVSGGAPLPPELLERFEEAPG--IKLVNGYGLTE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 802 TTIGVAvyevTKKGLSNQFSTTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAErFMEDpfit 881
Cdd:cd04433 151 TGGTVA----TGPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAA-VDED---- 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 882 dsRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSK--KEV 958
Cdd:cd04433 222 --GWYRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEaAVVGVPDPEWGERVVAVVVLRpgADL 299
|
330 340 350
....*....|....*....|....*....|....*..
gi 497785100 959 LDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKID 995
Cdd:cd04433 300 DAEELRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
516-1000 |
2.75e-51 |
|
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: 190.81 E-value: 2.75e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 516 VLNTPNSiaLSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERI 595
Cdd:cd17647 7 VVETPSL--NSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 596 EIITQDSKLKAIITHseyktsyegyevpilyidqlddflldeREDNLNVDCDSS-QLAYgiyTSGSTGIPKGVLVEHRNL 674
Cdd:cd17647 85 NIYLGVAKPRGLIVI---------------------------RAAGVVVGPDSNpTLSF---TSGSEGIPKGVLGRHFSL 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 675 SNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPakveeivqGKAIDW---YKITPSHL 751
Cdd:cd17647 135 AYYFPWMAKRFNLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTP--------GRLAEWmakYGATVTHL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 752 KalssesgtklfPRKGLILGGEASEWS-------WIKEIY--------RNIPASCKLFNHYGPSETTIGVAVYEVTKKG- 815
Cdd:cd17647 207 T-----------PAMGQLLTAQATTPFpklhhafFVGDILtkrdclrlQTLAENVRIVNMYGTTETQRAVSYFEVPSRSs 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 816 ----LSNQFSTTPIGSSLSNNRIYILD--DKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFITDS------ 883
Cdd:cd17647 276 dptfLKNLKDVMPAGRGMLNVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDhwnyld 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 884 ----------------RMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQ 947
Cdd:cd17647 356 kdnnepwrqfwlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEP 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 948 -LVAYYVSKKE-----------------------------VLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRK 997
Cdd:cd17647 436 tLVSYIVPRFDkpddesfaqedvpkevstdpivkgligyrKLIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKP 515
|
...
gi 497785100 998 ALP 1000
Cdd:cd17647 516 KLQ 518
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
512-999 |
3.85e-51 |
|
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: 188.93 E-value: 3.85e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESP 591
Cdd:cd05936 5 LEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 592 KERIEIITQDSKLKAIITHSEYKTSYEGYEVPILYIDqlddfllDEREDnlnvdcdssqLAYGIYTSGSTGIPKGVLVEH 671
Cdd:cd05936 85 PRELEHILNDSGAKALIVAVSFTDLLAAGAPLGERVA-------LTPED----------VAVLQYTSGTTGVPKGAMLTH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 672 RNLSNYIYAIQ--TKLGNKPKDRYLLLQSLAYDFCLTTIYT-SLLSGGTLffLLKEDAIDPAKVEEIVQgkaidwYKIT- 747
Cdd:cd05936 148 RNLVANALQIKawLEDLLEGDDVVLAALPLFHVFGLTVALLlPLALGATI--VLIPRFRPIGVLKEIRK------HRVTi 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 748 ----PSHLKALSSESGTKLFPRKGL--ILGGEAS-------EWswiKEIYRnipasCKLFNHYGPSETTIGVAV---YEV 811
Cdd:cd05936 220 fpgvPTMYIALLNAPEFKKRDFSSLrlCISGGAPlpvevaeRF---EELTG-----VPIVEGYGLTETSPVVAVnplDGP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 812 TKKGlsnqfsttPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFmedpfiTDSRMyKTGDI 891
Cdd:cd05936 292 RKPG--------SIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAF------VDGWL-RTGDI 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 892 GKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTvtKVRNE---EQLVAYYVSKKE--VLDKDLQTY 966
Cdd:cd05936 357 GYMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVV--GVPDPysgEAVKAFVVLKEGasLTEEEIIAF 434
|
490 500 510
....*....|....*....|....*....|...
gi 497785100 967 LKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05936 435 CREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1586-2046 |
3.93e-51 |
|
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: 190.42 E-value: 3.93e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1586 RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVT 1665
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1666 qtsleekLSKSDLPYlctdqsqdsedyslltkdksYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQET 1745
Cdd:cd17647 99 -------IRAAGVVV--------------------GPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSEND 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1746 KVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPV---VLDSILPEDIPSLQTVSTG 1822
Cdd:cd17647 152 KFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAmgqLLTAQATTPFPKLHHAFFV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1823 GERCPIKVAKRW-SLDRNF--YNVYGPTETTIATTWYRVSSP-------ECVQDSVPIGTPVPNTEVFILDP-DLNPV-P 1890
Cdd:cd17647 232 GDILTKRDCLRLqTLAENVriVNMYGTTETQRAVSYFEVPSRssdptflKNLKDVMPAGRGMLNVQLLVVNRnDRTQIcG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1891 MGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEI----------------------LYKTGDIGKVLHDGNLEHL 1948
Cdd:cd17647 312 IGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDHwnyldkdnnepwrqfwlgprdrLYRTGDLGRYLPNGDCECC 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1949 GRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEE---------------- 2012
Cdd:cd17647 392 GRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPDDESFAQedvpkevstdpivkgl 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 497785100 2013 -------------LRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSLP 2046
Cdd:cd17647 472 igyrklikdirefLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
48-473 |
4.92e-50 |
|
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: 184.44 E-value: 4.92e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 48 SYPLSSIQKQIWFMSQLNPELPIYNEHLIkINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVITKSEPTIqf 127
Cdd:cd20484 1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLC-FRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLS-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 128 LSLRGISGEEQQEILSeYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELerfYNMYSQN 207
Cdd:cd20484 78 FQEEDISSLKESEIIA-YLREKAKEPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSL---LDAYQAL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 208 GEINPEQSQEELTIqYHDYALWQEKLLTSENLEKGLEYWKEKLEGDLPMLSI-----GGITQEGTGvgSEYNFKIPNILT 282
Cdd:cd20484 154 LQGKQPTLASSPAS-YYDFVAWEQDMLAGAEGEEHRAYWKQQLSGTLPILELpadrpRSSAPSFEG--QTYTRRLPSELS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 283 DKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVIEYLQQVH 362
Cdd:cd20484 231 NQIKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQ 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 363 ETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLFVMQ-------------EPPTQFSLPGIKV-----EYELIptev 424
Cdd:cd20484 311 LTVLDGLDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQnflqstslqqflaEYQDVLSIEFVEGihqegEYELV---- 386
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 497785100 425 arfpltLSIIEGEE-MIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSP 473
Cdd:cd20484 387 ------LEVYEQEDrFTLNIKYNPDLFDASTIERMMEHYVKLAEELIANP 430
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
1109-1532 |
2.20e-48 |
|
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: 179.49 E-value: 2.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1109 PLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESkNIDPVQVVLKDLKCTINIL 1188
Cdd:cd19533 3 PLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEE-EGEPYQWIDPYTPVPIRHI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1189 DF-DENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIISNMPI 1267
Cdd:cd19533 82 DLsGDPDPEGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLKGRPA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1268 QlEQPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAPSLLELpldKPRPSMQSYNGSLIRMKLPEKHAVLIKEICEE 1347
Cdd:cd19533 162 P-PAPFGSFLDLVEEEQAYRQSERFERDRAFWTEQFEDLPEPVSL---ARRAPGRSLAFLRRTAELPPELTRTLLEAAEA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1348 AKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANR-NIQELEgILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGALE 1426
Cdd:cd19533 238 HGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRlGAAARQ-TPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1427 NQDISFERIVQELNPER--------SLSYNP-IYQVAFtlqNDEQGKNGNYGGLSVEEFEI----EWRTSKVDLTLiigq 1493
Cdd:cd19533 317 HQRYRYEDLRRDLGLTGelhplfgpTVNYMPfDYGLDF---GGVVGLTHNLSSGPTNDLSIfvydRDDESGLRIDF---- 389
|
410 420 430
....*....|....*....|....*....|....*....
gi 497785100 1494 skrgfemvmEYNTDLFRQQSIEQMLSDYIKIISQVIENP 1532
Cdd:cd19533 390 ---------DANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1571-2034 |
1.96e-46 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 177.61 E-value: 1.96e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1571 WVRSSPNHIALRFLD-----RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPI--- 1642
Cdd:COG0365 18 HAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVfpg 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1643 --------------------DSELPLNRRDFILKDASVGA----------IVTQTSLEEKLSKSDLPY--LCTDQSQDSE 1690
Cdd:COG0365 98 fgaealadriedaeakvlitADGGLRGGKVIDLKEKVDEAleelpslehvIVVGRTGADVPMEGDLDWdeLLAAASAEFE 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1691 DYSLLtkdksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDE-FNITQETKVGQFATISFDASLWQILMA-LLA 1768
Cdd:COG0365 178 PEPTD------ADDPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYvLDLKPGDVFWCTADIGWATGHSYIVYGpLLN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1769 GATlcVVSREEQLSTK------ALVKRFRdwnVTLADLPPVVLDSILPE--------DIPSLQTVSTGGERCPIKVAKRW 1834
Cdd:COG0365 252 GAT--VVLYEGRPDFPdpgrlwELIEKYG---VTVFFTAPTAIRALMKAgdeplkkyDLSSLRLLGSAGEPLNPEVWEWW 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1835 SldRNF----YNVYGPTETTIAttwyrVSSPECVQDSVP--IGTPVPNTEVFILDPDLNPVPMGVIGEIYIGG--VGVSN 1906
Cdd:COG0365 327 Y--EAVgvpiVDGWGQTETGGI-----FISNLPGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPGMFR 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1907 GYLNRDDLNEKRFiphpFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLG 1986
Cdd:COG0365 400 GYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVP 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 497785100 1987 DNQNYHTLVAYVVPH-GEWEEKKIIEEL----RSKLPEHMVPSIFVQMEELPR 2034
Cdd:COG0365 476 DEIRGQVVKAFVVLKpGVEPSDELAKELqahvREELGPYAYPREIEFVDELPK 528
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1596-2045 |
2.17e-46 |
|
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: 174.55 E-value: 2.17e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1596 RANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAA----YVPIDSELPLNRRDFILKDASVGAIVTQTSLEE 1671
Cdd:cd05922 2 GVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1672 KLSKSDLPYLCTDQSQDSEDY----SLLTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKV 1747
Cdd:cd05922 82 RLRDALPASPDPGTVLDADGIraarASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITADDRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1748 GQFATISFDASLWQILMALLAGATLcVVSREEQLStKALVKRFRDWNVT-LADLPPV--VLDSIL--PEDIPSLQTVSTG 1822
Cdd:cd05922 162 LTVLPLSYDYGLSVLNTHLLRGATL-VLTNDGVLD-DAFWEDLREHGATgLAGVPSTyaMLTRLGfdPAKLPSLRYLTQA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1823 GERCPIKVAKR-------WSLdrnfYNVYGPTETTIATTWYrvsSPECVQDSV-PIGTPVPNTEVFILDPDLNPVPMGVI 1894
Cdd:cd05922 240 GGRLPQETIARlrellpgAQV----YVMYGQTEATRRMTYL---PPERILEKPgSIGLAIPGGEFEILDDDGTPTPPGEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1895 GEIYIGGVGVSNGYLNRDdlnekRFIPHPFREEEILYkTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQ 1974
Cdd:cd05922 313 GEIVHRGPNVMKGYWNDP-----PYRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSI 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497785100 1975 TGVKEAIVQPLGDNQNyHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05922 387 GLIIEAAAVGLPDPLG-EKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1109-1532 |
1.77e-45 |
|
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: 171.09 E-value: 1.77e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1109 PLSDAQKRMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNIDPVQVVLKDLKCTINIL 1188
Cdd:cd19536 3 PLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQAQVPVTEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1189 DFDENRSEQDIMNYLTEKSM-EPFKLETGPLIRVHLVKSNPNEHVLLIVQ-HHIISDGWSLRIMMDELFAIYHQIISNMP 1266
Cdd:cd19536 83 DLTPLEEQLDPLRAYKEETKiRRFDLGRAPLVRAALVRKDERERFLLVISdHHSILDGWSLYLLVKEILAVYNQLLEYKP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1267 IQLEqPVYQYADYVNWqqnryTEEQINQQ--LQYWKEQLSGAPSlleLPLDKPRPSMQSYNGSLIRMKLPEKHAVLIKEI 1344
Cdd:cd19536 163 LSLP-PAQPYRDFVAH-----ERASIQQAasERYWREYLAGATL---ATLPALSEAVGGGPEQDSELLVSVPLPVRSRSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1345 CEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRN--IQELEGILGLFVNTLviPSTVK-GDRNFKSLLQQVNNQI 1421
Cdd:cd19536 234 AKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSeeTTGAERLLGLFLNTL--PLRVTlSEETVEDLLKRAQEQE 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1422 LGALENQDISFERIvqelnpERSLSYNPIYQVAFTLQNDEQGKNGNYGGLSVEE----FEIEWRTSkVDLTLIIGQSKRG 1497
Cdd:cd19536 312 LESLSHEQVPLADI------QRCSEGEPLFDSIVNFRHFDLDFGLPEWGSDEGMrrglLFSEFKSN-YDVNLSVLPKQDR 384
|
410 420 430
....*....|....*....|....*....|....*
gi 497785100 1498 FEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIENP 1532
Cdd:cd19536 385 LELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1585-1982 |
3.08e-44 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 168.93 E-value: 3.08e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1585 DRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIV 1664
Cdd:cd05911 8 GKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIF 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 TQTSLEEKLSKS--------------DLPYLCTDQSQDSEDYSlLTKDKSYP-------EDIAYIIYTSGTTGTPNGVMV 1723
Cdd:cd05911 88 TDPDGLEKVKEAakelgpkdkiivldDKPDGVLSIEDLLSPTL-GEEDEDLPpplkdgkDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1724 KHSSV--MNLISATIDEFNITQETKVgqFATISFD--ASLWQILMALLAGATLCVVSREEQLSTKALVKRFRdwnVTLAD 1799
Cdd:cd05911 167 SHRNLiaNLSQVQTFLYGNDGSNDVI--LGFLPLYhiYGLFTTLASLLNGATVIIMPKFDSELFLDLIEKYK---ITFLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1800 L-PPVVL-----DSILPEDIPSLQTVSTGGErcPI------KVAKRWSLDrNFYNVYGPTETTIATTW--YRVSSPECVq 1865
Cdd:cd05911 242 LvPPIAAalaksPLLDKYDLSSLRVILSGGA--PLskelqeLLAKRFPNA-TIKQGYGMTETGGILTVnpDGDDKPGSV- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1866 dsvpiGTPVPNTEVFILDPDLNP-VPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFreeeilYKTGDIGKVLHDGN 1944
Cdd:cd05911 318 -----GRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGY 386
|
410 420 430
....*....|....*....|....*....|....*...
gi 497785100 1945 LEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIV 1982
Cdd:cd05911 387 LYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAV 424
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1576-2045 |
1.61e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 167.77 E-value: 1.61e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:PRK07656 19 GDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQTSL--EEKLSKSDLPYL-----CTDQSQDSEDYSLLT-------KDKSY------PEDIAYIIYTSGTT 1715
Cdd:PRK07656 99 ARGDAKALFVLGLFlgVDYSATTRLPALehvviCETEEDDPHTEKMKTftdflaaGDPAErapevdPDDVADILFTSGTT 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1716 GTPNGVMVKHSSVMNLISATIDEFNITQETKVGQ----FATISFDASlwqILMALLAGATLCVVSreeQLSTKALVKRFR 1791
Cdd:PRK07656 179 GRPKGAMLTHRQLLSNAADWAEYLGLTEGDRYLAanpfFHVFGYKAG---VNAPLMRGATILPLP---VFDPDEVFRLIE 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1792 DWNVTLADLPPVVLDSIL------PEDIPSLQTVSTGGERCPIKVAKRWSLDRNFYNV---YGPTETTIATTWYRvssPE 1862
Cdd:PRK07656 253 TERITVLPGPPTMYNSLLqhpdrsAEDLSSLRLAVTGAASMPVALLERFESELGVDIVltgYGLSEASGVTTFNR---LD 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1863 CVQDSVP--IGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLnrDDLNEKRfipHPFREEEILYkTGDIGKVL 1940
Cdd:PRK07656 330 DDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYY--DDPEATA---AAIDADGWLH-TGDLGRLD 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1941 HDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVP-HGeweEKKIIEELRSKLPE 2019
Cdd:PRK07656 404 EEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLGEVGKAYVVLkPG---AELTEEELIAYCRE 480
|
490 500 510
....*....|....*....|....*....|
gi 497785100 2020 HM----VPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK07656 481 HLakykVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1553-2045 |
5.87e-43 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 166.13 E-value: 5.87e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1553 AESQPRSIKDCIQYsfenWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGI 1632
Cdd:PRK06187 1 MQDYPLTIGRILRH----GARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1633 LKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQTSLEEKLSK--SDLP----YLCTDQSQDSE------DYSLLTKDKS 1700
Cdd:PRK06187 77 PKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDSEFVPLLAAilPQLPtvrtVIVEGDGPAAPlapevgEYEELLAAAS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1701 --YPE------DIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETkVGQFATISFDASLWQI-LMALLAGAT 1771
Cdd:PRK06187 157 dtFDFpdidenDAAAMLYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDD-VYLVIVPMFHVHAWGLpYLALMAGAK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1772 LcVVSREEQlsTKALVKRFRDWNVTLADLPPVVLDSIL------PEDIPSLQTVSTGGERCPIKVAKRWS--LDRNFYNV 1843
Cdd:PRK06187 236 Q-VIPRRFD--PENLLDLIETERVTFFFAVPTIWQMLLkaprayFVDFSSLRLVIYGGAALPPALLREFKekFGIDLVQG 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1844 YGPTET--TIATTWYRVSSPECVQDSVPIGTPVPNTEVFILDPDLNPVPM--GVIGEIYIGGVGVSNGYLNRDDLNEKRF 1919
Cdd:PRK06187 313 YGMTETspVVSVLPPEDQLPGQWTKRRSAGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAETI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1920 IPHpfreeeiLYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV 1999
Cdd:PRK06187 393 DGG-------WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGERPVAVVV 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 2000 PHGewEEKKIIEELRS---------KLPEHMvpsIFVqmEELPRLNNKKVDRHSL 2045
Cdd:PRK06187 466 LKP--GATLDAKELRAflrgrlakfKLPKRI---AFV--DELPRTSVGKILKRVL 513
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1586-1999 |
7.60e-43 |
|
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: 165.49 E-value: 7.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1586 RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDselPLNRRDFI---LKDASVGA 1662
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTAN---PLSTPAEIakqVKDSGAKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1663 IVTQTSLEEKLSKSDLPYLCTDQ----------SQDSEDYSLLTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLI 1732
Cdd:cd05904 108 AFTTAELAEKLASLALPVVLLDSaefdslsfsdLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMV 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1733 SATIDEFNITQETKVGQFATISF--DASLWQILMALLA-GATLCVVSREEQLSTKALVKRFRdwnVTLADL-PPVVL--- 1805
Cdd:cd05904 188 AQFVAGEGSNSDSEDVFLCVLPMfhIYGLSSFALGLLRlGATVVVMPRFDLEELLAAIERYK---VTHLPVvPPIVLalv 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1806 --DSILPEDIPSLQTVSTGGERCPIKVAKRWSldRNFYNV-----YGPTETTIATTwyRVSSPECVQD-SVPIGTPVPNT 1877
Cdd:cd05904 265 ksPIVDKYDLSSLRQIMSGAAPLGKELIEAFR--AKFPNVdlgqgYGMTESTGVVA--MCFAPEKDRAkYGSVGRLVPNV 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1878 EVFILDPDLN-PVPMGVIGEIYIGGVGVSNGYLNRDDLNEKrfiphPFREEEILyKTGDIGKVLHDGNLEHLGRLDHQIK 1956
Cdd:cd05904 341 EAKIVDPETGeSLPPNQTGELWIRGPSIMKGYLNNPEATAA-----TIDKEGWL-HTGDLCYIDEDGYLFIVDRLKELIK 414
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 497785100 1957 VRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV 1999
Cdd:cd05904 415 YKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVV 457
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
49-473 |
1.26e-42 |
|
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: 162.09 E-value: 1.26e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 49 YPLSSIQKQIwFMSQLNPelPIYNEHLIKINLSGKVNIEALKKSFEQIVNRHQILRMRVKQT--EDSIEQVITKS-EPTI 125
Cdd:cd19542 2 YPCTPMQEGM-LLSQLRS--PGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESsaEGTFLQVVLKSlDPPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 126 QFLslrgisgEEQQEILSEYCRKEANYPyRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNmys 205
Cdd:cd19542 79 EEV-------ETDEDSLDALTRDLLDDP-TLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYN--- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 206 qngeinpeQSQEELTIQYHDYAlwqeKLLTSENLEKGLEYWKEKLEG----DLPMLSIGGITQEGTGVGSEYnfkipnil 281
Cdd:cd19542 148 --------GQLLPPAPPFSDYI----SYLQSQSQEESLQYWRKYLQGaspcAFPSLSPKRPAERSLSSTRRS-------- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 282 TDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRN--IRETRNVIGPFINTVVIRTKAEQNLSVIEYLQ 359
Cdd:cd19542 208 LAKLEAFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLR 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 360 QVHETTIQALENQDVPFEKVVEVLNpnrDVRANPFYQLLFVMQ--EPPTQFSLPGIKVEYELIPTEVARFPLTLSIIE-G 436
Cdd:cd19542 288 QLQQQYLRSLPHQHLSLREIQRALG---LWPSGTLFNTLVSYQnfEASPESELSGSSVFELSAAEDPTEYPVAVEVEPsG 364
|
410 420 430
....*....|....*....|....*....|....*..
gi 497785100 437 EEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSP 473
Cdd:cd19542 365 DSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
533-999 |
2.36e-42 |
|
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: 162.23 E-value: 2.36e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 533 TYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITHSe 612
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDS- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 613 yktSYEGYEVPILYIDQLDdfLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDR 692
Cdd:TIGR01923 80 ---LLEEKDFQADSLDRIE--AAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTEDDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 693 YLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEdaidpAKVEEIVQGKAIDWYKITPSHLKALSSESGTKLFPRKgLILGG 772
Cdd:TIGR01923 155 WLLSLPLYHISGLSILFRWLIEGATLRIVDKF-----NQLLEMIANERVTHISLVPTQLNRLLDEGGHNENLRK-ILLGG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 773 EASEWSWIKE-IYRNIPasckLFNHYGPSET--TIGVAVYEVTKKGLSNqfsttpiGSSLSNNRIYILDDKLRPVpsgip 849
Cdd:TIGR01923 229 SAIPAPLIEEaQQYGLP----IYLSYGMTETcsQVTTATPEMLHARPDV-------GRPLAGREIKIKVDNKEGH----- 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 850 GHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSH 929
Cdd:TIGR01923 293 GEIMVKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQH 365
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497785100 930 PSITEAIVtVTKVRNE--EQLVAYYVSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:TIGR01923 366 PGIQEAVV-VPKPDAEwgQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
520-1001 |
2.75e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 164.20 E-value: 2.75e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:PRK06187 20 PDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYIL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIITHSEYKTSYEG--YEVP----ILYIDQLDDFLLDER------------EDNLNVDCDSSQLAYGIYTSGST 661
Cdd:PRK06187 100 NDAEDRVVLVDSEFVPLLAAilPQLPtvrtVIVEGDGPAAPLAPEvgeyeellaaasDTFDFPDIDENDAAAMLYTSGTT 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 662 GIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLlkeDAIDPAKVEEIVQGKai 741
Cdd:PRK06187 180 GHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIVPMFHVHAWGLPYLALMAGAKQVIP---RRFDPENLLDLIETE-- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 742 dwyKITPSH-----LKALSSE---SGTKLFPRKGLILGGEAsewswikeiyrnIPAS----------CKLFNHYGPSETT 803
Cdd:PRK06187 255 ---RVTFFFavptiWQMLLKApraYFVDFSSLRLVIYGGAA------------LPPAllrefkekfgIDLVQGYGMTETS 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 804 iGVAVYEVTKKGLSNQFS---TTpiGSSLSNNRIYILDDKLRPVP--SGIPGHIYIAGEQVARGYLNREELTAERFmedp 878
Cdd:PRK06187 320 -PVVSVLPPEDQLPGQWTkrrSA--GRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETI---- 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 879 fitDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEaiVTVTKVRNE---EQLVAYYVSK 955
Cdd:PRK06187 393 ---DGGWLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAE--VAVIGVPDEkwgERPVAVVVLK 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 497785100 956 --KEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPE 1001
Cdd:PRK06187 468 pgATLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLRE 515
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
50-399 |
4.06e-42 |
|
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: 161.27 E-value: 4.06e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 50 PLSSIQKQIWFMSQLNPELPIYNeHLIKINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVITKSePTIQfLS 129
Cdd:cd20483 3 PMSTFQRRLWFLHNFLEDKTFLN-LLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDD-PSFH-LI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 130 LRGISGEEQQEI-LSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYSQNg 208
Cdd:cd20483 80 VIDLSEAADPEAaLDQLVRNLRRQELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDALRAG- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 209 eiNPEQSQEELTIQYHDYALWQEKLLTSENLEKGLEYWKEKLEG-------------DLPMLSIGGItqegtgvgSEYNF 275
Cdd:cd20483 159 --RDLATVPPPPVQYIDFTLWHNALLQSPLVQPLLDFWKEKLEGipdaskllpfakaERPPVKDYER--------STVEA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 276 KIPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVI 355
Cdd:cd20483 229 TLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFD 308
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 497785100 356 EYLQQVHETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLF 399
Cdd:cd20483 309 DLLESTKTTCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAV 352
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1587-2045 |
6.31e-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: 160.72 E-value: 6.31e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1587 SYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQ 1666
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1667 TSLEeklsksdlpylctdqsqdsedyslltkdksypeDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQE-T 1745
Cdd:cd05935 81 SELD---------------------------------DLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSdV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1746 KVGQ---FATISFDASLwqiLMALLAGATLCVVSREEQlstKALVKRFRDWNVTL-ADLPPVVLD-----SILPEDIPSL 1816
Cdd:cd05935 128 ILAClplFHVTGFVGSL---NTAVYVGGTYVLMARWDR---ETALELIEKYKVTFwTNIPTMLVDllatpEFKTRDLSSL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1817 QTVSTGGERCPIKVAKRWsLDR---NFYNVYGPTETTIATTwyrvSSPECVQDSVPIGTPVPNTEVFILDP-DLNPVPMG 1892
Cdd:cd05935 202 KVLTGGGAPMPPAVAEKL-LKLtglRFVEGYGLTETMSQTH----TNPPLRPKLQCLGIP*FGVDARVIDIeTGRELPPN 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1893 VIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREeeiLYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLN 1972
Cdd:cd05935 277 EVGEIVVRGPQIFKGYWNRPEETEESFIEIKGRR---FFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLY 353
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497785100 1973 LQTGVKEAIVQPLGDNQNYHTLVAYVV----PHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05935 354 KHPAI*EVCVISVPDERVGEEVKAFIVlrpeYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
530-994 |
7.54e-42 |
|
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: 162.00 E-value: 7.54e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 530 RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKEriEIITQ--DSKLKAI 607
Cdd:cd05911 9 KELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTAD--ELAHQlkISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 608 IT-HSEYKTSYE-------GYEV--------PILYIDQLDDFLLDEREDNL---NVDCDSsQLAYGIYTSGSTGIPKGVL 668
Cdd:cd05911 87 FTdPDGLEKVKEaakelgpKDKIivlddkpdGVLSIEDLLSPTLGEEDEDLpppLKDGKD-DTAAILYSSGTTGLPKGVC 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 669 VEHRNL--SNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLffllkedAIDPaKVEEIVQGKAIDWYKI 746
Cdd:cd05911 166 LSHRNLiaNLSQVQTFLYGNDGSNDVILGFLPLYHIYGLFTTLASLLNGATV-------IIMP-KFDSELFLDLIEKYKI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 747 T-----PSHLKALSSESGTKLFPRKGL--ILGGEASEWSWIKEIYRNIPASCKLFNHYGPSETTIGVAVYevtkKGLSNQ 819
Cdd:cd05911 238 TflylvPPIAAALAKSPLLDKYDLSSLrvILSGGAPLSKELQELLAKRFPNATIKQGYGMTETGGILTVN----PDGDDK 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 820 FSTTpiGSSLSNNRIYILDDKLRP-VPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKILYTG 898
Cdd:cd05911 314 PGSV--GRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDG 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 899 EIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKK--EVLDKDLQTYLKQKLPpnl 975
Cdd:cd05911 386 YLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADaAVIGIPDEVSGELPRAYVVRKPgeKLTEKEVKDYVAKKVA--- 462
|
490 500
....*....|....*....|....
gi 497785100 976 vPAY-----LVKMDTLPRHAHGKI 994
Cdd:cd05911 463 -SYKqlrggVVFVDEIPKSASGKI 485
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1569-2045 |
6.50e-41 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 159.36 E-value: 6.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1569 ENW----VRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDS 1644
Cdd:PRK03640 5 PNWlkqrAFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1645 ELPLNRRDFILKDASVGAIVTQTSLEEKLSKSDLPYLCTDQSQDSEDYSLLTkdkSYPED-IAYIIYTSGTTGTPNGVMV 1723
Cdd:PRK03640 85 RLSREELLWQLDDAEVKCLITDDDFEAKLIPGISVKFAELMNGPKEEAEIQE---EFDLDeVATIMYTSGTTGKPKGVIQ 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1724 ---KH-----SSVMNLISATIDEFNItqetkvgqfATISFDASLWQILM-ALLAGATLCVVSR-EEQLSTKALVKRfrdw 1793
Cdd:PRK03640 162 tygNHwwsavGSALNLGLTEDDCWLA---------AVPIFHISGLSILMrSVIYGMRVVLVEKfDAEKINKLLQTG---- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1794 NVTLADLPPVVLDSILpEDIP------SLQTVSTGGERCP---IKVAKRWSLDrnFYNVYGPTETT--IATTwyrvsSPE 1862
Cdd:PRK03640 229 GVTIISVVSTMLQRLL-ERLGegtypsSFRCMLLGGGPAPkplLEQCKEKGIP--VYQSYGMTETAsqIVTL-----SPE 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1863 CVQDSV-PIGTPVPNTEVFILDpDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFreeeilyKTGDIGKVLH 1941
Cdd:PRK03640 301 DALTKLgSAGKPLFPCELKIEK-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1942 DGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHM 2021
Cdd:PRK03640 373 EGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYK 452
|
490 500
....*....|....*....|....
gi 497785100 2022 VPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK03640 453 VPKRFYFVEELPRNASGKLLRHEL 476
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1568-2040 |
1.07e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 160.13 E-value: 1.07e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSS---PNHIALRFLDRSYTYDEVNKRANKIANQLY-KMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPID 1643
Cdd:PRK08314 13 FHNLEVSArryPDKTAIVFYGRAISYRELLEEAERLAGYLQqECGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1644 selPLNRRD---FILKDA-SVGAIVTQtSLEEKLSK---------------SD---------LPYLCT----DQSQDSED 1691
Cdd:PRK08314 93 ---PMNREEelaHYVTDSgARVAIVGS-ELAPKVAPavgnlrlrhvivaqySDylpaepeiaVPAWLRaeppLQALAPGG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1692 YSLLTKD----------KSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVgqFATIS-FDASLW 1760
Cdd:PRK08314 169 VVAWKEAlaaglappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVV--LAVLPlFHVTGM 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1761 QILM--ALLAGATLCVVSREEQLSTKALVKRFRdwnVTL-ADLPPVVLD-----SILPEDIPSLQTVSTGGERCPIKVAK 1832
Cdd:PRK08314 247 VHSMnaPIYAGATVVLMPRWDREAAARLIERYR---VTHwTNIPTMVVDflaspGLAERDLSSLRYIGGGGAAMPEAVAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1833 RWsLDR---NFYNVYGPTEtTIATTwyrVSSP------ECvqdsvpIGTPVPNTEVFILDPD-LNPVPMGVIGEIYIGGV 1902
Cdd:PRK08314 324 RL-KELtglDYVEGYGLTE-TMAQT---HSNPpdrpklQC------LGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1903 GVSNGYLNRDDLNEKRFIphpfreeEI----LYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVK 1978
Cdd:PRK08314 393 QVFKGYWNRPEATAEAFI-------EIdgkrFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQ 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 1979 EAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHM----VPSIFVQMEELPRLNNKKV 2040
Cdd:PRK08314 466 EACVIATPDPRRGETVKAVVVLRPEARGKTTEEEIIAWAREHMaaykYPRIVEFVDSLPKSGSGKI 531
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
521-999 |
1.33e-40 |
|
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: 157.07 E-value: 1.33e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 521 NSIALSDHERSYTYLQTNNRANQIARWLQKQG-IGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPkerieiit 599
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYP-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 qDSKLKAIITHSEyktsyegyevPILYIDqlddfllderednlnvdcdssqLAYGIYTSGSTGIPKGVLVEHRNLSNYIY 679
Cdd:cd05941 73 -LAELEYVITDSE----------PSLVLD----------------------PALILYTSGTTGRPKGVVLTHANLAANVR 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 680 AIQTKLGNKPKDRYLLlqslaydfCL---------TTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQG-----------K 739
Cdd:cd05941 120 ALVDAWRWTEDDVLLH--------VLplhhvhglvNALLCPLFAGASVEFLPKFDPKEVAISRLMPSItvfmgvptiytR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 740 AIDWYKITPSHLKALSSESGTKLfpRkgLILGGEA-------SEWswikeiyrnipasCKLFNH-----YGPSEttIGVA 807
Cdd:cd05941 192 LLQYYEAHFTDPQFARAAAAERL--R--LMVSGSAalpvptlEEW-------------EAITGHtllerYGMTE--IGMA 252
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 808 vyevtkkgLSNQFSTTPI----GSSLSNNRIYILDDK-LRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitd 882
Cdd:cd05941 253 --------LSNPLDGERRpgtvGMPLPGVQARIVDEEtGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW--- 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 883 srmYKTGDIGKILYTGEIQFLGRL-DGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKKEVLD 960
Cdd:cd05941 322 ---FKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSEcAVIGVPDPDWGERVVAVVVLRAGAAA 398
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 497785100 961 KDLQ---TYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05941 399 LSLEelkEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1585-2046 |
1.69e-40 |
|
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: 156.30 E-value: 1.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1585 DRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELplnRRDF---ILKDASVG 1661
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTAL---RGDElayIIDHSGAQ 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1662 AIVTqtsleeklsksdlpylctdqsqdsedyslltkdksypeDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNI 1741
Cdd:cd05934 78 LVVV--------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGL 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1742 TQEtKVGQFATISF--DASLWQILMALLAGATLCVVSReeqLSTKALVKRFRDWNVTLADLPPVVLDSILPedipslQTV 1819
Cdd:cd05934 120 GED-DVYLTVLPLFhiNAQAVSVLAALSVGATLVLLPR---FSASRFWSDVRRYGATVTNYLGAMLSYLLA------QPP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1820 STGGERCPIKVA--------------KRWSLdrNFYNVYGPTETTIATtwyrVSSPECVQDSVPIGTPVPNTEVFILDPD 1885
Cdd:cd05934 190 SPDDRAHRLRAAygapnppelheefeERFGV--RLLEGYGMTETIVGV----IGPRDEPRRPGSIGRPAPGYEVRIVDDD 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1886 LNPVPMGVIGEIYIGGV---GVSNGYLNRDDLNEKRFiphpfreEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRI 1962
Cdd:cd05934 264 GQELPAGEPGELVIRGLrgwGFFKGYYNMPEATAEAM-------RNGWFHTGDLGYRDADGFFYFVDRKKDMIRRRGENI 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1963 ELGEIESLLNLQTGVKEAIV----QPLGDNQnyhTLVAYVVPHGEWEEKKIIEE-LRSKLPEHMVPSiFVQM-EELPRLN 2036
Cdd:cd05934 337 SSAEVERAILRHPAVREAAVvavpDEVGEDE---VKAVVVLRPGETLDPEELFAfCEGQLAYFKVPR-YIRFvDDLPKTP 412
|
490
....*....|
gi 497785100 2037 NKKVDRHSLP 2046
Cdd:cd05934 413 TEKVAKAQLR 422
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
539-999 |
2.27e-39 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 154.14 E-value: 2.27e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 539 NRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGA----YLPLDVESPKERIEIITQDSKLKAIITH---- 610
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADagaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 611 SEYKTSYEGYEVPILYIDQldDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPK 690
Cdd:cd05922 81 DRLRDALPASPDPGTVLDA--DGIRAARASAPAHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYLGITAD 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 691 DRYLLLQSLAYDFCLTTIYTSLLSGGTLffLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSesgTKLFPRKGLIL 770
Cdd:cd05922 159 DRALTVLPLSYDYGLSVLNTHLLRGATL--VLTNDGVLDDAFWEDLREHGATGLAGVPSTYAMLTR---LGFDPAKLPSL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 771 ------GGEASEwSWIKEIYRNIPAScKLFNHYGPSETTIGVAVY---EVTKKGLSnqfsttpIGSSLSNNRIYILDDKL 841
Cdd:cd05922 234 ryltqaGGRLPQ-ETIARLRELLPGA-QVYVMYGQTEATRRMTYLppeRILEKPGS-------IGLAIPGGEFEILDDDG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 842 RPVPSGIPGHIYIAGEQVARGYLNREEltaerFMEDPFITDSRMYkTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEE 921
Cdd:cd05922 305 TPTPPGEPGEIVHRGPNVMKGYWNDPP-----YRRKEGRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTE 378
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 922 IQSQLLSHPSITEAIVTVTKVRNEEQLVAYYVSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05922 379 IEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1587-2045 |
2.78e-39 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 153.31 E-value: 2.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1587 SYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIdseLPLNRRD---FILKDASVGAI 1663
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPI---LPFFREHelaFILRRAKAKVF 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1664 VTQTSLEEklsksdlpylcTDQSQDsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQ 1743
Cdd:cd05903 78 VVPERFRQ-----------FDPAAM-------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGP 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1744 EtkvGQFATIS----FDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRdwnVTLADLPPVVLDSIL------PEDI 1813
Cdd:cd05903 134 G---DVFLVASpmahQTGFVYGFTLPLLLGAPVVLQDIWDPDKALALMREHG---VTFMMGATPFLTDLLnaveeaGEPL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1814 PSLQTVSTGGERCPIKVAKRWS--LDRNFYNVYGPTETTIATTwyRVSSPECVQDSVPIGTPVPNTEVFILDPDLNPVPM 1891
Cdd:cd05903 208 SRLRTFVCGGATVPRSLARRAAelLGAKVCSAYGSTECPGAVT--SITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1892 GVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfreEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLL 1971
Cdd:cd05903 286 GVEGELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLL 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497785100 1972 NLQTGVKEAIVQPLGDNQNYHTLVAYVV---PHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05903 359 LGHPGVIEAAVVALPDERLGERACAVVVtksGALLTFDELVAYLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1587-2045 |
3.17e-39 |
|
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: 152.50 E-value: 3.17e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1587 SYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAivtq 1666
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1667 tsleeklsksdlpylctdqsqdsedyslltkdksypEDIAYIIYTSGTTGTPNGVMVK---H-----SSVMNLisatide 1738
Cdd:cd05912 77 ------------------------------------DDIATIMYTSGTTGKPKGVQQTfgnHwwsaiGSALNL------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1739 fNITQETKVGQFATIsFDASLWQILM-ALLAGATLCVVSR-EEQLSTKALVKRfrdwNVTLADLPPVVLD---SILPEDI 1813
Cdd:cd05912 114 -GLTEDDNWLCALPL-FHISGLSILMrSVIYGMTVYLVDKfDAEQVLHLINSG----KVTIISVVPTMLQrllEILGEGY 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1814 P-SLQTVSTGGERCP---IKVAKrwslDRNF--YNVYGPTETT--IATTwyrvsSPECVQDSV-PIGTPVPNTEVFILDP 1884
Cdd:cd05912 188 PnNLRCILLGGGPAPkplLEQCK----EKGIpvYQSYGMTETCsqIVTL-----SPEDALNKIgSAGKPLFPVELKIEDD 258
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1885 DLNPvpmGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfreEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIEL 1964
Cdd:cd05912 259 GQPP---YEVGEILLKGPNVTKGYLNRPDATEESF-------ENGWFKTGDIGYLDEEGFLYVLDRRSDLIISGGENIYP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1965 GEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHS 2044
Cdd:cd05912 329 AEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHE 408
|
.
gi 497785100 2045 L 2045
Cdd:cd05912 409 L 409
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
512-1002 |
4.61e-39 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 155.27 E-value: 4.61e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNT------------PNSIAL-----SDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAML 574
Cdd:COG0365 3 FVGGRLNIayncldrhaegrGDKVALiwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 575 GVLKAGGAYLP----LDVESPKERIEiitqDSKLKAIITHSEYktSYEGYEVPilYIDQLD------------------- 631
Cdd:COG0365 83 ACARIGAVHSPvfpgFGAEALADRIE----DAEAKVLITADGG--LRGGKVID--LKEKVDealeelpslehvivvgrtg 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 632 -------DFLLDEREDNLNVDCDSSQL-----AYGIYTSGSTGIPKGVLVEHRN-LSNYIYAIQTKLGNKPKDRYlllqs 698
Cdd:COG0365 155 advpmegDLDWDELLAAASAEFEPEPTdaddpLFILYTSGTTGKPKGVVHTHGGyLVHAATTAKYVLDLKPGDVF----- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 699 laydFCLTTI----------YTSLLSGGTLFFL-LKEDAIDPAKVEEIVQgKaidwYKIT-----PSHLKALSSEsGTKL 762
Cdd:COG0365 230 ----WCTADIgwatghsyivYGPLLNGATVVLYeGRPDFPDPGRLWELIE-K----YGVTvfftaPTAIRALMKA-GDEP 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 763 FPR------KGLILGGEASE---WSWIkeiYRNIpaSCKLFNHYGPSETT---IGVAVYEVTKKGlsnqfSTT-PI-Gss 828
Cdd:COG0365 300 LKKydlsslRLLGSAGEPLNpevWEWW---YEAV--GVPIVDGWGQTETGgifISNLPGLPVKPG-----SMGkPVpG-- 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 829 lsnNRIYILDDKLRPVPSGIPGHIYIAGEQ--VARGYLNREELTAERFMEdpfiTDSRMYKTGDIGKILYTGEIQFLGRL 906
Cdd:COG0365 368 ---YDVAVVDEDGNPVPPGEEGELVIKGPWpgMFRGYWNDPERYRETYFG----RFPGWYRTGDGARRDEDGYFWILGRS 440
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 907 DGQVKIRGIRVEPEEIQSQLLSHPSITEAIVT-----VTKVRneeqLVAYYVSKKEV-----LDKDLQTYLKQKLPPNLV 976
Cdd:COG0365 441 DDVINVSGHRIGTAEIESALVSHPAVAEAAVVgvpdeIRGQV----VKAFVVLKPGVepsdeLAKELQAHVREELGPYAY 516
|
570 580
....*....|....*....|....*.
gi 497785100 977 PAYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:COG0365 517 PREIEFVDELPKTRSGKIMRRLLRKI 542
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
519-996 |
5.64e-39 |
|
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: 152.38 E-value: 5.64e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEII 598
Cdd:cd17631 8 HPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAIIthseyktsyegyevpilyidqlDDfllderednlnvdcdssqLAYGIYTSGSTGIPKGVLVEHRNLSNYI 678
Cdd:cd17631 88 LADSGAKVLF----------------------DD------------------LALLMYTSGTTGRPKGAMLTHRNLLWNA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 679 YAIQTKLGNKPKDRYLLLQSLaYDFCLTTIYT--SLLSGGTLFFLlkeDAIDPAKVEEivqgkAIDWYKIT-----PSHL 751
Cdd:cd17631 128 VNALAALDLGPDDVLLVVAPL-FHIGGLGVFTlpTLLRGGTVVIL---RKFDPETVLD-----LIERHRVTsfflvPTMI 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 752 KALSSE---SGTKLFPRKGLILGGEASEWSWIKEIYRnipASCKLFNHYGPSETTIGVAVY---EVTKKGLSnqfsttpI 825
Cdd:cd17631 199 QALLQHprfATTDLSSLRAVIYGGAPMPERLLRALQA---RGVKFVQGYGMTETSPGVTFLspeDHRRKLGS-------A 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 826 GSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmyKTGDIGKILYTGEIQFLGR 905
Cdd:cd17631 269 GRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDR 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 906 LDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYV--SKKEVLDKDLQTYLKQKLPPNLVPAYLVK 982
Cdd:cd17631 342 KKDMIISGGENVYPAEVEDVLYEHPAVAEvAVIGVPDEKWGEAVVAVVVprPGAELDEDELIAHCRERLARYKIPKSVEF 421
|
490
....*....|....
gi 497785100 983 MDTLPRHAHGKIDR 996
Cdd:cd17631 422 VDALPRNATGKILK 435
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1547-2045 |
9.54e-39 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 154.43 E-value: 9.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1547 DLLVKKAESQPRSIKDCIQYSFEN---------WVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVAL 1617
Cdd:PRK06178 9 ELRALQQAAWPAGIPREPEYPHGErplteylraWARERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1618 YHERSSEMIFGFLGILKCGAAYVPIDselPLNRR---DFILKDASVGAIVT-------------QTSLEEKLSKS----- 1676
Cdd:PRK06178 89 FLPNCPQFHIVFFGILKLGAVHVPVS---PLFREhelSYELNDAGAEVLLAldqlapvveqvraETSLRHVIVTSladvl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1677 ------DLPYLCTDQSQDSEDY-SLLT----------KDKSYPEDIAYIIYTSGTTGTPNGV------MVKHSSVMNLIS 1733
Cdd:PRK06178 166 paeptlPLPDSLRAPRLAAAGAiDLLPalractapvpLPPPALDALAALNYTGGTTGMPKGCehtqrdMVYTAAAAYAVA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1734 ATIDEFNITqetkvgqfatISFDASLW------QILMALLAGATLCVVSREEQLSTKALVKRFRdwnVTLADLPPVVLDS 1807
Cdd:PRK06178 246 VVGGEDSVF----------LSFLPEFWiagenfGLLFPLFSGATLVLLARWDAVAFMAAVERYR---VTRTVMLVDNAVE 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1808 IL--PE----DIPSLQTVstggeRCPIKVAK-------RW-----SLDRNFynVYGPTETTIA---TTWYRVSSPECVQD 1866
Cdd:PRK06178 313 LMdhPRfaeyDLSSLRQV-----RVVSFVKKlnpdyrqRWraltgSVLAEA--AWGMTETHTCdtfTAGFQDDDFDLLSQ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1867 SVPIGTPVPNTEVFILDPDLN-PVPMGVIGEIYIGGVGVSNGYLNRDDLNEkrfipHPFREEeiLYKTGDIGKVLHDGNL 1945
Cdd:PRK06178 386 PVFVGLPVPGTEFKICDFETGeLLPLGAEGEIVVRTPSLLKGYWNKPEATA-----EALRDG--WLHTGDIGKIDEQGFL 458
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1946 EHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPhgEWEEKKIIEELRSKLPEHM---- 2021
Cdd:PRK06178 459 HYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKGQVPVAFVQL--KPGADLTAAALQAWCRENMavyk 536
|
570 580
....*....|....*....|....
gi 497785100 2022 VPSIFVQmEELPRLNNKKVDRHSL 2045
Cdd:PRK06178 537 VPEIRIV-DALPMTATGKVRKQDL 559
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
49-473 |
1.32e-38 |
|
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: 150.68 E-value: 1.32e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 49 YPLSSIQKQIWFMSQLNPELPIYnEHLIKINLSGKVNIEALKKSFEQIVNRHQILR--MRVKQTEDSIEQVITKSEPTIQ 126
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVY-LHNYTYTVGRRLNLDLLLEALQVLIDRHDILRtsFIEDGLGQPVQVVHRQAQVPVT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 127 FLSLRGisGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVL-FSRHHILSDGWSASILLSELERFYNMys 205
Cdd:cd19536 81 ELDLTP--LEEQLDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERERFLLvISDHHSILDGWSLYLLVKEILAVYNQ-- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 206 qngeiNPEQSQEEL--TIQYHDYALWQEKLLTSENLEKgleYWKEKLEG-DLPMLSIGGITQEGTGVGSEYNFKIPNILT 282
Cdd:cd19536 157 -----LLEYKPLSLppAQPYRDFVAHERASIQQAASER---YWREYLAGaTLATLPALSEAVGGGPEQDSELLVSVPLPV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 283 DKlRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRN--IRETRNVIGPFINTVVIRTKAEQNlSVIEYLQQ 360
Cdd:cd19536 229 RS-RSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSeeTTGAERLLGLFLNTLPLRVTLSEE-TVEDLLKR 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 361 VHETTIQALENQDVPfekvveVLNPNRDVRANPFYQLLFVMQEPPTQFSLPGIK-----VEYELIPTEVARFPLTLSII- 434
Cdd:cd19536 307 AQEQELESLSHEQVP------LADIQRCSEGEPLFDSIVNFRHFDLDFGLPEWGsdegmRRGLLFSEFKSNYDVNLSVLp 380
|
410 420 430
....*....|....*....|....*....|....*....
gi 497785100 435 EGEEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSP 473
Cdd:cd19536 381 KQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1588-2045 |
2.44e-38 |
|
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: 150.66 E-value: 2.44e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1588 YTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDselplnrrdfilkdasvgAIVTQT 1667
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLF------------------ALFGPE 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1668 SLEEKLSKSDLPYLCTDQSqdsedyslltkdksypEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETkv 1747
Cdd:cd05971 69 ALEYRLSNSGASALVTDGS----------------DDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRD-- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1748 gqfATISFDASLWQ--------ILMALLAGATLcVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSILPEDIP----- 1814
Cdd:cd05971 131 ---GDLYWTPADWAwigglldvLLPSLYFGVPV-LAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQlkhaq 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1815 -SLQTVSTGGERcPIKVAKRWSLDR---NFYNVYGPTETTIATTWYRVSSPecvQDSVPIGTPVPNTEVFILDPDLNPVP 1890
Cdd:cd05971 207 vKLRAIATGGES-LGEELLGWAREQfgvEVNEFYGQTECNLVIGNCSALFP---IKPGSMGKPIPGHRVAIVDDNGTPLP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1891 MGVIGEIyigGVGVSN-----GYLNRDDLNEKRFIPHPFReeeilykTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELG 1965
Cdd:cd05971 283 PGEVGEI---AVELPDpvaflGYWNNPSATEKKMAGDWLL-------TGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPA 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1966 EIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV-PHGEWEEKKIIEEL----RSKLPEHMVPSIFVQMEELPRLNNKKV 2040
Cdd:cd05971 353 EIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlNPGETPSDALAREIqelvKTRLAAHEYPREIEFVNELPRTATGKI 432
|
....*
gi 497785100 2041 DRHSL 2045
Cdd:cd05971 433 RRREL 437
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
49-380 |
2.54e-38 |
|
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: 149.83 E-value: 2.54e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 49 YPLSSIQKQIWFMSQLNPELPIYN-EHLIKINlsGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVITKSEPT-IQ 126
Cdd:cd19533 2 LPLTSAQRGVWFAEQLDPEGSIYNlAEYLEIT--GPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVpIR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 127 FLSLRGISGEEqqEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYSQ 206
Cdd:cd19533 80 HIDLSGDPDPE--GAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYTALLK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 207 nGEINPEQSqeeltiqYHDYALWQEK---LLTSENLEKGLEYWKEKLEGDLPMLSIGGITQEGTGVGSEYNFKIPNILTD 283
Cdd:cd19533 158 -GRPAPPAP-------FGSFLDLVEEeqaYRQSERFERDRAFWTEQFEDLPEPVSLARRAPGRSLAFLRRTAELPPELTR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 284 KLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTKAEQNLSVIEYLQQVHE 363
Cdd:cd19533 230 TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSR 309
|
330
....*....|....*..
gi 497785100 364 TTIQALENQDVPFEKVV 380
Cdd:cd19533 310 ELRSLLRHQRYRYEDLR 326
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1585-2045 |
1.71e-37 |
|
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: 147.99 E-value: 1.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1585 DRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIV 1664
Cdd:cd05919 8 DRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 TqtsleeklsksdlpylctdqSQDsedyslltkdksypeDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDE-FNITQ 1743
Cdd:cd05919 88 T--------------------SAD---------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAREaLGLTP 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1744 ETKVGQFATISFDASLWQILM-ALLAGATLCV----VSREEQLSTKAlvkRFRD---WNVtladlpPVVLDSIL------ 1809
Cdd:cd05919 133 GDRVFSSAKMFFGYGLGNSLWfPLAVGASAVLnpgwPTAERVLATLA---RFRPtvlYGV------PTFYANLLdscags 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1810 PEDIPSLQTVSTGGERCPIKVAKRWsldrnfynvygpTETTIATTWYRVSSPECVQ-------DSVPIGT---PVPNTEV 1879
Cdd:cd05919 204 PDALRSLRLCVSAGEALPRGLGERW------------MEHFGGPILDGIGATEVGHiflsnrpGAWRLGStgrPVPGYEI 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1880 FILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRfiphpFREEeiLYKTGDIGKVLHDGNLEHLGRLDHQIKVRG 1959
Cdd:cd05919 272 RLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRAT-----FNGG--WYRTGDKFCRDADGWYTHAGRADDMLKVGG 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1960 FRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKI-----IEELRSKLPEHMVPSIFVQMEELPR 2034
Cdd:cd05919 345 QWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKSPAAPQESlardiHRHLLERLSAHKVPRRIAFVDELPR 424
|
490
....*....|.
gi 497785100 2035 LNNKKVDRHSL 2045
Cdd:cd05919 425 TATGKLQRFKL 435
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1588-2045 |
1.28e-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: 145.17 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1588 YTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSEL---PLNRRdfiLKDASVGAIV 1664
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLgpkDIEYR---LEAAGAKAIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 TQTsleeklsksdlpylctdqsqdsedyslltkdksypEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQE 1744
Cdd:cd05972 78 TDA-----------------------------------EDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPD 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1745 TKVGQFATISFDASLWQILMA-LLAGATLcVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSILPEDIPS-----LQT 1818
Cdd:cd05972 123 DIHWNIADPGWAKGAWSSFFGpWLLGATV-FVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSSykfshLRL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1819 VSTGGERCPIKVAKRW--SLDRNFYNVYGPTETTIATTWYRvsspecVQDSVP--IGTPVPNTEVFILDPDLNPVPMGVI 1894
Cdd:cd05972 202 VVSAGEPLNPEVIEWWraATGLPIRDGYGQTETGLTVGNFP------DMPVKPgsMGRPTPGYDVAIIDDDGRELPPGEE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1895 GEIYI--GGVGVSNGYLNrddlNEKRFIPHpFREEeiLYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLN 1972
Cdd:cd05972 276 GDIAIklPPPGLFLGYVG----DPEKTEAS-IRGD--YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESALL 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 1973 LQTGVKEAIVQPLGDNQNYHTLVAYVV-----PHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05972 349 EHPAVAEAAVVGSPDPVRGEVVKAFVVltsgyEPSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
47-473 |
5.42e-36 |
|
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: 143.39 E-value: 5.42e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 47 GSYPLSSIQKQIWFMSQLNPELPIYnEHLIKINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVITKSEPTIQ 126
Cdd:cd19546 3 DEVPATAGQLRTWLLARLDEETRGR-HLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAARP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 127 FLSLRGISGEEQQEILSEycrkEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMySQ 206
Cdd:cd19546 82 ELPVVPATEEELPALLAD----RAAHLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYGA-RR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 207 NGEInPEQSqeELTIQYHDYALWQEKLLTSENLEKGL-----EYWKEKLEGDLPMLSI------GGITQEGTGvgsEYNF 275
Cdd:cd19546 157 EGRA-PERA--PLPLQFADYALWERELLAGEDDRDSLigdqiAYWRDALAGAPDELELptdrprPVLPSRRAG---AVPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 276 KIPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIR-ETRNVIGPFINTVVIRTKAEQNLSV 354
Cdd:cd19546 231 RLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTF 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 355 IEYLQQVHETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLFVMQEPPTQ----FSLPGIKVEYELIPTEVARFPLT 430
Cdd:cd19546 311 RELLGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDpwdaPELPGLRTSPVPLGTEAMELDLS 390
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 497785100 431 LSIIE-------GEEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSP 473
Cdd:cd19546 391 LALTErrnddgdPDGLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1568-2000 |
9.44e-36 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 146.01 E-value: 9.44e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLD----RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPID 1643
Cdd:COG1022 17 LRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1644 SELPLNRRDFILKDASVGAIVTQTslEEKLSK-----SDLPYL----CTDQSQDSEDYSLLT------------------ 1696
Cdd:COG1022 97 PTSSAEEVAYILNDSGAKVLFVED--QEQLDKllevrDELPSLrhivVLDPRGLRDDPRLLSldellalgrevadpaele 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1697 --KDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKvgqfaTISFdASLWQI------LMALLA 1768
Cdd:COG1022 175 arRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDR-----TLSF-LPLAHVfertvsYYALAA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1769 GATLCVVSreeqlSTKALVKRFRDWNVTLADLPPVVLDSIlpedipsLQTVSTGGERCP----------IKVAKRWSLDR 1838
Cdd:COG1022 249 GATVAFAE-----SPDTLAEDLREVKPTFMLAVPRVWEKV-------YAGIQAKAEEAGglkrklfrwaLAVGRRYARAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1839 ------------------------------------------------NFYN--------VYGPTETTIATTwyrVSSPE 1862
Cdd:COG1022 317 lagkspslllrlkhaladklvfsklrealggrlrfavsggaalgpelaRFFRalgipvleGYGLTETSPVIT---VNRPG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1863 CVQ-DSVpiGTPVPNTEVFIlDPDlnpvpmgviGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFreeeilYKTGDIGKVLH 1941
Cdd:COG1022 394 DNRiGTV--GPPLPGVEVKI-AED---------GEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGELDE 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1942 DGNLEHLGRLDHQIKVR-GFRIELGEIESLLNLQTGVKEAIVqpLGDNQNYhtLVAYVVP 2000
Cdd:COG1022 456 DGFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVV--VGDGRPF--LAALIVP 511
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
532-999 |
1.24e-35 |
|
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: 142.09 E-value: 1.24e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 532 YTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIIths 611
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIV--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 612 eyktsyegyevpilyidqlddfllderednlnvdCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKD 691
Cdd:cd05972 78 ----------------------------------TDAEDPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRPDD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 692 RYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSE-------SGTKLFP 764
Cdd:cd05972 124 IHWNIADPGWAKGAWSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAYRMLIKQdlssykfSHLRLVV 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 765 RKGLILGGEASEWsWIKEIyrNIPasckLFNHYGPSETTIGVAVYEVT--KKGlsnqfsttPIGSSLSNNRIYILDDKLR 842
Cdd:cd05972 204 SAGEPLNPEVIEW-WRAAT--GLP----IRDGYGQTETGLTVGNFPDMpvKPG--------SMGRPTPGYDVAIIDDDGR 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 843 PVPSGIPGHIYIAGEQVA--RGYLNREELTAERFMEDPFITDSRMYKTGDigkilytGEIQFLGRLDGQVKIRGIRVEPE 920
Cdd:cd05972 269 ELPPGEEGDIAIKLPPPGlfLGYVGDPEKTEASIRGDYYLTGDRAYRDED-------GYFWFVGRADDIIKSSGYRIGPF 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 921 EIQSQLLSHPSITEAIVT--VTKVRNeeQLVAYYVSKK------EVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHG 992
Cdd:cd05972 342 EVESALLEHPAVAEAAVVgsPDPVRG--EVVKAFVVLTsgyepsEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISG 419
|
....*..
gi 497785100 993 KIDRKAL 999
Cdd:cd05972 420 KIRRVEL 426
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
532-999 |
1.44e-35 |
|
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: 142.19 E-value: 1.44e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 532 YTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIIThs 611
Cdd:cd05971 7 VTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 612 eyktsyegyevpilyidqlddfllDErednlnvdcdSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKD 691
Cdd:cd05971 85 ------------------------DG----------SDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 692 RYLLLQSLAYDFC---LTTIYTSLLSGGTLFfLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSE-SGTKLFPRK- 766
Cdd:cd05971 131 GDLYWTPADWAWIgglLDVLLPSLYFGVPVL-AHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQgEQLKHAQVKl 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 767 -GLILGGE---ASEWSWIKEIYrNIPAScklfNHYGPSETTIGVAvyevtkkGLSNQFSTTP--IGSSLSNNRIYILDDK 840
Cdd:cd05971 210 rAIATGGEslgEELLGWAREQF-GVEVN----EFYGQTECNLVIG-------NCSALFPIKPgsMGKPIPGHRVAIVDDN 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 841 LRPVPSGIPGhiYIAGEQ---VAR-GYLNREELTaerfmEDPFITDsrMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIR 916
Cdd:cd05971 278 GTPLPPGEVG--EIAVELpdpVAFlGYWNNPSAT-----EKKMAGD--WLLTGDLGRKDSDGYFWYVGRDDDVITSSGYR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 917 VEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYV-----SKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHA 990
Cdd:cd05971 349 IGPAEIEECLLKHPAVLMaAVVGIPDPIRGEIVKAFVVlnpgeTPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTA 428
|
....*....
gi 497785100 991 HGKIDRKAL 999
Cdd:cd05971 429 TGKIRRREL 437
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1586-2045 |
2.34e-35 |
|
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: 143.28 E-value: 2.34e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1586 RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVT 1665
Cdd:cd05959 28 GSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1666 QTSL----EEKLSKSDlPYLCT------DQSQDSEDY---------SLLTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHS 1726
Cdd:cd05959 108 SGELapvlAAALTKSE-HTLVVlivsggAGPEAGALLlaelvaaeaEQLKPAATHADDPAFWLYSSGSTGRPKGVVHLHA 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1727 SvmnlISATIDEF-----NITQETKVGQFATISFDASLWQ-ILMALLAGATlcVVSREEQLSTKALVKRFRDWNVTLADL 1800
Cdd:cd05959 187 D----IYWTAELYarnvlGIREDDVCFSAAKLFFAYGLGNsLTFPLSVGAT--TVLMPERPTPAAVFKRIRRYRPTVFFG 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1801 PPVVLDSIL------PEDIPSLQTVSTGGERCPIKVAKRWsldRNFYNV-----YGPTEttiATTWYRVSSPECVQDSVP 1869
Cdd:cd05959 261 VPTLYAAMLaapnlpSRDLSSLRLCVSAGEALPAEVGERW---KARFGLdildgIGSTE---MLHIFLSNRPGRVRYGTT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1870 iGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfreEEILYKTGDIGKVLHDGNLEHLG 1949
Cdd:cd05959 335 -GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF-------QGEWTRTGDKYVRDDDGFYTYAG 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1950 RLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPH-GEWEEKKIIEEL----RSKLPEHMVPS 2024
Cdd:cd05959 407 RADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVLRpGYEDSEALEEELkefvKDRLAPYKYPR 486
|
490 500
....*....|....*....|.
gi 497785100 2025 IFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05959 487 WIVFVDELPKTATGKIQRFKL 507
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1586-2000 |
3.60e-35 |
|
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: 141.19 E-value: 3.60e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1586 RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVT 1665
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1666 QTsleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQET 1745
Cdd:cd05907 84 ED----------------------------------PDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATEGD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1746 KVGQF---ATIsFDASLWQILmALLAGATLCVVSREEQLSTkALvKRF---------RDW-----NVTLADLPPV---VL 1805
Cdd:cd05907 130 RHLSFlplAHV-FERRAGLYV-PLLAGARIYFASSAETLLD-DL-SEVrptvflavpRVWekvyaAIKVKAVPGLkrkLF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1806 DSILpedIPSLQTVSTGGERCPIKVAKRW-SLDRNFYNVYGPTETTIATTwyrVSSPECVQ-DSVpiGTPVPNTEVFIlD 1883
Cdd:cd05907 206 DLAV---GGRLRFAASGGAPLPAELLHFFrALGIPVYEGYGLTETSAVVT---LNPPGDNRiGTV--GKPLPGVEVRI-A 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1884 PDlnpvpmgviGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFreeeilYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFR-I 1962
Cdd:cd05907 277 DD---------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRKKDLIITSGGKnI 341
|
410 420 430
....*....|....*....|....*....|....*...
gi 497785100 1963 ELGEIESLLNLQTGVKEAIVqpLGDNQNYhtLVAYVVP 2000
Cdd:cd05907 342 SPEPIENALKASPLISQAVV--IGDGRPF--LVALIVP 375
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1579-2045 |
2.93e-34 |
|
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step reaction consisting of the adenylation of malonate with ATP, followed by malonyl transfer from malonyl-AMP to CoA. Malonic acid and its derivatives are the building blocks of polyketides and malonyl-CoA serves as the substrate of polyketide synthases. Malonyl-CoA synthetase has broad substrate tolerance and can activate a variety of malonyl acid derivatives. MCS may play an important role in biosynthesis of polyketides, the important secondary metabolites with therapeutic and agrochemical utility.
Pssm-ID: 341264 [Multi-domain] Cd Length: 442 Bit Score: 138.58 E-value: 2.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1579 IALRFLDRSYTYDEVNKRANKIANQLY-KMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKD 1657
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLaLGKDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1658 ASVGAIVtqtsleeklsksdlpylctdqsqdsedyslltkdksypeDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATID 1737
Cdd:cd05941 83 SEPSLVL---------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1738 EFNITQETKV----------GQFATIsfdaslwqiLMALLAGATlCVVSREEQLSTKALVKRFRDWNVTLAdLPPV---V 1804
Cdd:cd05941 124 AWRWTEDDVLlhvlplhhvhGLVNAL---------LCPLFAGAS-VEFLPKFDPKEVAISRLMPSITVFMG-VPTIytrL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1805 LDSiLPEDIPSLQTVSTGGER-----------CPIKVAKRWS-------LDRnfynvYGPTETTIATtwyrvSSP---EC 1863
Cdd:cd05941 193 LQY-YEAHFTDPQFARAAAAErlrlmvsgsaaLPVPTLEEWEaitghtlLER-----YGMTEIGMAL-----SNPldgER 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1864 VQDSVpiGTPVPNTEVFILDPDLN-PVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFreeeilYKTGDIGKVLHD 1942
Cdd:cd05941 262 RPGTV--GMPLPGVQARIVDEETGePLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW------FKTGDLGVVDED 333
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1943 GNLEHLGRL-DHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKI---IEELRSKLP 2018
Cdd:cd05941 334 GYYWILGRSsVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGERVVAVVVLRAGAAALSLeelKEWAKQRLA 413
|
490 500
....*....|....*....|....*..
gi 497785100 2019 EHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05941 414 PYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
520-1001 |
3.90e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 139.65 E-value: 3.90e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:PRK07656 19 GDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYIL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIITHSEY-KTSYEGYE-VPIL----------------YIDQLDDFL----LDEREDNLNVDcDSSQLaygIYT 657
Cdd:PRK07656 99 ARGDAKALFVLGLFlGVDYSATTrLPALehvviceteeddphteKMKTFTDFLaagdPAERAPEVDPD-DVADI---LFT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 658 SGSTGIPKGVLVEHRN-LSNYiYAIQTKLGNKPKDRYLLLQSLAYDFCLTT-IYTSLLSGGTLFFLLKedaIDPAKVEEI 735
Cdd:PRK07656 175 SGTTGRPKGAMLTHRQlLSNA-ADWAEYLGLTEGDRYLAANPFFHVFGYKAgVNAPLMRGATILPLPV---FDPDEVFRL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 736 VQGkaidwYKIT-----PS-HLKALSSESGTK--LFPRKGLILGGEASEWSWIKEIYRNIPAScKLFNHYGPSETTiGVA 807
Cdd:PRK07656 251 IET-----ERITvlpgpPTmYNSLLQHPDRSAedLSSLRLAVTGAASMPVALLERFESELGVD-IVLTGYGLSEAS-GVT 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 808 vyevTKKGLSNQFSTTP--IGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFItdsrm 885
Cdd:PRK07656 324 ----TFNRLDDDRKTVAgtIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGWL----- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 886 yKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVT-VTKVRNEEQLVAYYVSK--KEVLDKD 962
Cdd:PRK07656 395 -HTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIgVPDERLGEVGKAYVVLKpgAELTEEE 473
|
490 500 510
....*....|....*....|....*....|....*....
gi 497785100 963 LQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPE 1001
Cdd:PRK07656 474 LIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
524-999 |
1.00e-33 |
|
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: 136.82 E-value: 1.00e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 524 ALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSK 603
Cdd:cd05919 3 AFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 604 LKAIITHSEyktsyegyevpilyidqlddfllderednlnvdcdssQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQT 683
Cdd:cd05919 83 ARLVVTSAD-------------------------------------DIAYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 684 K-LGNKPKDRYlllqslaydFCLTTIYTSLLSGGTLFFLLKEDA---IDPAKVeeivqgkaidwykiTPSHLKALSSESG 759
Cdd:cd05919 126 EaLGLTPGDRV---------FSSAKMFFGYGLGNSLWFPLAVGAsavLNPGWP--------------TAERVLATLARFR 182
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 760 tklfPRkglILGGeasewswIKEIYRNIPASCKLFNH-------------------------YGPSETTIGVAVYEVTKK 814
Cdd:cd05919 183 ----PT---VLYG-------VPTFYANLLDSCAGSPDalrslrlcvsagealprglgerwmeHFGGPILDGIGATEVGHI 248
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 815 GLSNQFSTTPIGSS---LSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDpfitdsrMYKTGDI 891
Cdd:cd05919 249 FLSNRPGAWRLGSTgrpVPGYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG-------WYRTGDK 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 892 GKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIvtVTKVRNEEQLV---AYYVSK-----KEVLDKDL 963
Cdd:cd05919 322 FCRDADGWYTHAGRADDMLKVGGQWVSPVEVESLIIQHPAVAEAA--VVAVPESTGLSrltAFVVLKspaapQESLARDI 399
|
490 500 510
....*....|....*....|....*....|....*.
gi 497785100 964 QTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05919 400 HRHLLERLSAHKVPRRIAFVDELPRTATGKLQRFKL 435
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
50-471 |
2.29e-33 |
|
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: 134.62 E-value: 2.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 50 PLSSIQKQIWFMSQLNPELPIYNehlikIN----LSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVITKSEPTI 125
Cdd:cd19537 3 ALSPIEREWWHKYQLSTGTSSFN-----VSfacrLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPPRV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 126 QFLSLRGIsgeeqqeilseycRKEANYPYRLEQENLIRMSIielseSSYSVLFSRHHILSDGWSASILLSELERFYnmys 205
Cdd:cd19537 78 QRVDTLDV-------------WKEINRPFDLEREDPIRVFI-----SPDTLLVVMSHIICDLTTLQLLLREVSAAY---- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 206 qNGEINPEQSQEeltiqYHDYALWQEKLLTSEnlekgLEYWKEKLEG----DLPmLSIGGITQEGTgvgSEYnFKIPNIL 281
Cdd:cd19537 136 -NGKLLPPVRRE-----YLDSTAWSRPASPED-----LDFWSEYLSGlpllNLP-RRTSSKSYRGT---SRV-FQLPGSL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 282 TDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGRNIRETRNVIGPFINTVVIRTK--AEQNLSVIEYLQ 359
Cdd:cd19537 200 YRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRfpSSSDASAADFLR 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 360 QVHETTIQALENQdVPFEKVVEVLNPNRDVRANPfyqlLF-VM--------QEPPtqFSLPGIKVEYelIPTEVARFPLT 430
Cdd:cd19537 280 AVRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHP----LFdVMvtfhddrgVSLA--LPIPGVEPLY--TWAEGAKFPLM 350
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 497785100 431 L--SIIEGEEMIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQ 471
Cdd:cd19537 351 FefTALSDDSLLLRLEYDTDCFSEEEIDRIESLILAALELLVE 393
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
531-999 |
5.49e-33 |
|
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: 134.01 E-value: 5.49e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 531 SYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGgaylpldvespkerIEIITQDSKLkaiith 610
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLG--------------AEAVLLNTRL------ 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 611 seykTSYEgyevpilYIDQLDDfllderednLNVDCDSsqLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPK 690
Cdd:cd05912 61 ----TPNE-------LAFQLKD---------SDVKLDD--IATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTED 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 691 DRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLlkeDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSESGTKLFPR-KGLI 769
Cdd:cd05912 119 DNWLCALPLFHISGLSILMRSVIYGMTVYLV---DKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPNNlRCIL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 770 LGGEASEWSWIKE-IYRNIPasckLFNHYGPSETTIGVAVyevtkkgLSNQFSTTPIGSS---LSNNRIYILDDKLRPvp 845
Cdd:cd05912 196 LGGGPAPKPLLEQcKEKGIP----VYQSYGMTETCSQIVT-------LSPEDALNKIGSAgkpLFPVELKIEDDGQPP-- 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 846 sGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQ 925
Cdd:cd05912 263 -YEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEV 334
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 926 LLSHPSITEAIVTVTKVRNEEQL-VAYYVSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05912 335 LLSHPAIKEAGVVGIPDDKWGQVpVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1571-1959 |
6.58e-33 |
|
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: 136.60 E-value: 6.58e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1571 WVRSSPNHIALRFLD------RSYTYDEVNKRANKIANQLYKMGiRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDs 1644
Cdd:cd05931 2 RAAARPDRPAYTFLDdeggreETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLP- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1645 eLPLNRRDF-----ILKDASVGAIVTQTSLEE-------KLSKSDLPYLCTDQSQDSEDYSLLTKDKSYPEDIAYIIYTS 1712
Cdd:cd05931 80 -PPTPGRHAerlaaILADAGPRVVLTTAAALAavrafaaSRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1713 GTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVG-------QFATISFdaslwqILMALLAGATlCVvsreeQLSTKA 1785
Cdd:cd05931 159 GSTGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVswlplyhDMGLIGG------LLTPLYSGGP-SV-----LMSPAA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1786 LVKRFRDWNVTLADLPPVV-----------LDSILPEDIP-----SLQTVSTGGErcPIKVAkrwSLDR----------- 1838
Cdd:cd05931 227 FLRRPLRWLRLISRYRATIsaapnfaydlcVRRVRDEDLEgldlsSWRVALNGAE--PVRPA---TLRRfaeafapfgfr 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1839 --NFYNVYGPTETTIATTWYRVSSPECV-------------------QDSVPI---GTPVPNTEVFILDPD-LNPVPMGV 1893
Cdd:cd05931 302 peAFRPSYGLAEATLFVSGGPPGTGPVVlrvdrdalagravavaaddPAARELvscGRPLPDQEVRIVDPEtGRELPDGE 381
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 1894 IGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYKTGDIGkVLHDGNLEHLGRLDHQIKVRG 1959
Cdd:cd05931 382 VGEIWVRGPSVASGYWGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRG 446
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
520-999 |
8.15e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 134.91 E-value: 8.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGiGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESP----KERI 595
Cdd:PRK07638 15 PNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKqdelKERL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 596 EIitqdSKLKAIITHSEYKTSYEGYEVPILYIDQLDDFLLDEREDNLNVDcdSSQLA--YGIYTSGSTGIPKGVLVEHRN 673
Cdd:PRK07638 94 AI----SNADMIVTERYKLNDLPDEEGRVIEIDEWKRMIEKYLPTYAPIE--NVQNApfYMGFTSGSTGKPKAFLRAQQS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 674 LSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKedaIDPAKVEEIVQGKAIDWYKITPSHLKA 753
Cdd:PRK07638 168 WLHSFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHLMRK---FIPNQVLDKLETENISVMYTVPTMLES 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 754 LSSESGTKLFPRKgLILGGeaSEWSWI-KEIYRNIPASCKLFNHYGPSETTIgvavyeVTkkGLSNQFSTTP---IGSSL 829
Cdd:PRK07638 245 LYKENRVIENKMK-IISSG--AKWEAEaKEKIKNIFPYAKLYEFYGASELSF------VT--ALVDEESERRpnsVGRPF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 830 SNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNrEELTAERFMEDPFITdsrmykTGDIGKILYTGEIQFLGRLDGQ 909
Cdd:PRK07638 314 HNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYII-GGVLARELNADGWMT------VRDVGYEDEEGFIYIVGREKNM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 910 VKIRGIRVEPEEIQSQLLSHPSITEAIvtVTKVRNE---EQLVAYYvsKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTL 986
Cdd:PRK07638 387 ILFGGINIFPEEIESVLHEHPAVDEIV--VIGVPDSywgEKPVAII--KGSATKQQLKSFCLQRLSSFKIPKEWHFVDEI 462
|
490
....*....|...
gi 497785100 987 PRHAHGKIDRKAL 999
Cdd:PRK07638 463 PYTNSGKIARMEA 475
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
80-473 |
1.38e-32 |
|
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: 132.42 E-value: 1.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 80 LSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIE-QVITKSEPtiqflslrgISGEEQQEiLSEYCRKEANYPYRLEQ 158
Cdd:cd19545 30 LPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLlQVVVKESP---------ISWTESTS-LDEYLEEDRAAPMGLGG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 159 EnLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNmysqnGEINPEQSQEELTIQYhdyalwqeklLTSEN 238
Cdd:cd19545 100 P-LVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQ-----GEPVPQPPPFSRFVKY----------LRQLD 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 239 LEKGLEYWKEKLEG----DLPMLSIGGITQEGTGVgSEYNFKIPNILTdklrklaeeQKVSLYSVWLAIYKIVISKYTQE 314
Cdd:cd19545 164 DEAAAEFWRSYLAGldpaVFPPLPSSRYQPRPDAT-LEHSISLPSSAS---------SGVTLATVLRAAWALVLSRYTGS 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 315 TDLAVGTPIAGRN--IRETRNVIGPFINTVVIRTKAEQNLSVIEYLQQVHETTIQALENQDVPFEKVVEVlnpNRDVRAN 392
Cdd:cd19545 234 DDVVFGVTLSGRNapVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNIRRL---GPDARAA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 393 PFYQLLFVMQEPPTQFSLPGIKVEYELIPTEVARF---PLTLSI-IEGEEMIGRVLYRTSILSEYEVQSFVQRLLQVADE 468
Cdd:cd19545 311 CNFQTLLVVQPALPSSTSESLELGIEEESEDLEDFssyGLTLECqLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQ 390
|
....*
gi 497785100 469 IVQSP 473
Cdd:cd19545 391 LASAP 395
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
522-1001 |
1.46e-32 |
|
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: 134.36 E-value: 1.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 522 SIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQD 601
Cdd:cd05926 5 ALVVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLAD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 602 SKLKAIIT------------HSEYKTSYE-GYEVPILYI----DQLDDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIP 664
Cdd:cd05926 85 LGSKLVLTpkgelgpasraaSKLGLAILElALDVGVLIRapsaESLSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 665 KGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLaydF----CLTTIYTSLLSGGTLFFLLKEDAidpAKVEEIVQGKA 740
Cdd:cd05926 165 KGVPLTHRNLAASATNITNTYKLTPDDRTLVVMPL---FhvhgLVASLLSTLAAGGSVVLPPRFSA---STFWPDVRDYN 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 741 IDWYKITPSHLKALSSESGTKLFPRKGLILGGEASEWSWIKEIYRNIPAS--CKLFNHYGPSETTigvavYEVTkkglSN 818
Cdd:cd05926 239 ATWYTAVPTIHQILLNRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATfgAPVLEAYGMTEAA-----HQMT----SN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 819 QFSTTP--IGS--SLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKI 894
Cdd:cd05926 310 PLPPGPrkPGSvgKPVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYL 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 895 LYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIvtVTKVRNE---EQLVAYYV--SKKEVLDKDLQTYLKQ 969
Cdd:cd05926 384 DADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAV--AFGVPDEkygEEVAAAVVlrEGASVTEEELRAFCRK 461
|
490 500 510
....*....|....*....|....*....|..
gi 497785100 970 KLPPNLVPAYLVKMDTLPRHAHGKIDRKALPE 1001
Cdd:cd05926 462 HLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1586-1999 |
4.13e-32 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 133.95 E-value: 4.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1586 RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAA-------YVPIDselplnrrdfILKDA 1658
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttanpfYTPAE----------IAKQA 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1659 SV-GA--IVTQTSLEEKLSK----SDLPYLCTDQSQD----------SEDYSLLTKDKSyPEDIAYIIYTSGTTGTPNGV 1721
Cdd:PLN02246 119 KAsGAklIITQSCYVDKLKGlaedDGVTVVTIDDPPEgclhfseltqADENELPEVEIS-PDDVVALPYSSGTTGLPKGV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1722 MVKHSSVMNLISATID----EFNITQETKVGQFATISFDASLWQILMA-LLAGATLCVVSREEQLSTKALVKRFRdwnVT 1796
Cdd:PLN02246 198 MLTHKGLVTSVAQQVDgenpNLYFHSDDVILCVLPMFHIYSLNSVLLCgLRVGAAILIMPKFEIGALLELIQRHK---VT 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1797 LADL-PPVVL-----DSILPEDIPSLQTVSTGGerCPIKVAKRWSLDRNFYNV-----YGPTET--------TIATTWYR 1857
Cdd:PLN02246 275 IAPFvPPIVLaiaksPVVEKYDLSSIRMVLSGA--APLGKELEDAFRAKLPNAvlgqgYGMTEAgpvlamclAFAKEPFP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1858 VSSPECvqdsvpiGTPVPNTEVFILDPDLN-PVPMGVIGEIYIGGVGVSNGYLNrDDLNEKRFIphpfrEEEILYKTGDI 1936
Cdd:PLN02246 353 VKSGSC-------GTVVRNAELKIVDPETGaSLPRNQPGEICIRGPQIMKGYLN-DPEATANTI-----DKDGWLHTGDI 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497785100 1937 GKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV 1999
Cdd:PLN02246 420 GYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVV 482
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
529-1000 |
4.85e-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. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 131.26 E-value: 4.85e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 529 ERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAII 608
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 609 ThseyktsyegyevpilyidqlddfllderednlnvdcdssQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNK 688
Cdd:cd05934 81 V----------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFGLG 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 689 PKDRYLLLQSLAYDFCL-TTIYTSLLSGGTLFFLlkeDAIDPAKVEEIVQGKAIDWYKITPSHLKALSS--ESGTKLFPR 765
Cdd:cd05934 121 EDDVYLTVLPLFHINAQaVSVLAALSVGATLVLL---PRFSASRFWSDVRRYGATVTNYLGAMLSYLLAqpPSPDDRAHR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 766 KGLILGGEASEWSWiKEIYRNIpaSCKLFNHYGPSETTIGVAVYEVTKKGlsnqfsTTPIGSSLSNNRIYILDDKLRPVP 845
Cdd:cd05934 198 LRAAYGAPNPPELH-EEFEERF--GVRLLEGYGMTETIVGVIGPRDEPRR------PGSIGRPAPGYEVRIVDDDGQELP 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 846 SGIPGHIYIAGEQ---VARGYLNREELTAERFMEDpfitdsrMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEI 922
Cdd:cd05934 269 AGEPGELVIRGLRgwgFFKGYYNMPEATAEAMRNG-------WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEV 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 923 QSQLLSHPSITEAIVTVTK--VRNEEQLVAYYVSKKEVLD-KDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05934 342 ERAILRHPAVREAAVVAVPdeVGEDEVKAVVVLRPGETLDpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQL 421
|
.
gi 497785100 1000 P 1000
Cdd:cd05934 422 R 422
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1564-2045 |
5.77e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 132.68 E-value: 5.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1564 IQYSFENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQL-YKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPI 1642
Cdd:PRK06839 4 IAYWIEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1643 DSELPLNRRDFILKDASVGAIVTQ-----TSLEEKLSKSDLPYLCTDQSQDSEDYSLLTKDKSyPEDIAYII-YTSGTTG 1716
Cdd:PRK06839 84 NIRLTENELIFQLKDSGTTVLFVEktfqnMALSMQKVSYVQRVISITSLKEIEDRKIDNFVEK-NESASFIIcYTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1717 TPNGVMVKH-----SSVMNL--ISATIDEFNIT-----QETKVGQFAtisfdaslwqiLMALLAGATLCVVSREEQLSTK 1784
Cdd:PRK06839 163 KPKGAVLTQenmfwNALNNTfaIDLTMHDRSIVllplfHIGGIGLFA-----------FPTLFAGGVIIVPRKFEPTKAL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1785 ALVKRFRdwnVTLADLPPVVLDSILPE---DIPSLQTVS---TGGERCPIKVAKRWsLDRN--FYNVYGPTETtiATTWY 1856
Cdd:PRK06839 232 SMIEKHK---VTVVMGVPTIHQALINCskfETTNLQSVRwfyNGGAPCPEELMREF-IDRGflFGQGFGMTET--SPTVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1857 RVSSPECVQDSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfrEEEILYkTGDI 1936
Cdd:PRK06839 306 MLSEEDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETI------QDGWLC-TGDL 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1937 GKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPH--GEWEEKKIIEELR 2014
Cdd:PRK06839 379 ARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKssSVLIEKDVIEHCR 458
|
490 500 510
....*....|....*....|....*....|.
gi 497785100 2015 SKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK06839 459 LFLAKYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1703-2042 |
1.08e-31 |
|
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: 128.53 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1703 EDIAYIIYTSGTTGTPNGVMVKHSS-VMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGAtLCVVSREeQL 1781
Cdd:cd17635 1 EDPLAVIFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGG-LCVTGGE-NT 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1782 STKALVKRFRDWNVTLADLPPVVLDSILPE------DIPSLQTVSTGGERcPIKVAKR---WSLDRNFYNVYGPTETTIA 1852
Cdd:cd17635 79 TYKSLFKILTTNAVTTTCLVPTLLSKLVSElksanaTVPSLRLIGYGGSR-AIAADVRfieATGLTNTAQVYGLSETGTA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1853 TtwyrvsspeCVQ---DSVPI---GTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIphpfre 1926
Cdd:cd17635 158 L---------CLPtddDSIEInavGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI------ 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1927 eEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEW-- 2004
Cdd:cd17635 223 -DGWVNTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELde 301
|
330 340 350
....*....|....*....|....*....|....*....
gi 497785100 2005 -EEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDR 2042
Cdd:cd17635 302 nAIRALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
520-999 |
1.11e-31 |
|
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: 132.11 E-value: 1.11e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIITHSEY---------KTSYEGYEV-------PILYIDQLDDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGI 663
Cdd:cd05959 98 EDSRARVVVVSGELapvlaaaltKSEHTLVVLivsggagPEAGALLLAELVAAEAEQLKPAATHADDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 664 PKGVLVEHRNL--SNYIYAIQTkLGNKPKDRYLLLQSL--AYDFclttiytsllsGGTLFF--------LLKEDAIDPAK 731
Cdd:cd05959 178 PKGVVHLHADIywTAELYARNV-LGIREDDVCFSAAKLffAYGL-----------GNSLTFplsvgattVLMPERPTPAA 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 732 V-EEIVQGKAIDWYKItPSHLKAL--SSESGTKLFPRKGLIL-GGEAsewswikeiyrnIPASckLFN----HYGpSETT 803
Cdd:cd05959 246 VfKRIRRYRPTVFFGV-PTLYAAMlaAPNLPSRDLSSLRLCVsAGEA------------LPAE--VGErwkaRFG-LDIL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 804 IGVAVYEVTKKGLSNQFSTTPIGSS---LSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMedpfi 880
Cdd:cd05959 310 DGIGSTEMLHIFLSNRPGRVRYGTTgkpVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ----- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 881 tdSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAivTVTKVRNEEQL---VAYYVSKK- 956
Cdd:cd05959 385 --GEWTRTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEA--AVVGVEDEDGLtkpKAFVVLRPg 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 497785100 957 ----EVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05959 461 yedsEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1587-2042 |
1.65e-31 |
|
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: 131.28 E-value: 1.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1587 SYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQ 1666
Cdd:cd05926 14 ALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1667 TSLEEKLSKSDLPYLCT-----------DQSQDSEDYSLLTKDK--------SYPEDIAYIIYTSGTTGTPNGVMVKHSS 1727
Cdd:cd05926 94 KGELGPASRAASKLGLAilelaldvgvlIRAPSAESLSNLLADKknaksegvPLPDDLALILHTSGTTGRPKGVPLTHRN 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1728 VMNLISATIDEFNITQETKV----------GQFATI--------------SFDASL-WQ---------------ILMALL 1767
Cdd:cd05926 174 LAASATNITNTYKLTPDDRTlvvmplfhvhGLVASLlstlaaggsvvlppRFSASTfWPdvrdynatwytavptIHQILL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1768 agatlcvvSREEQLSTKALVK-RF-RDWNvtlADLPPVVLDSILPE-DIPSLQTvstggercpikvakrwsldrnfynvY 1844
Cdd:cd05926 254 --------NRPEPNPESPPPKlRFiRSCS---ASLPPAVLEALEATfGAPVLEA-------------------------Y 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1845 GPTETTiattwYRVSS---PECVQD--SVPIGTpvpNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRF 1919
Cdd:cd05926 298 GMTEAA-----HQMTSnplPPGPRKpgSVGKPV---GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1920 IPHPFreeeilYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV 1999
Cdd:cd05926 370 FKDGW------FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKYGEEVAAAVV 443
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 497785100 2000 PHGEWEEKKI--IEELRSKLPEHMVPSIFVQMEELPRLNNKKVDR 2042
Cdd:cd05926 444 LREGASVTEEelRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQR 488
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
1135-1532 |
6.30e-31 |
|
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: 127.41 E-value: 6.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1135 SLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNIDPVQVVLKDLKctiniLDFDENRSEQDimnYLTEKSMEPFKLe 1214
Cdd:cd19545 27 VFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKESP-----ISWTESTSLDE---YLEEDRAAPMGL- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1215 TGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQiisnmpIQLEQPVyQYADYVnwqqnRYTEEQINQ 1294
Cdd:cd19545 98 GGPLVRLALVEDPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQG------EPVPQPP-PFSRFV-----KYLRQLDDE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1295 QLQ-YWKEQLSGAPSLLELPLdkPRPSMQSYNGSLIRmklpekHAVLIKEiCEEAKVTPYTIFLTFFNILLYRYTYQDKI 1373
Cdd:cd19545 166 AAAeFWRSYLAGLDPAVFPPL--PSSRYQPRPDATLE------HSISLPS-SASSGVTLATVLRAAWALVLSRYTGSDDV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1374 LVGTPIANRN--IQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGALENQDISFERIvQELNPERSLsyNPIY 1451
Cdd:cd19545 237 VFGVTLSGRNapVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMIPFEHTGLQNI-RRLGPDARA--ACNF 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1452 QVAFTLQNDEQGKNGNYGGLSVEEFEIEWR-TSKVDLTLIIGQSKRGFEMVMEYNTDLFRQQSIEQMLSDYIKIISQVIE 1530
Cdd:cd19545 314 QTLLVVQPALPSSTSESLELGIEEESEDLEdFSSYGLTLECQLSGSGLRVRARYDSSVISEEQVERLLDQFEHVLQQLAS 393
|
..
gi 497785100 1531 NP 1532
Cdd:cd19545 394 AP 395
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1571-2045 |
8.96e-31 |
|
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: 128.98 E-value: 8.96e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1571 WVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAayVPIDSeLPLNR 1650
Cdd:cd05920 24 SAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPVLA-LPSHR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1651 RdfilkdASVGAIVTQTslEEKLsksdlpYLCTDQsQDSEDYSLLTKD--KSYPeDIAYIIYTSGTTGTPNGVMVKHSSV 1728
Cdd:cd05920 101 R------SELSAFCAHA--EAVA------YIVPDR-HAGFDHRALARElaESIP-EVALFLLSGGTTGTPKLIPRTHNDY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1729 MNLISATIDEFNITQETK--VGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRdwnVTLADL-PPVV- 1804
Cdd:cd05920 165 AYNVRASAEVCGLDQDTVylAVLPAAHNFPLACPGVLGTLLAGGRVVLAPDPSPDAAFPLIEREG---VTVTALvPALVs 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1805 --LDSIL--PEDIPSLQTVSTGGERCPIKVAKRW--SLDRNFYNVYGPTETTIATTwyRVSSPECV----QdsvpiGTPV 1874
Cdd:cd05920 242 lwLDAAAsrRADLSSLRLLQVGGARLSPALARRVppVLGCTLQQVFGMAEGLLNYT--RLDDPDEViihtQ-----GRPM 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1875 -PNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFreeeilYKTGDIGKVLHDGNLEHLGRLDH 1953
Cdd:cd05920 315 sPDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRIKD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1954 QIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGeweEKKIIEELRSKLPE-----HMVPSIFVQ 2028
Cdd:cd05920 389 QINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGERSCAFVVLRD---PPPSAAQLRRFLRErglaaYKLPDRIEF 465
|
490
....*....|....*..
gi 497785100 2029 MEELPRLNNKKVDRHSL 2045
Cdd:cd05920 466 VDSLPLTAVGKIDKKAL 482
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
519-1002 |
1.10e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 128.54 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEII 598
Cdd:PRK03640 15 TPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQ 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAIITHSEYKTS-YEGYEVpilYIDQLDDflLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNlsNY 677
Cdd:PRK03640 95 LDDAEVKCLITDDDFEAKlIPGISV---KFAELMN--GPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVIQTYGN--HW 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 678 IYAIQT--KLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFllkEDAIDPAKVEEIVQGKAIDWYKITPSHLKALS 755
Cdd:PRK03640 168 WSAVGSalNLGLTEDDCWLAAVPIFHISGLSILMRSVIYGMRVVL---VEKFDAEKINKLLQTGGVTIISVVSTMLQRLL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 756 SESGTKLFPR--KGLILGG---------EASEwswikeiyRNIPasckLFNHYGPSETTIGVavyeVTkkgLSNQFSTTP 824
Cdd:PRK03640 245 ERLGEGTYPSsfRCMLLGGgpapkplleQCKE--------KGIP----VYQSYGMTETASQI----VT---LSPEDALTK 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 825 IGSS---LSNNRIYILDDkLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmyKTGDIGkilYTGEIQ 901
Cdd:PRK03640 306 LGSAgkpLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIG---YLDEEG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 902 FL---GRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVT-VTKVRNEEQLVAYYVSKKEVLDKDLQTYLKQKLPPNLVP 977
Cdd:PRK03640 375 FLyvlDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVgVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVP 454
|
490 500
....*....|....*....|....*
gi 497785100 978 AYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:PRK03640 455 KRFYFVEELPRNASGKLLRHELKQL 479
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
519-999 |
4.51e-30 |
|
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: 126.67 E-value: 4.51e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGayLPLdVESPKERieii 598
Cdd:cd05920 28 HPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPV-LALPSHR---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 tqDSKLKAIITHSEyktsyegyevPILYI--DQLDDFllDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNlsn 676
Cdd:cd05920 101 --RSELSAFCAHAE----------AVAYIvpDRHAGF--DHRALARELAESIPEVALFLLSGGTTGTPKLIPRTHND--- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 677 YIYAIQTKL---GNKPKDRYLLLQSLAYDFCLTT--IYTSLLSGGTL-----------FFLLKED-----AIDPAKVEEI 735
Cdd:cd05920 164 YAYNVRASAevcGLDQDTVYLAVLPAAHNFPLACpgVLGTLLAGGRVvlapdpspdaaFPLIEREgvtvtALVPALVSLW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 736 VQgkAIDWYKITPSHLKALSSeSGTKLFPrkglilggeasewswikEIYRNIPA--SCKLFNHYGPSEttiGVAVYevTK 813
Cdd:cd05920 244 LD--AAASRRADLSSLRLLQV-GGARLSP-----------------ALARRVPPvlGCTLQQVFGMAE---GLLNY--TR 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 814 KGLSNQFSTTPIGSSLS-NNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIG 892
Cdd:cd05920 299 LDDPDEVIIHTQGRPMSpDDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLV 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 893 KILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKKEVLD-KDLQTYLKQ- 969
Cdd:cd05920 373 RRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDaAVVAMPDELLGERSCAFVVLRDPPPSaAQLRRFLREr 452
|
490 500 510
....*....|....*....|....*....|....*
gi 497785100 970 -----KLPPNLVPaylvkMDTLPRHAHGKIDRKAL 999
Cdd:cd05920 453 glaayKLPDRIEF-----VDSLPLTAVGKIDKKAL 482
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
1097-1517 |
9.85e-30 |
|
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: 123.83 E-value: 9.85e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1097 SNISEAEKEkgiplsdaqkrMWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNI----- 1171
Cdd:cd19537 2 TALSPIERE-----------WWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGlrrsy 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1172 --DPVQVVLKDlkcTINIldfdenRSEqdiMNYlteksmePFKLETGPLIRVHLVKSnpnehVLLIVQHHIISDGWSLRI 1249
Cdd:cd19537 71 ssSPPRVQRVD---TLDV------WKE---INR-------PFDLEREDPIRVFISPD-----TLLVVMSHIICDLTTLQL 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1250 MMDELFAIYHQiisnmpIQLEQPVYQYADYVNWQQnRYTEEqinqQLQYWKEQLSGAPsLLELPldkPRPSMQSYNGSLI 1329
Cdd:cd19537 127 LLREVSAAYNG------KLLPPVRREYLDSTAWSR-PASPE----DLDFWSEYLSGLP-LLNLP---RRTSSKSYRGTSR 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1330 RMKLPEKHAVLIKEICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNIQELEGILGLFVNTLV--IPSTVKGD 1407
Cdd:cd19537 192 VFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPirIRFPSSSD 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1408 RNFKSLLQQVNNQILGALENQdISFERIVQELNPERSLSYNPIYQVAFTLQNDEQGKNgnygGLSVE--EFEIEW-RTSK 1484
Cdd:cd19537 272 ASAADFLRAVRRSSQAALAHA-IPWHQLLEHLGLPPDSPNHPLFDVMVTFHDDRGVSL----ALPIPgvEPLYTWaEGAK 346
|
410 420 430
....*....|....*....|....*....|....*..
gi 497785100 1485 ----VDLTLIigqSKRGFEMVMEYNTDLFRQQSIEQM 1517
Cdd:cd19537 347 fplmFEFTAL---SDDSLLLRLEYDTDCFSEEEIDRI 380
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
531-999 |
1.05e-29 |
|
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: 124.51 E-value: 1.05e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 531 SYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITH 610
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 611 SEyktsyegyevpilyidqLDDfllderednlnvdcdssqLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPK 690
Cdd:cd05935 81 SE-----------------LDD------------------LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 691 DryLLLQSLAYdFCLTTIYTSLLS----GGTLFFLLKEDaiDPAKVEEIVQGKAIDWYKITPSHLKALSS-ESGTKLFPR 765
Cdd:cd05935 126 D--VILACLPL-FHVTGFVGSLNTavyvGGTYVLMARWD--RETALELIEKYKVTFWTNIPTMLVDLLATpEFKTRDLSS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 766 KGLILGGEASEWSWIKEIYRNIpASCKLFNHYGPSETtigvaVYEVTKKGLSNQFSTTpIGSSLSNNRIYILD-DKLRPV 844
Cdd:cd05935 201 LKVLTGGGAPMPPAVAEKLLKL-TGLRFVEGYGLTET-----MSQTHTNPPLRPKLQC-LGIP*FGVDARVIDiETGREL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 845 PSGIPGHIYIAGEQVARGYLNREELTAERFMEdpfITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQS 924
Cdd:cd05935 274 PPNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 925 QLLSHPSITEA-IVTVTKVRNEEQLVAYYVSKKE----VLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05935 351 KLYKHPAI*EVcVISVPDERVGEEVKAFIVLRPEyrgkVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
531-994 |
1.59e-29 |
|
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: 124.03 E-value: 1.59e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 531 SYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVespkerieiITQDSKLKAIITH 610
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILP---------FFREHELAFILRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 611 SEYKTsyegyevpilyidqlddFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPK 690
Cdd:cd05903 72 AKAKV-----------------FVVPERFRQFDPAAMPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 691 DRYLLLQSLAYdfclttiYTSLLSGGTLFFLLKEDAI-----DPAKVEEIVQGKAIDWYKITPSHLKALSS---ESGTKL 762
Cdd:cd05903 135 DVFLVASPMAH-------QTGFVYGFTLPLLLGAPVVlqdiwDPDKALALMREHGVTFMMGATPFLTDLLNaveEAGEPL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 763 FPRKGLILGGEAsewswikeIYRNIPASC------KLFNHYGPSETTIGVAvyeVTKKGLSNQFSTTPiGSSLSNNRIYI 836
Cdd:cd05903 208 SRLRTFVCGGAT--------VPRSLARRAaellgaKVCSAYGSTECPGAVT---SITPAPEDRRLYTD-GRPLPGVEIKV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 837 LDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDpfitdsrMYKTGDIGKILYTGEIqflgRLDGQVK---IR 913
Cdd:cd05903 276 VDDTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAPEG-------WFRTGDLARLDEDGYL----RITGRSKdiiIR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 914 -GIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKKEVLD--KDLQTYL-KQKLPPNLVPAYLVKMDTLPR 988
Cdd:cd05903 345 gGENIPVLEVEDLLLGHPGVIEaAVVALPDERLGERACAVVVTKSGALLtfDELVAYLdRQGVAKQYWPERLVHVDDLPR 424
|
....*.
gi 497785100 989 HAHGKI 994
Cdd:cd05903 425 TPSGKV 430
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1588-2045 |
1.76e-29 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 124.15 E-value: 1.76e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1588 YTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSEL-PLNRRDFILKDASVGAIVTQ 1666
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFgPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1667 tSLEEKLSksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETK 1746
Cdd:cd05969 81 -ELYERTD---------------------------PEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDDI 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1747 VGQFATISFDA-SLWQILMALLAGATlcVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSILPE--------DIPSLQ 1817
Cdd:cd05969 133 YWCTADPGWVTgTVYGIWAPWLNGVT--NVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEgdelarkyDLSSLR 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1818 TVSTGGErcPIKV-AKRWS---LDRNFYNVYGPTET-TIATTWYrvsspECvQDSVP--IGTPVPNTEVFILDPDLNPVP 1890
Cdd:cd05969 211 FIHSVGE--PLNPeAIRWGmevFGVPIHDTWWQTETgSIMIANY-----PC-MPIKPgsMGKPLPGVKAAVVDENGNELP 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1891 MGVIGEIYI--GGVGVSNGYLNRDDLNEKRFIphpfreeEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIE 1968
Cdd:cd05969 283 PGTKGILALkpGWPSMFRGIWNDEERYKNSFI-------DGWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1969 SLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV-----PHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRH 2043
Cdd:cd05969 356 SALMEHPAVAEAGVIGKPDPLRGEIIKAFISlkegfEPSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRR 435
|
..
gi 497785100 2044 SL 2045
Cdd:cd05969 436 VL 437
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
520-999 |
4.35e-29 |
|
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: 123.77 E-value: 4.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSY--TYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVE-SPKERIE 596
Cdd:cd05923 15 PDACAIADPARGLrlTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRlKAAELAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 597 IITQDSKLKAIITH-SEYKTSYEGYEVPILYIDQLDDFLLDEREDNLNVD--CDSSQLAYGIYTSGSTGIPKGVLVEHRN 673
Cdd:cd05923 95 LIERGEMTAAVIAVdAQVMDAIFQSGVRVLALSDLVGLGEPESAGPLIEDppREPEQPAFVFYTSGTTGLPKGAVIPQRA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 674 LSNYIYAIQTKLGNKPKD--RYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDaiDPAKVEEIVQGKAIDWYKITPSHL 751
Cdd:cd05923 175 AESRVLFMSTQAGLRHGRhnVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEF--DPADALKLIEQERVTSLFATPTHL 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 752 KAL---SSESGTKLFPRKGLILGGEASEWSWIKEIYRNIPAscKLFNHYGPSET---TIGVAVYEVT--KKGLSNQFSTT 823
Cdd:cd05923 253 DALaaaAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG--EKVNIYGTTEAmnsLYMRDARTGTemRPGFFSEVRIV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 824 PIGSSLSNnriyilddklrPVPSGIPGHIYIA--GEQVARGYLNREELTAERFMEdpfitdsRMYKTGDIGKILYTGEIQ 901
Cdd:cd05923 331 RIGGSPDE-----------ALANGEEGELIVAaaADAAFTGYLNQPEATAKKLQD-------GWYRTGDVGYVDPSGDVR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 902 FLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVT-VTKVRNEEQLVAYYVSKKEVLDKDL--QTYLKQKLPPNLVPA 978
Cdd:cd05923 393 ILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIgVADERWGQSVTACVVPREGTLSADEldQFCRASELADFKRPR 472
|
490 500
....*....|....*....|.
gi 497785100 979 YLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05923 473 RYFFLDELPKNAMNKVLRRQL 493
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1586-2045 |
1.44e-28 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 122.87 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1586 RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVT 1665
Cdd:PRK08008 36 RRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1666 QTS---LEEKLSKSD---LPYLCTDQSQDSE-----DYSLL------TKDKSYP---EDIAYIIYTSGTTGTPNGVMVKH 1725
Cdd:PRK08008 116 SAQfypMYRQIQQEDatpLRHICLTRVALPAddgvsSFTQLkaqqpaTLCYAPPlstDDTAEILFTSGTTSRPKGVVITH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1726 SsvmNLISATIDEFNITQETKVGQFATI--SF--DASLWQILMALLAGATLCVVsreEQLSTKALVKRFRDWNVTLADLP 1801
Cdd:PRK08008 196 Y---NLRFAGYYSAWQCALRDDDVYLTVmpAFhiDCQCTAAMAAFSAGATFVLL---EKYSARAFWGQVCKYRATITECI 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1802 PVVLDSILpedipsLQTVSTgGER--C--------PIKVAKRWSLDRNF----YNVYGPTETTIattWYRVSSPECVQDS 1867
Cdd:PRK08008 270 PMMIRTLM------VQPPSA-NDRqhClrevmfylNLSDQEKDAFEERFgvrlLTSYGMTETIV---GIIGDRPGDKRRW 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1868 VPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGV---GVSNGYLNRDDLNEKRFiphpfrEEEILYKTGDIGKVLHDGN 1944
Cdd:PRK08008 340 PSIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVL------EADGWLHTGDTGYVDEEGF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1945 LEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPhgEWEEKKIIEELRSKLPEHM--- 2021
Cdd:PRK08008 414 FYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAFVVL--NEGETLSEEEFFAFCEQNMakf 491
|
490 500
....*....|....*....|....*
gi 497785100 2022 -VPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK08008 492 kVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1669-2041 |
1.65e-28 |
|
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: 122.05 E-value: 1.65e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1669 LEEKLSKSD--LPYLCTDQSQDSEDYSLLTKDKSyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETK 1746
Cdd:cd05909 112 LRAKISKADkcKAFLAGKFPPKWLLRIFGVAPVQ-PDDPAVILFTSGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1747 VGQ----FATISFDASLWqilMALLAGATlcVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSIL----PEDIPSLQT 1818
Cdd:cd05909 191 VFGalpfFHSFGLTGCLW---LPLLSGIK--VVFHPNPLDYKKIPELIYDKKATILLGTPTFLRGYAraahPEDFSSLRL 265
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1819 VSTGGERCPIKVAKRWsLDR---NFYNVYGPTETTIATTWYRVSSP---ECVqdsvpiGTPVPNTEVFILDPD-LNPVPM 1891
Cdd:cd05909 266 VVAGAEKLKDTLRQEF-QEKfgiRILEGYGTTECSPVISVNTPQSPnkeGTV------GRPLPGMEVKIVSVEtHEEVPI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1892 GVIGEIYIGGVGVSNGYLNRDDlnekrfiPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLL 1971
Cdd:cd05909 339 GEGGLLLVRGPNVMLGYLNEPE-------LTSFAFGDGWYDTGDIGKIDGEGFLTITGRLSRFAKIAGEMVSLEAIEDIL 411
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497785100 1972 N----LQTGVKEAIVQplgDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVD 2041
Cdd:cd05909 412 SeilpEDNEVAVVSVP---DGRKGEKIVLLTTTTDTDPSSLNDILKNAGISNLAKPSYIHQVEEIPLLGTGKPD 482
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1586-2041 |
1.99e-28 |
|
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: 122.35 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1586 RSYTYDEVNKRANKIANQLYKMGIRRGDRVALY---HERSSEMIFGFLGIlkcGAAYVPIDSELPLNRRDFILKDASVGA 1662
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLawnTHRHLELYYAVPGM---GAVLHTINPRLFPEQIAYIINHAEDRV 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1663 IVTQTSLEEKL--SKSDLPYLCTDQSQDSEDYSLLTKDK---SYPE-----------------DIAYIIYTSGTTGTPNG 1720
Cdd:cd12119 101 VFVDRDFLPLLeaIAPRLPTVEHVVVMTDDAAMPEPAGVgvlAYEEllaaespeydwpdfdenTAAAICYTSGTTGNPKG 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1721 VMVKHSSVM--NLISATIDEFNITQETKVGQFATIsFDASLWQI-LMALLAGATLCVVSReeQLSTKALVKRFRDWNVTL 1797
Cdd:cd12119 181 VVYSHRSLVlhAMAALLTDGLGLSESDVVLPVVPM-FHVNAWGLpYAAAMVGAKLVLPGP--YLDPASLAELIEREGVTF 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1798 ADLPPVVLDSILPE------DIPSLQTVSTGGERCPIKVAKRWS-LDRNFYNVYGPTET----TIAT-TWYRVSSPECVQ 1865
Cdd:cd12119 258 AAGVPTVWQGLLDHleangrDLSSLRRVVIGGSAVPRSLIEAFEeRGVRVIHAWGMTETsplgTVARpPSEHSNLSEDEQ 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1866 DSVPI--GTPVPNTEVFILDPDLNPVPM--GVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfreEEILYKTGDIGKVLH 1941
Cdd:cd12119 338 LALRAkqGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESEALT-------EDGWLRTGDVATIDE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1942 DGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEE--LRSKLPE 2019
Cdd:cd12119 411 DGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERPLAVVVLKEGATVTAEELLefLADKVAK 490
|
490 500
....*....|....*....|..
gi 497785100 2020 HMVPSIFVQMEELPRLNNKKVD 2041
Cdd:cd12119 491 WWLPDDVVFVDEIPKTSTGKID 512
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
650-999 |
2.38e-28 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 118.20 E-value: 2.38e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 650 QLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAidp 729
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQA--- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 730 akVEEIVQGKAIDWYKITPSHL-KALSSESGTKLFPRKGLILGGEASEWSWIKE--IYRNIPasckLFNHYGPSETTIGV 806
Cdd:cd17630 78 --LAEDLAPPGVTHVSLVPTQLqRLLDSGQGPAALKSLRAVLLGGAPIPPELLEraADRGIP----LYTTYGMTETASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 807 AVyevtkkGLSNQFSTTPIGSSLSNNRIYILDDklrpvpsgipGHIYIAGEQVARGYLNREEltaerfmEDPFiTDSRMY 886
Cdd:cd17630 152 AT------KRPDGFGRGGVGVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQL-------VPEF-NEDGWF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 887 KTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVT-VTKVRNEEQLVAYYVSKKEVLDKDLQT 965
Cdd:cd17630 208 TTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVgVPDEELGQRPVAVIVGRGPADPAELRA 287
|
330 340 350
....*....|....*....|....*....|....
gi 497785100 966 YLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd17630 288 WLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1571-2042 |
3.10e-28 |
|
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This family of MACS enzymes is found in archaea and bacteria. It is represented by the acyl-adenylating enzyme from Methanosarcina acetivorans (AAE_MA). AAE_MA is most active with propionate, butyrate, and the branched analogs: 2-methyl-propionate, butyrate, and pentanoate. The specific activity is weaker for smaller or larger acids.
Pssm-ID: 341274 [Multi-domain] Cd Length: 537 Bit Score: 121.83 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1571 WVRSSPNHIALRFLD-----RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSE 1645
Cdd:cd05970 26 MAKEYPDKLALVWCDdageeRIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1646 LPLNRRDFILKDASVGAIVT----------QTSLEEKLSKSDLPYLCTDQSQDSEDYSLLTKDKS----------YP--E 1703
Cdd:cd05970 106 LTAKDIVYRIESADIKMIVAiaednipeeiEKAAPECPSKPKLVWVGDPVPEGWIDFRKLIKNASpdferptansYPcgE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1704 DIAYIIYTSGTTGTPNgvMVKHSSVMNLISATIDEF--NITQETKVGQFATISFDASLW-QILMALLAGATLCVVSReEQ 1780
Cdd:cd05970 186 DILLVYFSSGTTGMPK--MVEHDFTYPLGHIVTAKYwqNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFVYDY-DK 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1781 LSTKALVKRFRDWNVTLADLPPVVLDSILPEDI-----PSLQTVSTGGERCPIKVAKRW--SLDRNFYNVYGPTETTIAT 1853
Cdd:cd05970 263 FDPKALLEKLSKYGVTTFCAPPTIYRFLIREDLsrydlSSLRYCTTAGEALNPEVFNTFkeKTGIKLMEGFGQTETTLTI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1854 TWYRVSSPEcvqdsvP--IGTPVPNTEVFILDPDLNPVPMGVIGEIYIG-----GVGVSNGYLnRDdlnekrfiphPFRE 1926
Cdd:cd05970 343 ATFPWMEPK------PgsMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgkPVGLFGGYY-KD----------AEKT 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1927 EEI----LYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVphg 2002
Cdd:cd05970 406 AEVwhdgYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIV--- 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 497785100 2003 EWEEKKIIEELRSKLPEHM--------VPSIFVQMEELPRLNNKKVDR 2042
Cdd:cd05970 483 LAKGYEPSEELKKELQDHVkkvtapykYPRIVEFVDELPKTISGKIRR 530
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1571-2040 |
4.48e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 120.76 E-value: 4.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1571 WVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNR 1650
Cdd:PRK06145 11 HARRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1651 RDFILKDA------------SVGAIVTQTSLEEKLSKSDLPYLCTDQSQDSEDYSlltkdkSYPEDIAYIIYTSGTTGTP 1718
Cdd:PRK06145 91 VAYILGDAgaklllvdeefdAIVALETPKIVIDAAAQADSRRLAQGGLEIPPQAA------VAPTDLVRLMYTSGTTDRP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1719 NGVMVKHSsvmNLISATIDE---FNITQETK---VGQFATI-SFD----ASLWQilmallaGATLCVVSREEQLSTKALV 1787
Cdd:PRK06145 165 KGVMHSYG---NLHWKSIDHviaLGLTASERllvVGPLYHVgAFDlpgiAVLWV-------GGTLRIHREFDPEAVLAAI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1788 KRFRdwnVTLADLPPVVLDSIL--PE----DIPSLQTVSTGGERCP---IKVAKRWSLDRNFYNVYGPTETTIATTWYRV 1858
Cdd:PRK06145 235 ERHR---LTCAWMAPVMLSRVLtvPDrdrfDLDSLAWCIGGGEKTPesrIRDFTRVFTRARYIDAYGLTETCSGDTLMEA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1859 SSPecVQDSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFReeeilykTGDIGK 1938
Cdd:PRK06145 312 GRE--IEKIGSTGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWFR-------SGDVGY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1939 VLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV--PHGEWEEKKIIEELRSK 2016
Cdd:PRK06145 383 LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVVVlnPGATLTLEALDRHCRQR 462
|
490 500
....*....|....*....|....
gi 497785100 2017 LPEHMVPSIFVQMEELPRLNNKKV 2040
Cdd:PRK06145 463 LASFKVPRQLKVRDELPRNPSGKV 486
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1572-2034 |
4.86e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 121.19 E-value: 4.86e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1572 VRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRR 1651
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1652 DFILKDASVGAIVTQTSLEEKLSK-------SDLPYLCTDQSQDSE------DYSLLTKDKSYP------EDIAYIIYTS 1712
Cdd:PRK08316 101 AYILDHSGARAFLVDPALAPTAEAalallpvDTLILSLVLGGREAPggwldfADWAEAGSVAEPdveladDDLAQILYTS 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1713 GTTGTPNGVMVKHSSVM-NLISATIDeFNITQETKVGQFATISFDASLWQILM-ALLAGATLCVVSREEQLSTKALVKRF 1790
Cdd:PRK08316 181 GTESLPKGAMLTHRALIaEYVSCIVA-GDMSADDIPLHALPLYHCAQLDVFLGpYLYVGATNVILDAPDPELILRTIEAE 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1791 RdwnVTLADLPPVVLDSIL------PEDIPSLQTVSTGGERCPIKVAKRWsLDR----NFYNVYGPTETT-IATtwyrVS 1859
Cdd:PRK08316 260 R---ITSFFAPPTVWISLLrhpdfdTRDLSSLRKGYYGASIMPVEVLKEL-RERlpglRFYNCYGQTEIApLAT----VL 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1860 SPEcVQDSVP--IGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFReeeilykTGDIG 1937
Cdd:PRK08316 332 GPE-EHLRRPgsAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWFH-------SGDLG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1938 KVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKII--EELRS 2015
Cdd:PRK08316 404 VMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPKAGATVTEDEliAHCRA 483
|
490
....*....|....*....
gi 497785100 2016 KLPEHMVPSIFVQMEELPR 2034
Cdd:PRK08316 484 RLAGFKVPKRVIFVDELPR 502
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1576-2045 |
7.81e-28 |
|
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: 120.31 E-value: 7.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSY--TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSEL-PLNRRD 1652
Cdd:cd05923 15 PDACAIADPARGLrlTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLkAAELAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1653 FILKDASVGAIVT---------QTSLEEKLSKSDLPylctdQSQDSEDYSLLTKDKSY-PEDIAYIIYTSGTTGTPNGVM 1722
Cdd:cd05923 95 LIERGEMTAAVIAvdaqvmdaiFQSGVRVLALSDLV-----GLGEPESAGPLIEDPPRePEQPAFVFYTSGTTGLPKGAV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1723 VKHSsvmnlisaTIDEFNITQETKVGQ--------------FATISFDASLwqiLMALLAGATLCVVSREEQLSTKALVK 1788
Cdd:cd05923 170 IPQR--------AAESRVLFMSTQAGLrhgrhnvvlglmplYHVIGFFAVL---VAALALDGTYVVVEEFDPADALKLIE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1789 RFRdwnVTLADLPPVVLDSIL------PEDIPSLQTVSTGGERCPIKVAKRWS--LDRNFYNVYGPTETtIATTWYRVSS 1860
Cdd:cd05923 239 QER---VTSLFATPTHLDALAaaaefaGLKLSSLRHVTFAGATMPDAVLERVNqhLPGEKVNIYGTTEA-MNSLYMRDAR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1861 PECVqdsvpiGTPVPNTEV---FILDPDLNPVPMGVIGEIYIGGVGVS--NGYLNRDDLNEKRFiphpfreEEILYKTGD 1935
Cdd:cd05923 315 TGTE------MRPGFFSEVrivRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKL-------QDGWYRTGD 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1936 IGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEE--L 2013
Cdd:cd05923 382 VGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQSVTACVVPREGTLSADELDQfcR 461
|
490 500 510
....*....|....*....|....*....|..
gi 497785100 2014 RSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05923 462 ASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
1109-1421 |
7.90e-28 |
|
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: 118.95 E-value: 7.90e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1109 PLSDAQKRMWF--LYRMESDsAYYNMPIsLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNIDPVQVVLKDLKCTIN 1186
Cdd:cd19547 3 PLAPMQEGMLFrgLFWPDSD-AYFNQNV-LELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDDLAPPWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1187 ILDF---DENRSEQDIMNYLTEKSMEPFKLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIIS 1263
Cdd:cd19547 81 LLDWsgeDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1264 NMPIQLEqPVYQYADYVNWQQNRytEEQINQQLQYWKEQLSgapSLLELPLDKPrPSMQSYNGSLIRMKLPEKHAVLIKE 1343
Cdd:cd19547 161 GREPQLS-PCRPYRDYVRWIRAR--TAQSEESERFWREYLR---DLTPSPFSTA-PADREGEFDTVVHEFPEQLTRLVNE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1344 ICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRNiQELEG---ILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQ 1420
Cdd:cd19547 234 AARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRP-PELEGsehMVGIFINTIPLRIRLDPDQTVTGLLETIHRD 312
|
.
gi 497785100 1421 I 1421
Cdd:cd19547 313 L 313
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1568-2042 |
8.59e-28 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 120.88 E-value: 8.59e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYV---PI-- 1642
Cdd:PRK05605 38 YDNAVARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVehnPLyt 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1643 DSELplnRRDFILKDASVgAIV------------TQTSLEEKLS---------------KSDLPYLCTDQSQ------DS 1689
Cdd:PRK05605 118 AHEL---EHPFEDHGARV-AIVwdkvaptverlrRTTPLETIVSvnmiaampllqrlalRLPIPALRKARAAltgpapGT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1690 EDYSLLTKD------------KSYPEDIAYIIYTSGTTGTPNGVMVKHSSVM-NLIS--ATIDEFNITQETKVGqfATIS 1754
Cdd:PRK05605 194 VPWETLVDAaiggdgsdvshpRPTPDDVALILYTSGTTGKPKGAQLTHRNLFaNAAQgkAWVPGLGDGPERVLA--ALPM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1755 FDASLWQILMAL--LAGATLCVVSREE-QLSTKALVKRFRDWnvtladLP--PVVLDSILPE------DIPSLQTVSTGG 1823
Cdd:PRK05605 272 FHAYGLTLCLTLavSIGGELVLLPAPDiDLILDAMKKHPPTW------LPgvPPLYEKIAEAaeergvDLSGVRNAFSGA 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1824 ERCPIKVAKRWSLDRNFYNV--YGPTETtiattwyrvsSPECVQDSVP-------IGTPVPNTEVFILDPDlNP---VPM 1891
Cdd:PRK05605 346 MALPVSTVELWEKLTGGLLVegYGLTET----------SPIIVGNPMSddrrpgyVGVPFPDTEVRIVDPE-DPdetMPD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1892 GVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFReeeilykTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLL 1971
Cdd:PRK05605 415 GEEGELLVRGPQVFKGYWNRPEETAKSFLDGWFR-------TGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVL 487
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497785100 1972 NLQTGVKEAIVQPLGDNQNYHTLVAYVV--PHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDR 2042
Cdd:PRK05605 488 REHPGVEDAAVVGLPREDGSEEVVAAVVlePGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
530-999 |
1.18e-27 |
|
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: 119.65 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 530 RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYL---PLDVESpkeriEIITQ--DSKL 604
Cdd:cd05904 31 RALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTtanPLSTPA-----EIAKQvkDSGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 605 KAIITHSEYKTSYEGYEVPILYIDQLDDFLLDEREDNLNVDCDS--------SQLAYGIYTSGSTGIPKGVLVEHRNL-- 674
Cdd:cd05904 106 KLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEppvvvikqDDVAALLYSSGTTGRSKGVMLTHRNLia 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 675 -SNYIYAIQTKLGNKPkDRYLLLQSLAYDFCLTTIYTSLLS-GGTLFFLLKEDAidpakvEEIVqgKAIDWYKIT----- 747
Cdd:cd05904 186 mVAQFVAGEGSNSDSE-DVFLCVLPMFHIYGLSSFALGLLRlGATVVVMPRFDL------EELL--AAIERYKVThlpvv 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 748 PSHLKALSSESGTKLFPRKGLI--------LGGEASEwswikEIYRNIPaSCKLFNHYGPSETTiGVAVYEVTKKGLSNQ 819
Cdd:cd05904 257 PPIVLALVKSPIVDKYDLSSLRqimsgaapLGKELIE-----AFRAKFP-NVDLGQGYGMTEST-GVVAMCFAPEKDRAK 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 820 FSTtpIGSSLSNNRIYILD-DKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFItdsrmyKTGDIGKILYTG 898
Cdd:cd05904 330 YGS--VGRLVPNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGWL------HTGDLCYIDEDG 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 899 EIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAivTVTKVRNEE--QL-VAYYV-------SKKEVLD---KDLQT 965
Cdd:cd05904 402 YLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDA--AVIPYPDEEagEVpMAFVVrkpgsslTEDEIMDfvaKQVAP 479
|
490 500 510
....*....|....*....|....*....|....*...
gi 497785100 966 YLKqklppnlvpaylVK----MDTLPRHAHGKIDRKAL 999
Cdd:cd05904 480 YKK------------VRkvafVDAIPKSPSGKILRKEL 505
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
653-996 |
3.91e-27 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 114.42 E-value: 3.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 653 YGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTlFFLLKEdaIDPAKV 732
Cdd:cd17633 4 YIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGT-FIGQRK--FNPKSW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 733 EEIVQGKAIDWYKITPSHLKALSSEsGTKLFPRKGLILGGEASEWSWIKEIYRNIPAScKLFNHYGPSETTIgvavyeVT 812
Cdd:cd17633 81 IRKINQYNATVIYLVPTMLQALART-LEPESKIKSIFSSGQKLFESTKKKLKNIFPKA-NLIEFYGTSELSF------IT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 813 KkgLSNQFSTTP--IGSSLSNNRIYILDDKlrpvpSGIPGHIYIAGEQVARGYLNREELTAERFMEdpfitdsrmykTGD 890
Cdd:cd17633 153 Y--NFNQESRPPnsVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGWMS-----------VGD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 891 IGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYVSKKEVLDKDLQTYLKQK 970
Cdd:cd17633 215 IGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTYKQLKRFLKQK 294
|
330 340
....*....|....*....|....*.
gi 497785100 971 LPPNLVPAYLVKMDTLPRHAHGKIDR 996
Cdd:cd17633 295 LSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
532-999 |
4.32e-27 |
|
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: 116.85 E-value: 4.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 532 YTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITHS 611
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 612 EYKtsyegyevpilyiDQLDDFLLDErednlnvdcdssqlaygIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKD 691
Cdd:cd05973 81 ANR-------------HKLDSDPFVM-----------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 692 RYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLkEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSeSGTKLFPRKGLILG 771
Cdd:cd05973 131 SFWNAADPGWAYGLYYAITGPLALGHPTILL-EGGFSVESTWRVIERLGVTNLAGSPTAYRLLMA-AGAEVPARPKGRLR 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 772 GEASEWSWIK-EIYRNIPASCKL--FNHYGPSETTIGVAvyevTKKGLSNQFSTTPIGSSLSNNRIYILDDKLRPVPSGI 848
Cdd:cd05973 209 RVSSAGEPLTpEVIRWFDAALGVpiHDHYGQTELGMVLA----NHHALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGE 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 849 PGHIYIAGEQVA----RGYLNREELTAerfmedpfitDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQS 924
Cdd:cd05973 285 PGRLAIDIANSPlmwfRGYQLPDTPAI----------DGGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVES 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 925 QLLSHPSITE-AIVTVTKVRNEEQLVAYYV-----SKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKA 998
Cdd:cd05973 355 ALIEHPAVAEaAVIGVPDPERTEVVKAFVVlrgghEGTPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFL 434
|
.
gi 497785100 999 L 999
Cdd:cd05973 435 L 435
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
518-998 |
2.30e-26 |
|
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: 116.18 E-value: 2.30e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 518 NTPNSIAL------SDHERSYTYLQTNNRANQIARWLQKQGiGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESP 591
Cdd:cd05931 5 ARPDRPAYtflddeGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPPTP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 592 ---KERIEIITQDSKLKAIITHSEYKTSYEGYEV--------PILYIDQLDDfllDEREDNLNVDCDSSQLAYGIYTSGS 660
Cdd:cd05931 84 grhAERLAAILADAGPRVVLTTAAALAAVRAFAAsrpaagtpRLLVVDLLPD---TSAADWPPPSPDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 661 TGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCL-TTIYTSLLSGGTLFFLLKEDAI-DPAK-VEEIVQ 737
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLiGGLLTPLYSGGPSVLMSPAAFLrRPLRwLRLISR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 738 GK---------AIDW--YKITPSHLKA--LSSesgtklfpRKGLILGGEASEWSWIKEIYR-----NIPASCkLFNHYGP 799
Cdd:cd05931 241 YRatisaapnfAYDLcvRRVRDEDLEGldLSS--------WRVALNGAEPVRPATLRRFAEafapfGFRPEA-FRPSYGL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 800 SETTIGVA---------VYEVTKKGLSNQFSTTPI-----------GSSLSNNRIYILD-DKLRPVPSGIPGHIYIAGEQ 858
Cdd:cd05931 312 AEATLFVSggppgtgpvVLRVDRDALAGRAVAVAAddpaarelvscGRPLPDQEVRIVDpETGRELPDGEVGEIWVRGPS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 859 VARGYLNREELTAERFMEDPFITDSRMYKTGDIGkILYTGEIQFLGRLDGQVKIRGIRVEPEEI-QSQLLSHPSITEAIV 937
Cdd:cd05931 392 VASGYWGRPEATAETFGALAATDEGGWLRTGDLG-FLHDGELYITGRLKDLIIVRGRNHYPQDIeATAEEAHPALRPGCV 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497785100 938 TVTKV--RNEEQLVAYYVSKKEVLDKDLQTYLKQ---------KLPPNLVpaYLVKMDTLPRHAHGKIDRKA 998
Cdd:cd05931 471 AAFSVpdDGEERLVVVAEVERGADPADLAAIAAAiraavarehGVAPADV--VLVRPGSIPRTSSGKIQRRA 540
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1575-2045 |
2.38e-26 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 115.65 E-value: 2.38e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1575 SPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGiRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFI 1654
Cdd:PRK07638 14 QPNKIAIKENDRVLTYKDWFESVCKVANWLNEKE-SKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1655 LKDASVGAIVTQTSLEEKLSKSDLPYLCTDQSQdsEDYSLLTKDKSYPEDIA----YIIYTSGTTGTPNGVMVKHSSVMN 1730
Cdd:PRK07638 93 LAISNADMIVTERYKLNDLPDEEGRVIEIDEWK--RMIEKYLPTYAPIENVQnapfYMGFTSGSTGKPKAFLRAQQSWLH 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1731 LISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVvsrEEQLSTKALVKRFRDWNVTLADLPPVVLDSILP 1810
Cdd:PRK07638 171 SFDCNVHDFHMKREDSVLIAGTLVHSLFLYGAISTLYVGQTVHL---MRKFIPNQVLDKLETENISVMYTVPTMLESLYK 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1811 ED--IPSLQTVSTGGERCPI----KVAKRWSLDRnFYNVYGPTETTIATTwyrVSSPECVQDSVPIGTPVPNTEVFILDP 1884
Cdd:PRK07638 248 ENrvIENKMKIISSGAKWEAeakeKIKNIFPYAK-LYEFYGASELSFVTA---LVDEESERRPNSVGRPFHNVQVRICNE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1885 DLNPVPMGVIGEIYIGGVGVSNGYlnrddLNEKRFIPHPFREEEIlyKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIEL 1964
Cdd:PRK07638 324 AGEEVQKGEIGTVYVKSPQFFMGY-----IIGGVLARELNADGWM--TVRDVGYEDEEGFIYIVGREKNMILFGGINIFP 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1965 GEIESLLNLQTGVKEAIVqpLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHS 2044
Cdd:PRK07638 397 EEIESVLHEHPAVDEIVV--IGVPDSYWGEKPVAIIKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARME 474
|
.
gi 497785100 2045 L 2045
Cdd:PRK07638 475 A 475
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
528-999 |
3.17e-26 |
|
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: 115.12 E-value: 3.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 528 HERSYTYLQTNNRANQIARWLQKQGIGkEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAI 607
Cdd:cd05909 4 LGTSLTYRKLLTGAIALARKLAKMTKE-GENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 608 ITHSEY-------KTSYEGYEVPILYIDQLDD---------------FLLDEREDNLNVDC-DSSQLAYGIYTSGSTGIP 664
Cdd:cd05909 83 LTSKQFieklklhHLFDVEYDARIVYLEDLRAkiskadkckaflagkFPPKWLLRIFGVAPvQPDDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 665 KGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLT-TIYTSLLSGGTLFFllKEDAIDPAKVEEIVQGKAIDW 743
Cdd:cd05909 163 KGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFFHSFGLTgCLWLPLLSGIKVVF--HPNPLDYKKIPELIYDKKATI 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 744 YKITPSHLKA-LSSESGTKLFPRKGLILGGEA---SEWSWIKEIYrNIPasckLFNHYGPSETTigvAVYEVTKKGLSNQ 819
Cdd:cd05909 241 LLGTPTFLRGyARAAHPEDFSSLRLVVAGAEKlkdTLRQEFQEKF-GIR----ILEGYGTTECS---PVISVNTPQSPNK 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 820 FSTtpIGSSLSNNRIYILD-DKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDpfitdsrMYKTGDIGKILYTG 898
Cdd:cd05909 313 EGT--VGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAFGDG-------WYDTGDIGKIDGEG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 899 EIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKV--RNEEQLVAYYVSkkEVLDKD-LQTYLKQKLPPNL 975
Cdd:cd05909 384 FLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVAVVSVPdgRKGEKIVLLTTT--TDTDPSsLNDILKNAGISNL 461
|
490 500
....*....|....*....|....*
gi 497785100 976 -VPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05909 462 aKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1577-1982 |
6.00e-26 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 115.38 E-value: 6.00e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1577 NHIALRFLD----RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDS---ELPLN 1649
Cdd:PRK04319 59 DKVALRYLDasrkEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEafmEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1650 RRdfiLKDASVGAIVTQTSLEEKLSKSDLPYLCT----DQSQDSE----DYSLLTKDKSY--------PEDIAYIIYTSG 1713
Cdd:PRK04319 139 DR---LEDSEAKVLITTPALLERKPADDLPSLKHvllvGEDVEEGpgtlDFNALMEQASDefdiewtdREDGAILHYTSG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1714 TTGTPNGVMVKHSSV-MNLISA--------------TIDEFNITQeTKVGQFAtisfdaslwqilmALLAGATLCVvsRE 1778
Cdd:PRK04319 216 STGKPKGVLHVHNAMlQHYQTGkyvldlheddvywcTADPGWVTG-TSYGIFA-------------PWLNGATNVI--DG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1779 EQLSTKALVKRFRDWNVTLADLPPVVL--------DSILPEDIPSLQTVSTGGErcPIKV-AKRWS---LDRNFYNVYGP 1846
Cdd:PRK04319 280 GRFSPERWYRILEDYKVTVWYTAPTAIrmlmgagdDLVKKYDLSSLRHILSVGE--PLNPeVVRWGmkvFGLPIHDNWWM 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1847 TET---TIATTwyrvssPecvqdSVPI-----GTPVPNTEVFILDPDLNPVPMGVIGEIYI--GGVGVSNGYLNRDDLNE 1916
Cdd:PRK04319 358 TETggiMIANY------P-----AMDIkpgsmGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYE 426
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 1917 KRFIPHpfreeeiLYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIV 1982
Cdd:PRK04319 427 SYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV 485
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
532-1004 |
6.29e-26 |
|
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: 113.37 E-value: 6.29e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 532 YTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITHS 611
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 612 EyktsyegyevpilyidqlddfLLDEREDNlnvdcdssQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKD 691
Cdd:cd05969 81 E---------------------LYERTDPE--------DPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 692 RYLL------LQSLAYdfcltTIYTSLLSGGTLffLLKEDAIDPAKVEEIVQGKAID-WYKiTPSHLKALSSE------- 757
Cdd:cd05969 132 IYWCtadpgwVTGTVY-----GIWAPWLNGVTN--VVYEGRFDAESWYGIIERVKVTvWYT-APTAIRMLMKEgdelark 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 758 ---SGTKLFPRKGLILGGEASEWSwiKEIYrNIPasckLFNHYGPSET-TIGVAVYevtkkgLSNQFSTTPIGSSLSNNR 833
Cdd:cd05969 204 ydlSSLRFIHSVGEPLNPEAIRWG--MEVF-GVP----IHDTWWQTETgSIMIANY------PCMPIKPGSMGKPLPGVK 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 834 IYILDDKLRPVPSGIPGHIYIAGE--QVARGYLNREEltaeRFmEDPFITDsrMYKTGDIGKILYTGEIQFLGRLDGQVK 911
Cdd:cd05969 271 AAVVDENGNELPPGTKGILALKPGwpSMFRGIWNDEE----RY-KNSFIDG--WYLTGDLAYRDEDGYFWFVGRADDIIK 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 912 IRGIRVEPEEIQSQLLSHPSITEA-IVTVTKVRNEEQLVAYYVSKK-----EVLDKDLQTYLKQKLPPNLVPAYLVKMDT 985
Cdd:cd05969 344 TSGHRVGPFEVESALMEHPAVAEAgVIGKPDPLRGEIIKAFISLKEgfepsDELKEEIINFVRQKLGAHVAPREIEFVDN 423
|
490
....*....|....*....
gi 497785100 986 LPRHAHGKIDRKALPEIQV 1004
Cdd:cd05969 424 LPKTRSGKIMRRVLKAKEL 442
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
512-937 |
6.61e-26 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 115.58 E-value: 6.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHE----RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLD 587
Cdd:COG1022 17 LRRRAARFPDRVALREKEdgiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIY 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 588 VESPKERIEIITQDS------------------------KLKAIITHSEYKtsyEGYEVPILYIDQL--------DDFLL 635
Cdd:COG1022 97 PTSSAEEVAYILNDSgakvlfvedqeqldkllevrdelpSLRHIVVLDPRG---LRDDPRLLSLDELlalgrevaDPAEL 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 636 DEREDNLNVDcdssQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLA--YDFCLTtiYTSLL 713
Cdd:COG1022 174 EARRAAVKPD----DLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLSFLPLAhvFERTVS--YYALA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 714 SGGTLFFL---------LKE-----------------DAIDpAKVEE--IVQGKAIDW-----YKItpSHLKALSSESGT 760
Cdd:COG1022 248 AGATVAFAespdtlaedLREvkptfmlavprvwekvyAGIQ-AKAEEagGLKRKLFRWalavgRRY--ARARLAGKSPSL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 761 KLFPRKGL-----------ILGGEA----------SEwsWIKEIYRN--IPasckLFNHYGPSETTIGVAVyevtkkgls 817
Cdd:COG1022 325 LLRLKHALadklvfsklreALGGRLrfavsggaalGP--ELARFFRAlgIP----VLEGYGLTETSPVITV--------- 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 818 NQFSTTPIGSS---LSNNRIYILDDklrpvpsgipGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKI 894
Cdd:COG1022 390 NRPGDNRIGTVgppLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGEL 453
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 497785100 895 LYTGEIQFLGR------LDGqvkirGIRVEPEEIQSQLLSHPSITEAIV 937
Cdd:COG1022 454 DEDGFLRITGRkkdlivTSG-----GKNVAPQPIENALKASPLIEQAVV 497
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
530-994 |
7.39e-26 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 115.37 E-value: 7.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 530 RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPL-DVESPKE---RIEiitqDSKLK 605
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIfGGFAPEAvagRII----DSSSR 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 606 AIITHSEYktsYE-GYEVPILYI--DQL------------------------------DDFLLDEREDNLNVDCDSSQLA 652
Cdd:cd17634 159 LLITADGG---VRaGRSVPLKKNvdDALnpnvtsvehvivlkrtgsdidwqegrdlwwRDLIAKASPEHQPEAMNAEDPL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 653 YGIYTSGSTGIPKGVLveHRNLSNYIYAIQTK---LGNKPKDRYLLLQSLAYDFCLT-TIYTSLLSGGTLF-FLLKEDAI 727
Cdd:cd17634 236 FILYTSGTTGKPKGVL--HTTGGYLVYAATTMkyvFDYGPGDIYWCTADVGWVTGHSyLLYGPLACGATTLlYEGVPNWP 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 728 DPAKVEEIVQGKAIDWYKITPSHLKALSSEsGTKLFPRKGL----ILGG-------EASEWSWiKEIYRnipASCKLFNH 796
Cdd:cd17634 314 TPARMWQVVDKHGVNILYTAPTAIRALMAA-GDDAIEGTDRsslrILGSvgepinpEAYEWYW-KKIGK---EKCPVVDT 388
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 797 YGPSETTIGVAVYEVTKKGLSNQFSTTPIgsslSNNRIYILDDKLRPVPSGIPGHIYIAGE--QVARGYLNREEltaeRF 874
Cdd:cd17634 389 WWQTETGGFMITPLPGAIELKAGSATRPV----FGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RF 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 875 MEDPFITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYV 953
Cdd:cd17634 461 EQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEaAVVGIPHAIKGQAPYAYVV 540
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 497785100 954 SKKEVLDKD-----LQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKI 994
Cdd:cd17634 541 LNHGVEPSPelyaeLRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1573-2046 |
1.06e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 114.25 E-value: 1.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1573 RSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRrd 1652
Cdd:PRK07788 60 RRAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQ-- 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1653 fiLKDAS----VGAIVTQTSLEEKLSK--SDLPYLCT-------DQSQDSEDYSL----LTKDKSYPEDIA----YIIYT 1711
Cdd:PRK07788 138 --LAEVAaregVKALVYDDEFTDLLSAlpPDLGRLRAwggnpddDEPSGSTDETLddliAGSSTAPLPKPPkpggIVILT 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1712 SGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATIsFDA---SLWQILMALlaGATLcVVSR----EEQLstk 1784
Cdd:PRK07788 216 SGTTGTPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPM-FHAtgwAHLTLAMAL--GSTV-VLRRrfdpEATL--- 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1785 ALVKRFRdwnVTLADLPPVVLDSIL---PE-----DIPSLQTVSTGGERCPIKVAKRwSLDRnF----YNVYGPTETTIA 1852
Cdd:PRK07788 289 EDIAKHK---ATALVVVPVMLSRILdlgPEvlakyDTSSLKIIFVSGSALSPELATR-ALEA-FgpvlYNLYGSTEVAFA 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1853 TtwyrVSSPECVQ-DSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRddlnekrfiPHPFREEEILy 1931
Cdd:PRK07788 364 T----IATPEDLAeAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDG---------RDKQIIDGLL- 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1932 KTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPH--GEWEEKKI 2009
Cdd:PRK07788 430 SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKApgAALDEDAI 509
|
490 500 510
....*....|....*....|....*....|....*....
gi 497785100 2010 IEELRSKLPEHMVPS--IFVqmEELPRLNNKKVDRHSLP 2046
Cdd:PRK07788 510 KDYVRDNLARYKVPRdvVFL--DELPRNPTGKVLKRELR 546
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1704-2042 |
1.99e-25 |
|
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: 109.42 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1704 DIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSreeQLST 1783
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQR---KFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1784 KALVKRFRDWNVTLADLPPVVLDSILPEDIP--SLQTVSTGGERCP---IKVAKRWSLDRNFYNVYGPTETTIATtwYRv 1858
Cdd:cd17633 78 KSWIRKINQYNATVIYLVPTMLQALARTLEPesKIKSIFSSGQKLFestKKKLKNIFPKANLIEFYGTSELSFIT--YN- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1859 sspeCVQDSVP---IGTPVPNTEVFILDPDlnpvpMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfreeeilYKTGD 1935
Cdd:cd17633 155 ----FNQESRPpnsVGRPFPNVEIEIRNAD-----GGEIGKIFVKSEMVFSGYVRGGFSNPDGW-----------MSVGD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1936 IGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGeWEEKKIIEELRS 2015
Cdd:cd17633 215 IGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDK-LTYKQLKRFLKQ 293
|
330 340
....*....|....*....|....*..
gi 497785100 2016 KLPEHMVPSIFVQMEELPRLNNKKVDR 2042
Cdd:cd17633 294 KLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
520-999 |
2.09e-25 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 113.30 E-value: 2.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSD-HERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEII 598
Cdd:PRK06087 37 PDKIAVVDnHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWREAELVWV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAIITHSEYK-TSYEGYEVPIlyIDQLDDF----LLD---------------EREDNLNVDC--DSSQLAYGIY 656
Cdd:PRK06087 117 LNKCQAKMFFAPTLFKqTRPVDLILPL--QNQLPQLqqivGVDklapatsslslsqiiADYEPLTTAIttHGDELAAVLF 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 657 TSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDfclttiyTSLLSGGTLFFLLK-----EDAIDPAK 731
Cdd:PRK06087 195 TSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHA-------TGFLHGVTAPFLIGarsvlLDIFTPDA 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 732 VEEIVQGKAIDW-YKITP---SHLKALsSESGTKLFPRKGLILGGEASEWSWIKEIYRnipASCKLFNHYGPSETTIGVA 807
Cdd:PRK06087 268 CLALLEQQRCTCmLGATPfiyDLLNLL-EKQPADLSALRFFLCGGTTIPKKVARECQQ---RGIKLLSVYGSTESSPHAV 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 808 VYevTKKGLSNQFSTTpiGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmYK 887
Cdd:PRK06087 344 VN--LDDPLSRFMHTD--GYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGW------YY 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 888 TGDIGKILYTGEIQFLGRlDGQVKIR-GIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKKEVLD---KD 962
Cdd:PRK06087 414 SGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDaCVVAMPDERLGERSCAYVVLKAPHHSltlEE 492
|
490 500 510
....*....|....*....|....*....|....*...
gi 497785100 963 LQTYL-KQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK06087 493 VVAFFsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1572-2000 |
2.60e-25 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 113.22 E-value: 2.60e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1572 VRSSPNHIAL------RFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIdse 1645
Cdd:PRK13295 34 VASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPL--- 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1646 LPLNRR---DFILKDA-SVGAIVTQT-------SLEEKLsKSDLPYL-------------------CTDQSQDSEDYSLL 1695
Cdd:PRK13295 111 MPIFRErelSFMLKHAeSKVLVVPKTfrgfdhaAMARRL-RPELPALrhvvvvggdgadsfealliTPAWEQEPDAPAIL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1696 TKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQEtkvgqfaTISFDAS--------LWQILMALL 1767
Cdd:PRK13295 190 ARLRPGPDDVTQLIYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGAD-------DVILMASpmahqtgfMYGLMMPVM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1768 AGATlcVVSREEQLSTKALvKRFRDWNVT--------LADLPPVVLDSilPEDIPSLQTVSTGGERCPIKVAKRWS--LD 1837
Cdd:PRK13295 263 LGAT--AVLQDIWDPARAA-ELIRTEGVTftmastpfLTDLTRAVKES--GRPVSSLRTFLCAGAPIPGALVERARaaLG 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1838 RNFYNVYGPTETTIATTWYRVSSPECVqdSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEK 1917
Cdd:PRK13295 338 AKIVSAWGMTENGAVTLTKLDDPDERA--STTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGT 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1918 RFiphpfreeEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAY 1997
Cdd:PRK13295 416 DA--------DGWFDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGERACAF 487
|
...
gi 497785100 1998 VVP 2000
Cdd:PRK13295 488 VVP 490
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1569-2042 |
2.73e-25 |
|
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: 113.74 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1569 ENWVRSSPNHIALRFLD-----RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPID 1643
Cdd:cd05968 68 DKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIF 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1644 SEL---PLNRRdfiLKDASVGAIVTQ---------TSLEEKLSKS-------------------DLPYLCTDQSQDSEDY 1692
Cdd:cd05968 148 SGFgkeAAATR---LQDAEAKALITAdgftrrgreVNLKEEADKAcaqcptvekvvvvrhlgndFTPAKGRDLSYDEEKE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1693 SLLTK-DKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMnlISATID---EFNITQETKVGQFATISFDASLWQILMALLA 1768
Cdd:cd05968 225 TAGDGaERTESEDPLMIIYTSGTTGKPKGTVHVHAGFP--LKAAQDmyfQFDLKPGDLLTWFTDLGWMMGPWLIFGGLIL 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1769 GATLCVVS------REEQLSTkaLVKRFRdwnVTLADLPPVVLDSILP--------EDIPSLQTV-STG----------- 1822
Cdd:cd05968 303 GATMVLYDgapdhpKADRLWR--MVEDHE---ITHLGLSPTLIRALKPrgdapvnaHDLSSLRVLgSTGepwnpepwnwl 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1823 -----GERCPIkvakrwsldrnfYNVYGPTETTIATTWYRVSSPecvqdSVPIG--TPVPNTEVFILDPDLNPVPmGVIG 1895
Cdd:cd05968 378 fetvgKGRNPI------------INYSGGTEISGGILGNVLIKP-----IKPSSfnGPVPGMKADVLDESGKPAR-PEVG 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1896 EIYIGG--VGVSNGYLnRDDlneKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNL 1973
Cdd:cd05968 440 ELVLLApwPGMTRGFW-RDE---DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNA 515
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497785100 1974 QTGVKEAIVQPLGDNQNYHTLVAYVV-PHGEWEEKKIIEELRSKLPEHM----VPSIFVQMEELPRLNNKKVDR 2042
Cdd:cd05968 516 HPAVLESAAIGVPHPVKGEAIVCFVVlKPGVTPTEALAEELMERVADELgkplSPERILFVKDLPKTRNAKVMR 589
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1702-2041 |
2.83e-25 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 115.02 E-value: 2.83e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1702 PEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQ----FATISFDASLWqilMALLAGATlcVVSR 1777
Cdd:PRK08633 781 PDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpfFHSFGLTVTLW---LPLLEGIK--VVYH 855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1778 EEQLSTKALVKRFRDWNVTLADLPPVVL------DSILPEDIPSLQTVSTGGERCPIKVA----KRWSLDrnFYNVYGPT 1847
Cdd:PRK08633 856 PDPTDALGIAKLVAKHRATILLGTPTFLrlylrnKKLHPLMFASLRLVVAGAEKLKPEVAdafeEKFGIR--ILEGYGAT 933
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1848 ETT-IATtwyrVSSP--ECVQDSVPIGT-------PVPNTEVFILDPD-LNPVPMGVIGEIYIGGVGVSNGYLNRD---- 1912
Cdd:PRK08633 934 ETSpVAS----VNLPdvLAADFKRQTGSkegsvgmPLPGVAVRIVDPEtFEELPPGEDGLILIGGPQVMKGYLGDPekta 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1913 ----DLNEKRFiphpfreeeilYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLN--LQTGVKEAIVQPLG 1986
Cdd:PRK08633 1010 evikDIDGIGW-----------YVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAkaLGGEEVVFAVTAVP 1078
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 1987 DNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVD 2041
Cdd:PRK08633 1079 DEKKGEKLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1585-2045 |
2.87e-25 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 112.48 E-value: 2.87e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1585 DRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIV 1664
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 TQTSLEEKLsKSDLPYLCTDQSQDS-----EDYSLLTKDKSYPE-DIAY--------------------IIYTSGTTGTP 1718
Cdd:PRK12406 89 AHADLLHGL-ASALPAGVTVLSVPTppeiaAAYRISPALLTPPAgAIDWegwlaqqepydgppvpqpqsMIYTSGTTGHP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1719 NGV-----MVKHSSVMNLISATIdeFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDW 1793
Cdd:PRK12406 168 KGVrraapTPEQAAAAEQMRALI--YGLKPGIRALLTGPLYHSAPNAYGLRAGRLGGVLVLQPRFDPEELLQLIERHRIT 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1794 N--------VTLADLPPVVLDSIlpeDIPSLQTVSTGGERCPIKVaKRWSLD---RNFYNVYGPTETTIATTwyrVSSPE 1862
Cdd:PRK12406 246 HmhmvptmfIRLLKLPEEVRAKY---DVSSLRHVIHAAAPCPADV-KRAMIEwwgPVIYEYYGSTESGAVTF---ATSED 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1863 CVQDSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSN-GYLNRDDlnEKRFIphpfrEEEILYKTGDIGKVLH 1941
Cdd:PRK12406 319 ALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPE--KRAEI-----DRGGFITSGDVGYLDA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1942 DGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPH--GEWEEKKIIEELRSKLPE 2019
Cdd:PRK12406 392 DGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQpgATLDEADIRAQLKARLAG 471
|
490 500
....*....|....*....|....*.
gi 497785100 2020 HMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK12406 472 YKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1588-2045 |
3.29e-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: 111.07 E-value: 3.29e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1588 YTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSelplnrrdfilkdasvgAIVTQt 1667
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFT-----------------AFGPK- 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1668 SLEEKLSKSDLPYLCTDQSQdsedyslltKDKsYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKV 1747
Cdd:cd05973 63 AIEHRLRTSGARLVVTDAAN---------RHK-LDSDPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPEDSF 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1748 GQFATISFDASLWQILMALLAGATLCVVSrEEQLSTKALVKRFRDWNVTLADLPPVVLDSILPEDIP-------SLQTVS 1820
Cdd:cd05973 133 WNAADPGWAYGLYYAITGPLALGHPTILL-EGGFSVESTWRVIERLGVTNLAGSPTAYRLLMAAGAEvparpkgRLRRVS 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1821 TGGERCPIKVAkRWSLDR---NFYNVYGPTE--TTIATTWyrvsSPECVQDSVPIGTPVPNTEVFILDPDLNPVPMGVIG 1895
Cdd:cd05973 212 SAGEPLTPEVI-RWFDAAlgvPIHDHYGQTElgMVLANHH----ALEHPVHAGSAGRAMPGWRVAVLDDDGDELGPGEPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1896 EIYIGgVGVS-----NGYLNRDDlneKRFIPHpfreeeiLYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESL 1970
Cdd:cd05973 287 RLAID-IANSplmwfRGYQLPDT---PAIDGG-------YYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPFDVESA 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1971 LNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHG-----EWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05973 356 LIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGghegtPALADELQLHVKKRLSAHAYPRTIHFVDELPKTPSGKIQRFLL 435
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1580-2045 |
3.67e-25 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 111.03 E-value: 3.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1580 ALRFLDRSYTYDEVNKRANKIANQL-YKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIdseLPLNRR---DFIL 1655
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLvGELGIVPGNRVLLRGSNSPELVACWFGIQKAGAIAVAT---MPLLRPkelAYIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVgaivTQTSLEEKLSKSDlpylctdqsqdsedyslltkdksypeDIAYIIYTSGTTGTPNGVMVKHSSVMnlisAT 1735
Cdd:cd05958 80 DKARI----TVALCAHALTASD--------------------------DICILAFTSGTTGAPKATMHFHRDPL----AS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1736 IDEF--NITQETK----VGQ---FATISFDASLwqiLMALLAGATLCVVSREEQLSTKALVKRFRdwnVTLADLPPVVLD 1806
Cdd:cd05958 126 ADRYavNVLRLREddrfVGSpplAFTFGLGGVL---LFPFGVGASGVLLEEATPDLLLSAIARYK---PTVLFTAPTAYR 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1807 SILP------EDIPSLQTVSTGGERCPIKVAKRWsldrnfYNVYG-PTETTI-ATTWYRVSSPECVQDSVP--IGTPVPN 1876
Cdd:cd05958 200 AMLAhpdaagPDLSSLRKCVSAGEALPAALHRAW------KEATGiPIIDGIgSTEMFHIFISARPGDARPgaTGKPVPG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1877 TEVFILDPDLNPVPMGVIGEIYIGGvgvSNGYLNRDDLNEKRFIphpfrEEEILYkTGDIGKVLHDGNLEHLGRLDHQIK 1956
Cdd:cd05958 274 YEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYV-----QGGWNI-TGDTYSRDPDGYFRHQGRSDDMIV 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1957 VRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPH-GEWEEKKIIEELRSKLPEHMV----PSIFVQMEE 2031
Cdd:cd05958 345 SGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpGVIPGPVLARELQDHAKAHIApykyPRAIEFVTE 424
|
490
....*....|....
gi 497785100 2032 LPRLNNKKVDRHSL 2045
Cdd:cd05958 425 LPRTATGKLQRFAL 438
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1704-2042 |
5.40e-25 |
|
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: 108.19 E-value: 5.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1704 DIAYIIYTSGTTGTPNGVMVkhsSVMNLISATidefnitqetkVGQFATISFDAS--------------LWQILMALLAG 1769
Cdd:cd17630 1 RLATVILTSGSTGTPKAVVH---TAANLLASA-----------AGLHSRLGFGGGdswllslplyhvggLAILVRSLLAG 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1770 ATLCVVSREEqlstkALVKRFRDWNVTLADLPPVVLDSIL-----PEDIPSLQTVSTGGERCPIKVAKRWSLDR-NFYNV 1843
Cdd:cd17630 67 AELVLLERNQ-----ALAEDLAPPGVTHVSLVPTQLQRLLdsgqgPAALKSLRAVLLGGAPIPPELLERAADRGiPLYTT 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1844 YGPTET--TIATTwyrvSSPECVQDSVpiGTPVPNTEVFILDPdlnpvpmgviGEIYIGGVGVSNGYLNRDdlnekrfIP 1921
Cdd:cd17630 142 YGMTETasQVATK----RPDGFGRGGV--GVLLPGRELRIVED----------GEIWVGGASLAMGYLRGQ-------LV 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1922 HPFREEEIlYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPH 2001
Cdd:cd17630 199 PEFNEDGW-FTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQRPVAVIVGR 277
|
330 340 350 360
....*....|....*....|....*....|....*....|.
gi 497785100 2002 GEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDR 2042
Cdd:cd17630 278 GPADPAELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDR 318
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
532-977 |
6.67e-25 |
|
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: 110.91 E-value: 6.67e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 532 YTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKErieiitqdsKLKAIITHS 611
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVE---------ELLYILNHS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 612 EYKTsyegyevpilyidqlddfllderednLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKD 691
Cdd:cd17640 77 ESVA--------------------------LVVENDSDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 692 RYLLLQSLAYDFCLTTIYTSLLSGGTLFF----LLKED--AIDP---AKVEEIvqgkaidWYKITPSHLKALSSESGTKL 762
Cdd:cd17640 131 RFLSILPIWHSYERSAEYFIFACGCSQAYtsirTLKDDlkRVKPhyiVSVPRL-------WESLYSGIQKQVSKSSPIKQ 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 763 FPRKGLILGGE--------ASEWSWIKEIYRNIpaSCKLFNHYGPSETTIGVAVyevtkkglsNQFSTTPIGSS---LSN 831
Cdd:cd17640 204 FLFLFFLSGGIfkfgisggGALPPHVDTFFEAI--GIEVLNGYGLTETSPVVSA---------RRLKCNVRGSVgrpLPG 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 832 NRIYILDDKLR-PVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKILYTGEIQFLGRL-DGQ 909
Cdd:cd17640 273 TEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW------FNTGDLGWLTCGGELVLTGRAkDTI 346
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 910 VKIRGIRVEPEEIQSQLLSHPSITEAIVTvtkVRNEEQLVAYYVSKKEVLDKDLQTYlKQKLPPNLVP 977
Cdd:cd17640 347 VLSNGENVEPQPIEEALMRSPFIEQIMVV---GQDQKRLGALIVPNFEELEKWAKES-GVKLANDRSQ 410
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1576-2000 |
6.86e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 111.62 E-value: 6.86e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDselPLNRRD--- 1652
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALH---PLGSLDdha 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1653 FILKDASV--------------GAIVTQ-TSLEEKLSKSDLPYLcTDQSQDSEDYSLLT-KDKSYPEDIAYIIYTSGTTG 1716
Cdd:PRK06188 103 YVLEDAGIstlivdpapfveraLALLARvPSLKHVLTLGPVPDG-VDLLAAAAKFGPAPlVAAALPPDIAGLAYTGGTTG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1717 TPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWqILMALLAGATLCVVSREEQLSTKALVKRFRdwnVT 1796
Cdd:PRK06188 182 KPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHAGGAF-FLPTLLRGGTVIVLAKFDPAEVLRAIEEQR---IT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1797 LADLPPVVLDSIL--PE----DIPSLQTVSTGGErcPIKVAK-RWSLDRN---FYNVYGPTETTIATTWYR-----VSSP 1861
Cdd:PRK06188 258 ATFLVPTMIYALLdhPDlrtrDLSSLETVYYGAS--PMSPVRlAEAIERFgpiFAQYYGQTEAPMVITYLRkrdhdPDDP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1862 E----CvqdsvpiGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIP---HpfreeeilykTG 1934
Cdd:PRK06188 336 KrltsC-------GRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDgwlH----------TG 398
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 1935 DIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVP 2000
Cdd:PRK06188 399 DVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEAVTAVVVL 464
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1704-2040 |
1.36e-24 |
|
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: 107.20 E-value: 1.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1704 DIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKV----GQFATISFDASlwqILMALLAGATlcvVSREE 1779
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYliinPFFHTFGYKAG---IVACLLTGAT---VVPVA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1780 QLSTKALVKRFRDWNVTLADLPPVVLDSILPE------DIPSLQTVSTGGERCPIKVAKRWSLDRNFYNV---YGPTETT 1850
Cdd:cd17638 75 VFDVDAILEAIERERITVLPGPPTLFQSLLDHpgrkkfDLSSLRAAVTGAATVPVELVRRMRSELGFETVltaYGLTEAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1851 IATTWYRVSSPECVQDSVpiGTPVPNTEVFILDPdlnpvpmgviGEIYIGGVGVSNGYLNRDDLNEKRFiphpfrEEEIL 1930
Cdd:cd17638 155 VATMCRPGDDAETVATTC--GRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAI------DADGW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1931 YKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV--PHGEWEEKK 2008
Cdd:cd17638 217 LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVarPGVTLTEED 296
|
330 340 350
....*....|....*....|....*....|..
gi 497785100 2009 IIEELRSKLPEHMVPSIFVQMEELPRLNNKKV 2040
Cdd:cd17638 297 VIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1568-2045 |
1.39e-24 |
|
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: 110.62 E-value: 1.39e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1568 FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAayVPIDSeLP 1647
Cdd:COG1021 31 LRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPVFA-LP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 LNRRdfilkdASVGAIVTQT-----------------SLEEKLsKSDLPYL----CTDQSQDSEDY-SLLTKDKSY---- 1701
Cdd:COG1021 108 AHRR------AEISHFAEQSeavayiipdrhrgfdyrALAREL-QAEVPSLrhvlVVGDAGEFTSLdALLAAPADLsepr 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1702 --PEDIAYIIYTSGTTGTPngvmvKhssvmnLISATIDEF-----------NITQETKVgqFATI----SFDASLWQILM 1764
Cdd:COG1021 181 pdPDDVAFFQLSGGTTGLP-----K------LIPRTHDDYlysvrasaeicGLDADTVY--LAALpaahNFPLSSPGVLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1765 ALLAGATLCVVSREEQLSTKALVKRFRdwnVTLADL-PPVVLD-----SILPEDIPSLQTVSTGGERCPIKVAKRW--SL 1836
Cdd:COG1021 248 VLYAGGTVVLAPDPSPDTAFPLIERER---VTVTALvPPLALLwldaaERSRYDLSSLRVLQVGGAKLSPELARRVrpAL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1837 DRNFYNVYGPTETTIATTwyRVSSPECVQDSVpIGTPV-PNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLN 1915
Cdd:COG1021 325 GCTLQQVFGMAEGLVNYT--RLDDPEEVILTT-QGRPIsPDDEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHN 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1916 EKRFIPHPFreeeilYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDnqnyHTL- 1994
Cdd:COG1021 402 ARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAMPD----EYLg 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 1995 ---VAYVVPHGEWEEKKIIEE-LRSK-LPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:COG1021 472 ersCAFVVPRGEPLTLAELRRfLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
524-999 |
1.96e-24 |
|
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: 109.10 E-value: 1.96e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 524 ALSDHERSYTYLQTNNRANQIARWLQ-KQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGG---AYLPLdvESPKERIEIIT 599
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLVgELGIVPGNRVLLRGSNSPELVACWFGIQKAGAiavATMPL--LRPKELAYILD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 qdsklKAIITHSeyktsyegyevpilyidqlddfLLDEREDNLNvdcDSSQLAYgiyTSGSTGIPKGVLVEHRNL--SNY 677
Cdd:cd05958 81 -----KARITVA----------------------LCAHALTASD---DICILAF---TSGTTGAPKATMHFHRDPlaSAD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 678 IYAIQTkLGNKPKDRYLLLQSLAYDFCLttiytsllsGGTLFFLLKEDA---IDPAKVEEIVQGkAIDWYKIT-----PS 749
Cdd:cd05958 128 RYAVNV-LRLREDDRFVGSPPLAFTFGL---------GGVLLFPFGVGAsgvLLEEATPDLLLS-AIARYKPTvlftaPT 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 750 HLKA---LSSESGTKLFPRKGLILGGEAsewswikeiyrnIPASC--KLFNHYGpSETTIGVAVYEVTKKGLSNQFSTTP 824
Cdd:cd05958 197 AYRAmlaHPDAAGPDLSSLRKCVSAGEA------------LPAALhrAWKEATG-IPIIDGIGSTEMFHIFISARPGDAR 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 825 IGSS---LSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGylNREELTAERFMEDPFITDSRMYKTGDigkilytGEIQ 901
Cdd:cd05958 264 PGATgkpVPGYEAKVVDDEGNPVPDGTIGRLAVRGPTGCRY--LADKRQRTYVQGGWNITGDTYSRDPD-------GYFR 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 902 FLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYVSKK------EVLDKDLQTYLKQKLPPNL 975
Cdd:cd05958 335 HQGRSDDMIVSGGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVLRpgvipgPVLARELQDHAKAHIAPYK 414
|
490 500
....*....|....*....|....
gi 497785100 976 VPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05958 415 YPRAIEFVTELPRTATGKLQRFAL 438
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1572-2045 |
2.36e-24 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 110.22 E-value: 2.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1572 VRSSPNHIALR-FLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPI-----DSE 1645
Cdd:PRK06087 33 ARAMPDKIAVVdNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLlpswrEAE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1646 LP--LNR---RDFIlkdasVGAIVTQTSLEEKLS--KSDLPYL----CTDQ----------SQDSEDYSLLTKDKS-YPE 1703
Cdd:PRK06087 113 LVwvLNKcqaKMFF-----APTLFKQTRPVDLILplQNQLPQLqqivGVDKlapatsslslSQIIADYEPLTTAITtHGD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1704 DIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMA-LLAGATlcVVSREEQLS 1782
Cdd:PRK06087 188 ELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGFLHGVTApFLIGAR--SVLLDIFTP 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1783 TKALVKRFRDWNVTLADLPPVVLDsIL------PEDIPSLQTVSTGGERCPIKVAKR-WSLDRNFYNVYGPTEttiattw 1855
Cdd:PRK06087 266 DACLALLEQQRCTCMLGATPFIYD-LLnllekqPADLSALRFFLCGGTTIPKKVAREcQQRGIKLLSVYGSTE------- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1856 yrvSSPECVqdsVPI-----------GTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpf 1924
Cdd:PRK06087 338 ---SSPHAV---VNLddplsrfmhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARAL----- 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1925 rEEEILYKTGDIGKVLHDGNLEHLGRlDHQIKVRGFR-IELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGE 2003
Cdd:PRK06087 407 -DEEGWYYSGDLCRMDEAGYIKITGR-KKDIIVRGGEnISSREVEDILLQHPKIHDACVVAMPDERLGERSCAYVVLKAP 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 497785100 2004 WEEKKIIEEL----RSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK06087 485 HHSLTLEEVVaffsRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1553-1971 |
3.04e-24 |
|
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: 109.68 E-value: 3.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1553 AESQPRSIKDCIQYSFENWVRSSPNHIALrflDRSY---TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGF 1629
Cdd:cd05906 5 PEGAPRTLLELLLRAAERGPTKGITYIDA---DGSEefqSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1630 LGILKCGaaYVPIDSELPLNRRDF---------ILKDASVGAIVTQTSLEEKLSK----SDLPYLCTDQSQDSEDYS--- 1693
Cdd:cd05906 82 WACVLAG--FVPAPLTVPPTYDEPnarlrklrhIWQLLGSPVVLTDAELVAEFAGletlSGLPGIRVLSIEELLDTAadh 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1694 -LLTKDksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKvgQFATISFD--ASLWQI-LMALLAG 1769
Cdd:cd05906 160 dLPQSR---PDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDV--FLNWVPLDhvGGLVELhLRAVYLG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1770 ATLCVVSREEQLSTKAlvkRFRDW------NVTLAdlpPVVLDSILPE----------DIPSLQTVSTGGERCPIKVA-- 1831
Cdd:cd05906 235 CQQVHVPTEEILADPL---RWLDLidryrvTITWA---PNFAFALLNDlleeiedgtwDLSSLRYLVNAGEAVVAKTIrr 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1832 -----KRWSL-DRNFYNVYGPTETTIATTWYRVSSPECVQDS---VPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGV 1902
Cdd:cd05906 309 llrllEPYGLpPDAIRPAFGMTETCSGVIYSRSFPTYDHSQAlefVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGP 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497785100 1903 GVSNGYLNRDDLNEKRFIphpfreEEILYKTGDIGkVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLL 1971
Cdd:cd05906 389 VVTKGYYNNPEANAEAFT------EDGWFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAV 450
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
530-937 |
3.97e-24 |
|
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: 108.07 E-value: 3.97e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 530 RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIIT 609
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 610 HseyktsyegyevpilyidqlddfllderednlnvdcDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKP 689
Cdd:cd05907 84 E------------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALAERLPATE 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 690 KDRYLLLQSLAYDF-CLTTIYTSLLSGGTLFFL-----LKED--AIDP---AKVEEIvqgkaidWYKITPSHLKALSSES 758
Cdd:cd05907 128 GDRHLSFLPLAHVFeRRAGLYVPLLAGARIYFAssaetLLDDlsEVRPtvfLAVPRV-------WEKVYAAIKVKAVPGL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 759 GTKLFPR------KGLILGGEAsewswikeiyrnIPASCKLFNH---------YGPSETTIGVAVYEVTKkglsNQFSTt 823
Cdd:cd05907 201 KRKLFDLavggrlRFAASGGAP------------LPAELLHFFRalgipvyegYGLTETSAVVTLNPPGD----NRIGT- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 824 pIGSSLSNNRIYILDDklrpvpsgipGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKILYTGEIQFL 903
Cdd:cd05907 264 -VGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHIT 326
|
410 420 430
....*....|....*....|....*....|....*
gi 497785100 904 GRL-DGQVKIRGIRVEPEEIQSQLLSHPSITEAIV 937
Cdd:cd05907 327 GRKkDLIITSGGKNISPEPIENALKASPLISQAVV 361
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1587-2046 |
4.09e-24 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 109.08 E-value: 4.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1587 SYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQ 1666
Cdd:PRK13382 68 TLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1667 TSLEEKLSK--SDLPYLCTDQSQDSEDYSLLT----------KDKSYPEDIAYIIYTSGTTGTPNGVmvKHS---SVMNL 1731
Cdd:PRK13382 148 EEFSATVDRalADCPQATRIVAWTDEDHDLTVevliaahagqRPEPTGRKGRVILLTSGTTGTPKGA--RRSgpgGIGTL 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1732 iSATIDEFNITQETKVGQFATIsFDAslW---QILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLAdlpPVVLDSI 1808
Cdd:PRK13382 226 -KAILDRTPWRAEEPTVIVAPM-FHA--WgfsQLVLAASLACTIVTRRRFDPEATLDLIDRHRATGLAVV---PVMFDRI 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1809 --LPEDI------PSLQTVSTGGERCPIKVAKRWsLDR---NFYNVYGPTETTIATTwyrvSSPECVQDSVPI-GTPVPN 1876
Cdd:PRK13382 299 mdLPAEVrnrysgRSLRFAAASGSRMRPDVVIAF-MDQfgdVIYNNYNATEAGMIAT----ATPADLRAAPDTaGRPAEG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1877 TEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDlneKRFIphpfreeEILYKTGDIGKVLHDGNLEHLGRLDHQIK 1956
Cdd:PRK13382 374 TEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGST---KDFH-------DGFMASGDVGYLDENGRLFVVGRDDEMIV 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1957 VRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKII--EELRSKLPEHMVPSIFVQMEELPR 2034
Cdd:PRK13382 444 SGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGASATPETlkQHVRDNLANYKVPRDIVVLDELPR 523
|
490
....*....|..
gi 497785100 2035 LNNKKVDRHSLP 2046
Cdd:PRK13382 524 GATGKILRRELQ 535
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
499-999 |
5.35e-24 |
|
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: 108.69 E-value: 5.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 499 GCKPFPTE--------------PIHVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQ 564
Cdd:COG1021 4 GFTPWPEEfaaryreagywrgeTLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 565 PCAKAIIAMLGVLKAGGayLPLDVESPKERIEI--ITQDSKLKAIITHSEY-KTSYEGY------EVP----ILYIDQLD 631
Cdd:COG1021 84 NVAEFVIVFFALFRAGA--IPVFALPAHRRAEIshFAEQSEAVAYIIPDRHrGFDYRALarelqaEVPslrhVLVVGDAG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 632 DF-----LLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNlsnYIYAIQTK---LGNKPKDRYLLLQSLAYDF 703
Cdd:COG1021 162 EFtsldaLLAAPADLSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDD---YLYSVRASaeiCGLDADTVYLAALPAAHNF 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 704 CLT--TIYTSLLSGGTL----------FFLL--KEDAIDPAKVEEIVQG--KAIDWYKITPSHLKALSSeSGTKLFPrkg 767
Cdd:COG1021 239 PLSspGVLGVLYAGGTVvlapdpspdtAFPLieRERVTVTALVPPLALLwlDAAERSRYDLSSLRVLQV-GGAKLSP--- 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 768 lilggeasewswikEIYRNIPAS--CKLFNHYGPSEttigvavyevtkkGLSN----------QFST--TPIGSslsNNR 833
Cdd:COG1021 315 --------------ELARRVRPAlgCTLQQVFGMAE-------------GLVNytrlddpeevILTTqgRPISP---DDE 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 834 IYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKILYTGEIQFLGRLDGQVkIR 913
Cdd:COG1021 365 VRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF------YRTGDLVRRTPDGYLVVEGRAKDQI-NR 437
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 914 -GIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKKEVLD-KDLQTYLKQKlppNL----VPAYLVKMDTL 986
Cdd:COG1021 438 gGEKIAAEEVENLLLAHPAVHDaAVVAMPDEYLGERSCAFVVPRGEPLTlAELRRFLRER---GLaafkLPDRLEFVDAL 514
|
570
....*....|...
gi 497785100 987 PRHAHGKIDRKAL 999
Cdd:COG1021 515 PLTAVGKIDKKAL 527
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1576-2045 |
1.04e-23 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 107.38 E-value: 1.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQTSLEeklsksdlpYLCTDQSQDSeDYSLLtkdksYPED----IAyIIYTSGTTGTPNGVMVKHSSVMNL 1731
Cdd:cd12118 98 RHSEAKVLFVDREFE---------YEDLLAEGDP-DFEWI-----PPADewdpIA-LNYTSGTTGRPKGVVYHHRGAYLN 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1732 ISATIDEFNITQETkVGQFATISFDASLWQIL--MALLAGATLCVvsreEQLSTKALVKRFRDWNVTLADLPPVVLDSIL 1809
Cdd:cd12118 162 ALANILEWEMKQHP-VYLWTLPMFHCNGWCFPwtVAAVGGTNVCL----RKVDAKAIYDLIEKHKVTHFCGAPTVLNMLA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1810 ---PEDIPSL-QTVS--TGGERCPIKV-AKRWSLDRNFYNVYGPTETT---IATTWyrvsSPEcvQDSVPI--------- 1870
Cdd:cd12118 237 napPSDARPLpHRVHvmTAGAPPPAAVlAKMEELGFDVTHVYGLTETYgpaTVCAW----KPE--WDELPTeerarlkar 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1871 -GTPVPN-TEVFILDPD-LNPVPM-GV-IGEIYIGGVGVSNGYLNRDDLNEKRFiphpfreEEILYKTGDIGkVLH-DGN 1944
Cdd:cd12118 311 qGVRYVGlEEVDVLDPEtMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF-------RGGWFHSGDLA-VIHpDGY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1945 LEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV--PHGEWEEKKIIEELRSKLPEHMV 2022
Cdd:cd12118 383 IEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWGEVPCAFVElkEGAKVTEEEIIAFCREHLAGFMV 462
|
490 500
....*....|....*....|...
gi 497785100 2023 PSIFVqMEELPRLNNKKVDRHSL 2045
Cdd:cd12118 463 PKTVV-FGELPKTSTGKIQKFVL 484
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1576-2041 |
1.20e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 107.66 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPI-----DSELplnr 1650
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVnyryvEDEL---- 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1651 rDFILKDASVGAIVTQTSLEEKLS--KSDLPYLCT----------DQSQDSEDY-SLLTK--------DKSyPEDIaYII 1709
Cdd:PRK07798 93 -RYLLDDSDAVALVYEREFAPRVAevLPRLPKLRTlvvvedgsgnDLLPGAVDYeDALAAgsperdfgERS-PDDL-YLL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1710 YTSGTTGTPNGVMVKHSSV-------MNLISATI--DEFNITQETKVGqFATISFD-------ASLWQILMALLAGATlC 1773
Cdd:PRK07798 170 YTGGTTGMPKGVMWRQEDIfrvllggRDFATGEPieDEEELAKRAAAG-PGMRRFPapplmhgAGQWAAFAALFSGQT-V 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1774 VVSREEQLSTKALVKRFRDWNVTL------ADLPPVV--LDSILPEDIPSLQTVSTGGERCPIKVAKRWsLD----RNFY 1841
Cdd:PRK07798 248 VLLPDVRFDADEVWRTIEREKVNVitivgdAMARPLLdaLEARGPYDLSSLFAIASGGALFSPSVKEAL-LEllpnVVLT 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1842 NVYGPTET----TIATTwyrvsspecvQDSVPIGTPV--PNTEVFILDPDLNPVPMG--VIGEIYIGGVgVSNGYLNRDD 1913
Cdd:PRK07798 327 DSIGSSETgfggSGTVA----------KGAVHTGGPRftIGPRTVVLDEDGNPVEPGsgEIGWIARRGH-IPLGYYKDPE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1914 LNEKRFiphPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDnQNYHT 1993
Cdd:PRK07798 396 KTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVVGVPD-ERWGQ 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 497785100 1994 LVAYVV---PHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVD 2041
Cdd:PRK07798 472 EVVAVVqlrEGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
513-1002 |
1.25e-23 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 107.25 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 513 EGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQ-GIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESP 591
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 592 KERIEIITQDSKLKAIITHSEYKTSYE-----GYEVPILYIDQLDDfLLDEREDNLNVDCDSSQLAYgIYTSGSTGIPKG 666
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVEKTFQNMALsmqkvSYVQRVISITSLKE-IEDRKIDNFVEKNESASFII-CYTSGTTGKPKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 667 VLVEHRNL----SNYIYAIQTKLgnkpKDRYLLLQSLaydFCLTTI----YTSLLSGGTLfflLKEDAIDPAKVEEIVQG 738
Cdd:PRK06839 167 AVLTQENMfwnaLNNTFAIDLTM----HDRSIVLLPL---FHIGGIglfaFPTLFAGGVI---IVPRKFEPTKALSMIEK 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 739 KAIDWYKITPSHLKAL---SSESGTKLFPRKGLILGGEASEWSWIKE-IYRNIPascklFNH-YGPSETTigVAVYEVTK 813
Cdd:PRK06839 237 HKVTVVMGVPTIHQALincSKFETTNLQSVRWFYNGGAPCPEELMREfIDRGFL-----FGQgFGMTETS--PTVFMLSE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 814 KGLSNQFSTtpIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERfmedpfITDSRMYkTGDIGK 893
Cdd:PRK06839 310 EDARRKVGS--IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET------IQDGWLC-TGDLAR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 894 ILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKKE--VLDKDLQTYLKQK 970
Cdd:PRK06839 381 VDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEvAVVGRQHVKWGEIPIAFIVKKSSsvLIEKDVIEHCRLF 460
|
490 500 510
....*....|....*....|....*....|..
gi 497785100 971 LPPNLVPAYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:PRK06839 461 LAKYKIPKEIVFLKELPKNATGKIQKAQLVNQ 492
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1580-2049 |
2.77e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 105.84 E-value: 2.77e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1580 ALRFLDRSYTYDEVNKRANKIANQLykmgiRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDAS 1659
Cdd:PRK07787 18 AVRIGGRVLSRSDLAGAATAVAERV-----AGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1660 VGAIVTqtslEEKLSKSDLPYLCTDQSQDSEdyslLTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEF 1739
Cdd:PRK07787 93 AQAWLG----PAPDDPAGLPHVPVRLHARSW----HRYPEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAW 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1740 NITQE-----------------------------TKVGQFATISFDAslwqilmALLAGATL-----CVVSR--EEQLST 1783
Cdd:PRK07787 165 QWTADdvlvhglplfhvhglvlgvlgplrignrfVHTGRPTPEAYAQ-------ALSEGGTLyfgvpTVWSRiaADPEAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1784 KALvKRFRDWNVTLADLPPVVLDSIlpedipslqTVSTGGErcpikVAKRwsldrnfynvYGPTETTIaTTWYRVSS--- 1860
Cdd:PRK07787 238 RAL-RGARLLVSGSAALPVPVFDRL---------AALTGHR-----PVER----------YGMTETLI-TLSTRADGerr 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1861 PECVqdsvpiGTPVPNTEVFILDPDLNPVPMGV--IGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFreeeilYKTGDIGK 1938
Cdd:PRK07787 292 PGWV------GLPLAGVETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAV 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1939 VLHDGNLEHLGR--LDhQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSK 2016
Cdd:PRK07787 360 VDPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQRIVAYVVGADDVAADELIDFVAQQ 438
|
490 500 510
....*....|....*....|....*....|...
gi 497785100 2017 LPEHMVPSIFVQMEELPRLNNKKVDRHSLPTAV 2049
Cdd:PRK07787 439 LSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
520-1002 |
2.96e-23 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 108.47 E-value: 2.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHE-RSYTYLQTNNRANQIARWLqKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEII 598
Cdd:PRK08633 629 WSRLAVADSTgGELSYGKALTGALALARLL-KRELKDEENVGILLPPSVAGALANLALLLAGKVPVNLNYTASEAALKSA 707
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAIITHSEY----KTSYEGYEVP----ILYIDQLDD-------------------FLLdEREDNLNVDCDssQL 651
Cdd:PRK08633 708 IEQAQIKTVITSRKFleklKNKGFDLELPenvkVIYLEDLKAkiskvdkltallaarllpaRLL-KRLYGPTFKPD--DT 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 652 AYGIYTSGSTGIPKGVLVEHRN-LSNyIYAIQTKLGNKPKDRylLLQSLA--YDFCLTtiytsllsgGTLFFLLKEDA-- 726
Cdd:PRK08633 785 ATIIFSSGSEGEPKGVMLSHHNiLSN-IEQISDVFNLRNDDV--ILSSLPffHSFGLT---------VTLWLPLLEGIkv 852
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 727 ---IDPAKVEEIvqGKAIDWYKI-----TPSHLKA-LSSESGTKL-FPRKGLILGG---------EASEWSWIKEIYRNi 787
Cdd:PRK08633 853 vyhPDPTDALGI--AKLVAKHRAtillgTPTFLRLyLRNKKLHPLmFASLRLVVAGaeklkpevaDAFEEKFGIRILEG- 929
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 788 pascklfnhYGPSETT--IGVAVYEVTKKGLSNQFSTTP--IGSSLSNNRIYILD-DKLRPVPSGIPGHIYIAGEQVARG 862
Cdd:PRK08633 930 ---------YGATETSpvASVNLPDVLAADFKRQTGSKEgsVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKG 1000
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 863 YLNREELTAERFMEdpfITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRG-----IRVEpEEIQSQLLShpsiTEAIV 937
Cdd:PRK08633 1001 YLGDPEKTAEVIKD---IDGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGemvplGAVE-EELAKALGG----EEVVF 1072
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 938 TVTKVRNE---EQLVAYYVSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:PRK08633 1073 AVTAVPDEkkgEKLVVLHTCGAEDVEELKRAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1586-2040 |
4.38e-23 |
|
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: 106.51 E-value: 4.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1586 RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPI--------------DSELPL--- 1648
Cdd:cd17634 83 RTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIfggfapeavagriiDSSSRLlit 162
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1649 -------NRRDFILKDASVGAIVTQTSLEEKL--SKSDLPYlctdQSQDSED--YSLLTKDKS--------YPEDIAYII 1709
Cdd:cd17634 163 adggvraGRSVPLKKNVDDALNPNVTSVEHVIvlKRTGSDI----DWQEGRDlwWRDLIAKASpehqpeamNAEDPLFIL 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1710 YTSGTTGTPNGVMvkHSSVMNLISATIDEFNITQ---------ETKVGQFATISfdaslWQILMALLAGAT-LCVVSREE 1779
Cdd:cd17634 239 YTSGTTGKPKGVL--HTTGGYLVYAATTMKYVFDygpgdiywcTADVGWVTGHS-----YLLYGPLACGATtLLYEGVPN 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1780 QLSTKALVKRFRDWNVTLADLPPVVLDSILPE--------DIPSLQTVSTGGERCPIKvAKRWsldrnFYNVYGPTETTI 1851
Cdd:cd17634 312 WPTPARMWQVVDKHGVNILYTAPTAIRALMAAgddaiegtDRSSLRILGSVGEPINPE-AYEW-----YWKKIGKEKCPV 385
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1852 ATTWYRVSSPECVQDSVPIGT---------PVPNTEVFILDPDLNPVPMGVIGEIYIGGV--GVSNGYLNRDDlnekRFI 1920
Cdd:cd17634 386 VDTWWQTETGGFMITPLPGAIelkagsatrPVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHE----RFE 461
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1921 PHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV- 1999
Cdd:cd17634 462 QTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAAVVGIPHAIKGQAPYAYVVl 541
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 497785100 2000 PHGEWEEKKIIEELRSKLPEHM----VPSIFVQMEELPRLNNKKV 2040
Cdd:cd17634 542 NHGVEPSPELYAELRNWVRKEIgplaTPDVVHWVDSLPKTRSGKI 586
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1588-2001 |
8.94e-23 |
|
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: 104.06 E-value: 8.94e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1588 YTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTqt 1667
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFV-- 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1668 sleeklsksdlpylctdqsqdsedyslltkdkSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISAtIDEFNITQETKV 1747
Cdd:cd05914 86 --------------------------------SDEDDVALINYTSGTTGNSKGVMLTYRNIVSNVDG-VKEVVLLGKGDK 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1748 gqfaTISF------DASLWQILMALLAGATlcVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSILPEDIPSLQTVST 1821
Cdd:cd05914 133 ----ILSIlplhhiYPLTFTLLLPLLNGAH--VVFLDKIPSAKIIALAFAQVTPTLGVPVPLVIEKIFKMDIIPKLTLKK 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1822 GGERC--PIKVAKRWSL---------------------------DRNFYNV-------YGPTETT--IATT-WYRVSSPE 1862
Cdd:cd05914 207 FKFKLakKINNRKIRKLafkkvheafggnikefviggakinpdvEEFLRTIgfpytigYGMTETApiISYSpPNRIRLGS 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1863 CvqdsvpiGTPVPNTEVFILDPDlnpvPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFreeeilYKTGDIGKVLHD 1942
Cdd:cd05914 287 A-------GKVIDGVEVRIDSPD----PATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKIDAE 349
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497785100 1943 GNLEHLGRLDHQIKV-RGFRIELGEIESLLNLQTGVKEA-IVQplgdnQNYHtLVAYVVPH 2001
Cdd:cd05914 350 GYLYIRGRKKEMIVLsSGKNIYPEEIEAKINNMPFVLESlVVV-----QEKK-LVALAYID 404
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
520-999 |
1.20e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 104.68 E-value: 1.20e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPL------------- 586
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALhplgslddhayvl 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 587 -DVESP---------KER-IEIITQDSKLKAIITHSEYktsyeGYEVPILyiDQLDDFLlDEREDNLNVDCDSSQLAYgi 655
Cdd:PRK06188 106 eDAGIStlivdpapfVERaLALLARVPSLKHVLTLGPV-----PDGVDLL--AAAAKFG-PAPLVAAALPPDIAGLAY-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 656 yTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDfCLTTIYTSLLSGGTLFFLlkeDAIDPAKVEEI 735
Cdd:PRK06188 176 -TGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFLMCTPLSHA-GGAFFLPTLLRGGTVIVL---AKFDPAEVLRA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 736 VQGKAIDWYKITPSHLKAL--SSESGTKLFPRKGLIL-GGEASEWSWIKE-IYRNIPAsckLFNHYGPSETTIGVAVYEV 811
Cdd:PRK06188 251 IEEQRITATFLVPTMIYALldHPDLRTRDLSSLETVYyGASPMSPVRLAEaIERFGPI---FAQYYGQTEAPMVITYLRK 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 812 TKKGLSNQFSTTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDpfitdsrMYKTGDI 891
Cdd:PRK06188 328 RDHDPDDPKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG-------WLHTGDV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 892 GKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSIteAIVTVTKVRNE---EQLVAYYVSKKE--VLDKDLQTY 966
Cdd:PRK06188 401 AREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAV--AQVAVIGVPDEkwgEAVTAVVVLRPGaaVDAAELQAH 478
|
490 500 510
....*....|....*....|....*....|...
gi 497785100 967 LKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK06188 479 VKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
530-999 |
1.63e-22 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 104.29 E-value: 1.63e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 530 RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGA-------YLPLdvespkeriEIITQ-- 600
Cdd:PLN02246 49 RVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttanpfYTPA---------EIAKQak 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 601 DSKLKAIITHSEY----KTSYEGYEVPILYIDQ-------LDDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLV 669
Cdd:PLN02246 120 ASGAKLIITQSCYvdklKGLAEDDGVTVVTIDDppegclhFSELTQADENELPEVEISPDDVVALPYSSGTTGLPKGVML 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 670 EHRNLSNYIyAIQT-----KLGNKPKDRYLLLQSLAYDFCLTTI-YTSLLSGGTLFFLLKedaIDPAKVEEIVQGkaidw 743
Cdd:PLN02246 200 THKGLVTSV-AQQVdgenpNLYFHSDDVILCVLPMFHIYSLNSVlLCGLRVGAAILIMPK---FEIGALLELIQR----- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 744 YKIT-----PSHLKALSSESGTKLFPRKGL--ILGGEASEWSWIKEIYRNIPASCKLFNHYGPSETTIGVAvyevtkkgL 816
Cdd:PLN02246 271 HKVTiapfvPPIVLAIAKSPVVEKYDLSSIrmVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMTEAGPVLA--------M 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 817 SNQFSTTPI-------GSSLSNNRIYILD-DKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFItdsrmyKT 888
Cdd:PLN02246 343 CLAFAKEPFpvksgscGTVVRNAELKIVDpETGASLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGWL------HT 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 889 GDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTK------------VRNE-----EQLVAY 951
Cdd:PLN02246 417 GDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKdevagevpvafvVRSNgseitEDEIKQ 496
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 497785100 952 YVSKKEVLDKDLQTylkqklppnlvpAYLVkmDTLPRHAHGKIDRKAL 999
Cdd:PLN02246 497 FVAKQVVFYKRIHK------------VFFV--DSIPKAPSGKILRKDL 530
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1554-2045 |
1.76e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 104.34 E-value: 1.76e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1554 ESQPRSIKDCIQYS-------FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMI 1626
Cdd:PRK06710 9 KSYPEEIPSTISYDiqplhkyVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAV 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1627 FGFLGILKCGAAYV---PIDSELPLNRR------------DFIL-KDASVGA-------IVT------------------ 1665
Cdd:PRK06710 89 IGYYGTLLAGGIVVqtnPLYTERELEYQlhdsgakvilclDLVFpRVTNVQSatkiehvIVTriadflpfpknllypfvq 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1666 --QTSLEEKLSKSDLPYLCTDQSQDSEDYSLLTKDksyPE-DIAYIIYTSGTTGTPNGVMVKHSsvmNLISATIDEFNIT 1742
Cdd:PRK06710 169 kkQSNLVVKVSESETIHLWNSVEKEVNTGVEVPCD---PEnDLALLQYTGGTTGFPKGVMLTHK---NLVSNTLMGVQWL 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1743 QETKVGQFATIS----FDASLWQILM--ALLAGATLCVVSReeqLSTKALVKRFRDWNVTLADLPPVVLDSILPE----- 1811
Cdd:PRK06710 243 YNCKEGEEVVLGvlpfFHVYGMTAVMnlSIMQGYKMVLIPK---FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSpllke 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1812 -DIPSLQTVSTGGERCPIKVAKRWS--LDRNFYNVYGPTETTIATtwyrvSSPECVQDSVP--IGTPVPNTEVFILDPDL 1886
Cdd:PRK06710 320 yDISSIRACISGSAPLPVEVQEKFEtvTGGKLVEGYGLTESSPVT-----HSNFLWEKRVPgsIGVPWPDTEAMIMSLET 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1887 NPV-PMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfreEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELG 1965
Cdd:PRK06710 395 GEAlPPGEIGEIVVKGPQIMKGYWNKPEETAAVL-------QDGWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPR 467
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1966 EIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV-PHGEWEEKKIIEEL-RSKLPEHMVPSIFVQMEELPRLNNKKVDRH 2043
Cdd:PRK06710 468 EVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVlKEGTECSEEELNQFaRKYLAAYKVPKVYEFRDELPKTTVGKILRR 547
|
..
gi 497785100 2044 SL 2045
Cdd:PRK06710 548 VL 549
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1108-1315 |
1.97e-22 |
|
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: 102.72 E-value: 1.97e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1108 IPLSDAQKrmWFLYRMESDSAYYNMPISLKIIGDLDYRAFTESIQEVNKRHDSLRTVFRESKNiDPVQVVLKDLKCTI-- 1185
Cdd:cd19534 2 VPLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDG-GWQQRIRGDVEELFrl 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1186 NILDFDENRSEQDIMNYLTE--KSMEpfkLETGPLIRVHLVKSNPNEHVLLIVQHHIISDGWSLRIMMDELFAIYHQIIS 1263
Cdd:cd19534 79 EVVDLSSLAQAAAIEALAAEaqSSLD---LEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALA 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 497785100 1264 NMPIQLEqPVYQYADYVNWQQNRYTEEQINQQLQYWKEQLSGAPSllELPLD 1315
Cdd:cd19534 156 GEPIPLP-SKTSFQTWAELLAEYAQSPALLEELAYWRELPAADYW--GLPKD 204
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
503-1001 |
2.37e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 103.96 E-value: 2.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 503 FPTEPIHVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGA 582
Cdd:PRK06710 21 YDIQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGI 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 583 YLPLDVESPKERIEIITQDSKLKAII----THSEYKTSYEGYEVPILYIDQLDDFLL----------------------- 635
Cdd:PRK06710 101 VVQTNPLYTERELEYQLHDSGAKVILcldlVFPRVTNVQSATKIEHVIVTRIADFLPfpknllypfvqkkqsnlvvkvse 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 636 -----------DEREDNLNVDCD-SSQLAYGIYTSGSTGIPKGVLVEHRNL-SNYIYAIQTKLGNKPKDRYLL-LQSLAY 701
Cdd:PRK06710 181 setihlwnsveKEVNTGVEVPCDpENDLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLYNCKEGEEVVLgVLPFFH 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 702 DFCLTTIYT-SLLSGGTLFFLLKedaIDPAKVEEIVQGKAIDWYKITPSHLKALSSESGTKLFPRKGL--ILGGEASEWS 778
Cdd:PRK06710 261 VYGMTAVMNlSIMQGYKMVLIPK---FDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYDISSIraCISGSAPLPV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 779 WIKEIYRNIPAScKLFNHYGPSETTigvavyEVTKKG-LSNQFSTTPIGSSLSNNRIYILD-DKLRPVPSGIPGHIYIAG 856
Cdd:PRK06710 338 EVQEKFETVTGG-KLVEGYGLTESS------PVTHSNfLWEKRVPGSIGVPWPDTEAMIMSlETGEALPPGEIGEIVVKG 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 857 EQVARGYLNREELTAErFMEDPFItdsrmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAI 936
Cdd:PRK06710 411 PQIMKGYWNKPEETAA-VLQDGWL------HTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVV 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 937 VT-VTKVRNEEQLVAYYVSKK--EVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPE 1001
Cdd:PRK06710 484 TIgVPDPYRGETVKAFVVLKEgtECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
49-473 |
2.67e-22 |
|
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: 102.00 E-value: 2.67e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 49 YPLSSIQKQIWFMSQLNPELPIY-NEHLIKinLSGKVNIEALKKSFEQIVNRHQILRMRV--KQTEDSIEQVITKSEPTI 125
Cdd:cd19547 2 YPLAPMQEGMLFRGLFWPDSDAYfNQNVLE--LVGGTDEDVLREAWRRVADRYEILRTGFtwRDRAEPLQYVRDDLAPPW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 126 QFLSLRGISGEEQQEILSEYCRKEANYPYRLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNMYS 205
Cdd:cd19547 80 ALLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGWCLSLIWGDVFRVYEELA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 206 QNGEinpeqSQEELTIQYHDYALW-QEKLLTSENLEKgleYWKEKLEGDLPM-LSIGGITQEGTGVGSEYNFkiPNILTD 283
Cdd:cd19547 160 HGRE-----PQLSPCRPYRDYVRWiRARTAQSEESER---FWREYLRDLTPSpFSTAPADREGEFDTVVHEF--PEQLTR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 284 KLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGR--NIRETRNVIGPFINTVVIRTKAEQNLSVIEYLQQV 361
Cdd:cd19547 230 LVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETI 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 362 HETTIQALENQDVPFEKVVEVLNPNRDVRANPFYQLLFVMQEPptQFSLPGIKVEYELI---PTEVARFPLTLSIIEGEE 438
Cdd:cd19547 310 HRDLATTAAHGHVPLAQIKSWASGERLSGGRVFDNLVAFENYP--EDNLPGDDLSIQIIdlhAQEKTEYPIGLIVLPLQK 387
|
410 420 430
....*....|....*....|....*....|....*
gi 497785100 439 MIGRVLYRTSILSEYEVQSFVQRLLQVADEIVQSP 473
Cdd:cd19547 388 LAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
520-995 |
2.69e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 103.43 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIITHSEY--------------KT-------SYEGYEVP-ILYIDQL----DDFLLDER-EDNLnvdcdssqla 652
Cdd:PRK07798 97 DDSDAVALVYEREFaprvaevlprlpklRTlvvvedgSGNDLLPGaVDYEDALaagsPERDFGERsPDDL---------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 653 YGIYTSGSTGIPKGVLVEHRNlsnyIY-----AIQTKLGNKPKDRYLLLQSLA-------YDFC-------LTTIYTSLL 713
Cdd:PRK07798 167 YLLYTGGTTGMPKGVMWRQED----IFrvllgGRDFATGEPIEDEEELAKRAAagpgmrrFPAPplmhgagQWAAFAALF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 714 SGGTLFfLLKEDAIDPAKVEEIVQG------------------KAIDWYKITP-SHLKALSSeSGTKLFP--RKGLIlgg 772
Cdd:PRK07798 243 SGQTVV-LLPDVRFDADEVWRTIERekvnvitivgdamarpllDALEARGPYDlSSLFAIAS-GGALFSPsvKEALL--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 773 easewswikEIYRNIpascKLFNHYGPSETTIGVAVyeVTKKGLSNQFSTT-PIGSslsnnRIYILDDKLRPVPSGIPGH 851
Cdd:PRK07798 318 ---------ELLPNV----VLTDSIGSSETGFGGSG--TVAKGAVHTGGPRfTIGP-----RTVVLDEDGNPVEPGSGEI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 852 IYIA-GEQVARGYLNREELTAERFmedPFITDSRMYKTGDIGKILYTGEIQFLGRldGQVKIR--GIRVEPEEIQSQLLS 928
Cdd:PRK07798 378 GWIArRGHIPLGYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGR--GSVCINtgGEKVFPEEVEEALKA 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497785100 929 HPSITEAIVtvtkV-RNEE---QLVAYYVSKKE---VLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKID 995
Cdd:PRK07798 453 HPDVADALV----VgVPDErwgQEVVAVVQLREgarPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
656-996 |
2.78e-22 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 100.82 E-value: 2.78e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 656 YTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDF-CLTTIYTSLLSGGTLFFLlkEDAIDPAKV-E 733
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLFHCFgSVLGVLACLTHGATMVFP--SPSFDPLAVlE 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 734 EIVQGKAIDWYKiTPSHLKALSSESGTKLFP----RKGLILGGEASEwswikEIYRnipascKLFNHYGPSETTIGVAVY 809
Cdd:cd05917 87 AIEKEKCTALHG-VPTMFIAELEHPDFDKFDlsslRTGIMAGAPCPP-----ELMK------RVIEVMNMKDVTIAYGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 810 EvTKKGLSNQFSTTPI-------GSSLSNNRIYILDDKLRPVPS-GIPGHIYIAGEQVARGYLNREELTAERfmedpfIT 881
Cdd:cd05917 155 E-TSPVSTQTRTDDSIekrvntvGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEA------ID 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 882 DSRMYKTGDIGKILYTGEIQFLGRLDGQVkIRGIR-VEPEEIQSQLLSHPSITEA-IVTVTKVRNEEQLVAYYVSK--KE 957
Cdd:cd05917 228 GDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVqVVGVPDERYGEEVCAWIRLKegAE 306
|
330 340 350
....*....|....*....|....*....|....*....
gi 497785100 958 VLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDR 996
Cdd:cd05917 307 LTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
519-999 |
2.79e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 103.04 E-value: 2.79e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEII 598
Cdd:PRK06145 15 TPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAIITHSEYKTSyEGYEVPILYIDQlddfllderednlNVDCDSSQLAYG------------------IYTSGS 660
Cdd:PRK06145 95 LGDAGAKLLLVDEEFDAI-VALETPKIVIDA-------------AAQADSRRLAQGgleippqaavaptdlvrlMYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 661 TGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSL----AYDFCLTTIytsLLSGGTLFFllkEDAIDPAKVEEIV 736
Cdd:PRK06145 161 TDRPKGVMHSYGNLHWKSIDHVIALGLTASERLLVVGPLyhvgAFDLPGIAV---LWVGGTLRI---HREFDPEAVLAAI 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 737 QGKAIDWYKITPSHLKALSSESGTKLFPRKGL---ILGGEASEWSWIKEIYRnIPASCKLFNHYGPSETTIGVAVYEVTK 813
Cdd:PRK06145 235 ERHRLTCAWMAPVMLSRVLTVPDRDRFDLDSLawcIGGGEKTPESRIRDFTR-VFTRARYIDAYGLTETCSGDTLMEAGR 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 814 KgLSNQFSTtpiGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmyKTGDIGK 893
Cdd:PRK06145 314 E-IEKIGST---GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGY 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 894 ILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYV-SKKEVLDKD-LQTYLKQK 970
Cdd:PRK06145 383 LDEEGFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEaAVIGVHDDRWGERITAVVVlNPGATLTLEaLDRHCRQR 462
|
490 500
....*....|....*....|....*....
gi 497785100 971 LPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK06145 463 LASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1588-1999 |
3.50e-22 |
|
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: 101.88 E-value: 3.50e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1588 YTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSEL-PLNRRDFILKDASVGAIVTQ 1666
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLtPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1667 TSleeklsKSDLPYLctdqsqdsedyslltkdksypediayIIYTSGTTGTPNGVM-------VKHSSVMNLISATIDE- 1738
Cdd:cd05974 81 NT------HADDPML--------------------------LYFTSGTTSKPKLVEhthrsypVGHLSTMYWIGLKPGDv 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1739 -FNITQEtkvgqfatiSFDASLWQILMA-LLAGATLCVVSrEEQLSTKALVKRFRDWNVTLADLPPVVLDSILPEDIPSL 1816
Cdd:cd05974 129 hWNISSP---------GWAKHAWSCFFApWNAGATVFLFN-YARFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1817 QT----VSTGGErcPI------KVAKRWSLdrNFYNVYGPTETTIATTwyrvSSPECVQDSVPIGTPVPNTEVFILDPDL 1886
Cdd:cd05974 199 DVklreVVGAGE--PLnpevieQVRRAWGL--TIRDGYGQTETTALVG----NSPGQPVKAGSMGRPLPGYRVALLDPDG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1887 NPVPMGVIGeIYIGG---VGVSNGYLNRDDLNEKRFiphpfreEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIE 1963
Cdd:cd05974 271 APATEGEVA-LDLGDtrpVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRIS 342
|
410 420 430
....*....|....*....|....*....|....*.
gi 497785100 1964 LGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV 1999
Cdd:cd05974 343 PFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIV 378
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
520-1002 |
3.51e-22 |
|
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: 102.99 E-value: 3.51e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSD--HERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPL-DVESPKERI- 595
Cdd:cd17642 31 PGTIAFTDahTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTnDIYNERELDh 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 596 ------------------EIITQDSKLKAI--ITHSEYKTSYEGYEVPILYIDQLDDFLLDERE---DNLNVDcdsSQLA 652
Cdd:cd17642 111 slniskptivfcskkglqKVLNVQKKLKIIktIIILDSKEDYKGYQCLYTFITQNLPPGFNEYDfkpPSFDRD---EQVA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 653 YGIYTSGSTGIPKGVLVEHRNL-SNYIYAIQTKLGNKPKDRYLLLQSLAY--DFCLTTIYTSLLSGGTLFFLlkedaidp 729
Cdd:cd17642 188 LIMNSSGSTGLPKGVQLTHKNIvARFSHARDPIFGNQIIPDTAILTVIPFhhGFGMFTTLGYLICGFRVVLM-------- 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 730 AKVEEIVQGKAIDWYKITpshlKALSSESGTKLFPRKGLILGGEASEWSWI--------KEIYRNIPASCKL---FNHYG 798
Cdd:cd17642 260 YKFEEELFLRSLQDYKVQ----SALLVPTLFAFFAKSTLVDKYDLSNLHEIasggaplsKEVGEAVAKRFKLpgiRQGYG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 799 PSETTIGVAVY--EVTKKGLSNQ----FSTTPI----GSSLSNNRiyilddklrpvpsgiPGHIYIAGEQVARGYLNREE 868
Cdd:cd17642 336 LTETTSAILITpeGDDKPGAVGKvvpfFYAKVVdldtGKTLGPNE---------------RGELCVKGPMIMKGYVNNPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 869 LTAERFMEDPFItdsrmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQL 948
Cdd:cd17642 401 ATKALIDKDGWL------HSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGEL 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 949 VAYYV---SKKEVLDKDLQTYLK-QKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:cd17642 475 PAAVVvleAGKTMTEKEVMDYVAsQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIREI 532
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
655-996 |
5.47e-22 |
|
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: 99.64 E-value: 5.47e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 655 IYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQS-LAYDFCLTTIYTSLLSGGTLffLLKEDAIDPAKVE 733
Cdd:cd17635 7 IFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLpATHIGGLWWILTCLIHGGLC--VTGGENTTYKSLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 734 EIVQGKAIDWYKITPSHLKALSSESGTKLFPRKGLILGGEASEWSWIKEIyRNIPAS--CKLFNHYGPSETtiGVAVYEV 811
Cdd:cd17635 85 KILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSRAIAADV-RFIEATglTNTAQVYGLSET--GTALCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 812 TKKGLSNQFSttpIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmyKTGDI 891
Cdd:cd17635 162 TDDDSIEINA---VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV-------NTGDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 892 GKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYVSKKEVLDKDLQTYLKQK- 970
Cdd:cd17635 232 GERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELVGLAVVASAELDENAIRALKHTi 311
|
330 340
....*....|....*....|....*....
gi 497785100 971 ---LPPNLVPAYLVKMDTLPRHAHGKIDR 996
Cdd:cd17635 312 rreLEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1141-1439 |
8.62e-22 |
|
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: 100.64 E-value: 8.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1141 DLDYRAFTESIQEVNKRHDSLRTVFREskniDPVQVVLKDLKC-TINILDFdENRSEQDIMNYLTE----KSMEPFKLET 1215
Cdd:cd19535 36 DLDPDRLERAWNKLIARHPMLRAVFLD----DGTQQILPEVPWyGITVHDL-RGLSEEEAEAALEElrerLSHRVLDVER 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1216 GPLIRVHLVKSNPNEHVLlivqhHI-----ISDGWSLRIMMDELFAIYHqiisNMPIQLEQPVYQYADYVNWQQNRyTEE 1290
Cdd:cd19535 111 GPLFDIRLSLLPEGRTRL-----HLsidllVADALSLQILLRELAALYE----DPGEPLPPLELSFRDYLLAEQAL-RET 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1291 QINQQLQYWKEQLS---GAPsllELPL-------DKPRPSMQSYngslirmKLPEKHAVLIKEICEEAKVTPYTIFLTFF 1360
Cdd:cd19535 181 AYERARAYWQERLPtlpPAP---QLPLakdpeeiKEPRFTRREH-------RLSAEQWQRLKERARQHGVTPSMVLLTAY 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1361 NILLYRYTYQDKILVGTPIANRN--IQELEGILGLFVNTLVIPSTVKGDRNFKSLLQQVNNQILGALENQDISFERIVQE 1438
Cdd:cd19535 251 AEVLARWSGQPRFLLNLTLFNRLplHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSYSGVVVVRR 330
|
.
gi 497785100 1439 L 1439
Cdd:cd19535 331 L 331
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
520-999 |
1.34e-21 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 101.22 E-value: 1.34e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAylPLDVESPKERIEIIT 599
Cdd:PRK10946 37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSELNA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 -----QDSKLKAIITHS---------EYKTSYEGYEVPILYIDQ----LDDFLLDEREDNLNVDCDSSQLAYGIYTSGST 661
Cdd:PRK10946 115 yasqiEPALLIADRQHAlfsdddflnTLVAEHSSLRVVLLLNDDgehsLDDAINHPAEDFTATPSPADEVAFFQLSGGST 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 662 GIPKgvLVEhRNLSNYIYAIQTKL---GNKPKDRYLLLQSLAYDFCLTT--IYTSLLSGGTLFFllkedAIDPAKVE--E 734
Cdd:PRK10946 195 GTPK--LIP-RTHNDYYYSVRRSVeicGFTPQTRYLCALPAAHNYPMSSpgALGVFLAGGTVVL-----APDPSATLcfP 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 735 IVQGKAIDWYKITPSH----LKALS-SESGTKLFPRKGLILGGEA-SEwswikEIYRNIPA--SCKLFNHYGPSEttiGV 806
Cdd:PRK10946 267 LIEKHQVNVTALVPPAvslwLQAIAeGGSRAQLASLKLLQVGGARlSE-----TLARRIPAelGCQLQQVFGMAE---GL 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 807 AVYevTKKGLSNQFSTTPIGSSLSNN-RIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrm 885
Cdd:PRK10946 339 VNY--TRLDDSDERIFTTQGRPMSPDdEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF------ 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 886 YKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKKEVLDKDLQ 964
Cdd:PRK10946 411 YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHaALVSMEDELMGEKSCAFLVVKEPLKAVQLR 490
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 497785100 965 TYLKQ------KLPPNlvpaylVKM-DTLPRHAHGKIDRKAL 999
Cdd:PRK10946 491 RFLREqgiaefKLPDR------VECvDSLPLTAVGKVDKKQL 526
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
519-1001 |
1.53e-21 |
|
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: 101.03 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIAL---SDH--ERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKE 593
Cdd:cd05970 30 YPDKLALvwcDDAgeERIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 594 RIEIITQDSKLKAIITHSEY-------KTSYEGYEVPILY------IDQLDDF--LLDE-------REDNLNVDCDSSQL 651
Cdd:cd05970 110 DIVYRIESADIKMIVAIAEDnipeeieKAAPECPSKPKLVwvgdpvPEGWIDFrkLIKNaspdferPTANSYPCGEDILL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 652 AYgiYTSGSTGIPKgvLVEHRNLSNYIYAIQTKLGN--KPKDRYLLLQSLAYDFCL-TTIYTSLLSGGTLFfLLKEDAID 728
Cdd:cd05970 190 VY--FSSGTTGMPK--MVEHDFTYPLGHIVTAKYWQnvREGGLHLTVADTGWGKAVwGKIYGQWIAGAAVF-VYDYDKFD 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 729 PAKVEEIVQGKAIDWYKITPSHLKALSSESGTK--LFPRKGLILGGEASEWSwIKEIYRNIpASCKLFNHYGPSETTIGV 806
Cdd:cd05970 265 PKALLEKLSKYGVTTFCAPPTIYRFLIREDLSRydLSSLRYCTTAGEALNPE-VFNTFKEK-TGIKLMEGFGQTETTLTI 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 807 AVYEVT--KKGlsnqfsttPIGSSLSNNRIYILDDKLRPVPSGIPGHIYI---AGEQVA--RGYLNREELTAERFMEDpf 879
Cdd:cd05970 343 ATFPWMepKPG--------SMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtsKGKPVGlfGGYYKDAEKTAEVWHDG-- 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 880 itdsrMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLV-AYYVSKK-- 956
Cdd:cd05970 413 -----YYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVkATIVLAKgy 487
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 497785100 957 ---EVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPE 1001
Cdd:cd05970 488 epsEELKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1576-1910 |
1.91e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 101.01 E-value: 1.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:PRK07786 31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQTSLEEKLS--KSDLPYLCT-----DQSQDS----EDYSLLTKDKSYPEDI-----AYIIYTSGTTGTPN 1719
Cdd:PRK07786 111 SDCGAHVVVTEAALAPVATavRDIVPLLSTvvvagGSSDDSvlgyEDLLAEAGPAHAPVDIpndspALIMYTSGTTGRPK 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1720 GVMVKHSSVMNLISATIDEFNITQETKVGQFATISFD-ASLWQILMALLAGATLCV-------------VSREEQLSTKA 1785
Cdd:PRK07786 191 GAVLTHANLTGQAMTCLRTNGADINSDVGFVGVPLFHiAGIGSMLPGLLLGAPTVIyplgafdpgqlldVLEAEKVTGIF 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1786 LVKrfRDWNVTLADlppvvlDSILPEDIpSLQTVSTGGERCPIKVAKRWSL---DRNFYNVYGPTETTIATtwyrvsspe 1862
Cdd:PRK07786 271 LVP--AQWQAVCAE------QQARPRDL-ALRVLSWGAAPASDTLLRQMAAtfpEAQILAAFGQTEMSPVT--------- 332
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 1863 CV---QDSV----PIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLN 1910
Cdd:PRK07786 333 CMllgEDAIrklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWN 387
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1561-2042 |
2.56e-21 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 100.62 E-value: 2.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1561 KDCIQYSFENWVRSSPNHIAL--RFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAA 1638
Cdd:PRK12583 17 TQTIGDAFDATVARFPDREALvvRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1639 YVPIDSELPLNRRDFILKDASVGAIVT--------------------QTSLEEKLSKSDLPYLCTDQSQDSEDYSLLTkd 1698
Cdd:PRK12583 97 LVNINPAYRASELEYALGQSGVRWVICadafktsdyhamlqellpglAEGQPGALACERLPELRGVVSLAPAPPPGFL-- 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1699 kSYPE-----------------------DIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKV-------- 1747
Cdd:PRK12583 175 -AWHElqargetvsrealaerqasldrdDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLcvpvplyh 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1748 ------GQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFrdwnvtLADLPPVVLDSIlpeDIPSLQTVST 1821
Cdd:PRK12583 254 cfgmvlANLGCMTVGACLVYPNEAFDPLATLQAVEEERCTALYGVPTMF------IAELDHPQRGNF---DLSSLRTGIM 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1822 GGERCPIKVAKRWSLDRNFYNV---YGPTETTiattwyRVSSPECVQDSVP-----IGTPVPNTEVFILDPDLNPVPMGV 1893
Cdd:PRK12583 325 AGAPCPIEVMRRVMDEMHMAEVqiaYGMTETS------PVSLQTTAADDLErrvetVGRTQPHLEVKVVDPDGATVPRGE 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1894 IGEIYIGGVGVSNGYLNRDDLNEKRFiphpfrEEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNL 1973
Cdd:PRK12583 399 IGELCTRGYSVMKGYWNNPEATAESI------DEDGWMHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFT 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497785100 1974 QTGVKEAIVQPLGDNQNYHTLVAYVV--PHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDR 2042
Cdd:PRK12583 473 HPAVADVQVFGVPDEKYGEEIVAWVRlhPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
519-1001 |
2.95e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 99.88 E-value: 2.95e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIALSD--HERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIE 596
Cdd:PRK09088 8 QPQRLAAVDlaLGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 597 IITQDSKLKAIITHSEYKTSYEGYEVPILYIDQLDDFLLDEREdnlNVDCDSSQLAygIYTSGSTGIPKGVLVEHRNL-- 674
Cdd:PRK09088 88 ALLQDAEPRLLLGDDAVAAGRTDVEDLAAFIASADALEPADTP---SIPPERVSLI--LFTSGTSGQPKGVMLSERNLqq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 675 SNYIYAIQTKLGNKpkDRYLLLQSLAYDFCL-TTIYTSLLSGGTLfflLKEDAIDPAKVEEIV--QGKAIDWYKITPSHL 751
Cdd:PRK09088 163 TAHNFGVLGRVDAH--SSFLCDAPMFHIIGLiTSVRPVLAVGGSI---LVSNGFEPKRTLGRLgdPALGITHYFCVPQMA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 752 KALSSESG---TKLFPRKGLILGG----EASEWSWIKEiyrNIPASCKlfnhYGPSE--TTIGVAV--YEVTKKGLSNQF 820
Cdd:PRK09088 238 QAFRAQPGfdaAALRHLTALFTGGaphaAEDILGWLDD---GIPMVDG----FGMSEagTVFGMSVdcDVIRAKAGAAGI 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 821 STTPIGSSlsnnriyILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKILYTGEI 900
Cdd:PRK09088 311 PTPTVQTR-------VVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW------FRTGDIARRDADGFF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 901 QFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKKE--VLDKDLQTYLKQKLPPNLVP 977
Cdd:PRK09088 378 WVVDRKKDMFISGGENVYPAEIEAVLADHPGIREcAVVGMADAQWGEVGYLAIVPADGapLDLERIRSHLSTRLAKYKVP 457
|
490 500
....*....|....*....|....
gi 497785100 978 AYLVKMDTLPRHAHGKIDRKALPE 1001
Cdd:PRK09088 458 KHLRLVDALPRTASGKLQKARLRD 481
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
519-994 |
3.89e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 99.62 E-value: 3.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEII 598
Cdd:PRK08316 24 YPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAIITHSEY-----KTSYEGYEVPILYIDQL------------DDFLLDEREDNLNVDCDSSQLAYGIYTSGST 661
Cdd:PRK08316 104 LDHSGARAFLVDPALaptaeAALALLPVDTLILSLVLggreapggwldfADWAEAGSVAEPDVELADDDLAQILYTSGTE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 662 GIPKGVLVEHRNL-SNYIYAIqTKLGNKPKDRYL----LLQSLAYD-FCLTTIYtsllSGGTLFFLlkeDAIDPAKVEEI 735
Cdd:PRK08316 184 SLPKGAMLTHRALiAEYVSCI-VAGDMSADDIPLhalpLYHCAQLDvFLGPYLY----VGATNVIL---DAPDPELILRT 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 736 vqgkaIDWYKIT---------------PSHLKA-LSSesgtkLfpRKGL----ILGGEAsewswIKEIYRNIPAsCKLFN 795
Cdd:PRK08316 256 -----IEAERITsffapptvwisllrhPDFDTRdLSS-----L--RKGYygasIMPVEV-----LKELRERLPG-LRFYN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 796 HYGPSEttigVAVY-------EVTKKGLSnqfsttpIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREE 868
Cdd:PRK08316 318 CYGQTE----IAPLatvlgpeEHLRRPGS-------AGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 869 LTAERFMEDPFitdsrmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQ 947
Cdd:PRK08316 387 KTAEAFRGGWF-------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEvAVIGLPDPKWIEA 459
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 497785100 948 LVAYYVSK--KEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKI 994
Cdd:PRK08316 460 VTAVVVPKagATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1585-2039 |
4.43e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 99.59 E-value: 4.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1585 DRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIV 1664
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 TQTSLEE------KLSKSDLPYLCTDQSQDS--EDYSLLTKDKSyPEDIA------YIIYTSGTTGTPNGVM-------V 1723
Cdd:PRK08276 89 VSAALADtaaelaAELPAGVPLLLVVAGPVPgfRSYEEALAAQP-DTPIAdetagaDMLYSSGTTGRPKGIKrplpgldP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1724 KHSSVMNLISATIDeFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRdwnVTLADLPPV 1803
Cdd:PRK08276 168 DEAPGMMLALLGFG-MYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDAEEALALIERYR---VTHSQLVPT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1804 VLDSI--LPE------DIPSLQTVSTGGERCPIKVaKRWSLD---RNFYNVYGPTE---TTIATT--WYRvsSPECVqds 1867
Cdd:PRK08276 244 MFVRMlkLPEevraryDVSSLRVAIHAAAPCPVEV-KRAMIDwwgPIIHEYYASSEgggVTVITSedWLA--HPGSV--- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1868 vpiGTPVpNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFreeeilYKTGDIGKVLHDGNLEH 1947
Cdd:PRK08276 318 ---GKAV-LGEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHGW------VTVGDVGYLDEDGYLYL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1948 LGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPH-----GEWEEKKIIEELRSKLPEHMV 2022
Cdd:PRK08276 388 TDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGERVKAVVQPAdgadaGDALAAELIAWLRGRLAHYKC 467
|
490
....*....|....*..
gi 497785100 2023 PSIFVQMEELPRLNNKK 2039
Cdd:PRK08276 468 PRSIDFEDELPRTPTGK 484
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
530-999 |
6.62e-21 |
|
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: 98.86 E-value: 6.62e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 530 RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIIT 609
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 610 HSEY----------KTSYEGYEV-------PILYIDQLDDF--LLDEREDNLN-VDCDSSQlAYGI-YTSGSTGIPKGVL 668
Cdd:cd12119 104 DRDFlplleaiaprLPTVEHVVVmtddaamPEPAGVGVLAYeeLLAAESPEYDwPDFDENT-AAAIcYTSGTTGNPKGVV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 669 VEHRnlSNYIYAIQTK----LGNKPKDRYLLLQSL----AYDfcltTIYTSLLSGGTLffLLKEDAIDPAKVEEIVQGka 740
Cdd:cd12119 183 YSHR--SLVLHAMAALltdgLGLSESDVVLPVVPMfhvnAWG----LPYAAAMVGAKL--VLPGPYLDPASLAELIER-- 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 741 idwYKITPSH---------LKALSSEsGTKLFPRKGLILGGEASEWSWIKEI-YRNIPasckLFNHYGPSET-TIGVAVY 809
Cdd:cd12119 253 ---EGVTFAAgvptvwqglLDHLEAN-GRDLSSLRRVVIGGSAVPRSLIEAFeERGVR----VIHAWGMTETsPLGTVAR 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 810 ---EVTKKGLSNQFST-TPIGSSLSNNRIYILDDKLRPVPS--GIPGHIYIAGEQVARGYLNREElTAERFMEDPFItds 883
Cdd:cd12119 325 ppsEHSNLSEDEQLALrAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDE-ESEALTEDGWL--- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 884 rmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKK--EVLD 960
Cdd:cd12119 401 ---RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEaAVIGVPHPKWGERPLAVVVLKEgaTVTA 477
|
490 500 510
....*....|....*....|....*....|....*....
gi 497785100 961 KDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd12119 478 EELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
655-1001 |
6.76e-21 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 99.19 E-value: 6.76e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 655 IYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEE 734
Cdd:PRK05852 182 MFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAHTFWD 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 735 IVQGKAIDWYKITPSHLKALSSESGTKLFPRKGLIL-------------GGEASEWSWIKeiyrniPASCKlfnhYGPSE 801
Cdd:PRK05852 262 DIKAVGATWYTAVPTIHQILLERAATEPSGRKPAALrfirscsapltaeTAQALQTEFAA------PVVCA----FGMTE 331
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 802 TTIGVAVYEVTKKGLSNQ--FSTTPIGSSlSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFmedpf 879
Cdd:PRK05852 332 ATHQVTTTQIEGIGQTENpvVSTGLVGRS-TGAQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANF----- 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 880 iTDSrMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIV-TVTKVRNEEQLVAYYVSKK-- 956
Cdd:PRK05852 406 -TDG-WLRTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVfGVPDQLYGEAVAAVIVPREsa 483
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 497785100 957 EVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPE 1001
Cdd:PRK05852 484 PPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1572-2045 |
6.96e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 99.05 E-value: 6.96e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1572 VRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRR 1651
Cdd:PRK06164 20 ARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1652 DFILKDASVGAIVTQTS---------LEEKLSKSDLP----YLCTDQSQDSEDYSL-----------------LTKDKSY 1701
Cdd:PRK06164 100 AHILGRGRARWLVVWPGfkgidfaaiLAAVPPDALPPlraiAVVDDAADATPAPAPgarvqlfalpdpappaaAGERAAD 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1702 PEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVvsrEEQL 1781
Cdd:PRK06164 180 PDAGALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVC---EPVF 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1782 STKALVKRFRDWNVTLADLPPVVLDSILpedipslqtvSTGGERCPIKVAKR---------------WSLDRNF--YNVY 1844
Cdd:PRK06164 257 DAARTARALRRHRVTHTFGNDEMLRRIL----------DTAGERADFPSARLfgfasfapalgelaaLARARGVplTGLY 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1845 GPTETTIATTWYRVSSPECVQdSVPIGTPV-PNTEVFILDPDLNPV-PMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPH 1922
Cdd:PRK06164 327 GSSEVQALVALQPATDPVSVR-IEGGGRPAsPEARVRARDPQDGALlPDGESGEIEIRAPSLMRGYLDNPDATARALTDD 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1923 PFreeeilYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAivQPLG-DNQNYHTLVAYVVPH 2001
Cdd:PRK06164 406 GY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAA--QVVGaTRDGKTVPVAFVIPT 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 497785100 2002 --GEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRL---NNKKVDRHSL 2045
Cdd:PRK06164 478 dgASPDEAGLMAACREALAGFKVPARVQVVEAFPVTesaNGAKIQKHRL 526
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1587-1999 |
7.73e-21 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 99.15 E-value: 7.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1587 SYTYDEVNKRANKIANQLYK-MGIRRGDRVALYHERSSEMIFGFLGILKCGAAYV---PIDSELPLNRRdfiLKDASVGA 1662
Cdd:PLN02574 66 SISYSELQPLVKSMAAGLYHvMGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTtmnPSSSLGEIKKR---VVDCSVGL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1663 IVTQTSLEEKLSKSDLPYLCTDQSQDSED--------YSLLTKDKSY-------PEDIAYIIYTSGTTGTPNGVMVKHSs 1727
Cdd:PLN02574 143 AFTSPENVEKLSPLGVPVIGVPENYDFDSkriefpkfYELIKEDFDFvpkpvikQDDVAAIMYSSGTTGASKGVVLTHR- 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1728 vmNLIsATIDEFnitqetkvgqfatISFDASLWQ----------------------ILMALLA-GATLCVVSREEQLSTK 1784
Cdd:PLN02574 222 --NLI-AMVELF-------------VRFEASQYEypgsdnvylaalpmfhiyglslFVVGLLSlGSTIVVMRRFDASDMV 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1785 ALVKRFRdwnVT-LADLPPVVL------DSILPEDIPSLQTVSTGGERCPIKVAKRW--SLDR-NFYNVYGPTETTIATT 1854
Cdd:PLN02574 286 KVIDRFK---VThFPVVPPILMaltkkaKGVCGEVLKSLKQVSCGAAPLSGKFIQDFvqTLPHvDFIQGYGMTESTAVGT 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1855 wyRVSSPECVQDSVPIGTPVPNTEVFILDPDLNP-VPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIphpfreEEILYKT 1933
Cdd:PLN02574 363 --RGFNTEKLSKYSSVGLLAPNMQAKVVDWSTGClLPPGNCGELWIQGPGVMKGYLNNPKATQSTID------KDGWLRT 434
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 1934 GDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV 1999
Cdd:PLN02574 435 GDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVV 500
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
530-999 |
8.64e-21 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 98.60 E-value: 8.64e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 530 RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIIT 609
Cdd:PRK08008 36 RRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 610 HSEYKTSYEGYEVP-------ILYIDQLD-------DF--LLDEREDNLN--VDCDSSQLAYGIYTSGSTGIPKGVLVEH 671
Cdd:PRK08008 116 SAQFYPMYRQIQQEdatplrhICLTRVALpaddgvsSFtqLKAQQPATLCyaPPLSTDDTAEILFTSGTTSRPKGVVITH 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 672 RNL--SNYIYAIQTKLgnKPKDRYL-LLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAidpakveeivqgKAIdW----- 743
Cdd:PRK08008 196 YNLrfAGYYSAWQCAL--RDDDVYLtVMPAFHIDCQCTAAMAAFSAGATFVLLEKYSA------------RAF-Wgqvck 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 744 YKITPSHLKALSSesgtklfprKGLILGgEASEWS---WIKEI--YRNIPASCK----------LFNHYGPSETTIGVav 808
Cdd:PRK08008 261 YRATITECIPMMI---------RTLMVQ-PPSANDrqhCLREVmfYLNLSDQEKdafeerfgvrLLTSYGMTETIVGI-- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 809 yevtkkglsnqfsttpIGSSLSNNRIY-------------ILDDKLRPVPSGIPGHIYI---AGEQVARGYLNREELTAE 872
Cdd:PRK08008 329 ----------------IGDRPGDKRRWpsigrpgfcyeaeIRDDHNRPLPAGEIGEICIkgvPGKTIFKEYYLDPKATAK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 873 RFMEDPFItdsrmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYY 952
Cdd:PRK08008 393 VLEADGWL------HTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKAF 466
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 497785100 953 VSKKE---VLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK08008 467 VVLNEgetLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1569-2045 |
1.20e-20 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 98.42 E-value: 1.20e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1569 ENWVRSSPNHIALRFLDR--SYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSEL 1646
Cdd:PRK05852 23 EVAATRLPEAPALVVTADriAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPAL 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1647 PLNrrDFILKDASVGAIVTqtsLEEKLSKSD--------LPYLCTDQSQDSEDYSLL----------TKDKSYPE----D 1704
Cdd:PRK05852 103 PIA--EQRVRSQAAGARVV---LIDADGPHDraepttrwWPLTVNVGGDSGPSGGTLsvhldaatepTPATSTPEglrpD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1705 IAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTK 1784
Cdd:PRK05852 178 DAMIMFTGGTTGLPKMVPWTHANIASSVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLATLASGGAVLLPARGRFSAH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1785 ALVKRFRDWNVTLADLPPVVlDSILPEdipSLQTVSTGGERCPIKVAKRWS----------LDRNF----YNVYGPTETT 1850
Cdd:PRK05852 258 TFWDDIKAVGATWYTAVPTI-HQILLE---RAATEPSGRKPAALRFIRSCSapltaetaqaLQTEFaapvVCAFGMTEAT 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1851 IATTWYRVSSPECVQDSVPIGTPVPNT---EVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFRee 1927
Cdd:PRK05852 334 HQVTTTQIEGIGQTENPVVSTGLVGRStgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWLR-- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1928 eilykTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEK 2007
Cdd:PRK05852 412 -----TGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQLYGEAVAAVIVPRESAPPT 486
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 497785100 2008 KI--IEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK05852 487 AEelVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAV 526
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1586-1999 |
1.87e-20 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 97.74 E-value: 1.87e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1586 RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYV---PIDSELPLNRRdfiLKDASVGA 1662
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSganPTALESEIKKQ---AEAAGAKL 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1663 IVTQTSLEEKLSKSDLPYL------------------CTDQSQDSEDYSLLTKdksypEDIAYIIYTSGTTGTPNGVMVK 1724
Cdd:PLN02330 131 IVTNDTNYGKVKGLGLPVIvlgeekiegavnwkelleAADRAGDTSDNEEILQ-----TDLCALPFSSGTTGISKGVMLT 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1725 HSS-VMNLISATideFNITQETkVGQFATISFDA-----SLWQILMALLAGATLCVVSREEQLST--KALVKRfrdwNVT 1796
Cdd:PLN02330 206 HRNlVANLCSSL---FSVGPEM-IGQVVTLGLIPffhiyGITGICCATLRNKGKVVVMSRFELRTflNALITQ----EVS 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1797 LADL-PPVVL----DSILPE-DIPSLQTVSTGGERCPIKVAKRWSLDRNFYNV-----YGPTE-TTIATTWYRVSSPECV 1864
Cdd:PLN02330 278 FAPIvPPIILnlvkNPIVEEfDLSKLKLQAIMTAAAPLAPELLTAFEAKFPGVqvqeaYGLTEhSCITLTHGDPEKGHGI 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1865 QDSVPIGTPVPNTEVFILDPDLN-PVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfrEEEILYKTGDIGKVLHDG 1943
Cdd:PLN02330 358 AKKNSVGFILPNLEVKFIDPDTGrSLPKNTPGELCVRSQCVMQGYYNNKEETDRTI------DEDGWLHTGDIGYIDDDG 431
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 1944 NLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV 1999
Cdd:PLN02330 432 DIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVV 487
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1555-1999 |
2.06e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 97.78 E-value: 2.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1555 SQPRSIKDCIQYSFenwvRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILK 1634
Cdd:PRK07059 20 SQYPSLADLLEESF----RQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLR 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1635 CGAAYVPIDselPL---NRRDFILKDASVGAIVT----QTSLEEKLSKSDLPYLCTDQSQD------------------- 1688
Cdd:PRK07059 96 AGYVVVNVN---PLytpRELEHQLKDSGAEAIVVlenfATTVQQVLAKTAVKHVVVASMGDllgfkghivnfvvrrvkkm 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1689 ----------------SEDYSL-LTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSsvmNLISatidefNITQ-------- 1743
Cdd:PRK07059 173 vpawslpghvrfndalAEGARQtFKPVKLGPDDVAFLQYTGGTTGVSKGATLLHR---NIVA------NVLQmeawlqpa 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1744 ---ETKVGQFATISfDASLWQI-------LMALLAGATLCVVSREEQLstKALVKRFRDWNVTLadLPPV--VLDSIL-- 1809
Cdd:PRK07059 244 fekKPRPDQLNFVC-ALPLYHIfaltvcgLLGMRTGGRNILIPNPRDI--PGFIKELKKYQVHI--FPAVntLYNALLnn 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1810 PE----DIPSLQTVSTGGERCPIKVAKRWsldrnfYNV--------YGPTETTIATTWYRVSSPECvqdSVPIGTPVPNT 1877
Cdd:PRK07059 319 PDfdklDFSKLIVANGGGMAVQRPVAERW------LEMtgcpitegYGLSETSPVATCNPVDATEF---SGTIGLPLPST 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1878 EVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFreeeilYKTGDIGKVLHDGNLEHLGRLDHQIKV 1957
Cdd:PRK07059 390 EVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILV 463
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 497785100 1958 RGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV 1999
Cdd:PRK07059 464 SGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV 505
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1589-2045 |
3.23e-20 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 96.68 E-value: 3.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQT- 1667
Cdd:PRK13391 26 TYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAa 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1668 -----SLEEKLSKSDLPYLCTDQSQDSEDY-SLLTKDKSYPED-IA------YIIYTSGTTGTPNGVMVKHSSV-----M 1729
Cdd:PRK13391 106 kldvaRALLKQCPGVRHRLVLDGDGELEGFvGYAEAVAGLPATpIAdeslgtDMLYSSGTTGRPKGIKRPLPEQppdtpL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1730 NLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSR---EEQLstkALVKRFRdwnVTLADLPPVVLD 1806
Cdd:PRK13391 186 PLTAFLQRLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHfdaEQYL---ALIEEYG---VTHTQLVPTMFS 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1807 SI--LPE------DIPSLQTVSTGGERCPIKVAK---RWsLDRNFYNVYGPTETTIATTwyrVSSPECVQDSVPIGTPVP 1875
Cdd:PRK13391 260 RMlkLPEevrdkyDLSSLEVAIHAAAPCPPQVKEqmiDW-WGPIIHEYYAATEGLGFTA---CDSEEWLAHPGTVGRAMF 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1876 NtEVFILDPDLNPVPMGVIGEIYIGGvGVSNGYLNRDDLNEKRFIPHPfreeeILYKTGDIGKVLHDGNLEHLGRLDHQI 1955
Cdd:PRK13391 336 G-DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG-----TWSTVGDIGYVDEDGYLYLTDRAAFMI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1956 KVRGFRIELGEIESLL-----------------NLQTGVKeAIVQPL----GDNQNYHTLVAYvvphgeweekkiieeLR 2014
Cdd:PRK13391 409 ISGGVNIYPQEAENLLithpkvadaavfgvpneDLGEEVK-AVVQPVdgvdPGPALAAELIAF---------------CR 472
|
490 500 510
....*....|....*....|....*....|.
gi 497785100 2015 SKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK13391 473 QRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
530-999 |
5.64e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 96.24 E-value: 5.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 530 RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGgaYLPLDVE---SPKErIEIITQDSKLKA 606
Cdd:PRK07059 47 KAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAG--YVVVNVNplyTPRE-LEHQLKDSGAEA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 607 IITHSEYKTSYE--------------------GYE--------------VPILYIDQ---LDDFLLDEREDNLN-VDCDS 648
Cdd:PRK07059 124 IVVLENFATTVQqvlaktavkhvvvasmgdllGFKghivnfvvrrvkkmVPAWSLPGhvrFNDALAEGARQTFKpVKLGP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 649 SQLAYGIYTSGSTGIPKGVLVEHRN-LSNYIYA---IQTKLGNKPKDRYLLLQS---LAYDFCLTTIYTSLLSGGTLFFL 721
Cdd:PRK07059 204 DDVAFLQYTGGTTGVSKGATLLHRNiVANVLQMeawLQPAFEKKPRPDQLNFVCalpLYHIFALTVCGLLGMRTGGRNIL 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 722 LKEDAIDPAKVEEIVQgkaidwYKIT--PS----HLKALSSESGTKL-FPRKGLILGG-----EASEWSWIKEiyrnipA 789
Cdd:PRK07059 284 IPNPRDIPGFIKELKK------YQVHifPAvntlYNALLNNPDFDKLdFSKLIVANGGgmavqRPVAERWLEM------T 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 790 SCKLFNHYGPSETTIGVAVYEVTkkglSNQFSTTpIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREEL 869
Cdd:PRK07059 352 GCPITEGYGLSETSPVATCNPVD----ATEFSGT-IGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDE 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 870 TAERFMEDPFitdsrmYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQL 948
Cdd:PRK07059 427 TAKVMTADGF------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEvAAVGVPDEHSGEAV 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 497785100 949 VAYYVSKKEVL-DKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK07059 501 KLFVVKKDPALtEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1575-2034 |
6.53e-20 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 95.71 E-value: 6.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1575 SPNHIALRFLD-RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDF 1653
Cdd:PRK07514 15 DRDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1654 ILKDASVGAIVTQTSLEEKLSK------------------SDLPYLCTDQSQDSEDYSlltKDksyPEDIAYIIYTSGTT 1715
Cdd:PRK07514 95 FIGDAEPALVVCDPANFAWLSKiaaaagaphvetldadgtGSLLEAAAAAPDDFETVP---RG---ADDLAAILYTSGTT 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1716 GTPNGVMVKHSsvmNLIS---ATIDEFNITQETKV----------GQFATISfdaslwqilMALLAGATLcvvsreeqls 1782
Cdd:PRK07514 169 GRSKGAMLSHG---NLLSnalTLVDYWRFTPDDVLihalpifhthGLFVATN---------VALLAGASM---------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1783 tkALVKRFrDWNVTLADLP--------PVVLDSILPEdiPSLQTVSTGGER------CP--IKVAKRWS-------LDRn 1839
Cdd:PRK07514 227 --IFLPKF-DPDAVLALMPratvmmgvPTFYTRLLQE--PRLTREAAAHMRlfisgsAPllAETHREFQertghaiLER- 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1840 fynvYGPTETTIATtwyrvSSPeCVQDSVP--IGTPVPNTEVFILDPDLN-PVPMGVIGEIYIGGVGVSNGYLNRDDLNE 1916
Cdd:PRK07514 301 ----YGMTETNMNT-----SNP-YDGERRAgtVGFPLPGVSLRVTDPETGaELPPGEIGMIEVKGPNVFKGYWRMPEKTA 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1917 KRFIPHPFreeeilYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIV----QP-LGDnqny 1991
Cdd:PRK07514 371 EEFRADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVigvpHPdFGE---- 440
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 497785100 1992 hTLVAYVVPH--GEWEEKKIIEELRSKLPEHMVPSIFVQMEELPR 2034
Cdd:PRK07514 441 -GVTAVVVPKpgAALDEAAILAALKGRLARFKQPKRVFFVDELPR 484
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
528-999 |
9.14e-20 |
|
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: 96.02 E-value: 9.14e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 528 HERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAI 607
Cdd:cd05968 88 TSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKAL 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 608 ITHSeyKTSYEGYEV-----------------------------------PILYIDQL----DDFLLDEREDNLNVdcds 648
Cdd:cd05968 168 ITAD--GFTRRGREVnlkeeadkacaqcptvekvvvvrhlgndftpakgrDLSYDEEKetagDGAERTESEDPLMI---- 241
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 649 sqlaygIYTSGSTGIPKGVLVEHRNLSnyIYAIQT---KLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFflLKED 725
Cdd:cd05968 242 ------IYTSGTTGKPKGTVHVHAGFP--LKAAQDmyfQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMV--LYDG 311
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 726 AID---PAKVEEIVQGKAIDWYKITPSHLKALSSEsGTKLFPRKGL----ILGGEASEW---SWIKEIYRNIPASCKLFN 795
Cdd:cd05968 312 APDhpkADRLWRMVEDHEITHLGLSPTLIRALKPR-GDAPVNAHDLsslrVLGSTGEPWnpePWNWLFETVGKGRNPIIN 390
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 796 HYGPSETTIGVAVYEVTKKGLSNQFSTTPIGSSLSnnriyILDDKLRPVPSGIpghiyiaGEQV--------ARGYLNRE 867
Cdd:cd05968 391 YSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKAD-----VLDESGKPARPEV-------GELVllapwpgmTRGFWRDE 458
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 868 EltaeRFMEDPFITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEE 946
Cdd:cd05968 459 D----RYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLEsAAIGVPHPVKGE 534
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 947 QLVAYYVSK-----KEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05968 535 AIVCFVVLKpgvtpTEALAEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1588-2000 |
1.01e-19 |
|
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: 94.73 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1588 YTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQT 1667
Cdd:cd17640 6 ITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVEN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1668 SleeklsksdlpylctdqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSsvmNLISaTIDEFNITQETKV 1747
Cdd:cd17640 86 D---------------------------------SDDLATIIYTSGTTGNPKGVMLTHA---NLLH-QIRSLSDIVPPQP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1748 GQfATISFdASLWQILMALLAgaTLCVVSREEQLSTKalVKRFRDwnvTLADLPPVVLDSI--LPEDIPS---------- 1815
Cdd:cd17640 129 GD-RFLSI-LPIWHSYERSAE--YFIFACGCSQAYTS--IRTLKD---DLKRVKPHYIVSVprLWESLYSgiqkqvskss 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1816 ------LQTVSTGGErcpIKV------AKRWSLDRnFYNV--------YGPTETTIATTWYRVSSPecVQDSVpiGTPVP 1875
Cdd:cd17640 200 pikqflFLFFLSGGI---FKFgisgggALPPHVDT-FFEAigievlngYGLTETSPVVSARRLKCN--VRGSV--GRPLP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1876 NTEVFILDPDLN-PVPMGVIGEIYIGGVGVSNGYLNRddlnekrfiphPFREEEIL-----YKTGDIGKVLHDGNLEHLG 1949
Cdd:cd17640 272 GTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKN-----------PEATSKVLdsdgwFNTGDLGWLTCGGELVLTG 340
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 497785100 1950 RLDHQIKVR-GFRIELGEIESLLNLQTGVKEAIVqpLGDNQNyhTLVAYVVP 2000
Cdd:cd17640 341 RAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMV--VGQDQK--RLGALIVP 388
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
519-999 |
1.13e-19 |
|
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: 95.43 E-value: 1.13e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDV----ESPKER 594
Cdd:cd05906 27 GITYIDADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLTVpptyDEPNAR 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 595 IEIITQDSKL---KAIITHSEYKTSYEgyevPILYIDQLDDFLLDEREDNLN-------VDCDSSQLAYGIYTSGSTGIP 664
Cdd:cd05906 107 LRKLRHIWQLlgsPVVLTDAELVAEFA----GLETLSGLPGIRVLSIEELLDtaadhdlPQSRPDDLALLMLTSGSTGFP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 665 KGVLVEHRNLSNYIYAIQTKLGNKPKDRYL----------LLQSLAYDFCL--TTIY--TSLLSGGTLFFLlkeDAIDPA 730
Cdd:cd05906 183 KAVPLTHRNILARSAGKIQHNGLTPQDVFLnwvpldhvggLVELHLRAVYLgcQQVHvpTEEILADPLRWL---DLIDRY 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 731 KVeeivqgkAIDWykiTPSHLKALSSESGTKLFPRKG-------LILGGEAsewswikeiyrNIPASCKLFNH------- 796
Cdd:cd05906 260 RV-------TITW---APNFAFALLNDLLEEIEDGTWdlsslryLVNAGEA-----------VVAKTIRRLLRllepygl 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 797 --------YGPSETTIGVAVYEV-TKKGLSNQFSTTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNRE 867
Cdd:cd05906 319 ppdairpaFGMTETCSGVIYSRSfPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 868 ELTAERFMEDPFitdsrmYKTGDIGkILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNE-- 945
Cdd:cd05906 399 EANAEAFTEDGW------FRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAFAVRDPga 471
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497785100 946 --EQLVAYYVSKKEVLD------KDLQTYLKQKLppNLVPAYLV--KMDTLPRHAHGKIDRKAL 999
Cdd:cd05906 472 etEELAIFFVPEYDLQDalsetlRAIRSVVSREV--GVSPAYLIplPKEEIPKTSLGKIQRSKL 533
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1589-2045 |
1.62e-19 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 95.48 E-value: 1.62e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQTS 1668
Cdd:PRK06060 32 THGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1669 LEEKLSKS---DLPYLCTDQSQ-DSEDYSLLTKDKSypediAYIIYTSGTTGTPNGVMVKHSSVMNLISATI-DEFNITQ 1743
Cdd:PRK06060 112 LRDRFQPSrvaEAAELMSEAARvAPGGYEPMGGDAL-----AYATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1744 E----TKVGQFATISFDASLWqilMALLAGATLCV----VSREeqlSTKALVKRFRDwnVTLADLPPV---VLDSILPED 1812
Cdd:PRK06060 187 EdtglCSARMYFAYGLGNSVW---FPLATGGSAVInsapVTPE---AAAILSARFGP--SVLYGVPNFfarVIDSCSPDS 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1813 IPSLQTVSTGGERCPIKVAKRWSldrNFYN----VYGPTETTIATTWyrVSSpeCVQDSVP--IGTPVPNTEVFILDPDL 1886
Cdd:PRK06060 259 FRSLRCVVSAGEALELGLAERLM---EFFGgipiLDGIGSTEVGQTF--VSN--RVDEWRLgtLGRVLPPYEIRVVAPDG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1887 NPVPMGVIGEIYIGGVGVSNGYLNRddlnekrfiPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGE 1966
Cdd:PRK06060 332 TTAGPGVEGDLWVRGPAIAKGYWNR---------PDSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPRE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1967 IESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIE-----ELRSKLPEHMVPSIFVQMEELPRLNNKKVD 2041
Cdd:PRK06060 403 VERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGSVMrdlhrGLLNRLSAFKVPHRFAVVDRLPRTPNGKLV 482
|
....
gi 497785100 2042 RHSL 2045
Cdd:PRK06060 483 RGAL 486
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1555-1730 |
1.67e-19 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 95.33 E-value: 1.67e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1555 SQPRSIKDciqySFENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILK 1634
Cdd:PRK08279 34 DSKRSLGD----VFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1635 CGAAYVPIDSELplnRRDFI---LKDASVGAIVTQTSLEEKLS--KSDLP------YLCTDQSQDSEDYSLL-------- 1695
Cdd:PRK08279 110 LGAVVALLNTQQ---RGAVLahsLNLVDAKHLIVGEELVEAFEeaRADLArpprlwVAGGDTLDDPEGYEDLaaaaagap 186
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 497785100 1696 -----TKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMN 1730
Cdd:PRK08279 187 ttnpaSRSGVTAKDTAFYIYTSGTTGLPKAAVMSHMRWLK 226
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1708-2042 |
1.88e-19 |
|
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: 91.95 E-value: 1.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1708 IIYTSGTTGTPNGVMVKHSsvmNLISA---TIDEFNITQEtkvgqfatisfDASLwQIL-----MAL-LAGATLCVVSRE 1778
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHG---NLIAAnlqLIHAMGLTEA-----------DVYL-NMLplfhiAGLnLALATFHAGGAN 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1779 ---EQLSTKALVKRFRDWNVTL-ADLPPVvLDSIL------PEDIPSLQTVStgGERCPiKVAKRWSLDRN--FYNVYGP 1846
Cdd:cd17637 70 vvmEKFDPAEALELIEEEKVTLmGSFPPI-LSNLLdaaeksGVDLSSLRHVL--GLDAP-ETIQRFEETTGatFWSLYGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1847 TETTIATTWYRVSS-PECVqdsvpiGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEkrfipHPFR 1925
Cdd:cd17637 146 TETSGLVTLSPYRErPGSA------GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTA-----YTFR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1926 EEeiLYKTGDIGKVLHDGNLEHLGRLDHQ--IKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGE 2003
Cdd:cd17637 215 NG--WHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGEGIKAVCVLKPG 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 497785100 2004 WEEKKI-------IEELRSKLPEHMVpsiFVqmEELPRLNNKKVDR 2042
Cdd:cd17637 293 ATLTADeliefvgSRIARYKKPRYVV---FV--EALPKTADGSIDR 333
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
643-999 |
1.95e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 94.83 E-value: 1.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 643 NVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNL-SNYIYAIQTKLGNKPKDRYLLLQSLA----YDFCLTTIYTSLLSGGT 717
Cdd:PRK05677 201 EANPQADDVAVLQYTGGTTGVAKGAMLTHRNLvANMLQCRALMGSNLNEGCEILIAPLPlyhiYAFTFHCMAMMLIGNHN 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 718 LFFLLKEDAidPAKVEEIVQGKAIDWYKITPSHLKALSSESGTKL-FPRKGLILGGEASEWSWIKEIYRNIpASCKLFNH 796
Cdd:PRK05677 281 ILISNPRDL--PAMVKELGKWKFSGFVGLNTLFVALCNNEAFRKLdFSALKLTLSGGMALQLATAERWKEV-TGCAICEG 357
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 797 YGPSETTIGVAVYEVTkkglSNQFSTtpIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFME 876
Cdd:PRK05677 358 YGMTETSPVVSVNPSQ----AIQVGT--IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEILDS 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 877 DPFItdsrmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSK 955
Cdd:PRK05677 432 DGWL------KTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQcAAIGVPDEKSGEAIKVFVVVK 505
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 497785100 956 -KEVLDKD-LQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK05677 506 pGETLTKEqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
530-1005 |
2.77e-19 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 94.28 E-value: 2.77e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 530 RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIIT 609
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFSGANPTALESEIKKQAEAAGAKLIVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 610 HSEYKTSYEGYEVPILYIDQL--------DDFL--LDEREDNL-NVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNL-SN- 676
Cdd:PLN02330 134 NDTNYGKVKGLGLPVIVLGEEkiegavnwKELLeaADRAGDTSdNEEILQTDLCALPFSSGTTGISKGVMLTHRNLvANl 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 677 ------------------------YIYAIQ----TKLGNKPKdryLLLQSlayDFCLTTIYTSLLSGGTLFfllkeDAID 728
Cdd:PLN02330 214 csslfsvgpemigqvvtlglipffHIYGITgiccATLRNKGK---VVVMS---RFELRTFLNALITQEVSF-----APIV 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 729 PAKVEEIVQGKAIDWYKITPSHLKALSSeSGTKLFPRkgLILGGEAS-EWSWIKEIYRNIPASCKLFNHYGPSEttigva 807
Cdd:PLN02330 283 PPIILNLVKNPIVEEFDLSKLKLQAIMT-AAAPLAPE--LLTAFEAKfPGVQVQEAYGLTEHSCITLTHGDPEK------ 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 808 vyevtKKGLSNQFSttpIGSSLSNNRIYILD-DKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFItdsrmy 886
Cdd:PLN02330 354 -----GHGIAKKNS---VGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGWL------ 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 887 KTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKKEVLDK--DL 963
Cdd:PLN02330 420 HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDaAVVPLPDEEAGEIPAACVVINPKAKESeeDI 499
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 497785100 964 QTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEIQVS 1005
Cdd:PLN02330 500 LNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLS 541
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
519-999 |
3.34e-19 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 93.95 E-value: 3.34e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 519 TPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLdveSPKERIE-- 596
Cdd:PRK06178 46 RPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPV---SPLFREHel 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 597 -----------IITQDSKLKAIITHSE-------YKTSY-------------EGYEVPILYIDQLDDFLLDEREDNLNV- 644
Cdd:PRK06178 123 syelndagaevLLALDQLAPVVEQVRAetslrhvIVTSLadvlpaeptlplpDSLRAPRLAAAGAIDLLPALRACTAPVp 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 645 ----DCDSsqLAYGIYTSGSTGIPKGVLVEHRNLsnyIY------AIQTKLGNKPkdryLLLQSLAY------DFCLttI 708
Cdd:PRK06178 203 lpppALDA--LAALNYTGGTTGMPKGCEHTQRDM---VYtaaaayAVAVVGGEDS----VFLSFLPEfwiageNFGL--L 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 709 YtSLLSGGTLFFLLKEDAIDPAKveeivqgkAIDWYKIT---------------P-SHLKALSSESGTKLFprkglilgg 772
Cdd:PRK06178 272 F-PLFSGATLVLLARWDAVAFMA--------AVERYRVTrtvmlvdnavelmdhPrFAEYDLSSLRQVRVV--------- 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 773 easewSWIKEI---YRNipASCKLfnhygpSETTIGVAVYEVTKKGLSNQFST-----------TPI--GSSLSNNRIYI 836
Cdd:PRK06178 334 -----SFVKKLnpdYRQ--RWRAL------TGSVLAEAAWGMTETHTCDTFTAgfqdddfdllsQPVfvGLPVPGTEFKI 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 837 LD-DKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDpfitdsrMYKTGDIGKILYTGEIQFLGRLDGQVKIRGI 915
Cdd:PRK06178 401 CDfETGELLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDG-------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGM 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 916 RVEPEEIQSQLLSHPSI-TEAIVTVTKVRNEEQLVAYYVSKKE--VLDKDLQTYLKQKLPPNLVPAYLVkMDTLPRHAHG 992
Cdd:PRK06178 474 SVFPSEVEALLGQHPAVlGSAVVGRPDPDKGQVPVAFVQLKPGadLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATG 552
|
....*..
gi 497785100 993 KIDRKAL 999
Cdd:PRK06178 553 KVRKQDL 559
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
520-1001 |
4.07e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 93.49 E-value: 4.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQ-GIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEII 598
Cdd:PRK08314 24 PDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAIITHSEYK-----------------TSYEGYeVPILYIDQLDDFLLDERE----DNLNV----DCDSSQLAY 653
Cdd:PRK08314 104 VTDSGARVAIVGSELApkvapavgnlrlrhvivAQYSDY-LPAEPEIAVPAWLRAEPPlqalAPGGVvawkEALAAGLAP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 654 GI------------YTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLllqSLAYDFCLT----TIYTSLLSGGT 717
Cdd:PRK08314 183 PPhtagpddlavlpYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVL---AVLPLFHVTgmvhSMNAPIYAGAT 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 718 LFFLLKEDAiDPAkveeivqGKAIDWYKIT-----PSHLKALSSESGTKLFPRKGL--ILGGEASewswikeiyrnIPAS 790
Cdd:PRK08314 260 VVLMPRWDR-EAA-------ARLIERYRVThwtniPTMVVDFLASPGLAERDLSSLryIGGGGAA-----------MPEA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 791 C--KLFNH--------YGPSETT---------------IGVAVYEVtkkglsnqfsttpigsslsNNRIyILDDKLRPVP 845
Cdd:PRK08314 321 VaeRLKELtgldyvegYGLTETMaqthsnppdrpklqcLGIPTFGV-------------------DARV-IDPETLEELP 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 846 SGIPGHIYIAGEQVARGYLNREELTAERFMEdpfITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQ 925
Cdd:PRK08314 381 PGEVGEIVVHGPQVFKGYWNRPEATAEAFIE---IDGKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENL 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 926 LLSHPSITEAIVTVTK-VRNEEQLVAYYVSKKEVLDK----DLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALP 1000
Cdd:PRK08314 458 LYKHPAIQEACVIATPdPRRGETVKAVVVLRPEARGKtteeEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKILWRQLQ 537
|
.
gi 497785100 1001 E 1001
Cdd:PRK08314 538 E 538
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1586-2000 |
4.12e-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: 93.92 E-value: 4.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1586 RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAayvpIDS---------ELPLNRRDF--- 1653
Cdd:cd05967 81 RTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGA----IHSvvfggfaakELASRIDDAkpk 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1654 ILKDASVGA----IVTQTSLEEK--------------LSKSDLPYLCTDQSQDSEDYSLLTKDKSYP------EDIAYII 1709
Cdd:cd05967 157 LIVTASCGIepgkVVPYKPLLDKalelsghkphhvlvLNRPQVPADLTKPGRDLDWSELLAKAEPVDcvpvaaTDPLYIL 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1710 YTSGTTGTPNGVmVK----HSSVMNLISATIdeFNITQ------ETKVGQFATISFdaslwqILMA-LLAGATLCV---- 1774
Cdd:cd05967 237 YTSGTTGKPKGV-VRdnggHAVALNWSMRNI--YGIKPgdvwwaASDVGWVVGHSY------IVYGpLLHGATTVLyegk 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1775 ------------VSREEQLST--------KALVKRFRDWnvtladlppvvlDSILPEDIPSLQTVSTGGERCPIKVAKrW 1834
Cdd:cd05967 308 pvgtpdpgafwrVIEKYQVNAlftaptaiRAIRKEDPDG------------KYIKKYDLSSLRTLFLAGERLDPPTLE-W 374
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1835 ---SLDRNFYNVYGPTETTiattWYRVSSPECVQD-SVPIGT---PVPNTEVFILDPDLNPVPMGVIGEIYIGGvGVSNG 1907
Cdd:cd05967 375 aenTLGVPVIDHWWQTETG----WPITANPVGLEPlPIKAGSpgkPVPGYQVQVLDEDGEPVGPNELGNIVIKL-PLPPG 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1908 YLNRDDLNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGD 1987
Cdd:cd05967 450 CLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVVGVRD 529
|
490
....*....|...
gi 497785100 1988 NQNYHTLVAYVVP 2000
Cdd:cd05967 530 ELKGQVPLGLVVL 542
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
508-1002 |
4.45e-19 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 93.58 E-value: 4.45e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 508 IHVQFEGQVLNTPNSIAL------SDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGG 581
Cdd:PRK13295 26 INDDLDACVASCPDKTAVtavrlgTGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 582 AYLPLdvespkeriEIITQDSKLKAIITHSEYKT-----SYEGY-----------EVP----ILYI-----DQLDDFLLD 636
Cdd:PRK13295 106 VLNPL---------MPIFRERELSFMLKHAESKVlvvpkTFRGFdhaamarrlrpELPalrhVVVVggdgaDSFEALLIT 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 637 EREDN-------LNVDC----DSSQLaygIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDfcl 705
Cdd:PRK13295 177 PAWEQepdapaiLARLRpgpdDVTQL---IYTSGTTGEPKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAHQ--- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 706 ttiyTSLLSGGTLFFLLKEDAI-----DPAKVEEIVQGKAIDW-YKITP--SHLKALSSESGTKLFPRKGLILGGEASEW 777
Cdd:PRK13295 251 ----TGFMYGLMMPVMLGATAVlqdiwDPARAAELIRTEGVTFtMASTPflTDLTRAVKESGRPVSSLRTFLCAGAPIPG 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 778 SWIKEIYRNIPAscKLFNHYGPSETtigvAVYEVTKKGLSNQFSTTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGE 857
Cdd:PRK13295 327 ALVERARAALGA--KIVSAWGMTEN----GAVTLTKLDDPDERASTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGC 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 858 QVARGYLNREELTAerfmedpfiTDSR-MYKTGDIGKILYTGEIQFLGRlDGQVKIRG---IRVepEEIQSQLLSHPSIT 933
Cdd:PRK13295 401 SNFGGYLKRPQLNG---------TDADgWFDTGDLARIDADGYIRISGR-SKDVIIRGgenIPV--VEIEALLYRHPAIA 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497785100 934 E-AIVTVTKVRNEEQLVAYYVSKK-EVLD-KDLQTYLK-QKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:PRK13295 469 QvAIVAYPDERLGERACAFVVPRPgQSLDfEEMVEFLKaQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREM 541
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
532-996 |
4.59e-19 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341240 [Multi-domain] Cd Length: 463 Bit Score: 92.89 E-value: 4.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 532 YTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITHS 611
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVSD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 612 EyktsyegyevpilyidqlDDfllderednlnvdcdssqLAYGIYTSGSTGIPKGVLVEHRNL-SNYIYAIQTKLGnKPK 690
Cdd:cd05914 88 E------------------DD------------------VALINYTSGTTGNSKGVMLTYRNIvSNVDGVKEVVLL-GKG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 691 DRYLLLQSLAYDF-CLTTIYTSLLSGGTLFFLlkeDAIDPAKVE-------------------------EIVQGKAIDWY 744
Cdd:cd05914 131 DKILSILPLHHIYpLTFTLLLPLLNGAHVVFL---DKIPSAKIIalafaqvtptlgvpvplviekifkmDIIPKLTLKKF 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 745 KITPShlKALSSESGTKLFPRKGL-ILGGEasewswIKEIyrnIPASCKLFNHYGPSETTIGVAV---YEVTKKG----- 815
Cdd:cd05914 208 KFKLA--KKINNRKIRKLAFKKVHeAFGGN------IKEF---VIGGAKINPDVEEFLRTIGFPYtigYGMTETApiisy 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 816 -LSNQFSTTPIGSSLSNNRIYILDdklrPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKI 894
Cdd:cd05914 277 sPPNRIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW------FHTGDLGKI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 895 LYTGEIQFLGRLDGQ-VKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYY--VSKKEVLDKDLQTYLKQKL 971
Cdd:cd05914 347 DAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLVALAYIDPdfLDVKALKQRNIIDAIKWEV 426
|
490 500 510
....*....|....*....|....*....|....*
gi 497785100 972 PPNL---VPAY-------LVKMDtLPRHAHGKIDR 996
Cdd:cd05914 427 RDKVnqkVPNYkkiskvkIVKEE-FEKTPKGKIKR 460
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1702-2045 |
5.09e-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: 341241 [Multi-domain] Cd Length: 349 Bit Score: 90.80 E-value: 5.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1702 PEDIAYIIYTSGTTGTPNGVMVKHSSVMNlisatiDEFNITQETKVGQFATISFDASLWQ-------ILMALLAGATLCV 1774
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVN------NGYFIGERLGLTEQDRLCIPVPLFHcfgsvlgVLACLTHGATMVF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1775 VSRE-EQLSTKALVKRFRdwNVTLADLPPVVLDSI-LPE----DIPSLQTVSTGGERCPIKVAKRWSLDRNFYNV---YG 1845
Cdd:cd05917 75 PSPSfDPLAVLEAIEKEK--CTALHGVPTMFIAELeHPDfdkfDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVtiaYG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1846 PTETTIATTWYRV-SSPECVQDSVpiGTPVPNTEVFILDPDLNPVPM-GVIGEIYIGGVGVSNGYLNRDDLNEKRFiphp 1923
Cdd:cd05917 153 MTETSPVSTQTRTdDSIEKRVNTV--GRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAI---- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1924 frEEEILYKTGDIGKVLHDGNLEHLGRLDHQIkVRGFR-IELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV--P 2000
Cdd:cd05917 227 --DGDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGGEnIYPREIEEFLHTHPKVSDVQVVGVPDERYGEEVCAWIRlkE 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*
gi 497785100 2001 HGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05917 304 GAELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1576-2058 |
5.50e-19 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 93.15 E-value: 5.50e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLD--RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELP---LNR 1650
Cdd:PRK05857 28 PEAIALRRCDgtSALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPiaaIER 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1651 RDFILKDASV----GAIVTQTSLEEKLSKsdLPYLCTDQSQDSeDYSLLTKDKSYP--------EDIAYIIYTSGTTGTP 1718
Cdd:PRK05857 108 FCQITDPAAAlvapGSKMASSAVPEALHS--IPVIAVDIAAVT-RESEHSLDAASLagnadqgsEDPLAMIFTSGTTGEP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1719 NGVMVKHSSV-----------MNLISATIDE--FNITQETKVGqfatisfdaSLWQILMALLAGAtLCVVSREEQLStka 1785
Cdd:PRK05857 185 KAVLLANRTFfavpdilqkegLNWVTWVVGEttYSPLPATHIG---------GLWWILTCLMHGG-LCVTGGENTTS--- 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1786 LVKRFRDWNVTLADLPPVVLDSILPE------DIPSLQTVSTGGERCpIKVAKRW--SLDRNFYNVYGPTETTIATTWYR 1857
Cdd:PRK05857 252 LLEILTTNAVATTCLVPTLLSKLVSElksanaTVPSLRLVGYGGSRA-IAADVRFieATGVRTAQVYGLSETGCTALCLP 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1858 VSSPECVQ-DSVPIGTPVPNTEVFILDPD------LNPVPMGVIGEIYIGGVGVSNGYLNrddlnekrfipHPFREEEIL 1930
Cdd:PRK05857 331 TDDGSIVKiEAGAVGRPYPGVDVYLAATDgigptaPGAGPSASFGTLWIKSPANMLGYWN-----------NPERTAEVL 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1931 ----YKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDnQNYHTLVAYVVPHGEWEE 2006
Cdd:PRK05857 400 idgwVNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPD-EEFGALVGLAVVASAELD 478
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2007 KKIIEELRSKLPEH--------MVPSIFVQMEELPRLNNKKVDRHSLPTAVHIFRQQKVI 2058
Cdd:PRK05857 479 ESAARALKHTIAARfrresepmARPSTIVIVTDIPRTQSGKVMRASLAAAATADKARVVV 538
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1575-2128 |
6.90e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 94.85 E-value: 6.90e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1575 SPNHIALRFL------DRSYTYDEVNKRANKIANQLYKMGIRrGDRVALYHERSSEMIFGFLGILKCGA----AYVPIDS 1644
Cdd:PRK05691 22 TPDRLALRFLaddpgeGVVLSYRDLDLRARTIAAALQARASF-GDRAVLLFPSGPDYVAAFFGCLYAGViavpAYPPESA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1645 ELPLNRRDF-ILKDASVGAIVTQTSLE------EKLSKSDLP-YLCTDQsQDSEDYSLLTKDKSYPEDIAYIIYTSGTTG 1716
Cdd:PRK05691 101 RRHHQERLLsIIADAEPRLLLTVADLRdsllqmEELAAANAPeLLCVDT-LDPALAEAWQEPALQPDDIAFLQYTSGSTA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1717 TPNGVMVKHSsvmNLISatiDEFNITQETKVGQ------------FATISFDASLWQ--------ILMA---LLA----- 1768
Cdd:PRK05691 180 LPKGVQVSHG---NLVA---NEQLIRHGFGIDLnpddvivswlplYHDMGLIGGLLQpifsgvpcVLMSpayFLErplrw 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1769 -------GAT----------LCVvsreEQLSTKALVK-RFRDWNVTLADLPPVVLDsilpedipSLQTVSTGGERCpikv 1830
Cdd:PRK05691 254 leaiseyGGTisggpdfayrLCS----ERVSESALERlDLSRWRVAYSGSEPIRQD--------SLERFAEKFAAC---- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1831 akRWSLDrNFYNVYGPTETTIATTWYR------------------VSSPECVQDSVPIGTPVPNTEVFILDP-DLNPVPM 1891
Cdd:PRK05691 318 --GFDPD-SFFASYGLAEATLFVSGGRrgqgipaleldaealarnRAEPGTGSVLMSCGRSQPGHAVLIVDPqSLEVLGD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1892 GVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFReeeILYKTGDIGkVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLL 1971
Cdd:PRK05691 395 NRVGEIWASGPSIAHGYWRNPEASAKTFVEHDGR---TWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYPQDIEKTV 470
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1972 NLQTGV-KEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKII-----EELRSKLPE--HMVPSIFVQME--ELPRLNNKKVD 2041
Cdd:PRK05691 471 EREVEVvRKGRVAAFAVNHQGEEGIGIAAEISRSVQKILPpqaliKSIRQAVAEacQEAPSVVLLLNpgALPKTSSGKLQ 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2042 RHSLPT--------AVHIFRQQKVIQK-----PVTEEEVVVAECWAETLNlpIDNIGLNSNFFELGGHSLTATQLVARIS 2108
Cdd:PRK05691 551 RSACRLrladgsldSYALFPALQAVEAaqtaaSGDELQARIAAIWCEQLK--VEQVAADDHFFLLGGNSIAATQVVARLR 628
|
650 660
....*....|....*....|
gi 497785100 2109 ELFEIELPIKAIFEYPTIQA 2128
Cdd:PRK05691 629 DELGIDLNLRQLFEAPTLAA 648
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
657-999 |
8.43e-19 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 90.49 E-value: 8.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 657 TSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKpkDRYLL---------LQSLAydfclttiyTSLLSGGTLFFLLKEDAI 727
Cdd:PRK07824 43 TSGTTGTPKGAMLTAAALTASADATHDRLGGP--GQWLLalpahhiagLQVLV---------RSVIAGSEPVELDVSAGF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 728 DPAKVEEIVQGKAID--WYKITPSHL-KALSSESGTKLFPRKGLILGGEASEWSWIKEiyRNIPASCKLFNHYGPSETTi 804
Cdd:PRK07824 112 DPTALPRAVAELGGGrrYTSLVPMQLaKALDDPAATAALAELDAVLVGGGPAPAPVLD--AAAAAGINVVRTYGMSETS- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 805 GVAVYEvtkkglsnqfsttpiGSSLSNNRIYILDdklrpvpsgipGHIYIAGEQVARGYLNREEltaerfmEDPFiTDSR 884
Cdd:PRK07824 189 GGCVYD---------------GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPF-AEPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 885 MYKTGDIGkILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYV---SKKEVLD 960
Cdd:PRK07824 235 WFRTDDLG-ALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADcAVFGLPDDRLGQRVVAAVVgdgGPAPTLE 313
|
330 340 350
....*....|....*....|....*....|....*....
gi 497785100 961 kDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK07824 314 -ALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
520-994 |
8.72e-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: 91.98 E-value: 8.72e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIqLQPcakAIIAML----GVLKAGGAYLPLDVESPKERI 595
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAV-LAP---NTPAMYelhfGVPMAGAVLNALNTRLDAEEI 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 596 EIITQDSKLKAIITHSEYktsyegyevpiLYIDQL----DDFLLDEREDnlnvDCDSSQLAygiYTSGSTGIPKGVLVEH 671
Cdd:cd12118 94 AFILRHSEAKVLFVDREF-----------EYEDLLaegdPDFEWIPPAD----EWDPIALN---YTSGTTGRPKGVVYHH 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 672 RnlSNYIYAIQTKLGNKPKDRYLLLQSLAYDFC--LTTIYTSLLSGGTLFFLLKEDAidpakvEEIVqgKAIDWYKIT-- 747
Cdd:cd12118 156 R--GAYLNALANILEWEMKQHPVYLWTLPMFHCngWCFPWTVAAVGGTNVCLRKVDA------KAIY--DLIEKHKVThf 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 748 ---PSHLKAL--SSESGTKLFPRK-GLILGGEASEWSWIKEIYrniPASCKLFNHYGPSETTIGVAVYEvtkkgLSNQFS 821
Cdd:cd12118 226 cgaPTVLNMLanAPPSDARPLPHRvHVMTAGAPPPAAVLAKME---ELGFDVTHVYGLTETYGPATVCA-----WKPEWD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 822 TTPIG-----------SSLSNNRIYILD-DKLRPVP---SGIpGHIYIAGEQVARGYLNREELTAERFmEDPFitdsrmY 886
Cdd:cd12118 298 ELPTEerarlkarqgvRYVGLEEVDVLDpETMKPVPrdgKTI-GEIVFRGNIVMKGYLKNPEATAEAF-RGGW------F 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 887 KTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEA-IVTVTKVRNEEQLVAYYVSK--KEVLDKDL 963
Cdd:cd12118 370 HSGDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAaVVARPDEKWGEVPCAFVELKegAKVTEEEI 449
|
490 500 510
....*....|....*....|....*....|.
gi 497785100 964 QTYLKQKLPPNLVPAYLVKMDtLPRHAHGKI 994
Cdd:cd12118 450 IAFCREHLAGFMVPKTVVFGE-LPKTSTGKI 479
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1702-1971 |
1.31e-18 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 91.80 E-value: 1.31e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1702 PEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATiSFDASLWQ--ILMALLAGatLCVVSREE 1779
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSPKEDDVMMSFLP-PFHAYGFNscTLFPLLSG--VPVVFAYN 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1780 QLSTKALVKRFRDWNVTLADLPPVVLDSILP------EDIPSLQTVSTGGErcPIKVAKRWSLDRNF-----YNVYGPTE 1848
Cdd:PRK06334 259 PLYPKKIVEMIDEAKVTFLGSTPVFFDYILKtakkqeSCLPSLRFVVIGGD--AFKDSLYQEALKTFphiqlRQGYGTTE 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1849 TTIATTWYRVSSPecvQDSVPIGTPVPNTEVFILDPDLN-PVPMGVIGEIYIGGVGVSNGYLNRDDlnekrfiPHPFRE- 1926
Cdd:PRK06334 337 CSPVITINTVNSP---KHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEDF-------GQGFVEl 406
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 497785100 1927 -EEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLL 1971
Cdd:PRK06334 407 gGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1571-1987 |
1.39e-18 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 91.09 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1571 WVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPlnr 1650
Cdd:PRK09029 12 WAQVRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLP--- 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1651 rdfilkDASVGAIVTQTSLEEKLSKSDLPYLCTDQSQDSEDYSLLTKDKSYPEDIAYIIYTSGTTGTPNGVMvkHSSVMN 1730
Cdd:PRK09029 89 ------QPLLEELLPSLTLDFALVLEGENTFSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAV--HTAQAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1731 LISAtidefnitqetkVGQFATISFDA------SL-------------WqilmaLLAGATLCVvsREEQLSTKALVKrfr 1791
Cdd:PRK09029 161 LASA------------EGVLSLMPFTAqdswllSLplfhvsgqgivwrW-----LYAGATLVV--RDKQPLEQALAG--- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1792 dwnVTLADLPPVVLDSILPEDIPSLQT--VSTGGERCPIKVAKR--------WSldrnfynVYGPTETtiATTwyrVssp 1861
Cdd:PRK09029 219 ---CTHASLVPTQLWRLLDNRSEPLSLkaVLLGGAAIPVELTEQaeqqgircWC-------GYGLTEM--AST---V--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1862 eCVQ--DSVP-IGTPVPNTEVFILDpdlnpvpmgviGEIYIGGVGVSNGYLnRDDLnekrfiPHPFREEEILYKTGDIGk 1938
Cdd:PRK09029 281 -CAKraDGLAgVGSPLPGREVKLVD-----------GEIWLRGASLALGYW-RQGQ------LVPLVNDEGWFATRDRG- 340
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 497785100 1939 VLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGD 1987
Cdd:PRK09029 341 EWQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVAD 389
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1573-2045 |
1.56e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 91.41 E-value: 1.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1573 RSSPNHIALRFL--DRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNR 1650
Cdd:PRK09088 6 RLQPQRLAAVDLalGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1651 RDFILKDASVGAIVTQTSLEE-KLSKSDLPYLCtdQSQDSEDysLLTKDKSYPEDIAYIIYTSGTTGTPNGVMVkhsSVM 1729
Cdd:PRK09088 86 LDALLQDAEPRLLLGDDAVAAgRTDVEDLAAFI--ASADALE--PADTPSIPPERVSLILFTSGTSGQPKGVML---SER 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1730 NLISATIDeFNITqeTKVGQFATISFDASLWQIL-------MALLAGATLCVvsrEEQLSTKALVKRFRD--WNVTLADL 1800
Cdd:PRK09088 159 NLQQTAHN-FGVL--GRVDAHSSFLCDAPMFHIIglitsvrPVLAVGGSILV---SNGFEPKRTLGRLGDpaLGITHYFC 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1801 PPVVLDSIL------PEDIPSLQTVSTGGERCPIKVAKRWsLDRNFYNV--YGPTEttiATTWYRVSSPECVQDSV--PI 1870
Cdd:PRK09088 233 VPQMAQAFRaqpgfdAAALRHLTALFTGGAPHAAEDILGW-LDDGIPMVdgFGMSE---AGTVFGMSVDCDVIRAKagAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1871 GTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfrEEEILYKTGDIGKVLHDGNLEHLGR 1950
Cdd:PRK09088 309 GIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWFRTGDIARRDADGFFWVVDR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1951 LDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQ--NYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQ 2028
Cdd:PRK09088 383 KKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQwgEVGYLAIVPADGAPLDLERIRSHLSTRLAKYKVPKHLRL 462
|
490
....*....|....*..
gi 497785100 2029 MEELPRLNNKKVDRHSL 2045
Cdd:PRK09088 463 VDALPRTASGKLQKARL 479
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1588-1982 |
1.57e-18 |
|
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: 91.76 E-value: 1.57e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1588 YTYDEVNKRANKIANQLYKM-GIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELplNRRDFI--LKDASVGAIV 1664
Cdd:cd05928 42 WSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQL--TAKDILyrLQASKAKCIV 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 TQTSLEEKLSK--SDLPYLCT-----DQSQD------------SEDYSLLtkdKSYPEDIAYIIYTSGTTGTPNgvMVKH 1725
Cdd:cd05928 120 TSDELAPEVDSvaSECPSLKTkllvsEKSRDgwlnfkellneaSTEHHCV---ETGSQEPMAIYFTSGTTGSPK--MAEH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1726 SSVMNLISATIDEFNITQETKVGQFATIS----FDASLWQILMALLAGAtlCV-VSREEQLSTKALVKRFRDWNVTLADL 1800
Cdd:cd05928 195 SHSSLGLGLKVNGRYWLDLTASDIMWNTSdtgwIKSAWSSLFEPWIQGA--CVfVHHLPRFDPLVILKTLSSYPITTFCG 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1801 PPVVLDSILPEDI-----PSLQTVSTGGERCPIKVAKRW----SLDrnFYNVYGPTETTI--ATTWYRVSSPECvqdsvp 1869
Cdd:cd05928 273 APTVYRMLVQQDLssykfPSLQHCVTGGEPLNPEVLEKWkaqtGLD--IYEGYGQTETGLicANFKGMKIKPGS------ 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1870 IGTPVPNTEVFILDPDLNPVPMGVIGEIYI-----GGVGVSNGYLNrddlnekrfipHPFREEEIL----YKTGDIGKVL 1940
Cdd:cd05928 345 MGKASPPYDVQIIDDNGNVLPPGTEGDIGIrvkpiRPFGLFSGYVD-----------NPEKTAATIrgdfYLTGDRGIMD 413
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 497785100 1941 HDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIV 1982
Cdd:cd05928 414 EDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAV 455
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1575-2042 |
2.69e-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: 90.51 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1575 SPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPlnRRDF- 1653
Cdd:cd05929 5 DLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAP--RAEAc 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1654 ----ILKDASV-------GAIVTQTSLEEKLSKSDLPylctdqsqdsedyslLTKDKSYPEDIayiIYTSGTTGTPNGVM 1722
Cdd:cd05929 83 aiieIKAAALVcglftggGALDGLEDYEAAEGGSPET---------------PIEDEAAGWKM---LYSGGTTGRPKGIK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1723 VKHSSVMNLIS-----ATIDEFNITQETKVGqfATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRdwnVTL 1797
Cdd:cd05929 145 RGLPGGPPDNDtlmaaALGFGPGADSVYLSP--APLYHAAPFRWSMTALFMGGTLVLMEKFDPEEFLRLIERYR---VTF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1798 ADLPPVVLDSILP--------EDIPSLQTVSTGGERCPIKVAKRWS--LDRNFYNVYGPTETtIATTWyrVSSPECVQDS 1867
Cdd:cd05929 220 AQFVPTMFVRLLKlpeavrnaYDLSSLKRVIHAAAPCPPWVKEQWIdwGGPIIWEYYGGTEG-QGLTI--INGEEWLTHP 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1868 VPIGTPVpNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNgYLNRDDLNEKRFIPHPFReeeilyKTGDIGKVLHDGNLEH 1947
Cdd:cd05929 297 GSVGRAV-LGKVHILDEDGNEVPPGEIGEVYFANGPGFE-YTNDPEKTAAARNEGGWS------TLGDVGYLDEDGYLYL 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1948 LGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPH-----GEWEEKKIIEELRSKLPEHMV 2022
Cdd:cd05929 369 TDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQRVHAVVQPApgadaGTALAEELIAFLRDRLSRYKC 448
|
490 500
....*....|....*....|
gi 497785100 2023 PSIFVQMEELPRLNNKKVDR 2042
Cdd:cd05929 449 PRSIEFVAELPRDDTGKLYR 468
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
655-994 |
3.05e-18 |
|
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: 88.33 E-value: 3.05e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 655 IYTSGSTGIPKGVLVEHRNlSNYIYAIQTKLGN-KPKDRYLLLQSLAYDFCLTT-IYTSLLSGGTLfflLKEDAIDPAKV 732
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQ-TLRAAAAWADCADlTEDDRYLIINPFFHTFGYKAgIVACLLTGATV---VPVAVFDVDAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 733 EEIVQGKAIDWYKITPSHLKALSSESGTKLFPRKGL---ILGGEASEWSWIKEIYRNIPASCKLfNHYGPSETTIGVavy 809
Cdd:cd17638 82 LEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLraaVTGAATVPVELVRRMRSELGFETVL-TAYGLTEAGVAT--- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 810 eVTKKGLSNQFSTTPIGSSLSNNRIYILDDklrpvpsgipGHIYIAGEQVARGYLNREELTAERFMEDPFItdsrmyKTG 889
Cdd:cd17638 158 -MCRPGDDAETVATTCGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGWL------HTG 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 890 DIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKKEV-LDK-DLQTY 966
Cdd:cd17638 221 DVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQvAVIGVPDERMGEVGKAFVVARPGVtLTEeDVIAW 300
|
330 340
....*....|....*....|....*...
gi 497785100 967 LKQKLPPNLVPAYLVKMDTLPRHAHGKI 994
Cdd:cd17638 301 CRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
655-1002 |
3.49e-18 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 90.67 E-value: 3.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 655 IYTSGSTGIPKGVLVEHRNL------------SNYIYAIQTKLgnkpkdrYLLLQSLAYDFCLTTIYTSLLS-GGTLFFL 721
Cdd:PLN02574 204 MYSSGTTGASKGVVLTHRNLiamvelfvrfeaSQYEYPGSDNV-------YLAALPMFHIYGLSLFVVGLLSlGSTIVVM 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 722 LKEDAidpakvEEIVqgKAIDWYKIT-----PSHLKALS-SESGTKLFPRKGLIL---GGEASEWSWIKEIYRNIPaSCK 792
Cdd:PLN02574 277 RRFDA------SDMV--KVIDRFKVThfpvvPPILMALTkKAKGVCGEVLKSLKQvscGAAPLSGKFIQDFVQTLP-HVD 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 793 LFNHYGPSETTiGVAVYEVTKKGLSNQFSttpIGSSLSNNRIYILD-DKLRPVPSGIPGHIYIAGEQVARGYLNREELTA 871
Cdd:PLN02574 348 FIQGYGMTEST-AVGTRGFNTEKLSKYSS---VGLLAPNMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 872 ERFMEDPFItdsrmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAivTVTKVRNEEQ---L 948
Cdd:PLN02574 424 STIDKDGWL------RTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDA--AVTAVPDKECgeiP 495
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 949 VAYYVSKKE--VLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:PLN02574 496 VAFVVRRQGstLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRRELKRS 551
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1589-1978 |
3.53e-18 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 89.83 E-value: 3.53e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQTs 1668
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQEAEPDAFIGIP- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1669 leeklsKSDLPylctdqsqdsedyslltkdksypediAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKvg 1748
Cdd:cd05910 83 ------KADEP--------------------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV-- 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1749 QFATISFDAsLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLPPVVLDSI----LPEDI--PSLQTVSTG 1822
Cdd:cd05910 129 DLATFPLFA-LFGPALGLTSVIPDMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVarycAQHGItlPSLRRVLSA 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1823 GERCPIKVAKRW----SLDRNFYNVYGPTE----TTIATTWYRVSSPECVQD--SVPIGTPVPNTEVFILDPDLNP---- 1888
Cdd:cd05910 208 GAPVPIALAARLrkmlSDEAEILTPYGATEalpvSSIGSRELLATTTAATSGgaGTCVGRPIPGVRVRIIEIDDEPiaew 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1889 -----VPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPfrEEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIE 1963
Cdd:cd05910 288 ddtleLPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDN--SEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLY 365
|
410
....*....|....*
gi 497785100 1964 LGEIESLLNLQTGVK 1978
Cdd:cd05910 366 TEPVERVFNTHPGVR 380
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
565-999 |
3.89e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 90.05 E-value: 3.89e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 565 PCAKAIIAMLGVLKAGGAYLPLDVES-PKERIEIITqDSKLKAIIThseyKTSYEGYEVPILYIDqlddflLDEREDNLN 643
Cdd:PRK07787 54 PTLATVLAVVGALIAGVPVVPVPPDSgVAERRHILA-DSGAQAWLG----PAPDDPAGLPHVPVR------LHARSWHRY 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 644 VDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDryLLLQSL----AYDFCLTTIyTSLLSGGTLF 719
Cdd:PRK07787 123 PEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWTADD--VLVHGLplfhVHGLVLGVL-GPLRIGNRFV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 720 FLLKedaIDPAKVEEIVQGKA-------IDWYKIT--PSHLKALSSESgtklfprkgLILGGEASewswikeiyrnIPAS 790
Cdd:PRK07787 200 HTGR---PTPEAYAQALSEGGtlyfgvpTVWSRIAadPEAARALRGAR---------LLVSGSAA-----------LPVP 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 791 -----CKLFNH-----YGPSETTIGVAVY---EvTKKGLsnqfsttpIGSSLSNNRIYILDDKLRPVPSGIP--GHIYIA 855
Cdd:PRK07787 257 vfdrlAALTGHrpverYGMTETLITLSTRadgE-RRPGW--------VGLPLAGVETRLVDEDGGPVPHDGEtvGELQVR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 856 GEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKILYTGEIQFLGR--LDgQVKIRGIRVEPEEIQSQLLSHPSIT 933
Cdd:PRK07787 328 GPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGResTD-LIKSGGYRIGAGEIETALLGHPGVR 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497785100 934 EAivTVTKVRNE---EQLVAYYVSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK07787 401 EA--AVVGVPDDdlgQRIVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1588-1999 |
4.40e-18 |
|
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: 90.28 E-value: 4.40e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1588 YTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPID---SELPLNRRDFILKDASVgaIV 1664
Cdd:cd17642 45 YSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNdiyNERELDHSLNISKPTIV--FC 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 TQTSLEEKLS-KSDLPYLCT----DQSQDSEDYSLLTKDKSYP------------------EDIAYIIYTSGTTGTPNGV 1721
Cdd:cd17642 123 SKKGLQKVLNvQKKLKIIKTiiilDSKEDYKGYQCLYTFITQNlppgfneydfkppsfdrdEQVALIMNSSGSTGLPKGV 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1722 MVKHSSVMNLISATIDEFNITQ---ETKV----------GQFATISFdaslwqilmaLLAGATLCVVSR-EEQLSTKALv 1787
Cdd:cd17642 203 QLTHKNIVARFSHARDPIFGNQiipDTAIltvipfhhgfGMFTTLGY----------LICGFRVVLMYKfEEELFLRSL- 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1788 krfRDWNVTLADLPPVVLdSILPE-------DIPSLQTVSTGGerCPI------KVAKRWSLdrNFYNV-YGPTETTIAT 1853
Cdd:cd17642 272 ---QDYKVQSALLVPTLF-AFFAKstlvdkyDLSNLHEIASGG--APLskevgeAVAKRFKL--PGIRQgYGLTETTSAI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1854 twyrVSSPEcvQDSVP--IGTPVPNTEVFILDPDLNPVpMGV--IGEIYIGGVGVSNGYLNRDDLNEKRFIphpfreEEI 1929
Cdd:cd17642 344 ----LITPE--GDDKPgaVGKVVPFFYAKVVDLDTGKT-LGPneRGELCVKGPMIMKGYVNNPEATKALID------KDG 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1930 LYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV 1999
Cdd:cd17642 411 WLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVV 480
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1702-2045 |
4.70e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 90.21 E-value: 4.70e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1702 PEDIAYIIYTSGTTGTPNGVMVKHSS-VMN------LISATIDEfniTQETKVGQFATISFDASLWQILMALLAGATLCV 1774
Cdd:PRK05677 206 ADDVAVLQYTGGTTGVAKGAMLTHRNlVANmlqcraLMGSNLNE---GCEILIAPLPLYHIYAFTFHCMAMMLIGNHNIL 282
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1775 VSREEQLStkALVKRFRDWN----VTLADLPpVVL---DSILPEDIPSLQTVSTGGERCPIKVAKRWSLDRN--FYNVYG 1845
Cdd:PRK05677 283 ISNPRDLP--AMVKELGKWKfsgfVGLNTLF-VALcnnEAFRKLDFSALKLTLSGGMALQLATAERWKEVTGcaICEGYG 359
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1846 PTETTIATTwyrVSSPECVQDSVpIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfr 1925
Cdd:PRK05677 360 MTETSPVVS---VNPSQAIQVGT-IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEIL------ 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1926 EEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV--PHGE 2003
Cdd:PRK05677 430 DSDGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVFVVvkPGET 509
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 497785100 2004 WEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK05677 510 LTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1576-2047 |
6.49e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 89.67 E-value: 6.49e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQTSLEEKLSKSDLPYLCTDQSQDSEDYSLLTKDKSYPEDIayIIYTSGTTGTPNGVmVKHSSVMNLISAT 1735
Cdd:PRK13383 129 RAHHISTVVADNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPGRI--VLLTSGTTGKPKGV-PRAPQLRSAVGVW 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1736 IDEFNITQeTKVGQFATISfdaslwqilMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLADLP----------PVVL 1805
Cdd:PRK13383 206 VTILDRTR-LRTGSRISVA---------MPMFHGLGLGMLMLTIALGGTVLTHRHFDAEAALAQASlhradaftavPVVL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1806 DSIL--PEDI------PSLQTVSTGGERCPIKVAKRW--SLDRNFYNVYGPTETTIATtwyrVSSPECVQDSV-PIGTPV 1874
Cdd:PRK13383 276 ARILelPPRVrarnplPQLRVVMSSGDRLDPTLGQRFmdTYGDILYNGYGSTEVGIGA----LATPADLRDAPeTVGKPV 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1875 PNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYlnrDDLNEKRFIphpfreeEILYKTGDIGKVLHDGNLEHLGRLDHQ 1954
Cdd:PRK13383 352 AGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRY---TDGGGKAVV-------DGMTSTGDMGYLDNAGRLFIVGREDDM 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1955 IKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV--PHGEWEEKKIIEELRSKLPEHMVPSIFVQMEEL 2032
Cdd:PRK13383 422 IISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVlhPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSI 501
|
490
....*....|....*
gi 497785100 2033 PRLNNKKVDRHSLPT 2047
Cdd:PRK13383 502 PRNPTGKVLRKELPG 516
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1573-1953 |
8.67e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 89.57 E-value: 8.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1573 RSSPNHIALRFLDRSY----------TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPI 1642
Cdd:PRK09274 17 QERPDQLAVAVPGGRGadgklaydelSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1643 D--------------SEL------P---LNRRDFILKDASVGAIVT--------QTSLEEKLSKSDL-PYLCTDqsqdse 1690
Cdd:PRK09274 97 DpgmgiknlkqclaeAQPdafigiPkahLARRLFGWGKPSVRRLVTvggrllwgGTTLATLLRDGAAaPFPMAD------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1691 dyslltkdkSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQetkvGQFATISFDaslwqiLMALLA-- 1768
Cdd:PRK09274 171 ---------LAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEP----GEIDLPTFP------LFALFGpa 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1769 -GATlCVV-----SREEQLSTKALVKRFRDWNVTLADLPPVVLDSIL------PEDIPSLQTVSTGGERCPIKVAKRWSL 1836
Cdd:PRK09274 232 lGMT-SVIpdmdpTRPATVDPAKLFAAIERYGVTNLFGSPALLERLGrygeanGIKLPSLRRVISAGAPVPIAVIERFRA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1837 ----DRNFYNVYGPTE----TTIA------TTWYRVSSPE--CVqdsvpiGTPVPNTEVFILDPDLNP---------VPM 1891
Cdd:PRK09274 311 mlppDAEILTPYGATEalpiSSIEsreilfATRAATDNGAgiCV------GRPVDGVEVRIIAISDAPipewddalrLAT 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497785100 1892 GVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPfrEEEILYKTGDIGKVLHDGNLEHLGRLDH 1953
Cdd:PRK09274 385 GEIGEIVVAGPMVTRSYYNRPEATRLAKIPDG--QGDVWHRMGDLGYLDAQGRLWFCGRKAH 444
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1708-1982 |
9.30e-18 |
|
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: 86.97 E-value: 9.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1708 IIYTSGTTGTPNGVMVKHSSVM--NLISATIDefNITQETkvgqfatiSFDAS--LWQI--LMALLA----GATLCVVSR 1777
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLaqALVLAVLQ--AIDEGT--------VFLNSgpLFHIgtLMFTLAtfhaGGTNVFVRR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1778 EEQLSTKALVKRFRdwnVTLADLPPVVLDSIL------PEDIPSLQTVSTGGERCPIKVAKRWSLDRNFYNvYGPTETTI 1851
Cdd:cd17636 75 VDAEEVLELIEAER---CTHAFLLPPTIDQIVelnadgLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPGG-YGQTEVMG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1852 ATTWYRVSspecVQDSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfreEEILY 1931
Cdd:cd17636 151 LATFAALG----GGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRT-------RGGWH 219
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 497785100 1932 KTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIV 1982
Cdd:cd17636 220 HTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAV 270
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
656-1001 |
1.46e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 88.90 E-value: 1.46e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 656 YTSGSTGIPKGVLVEHRNL-SNyiyAIQTK-----LGNKPkDRYLLLQSLAYDFCLTTIYT-SLLSGGTLFFLlkeDAID 728
Cdd:PRK05605 226 YTSGTTGKPKGAQLTHRNLfAN---AAQGKawvpgLGDGP-ERVLAALPMFHAYGLTLCLTlAVSIGGELVLL---PAPD 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 729 PAKVEEIVQGKAIDWYKITP---SHLKALSSESGTKLFPRKGLILGgeASewswikeiyrNIPASC----------KLFN 795
Cdd:PRK05605 299 IDLILDAMKKHPPTWLPGVPplyEKIAEAAEERGVDLSGVRNAFSG--AM----------ALPVSTvelwekltggLLVE 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 796 HYGPSET----------------TIGVAvyevtkkglsnqFSTTPIgsslsnnRIYILDDKLRPVPSGIPGHIYIAGEQV 859
Cdd:PRK05605 367 GYGLTETspiivgnpmsddrrpgYVGVP------------FPDTEV-------RIVDPEDPDETMPDGEEGELLVRGPQV 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 860 ARGYLNREELTAERFMEDpfitdsrMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEA-IVT 938
Cdd:PRK05605 428 FKGYWNRPEETAKSFLDG-------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAaVVG 500
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 939 VTKVRNEEQLVAYYVSKK-EVLDKD-LQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPE 1001
Cdd:PRK05605 501 LPREDGSEEVVAAVVLEPgAALDPEgLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRREVRE 565
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
512-999 |
1.54e-17 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 88.57 E-value: 1.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQ-GIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYL---PLd 587
Cdd:PRK08974 29 FEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVnvnPL- 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 588 vESPKErIEIITQDSKLKAIITHSEYKTSYEG--YEVPILYI------DQLD-------DFLLD---------------- 636
Cdd:PRK08974 108 -YTPRE-LEHQLNDSGAKAIVIVSNFAHTLEKvvFKTPVKHViltrmgDQLStakgtlvNFVVKyikrlvpkyhlpdais 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 637 --------EREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRN-LSNYIYA--IQTKLGNKPKDRYLLLQSLAYDFCL 705
Cdd:PRK08974 186 frsalhkgRRMQYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQAkaAYGPLLHPGKELVVTALPLYHIFAL 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 706 TTiyTSLL---SGGTLFFLLKEDAIdPAKVEEIVQgkaidwYKITP-----SHLKAL-SSESGTKL-FPRKGLILGGEAS 775
Cdd:PRK08974 266 TV--NCLLfieLGGQNLLITNPRDI-PGFVKELKK------YPFTAitgvnTLFNALlNNEEFQELdFSSLKLSVGGGMA 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 776 EWSWIKEIYRNIpASCKLFNHYGPSETTIGVAVYEVTKKGLSNQfsttpIGSSLSNNRIYILDDKLRPVPSGIPGHIYIA 855
Cdd:PRK08974 337 VQQAVAERWVKL-TGQYLLEGYGLTECSPLVSVNPYDLDYYSGS-----IGLPVPSTEIKLVDDDGNEVPPGEPGELWVK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 856 GEQVARGYLNREELTAErfmedpFITDSRMyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEa 935
Cdd:PRK08974 411 GPQVMLGYWQRPEATDE------VIKDGWL-ATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLE- 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 936 iVTVTKVRNE---EQLVAYYVSKKEVLDKD-LQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK08974 483 -VAAVGVPSEvsgEAVKIFVVKKDPSLTEEeLITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
520-1002 |
2.25e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 88.06 E-value: 2.25e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:PRK07788 63 PDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVA 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIITHSEY-------KTSYEGYEVPILYIDQ----------LDDFLldEREDNLNVDCDSSQLAYGIYTSGSTG 662
Cdd:PRK07788 143 AREGVKALVYDDEFtdllsalPPDLGRLRAWGGNPDDdepsgstdetLDDLI--AGSSTAPLPKPPKPGGIVILTSGTTG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 663 IPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKedaIDPAKVEEivqgkAID 742
Cdd:PRK07788 221 TPKGAPRPEPSPLAPLAGLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLRRR---FDPEATLE-----DIA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 743 WYKIT-----PSHLKA-------------LSS-----ESGTKLFPRkgLILGGEASewswIKEIyrnipasckLFNHYGP 799
Cdd:PRK07788 293 KHKATalvvvPVMLSRildlgpevlakydTSSlkiifVSGSALSPE--LATRALEA----FGPV---------LYNLYGS 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 800 SEttigVAVYEV-TKKGLSNQFSTT---PIGSslsnnRIYILDDKLRPVPSGIPGHIYIAGEQVARGYlnreelTAERfm 875
Cdd:PRK07788 358 TE----VAFATIaTPEDLAEAPGTVgrpPKGV-----TVKILDENGNEVPRGVVGRIFVGNGFPFEGY------TDGR-- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 876 eDPFITDSRMyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAivTVTKVRNEE---QLVAYY 952
Cdd:PRK07788 421 -DKQIIDGLL-SSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEA--AVIGVDDEEfgqRLRAFV 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 497785100 953 VSKK-EVLDKD-LQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:PRK07788 497 VKAPgAALDEDaIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
520-1001 |
2.30e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 87.79 E-value: 2.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:PRK07470 21 PDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIITHSEYK---------TSYEGYEVPI------LYIDQLDDFLLDEREDNLNVDCDssQLAYGIYTSGSTGIP 664
Cdd:PRK07470 101 EASGARAMICHADFPehaaavraaSPDLTHVVAIggaragLDYEALVARHLGARVANAAVDHD--DPCWFFFTSGTTGRP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 665 KGVLVEHRNLSnyiYAIQTKL-----GNKPKDRYLLLQSLAYDfclTTIYTSL-LSGGTLFFLLKEDAIDPAKVEEIVQG 738
Cdd:PRK07470 179 KAAVLTHGQMA---FVITNHLadlmpGTTEQDASLVVAPLSHG---AGIHQLCqVARGAATVLLPSERFDPAEVWALVER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 739 kaidwYKIT-----PSHLKALSSESGTKLFPRKGL---ILGGEAsewswikeIYRnipASCK---------LFNHYGPSE 801
Cdd:PRK07470 253 -----HRVTnlftvPTILKMLVEHPAVDRYDHSSLryvIYAGAP--------MYR---ADQKralaklgkvLVQYFGLGE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 802 TT--------------------IGVAVYEVTkkGLSNQfsttpigsslsnnriyILDDKLRPVPSGIPGHIYIAGEQVAR 861
Cdd:PRK07470 317 VTgnitvlppalhdaedgpdarIGTCGFERT--GMEVQ----------------IQDDEGRELPPGETGEICVIGPAVFA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 862 GYLNREELTAERFMEDPFitdsrmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVT 940
Cdd:PRK07470 379 GYYNNPEANAKAFRDGWF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEvAVLGVP 451
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497785100 941 KVRNEEQLVAYYVSKK--EVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPE 1001
Cdd:PRK07470 452 DPVWGEVGVAVCVARDgaPVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1589-2040 |
2.42e-17 |
|
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: 87.66 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGaayVPIdselplnrrdfilkdASVGAIVTQTS 1668
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPI---------------VTVYATLGEDA 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1669 LEEKLSKSDLPYLCTDQSqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMVKHSSV---MNLISATIDEFNITQET 1745
Cdd:cd17639 69 LIHSLNETECSAIFTDGK---------------PDDLACIMYTSGSTGNPKGVMLTHGNLvagIAGLGDRVPELLGPDDR 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1746 KVG--QFATI-SFDASLwqilMALLAGATLCVvSREEQLSTKALVKRFRDWNV---TLADLPPVVLDSI-------LPED 1812
Cdd:cd17639 134 YLAylPLAHIfELAAEN----VCLYRGGTIGY-GSPRTLTDKSKRGCKGDLTEfkpTLMVGVPAIWDTIrkgvlakLNPM 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1813 IPSLQTV-STGGERcpiKVAK-RWSLD----------------------------------RNFYNV--------YGPTE 1848
Cdd:cd17639 209 GGLKRTLfWTAYQS---KLKAlKEGPGtplldelvfkkvraalggrlrymlsggaplsadtQEFLNIvlcpviqgYGLTE 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1849 TTIATTwyrVSSPECVQDSVpIGTPVPNTEVFILD-PDL-----NPVPMGvigEIYIGGVGVSNGYLNRDDLNEKRFIPH 1922
Cdd:cd17639 286 TCAGGT---VQDPGDLETGR-VGPPLPCCEIKLVDwEEGgystdKPPPRG---EILIRGPNVFKGYYKNPEKTKEAFDGD 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1923 PFreeeilYKTGDIGKVLHDGNLEHLGRLDHQIKVR-GFRIELGEIESLLNLQTGVKEAIVqpLGD-NQNYhtLVAYVVP 2000
Cdd:cd17639 359 GW------FHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICV--YADpDKSY--PVAIVVP 428
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 497785100 2001 hgeweekkIIEELRSKLPEHMVPSIfvQMEELprLNNKKV 2040
Cdd:cd17639 429 --------NEKHLTKLAEKHGVINS--EWEEL--CEDKKL 456
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
50-253 |
2.49e-17 |
|
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: 86.92 E-value: 2.49e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 50 PLSSIQKqiWFMSQLNPELPIYNeHLIKINLSGKVNIEALKKSFEQIVNRHQILRMRVKQTEDSIEQVITK-SEPTIQF- 127
Cdd:cd19534 3 PLTPIQR--WFFEQNLAGRHHFN-QSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGdVEELFRLe 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 128 -LSLRGISGEEQQEILSEYCRKEANypyrLEQENLIRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYnmysq 206
Cdd:cd19534 80 vVDLSSLAQAAAIEALAAEAQSSLD----LEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAY----- 150
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 497785100 207 NGEINPEQSQEELTIQYHDYALWQEKLLTSENLEKGLEYWKEKLEGD 253
Cdd:cd19534 151 EQALAGEPIPLPSKTSFQTWAELLAEYAQSPALLEELAYWRELPAAD 197
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1589-2040 |
2.89e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 87.37 E-value: 2.89e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQTS 1668
Cdd:PRK13390 26 SYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1669 LEEKLSK--SDLPYLCT-----DQSQDSEDySLLTKDKSYPEDI--AYIIYTSGTTGTPNGVMVkhssvmNLISATIDE- 1738
Cdd:PRK13390 106 LDGLAAKvgADLPLRLSfggeiDGFGSFEA-ALAGAGPRLTEQPcgAVMLYSSGTTGFPKGIQP------DLPGRDVDAp 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1739 -----------FNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRdwnVTLADLPPVVLDS 1807
Cdd:PRK13390 179 gdpivaiarafYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLAKRFDAQATLGHVERYR---ITVTQMVPTMFVR 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1808 ILP--------EDIPSLQTVSTGGERCPIKVAKR---WsLDRNFYNVYGPTETTIATTwyrVSSPECVQDSVPIGTPVPN 1876
Cdd:PRK13390 256 LLKldadvrtrYDVSSLRAVIHAAAPCPVDVKHAmidW-LGPIVYEYYSSTEAHGMTF---IDSPDWLAHPGSVGRSVLG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1877 TeVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNR-DDLNEKRFIPHPFreeeiLYKTGDIGKVLHDGNLEHLGRLDHQI 1955
Cdd:PRK13390 332 D-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDpEKTAAAQHPAHPF-----WTTVGDLGSVDEDGYLYLADRKSFMI 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1956 KVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYV-VPHGEWEEKKIIEEL----RSKLPEHMVPSIFVQME 2030
Cdd:PRK13390 406 ISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIqLVEGIRGSDELARELidytRSRIAHYKAPRSVEFVD 485
|
490
....*....|
gi 497785100 2031 ELPRLNNKKV 2040
Cdd:PRK13390 486 ELPRTPTGKL 495
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
1636-2148 |
2.92e-17 |
|
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: 88.61 E-value: 2.92e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1636 GAAYVPIDSELPLNRRDFILKDASVGAIVTQTSLEEKLSKSDLPYLCTDQSQDSEDYSLLTKDKSYPEDIAYIIYTSGTT 1715
Cdd:COG3319 73 LALAALAALAALALALAAAAAALLLAALALLLALLAALALALLALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAA 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1716 GTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNV 1795
Cdd:COG3319 153 GLGGGGGGAGVLVLVLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAAL 232
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1796 TLADLPPVVLDSI-----------LPEDIPSLQTVSTGGERCPIKVAKRWSLDRNFYNVYGPTETTIATTWYRVSSPECV 1864
Cdd:COG3319 233 LALLLALLLLLLAalllllalallLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVA 312
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1865 QDSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREE--EILYKTGDIGKVLHD 1942
Cdd:COG3319 313 GALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGarGRLRRGGDRGRRLGG 392
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1943 GNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMV 2022
Cdd:COG3319 393 GLLLGLGRLRLQRLRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPL 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2023 PSIFVQMEELPRLNNKKVDRhslPTAVHIFRQQKVIQKPVTEEEVVVAECWAETLNLPIDNIGLNSNFFELGGHSLTATQ 2102
Cdd:COG3319 473 PPALLLLLLLLLLLLLAALL---LAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALL 549
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 497785100 2103 LVARISELFEIELPIKAIFEYPTIQAILDFIVEMKLELGGEELDSL 2148
Cdd:COG3319 550 LLLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPLVPL 595
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
1564-1959 |
3.31e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 87.86 E-value: 3.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1564 IQYSFENWVRSSPNHIALRFLD---------RSYTYDEVNKRANKIANQLYKMGiRRGDRVALYHERSSEMIFGFLGILK 1634
Cdd:PRK07769 23 LVRHVERWAKVRGDKLAYRFLDfsterdgvaRDLTWSQFGARNRAVGARLQQVT-KPGDRVAILAPQNLDYLIAFFGALY 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1635 CGAAYVPI-DSELP--LNRRDFILKDASVGAIVTQTSLEEKLSK--SDLP------YLCTDQSQDSEDySLLTKDKSYPE 1703
Cdd:PRK07769 102 AGRIAVPLfDPAEPghVGRLHAVLDDCTPSAILTTTDSAEGVRKffRARPakerprVIAVDAVPDEVG-ATWVPPEANED 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1704 DIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVvsreeqLST 1783
Cdd:PRK07769 181 TIAYLQYTSGSTRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITF------MSP 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1784 KALVKRFRDWNVTLAD------------------------LPPvvlDSILPEDIPSLQTVSTGGErcPIKVAkrwSLdRN 1839
Cdd:PRK07769 255 AAFVRRPGRWIRELARkpggtggtfsaapnfafehaaargLPK---DGEPPLDLSNVKGLLNGSE--PVSPA---SM-RK 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1840 FYNVYGP---TETTI--------ATTWyrVSSPEcVQDS------------------VPIGTPVPNTEV----------- 1879
Cdd:PRK07769 326 FNEAFAPyglPPTAIkpsygmaeATLF--VSTTP-MDEEptviyvdrdelnagrfveVPADAPNAVAQVsagkvgvsewa 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1880 FILDPD-LNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRF-------IPHPFRE----EEILYKTGDIGkVLHDGNLEH 1947
Cdd:PRK07769 403 VIVDPEtASELPDGQIGEIWLHGNNIGTGYWGKPEETAATFqnilksrLSESHAEgapdDALWVRTGDYG-VYFDGELYI 481
|
490
....*....|..
gi 497785100 1948 LGRLDHQIKVRG 1959
Cdd:PRK07769 482 TGRVKDLVIIDG 493
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1703-2045 |
4.77e-17 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 85.10 E-value: 4.77e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1703 EDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITqetkvGQF--ATISFDASLWQILM-ALLAGATLCVVSREE 1779
Cdd:PRK07824 35 DDVALVVATSGTTGTPKGAMLTAAALTASADATHDRLGGP-----GQWllALPAHHIAGLQVLVrSVIAGSEPVELDVSA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1780 QLSTKALVKRFR--DWNVTLADLPPVVLDSIL--PEDIPSLQT---VSTGGERCPIKVAKRWS-LDRNFYNVYGPTETti 1851
Cdd:PRK07824 110 GFDPTALPRAVAelGGGRRYTSLVPMQLAKALddPAATAALAEldaVLVGGGPAPAPVLDAAAaAGINVVRTYGMSET-- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1852 attwyrvsSPECVQDsvpiGTPVPNTEVFILDpdlnpvpmgviGEIYIGGVGVSNGYLNRDDlnekrfiPHPFREEEiLY 1931
Cdd:PRK07824 188 --------SGGCVYD----GVPLDGVRVRVED-----------GRIALGGPTLAKGYRNPVD-------PDPFAEPG-WF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1932 KTGDIGkVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGewEEKKIIE 2011
Cdd:PRK07824 237 RTDDLG-ALDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRLGQRVVAAVVGDG--GPAPTLE 313
|
330 340 350
....*....|....*....|....*....|....*...
gi 497785100 2012 ELRSK----LPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK07824 314 ALRAHvartLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1581-2045 |
6.48e-17 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 86.74 E-value: 6.48e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1581 LRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASV 1660
Cdd:PRK06155 40 LVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGA 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1661 GAIVTQTSLEEKLSKSDLPYL--------------CTDQSQDSEDY----SLLTKDKSYPEDIAYIIYTSGTTGTPNGVM 1722
Cdd:PRK06155 120 RLLVVEAALLAALEAADPGDLplpavwlldapasvSVPAGWSTAPLppldAPAPAAAVQPGDTAAILYTSGTTGPSKGVC 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1723 VKHSSVMNLISATIDEFNITQE----TKVGQFATISFdASLWQilmALLAGATLCVvsrEEQLSTKALVKRFRDWNVTLA 1798
Cdd:PRK06155 200 CPHAQFYWWGRNSAEDLEIGADdvlyTTLPLFHTNAL-NAFFQ---ALLAGATYVL---EPRFSASGFWPAVRRHGATVT 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1799 DLPPVVLdSIL------PEDIPSLQTVSTGG-----------ERCPIKVAkrwsldrnfyNVYGPTETT--IATTWyrvs 1859
Cdd:PRK06155 273 YLLGAMV-SILlsqparESDRAHRVRVALGPgvpaalhaafrERFGVDLL----------DGYGSTETNfvIAVTH---- 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1860 specvQDSVP--IGTPVPNTEVFILDPDLNPVPMGVIGEIYIGG---VGVSNGYLNrddlnekrfIPHPFRE--EEILYK 1932
Cdd:PRK06155 338 -----GSQRPgsMGRLAPGFEARVVDEHDQELPDGEPGELLLRAdepFAFATGYFG---------MPEKTVEawRNLWFH 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1933 TGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQP----LGDNQnyhTLVAYVVPHGEWEEKK 2008
Cdd:PRK06155 404 TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPvpseLGEDE---VMAAVVLRDGTALEPV 480
|
490 500 510
....*....|....*....|....*....|....*...
gi 497785100 2009 IIEEL-RSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK06155 481 ALVRHcEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
531-1001 |
6.70e-17 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 86.39 E-value: 6.70e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 531 SYTYLQTNnrANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIItqdskLKAIITH 610
Cdd:cd05908 17 SYRHLREE--ALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIGSNEEHKLKL-----NKVWNTL 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 611 SEyktsyegyevPILYIDqldDFLLDEREDnlnvdcdssQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPK 690
Cdd:cd05908 90 KN----------PYLITE---EEVLCELAD---------ELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 691 DRYLLLQSLAYDFCLTTIY-TSLLSGGTLFFLLKEDAIdpakVEEIVQGKAIDWYKITpshlkALSSES-GTKLF----- 763
Cdd:cd05908 148 DRILSWMPLTHDMGLIAFHlAPLIAGMNQYLMPTRLFI----RRPILWLKKASEHKAT-----IVSSPNfGYKYFlktlk 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 764 PRKG----------LILGGEASEWSWIKEIYR-----NIPASCkLFNHYGPSETTIGVA--------------------- 807
Cdd:cd05908 219 PEKAndwdlssirmILNGAEPIDYELCHEFLDhmskyGLKRNA-ILPVYGLAEASVGASlpkaqspfktitlgrrhvthg 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 808 --VYEVTKKGlSNQFSTTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFItdsrm 885
Cdd:cd05908 298 epEPEVDKKD-SECLTFVEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGWL----- 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 886 yKTGDIGkILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRN----EEQLVAYYVSKKEV--- 958
Cdd:cd05908 372 -KTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAEELEGVELGRVVACGVNNsntrNEEIFCFIEHRKSEddf 449
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 497785100 959 --LDKDLQTYLKQ--KLPPNLVpaylVKMDTLPRHAHGKIDRKALPE 1001
Cdd:cd05908 450 ypLGKKIKKHLNKrgGWQINEV----LPIRRIPKTTSGKVKRYELAQ 492
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
655-996 |
7.31e-17 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 84.24 E-value: 7.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 655 IYTSGSTGIPKGVLVEHRNLsnyIYA-IQTKL--GNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLlkeDAIDPAK 731
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNL---IAAnLQLIHamGLTEADVYLNMLPLFHIAGLNLALATFHAGGANVVM---EKFDPAE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 732 VEEIVQGKAIDWYKITPSHLKALSSE---SGTKLFPRKgLILGGEASEWswIKEIYRNIPAscKLFNHYGPSETTiGVAV 808
Cdd:cd17637 80 ALELIEEEKVTLMGSFPPILSNLLDAaekSGVDLSSLR-HVLGLDAPET--IQRFEETTGA--TFWSLYGQTETS-GLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 809 YevtkkGLSNQFSTTpIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDpfitdsrMYKT 888
Cdd:cd17637 154 L-----SPYRERPGS-AGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG-------WHHT 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 889 GDIGKILYTGEIQFLGR-----LdgqVKIRGIRVEPEEIQSQLLSHPSITEAIVT-VTKVRNEEQLVAYYVSK--KEVLD 960
Cdd:cd17637 221 GDLGRFDEDGYLWYAGRkpekeL---IKPGGENVYPAEVEKVILEHPAIAEVCVIgVPDPKWGEGIKAVCVLKpgATLTA 297
|
330 340 350
....*....|....*....|....*....|....*.
gi 497785100 961 KDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDR 996
Cdd:cd17637 298 DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1588-2001 |
8.43e-17 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are eukaryotic fatty acid CoA synthetases that activate fatty acids with chain lengths of 12 to 20. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells.
Pssm-ID: 341250 [Multi-domain] Cd Length: 545 Bit Score: 86.12 E-value: 8.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1588 YTYDEVNKRANKIANQLYKMGIRR--GDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVT 1665
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1666 QTSLE-------EKLSKSDLPYLctdqsqdsedysllTKDKsyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDE 1738
Cdd:cd05927 86 DAGVKvysleefEKLGKKNKVPP--------------PPPK--PEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKI 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1739 FNITQET-----------------KVGQFATISFDASL--WQ----ILM---ALLAGATLCVVSR---------EEQLST 1783
Cdd:cd05927 150 LEILNKInptdvyisylplahifeRVVEALFLYHGAKIgfYSgdirLLLddiKALKPTVFPGVPRvlnriydkiFNKVQA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1784 KALVKRFR-DW--NVTLADL------PPVVLDSILPEDIPSL-----QTVSTGGERCPIKVAK--RWSLDRNFYNVYGPT 1847
Cdd:cd05927 230 KGPLKRKLfNFalNYKLAELrsgvvrASPFWDKLVFNKIKQAlggnvRLMLTGSAPLSPEVLEflRVALGCPVLEGYGQT 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1848 ETTIATTwyrVSSPecvQDSVP--IGTPVPNTEVFILD-PDLN-----PVPMgviGEIYIGGVGVSNGYLNRDDLNEKRF 1919
Cdd:cd05927 310 ECTAGAT---LTLP---GDTSVghVGGPLPCAEVKLVDvPEMNydakdPNPR---GEVCIRGPNVFSGYYKDPEKTAEAL 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1920 iphpfrEEEILYKTGDIGKVLHDGNLEHLGRLDHQIK-VRGFRIELGEIESLLNLQTGVKEAIVQplGDNQNYHtLVAYV 1998
Cdd:cd05927 381 ------DEDGWLHTGDIGEWLPNGTLKIIDRKKNIFKlSQGEYVAPEKIENIYARSPFVAQIFVY--GDSLKSF-LVAIV 451
|
...
gi 497785100 1999 VPH 2001
Cdd:cd05927 452 VPD 454
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1576-1959 |
1.38e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 85.76 E-value: 1.38e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLD---------RSYTYDEVNKRANKIANQLYKMGiRRGDRVALYHERSSEMIFGFLGILKCGAAYVPidseL 1646
Cdd:PRK05850 15 PDDAAFTFIDyeqdpagvaETLTWSQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAFLGALQAGLIAVP----L 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1647 PL-------NRRDFILKDASVGAIVTQTSLEEKLSKsdlpYLCTDQSQ-------------DSEDYSLLTKDKsyPEDIA 1706
Cdd:PRK05850 90 SVpqggahdERVSAVLRDTSPSVVLTTSAVVDDVTE----YVAPQPGQsappvievdlldlDSPRGSDARPRD--LPSTA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1707 YIIYTSGTTGTPNGVMVKHSsvmNLISatidefNITQETKvGQFA----TISFDASL--WQIL---MALLAGATLCVVS- 1776
Cdd:PRK05850 164 YLQYTSGSTRTPAGVMVSHR---NVIA------NFEQLMS-DYFGdtggVPPPDTTVvsWLPFyhdMGLVLGVCAPILGg 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1777 -REEQLSTKALVKRFRDWNVTLADLPPVVldSILP-------------EDIPSL-----QTVSTGGERCPIKVAKRWsLD 1837
Cdd:PRK05850 234 cPAVLTSPVAFLQRPARWMQLLASNPHAF--SAAPnfafelavrktsdDDMAGLdlggvLGIISGSERVHPATLKRF-AD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1838 RnF--YNV--------YGPTETT--IATTWYRvSSPECVQ---DSVPIGTPVP----------------NTEVFILDPDL 1886
Cdd:PRK05850 311 R-FapFNLretairpsYGLAEATvyVATREPG-QPPESVRfdyEKLSAGHAKRcetgggtplvsygsprSPTVRIVDPDT 388
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497785100 1887 N-PVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRF-----IPHPFREEEILYKTGDIGkVLHDGNLEHLGRLDHQIKVRG 1959
Cdd:PRK05850 389 CiECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatlvDPSPGTPEGPWLRTGDLG-FISEGELFIVGRIKDLLIVDG 466
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1576-2047 |
1.40e-16 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 85.67 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:PLN02479 34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQTS-----------LEEKLSKSDLPYLCT---DQSQDSEDYS-------------LLTKDKSY----PED 1704
Cdd:PLN02479 114 EHSKSEVVMVDQEfftlaeealkiLAEKKKSSFKPPLLIvigDPTCDPKSLQyalgkgaieyekfLETGDPEFawkpPAD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1705 ----IAyIIYTSGTTGTPNGVMVKH--SSVMNLISATIDEFNitqETKVGQFATISFDASLW--QILMALLAGATLCVvs 1776
Cdd:PLN02479 194 ewqsIA-LGYTSGTTASPKGVVLHHrgAYLMALSNALIWGMN---EGAVYLWTLPMFHCNGWcfTWTLAALCGTNICL-- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1777 reEQLSTKALVKRFRDWNVTLADLPPVVL---------DSILPedIPSLQTVSTGGERCPIKVAKRWSlDRNF--YNVYG 1845
Cdd:PLN02479 268 --RQVTAKAIYSAIANYGVTHFCAAPVVLntivnapksETILP--LPRVVHVMTAGAAPPPSVLFAMS-EKGFrvTHTYG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1846 PTETTIATT---WyrvsSPEcvQDSVPIGTP-----------VPNTEVFILDP-DLNPVPM--GVIGEIYIGGVGVSNGY 1908
Cdd:PLN02479 343 LSETYGPSTvcaW----KPE--WDSLPPEEQarlnarqgvryIGLEGLDVVDTkTMKPVPAdgKTMGEIVMRGNMVMKGY 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1909 LNRDDLNEKRFiphpfreEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDN 1988
Cdd:PLN02479 417 LKNPKANEEAF-------ANGWFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPDE 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 1989 QNYHTLVAYVVPHGEWEEKKIIEEL-------RSKLPEHMVPSIFVqMEELPRLNNKKVDRHSLPT 2047
Cdd:PLN02479 490 RWGESPCAFVTLKPGVDKSDEAALAedimkfcRERLPAYWVPKSVV-FGPLPKTATGKIQKHVLRA 554
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
653-995 |
1.67e-16 |
|
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: 83.59 E-value: 1.67e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 653 YGIYTSGSTGIPKGVLVEH----------RNLSNYIYA-----IQTKLGNKPKdRYLLLQSLAYDFCLTTIYTSLLSGGT 717
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQedifrmlmggADFGTGEFTpsedaHKAAAAAAGT-VMFPAPPLMHGTGSWTAFGGLLGGQT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 718 LFF---------LLKE-------------DAIDPAKVEEIVQGKAIDWykitpSHLKALSSeSGTKLFP--RKGLIlgge 773
Cdd:cd05924 86 VVLpddrfdpeeVWRTiekhkvtsmtivgDAMARPLIDALRDAGPYDL-----SSLFAISS-GGALLSPevKQGLL---- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 774 asewswikEIYRNIpascKLFNHYGPSETTIGVAVYeVTKKGLSNQFSTTPigsslsNNRIYILDDKLRPVP--SGIPGH 851
Cdd:cd05924 156 --------ELVPNI----TLVDAFGSSETGFTGSGH-SAGSGPETGPFTRA------NPDTVVLDDDGRVVPpgSGGVGW 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 852 IYIAGeQVARGYLNREELTAERFMEdpfITDSRMYKTGDIGKILYTGEIQFLGRldGQVKIR--GIRVEPEEIQSQLLSH 929
Cdd:cd05924 217 IARRG-HIPLGYYGDEAKTAETFPE---VDGVRYAVPGDRATVEADGTVTLLGR--GSVCINtgGEKVFPEEVEEALKSH 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497785100 930 PSITEAIVTVTKVRNEEQLVAYYVSKKEVLDKD---LQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKID 995
Cdd:cd05924 291 PAVYDVLVVGRPDERWGQEVVAVVQLREGAGVDleeLREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
532-938 |
1.68e-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: 85.34 E-value: 1.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 532 YTYLQTNNRANQIARWLQKQGI--GKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIIT 609
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 610 HSEYKT-SYEgyEVPILYIDQLDDFLLDEREDnlnvdcdssqLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNK 688
Cdd:cd05927 86 DAGVKVySLE--EFEKLGKKNKVPPPPPKPED----------LATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEIL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 689 PK----DRYLLLQSLAYDFCLTTIYTSLLSGGTLFF------LLKED--AIDP--------------AKVEEIVQGK--- 739
Cdd:cd05927 154 NKinptDVYISYLPLAHIFERVVEALFLYHGAKIGFysgdirLLLDDikALKPtvfpgvprvlnriyDKIFNKVQAKgpl 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 740 -------AID----------------WYKITPSHLKALssesgtkLFPRKGLILGGEASEWSWIKEIYRNIPAsCKLFNH 796
Cdd:cd05927 234 krklfnfALNyklaelrsgvvraspfWDKLVFNKIKQA-------LGGNVRLMLTGSAPLSPEVLEFLRVALG-CPVLEG 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 797 YGPSETTIGVAVyevtkkGLSNQFSTTPIGSSLSNNRIyilddKLRPVP------SGIP--GHIYIAGEQVARGYLNREE 868
Cdd:cd05927 306 YGQTECTAGATL------TLPGDTSVGHVGGPLPCAEV-----KLVDVPemnydaKDPNprGEVCIRGPNVFSGYYKDPE 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497785100 869 LTAERFMEDPFitdsrmYKTGDIGKILYTGEIQFLGRLDGQVKI-RGIRVEPEEIQSQLLSHPSITEAIVT 938
Cdd:cd05927 375 KTAEALDEDGW------LHTGDIGEWLPNGTLKIIDRKKNIFKLsQGEYVAPEKIENIYARSPFVAQIFVY 439
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
1109-1425 |
1.91e-16 |
|
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: 84.03 E-value: 1.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1109 PLSDAQKRMWFLYRMESDSAYYNMPISLKI--IGDLDyrAFTESIQEVNKRHDSLRTVFReSKNID-PVQVVLKDLKCTI 1185
Cdd:cd19544 3 PLAPLQEGILFHHLLAEEGDPYLLRSLLAFdsRARLD--AFLAALQQVIDRHDILRTAIL-WEGLSePVQVVWRQAELPV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1186 NILDFDEnrsEQDIMNYLTEKsMEP----FKLETGPLIRVHLVKSNPN-EHVLLIVQHHIISDGWSLRIMMDELFAiyhq 1260
Cdd:cd19544 80 EELTLDP---GDDALAQLRAR-FDPrryrLDLRQAPLLRAHVAEDPANgRWLLLLLFHHLISDHTSLELLLEEIQA---- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1261 IISNMPIQLEQPVyQYADYVnwQQNRYTEEQINQQlQYWKEQLSG-----AP-SLLELPLDkprpsmqsynGSLI---RM 1331
Cdd:cd19544 152 ILAGRAAALPPPV-PYRNFV--AQARLGASQAEHE-AFFREMLGDvdeptAPfGLLDVQGD----------GSDIteaRL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1332 KLPEKHAVLIKEICEEAKVTPYTIFLTFFNILLYRYTYQDKILVGTPIANRnIQELEGI---LGLFVNTLviPSTVK-GD 1407
Cdd:cd19544 218 ALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGR-MQGGAGAdraLGMFINTL--PLRVRlGG 294
|
330
....*....|....*...
gi 497785100 1408 RNFKSLLQQVNNQiLGAL 1425
Cdd:cd19544 295 RSVREAVRQTHAR-LAEL 311
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
495-1004 |
3.31e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 84.44 E-value: 3.31e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 495 YNQSGCKPFPTEPIHVQFEGQVLNTPNSIAL--SDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIA 572
Cdd:PRK12583 7 YQGGGDKPLLTQTIGDAFDATVARFPDREALvvRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 573 MLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITHSEYKTS----------------------------------YE 618
Cdd:PRK12583 87 QFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKTSdyhamlqellpglaegqpgalacerlpelrgvvsLA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 619 GYEVPILYI--------DQLDDFLLDEREDNLNVDcDSSQLAYgiyTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPK 690
Cdd:PRK12583 167 PAPPPGFLAwhelqargETVSREALAERQASLDRD-DPINIQY---TSGTTGFPKGATLSHHNILNNGYFVAESLGLTEH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 691 DRylLLQSLAYDFCLTTIYTSLL---SGGTLffLLKEDAIDPAKVeeivqgkaidwykitpshLKALSSESGTKLF---- 763
Cdd:PRK12583 243 DR--LCVPVPLYHCFGMVLANLGcmtVGACL--VYPNEAFDPLAT------------------LQAVEEERCTALYgvpt 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 764 --------PRKGL---------ILGGEASEWSWIKEIYRNIPAScKLFNHYGPSETTigvAVYEVTKKGLSNQFSTTPIG 826
Cdd:PRK12583 301 mfiaeldhPQRGNfdlsslrtgIMAGAPCPIEVMRRVMDEMHMA-EVQIAYGMTETS---PVSLQTTAADDLERRVETVG 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 827 SSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDPFitdsrMYkTGDIGKILYTGEIQFLGRL 906
Cdd:PRK12583 377 RTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW-----MH-TGDLATMDEQGYVRIVGRS 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 907 DGQVkIRG-IRVEPEEIQSQLLSHPSITEaiVTVTKVRNE---EQLVAYYVSK--KEVLDKDLQTYLKQKLPPNLVPAYL 980
Cdd:PRK12583 451 KDMI-IRGgENIYPREIEEFLFTHPAVAD--VQVFGVPDEkygEEIVAWVRLHpgHAASEEELREFCKARIAHFKVPRYF 527
|
570 580
....*....|....*....|....
gi 497785100 981 VKMDTLPRHAHGKIDRKALPEIQV 1004
Cdd:PRK12583 528 RFVDEFPMTVTGKVQKFRMREISI 551
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
2073-2135 |
3.75e-16 |
|
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: 74.89 E-value: 3.75e-16
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497785100 2073 WAETLNLPIDNIGLNSNFF-ELGGHSLTATQLVARISELFEIELPIKAIFEYPTIQAILDFIVE 2135
Cdd:COG0236 14 IAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1853-2135 |
5.88e-16 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 80.95 E-value: 5.88e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1853 TTWYRVSSPECVQDSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFREEEILYK 1932
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1933 TGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIE----SLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKK 2008
Cdd:COG3433 81 QADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEelllVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 2009 IIEELRsKLPEHMVPSIFVQMEELPRLNNKKVDRHSLPTAVHIFRQQKVIQKPVTEEEVVVAEC----WAETLNLPIDNI 2084
Cdd:COG3433 161 ALAALD-KVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASPAPALETALTEEElradVAELLGVDPEEI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 497785100 2085 GLNSNFFELGGHSLTATQLVARISELFeIELPIKAIFEYPTIQAILDFIVE 2135
Cdd:COG3433 240 DPDDNLFDLGLDSIRLMQLVERWRKAG-LDVSFADLAEHPTLAAWWALLAA 289
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1702-2045 |
6.47e-16 |
|
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: 81.76 E-value: 6.47e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1702 PEDIAYIIYTSGTTGTPNGVMVKHSS------VMNLISatidefnITQETKVGQFATISF--DASLWQILMALLAGATLC 1773
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPKLAQHTHSNevynawMLALNS-------LFDPDDVLLCGLPLFhvNGSVVTLLTPLASGAHVV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1774 VVS----REEQLSTK--ALVKRFRdwnVTLADLPPVVLDSILP----EDIPSLQTVSTGGERCPIKVAKRW--SLDRNFY 1841
Cdd:cd05944 74 LAGpagyRNPGLFDNfwKLVERYR---ITSLSTVPTVYAALLQvpvnADISSLRFAMSGAAPLPVELRARFedATGLPVV 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1842 NVYGPTETTIATTwyrVSSPECVQDSVPIGTPVPNTEVFI--LDPD---LNPVPMGVIGEIYIGGVGVSNGYLNrDDLNE 1916
Cdd:cd05944 151 EGYGLTEATCLVA---VNPPDGPKRPGSVGLRLPYARVRIkvLDGVgrlLRDCAPDEVGEICVAGPGVFGGYLY-TEGNK 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1917 KRFIphpfreEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLL--NLQTGVKEAIVQPlgDNQNYHTL 1994
Cdd:cd05944 227 NAFV------ADGWLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALlrHPAVAFAGAVGQP--DAHAGELP 298
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 497785100 1995 VAYV--VPHGEWEEKKIIEELRSKLPEH-MVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:cd05944 299 VAYVqlKPGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1557-2045 |
8.52e-16 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 83.18 E-value: 8.52e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1557 PRSIkDCIQYS-----FENWVRSSPNHIALRFLDRSYTYDEVNKRANKIANQLY-KMGIRRGDRVALYHERSSEMIFGFL 1630
Cdd:PRK08974 14 PAEI-NPDRYQslvdmFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQnGLGLKKGDRVALMMPNLLQYPIALF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1631 GILKCGAA-------YVPIDSELPLNrrdfilkDASVGAIV---------------TQ------TSLEEKLS-------- 1674
Cdd:PRK08974 93 GILRAGMIvvnvnplYTPRELEHQLN-------DSGAKAIVivsnfahtlekvvfkTPvkhvilTRMGDQLStakgtlvn 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1675 -----------KSDLPYLCTDQSQDSEDYSL-LTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVM-NLISATIDEFNI 1741
Cdd:PRK08974 166 fvvkyikrlvpKYHLPDAISFRSALHKGRRMqYVKPELVPEDLAFLQYTGGTTGVAKGAMLTHRNMLaNLEQAKAAYGPL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1742 TQETKvgQFATISFdaSLWQILmALLAGATLCVvsreEQLSTKALVKRFRDWNVTLADL---PPVVL-------DSIL-- 1809
Cdd:PRK08974 246 LHPGK--ELVVTAL--PLYHIF-ALTVNCLLFI----ELGGQNLLITNPRDIPGFVKELkkyPFTAItgvntlfNALLnn 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1810 PE----DIPSLQTVSTGGERCPIKVAKRWS--LDRNFYNVYGPTETTIATTWYRVsspECVQDSVPIGTPVPNTEVFILD 1883
Cdd:PRK08974 317 EEfqelDFSSLKLSVGGGMAVQQAVAERWVklTGQYLLEGYGLTECSPLVSVNPY---DLDYYSGSIGLPVPSTEIKLVD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1884 PDLNPVPMGVIGEIYIGGVGVSNGYLNRddlnekrfiphPFREEEIL----YKTGDIGKVLHDGNLEHLGRLDHQIKVRG 1959
Cdd:PRK08974 394 DDGNEVPPGEPGELWVKGPQVMLGYWQR-----------PEATDEVIkdgwLATGDIAVMDEEGFLRIVDRKKDMILVSG 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1960 FRIELGEIESLLNLQTGVKE--AIVQPlgdNQNYHTLV-AYVVPHGEWEEKKIIEE-LRSKLPEHMVPSIFVQMEELPRL 2035
Cdd:PRK08974 463 FNVYPNEIEDVVMLHPKVLEvaAVGVP---SEVSGEAVkIFVVKKDPSLTEEELIThCRRHLTGYKVPKLVEFRDELPKS 539
|
570
....*....|
gi 497785100 2036 NNKKVDRHSL 2045
Cdd:PRK08974 540 NVGKILRREL 549
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
507-1002 |
9.81e-16 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 83.13 E-value: 9.81e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 507 PIHVQFEGQVLNT-------------PNSIAL------SDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCA 567
Cdd:cd05967 39 PFTRWFVGGRLNTcynaldrhveagrGDQIALiydspvTGTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 568 KAIIAMLGVLKAG-------GAYLPLDVESpkeRIEiitqDSKLKAIITHS---------EYKT---------------- 615
Cdd:cd05967 119 EAAIAMLACARIGaihsvvfGGFAAKELAS---RID----DAKPKLIVTAScgiepgkvvPYKPlldkalelsghkphhv 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 616 -SYEGYEVPILYIDQLDDFLLDE-REDNLNVDC---DSSQLAYGIYTSGSTGIPKGVLvehRNLSNYI----YAIQTKLG 686
Cdd:cd05967 192 lVLNRPQVPADLTKPGRDLDWSElLAKAEPVDCvpvAATDPLYILYTSGTTGKPKGVV---RDNGGHAvalnWSMRNIYG 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 687 NKPKDRYlllqslaydFCLTTI----------YTSLLSGGT-LFFLLKEDAI-DPAkveeiVQGKAIDWYKIT-----PS 749
Cdd:cd05967 269 IKPGDVW---------WAASDVgwvvghsyivYGPLLHGATtVLYEGKPVGTpDPG-----AFWRVIEKYQVNalftaPT 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 750 HLKALSSESGTKLFPRK-------GLILGGE---ASEWSWIKEIYrNIPasckLFNHYGPSETTIGVAVyevTKKGLSNQ 819
Cdd:cd05967 335 AIRAIRKEDPDGKYIKKydlsslrTLFLAGErldPPTLEWAENTL-GVP----VIDHWWQTETGWPITA---NPVGLEPL 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 820 fsTTPIGS---SLSNNRIYILDDKLRPVPSGIPGHIYIAGEqVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKILY 896
Cdd:cd05967 407 --PIKAGSpgkPVPGYQVQVLDEDGEPVGPNELGNIVIKLP-LPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 897 TGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAivTVTKVRNE---EQLVAYYVSKKEV------LDKDLQTYL 967
Cdd:cd05967 484 DGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAEC--AVVGVRDElkgQVPLGLVVLKEGVkitaeeLEKELVALV 561
|
570 580 590
....*....|....*....|....*....|....*
gi 497785100 968 KQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:cd05967 562 REQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKI 596
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
2072-2128 |
1.85e-15 |
|
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: 72.60 E-value: 1.85e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 497785100 2072 CWAETLNLPIDNIGLNSNFFELGGHSLTATQLVARISELFEIELPIKAIFEYPTIQA 2128
Cdd:pfam00550 6 LLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
501-696 |
5.64e-15 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 80.69 E-value: 5.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 501 KPFPTEPIHVQFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAG 580
Cdd:PRK08279 32 TPDSKRSLGDVFEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 581 -----------GAYLP--LDVESPK---------ERIEIITQDSKlkaiITHSEYKTSYEGYEVPILYIDqLDDFLLDER 638
Cdd:PRK08279 112 avvallntqqrGAVLAhsLNLVDAKhlivgeelvEAFEEARADLA----RPPRLWVAGGDTLDDPEGYED-LAAAAAGAP 186
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497785100 639 EDNLNVDCDSS--QLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDR-YLLL 696
Cdd:PRK08279 187 TTNPASRSGVTakDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDDVlYCCL 247
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
530-994 |
6.40e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 79.95 E-value: 6.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 530 RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIIT 609
Cdd:PRK08276 10 EVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 610 HSEYKTSYEG------YEVPILYID--QLDDFL-LDErednlnvdCDSSQLAYGI----------YTSGSTGIPKGVLVE 670
Cdd:PRK08276 90 SAALADTAAElaaelpAGVPLLLVVagPVPGFRsYEE--------ALAAQPDTPIadetagadmlYSSGTTGRPKGIKRP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 671 ------HRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAidpakvEEIVQgkAIDWY 744
Cdd:PRK08276 162 lpgldpDEAPGMMLALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVMEKFDA------EEALA--LIERY 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 745 KITPSH--------LKALSSESGTK--LFPRKGLILGG--------EAS-EWsW---IKEIYrnipAScklfnhygpSET 802
Cdd:PRK08276 234 RVTHSQlvptmfvrMLKLPEEVRARydVSSLRVAIHAAapcpvevkRAMiDW-WgpiIHEYY----AS---------SEG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 803 tIGVAVYE----VTKKGLSNQfsttPIGSslsnnRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMEDP 878
Cdd:PRK08276 300 -GGVTVITsedwLAHPGSVGK----AVLG-----EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARNPHG 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 879 FITdsrmykTGDIGkilYTGEIQFLGRLD--------GQVKIRgirvePEEIQSQLLSHPSIteAIVTVTKVRNE---EQ 947
Cdd:PRK08276 370 WVT------VGDVG---YLDEDGYLYLTDrksdmiisGGVNIY-----PQEIENLLVTHPKV--ADVAVFGVPDEemgER 433
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 497785100 948 LVAYY-----VSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKI 994
Cdd:PRK08276 434 VKAVVqpadgADAGDALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKL 485
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
532-939 |
6.82e-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: 79.82 E-value: 6.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 532 YTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITHS 611
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVGK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 612 --EYKTSYEGY-EVPILYIDQLDDFLLDEREDNLNVDC----------DSSQLAYGIYTSGSTGIPKGVLvehRNLSNYI 678
Cdd:cd05932 87 ldDWKAMAPGVpEGLISISLPPPSAANCQYQWDDLIAQhppleerptrFPEQLATLIYTSGTTGQPKGVM---LTFGSFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 679 YAIQ---TKLGNKPKDRYLLLQSLAYDFCLTTIY-TSLLSGGTLFFLLKEDAIdPAKVEE--------------IVQGKA 740
Cdd:cd05932 164 WAAQagiEHIGTEENDRMLSYLPLAHVTERVFVEgGSLYGGVLVAFAESLDTF-VEDVQRarptlffsvprlwtKFQQGV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 741 IDwyKITPSHLKAL------SSESGTKLFPRKGL-----ILGGEASEWSWIKEIYRNIpaSCKLFNHYGPSETtigVAVY 809
Cdd:cd05932 243 QD--KIPQQKLNLLlkipvvNSLVKRKVLKGLGLdqcrlAGCGSAPVPPALLEWYRSL--GLNILEAYGMTEN---FAYS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 810 EVTKKGlSNQFSTtpIGSSLSNNRIYILDDklrpvpsgipGHIYIAGEQVARGYLNREELTAERFMEDPFItdsrmyKTG 889
Cdd:cd05932 316 HLNYPG-RDKIGT--VGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFL------RTG 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 497785100 890 DIGKILYTGEIQFLGRLDGQVKI-RGIRVEPEEIQSQLLSHPSItEAIVTV 939
Cdd:cd05932 377 DKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRV-EMVCVI 426
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
520-987 |
8.90e-15 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 79.79 E-value: 8.90e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:PRK06164 24 PDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRYRSHEVAHIL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIIthseYKTSYEGYEVPILYIDQLDDFLLDEREDNLnVDCDSSQL---------------------------- 651
Cdd:PRK06164 104 GRGRARWLV----VWPGFKGIDFAAILAAVPPDALPPLRAIAV-VDDAADATpapapgarvqlfalpdpappaaageraa 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 652 -----AYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLfflLKEDA 726
Cdd:PRK06164 179 dpdagALLFTTSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPL---VCEPV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 727 IDPAKVEEIVQGkaidwYKITpsHLKAlSSESGTKLFPrkgliLGGEASEWSWIKEI--------YRNIPASCK-----L 793
Cdd:PRK06164 256 FDAARTARALRR-----HRVT--HTFG-NDEMLRRILD-----TAGERADFPSARLFgfasfapaLGELAALARargvpL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 794 FNHYGPSETTIGVAVYEVTkkglsNQFSTTPIGSSL---SNNRIYILD-DKLRPVPSGIPGHIYIAGEQVARGYLNREEL 869
Cdd:PRK06164 323 TGLYGSSEVQALVALQPAT-----DPVSVRIEGGGRpasPEARVRARDpQDGALLPDGESGEIEIRAPSLMRGYLDNPDA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 870 TAERFMEDPFitdsrmYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLV 949
Cdd:PRK06164 398 TARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPV 471
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 497785100 950 AYYVSKK-EVLD-KDLQTYLKQKLPPNLVPAYLVKMDTLP 987
Cdd:PRK06164 472 AFVIPTDgASPDeAGLMAACREALAGFKVPARVQVVEAFP 511
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1585-1982 |
1.22e-14 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 79.46 E-value: 1.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1585 DRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIV 1664
Cdd:PLN02860 30 NRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLV 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 TQTSLE---EKLSKSDLP----YLCTDQSQDS---EDYSLLTKD--------------KSYPEDIAYIIYTSGTTGTPNG 1720
Cdd:PLN02860 110 TDETCSswyEELQNDRLPslmwQVFLESPSSSvfiFLNSFLTTEmlkqralgtteldyAWAPDDAVLICFTSGTTGRPKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1721 VMVKHSSVmnlisatidefnITQEtkVGQFATISFD--------ASLWQI------LMALLAGATLCVVSREEqlsTKAL 1786
Cdd:PLN02860 190 VTISHSAL------------IVQS--LAKIAIVGYGeddvylhtAPLCHIgglssaLAMLMVGACHVLLPKFD---AKAA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1787 VKRFRDWNVT--------LADLPPVVLDSILPEDIPSLQTVSTGGERCP---IKVAKRWSLDRNFYNVYGPTETTIATTW 1855
Cdd:PLN02860 253 LQAIKQHNVTsmitvpamMADLISLTRKSMTWKVFPSVRKILNGGGSLSsrlLPDAKKLFPNAKLFSAYGMTEACSSLTF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1856 YRVSSPECV-------------QDSVP------IGTPVPNTEVFILDPDLNPVpmgviGEIYIGGVGVSNGY--LNRDDL 1914
Cdd:PLN02860 333 MTLHDPTLEspkqtlqtvnqtkSSSVHqpqgvcVGKPAPHVELKIGLDESSRV-----GRILTRGPHVMLGYwgQNSETA 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 1915 NEkrfiphpfREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIV 1982
Cdd:PLN02860 408 SV--------LSNDGWLDTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVV 467
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
515-1005 |
1.25e-14 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 79.42 E-value: 1.25e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 515 QVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKER 594
Cdd:PRK06155 30 QAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQ 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 595 IEIITQDSKLKAIITHSEYKTSYEGYEVPILYIDQLddFLLDEREDNL---------------NVDCDSSQ---LAYGIY 656
Cdd:PRK06155 110 LEHILRNSGARLLVVEAALLAALEAADPGDLPLPAV--WLLDAPASVSvpagwstaplppldaPAPAAAVQpgdTAAILY 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 657 TSGSTGIPKGVLVEHRNLsnYIYAIQT--KLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAID--PAKV 732
Cdd:PRK06155 188 TSGTTGPSKGVCCPHAQF--YWWGRNSaeDLEIGADDVLYTTLPLFHTNALNAFFQALLAGATYVLEPRFSASGfwPAVR 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 733 EeivQGKAIDWY--KITPSHLKALSSESGTKLFPRKGLILGGEAsewswikEIYRNIPASC--KLFNHYGPSETTIGVAV 808
Cdd:PRK06155 266 R---HGATVTYLlgAMVSILLSQPARESDRAHRVRVALGPGVPA-------ALHAAFRERFgvDLLDGYGSTETNFVIAV 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 809 YEVTKKGLSnqfsttpIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQ---VARGYLNREELTAERFMEDPFitdsrm 885
Cdd:PRK06155 336 THGSQRPGS-------MGRLAPGFEARVVDEHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAWRNLWF------ 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 886 yKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAivTVTKVRNE----EQLVAYYVSKKEVLD- 960
Cdd:PRK06155 403 -HTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAA--AVFPVPSElgedEVMAAVVLRDGTALEp 479
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 497785100 961 KDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEIQVS 1005
Cdd:PRK06155 480 VALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLREQGVT 524
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
656-1002 |
1.39e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 79.10 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 656 YTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQS-----LA-------YDF---CLTTI------------ 708
Cdd:PRK12492 214 YTGGTTGLAKGAMLTHGNLVANMLQVRACLSQLGPDGQPLMKEgqevmIAplplyhiYAFtanCMCMMvsgnhnvlitnp 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 709 --------------YTSLLSGGTLFFLLKEDAidpakveeivQGKAIDWykitpSHLKALSSeSGTKLfprkgliLGGEA 774
Cdd:PRK12492 294 rdipgfikelgkwrFSALLGLNTLFVALMDHP----------GFKDLDF-----SALKLTNS-GGTAL-------VKATA 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 775 SEWSWIkeiyrnipASCKLFNHYGPSETTigvAVYEVTKKGLSNQFSTtpIGSSLSNNRIYILDDKLRPVPSGIPGHIYI 854
Cdd:PRK12492 351 ERWEQL--------TGCTIVEGYGLTETS---PVASTNPYGELARLGT--VGIPVPGTALKVIDDDGNELPLGERGELCI 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 855 AGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE 934
Cdd:PRK12492 418 KGPQVMKGYWQQPEATAEALDAEGW------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVAN 491
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 935 -AIVTVTKVRNEEQLVAYYVSKKEVLDKD-LQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:PRK12492 492 cAAIGVPDERSGEAVKLFVVARDPGLSVEeLKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
520-1002 |
1.49e-14 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 79.29 E-value: 1.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIqLQPCAKAIIAMLGVLKAGGAYL-PLDVESPKERIEII 598
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSV-LAPNTPAMYEMHFAVPMAGAVLnPINTRLDATSIAAI 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAIITHSEYK----------TSYEGY-EVPILYIDQLDdFLLDEREDNLNVDC-------DSSQLAYGI----- 655
Cdd:PLN03102 107 LRHAKPKILFVDRSFEplarevlhllSSEDSNlNLPVIFIHEID-FPKRPSSEELDYECliqrgepTPSLVARMFriqde 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 656 -------YTSGSTGIPKGVLVEHRN--LSNYIYAIQTKLGNKPkdryLLLQSLAYDFC--LTTIYTSLLSGGTlffllkE 724
Cdd:PLN03102 186 hdpislnYTSGTTADPKGVVISHRGayLSTLSAIIGWEMGTCP----VYLWTLPMFHCngWTFTWGTAARGGT------S 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 725 DAIDPAKVEEIVqgKAIDWYKIT-----PSHLKALSSESGTKLFPRKG---LILGGEASEWSWIKEIYRnipASCKLFNH 796
Cdd:PLN03102 256 VCMRHVTAPEIY--KNIEMHNVThmccvPTVFNILLKGNSLDLSPRSGpvhVLTGGSPPPAALVKKVQR---LGFQVMHA 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 797 YGPSETTIGVAVYEVT---KKGLSNQFSTTPIGSSLSNNRIYILDDKLRPVPSGIP------GHIYIAGEQVARGYLNRE 867
Cdd:PLN03102 331 YGLTEATGPVLFCEWQdewNRLPENQQMELKARQGVSILGLADVDVKNKETQESVPrdgktmGEIVIKGSSIMKGYLKNP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 868 ELTAERFMEDpfitdsrMYKTGDIGKILYTGEIQFLGR-----LDGQVKIRGIRVE------PEEIQSQLLS--HPSITE 934
Cdd:PLN03102 411 KATSEAFKHG-------WLNTGDVGVIHPDGHVEIKDRskdiiISGGENISSVEVEnvlykyPKVLETAVVAmpHPTWGE 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 935 AIVTVTKVRNEEQLVAYYVSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:PLN03102 484 TPCAFVVLEKGETTKEDRVDKLVTRERDLIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKLRDI 551
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1582-2045 |
1.54e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 79.15 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1582 RFLDR--------SYTYDEVNKRANKIANQLY-KMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRD 1652
Cdd:PRK08751 37 KFADRpayhsfgkTITYREADQLVEQFAAYLLgELQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1653 FILKDASVGAIVTQ----TSLEEKLSKSDLPYLCTDQSQD--------------------SEDYSL-------------- 1694
Cdd:PRK08751 117 HQLIDSGASVLVVIdnfgTTVQQVIADTPVKQVITTGLGDmlgfpkaalvnfvvkyvkklVPEYRIngairfrealalgr 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1695 ---LTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSS-VMNLISATiDEFNITQETKVGQFATISfDASLWQILmALLA-- 1768
Cdd:PRK08751 197 khsMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNlVANMQQAH-QWLAGTGKLEEGCEVVIT-ALPLYHIF-ALTAng 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1769 ------GATLCVVSREEQLST--KALvKRFRDWNVT--------LADLPPvvLDSIlpeDIPSLQTVSTGGERCPIKVAK 1832
Cdd:PRK08751 274 lvfmkiGGCNHLISNPRDMPGfvKEL-KKTRFTAFTgvntlfngLLNTPG--FDQI---DFSSLKMTLGGGMAVQRSVAE 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1833 RWS--LDRNFYNVYGPTETTIATtwyrVSSPECVQD-SVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYL 1909
Cdd:PRK08751 348 RWKqvTGLTLVEAYGLTETSPAA----CINPLTLKEyNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYW 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1910 NRDDLNEKRFiphpfrEEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQ 1989
Cdd:PRK08751 424 KRPEETAKVM------DADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEK 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 497785100 1990 NYHTLVAYVVPHGEWEEKKIIEE-LRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK08751 498 SGEIVKVVIVKKDPALTAEDVKAhARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1014-1089 |
2.90e-14 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 69.88 E-value: 2.90e-14
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497785100 1014 PMNRLEEKMKDVWEKILERPVPSI--DDSFFK-LGGHSLLATRLVSMIRKEFKVELSIKEFFEKPSIRELSTHLLQLEA 1089
Cdd:COG0236 2 PREELEERLAEIIAEVLGVDPEEItpDDSFFEdLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1589-1968 |
3.15e-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: 77.91 E-value: 3.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSElplNRRDFILKDASVGaivtqts 1668
Cdd:cd05908 17 SYRHLREEALGYLGALQELGIKPGQEVVFQITHNNKFLYLFWACLLGGMIAVPVSIG---SNEEHKLKLNKVW------- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1669 leEKLSKsdlPYLCTDqsqdsedyslLTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVG 1748
Cdd:cd05908 87 --NTLKN---PYLITE----------EEVLCELADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRIL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1749 QFATISFDaslwqilMALLAGATLCVVSREEQL--STKALVKRFRDW-------NVTLADLP----PVVLDSILPE---- 1811
Cdd:cd05908 152 SWMPLTHD-------MGLIAFHLAPLIAGMNQYlmPTRLFIRRPILWlkkasehKATIVSSPnfgyKYFLKTLKPEkand 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1812 -DIPSLQTVSTGGErcPIKVA---------KRWSLDRN-FYNVYGPTETTIATTWYRVSSP--------ECVQDSVPI-- 1870
Cdd:cd05908 225 wDLSSIRMILNGAE--PIDYElchefldhmSKYGLKRNaILPVYGLAEASVGASLPKAQSPfktitlgrRHVTHGEPEpe 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1871 --------------GTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPFreeeilYKTGDI 1936
Cdd:cd05908 303 vdkkdsecltfvevGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW------LKTGDL 376
|
410 420 430
....*....|....*....|....*....|..
gi 497785100 1937 GkVLHDGNLEHLGRLDHQIKVRGFRIELGEIE 1968
Cdd:cd05908 377 G-FIRNGRLVITGREKDIIFVNGQNVYPHDIE 407
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1550-1910 |
3.28e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 77.93 E-value: 3.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1550 VKKAESQPRsIKDCIQYSFENWVRSSPNHIALRFLDRS--YTYDEVNKRANKIANQLYKMGIRRGDRVALY-HERSSEMI 1626
Cdd:PRK08315 5 VRGPTDVPL-LEQTIGQLLDRTAARYPDREALVYRDQGlrWTYREFNEEVDALAKGLLALGIEKGDRVGIWaPNVPEWVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1627 FGFlGILKCGAAYVPID-----SELplnrrDFILKDASVGAIVT--------------------QTSLEEKLSKSDLP-- 1679
Cdd:PRK08315 84 TQF-ATAKIGAILVTINpayrlSEL-----EYALNQSGCKALIAadgfkdsdyvamlyelapelATCEPGQLQSARLPel 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1680 ----YLCTDQSQDSEDYSLLTKDKSYPEDIAY--------------IIYTSGTTGTPNGVMVKHSSVMN---LISATIde 1738
Cdd:PRK08315 158 rrviFLGDEKHPGMLNFDELLALGRAVDDAELaarqatldpddpinIQYTSGTTGFPKGATLTHRNILNngyFIGEAM-- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1739 fNITQETKV--------------GQFATISFDASLWQILMALLAGATLCVVSREEQLStkalvkrfrdwnvtLADLPPV- 1803
Cdd:PRK08315 236 -KLTEEDRLcipvplyhcfgmvlGNLACVTHGATMVYPGEGFDPLATLAAVEEERCTA--------------LYGVPTMf 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1804 --VLDsiLPE----DIPSLQTVSTGGERCPIKVAKRWSLDRNFYNV---YGPTETTIATTWYRVSSPECVQDSVpIGTPV 1874
Cdd:PRK08315 301 iaELD--HPDfarfDLSSLRTGIMAGSPCPIEVMKRVIDKMHMSEVtiaYGMTETSPVSTQTRTDDPLEKRVTT-VGRAL 377
|
410 420 430
....*....|....*....|....*....|....*..
gi 497785100 1875 PNTEVFILDPDLN-PVPMGVIGEIYIGGVGVSNGYLN 1910
Cdd:PRK08315 378 PHLEVKIVDPETGeTVPRGEQGELCTRGYSVMKGYWN 414
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
835-1084 |
3.61e-14 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 75.56 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 835 YILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERfmedPFITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRG 914
Cdd:COG3433 32 LIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFI----PVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQQVV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 915 IRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQ----LVAYYVSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHA 990
Cdd:COG3433 108 IRAERGEEEELLLVLRAAAVVRVAVLAALRGAGvgllLIVGAVAALDGLAAAAALAALDKVPPDVVAASAVVALDALLLL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 991 HGKIDRKALPEIQVSNWNEIEIQP-----MNRLEEKMKDVWEKILERPVPSI--DDSFFKLGGHSLLATRLVSMIRKEFk 1063
Cdd:COG3433 188 ALKVVARAAPALAAAEALLAAASPapaleTALTEEELRADVAELLGVDPEEIdpDDNLFDLGLDSIRLMQLVERWRKAG- 266
|
250 260
....*....|....*....|.
gi 497785100 1064 VELSIKEFFEKPSIRELSTHL 1084
Cdd:COG3433 267 LDVSFADLAEHPTLAAWWALL 287
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
520-1000 |
3.95e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 77.73 E-value: 3.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIIT 599
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 600 QDSKLKAIITHSEYKTSYEGYEVPILYIDQLDDflldEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIY 679
Cdd:PRK13383 129 RAHHISTVVADNEFAERIAGADDAVAVIDPATA----GAEESGGRPAVAAPGRIVLLTSGTTGKPKGVPRAPQLRSAVGV 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 680 AI----QTKLgnKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDA-----------IDPAKVEEIVQGKAIDwy 744
Cdd:PRK13383 205 WVtildRTRL--RTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTHRHFDAeaalaqaslhrADAFTAVPVVLARILE-- 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 745 kiTPSHLKALSS--------ESGTKLFPRKGlilggeasewSWIKEIYRNIpasckLFNHYGPSETTIGVAVyevTKKGL 816
Cdd:PRK13383 281 --LPPRVRARNPlpqlrvvmSSGDRLDPTLG----------QRFMDTYGDI-----LYNGYGSTEVGIGALA---TPADL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 817 SNQFSTtpIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREeltaerfmeDPFITDSrMYKTGDIGKILY 896
Cdd:PRK13383 341 RDAPET--VGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGG---------GKAVVDG-MTSTGDMGYLDN 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 897 TGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKKEV-LDKD-LQTYLKQKLPP 973
Cdd:PRK13383 409 AGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADnAVIGVPDERFGHRLAAFVVLHPGSgVDAAqLRDYLKDRVSR 488
|
490 500
....*....|....*....|....*..
gi 497785100 974 NLVPAYLVKMDTLPRHAHGKIDRKALP 1000
Cdd:PRK13383 489 FEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1579-1959 |
5.39e-14 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 77.47 E-value: 5.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1579 IALRFLDRSY---------TYDEVNKRANKIANQLYKMgIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDS-ELP- 1647
Cdd:PRK12476 51 VAYRYLDHSHsaagcavelTWTQLGVRLRAVGARLQQV-AGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLFApELPg 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 -LNRRDFILKDASVGAIVTQTSLEE-------KLSKSDLPYLCT-DQSQDS--EDYSLLTKDKsypEDIAYIIYTSGTTG 1716
Cdd:PRK12476 130 hAERLDTALRDAEPTVVLTTTAAAEavegflrNLPRLRRPRVIAiDAIPDSagESFVPVELDT---DDVSHLQYTSGSTR 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1717 TPNGVMVKHSSVM-NLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATLCVVS-----REEQLSTKALVKRF 1790
Cdd:PRK12476 207 PPVGVEITHRAVGtNLVQMILSIDLLDRNTHGVSWLPLYHDMGLSMIGFPAVYGGHSTLMSptafvRRPQRWIKALSEGS 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1791 RDWNVTLA---------------------DLPPVVLdsilpedIPSLQTVSTGGERCPIKVAKRWSLDRN-FYNVYGPTE 1848
Cdd:PRK12476 287 RTGRVVTAapnfayewaaqrglpaegddiDLSNVVL-------IIGSEPVSIDAVTTFNKAFAPYGLPRTaFKPSYGIAE 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1849 TT--IATT------------------WYRVSSPECVQDSVP---IGTPVPNTEVFILDPDL-NPVPMGVIGEIYIGGVGV 1904
Cdd:PRK12476 360 ATlfVATIapdaepsvvyldreqlgaGRAVRVAADAPNAVAhvsCGQVARSQWAVIVDPDTgAELPDGEVGEIWLHGDNI 439
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497785100 1905 SNGYLNRDDLNEKRF-------IP---HPFREEE--ILYKTGDIGKVLhDGNLEHLGRLDHQIKVRG 1959
Cdd:PRK12476 440 GRGYWGRPEETERTFgaklqsrLAegsHADGAADdgTWLRTGDLGVYL-DGELYITGRIADLIVIDG 505
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
529-995 |
5.43e-14 |
|
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: 77.09 E-value: 5.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 529 ERSYTYLQTNNRANQIARWLQKQ-GIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAylpldvespkerIEIITQDSKLKAI 607
Cdd:cd05937 3 GKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAA------------PAFINYNLSGDPL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 608 ItHSeYKTSyegyEVPILYIDQLDDFLLderednlnvdcdssqlaygIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGN 687
Cdd:cd05937 71 I-HC-LKLS----GSRFVIVDPDDPAIL-------------------IYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 688 KPKDRYL----LLQSLAYDFCLTTIytsLLSGGTLFFLLK-------EDAIDPAKVeeIVQ--GKAIDWYKITPSHLK-- 752
Cdd:cd05937 126 KNGDRTYtcmpLYHGTAAFLGACNC---LMSGGTLALSRKfsasqfwKDVRDSGAT--IIQyvGELCRYLLSTPPSPYdr 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 753 ----------ALSSESGTKLFPRKGLilggeasewSWIKEIYRNIPASCKLFNHYGPSETTIGVAVY-EVTKKGLSNQFs 821
Cdd:cd05937 201 dhkvrvawgnGLRPDIWERFRERFNV---------PEIGEFYAATEGVFALTNHNVGDFGAGAIGHHgLIRRWKFENQV- 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 822 tTPIGSSLSNNRIYiLDDK---LRPVPSGIPGHIYIA----GEQVARGYLNREELTAERFMEDPFITDSRMYKTGDIGKI 894
Cdd:cd05937 271 -VLVKMDPETDDPI-RDPKtgfCVRAPVGEPGEMLGRvpfkNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLLRQ 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 895 LYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLV--AYYVSKKEVLDKD------LQTY 966
Cdd:cd05937 349 DADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVKVPGHDGRAgcAAITLEESSAVPTeftkslLASL 428
|
490 500 510
....*....|....*....|....*....|..
gi 497785100 967 LKQKLPPNLVPAYL---VKMDTLPRHAHGKID 995
Cdd:cd05937 429 ARKNLPSYAVPLFLrltEEVATTDNHKQQKGV 460
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1584-1968 |
6.01e-14 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 77.35 E-value: 6.01e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1584 LDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRD-FI------LK 1656
Cdd:PRK09192 46 LEEALPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLPLPMGFGGREsYIaqlrgmLA 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1657 DASVGAIVTQTSLEEKLSK----SDLPYLCTDQSQDSEDYSLLTKDKSYPEDIAYIIYTSGTTGTPNGVMVKHSSVM-NL 1731
Cdd:PRK09192 126 SAQPAAIITPDELLPWVNEathgNPLLHVLSHAWFKALPEADVALPRPTPDDIAYLQYSSGSTRFPRGVIITHRALMaNL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1732 ISATIDEFNITQETKVGQFATISFDASLWQILMALLAgatlCVVSrEEQLSTKALVKRFRDW-------NVTLADLPPVV 1804
Cdd:PRK09192 206 RAISHDGLKVRPGDRCVSWLPFYHDMGLVGFLLTPVA----TQLS-VDYLPTRDFARRPLQWldlisrnRGTISYSPPFG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1805 LD---------SILPEDIPSLQTVSTGGERCPIKVAKRWSL--------DRNFYNVYGPTETTIATTW------YRV--- 1858
Cdd:PRK09192 281 YElcarrvnskDLAELDLSCWRVAGIGADMIRPDVLHQFAEafapagfdDKAFMPSYGLAEATLAVSFsplgsgIVVeev 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1859 ---------------SSPECVQDSVPIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYlnrddlnekrfiphp 1923
Cdd:PRK09192 361 drdrleyqgkavapgAETRRVRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGY--------------- 425
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 497785100 1924 FREEEI--------LYKTGDIGKVLhDGNLEHLGRLDHQIKVRGFRIELGEIE 1968
Cdd:PRK09192 426 FRDEESqdvlaadgWLDTGDLGYLL-DGYLYITGRAKDLIIINGRNIWPQDIE 477
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
656-950 |
6.68e-14 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 77.15 E-value: 6.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 656 YTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAidpAKVEEI 735
Cdd:PLN02860 179 FTSGTTGRPKGVTISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLLPKFDA---KAALQA 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 736 VQGKAIDWYKITPS---HLKALSSESGT-KLFPRKGLILGGEASEWSWIKEIYRNIPASCKLFNHYGPSETTIG---VAV 808
Cdd:PLN02860 256 IKQHNVTSMITVPAmmaDLISLTRKSMTwKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEACSSltfMTL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 809 YEVTKKGLSNQFSTTPIGSSLSNN--------------RIYILDDKLRPVpsgipGHIYIAGEQVARGYLNREELTAERF 874
Cdd:PLN02860 336 HDPTLESPKQTLQTVNQTKSSSVHqpqgvcvgkpaphvELKIGLDESSRV-----GRILTRGPHVMLGYWGQNSETASVL 410
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497785100 875 MEDPFItdsrmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVT-VTKVRNEEQLVA 950
Cdd:PLN02860 411 SNDGWL------DTGDIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVgVPDSRLTEMVVA 481
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
1589-2045 |
1.25e-13 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 76.36 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLY-KMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQT 1667
Cdd:PRK05620 40 TFAAIGARAAALAHALHdELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVADP 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1668 SLEEKLSK--SDLP------YLCTDQSQDSE----------DYSLLTKDKS----YPE----DIAYIIYTSGTTGTPNGV 1721
Cdd:PRK05620 120 RLAEQLGEilKECPcvravvFIGPSDADSAAahmpegikvySYEALLDGRStvydWPEldetTAAAICYSTGTTGAPKGV 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1722 MVKHSSV----MNLISAtiDEFNITQETK----VGQFATISfdaslWQI-LMALLAGATLcvVSREEQLSTKALVKRFRD 1792
Cdd:PRK05620 200 VYSHRSLylqsLSLRTT--DSLAVTHGESflccVPIYHVLS-----WGVpLAAFMSGTPL--VFPGPDLSAPTLAKIIAT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1793 WNVTLADLPPVVLDSIL-------PEDIpSLQTVSTGGERCPIKVAKRWSlDR---NFYNVYGPTET----TIA------ 1852
Cdd:PRK05620 271 AMPRVAHGVPTLWIQLMvhylknpPERM-SLQEIYVGGSAVPPILIKAWE-ERygvDVVHVWGMTETspvgTVArppsgv 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1853 ---TTW-YRVSspecvQDSVPIGTP--VPNTEVFILDPDLNPvpmgviGEIYIGGVGVSNGYLnRDDLNEKRFIPHPFRE 1926
Cdd:PRK05620 349 sgeARWaYRVS-----QGRFPASLEyrIVNDGQVMESTDRNE------GEIQVRGNWVTASYY-HSPTEEGGGAASTFRG 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1927 EEILY-----------KTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYH--- 1992
Cdd:PRK05620 417 EDVEDandrftadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGErpl 496
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 1993 --TLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK05620 497 avTVLAPGIEPTRETAERLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
501-1002 |
1.45e-13 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 76.06 E-value: 1.45e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 501 KPFPT------EPIHVQ-FEGQVLN------------TPNSIAL------SDHERSYTYLQTNNRANQIARWLQKQGIGK 555
Cdd:cd05966 29 KPWDKvldwskGPPFIKwFEGGKLNisyncldrhlkeRGDKVAIiwegdePDQSRTITYRELLREVCRFANVLKSLGVKK 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 556 EDFIGIQLQPCAKAIIAMLGVLKAG-------GAYLPldvESPKERIE------IITQDS--------KLKAII------ 608
Cdd:cd05966 109 GDRVAIYMPMIPELVIAMLACARIGavhsvvfAGFSA---ESLADRINdaqcklVITADGgyrggkviPLKEIVdealek 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 609 ----------THSEYKTSY-EGYEVPilyidqLDDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLveHRNLSNY 677
Cdd:cd05966 186 cpsvekvlvvKRTGGEVPMtEGRDLW------WHDLMAKQSPECEPEWMDSEDPLFILYTSGSTGKPKGVV--HTTGGYL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 678 IYAIQTK---LGNKPKDRYlllqslaydFCLTTI----------YTSLLSGGTLffLLKEDAI---DPAKVEEIvqgkaI 741
Cdd:cd05966 258 LYAATTFkyvFDYHPDDIY---------WCTADIgwitghsyivYGPLANGATT--VMFEGTPtypDPGRYWDI-----V 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 742 DWYKIT-----PSHLKALSS--ESGTKLFPRKGL-ILG--GE---ASEWSWikeiyrnipasckLFNHYGPSETTIgVAV 808
Cdd:cd05966 322 EKHKVTifytaPTAIRALMKfgDEWVKKHDLSSLrVLGsvGEpinPEAWMW-------------YYEVIGKERCPI-VDT 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 809 YEVTKKGlSNQFSTTPIGSSL---SNNR------IYILDDKLRPVPSGIPGhiYIAGEQ----VARGYLNREEltaeRFM 875
Cdd:cd05966 388 WWQTETG-GIMITPLPGATPLkpgSATRpffgiePAILDEEGNEVEGEVEG--YLVIKRpwpgMARTIYGDHE----RYE 460
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 876 EDPFITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVS 954
Cdd:cd05966 461 DTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEaAVVGRPHDIKGEAIYAFVTL 540
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|...
gi 497785100 955 K-----KEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:cd05966 541 KdgeepSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIMRRILRKI 593
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
888-1000 |
1.72e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 75.07 E-value: 1.72e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 888 TGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVtVTKVRN--EEQLVAYYVSKKEVLDKDLQT 965
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVV-YRGKDPvaGERVKAKVISHEEIDPVQLRE 373
|
90 100 110
....*....|....*....|....*....|....*
gi 497785100 966 YLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALP 1000
Cdd:PRK08308 374 WCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1571-2000 |
1.95e-13 |
|
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); Acetyl-CoA synthetase (ACS, EC 6.2.1.1, acetate#CoA ligase or acetate:CoA ligase (AMP-forming)) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is widely present in all living organisms. The activity of this enzyme is crucial for maintaining the required levels of acetyl-CoA, a key intermediate in many important biosynthetic and catabolic processes. Acetyl-CoA is used in the biosynthesis of glucose, fatty acids, and cholesterol. It can also be used in the production of energy in the citric acid cycle. Eukaryotes typically have two isoforms of acetyl-CoA synthetase, a cytosolic form involved in biosynthetic processes and a mitochondrial form primarily involved in energy generation.
Pssm-ID: 341270 [Multi-domain] Cd Length: 608 Bit Score: 75.68 E-value: 1.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1571 WVRSSPNHIALRF------LDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPI-- 1642
Cdd:cd05966 62 HLKERGDKVAIIWegdepdQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVfa 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1643 ------------DSELPL-------NRRDFI--LK---DASVGA--------IVTQTSLEEKLSKS-DLPY--LCTDQSQ 1687
Cdd:cd05966 142 gfsaesladrinDAQCKLvitadggYRGGKVipLKeivDEALEKcpsvekvlVVKRTGGEVPMTEGrDLWWhdLMAKQSP 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1688 DSEDYSLltkDksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATID-EFNITQETKVGQFATISfdaslW-----Q 1761
Cdd:cd05966 222 ECEPEWM---D---SEDPLFILYTSGSTGKPKGVVHTTGGYLLYAATTFKyVFDYHPDDIYWCTADIG-----WitghsY 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1762 ILMA-LLAGATlCVVSreEQLSTKALVKRFRD----WNVTLADLPPVVLDSIL--PEDIP------SLQTVSTGGErcPI 1828
Cdd:cd05966 291 IVYGpLANGAT-TVMF--EGTPTYPDPGRYWDivekHKVTIFYTAPTAIRALMkfGDEWVkkhdlsSLRVLGSVGE--PI 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1829 KV-AKRWsldrnFYNVYGPTETTIATTWYR-------VSSPECVQDSVP--IGTPVPNTEVFILDPDLNPVPMGVIGEIY 1898
Cdd:cd05966 366 NPeAWMW-----YYEVIGKERCPIVDTWWQtetggimITPLPGATPLKPgsATRPFFGIEPAILDEEGNEVEGEVEGYLV 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1899 IGGV--GVSNGYLNrddlNEKRFIPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTG 1976
Cdd:cd05966 441 IKRPwpGMARTIYG----DHERYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPA 516
|
490 500
....*....|....*....|....
gi 497785100 1977 VKEAIVQPLGDNQNYHTLVAYVVP 2000
Cdd:cd05966 517 VAEAAVVGRPHDIKGEAIYAFVTL 540
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
84-383 |
1.97e-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: 74.83 E-value: 1.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 84 VNIEALKKSFEQIVNRHQILRMRVkqTEDSIEQVITKS-EPTIQFLSLRGISGEEQQEILSEYcRKE-ANYPYRLEQENL 161
Cdd:cd19535 37 LDPDRLERAWNKLIARHPMLRAVF--LDDGTQQILPEVpWYGITVHDLRGLSEEEAEAALEEL-RERlSHRVLDVERGPL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 162 IRMSIIELSESSYSVLFSRHHILSDGWSASILLSELERFYNmysqngeiNPEQSQEELTIQYHDYALWQEKLLTSEnLEK 241
Cdd:cd19535 114 FDIRLSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYE--------DPGEPLPPLELSFRDYLLAEQALRETA-YER 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 242 GLEYWKEKLEgDLPM-----LSIGGITQEGTGVgSEYNFKIPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETD 316
Cdd:cd19535 185 ARAYWQERLP-TLPPapqlpLAKDPEEIKEPRF-TRREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARWSGQPR 262
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497785100 317 LAVGTPIAGRN--IRETRNVIGPFINTVVIRTKAEQNLSVIEYLQQVHETTIQALENQDVPfeKVVEVL 383
Cdd:cd19535 263 FLLNLTLFNRLplHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHSSYS--GVVVVR 329
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1020-1079 |
3.24e-13 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 66.05 E-value: 3.24e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497785100 1020 EKMKDVWEKILERPVPSI--DDSFFKLGGHSLLATRLVSMIRKEFKVELSIKEFFEKPSIRE 1079
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIdpDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1585-1982 |
4.31e-13 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 73.93 E-value: 4.31e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1585 DRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIV 1664
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 TqtsleeklsksdlpylctdqsqdsedyslltkdksypeDIAYIIYTSGTTGTPNGVMVKHSSVMNLisatidefnitqe 1744
Cdd:cd05940 81 V--------------------------------------DAALYIYTSGTTGLPKAAIISHRRAWRG------------- 109
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1745 TKVGQFATISFDASLWQILMALL--AGATLCVVSREEQLSTKALVKRF---------RDWNVT-----------LADLPP 1802
Cdd:cd05940 110 GAFFAGSGGALPSDVLYTCLPLYhsTALIVGWSACLASGATLVIRKKFsasnfwddiRKYQATifqyigelcryLLNQPP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1803 VvldsilPEDIP-SLQTVSTGGERCPI--KVAKRWSLDRnFYNVYGPTETTIAtTWYRVSSPECVQDSVPIGTPVPNTEV 1879
Cdd:cd05940 190 K------PTERKhKVRMIFGNGLRPDIweEFKERFGVPR-IAEFYAATEGNSG-FINFFGKPGAIGRNPSLLRKVAPLAL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1880 FILDPD-----------LNPVPMGVIGE-IY-IGGVGVSNGYLNRDDLNEKRfIPHPFREEEILYKTGDIGKVLHDGNLE 1946
Cdd:cd05940 262 VKYDLEsgepirdaegrCIKVPRGEPGLlISrINPLEPFDGYTDPAATEKKI-LRDVFKKGDAWFNTGDLMRLDGEGFWY 340
|
410 420 430
....*....|....*....|....*....|....*.
gi 497785100 1947 HLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIV 1982
Cdd:cd05940 341 FVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANV 376
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
655-937 |
4.73e-13 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 72.72 E-value: 4.73e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 655 IYTSGSTGIPKGVLVEHRNL--SNYIYAIQTKLGNKPkdRYL----LLQSLAYDFCLTTiytsLLSGGTLFFLLKedaID 728
Cdd:cd17636 6 IYTAAFSGRPNGALLSHQALlaQALVLAVLQAIDEGT--VFLnsgpLFHIGTLMFTLAT----FHAGGTNVFVRR---VD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 729 PAKVEEIVQGKAIDWYKITPSHLKALSSESGTKLFPRKGLILGGEASEWSwikeiyRNIPASCKLFNH----YGPSETTi 804
Cdd:cd17636 77 AEEVLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEWN------DMATVDTSPWGRkpggYGQTEVM- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 805 GVAVYE-VTKKGLSNQFSTTPIGsslsnnRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFMedpfitdS 883
Cdd:cd17636 150 GLATFAaLGGGAIGGAGRPSPLV------QVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR-------G 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 497785100 884 RMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIV 937
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAV 270
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
1585-1726 |
4.95e-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: 74.00 E-value: 4.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1585 DRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIV 1664
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497785100 1665 TQTSLEEKLSKSDLPYLCTDQSQDsedyslltkdksypeDIAYIIYTSGTTGTPNGVMVKHS 1726
Cdd:cd05939 81 FNLLDPLLTQSSTEPPSQDDVNFR---------------DKLFYIYTSGTTGLPKAAVIVHS 127
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1702-2041 |
5.19e-13 |
|
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: 72.80 E-value: 5.19e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1702 PEDIaYIIYTSGTTGTPNGVMVKH----SSVMNLISATIDEFNITQET---KVGQFATISFDA-------SLWQILMALL 1767
Cdd:cd05924 3 ADDL-YILYTGGTTGMPKGVMWRQedifRMLMGGADFGTGEFTPSEDAhkaAAAAAGTVMFPApplmhgtGSWTAFGGLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1768 AGATLCVVSREeqLSTKALVKRFRDWNVTL------ADLPPVV--LDSILPEDIPSLQTVSTGGERCPIKVAKRW---SL 1836
Cdd:cd05924 82 GGQTVVLPDDR--FDPEEVWRTIEKHKVTSmtivgdAMARPLIdaLRDAGPYDLSSLFAISSGGALLSPEVKQGLlelVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1837 DRNFYNVYGPTETTIATTwyrVSSPECVQDSVPIGTPVPNTEVfiLDPDLNPVPMGVIGEIYIGGVG-VSNGYLNRDDLN 1915
Cdd:cd05924 160 NITLVDAFGSSETGFTGS---GHSAGSGPETGPFTRANPDTVV--LDDDGRVVPPGSGGVGWIARRGhIPLGYYGDEAKT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1916 EKRFiphpFREEEILYK-TGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDnQNYHTL 1994
Cdd:cd05924 235 AETF----PEVDGVRYAvPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPD-ERWGQE 309
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 497785100 1995 VAYVV---PHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVD 2041
Cdd:cd05924 310 VVAVVqlrEGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
533-930 |
5.95e-13 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 73.79 E-value: 5.95e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 533 TYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGgaylpldvespkerIEIITQDSKL--KAIItH 610
Cdd:cd17639 7 SYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN--------------IPIVTVYATLgeDALI-H 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 611 SEYKTsyegyEVPILYIDQlddfllderednlnvdcDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGN--K 688
Cdd:cd17639 72 SLNET-----ECSAIFTDG-----------------KPDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPEllG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 689 PKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFF-----LLkeDAI------D------------PAKVEEIVQG------- 738
Cdd:cd17639 130 PDDRYLAYLPLAHIFELAAENVCLYRGGTIGYgsprtLT--DKSkrgckgDltefkptlmvgvPAIWDTIRKGvlaklnp 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 739 -----KAIDW--YKitpSHLKALSSESGTKLF-------PRKGL------ILGG------EASEWSwikeiyrNIpASCK 792
Cdd:cd17639 208 mgglkRTLFWtaYQ---SKLKALKEGPGTPLLdelvfkkVRAALggrlryMLSGgaplsaDTQEFL-------NI-VLCP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 793 LFNHYGPSETTIGVAVYEVtkkglsNQFSTTPIGSSLSNNRIYILD-DKLRPVPSGIP--GHIYIAGEQVARGYLNREEL 869
Cdd:cd17639 277 VIQGYGLTETCAGGTVQDP------GDLETGRVGPPLPCCEIKLVDwEEGGYSTDKPPprGEILIRGPNVFKGYYKNPEK 350
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497785100 870 TAERFMEDpfitdsRMYKTGDIGKILYTGEIQFLGRLDGQVKIR-GIRVEPEEIQSQLLSHP 930
Cdd:cd17639 351 TKEAFDGD------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNP 406
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1587-1961 |
5.99e-13 |
|
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: 73.92 E-value: 5.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1587 SYTYDEVNKRANKIANQLY-KMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVT 1665
Cdd:cd05905 14 TLTWGKLLSRAEKIAAVLQkKVGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVALT 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1666 QTSLEEKLSKSDLPYLCTDQSQDS---------EDYSLLTKDKSYP---------EDIAYIIYTSGTTGTPNGVMVKHSS 1727
Cdd:cd05905 94 VEACLKGLPKKLLKSKTAAEIAKKkgwpkildfVKIPKSKRSKLKKwgphpptrdGDTAYIEYSFSSDGSLSGVAVSHSS 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1728 VMNlISATIDEFNITQETKVgqFATI---SFDASLWQ-ILMALLAGATLCVVSREE-------------QLSTKALVKRF 1790
Cdd:cd05905 174 LLA-HCRALKEACELYESRP--LVTVldfKSGLGLWHgCLLSVYSGHHTILIPPELmktnpllwlqtlsQYKVRDAYVKL 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1791 RDWNVTLADLPPVVldSILPEDIPSLQTVSTggerCPIKVAKRWSLDR--NFYNVY---GPTETTIAT----------TW 1855
Cdd:cd05905 251 RTLHWCLKDLSSTL--ASLKNRDVNLSSLRM----CMVPCENRPRISScdSFLKLFqtlGLSPRAVSTefgtrvnpfiCW 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1856 YRVSSPE---------------------------CVQDSvpiGTPVPNTEVFILDPD-LNPVPMGVIGEIYIGGVGVSNG 1907
Cdd:cd05905 325 QGTSGPEpsrvyldmralrhgvvrlderdkpnslPLQDS---GKVLPGAQVAIVNPEtKGLCKDGEIGEIWVNSPANASG 401
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1908 YLNRDDLNEKRF------IPHPFREEEILYKTGDIGKVLH----DGNLEH------LGRLDHQIKVRGFR 1961
Cdd:cd05905 402 YFLLDGETNDTFkvfpstRLSTGITNNSYARTGLLGFLRPtkctDLNVEEhdllfvVGSIDETLEVRGLR 471
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
655-999 |
7.22e-13 |
|
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: 73.57 E-value: 7.22e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 655 IYTSGSTGIPKGVLVEHRNLSNYIYAI---QTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAidpak 731
Cdd:cd05929 131 LYSGGTTGRPKGIKRGLPGGPPDNDTLmaaALGFGPGADSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFDP----- 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 732 vEEIVQgkAIDWYKIT-----PSH---LKALSSESGTK--LFPRKGLILGGeASEWSWIKEIYrnI----PascKLFNHY 797
Cdd:cd05929 206 -EEFLR--LIERYRVTfaqfvPTMfvrLLKLPEAVRNAydLSSLKRVIHAA-APCPPWVKEQW--IdwggP---IIWEYY 276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 798 GPSETtIGVAVYE----VTKKGLSNQfsttPIGSslsnnRIYILDDKLRPVPSGIPGHIYIAGEQvARGYLNREELTAER 873
Cdd:cd05929 277 GGTEG-QGLTIINgeewLTHPGSVGR----AVLG-----KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAA 345
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 874 FMEDPFITdsrmykTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTvtKVRNEE---QLVA 950
Cdd:cd05929 346 RNEGGWST------LGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVV--GVPDEElgqRVHA 417
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 497785100 951 YY-----VSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05929 418 VVqpapgADAGTALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1589-1974 |
8.76e-13 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 73.90 E-value: 8.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVG-AIVTQT 1667
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGLYCVPLYDTLGAGAVEFIISHSEVSiVFVEEK 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1668 SLEE--KLSKSDLPYLCT---------DQSQDSEDYSL----------LTKDKSY------PEDIAYIIYTSGTTGTPNG 1720
Cdd:PLN02614 161 KISElfKTCPNSTEYMKTvvsfggvsrEQKEEAETFGLviyawdeflkLGEGKQYdlpikkKSDICTIMYTSGTTGDPKG 240
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1721 VMVKHSSVMNLISATI-------------DEF-----------NITQETKVGQFATISF---DASLWQILMALLAGATLC 1773
Cdd:PLN02614 241 VMISNESIVTLIAGVIrllksanaaltvkDVYlsylplahifdRVIEECFIQHGAAIGFwrgDVKLLIEDLGELKPTIFC 320
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1774 VVSR---------EEQLSTKALVKRFrdwnvtladlppvVLDSILPEDIPSLQTVSTGGERCPI-------KV------- 1830
Cdd:PLN02614 321 AVPRvldrvysglQKKLSDGGFLKKF-------------VFDSAFSYKFGNMKKGQSHVEASPLcdklvfnKVkqglggn 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1831 --------AKRWSLDRNFYNV---------YGPTETTIATTwyrVSSPECVQDSVPIGTPVPNTEVFILD-PDLNPVPMG 1892
Cdd:PLN02614 388 vriilsgaAPLASHVESFLRVvacchvlqgYGLTESCAGTF---VSLPDELDMLGTVGPPVPNVDIRLESvPEMEYDALA 464
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1893 VI--GEIYIGGVGVSNGYLNRDDLNEKRFIphpfreeEILYKTGDIGKVLHDGNLEHLGRldhqiKVRGFRIELGEIESL 1970
Cdd:PLN02614 465 STprGEICIRGKTLFSGYYKREDLTKEVLI-------DGWLHTGDVGEWQPNGSMKIIDR-----KKNIFKLSQGEYVAV 532
|
....
gi 497785100 1971 LNLQ 1974
Cdd:PLN02614 533 ENIE 536
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
532-937 |
2.13e-12 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 71.83 E-value: 2.13e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 532 YTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLP----LDVESPKERIEIitqdskLKAI 607
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPattlLTPDDLRDRVDR------GGAV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 608 ITHSEYKTSyegyevpilyidqlddfllderednlnvdCDSSQLAYgiYTSGSTGIPKgvLVEHRNLSNYIYAIQTK--L 685
Cdd:cd05974 75 YAAVDENTH-----------------------------ADDPMLLY--FTSGTTSKPK--LVEHTHRSYPVGHLSTMywI 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 686 GNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEivqgkAIDWYKIT-----PSHLKALSSE--S 758
Cdd:cd05974 122 GLKPGDVHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYARFDAKRVLA-----ALVRYGVTtlcapPTVWRMLIQQdlA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 759 GTKLFPRKgLILGGEASEWSWIKEIYRNIPASCKlfNHYGPSETT--IGVAVYEVTKKGlsnqfsttPIGSSLSNNRIYI 836
Cdd:cd05974 197 SFDVKLRE-VVGAGEPLNPEVIEQVRRAWGLTIR--DGYGQTETTalVGNSPGQPVKAG--------SMGRPLPGYRVAL 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 837 LDDKLRPVPSGIPGHIYIAGEQVA--RGYLNREELTAERfMEDPFitdsrmYKTGDIGKILYTGEIQFLGRLDGQVKIRG 914
Cdd:cd05974 266 LDPDGAPATEGEVALDLGDTRPVGlmKGYAGDPDKTAHA-MRGGY------YRTGDIAMRDEDGYLTYVGRADDVFKSSD 338
|
410 420
....*....|....*....|...
gi 497785100 915 IRVEPEEIQSQLLSHPSITEAIV 937
Cdd:cd05974 339 YRISPFELESVLIEHPAVAEAAV 361
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
520-1001 |
2.95e-12 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 71.45 E-value: 2.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHE-RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEII 598
Cdd:PRK07514 16 RDAPFIETPDgLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYF 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDSKLKAII----THSEYKTSYEGYEVPILYIdqLDDF----LLD----EREDNLNVDCDSSQLAYGIYTSGSTGIPKG 666
Cdd:PRK07514 96 IGDAEPALVVcdpaNFAWLSKIAAAAGAPHVET--LDADgtgsLLEaaaaAPDDFETVPRGADDLAAILYTSGTTGRSKG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 667 VLVEHRNL-SNYIyAIQTKLGNKPKDRylLLQSLAydfclttIY----------TSLLSGGTLFFLLKedaIDPAKVeei 735
Cdd:PRK07514 174 AMLSHGNLlSNAL-TLVDYWRFTPDDV--LIHALP-------IFhthglfvatnVALLAGASMIFLPK---FDPDAV--- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 736 vqgkaidwykitpshlkalssesgTKLFPRKGLILGgeasewswIKEIY----------RNIPASCKLF----------- 794
Cdd:PRK07514 238 ------------------------LALMPRATVMMG--------VPTFYtrllqeprltREAAAHMRLFisgsapllaet 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 795 --------NH-----YGPSETTIGVavyevtkkglSNQFSTTPIGSS----LSNNRIYILD-DKLRPVPSGIPGHIYIAG 856
Cdd:PRK07514 286 hrefqertGHailerYGMTETNMNT----------SNPYDGERRAGTvgfpLPGVSLRVTDpETGAELPPGEIGMIEVKG 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 857 EQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-A 935
Cdd:PRK07514 356 PNVFKGYWRMPEKTAEEFRADGF------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVEsA 429
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 936 IVTVTKVRNEEQLVAYYVSKKEV-LD-KDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPE 1001
Cdd:PRK07514 430 VIGVPHPDFGEGVTAVVVPKPGAaLDeAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
511-994 |
3.94e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 71.35 E-value: 3.94e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 511 QFEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVE- 589
Cdd:PRK07786 22 QLARHALMQPDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRl 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 590 SPKErIEIITQDSKLKAIITH-------SEYKTSYEGYEVPILYIDQLDDFLLDeREDNLN--------VDCDSSQLAYG 654
Cdd:PRK07786 102 TPPE-IAFLVSDCGAHVVVTEaalapvaTAVRDIVPLLSTVVVAGGSSDDSVLG-YEDLLAeagpahapVDIPNDSPALI 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 655 IYTSGSTGIPKGVLVEHRNLS-NYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGG-TLFFLLKedAIDPAKV 732
Cdd:PRK07786 180 MYTSGTTGRPKGAVLTHANLTgQAMTCLRTNGADINSDVGFVGVPLFHIAGIGSMLPGLLLGApTVIYPLG--AFDPGQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 733 EEIVQGKAIDWYKITPSHLKALSSESGTKlfPR----KGLILGGEASEWSWIKEIYRNIPAScKLFNHYGPSETTIGVAV 808
Cdd:PRK07786 258 LDVLEAEKVTGIFLVPAQWQAVCAEQQAR--PRdlalRVLSWGAAPASDTLLRQMAATFPEA-QILAAFGQTEMSPVTCM 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 809 YE----VTKKGlsnqfsttPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERFmedpfitDSR 884
Cdd:PRK07786 335 LLgedaIRKLG--------SVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAF-------AGG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 885 MYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIV-------------TVTKVRNEEQLVAy 951
Cdd:PRK07786 400 WFHSGDLVRQDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVigradekwgevpvAVAAVRNDDAALT- 478
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 497785100 952 yvskkevLDkDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKI 994
Cdd:PRK07786 479 -------LE-DLAEFLTDRLARYKHPKALEIVDALPRNPAGKV 513
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
834-1001 |
4.41e-12 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 71.33 E-value: 4.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 834 IYILDDKLRPVPSGIPGHIYIAGEQVARGYLNReelTAERFMEDpfitdsrMYKTGDIGKILYTGEIQFLGRLDGQVKIR 913
Cdd:PRK13382 376 IRILDQDFREVPTGEVGTIFVRNDTQFDGYTSG---STKDFHDG-------FMASGDVGYLDENGRLFVVGRDDEMIVSG 445
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 914 GIRVEPEEIQSQLLSHPSITEAivTVTKVRNEE---QLVAYYVSKKEV--LDKDLQTYLKQKLPPNLVPAYLVKMDTLPR 988
Cdd:PRK13382 446 GENVYPIEVEKTLATHPDVAEA--AVIGVDDEQygqRLAAFVVLKPGAsaTPETLKQHVRDNLANYKVPRDIVVLDELPR 523
|
170
....*....|...
gi 497785100 989 HAHGKIDRKALPE 1001
Cdd:PRK13382 524 GATGKILRRELQA 536
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1572-2001 |
6.24e-12 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 70.83 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1572 VRSSPNHIALRFLDRSYTYDEVNKRANKIANQLykMGIRRGDR---VALYHERSSEMIFGFLGILKCGAAYVPIDselPL 1648
Cdd:PRK13388 11 DRAGDDTIAVRYGDRTWTWREVLAEAAARAAAL--IALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLVGLN---TT 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1649 NRRDFILKD---ASVGAIVTQTSLEEKLSKSDLPylctdqsqdsEDYSLLTKDKSYPEDIAY-----------------I 1708
Cdd:PRK13388 86 RRGAALAADirrADCQLLVTDAEHRPLLDGLDLP----------GVRVLDVDTPAYAELVAAagaltphrevdamdpfmL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1709 IYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITqETKVGQFATISFD----ASLWQIlmALLAGATLCVVSReeqLSTK 1784
Cdd:PRK13388 156 IFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLT-RDDVCYVSMPLFHsnavMAGWAP--AVASGAAVALPAK---FSAS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1785 ALVKRFRDWNVTLADLPPVVLDSIL-----PEDIPSLQTVSTGGERCPIKVAKrwsLDRNF----YNVYGPTETTIATTw 1855
Cdd:PRK13388 230 GFLDDVRRYGATYFNYVGKPLAYILatperPDDADNPLRVAFGNEASPRDIAE---FSRRFgcqvEDGYGSSEGAVIVV- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1856 yrvSSPECVQDSvpIGTPVPNteVFILDPD-LNPVPMGV-------------IGEIY-IGGVGVSNGYLNRDDLNEKRfI 1920
Cdd:PRK13388 306 ---REPGTPPGS--IGRGAPG--VAIYNPEtLTECAVARfdahgallnadeaIGELVnTAGAGFFEGYYNNPEATAER-M 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1921 PHPfreeeiLYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVP 2000
Cdd:PRK13388 378 RHG------MYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVGDQVMAALVL 451
|
.
gi 497785100 2001 H 2001
Cdd:PRK13388 452 R 452
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
532-999 |
7.06e-12 |
|
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: 70.54 E-value: 7.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 532 YTYLQTNNRANQIARWLQKQGIGKEDFIGiQLQPCAKAIIAM-LGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITH 610
Cdd:cd05915 25 TTYAEVYQRARRLMGGLRALGVGVGDRVA-TLGFNHFRHLEAyFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLLFD 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 611 SEYKTSYEGYEVPILYI----------DQLDDFLLDEREDNLNV----DCDSSQLAYgiyTSGSTGIPKGVLVEHRN--L 674
Cdd:cd05915 104 PNLLPLVEAIRGELKTVqhfvvmdekaPEGYLAYEEALGEEADPvrvpERAACGMAY---TTGTTGLPKGVVYSHRAlvL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 675 SNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFfLLKEDAIDPAKVEEIVQGKAIDWYKITPS-HLKA 753
Cdd:cd05915 181 HSLAASLVDGTALSEKDVVLPVVPMFHVNAWCLPYAATLVGAKQV-LPGPRLDPASLVELFDGEGVTFTAGVPTVwLALA 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 754 LSSESGTKLFPRKGLILGGEASEWSWIKEIYRniPASCKLFNHYGPSET-TIGVAVYEVTkkglsnQFSTTPIGSSLsnn 832
Cdd:cd05915 260 DYLESTGHRLKTLRRLVVGGSAAPRSLIARFE--RMGVEVRQGYGLTETsPVVVQNFVKS------HLESLSEEEKL--- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 833 RIYILD---------DKLRPVPSGIPGH------IYIAGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKILYT 897
Cdd:cd05915 329 TLKAKTglpiplvrlRVADEEGRPVPKDgkalgeVQLKGPWITGGYYGNEEATRSALTPDGF------FRTGDIAVWDEE 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 898 GEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEA-IVTVTKVRNEEQLVAYY-VSKKEVLDKDLQTYLKQKLPP-N 974
Cdd:cd05915 403 GYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAaVVAIPHPKWQERPLAVVvPRGEKPTPEELNEHLLKAGFAkW 482
|
490 500
....*....|....*....|....*
gi 497785100 975 LVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05915 483 QLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
574-999 |
7.65e-12 |
|
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: 70.19 E-value: 7.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 574 LGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITHSEYKTSYE--GYEVPILYIDQL---------DDF--LLDERED 640
Cdd:cd05928 85 VACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDELAPEVDsvASECPSLKTKLLvseksrdgwLNFkeLLNEAST 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 641 NLNVDCDSSQLAYGIY-TSGSTGIPKgvLVEHRNLSnyiyaiqTKLGNKPKDRYLL-LQSLAYDFCLT----------TI 708
Cdd:cd05928 165 EHHCVETGSQEPMAIYfTSGTTGSPK--MAEHSHSS-------LGLGLKVNGRYWLdLTASDIMWNTSdtgwiksawsSL 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 709 YTSLLSGGTLFFLLKedaidpAKVEEIVQGKAIDWYKIT-----PSHLKALSSESGTKL-FPR-KGLILGGEA------S 775
Cdd:cd05928 236 FEPWIQGACVFVHHL------PRFDPLVILKTLSSYPITtfcgaPTVYRMLVQQDLSSYkFPSlQHCVTGGEPlnpevlE 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 776 EWSWIK--EIYRNipascklfnhYGPSETTIGVAVYevtkKGLsnQFSTTPIGSSLSNNRIYILDDKLRPVPSGIPGHIY 853
Cdd:cd05928 310 KWKAQTglDIYEG----------YGQTETGLICANF----KGM--KIKPGSMGKASPPYDVQIIDDNGNVLPPGTEGDIG 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 854 IAGEQVA-----RGYLNREELTAERFMEDpfitdsrMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLS 928
Cdd:cd05928 374 IRVKPIRpfglfSGYVDNPEKTAATIRGD-------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIE 446
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497785100 929 HPSITEAIVTVT--KVRNEE-----QLVAYYVSK-KEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05928 447 HPAVVESAVVSSpdPIRGEVvkafvVLAPQFLSHdPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
1585-2048 |
8.20e-12 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 69.68 E-value: 8.20e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1585 DRSYTYDEVNKRAnKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIV 1664
Cdd:PRK08308 6 DEEYSKSDFDLRL-QRYEEMEQFQEAAGNRFAVCLKDPFDIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGCHGLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 TQtslEEKLSKSDLPylctdqSQDSEDYSLLTkdksypediayiiYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQE 1744
Cdd:PRK08308 85 YG---ESDFTKLEAV------NYLAEEPSLLQ-------------YSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1745 TKVGQFATISFDASL-WQILMALLAGATLCVVSreeQLSTKALVKRFRDWNV-TLADLPPVV--LDSILPEDIpSLQTVS 1820
Cdd:PRK08308 143 ETPIVACPVTHSYGLiCGVLAALTRGSKPVIIT---NKNPKFALNILRNTPQhILYAVPLMLhiLGRLLPGTF-QFHAVM 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1821 TGGERCPikvakrwslDRNFYNVYGptETTIATTWYRVSSPECVQDSVPIGTPVpntevfildpDL-NPVPMgvigeiyi 1899
Cdd:PRK08308 219 TSGTPLP---------EAWFYKLRE--RTTYMMQQYGCSEAGCVSICPDMKSHL----------DLgNPLPH-------- 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1900 ggVGVSNGylnrDDLNEKRFIPHPFREEEIlyKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKE 1979
Cdd:PRK08308 270 --VSVSAG----SDENAPEEIVVKMGDKEI--FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQE 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 497785100 1980 AIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSLPTA 2048
Cdd:PRK08308 342 AVVYRGKDPVAGERVKAKVISHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLELG 410
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1576-1950 |
1.70e-11 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 69.60 E-value: 1.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRS--------YTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAyVPIDselP 1647
Cdd:PRK07529 39 PDAPALSFLLDAdpldrpetWTYAELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPIN---P 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 LNRRDFI---LKDASVGAIVT-----QTSLEEKLS----------------------------------KSDLPYLCTDQ 1685
Cdd:PRK07529 115 LLEPEQIaelLRAAGAKVLVTlgpfpGTDIWQKVAevlaalpelrtvvevdlarylpgpkrlavplirrKAHARILDFDA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1686 SQDSEDYSLLTKDKSY-PEDIAYIIYTSGTTGTPNGVMVKHSS-VMN--LISATIDEfnitQETKVGQFATISF--DASL 1759
Cdd:PRK07529 195 ELARQPGDRLFSGRPIgPDDVAAYFHTGGTTGMPKLAQHTHGNeVANawLGALLLGL----GPGDTVFCGLPLFhvNALL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1760 WQILMALLAGATLCVVS----REEQlstkaLVKRFRD----WNVTLADLPPVVLDSIL--P---EDIPSLQTVSTGGERC 1826
Cdd:PRK07529 271 VTGLAPLARGAHVVLATpqgyRGPG-----VIANFWKiverYRINFLSGVPTVYAALLqvPvdgHDISSLRYALCGAAPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1827 PIKVAkrwsldRNF--------YNVYGPTETTIATTwyrVSSPECVQDSVPIGTPVPNTEVFI--LDPD---LNPVPMGV 1893
Cdd:PRK07529 346 PVEVF------RRFeaatgvriVEGYGLTEATCVSS---VNPPDGERRIGSVGLRLPYQRVRVviLDDAgryLRDCAVDE 416
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 497785100 1894 IGEIYIGGVGVSNGYLNRDDlNEKRFIphpfreEEILYKTGDIGKVLHDGNLEHLGR 1950
Cdd:PRK07529 417 VGVLCIAGPNVFSGYLEAAH-NKGLWL------EDGWLNTGDLGRIDADGYFWLTGR 466
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
655-941 |
1.81e-11 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 69.03 E-value: 1.81e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 655 IYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDR----YLLLQSLAYDFCLTTIYTSLlsggtlffllkeDAIDPA 730
Cdd:cd05910 91 LFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVdlatFPLFALFGPALGLTSVIPDM------------DPTRPA 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 731 KV--EEIVQgkAIDWYKIT-----PSHLKALS---SESGTKLFPRKGLILGGEASEWSWIKEIYRNIPASCKLFNHYGPS 800
Cdd:cd05910 159 RAdpQKLVG--AIRQYGVSivfgsPALLERVArycAQHGITLPSLRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGAT 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 801 E----TTIGVAVYEVTKKGLSNQFSTTPIGSSLSNNRIYILD---------DKLRPVPSGIPGHIYIAGEQVARGYLNRE 867
Cdd:cd05910 237 EalpvSSIGSRELLATTTAATSGGAGTCVGRPIPGVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRP 316
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 868 ELTAERFMEDPfiTDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTK 941
Cdd:cd05910 317 VATALAKIDDN--SEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRsALVGVGK 389
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
512-999 |
2.69e-11 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 68.75 E-value: 2.69e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHERSYTYLQTNNRANQIARWLQKQ-GIGKEDFIGIQLQPCAKAIIAMLGVLKAG---------- 580
Cdd:PRK08751 31 FATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGltvvnvnply 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 581 ------------GAYLPLDVESPKERIEIITQDSKLKAIITHS-------------EYKTSYEGYEVPILYIDQLDDF-- 633
Cdd:PRK08751 111 tprelkhqlidsGASVLVVIDNFGTTVQQVIADTPVKQVITTGlgdmlgfpkaalvNFVVKYVKKLVPEYRINGAIRFre 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 634 --LLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRNL-SNYIYAIQ--TKLGNKPKDRYLLLQSLA--YDFCLT 706
Cdd:PRK08751 191 alALGRKHSMPTLQIEPDDIAFLQYTGGTTGVAKGAMLTHRNLvANMQQAHQwlAGTGKLEEGCEVVITALPlyHIFALT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 707 TIYTSLLSGGTLFFLLKEDAIDPAKVEEIVQGKAIDWYKITPSHLKALSSESGTKL-FPRKGLILGGEASEWSWIKEIYR 785
Cdd:PRK08751 271 ANGLVFMKIGGCNHLISNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTPGFDQIdFSSLKMTLGGGMAVQRSVAERWK 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 786 NIpASCKLFNHYGPSETTIGVAVYEVTKKGLSNQfsttpIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLN 865
Cdd:PRK08751 351 QV-TGLTLVEAYGLTETSPAACINPLTLKEYNGS-----IGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWK 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 866 REELTAERFMEDPFItdsrmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRN 944
Cdd:PRK08751 425 RPEETAKVMDADGWL------HTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEvAAVGVPDEKS 498
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 945 EEQLVAYYVSKKEVLD-KDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK08751 499 GEIVKVVIVKKDPALTaEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
711-1002 |
3.65e-11 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 67.71 E-value: 3.65e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 711 SLLSGGTLFFL----LKEDAIDPAKVEEIvqgkaidWYKITPSHLKALSSESGTKLFPRKGLILGGeASEWSWIKEIYRN 786
Cdd:PRK07445 181 SFLTGGKLVILpykrLKSGQELPPNPSDF-------FLSLVPTQLQRLLQLRPQWLAQFRTILLGG-APAWPSLLEQARQ 252
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 787 ipASCKLFNHYGPSETTIGVAVYevtkkgLSNQFSTTPIGSS--LSNNRIYILDDKLrpvpsgipGHIYIAGEQVARGYL 864
Cdd:PRK07445 253 --LQLRLAPTYGMTETASQIATL------KPDDFLAGNNSSGqvLPHAQITIPANQT--------GNITIQAQSLALGYY 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 865 nreeltaerfmedPFITDS-RMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLShpsiTEAI--VTVTK 941
Cdd:PRK07445 317 -------------PQILDSqGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILA----TGLVqdVCVLG 379
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 942 VRNE---EQLVAYYVSKKEVLDKD-LQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEI 1002
Cdd:PRK07445 380 LPDPhwgEVVTAIYVPKDPSISLEeLKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1573-2040 |
4.00e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 68.14 E-value: 4.00e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1573 RSSPNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSEL-P---- 1647
Cdd:PRK07470 18 RRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQtPdeva 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1648 -LNR----RDFILKDASVG--AIVTQTSLEEKLSksdlpyLCTDQSQDSEDYSLLTK----DKSYPEDIAY-----IIYT 1711
Cdd:PRK07470 98 yLAEasgaRAMICHADFPEhaAAVRAASPDLTHV------VAIGGARAGLDYEALVArhlgARVANAAVDHddpcwFFFT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1712 SGTTGTPNGVMVKHSS----VMN----LISATidefniTQETKVGQFATISFDASLWQiLMALLAGATlCVVSREEQLST 1783
Cdd:PRK07470 172 SGTTGRPKAAVLTHGQmafvITNhladLMPGT------TEQDASLVVAPLSHGAGIHQ-LCQVARGAA-TVLLPSERFDP 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1784 K---ALVKRfrdWNVT-LADLPPVVldSILPE-------DIPSLQTVSTGGE---RCPIKVAKRwSLDRNFYNVYGPTET 1849
Cdd:PRK07470 244 AevwALVER---HRVTnLFTVPTIL--KMLVEhpavdryDHSSLRYVIYAGApmyRADQKRALA-KLGKVLVQYFGLGEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1850 TIATTWY--RVSSPECVqDSVPIGT---PVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFIPHPF 1924
Cdd:PRK07470 318 TGNITVLppALHDAEDG-PDARIGTcgfERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1925 ReeeilykTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPH--G 2002
Cdd:PRK07470 397 R-------TGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWGEVGVAVCVARdgA 469
|
490 500 510
....*....|....*....|....*....|....*...
gi 497785100 2003 EWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKV 2040
Cdd:PRK07470 470 PVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1583-1982 |
4.06e-11 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 67.84 E-value: 4.06e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1583 FLDRSYTYDEVNKRANKIANQLYK-MGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELplnrrdfilkdasvg 1661
Cdd:cd05937 1 FEGKTWTYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNL--------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1662 aivTQTSLEEKLSKSDLPYLCTDqsqdsedyslltkdksyPEDIAYIIYTSGTTGTPNGVMV---KHSSVMNLISATID- 1737
Cdd:cd05937 66 ---SGDPLIHCLKLSGSRFVIVD-----------------PDDPAILIYTSGTTGLPKAAAIswrRTLVTSNLLSHDLNl 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1738 EFNITQETKVGQFATISFDASLWQILMallAGATLCvvsreeqLSTKALVKRF----RDWNVT-----------LADLPP 1802
Cdd:cd05937 126 KNGDRTYTCMPLYHGTAAFLGACNCLM---SGGTLA-------LSRKFSASQFwkdvRDSGATiiqyvgelcryLLSTPP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1803 VVLDSilpedIPSLQTVSTGGERCPIkvakrWSLDRNFYNV------YGPTETTIATTWYRVS--SPECVQDSVPIG--- 1871
Cdd:cd05937 196 SPYDR-----DHKVRVAWGNGLRPDI-----WERFRERFNVpeigefYAATEGVFALTNHNVGdfGAGAIGHHGLIRrwk 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1872 -----TPV---PNTEVFILDPDLN---PVPMGVIGEIyIGGVGVSN-----GYLNRDDLNEKRFIPHPFREEEILYKTGD 1935
Cdd:cd05937 266 fenqvVLVkmdPETDDPIRDPKTGfcvRAPVGEPGEM-LGRVPFKNreafqGYLHNEDATESKLVRDVFRKGDIYFRTGD 344
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 497785100 1936 IGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIV 1982
Cdd:cd05937 345 LLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANV 391
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1703-2045 |
5.04e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 67.92 E-value: 5.04e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1703 EDIAYIIYTSGTTGTPNGVMVKHSSV---MNLISATIDEFNITQET--KVGQFATISfDASLWQIlMALLAGATLCVVSR 1777
Cdd:PRK12492 207 DDIAVLQYTGGTTGLAKGAMLTHGNLvanMLQVRACLSQLGPDGQPlmKEGQEVMIA-PLPLYHI-YAFTANCMCMMVSG 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1778 EEQL------STKALVKRFRDWNVT----LADLPPVVLDSilPE----DIPSLQTVSTGGERCPIKVAKRWSLDRNFYNV 1843
Cdd:PRK12492 285 NHNVlitnprDIPGFIKELGKWRFSallgLNTLFVALMDH--PGfkdlDFSALKLTNSGGTALVKATAERWEQLTGCTIV 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1844 --YGPTETT-IATTwyrvsSPECVQDSV-PIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRF 1919
Cdd:PRK12492 363 egYGLTETSpVAST-----NPYGELARLgTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1920 iphpfrEEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVV 1999
Cdd:PRK12492 438 ------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEAVKLFVV 511
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 497785100 2000 PH-GEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK12492 512 ARdPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
652-999 |
5.40e-11 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 68.13 E-value: 5.40e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 652 AYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTK-LGNKPKDRYLLLQSLAYDFCL-TTIYTSLLSGGTLffllkedAIDP 729
Cdd:PRK06060 148 AYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKaLRLTPEDTGLCSARMYFAYGLgNSVWFPLATGGSA-------VINS 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 730 AKVEeiVQGKAIDWYKITPSHL-----------KALSSESGTKLfprKGLILGGEASEwswikeiyrnIPASCKLFNHYG 798
Cdd:PRK06060 221 APVT--PEAAAILSARFGPSVLygvpnffarviDSCSPDSFRSL---RCVVSAGEALE----------LGLAERLMEFFG 285
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 799 PSETTIGVAVYEVTKKGLSN---QFSTTPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREeltaerfm 875
Cdd:PRK06060 286 GIPILDGIGSTEVGQTFVSNrvdEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP-------- 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 876 eDPFITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYV- 953
Cdd:PRK06060 358 -DSPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEaAVVAVRESTGASTLQAFLVa 436
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 497785100 954 SKKEVLDKDLQTYLKQKLPPNL----VPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK06060 437 TSGATIDGSVMRDLHRGLLNRLsafkVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1576-1943 |
8.74e-11 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 66.89 E-value: 8.74e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQTSLEE-------KLSKSDLPYLCTDQSQDSE-------DYS--LLTKDKSY----PED----IAyIIYT 1711
Cdd:PRK08162 112 RHGEAKVLIVDTEFAEvarealaLLPGPKPLVIDVDDPEYPGgrfigalDYEafLASGDPDFawtlPADewdaIA-LNYT 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1712 SGTTGTPNGVMVKH-SSVMNLISatidefNITqETKVGQFATIsfdasLWQILM------------ALLAGATLCVvsre 1778
Cdd:PRK08162 191 SGTTGNPKGVVYHHrGAYLNALS------NIL-AWGMPKHPVY-----LWTLPMfhcngwcfpwtvAARAGTNVCL---- 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1779 EQLSTKALVKRFRDWNVTLADLPPVVLDSIL--PED----IPSLQTVSTGGERCPIKV-AKRWSLDRNFYNVYGPTETTI 1851
Cdd:PRK08162 255 RKVDPKLIFDLIREHGVTHYCGAPIVLSALInaPAEwragIDHPVHAMVAGAAPPAAViAKMEEIGFDLTHVYGLTETYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1852 ATT-------WYRVSSPECVQDSVPIGTPVPNTE-VFILDPD-LNPVPMG--VIGEIYIGGVGVSNGYLNRDDLNEKRFi 1920
Cdd:PRK08162 335 PATvcawqpeWDALPLDERAQLKARQGVRYPLQEgVTVLDPDtMQPVPADgeTIGEIMFRGNIVMKGYLKNPKATEEAF- 413
|
410 420
....*....|....*....|....
gi 497785100 1921 phpfreEEILYKTGDIGkVLH-DG 1943
Cdd:PRK08162 414 ------AGGWFHTGDLA-VLHpDG 430
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1576-2045 |
9.98e-11 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 66.94 E-value: 9.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYV--------------- 1640
Cdd:PRK10946 37 SDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVAPVnalfshqrselnaya 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1641 -PIDSELPLNRRDFIL--KDASVGAIVTQ-TSLEEKLSKSDLPYLCTDQ--SQDSEDYsllTKDKSYPEDIAYIIYTSGT 1714
Cdd:PRK10946 117 sQIEPALLIADRQHALfsDDDFLNTLVAEhSSLRVVLLLNDDGEHSLDDaiNHPAEDF---TATPSPADEVAFFQLSGGS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1715 TGTPNGVMVKHSSVMNLISATIDEFNITQETK--VGQFATISFDASLWQILMALLAGATLCVVSREEQLSTKALVKRFRd 1792
Cdd:PRK10946 194 TGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRylCALPAAHNYPMSSPGALGVFLAGGTVVLAPDPSATLCFPLIEKHQ- 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1793 wnVTLADL-PPVV---LDSILPED----IPSLQTVSTGGERCPIKVAKRWS--LDRNFYNVYGPTETTIATTwyRVSSPe 1862
Cdd:PRK10946 273 --VNVTALvPPAVslwLQAIAEGGsraqLASLKLLQVGGARLSETLARRIPaeLGCQLQQVFGMAEGLVNYT--RLDDS- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1863 cvqDSVPIGT---PV-PNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfrEEEILYKTGDIGK 1938
Cdd:PRK10946 348 ---DERIFTTqgrPMsPDDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAF------DANGFYCSGDLVS 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1939 VLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKIIEELRS--- 2015
Cdd:PRK10946 419 IDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELMGEKSCAFLVVKEPLKAVQLRRFLREqgi 498
|
490 500 510
....*....|....*....|....*....|...
gi 497785100 2016 ---KLPEHmvpsiFVQMEELPRLNNKKVDRHSL 2045
Cdd:PRK10946 499 aefKLPDR-----VECVDSLPLTAVGKVDKKQL 526
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1589-1968 |
1.11e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 66.56 E-value: 1.11e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSelPLNRRDFIL--KD--ASVGAIV 1664
Cdd:PRK07768 31 TWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQ--PTPRTDLAVwaEDtlRVIGMIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 TQT--------SLEEKLSKSDLPYLCTDQSQDSEDYSLLTKDksyPEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATI 1736
Cdd:PRK07768 109 AKAvvvgepflAAAPVLEEKGIRVLTVADLLAADPIDPVETG---EDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1737 DEFNITQETKVgqfaTISfdaslWQIL---MALLA--------GATLCVVSREEQLST----KALVKRFRDwNVTLA--- 1798
Cdd:PRK07768 186 VAAEFDVETDV----MVS-----WLPLfhdMGMVGfltvpmyfGAELVKVTPMDFLRDpllwAELISKYRG-TMTAApnf 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1799 --DLPPVVLDSILPE---DIPSLQTVSTGGErcPIKVA---------KRWSLDRN-FYNVYGPTETTIAttwyrVSSPEC 1863
Cdd:PRK07768 256 ayALLARRLRRQAKPgafDLSSLRFALNGAE--PIDPAdvedlldagARFGLRPEaILPAYGMAEATLA-----VSFSPC 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1864 ----VQDSV-----------------------PIGTPVPNTEVFILDPDLNPVPMGVIGEIYIGGVGVSNGYLNRDDlne 1916
Cdd:PRK07768 329 gaglVVDEVdadllaalrravpatkgntrrlaTLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLTMDG--- 405
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 497785100 1917 krfiPHPFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIE 1968
Cdd:PRK07768 406 ----FIPAQDADGWLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIE 453
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1576-2045 |
1.55e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 66.20 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1576 PNHIALRFLDRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFIL 1655
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLDATSIAAIL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1656 KDASVGAIVTQTSLEeKLSKSDLPYLCTDQSQ-------------------DSEDYS-LLTKDKSYPEDIAYII------ 1709
Cdd:PLN03102 108 RHAKPKILFVDRSFE-PLAREVLHLLSSEDSNlnlpvifiheidfpkrpssEELDYEcLIQRGEPTPSLVARMFriqdeh 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1710 ------YTSGTTGTPNGVMVKH-SSVMNLISATID-EFNItqetkvgqfatisFDASLWQILM------------ALLAG 1769
Cdd:PLN03102 187 dpislnYTSGTTADPKGVVISHrGAYLSTLSAIIGwEMGT-------------CPVYLWTLPMfhcngwtftwgtAARGG 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1770 ATLCVvsreEQLSTKALVKRFRDWNVTLADLPPVVLDSILPEDIPSLQ------TVSTGGERCPIKVAKR-WSLDRNFYN 1842
Cdd:PLN03102 254 TSVCM----RHVTAPEIYKNIEMHNVTHMCCVPTVFNILLKGNSLDLSprsgpvHVLTGGSPPPAALVKKvQRLGFQVMH 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1843 VYGPTETT-------IATTWYRVSSPECVQDSVPIG--------TPVPNTEVfildpdLNPVPMG--VIGEIYIGGVGVS 1905
Cdd:PLN03102 330 AYGLTEATgpvlfceWQDEWNRLPENQQMELKARQGvsilgladVDVKNKET------QESVPRDgkTMGEIVIKGSSIM 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1906 NGYLNRDDLNEKRFiPHPFreeeilYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPL 1985
Cdd:PLN03102 404 KGYLKNPKATSEAF-KHGW------LNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAM 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497785100 1986 GDNQNYHTLVAYVV-PHGEWEEKKIIEEL-----------RSKLPEHMVPSIFVQMEELPRLNNKKVDRHSL 2045
Cdd:PLN03102 477 PHPTWGETPCAFVVlEKGETTKEDRVDKLvtrerdlieycRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
1589-1982 |
1.68e-10 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 65.93 E-value: 1.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALY---HERSSEMIFGFLGIlkcGAAYVPIDSELPLNRRDFILKDASVGAIVT 1665
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI---GAICHTVNPRLFPEQIAWIINHAEDRVVIT 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1666 QTSLEEKLSKsdlpylCTDQSQDSEDYSLLTKDKSYPED-----IAY-----------------------IIYTSGTTGT 1717
Cdd:PRK06018 118 DLTFVPILEK------IADKLPSVERYVVLTDAAHMPQTtlknaVAYeewiaeadgdfawktfdentaagMCYTSGTTGD 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1718 PNGVMVKH-SSVMN-LISATIDEFNITQETKVGQFATIsFDASLWQILMA--------LLAGATLCVVSREEQLSTKalv 1787
Cdd:PRK06018 192 PKGVLYSHrSNVLHaLMANNGDALGTSAADTMLPVVPL-FHANSWGIAFSapsmgtklVMPGAKLDGASVYELLDTE--- 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1788 krfrdwNVTLADLPPVV----LDSILPED--IPSLQTVSTGGERCPIKVAKRWS-LDRNFYNVYGPTETTIATTWYRVSS 1860
Cdd:PRK06018 268 ------KVTFTAGVPTVwlmlLQYMEKEGlkLPHLKMVVCGGSAMPRSMIKAFEdMGVEVRHAWGMTEMSPLGTLAALKP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1861 P-ECVQDSVPI------GTPVPNTEVFILDPDLNPVPMG--VIGEIYIGGVGVSNGYLNRDD--LNEKRFiphpfreeei 1929
Cdd:PRK06018 342 PfSKLPGDARLdvlqkqGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYRVDGeiLDDDGF---------- 411
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 497785100 1930 lYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIV 1982
Cdd:PRK06018 412 -FDTGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAV 463
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
529-1010 |
1.99e-10 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 66.07 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 529 ERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGA----YLPLDVESPKERI------EII 598
Cdd:PLN02654 118 DASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVhsvvFAGFSAESLAQRIvdckpkVVI 197
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 599 TQDS--------KLKAIITHSEYKTSYEGYEVPILYidQLDDFLLDERED----------------NLNVDC-----DSS 649
Cdd:PLN02654 198 TCNAvkrgpktiNLKDIVDAALDESAKNGVSVGICL--TYENQLAMKREDtkwqegrdvwwqdvvpNYPTKCevewvDAE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 650 QLAYGIYTSGSTGIPKGVLveHRNLSNYIYAIQT---KLGNKPKDRYLLLQSLAYdfcLT----TIYTSLLSGGT-LFFL 721
Cdd:PLN02654 276 DPLFLLYTSGSTGKPKGVL--HTTGGYMVYTATTfkyAFDYKPTDVYWCTADCGW---ITghsyVTYGPMLNGATvLVFE 350
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 722 LKEDAIDPAKVEEIVqgkaiDWYKIT-----PSHLKALsSESGTKL---FPRKGL-ILG--GE---ASEWSWikeiyrni 787
Cdd:PLN02654 351 GAPNYPDSGRCWDIV-----DKYKVTifytaPTLVRSL-MRDGDEYvtrHSRKSLrVLGsvGEpinPSAWRW-------- 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 788 pasckLFNHYGPSETTIGVAVYEVTKKGlsnqFSTTPI--------GSS---LSNNRIYILDDKLRPVPSGIPGHIYIAG 856
Cdd:PLN02654 417 -----FFNVVGDSRCPISDTWWQTETGG----FMITPLpgawpqkpGSAtfpFFGVQPVIVDEKGKEIEGECSGYLCVKK 487
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 857 E-----QVARGYLNREELTAERfmedPFitdSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPS 931
Cdd:PLN02654 488 SwpgafRTLYGDHERYETTYFK----PF---AGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQ 560
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 932 ITEAivTVTKVRNEEQLVAYY--------VSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPEIQ 1003
Cdd:PLN02654 561 CAEA--AVVGIEHEVKGQGIYafvtlvegVPYSEELRKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRILRKIA 638
|
....*..
gi 497785100 1004 VSNWNEI 1010
Cdd:PLN02654 639 SRQLDEL 645
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
520-924 |
2.25e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 65.73 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALS--DHER-------SYTYLQTNNRANQIARWLQKQG-IGKEDFIgiqLQPCA-KAIIAMLGVLKAGGAYLPLDV 588
Cdd:PRK05850 15 PDDAAFTfiDYEQdpagvaeTLTWSQLYRRTLNVAEELRRHGsTGDRAVI---LAPQGlEYIVAFLGALQAGLIAVPLSV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 589 ESP---KERIEIITQDSKLKAIITHS-------EYKTSYEGYEVP-ILYIDQLDdflLD-EREDNLNVDcDSSQLAYGIY 656
Cdd:PRK05850 92 PQGgahDERVSAVLRDTSPSVVLTTSavvddvtEYVAPQPGQSAPpVIEVDLLD---LDsPRGSDARPR-DLPSTAYLQY 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 657 TSGSTGIPKGVLVEHRNL-SNYIYAIQTKLGNKPK----------------DRYLLLQSLAYDFC-LTTIYTSLLSggtl 718
Cdd:PRK05850 168 TSGSTRTPAGVMVSHRNViANFEQLMSDYFGDTGGvpppdttvvswlpfyhDMGLVLGVCAPILGgCPAVLTSPVA---- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 719 fFLLKedaidPAKveeivqgkaidWYKITPSHLKALSSES--GTKLFPRK-------GLILGG-----EASEwswikeiy 784
Cdd:PRK05850 244 -FLQR-----PAR-----------WMQLLASNPHAFSAAPnfAFELAVRKtsdddmaGLDLGGvlgiiSGSE-------- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 785 RNIPASCKLFNH---------------YGPSETTIGVAVYEVTKKGLSNQFSTtpigSSLSNNR---------------- 833
Cdd:PRK05850 299 RVHPATLKRFADrfapfnlretairpsYGLAEATVYVATREPGQPPESVRFDY----EKLSAGHakrcetgggtplvsyg 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 834 ------IYILD-DKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERF---MEDPF--ITDSRMYKTGDIGkILYTGEIQ 901
Cdd:PRK05850 375 sprsptVRIVDpDTCIECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSpgTPEGPWLRTGDLG-FISEGELF 453
|
490 500
....*....|....*....|...
gi 497785100 902 FLGRLDGQVKIRGIRVEPEEIQS 924
Cdd:PRK05850 454 IVGRIKDLLIVDGRNHYPDDIEA 476
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
521-1001 |
2.80e-10 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 65.30 E-value: 2.80e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 521 NSIAL----SDHERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPL----DVESPK 592
Cdd:PRK04319 59 DKVALryldASRKEKYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLfeafMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 593 ERIEiitqDSKLKAIITHSEYKTSYEGYEVP----ILYIDQLD-------DF--LLDEREDNLN-VDCDSSQLAYGIYTS 658
Cdd:PRK04319 139 DRLE----DSEAKVLITTPALLERKPADDLPslkhVLLVGEDVeegpgtlDFnaLMEQASDEFDiEWTDREDGAILHYTS 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 659 GSTGIPKGVLVEHRN-LSNYIYAiQTKLGNKPKDRYlllqslaydFCltT------------IYTSLLSGGTLffLLKED 725
Cdd:PRK04319 215 GSTGKPKGVLHVHNAmLQHYQTG-KYVLDLHEDDVY---------WC--TadpgwvtgtsygIFAPWLNGATN--VIDGG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 726 AIDPAKVEEIVQGKAID-WYKiTPSHLKALSSeSGTKLFPRKGLI-----------LGGEASEWSwiKEIYrNIPasckL 793
Cdd:PRK04319 281 RFSPERWYRILEDYKVTvWYT-APTAIRMLMG-AGDDLVKKYDLSslrhilsvgepLNPEVVRWG--MKVF-GLP----I 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 794 FNHYGPSET-TIGVAVY---EVtKKGlsnqfsttPIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGE--QVARGYLNRE 867
Cdd:PRK04319 352 HDNWWMTETgGIMIANYpamDI-KPG--------SMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGwpSMMRGIWNNP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 868 ELTAERFMEDpfitdsrMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVtVTK---VRN 944
Cdd:PRK04319 423 EKYESYFAGD-------WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGV-IGKpdpVRG 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 945 EeqLVAYYVSKK------EVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDR---KA----LPE 1001
Cdd:PRK04319 495 E--IIKAFVALRpgyepsEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRrvlKAwelgLPE 562
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
529-1001 |
6.57e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.95 E-value: 6.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 529 ERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAII 608
Cdd:PRK12406 9 DRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 609 THSEYKTSYEG--------YEVP----ILYIDQLDDFLLDEREDNLNVD--CDSSQLAYG---------IYTSGSTGIPK 665
Cdd:PRK12406 89 AHADLLHGLASalpagvtvLSVPtppeIAAAYRISPALLTPPAGAIDWEgwLAQQEPYDGppvpqpqsmIYTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 666 GV-----LVEHrnLSNYIYAIQTKLGNKPKDRYL----LLQSLAYDFCLTtiytSLLSGGTLFFLLKEDAidpakvEEIV 736
Cdd:PRK12406 169 GVrraapTPEQ--AAAAEQMRALIYGLKPGIRALltgpLYHSAPNAYGLR----AGRLGGVLVLQPRFDP------EELL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 737 QgkAIDWYKITPSHLKALSSESGTKLFP--RKGLILggeaSEWSWIKEIYRNIPASCK----------LFNHYGPSETti 804
Cdd:PRK12406 237 Q--LIERHRITHMHMVPTMFIRLLKLPEevRAKYDV----SSLRHVIHAAAPCPADVKramiewwgpvIYEYYGSTES-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 805 GVAVYEVTKKGLSNQFSttpIGSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVAR-GYLNREELTAErFMEDPFITds 883
Cdd:PRK12406 309 GAVTFATSEDALSHPGT---VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE-IDRGGFIT-- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 884 rmykTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AIVTVTKVRNEEQLVAYYVSKKEV-LD- 960
Cdd:PRK12406 383 ----SGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDcAVFGIPDAEFGEALMAVVEPQPGAtLDe 458
|
490 500 510 520
....*....|....*....|....*....|....*....|.
gi 497785100 961 KDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKIDRKALPE 1001
Cdd:PRK12406 459 ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRD 499
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
529-980 |
6.67e-10 |
|
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: 63.91 E-value: 6.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 529 ERSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAylpldvespkerIEIITQDSKLKAiI 608
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAV------------AALINYNLRGES-L 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 609 THSeyktsyegyevpiLYIDQLDDFLLDerednlnvdcdssqLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNK 688
Cdd:cd05940 68 AHC-------------LNVSSAKHLVVD--------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 689 PKDR-YL---LLQSLAYDFCLTtiyTSLLSGGTLFFLLKEDAID--PAKVEE---IVQ--GKAIDWYKITPSHlkalSSE 757
Cdd:cd05940 121 PSDVlYTclpLYHSTALIVGWS---ACLASGATLVIRKKFSASNfwDDIRKYqatIFQyiGELCRYLLNQPPK----PTE 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 758 SGTKLfpRKGLILGGEASEWSWIKEIYrNIPASCKLfnhYGPSETTIgvavyevtkkGLSNQFSTT-------PIGSSLS 830
Cdd:cd05940 194 RKHKV--RMIFGNGLRPDIWEEFKERF-GVPRIAEF---YAATEGNS----------GFINFFGKPgaigrnpSLLRKVA 257
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 831 NNRIYILD----DKLRP-------VPSGIPGH-IY-IAGEQVARGYLNREElTAERFMEDPFITDSRMYKTGDIGKILYT 897
Cdd:cd05940 258 PLALVKYDlesgEPIRDaegrcikVPRGEPGLlISrINPLEPFDGYTDPAA-TEKKILRDVFKKGDAWFNTGDLMRLDGE 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 898 GEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEE---QLVAYYVSKKEVLD-KDLQTYLKQKLPP 973
Cdd:cd05940 337 GFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGTDgraGMAAIVLQPNEEFDlSALAAHLEKNLPG 416
|
....*..
gi 497785100 974 NLVPAYL 980
Cdd:cd05940 417 YARPLFL 423
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
520-971 |
7.22e-10 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 63.74 E-value: 7.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 520 PNSIALSDHERSYTYLQTNNRANQIARWLQKQGIGKEDfiGIQLqpCAK----AIIAMLGVLKAGGAYLPLDVESPKERI 595
Cdd:PRK09029 17 PQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGS--GVAL--RGKnspeTLLAYLALLQCGARVLPLNPQLPQPLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 596 EIITQDSKLKAIITHSEYKTsyegyevpilyIDQLDDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRN-- 673
Cdd:PRK09029 93 EELLPSLTLDFALVLEGENT-----------FSALTSLHLQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAhl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 674 ------LSNYIYAiqtklgnkPKDRYLLlqSLAYdF---CLTTIYTSLLSGGTLFFLlkedaiDPAKVEEIVQGkaidwy 744
Cdd:PRK09029 162 asaegvLSLMPFT--------AQDSWLL--SLPL-FhvsGQGIVWRWLYAGATLVVR------DKQPLEQALAG------ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 745 kIT-----PSHLKALSSESGTKLFPRKGLiLGGEAsewswikeiyrnIPAS-----------CklFNHYGPSE--TTigv 806
Cdd:PRK09029 219 -CThaslvPTQLWRLLDNRSEPLSLKAVL-LGGAA------------IPVElteqaeqqgirC--WCGYGLTEmaST--- 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 807 avyeVTKK---GLSNqfsttpIGSSLSNNRIYILDDKlrpvpsgipghIYIAGEQVARGYLNREELTaerfmedPFITDS 883
Cdd:PRK09029 280 ----VCAKradGLAG------VGSPLPGREVKLVDGE-----------IWLRGASLALGYWRQGQLV-------PLVNDE 331
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 884 RMYKTGDIGkILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIvtVTKVRNEE---QLVAYYVSKKEVLD 960
Cdd:PRK09029 332 GWFATRDRG-EWQNGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVF--VVPVADAEfgqRPVAVVESDSEAAV 408
|
490
....*....|.
gi 497785100 961 KDLQTYLKQKL 971
Cdd:PRK09029 409 VNLAEWLQDKL 419
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
2072-2135 |
7.74e-10 |
|
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: 57.26 E-value: 7.74e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 2072 CWAETLNLPI-DNIGLNSNFFELGGHSLTATQLVARISELFEIELPIKAIFEYPTIQAILDFIVE 2135
Cdd:smart00823 20 QVAAVLGHAAaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
644-905 |
1.25e-09 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 63.38 E-value: 1.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 644 VDCDSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLL---LQSLaYDFCL--TTIYTSLlsggtl 718
Cdd:PRK09274 169 ADLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLPtfpLFAL-FGPALgmTSVIPDM------ 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 719 ffllkeDAIDPAKV--EEIVQgkAIDWYKIT-----PSHLKALS--SESGTKLFP--RKGLILGGEASEWSwIKEIYRNI 787
Cdd:PRK09274 242 ------DPTRPATVdpAKLFA--AIERYGVTnlfgsPALLERLGryGEANGIKLPslRRVISAGAPVPIAV-IERFRAML 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 788 PASCKLFNHYGPSE----TTIG-----VAVYEVTKKGlsnqfSTTPIGSSLSNNRIYILD---------DKLRPVPSGIP 849
Cdd:PRK09274 313 PPDAEILTPYGATEalpiSSIEsreilFATRAATDNG-----AGICVGRPVDGVEVRIIAisdapipewDDALRLATGEI 387
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 497785100 850 GHIYIAGEQVARGYLNREELTAERFMEDPfitDSRMY-KTGDIGKILYTGEIQFLGR 905
Cdd:PRK09274 388 GEIVVAGPMVTRSYYNRPEATRLAKIPDG---QGDVWhRMGDLGYLDAQGRLWFCGR 441
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
648-999 |
1.51e-09 |
|
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: 62.11 E-value: 1.51e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 648 SSQLAYGIYTSGSTGIPKgvLVEHRNlSNYIY---AIQTKLGNKPKDRYLLLQSLAYDF-CLTTIYTSLLSGGTLFFLLK 723
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPK--LAQHTH-SNEVYnawMLALNSLFDPDDVLLCGLPLFHVNgSVVTLLTPLASGAHVVLAGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 724 EDAIDPAKVEEIvqGKAIDWYKIT-----PSHLKALSSESGTK-LFPRKGLILGGEASEwswiKEIYRNIPASCKL--FN 795
Cdd:cd05944 78 AGYRNPGLFDNF--WKLVERYRITslstvPTVYAALLQVPVNAdISSLRFAMSGAAPLP----VELRARFEDATGLpvVE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 796 HYGPSETTIGVAVyevtkkglsnQFSTTP--IGS-----SLSNNRIYILD---DKLRPVPSGIPGHIYIAGEQVARGYLN 865
Cdd:cd05944 152 GYGLTEATCLVAV----------NPPDGPkrPGSvglrlPYARVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYLY 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 866 rEELTAERFMEDPFItdsrmyKTGDIGKILYTGEIQFLGRLDGQVkIRG-IRVEPEEIQSQLLSHPSIT-EAIVTVTKVR 943
Cdd:cd05944 222 -TEGNKNAFVADGWL------NTGDLGRLDADGYLFITGRAKDLI-IRGgHNIDPALIEEALLRHPAVAfAGAVGQPDAH 293
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 497785100 944 NEEQLVAY--YVSKKEVLDKDLQTYLKQKLPPNL-VPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:cd05944 294 AGELPVAYvqLKPGAVVEEEELLAWARDHVPERAaVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
512-994 |
2.02e-09 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 62.52 E-value: 2.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 512 FEGQVLNTPNSIALSDHERS--YTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGG-------A 582
Cdd:PRK08315 22 LDRTAARYPDREALVYRDQGlrWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAilvtinpA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 583 YLPLDVESpkerieIITQdSKLKAIITHSEYKTS-YEG--YEV-----------------P----ILYIDQ--------- 629
Cdd:PRK08315 102 YRLSELEY------ALNQ-SGCKALIAADGFKDSdYVAmlYELapelatcepgqlqsarlPelrrVIFLGDekhpgmlnf 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 630 ---------LDDFLLDEREDNLNVDcDssqlAYGI-YTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLL---- 695
Cdd:PRK08315 175 dellalgraVDDAELAARQATLDPD-D----PINIqYTSGTTGFPKGATLTHRNILNNGYFIGEAMKLTEEDRLCIpvpl 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 696 -------LQSLAydfCLTtiytsllSGGTLFFLLkeDAIDPAKVeeivqgkaidwykitpshLKALSSESGTKL------ 762
Cdd:PRK08315 250 yhcfgmvLGNLA---CVT-------HGATMVYPG--EGFDPLAT------------------LAAVEEERCTALygvptm 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 763 ---------FP-------RKGlILGGeasewswikeiyrnipASC------KLFNHYGPSETTIgvaVYEVTKKG-LSNQ 819
Cdd:PRK08315 300 fiaeldhpdFArfdlsslRTG-IMAG----------------SPCpievmkRVIDKMHMSEVTI---AYGMTETSpVSTQ 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 820 FST--------TPIGSSLSNNRIYILD-DKLRPVPSGIPGHIYIAGEQVARGYLNREELTAERfmedpfITDSRMYKTGD 890
Cdd:PRK08315 360 TRTddplekrvTTVGRALPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA------IDADGWMHTGD 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 891 IGKIlytgeiqflgRLDGQVKIRG------IR----VEPEEIQSQLLSHPSITEA-IVTVTKVRNEEQLVAYYVSKK-EV 958
Cdd:PRK08315 434 LAVM----------DEEGYVNIVGrikdmiIRggenIYPREIEEFLYTHPKIQDVqVVGVPDEKYGEEVCAWIILRPgAT 503
|
570 580 590
....*....|....*....|....*....|....*..
gi 497785100 959 LDK-DLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKI 994
Cdd:PRK08315 504 LTEeDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGKI 540
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
747-996 |
2.34e-09 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 62.09 E-value: 2.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 747 TPSHLKALSSE--------SGTKLfprKGLILGGEAseWS-----WIKEIYRnipasCKLFNHYGPSETTIGVAvYE-VT 812
Cdd:COG1541 182 TPSYLLYLAEVaeeegidpRDLSL---KKGIFGGEP--WSeemrkEIEERWG-----IKAYDIYGLTEVGPGVA-YEcEA 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 813 KKGLSnqfsttpigssLSNNRIY--ILD-DKLRPVPSGIPGHIYIAGeqvargyLNREELtaerfmedPFItdsRmYKTG 889
Cdd:COG1541 251 QDGLH-----------IWEDHFLveIIDpETGEPVPEGEEGELVVTT-------LTKEAM--------PLI---R-YRTG 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 890 DIGKILYT-----------GEIqfLGRLDGQVKIRGIRVEPEEIQSQLLSHPSIT-EAIVTVTKVRNEEQLV-------- 949
Cdd:COG1541 301 DLTRLLPEpcpcgrthpriGRI--LGRADDMLIIRGVNVFPSQIEEVLLRIPEVGpEYQIVVDREGGLDELTvrvelapg 378
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 497785100 950 AYYVSKKEVLDKDLQTYLkqKLPPNLVpayLVKMDTLPRHAhGK----IDR 996
Cdd:COG1541 379 ASLEALAEAIAAALKAVL--GLRAEVE---LVEPGSLPRSE-GKakrvIDR 423
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1582-1951 |
5.17e-09 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 61.33 E-value: 5.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1582 RFLDrsYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVG 1661
Cdd:cd05932 3 QVVE--FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1662 AIV---------TQTSLEEKLSKSDLPYLCTDQSQDSED-----YSLLT-KDKSYPEDIAYIIYTSGTTGTPNGVMVKHS 1726
Cdd:cd05932 81 ALFvgklddwkaMAPGVPEGLISISLPPPSAANCQYQWDdliaqHPPLEeRPTRFPEQLATLIYTSGTTGQPKGVMLTFG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1727 SVMNLISATIDEFNITQETKVGQFATISFDASLWQILMALLAGATlcVVSREEQLST-KALVKRFRD---------WNV- 1795
Cdd:cd05932 161 SFAWAAQAGIEHIGTEENDRMLSYLPLAHVTERVFVEGGSLYGGV--LVAFAESLDTfVEDVQRARPtlffsvprlWTKf 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1796 ---TLADLPPVVLDSILpeDIPSL---------------QTVSTGGERCPIKVAK-RW--SLDRNFYNVYGPTETTIATT 1854
Cdd:cd05932 239 qqgVQDKIPQQKLNLLL--KIPVVnslvkrkvlkglgldQCRLAGCGSAPVPPALlEWyrSLGLNILEAYGMTENFAYSH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1855 wyrVSSPECVQDSVpIGTPVPNTEVFIlDPDlnpvpmgviGEIYIGGVGVSNGYLNRDDLNEKRFiphpfrEEEILYKTG 1934
Cdd:cd05932 317 ---LNYPGRDKIGT-VGNAGPGVEVRI-SED---------GEILVRSPALMMGYYKDPEATAEAF------TADGFLRTG 376
|
410
....*....|....*..
gi 497785100 1935 DIGKVLHDGNLEHLGRL 1951
Cdd:cd05932 377 DKGELDADGNLTITGRV 393
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
556-929 |
2.10e-08 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 59.44 E-value: 2.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 556 EDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIITHSEY-----KTSYEGYEVP--ILYID 628
Cdd:PRK06334 67 DQHIGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLmqhlaQTHGEDAEYPfsLIYME 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 629 QLDDFL--LDEREDNLNVDC--------------DSSQLAYGIYTSGSTGIPKGVLVEHRNLsnyiyaiqtkLGNK---- 688
Cdd:PRK06334 147 EVRKELsfWEKCRIGIYMSIpfewlmrwfgvsdkDPEDVAVILFTSGTEKLPKGVPLTHANL----------LANQracl 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 689 ----PKDRYLLLQSL----AYDFCLTTIYtSLLSGGTLFFllKEDAIDPAKVEEIVQGKAIDWYKITP---SHLKALSSE 757
Cdd:PRK06334 217 kffsPKEDDVMMSFLppfhAYGFNSCTLF-PLLSGVPVVF--AYNPLYPKKIVEMIDEAKVTFLGSTPvffDYILKTAKK 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 758 SGTKLFPRKGLILGGEASEWSWIKEIYRNIPaSCKLFNHYGPSETTIGVAVYevTKKGLSNQfstTPIGSSLSNNRIYIL 837
Cdd:PRK06334 294 QESCLPSLRFVVIGGDAFKDSLYQEALKTFP-HIQLRQGYGTTECSPVITIN--TVNSPKHE---SCVGMPIRGMDVLIV 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 838 DDKLR-PVPSGIPGHIYIAGEQVARGYLNREEltAERFMEdpfITDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIR 916
Cdd:PRK06334 368 SEETKvPVSSGETGLVLTRGTSLFSGYLGEDF--GQGFVE---LGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEM 442
|
410
....*....|...
gi 497785100 917 VEPEEIQSQLLSH 929
Cdd:PRK06334 443 VSLEALESILMEG 455
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
533-906 |
2.15e-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: 59.29 E-value: 2.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 533 TYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGG--------------AYLPLD-------VESP 591
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGiavgiyttnspeacQYVAETseanilvVENQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 592 K--ERIEIItQDS--KLKAIIthsEYKTSYEGYEvPILYidQLDDFL----------LDEREDNLNVDcdssQLAYGIYT 657
Cdd:cd05933 90 KqlQKILQI-QDKlpHLKAII---QYKEPLKEKE-PNLY--SWDEFMelgrsipdeqLDAIISSQKPN----QCCTLIYT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 658 SGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDR-------YLLLQSLA---YDfclttIYTSLLSGGTLFF------- 720
Cdd:cd05933 159 SGTTGMPKGVMLSHDNITWTAKAASQHMDLRPATVgqesvvsYLPLSHIAaqiLD-----IWLPIKVGGQVYFaqpdalk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 721 -----LLKEdaIDPA----------KVEEIVQGKAID----------WYK-ITPSH-LKALSSESGTKLFPR--KGLI-- 769
Cdd:cd05933 234 gtlvkTLRE--VRPTafmgvprvweKIQEKMKAVGAKsgtlkrkiasWAKgVGLETnLKLMGGESPSPLFYRlaKKLVfk 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 770 -----LG---------GEASEWSWIKEIYR--NIPasckLFNHYGPSETTIGVAVyevtkkGLSNQFSTTPIGSSLSNNR 833
Cdd:cd05933 312 kvrkaLGldrcqkfftGAAPISRETLEFFLslNIP----IMELYGMSETSGPHTI------SNPQAYRLLSCGKALPGCK 381
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497785100 834 IYILDdklrPVPSGIpGHIYIAGEQVARGYLNREELTAERFMEDPFItdsrmyKTGDIGKILYTGEIQFLGRL 906
Cdd:cd05933 382 TKIHN----PDADGI-GEICFWGRHVFMGYLNMEDKTEEAIDEDGWL------HSGDLGKLDEDGFLYITGRI 443
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1583-1728 |
3.25e-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: 58.84 E-value: 3.25e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1583 FLDRSYTYDEVNKRANKIANQLYK-MGIRRGDRVALYHERSSEMIFGFLGILK--CGAAYvpidseLPLNRRDFILKDA- 1658
Cdd:cd05938 1 FEGETYTYRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKlgCPVAF------LNTNIRSKSLLHCf 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1659 -SVGAIVT------QTSLEE---KLSKSDLPYLCTDQSQDSEDY-SLLTK-----DKSYPEDI---------AYIIYTSG 1713
Cdd:cd05938 75 rCCGAKVLvvapelQEAVEEvlpALRADGVSVWYLSHTSNTEGViSLLDKvdaasDEPVPASLrahvtikspALYIYTSG 154
|
170
....*....|....*
gi 497785100 1714 TTGTPNGVMVKHSSV 1728
Cdd:cd05938 155 TTGLPKAARISHLRV 169
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
528-923 |
3.30e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 58.97 E-value: 3.30e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 528 HERSYTYLQTNNRAnqIARWLQkQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPL-DVESP--KERIEIITQDSKL 604
Cdd:PRK07769 54 RDLTWSQFGARNRA--VGARLQ-QVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLHAVLDDCTP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 605 KAIITHSEyktSYEGY----------EVP-ILYIDQLDDfllDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVLVEHRN 673
Cdd:PRK07769 131 SAILTTTD---SAEGVrkffrarpakERPrVIAVDAVPD---EVGATWVPPEANEDTIAYLQYTSGSTRIPAGVQITHLN 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 674 LSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFL------------LKEDAIDPAKVEEIvqgkai 741
Cdd:PRK07769 205 LPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMspaafvrrpgrwIRELARKPGGTGGT------ 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 742 dwYKITPSHLKALSSESGtklFPR-----------KGLILGGEASEWSWIKEIYrnipascKLFNHYGPSETTI----GV 806
Cdd:PRK07769 279 --FSAAPNFAFEHAAARG---LPKdgeppldlsnvKGLLNGSEPVSPASMRKFN-------EAFAPYGLPPTAIkpsyGM 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 807 AvyEVTkkgLSnqFSTTPIGSS----------LSNNRIYILD--------------------------DKLRPVPSGIPG 850
Cdd:PRK07769 347 A--EAT---LF--VSTTPMDEEptviyvdrdeLNAGRFVEVPadapnavaqvsagkvgvsewavivdpETASELPDGQIG 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 851 HIYIAGEQVARGYLNREELTAERF---------------MEDpfitDSRMYKTGDIGkILYTGEIQFLGRLDGQVKIRGI 915
Cdd:PRK07769 420 EIWLHGNNIGTGYWGKPEETAATFqnilksrlseshaegAPD----DALWVRTGDYG-VYFDGELYITGRVKDLVIIDGR 494
|
....*...
gi 497785100 916 RVEPEEIQ 923
Cdd:PRK07769 495 NHYPQDLE 502
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1017-1086 |
3.77e-08 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 52.64 E-value: 3.77e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497785100 1017 RLEEKMKDVWEKILERPVPSIDD---SFFKLGGHSLLATRLVSMIRKEFKVELSIKEFFEKPSIRELSTHLLQ 1086
Cdd:smart00823 12 LLLDLVREQVAAVLGHAAAEAIDpdrPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAA 84
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1589-2000 |
4.90e-08 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 58.20 E-value: 4.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVGAIVTQTS 1668
Cdd:PLN02387 108 TYGQVFERVCNFASGLVALGHNKEERVAIFADTRAEWLIALQGCFRQNITVVTIYASLGEEALCHSLNETEVTTVICDSK 187
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1669 LEEKLS------KSDLPYLCTDQSQDSEDYSL----------------LTKDKSY------PEDIAYIIYTSGTTGTPNG 1720
Cdd:PLN02387 188 QLKKLIdissqlETVKRVIYMDDEGVDSDSSLsgssnwtvssfsevekLGKENPVdpdlpsPNDIAVIMYTSGSTGLPKG 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1721 VMVKHSSVMNLISA---TIDE----------------FNITQETKV-GQFATISFDASLwqilmallagaTLCVVSREEQ 1780
Cdd:PLN02387 268 VMMTHGNIVATVAGvmtVVPKlgkndvylaylplahiLELAAESVMaAVGAAIGYGSPL-----------TLTDTSNKIK 336
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1781 LSTKALVKRFRDwnvTLADLPPVVLDSIlpEDiPSLQTVSTGGercpiKVAKR--------------------WSLDRNF 1840
Cdd:PLN02387 337 KGTKGDASALKP---TLMTAVPAILDRV--RD-GVRKKVDAKG-----GLAKKlfdiaykrrlaaiegswfgaWGLEKLL 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1841 YNV-------------------------------------------YGPTETTIATTWYRVSSPecvqdSV-PIGTPVPN 1876
Cdd:PLN02387 406 WDAlvfkkiravlggrirfmlsggaplsgdtqrfiniclgapigqgYGLTETCAGATFSEWDDT-----SVgRVGPPLPC 480
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1877 TEVFILDPDL-------NPVPMgviGEIYIGGVGVSNGYLNrddlNEKrfiphpfREEEIlYK----------TGDIGKV 1939
Cdd:PLN02387 481 CYVKLVSWEEggylisdKPMPR---GEIVIGGPSVTLGYFK----NQE-------KTDEV-YKvdergmrwfyTGDIGQF 545
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 1940 LHDGNLEHLGRLDHQIKVR-GFRIELGEIESLLnlqtgvkeaIVQPLGDNQNYHT------LVAYVVP 2000
Cdd:PLN02387 546 HPDGCLEIIDRKKDIVKLQhGEYVSLGKVEAAL---------SVSPYVDNIMVHAdpfhsyCVALVVP 604
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
834-999 |
6.22e-08 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 57.78 E-value: 6.22e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 834 IYILDDKLRPVPSGIPGHIYIAGEQVARgYLNREELTAERFMEDPfitdsRMYKTGDIGkilYTGEIQFLGRLDGQVKI- 912
Cdd:PRK13391 338 LHILDDDGAELPPGEPGTIWFEGGRPFE-YLNDPAKTAEARHPDG-----TWSTVGDIG---YVDEDGYLYLTDRAAFMi 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 913 --RGIRVEPEEIQSQLLSHPSITEAivTVTKVRNEE---------QLVAyYVSKKEVLDKDLQTYLKQKLPPNLVPAYLV 981
Cdd:PRK13391 409 isGGVNIYPQEAENLLITHPKVADA--AVFGVPNEDlgeevkavvQPVD-GVDPGPALAAELIAFCRQRLSRQKCPRSID 485
|
170
....*....|....*...
gi 497785100 982 KMDTLPRHAHGKIDRKAL 999
Cdd:PRK13391 486 FEDELPRLPTGKLYKRLL 503
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
1759-2054 |
1.03e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 56.93 E-value: 1.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1759 LWQILMALLAGATLCVVSREEQLSTKALVKRFRDWNVTLAdlpPVVLDSILPEDIPSLQ---TVSTGGercpikvAKRWS 1835
Cdd:PRK07445 175 LMQFMRSFLTGGKLVILPYKRLKSGQELPPNPSDFFLSLV---PTQLQRLLQLRPQWLAqfrTILLGG-------APAWP 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1836 --LDR-NFYNV-----YGPTETT--IATTwyrvsSPE---CVQDSVpiGTPVPNTEVFILDPDlnpvpmgvIGEIYIGGV 1902
Cdd:PRK07445 245 slLEQaRQLQLrlaptYGMTETAsqIATL-----KPDdflAGNNSS--GQVLPHAQITIPANQ--------TGNITIQAQ 309
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1903 GVSNGYlnrddlnekrfIPHpFREEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLnLQTG-VKEAI 1981
Cdd:PRK07445 310 SLALGY-----------YPQ-ILDSQGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAI-LATGlVQDVC 376
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497785100 1982 VQPLGDNQNYHTLVAYVVP-HGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVDRHSLPTAVHIFRQ 2054
Cdd:PRK07445 377 VLGLPDPHWGEVVTAIYVPkDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQIAVQRLG 450
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
533-934 |
1.32e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 57.06 E-value: 1.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 533 TYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPL----DVESPKERIE------------ 596
Cdd:PTZ00237 94 TYYQLYEKVCEFSRVLLNLNISKNDNVLIYMANTLEPLIAMLSCARIGATHCVLfdgySVKSLIDRIEtitpkliittny 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 597 ------IITQDSKLKAIITHSEYKTSYegyeVPILYIDQLDDF-----------------LLDE----REDNLN-----V 644
Cdd:PTZ00237 174 gilndeIITFTPNLKEAIELSTFKPSN----VITLFRNDITSEsdlkkietiptipntlsWYDEikkiKENNQSpfyeyV 249
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 645 DCDSSQLAYGIYTSGSTGIPKGVLVEH-RNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLSGGTlfFLLK 723
Cdd:PTZ00237 250 PVESSHPLYILYTSGTTGNSKAVVRSNgPHLVGLKYYWRSIIEKDIPTVVFSHSSIGWVSFHGFLYGSLSLGNT--FVMF 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 724 EDAIDPAKVEEIVQGKAIDWYKIT-----PSHLKAL--SSESGTKLFPR------KGLILGGEASEWSWIKEIYRNIpaS 790
Cdd:PTZ00237 328 EGGIIKNKHIEDDLWNTIEKHKVThtltlPKTIRYLikTDPEATIIRSKydlsnlKEIWCGGEVIEESIPEYIENKL--K 405
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 791 CKLFNHYGPSETTIgvaVYEVTKKGLSNQFSTT-------------PIGSSLSNNRIYILDDKLrPVPSGIpghiyiage 857
Cdd:PTZ00237 406 IKSSRGYGQTEIGI---TYLYCYGHINIPYNATgvpsifikpsilsEDGKELNVNEIGEVAFKL-PMPPSF--------- 472
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 858 qvARGYLNREELTAERFMEDPfitdsRMYKTGDIGkilYTGEIQFLG---RLDGQVKIRGIRVEPEEIQSQLLSHPSITE 934
Cdd:PTZ00237 473 --ATTFYKNDEKFKQLFSKFP-----GYYNSGDLG---FKDENGYYTivsRSDDQIKISGNKVQLNTIETSILKHPLVLE 542
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1557-1940 |
1.53e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 56.59 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1557 PRSIKDciqySFENWVRSSPNHIALRFLD------RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFL 1630
Cdd:PRK12582 48 PRSIPH----LLAKWAAEAPDRPWLAQREpghgqwRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTL 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1631 GILKCGAAYVPIDSELPLNRRDFI-LKD-----------ASVGAIVTQtSLEEkLSKSDLPYLCTDQSQDSEDYS----L 1694
Cdd:PRK12582 124 AAMQAGVPAAPVSPAYSLMSHDHAkLKHlfdlvkprvvfAQSGAPFAR-ALAA-LDLLDVTVVHVTGPGEGIASIafadL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1695 LTK------DKSY----PEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVGQF-----------ATI 1753
Cdd:PRK12582 202 AATpptaavAAAIaaitPDTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPVSldwmpwnhtmgGNA 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1754 SFDASLWqilmallAGATLCVvsrEEQLSTKAL----VKRFRDWN-VTLADLP-------------PVVLDSI------- 1808
Cdd:PRK12582 282 NFNGLLW-------GGGTLYI---DDGKPLPGMfeetIRNLREISpTVYGNVPagyamlaeamekdDALRRSFfknlrlm 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1809 ------LPEDI-PSLQ--TVSTGGERCPikvakrwsldrnFYNVYGPTET---TIATTWyrvsSPECVQDsvpIGTPVPN 1876
Cdd:PRK12582 352 ayggatLSDDLyERMQalAVRTTGHRIP------------FYTGYGATETaptTTGTHW----DTERVGL---IGLPLPG 412
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497785100 1877 TEvfildpdLNPVPMGVIGEIYIGGVGVSNGYLNRDDLNEKRFiphpfrEEEILYKTGDIGKVL 1940
Cdd:PRK12582 413 VE-------LKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAF------DEEGFYRLGDAARFV 463
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1589-1729 |
1.60e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 56.77 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVG-AIVTQT 1667
Cdd:PLN02861 79 TYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGITYVPLYDTLGANAVEFIINHAEVSiAFVQES 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1668 SLEEKLS----------------------KSDLPYLCTD-------QSQDSEDYSLLTKDKSypeDIAYIIYTSGTTGTP 1718
Cdd:PLN02861 159 KISSILSclpkcssnlktivsfgdvsseqKEEAEELGVScfsweefSLMGSLDCELPPKQKT---DICTIMYTSGTTGEP 235
|
170
....*....|.
gi 497785100 1719 NGVMVKHSSVM 1729
Cdd:PLN02861 236 KGVILTNRAII 246
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
652-994 |
1.88e-07 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 56.17 E-value: 1.88e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 652 AYGIYTSGSTGIPKGVLVEhrnlsnyiyaIQTKLGNKPKDRYLLLQSLAYDFCLTTIYTSLLS----------------G 715
Cdd:PRK13390 151 AVMLYSSGTTGFPKGIQPD----------LPGRDVDAPGDPIVAIARAFYDISESDIYYSSAPiyhaaplrwcsmvhalG 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 716 GTLFFLLKEDAIDPAKveeivqgkAIDWYKITPSH--------LKALSSESGTK--LFPRKGLILGG-------EASEWS 778
Cdd:PRK13390 221 GTVVLAKRFDAQATLG--------HVERYRITVTQmvptmfvrLLKLDADVRTRydVSSLRAVIHAAapcpvdvKHAMID 292
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 779 WIKEIyrnipasckLFNHYGPSETTiGVAVYEvTKKGLSNQFSttpIGSSLSNNrIYILDDKLRPVPSGIPGHIYIAGEQ 858
Cdd:PRK13390 293 WLGPI---------VYEYYSSTEAH-GMTFID-SPDWLAHPGS---VGRSVLGD-LHICDDDGNELPAGRIGTVYFERDR 357
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 859 VARGYLNREELTAE-RFMEDPFITdsrmyKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITE-AI 936
Cdd:PRK13390 358 LPFRYLNDPEKTAAaQHPAHPFWT-----TVGDLGSVDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDvAV 432
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 497785100 937 VTVTKVRNEEQLVAYY-----VSKKEVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGKI 994
Cdd:PRK13390 433 IGVPDPEMGEQVKAVIqlvegIRGSDELARELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKL 495
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
1589-1981 |
2.60e-07 |
|
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: 55.83 E-value: 2.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIdseLPLNRRD---FILKDASVGAIV- 1664
Cdd:cd05933 10 TYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGI---YTTNSPEacqYVAETSEANILVv 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1665 -TQTSLEEKLS-KSDLPYL----------------------CTDQSQDSEDYSLLTK-DKSYPEDIAYIIYTSGTTGTPN 1719
Cdd:cd05933 87 eNQKQLQKILQiQDKLPHLkaiiqykeplkekepnlyswdeFMELGRSIPDEQLDAIiSSQKPNQCCTLIYTSGTTGMPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1720 GVMVKHSSVMNLISATIDEFNItQETKVGQFATISF------DASLWQILMALLAGATLCVVSREEQLSTkaLVKRFRDW 1793
Cdd:cd05933 167 GVMLSHDNITWTAKAASQHMDL-RPATVGQESVVSYlplshiAAQILDIWLPIKVGGQVYFAQPDALKGT--LVKTLREV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1794 NVTLADLPPVVLDSILpEDIPSL----------------------QTVSTGGERCPI---KVAKR--------------- 1833
Cdd:cd05933 244 RPTAFMGVPRVWEKIQ-EKMKAVgaksgtlkrkiaswakgvgletNLKLMGGESPSPlfyRLAKKlvfkkvrkalgldrc 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1834 ------------------WSLDRNFYNVYGPTETTIATTwyrVSSPECVQdSVPIGTPVPNTEVFILDPDLNPvpmgvIG 1895
Cdd:cd05933 323 qkfftgaapisretleffLSLNIPIMELYGMSETSGPHT---ISNPQAYR-LLSCGKALPGCKTKIHNPDADG-----IG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1896 EIYIGGVGVSNGYLNRDDLNEKRFiphpfrEEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGfrielGEIESLLNLQT 1975
Cdd:cd05933 394 EICFWGRHVFMGYLNMEDKTEEAI------DEDGWLHSGDLGKLDEDGFLYITGRIKELIITAG-----GENVPPVPIED 462
|
....*.
gi 497785100 1976 GVKEAI 1981
Cdd:cd05933 463 AVKKEL 468
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1589-1733 |
3.25e-07 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 55.49 E-value: 3.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYH-ERSSEMIFGflgiLKCgAAY----VPIDSELPLNRRDFILKDASVGAI 1663
Cdd:PLN02736 80 TYGEAGTARTAIGSGLVQHGIPKGACVGLYFiNRPEWLIVD----HAC-SAYsyvsVPLYDTLGPDAVKFIVNHAEVAAI 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1664 -VTQTSLEEKLS-----------------KSDLPYLCTDQSQDSEDYS-LLTKDKSY--------PEDIAYIIYTSGTTG 1716
Cdd:PLN02736 155 fCVPQTLNTLLSclseipsvrlivvvggaDEPLPSLPSGTGVEIVTYSkLLAQGRSSpqpfrppkPEDVATICYTSGTTG 234
|
170
....*....|....*..
gi 497785100 1717 TPNGVMVKHSsvmNLIS 1733
Cdd:PLN02736 235 TPKGVVLTHG---NLIA 248
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
657-999 |
8.28e-07 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 54.19 E-value: 8.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 657 TSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDF-CLTTIYTSLLSGGTLFFLLKEDAIDPAKVEEI 735
Cdd:PRK07529 221 TGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGDTVFCGLPLFHVNaLLVTGLAPLARGAHVVLATPQGYRGPGVIANF 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 736 vqGKAIDWYKIT-----PSHLKAL----------SS----ESGTKLFPRkglilggeasewswikEIYRNIPASC--KLF 794
Cdd:PRK07529 301 --WKIVERYRINflsgvPTVYAALlqvpvdghdiSSlryaLCGAAPLPV----------------EVFRRFEAATgvRIV 362
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 795 NHYGPSETTIGVAVyevtkkglsnQFSTTP--IGSS-----LSNNRIYILDDK---LRPVPSGIPGHIYIAGEQVARGYL 864
Cdd:PRK07529 363 EGYGLTEATCVSSV----------NPPDGErrIGSVglrlpYQRVRVVILDDAgryLRDCAVDEVGVLCIAGPNVFSGYL 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 865 NreeltaERFMEDPFItDSRMYKTGDIGKILYTGEIQFLGRldgqVK---IRG---IrvEPEEIQSQLLSHPSITEAIVt 938
Cdd:PRK07529 433 E------AAHNKGLWL-EDGWLNTGDLGRIDADGYFWLTGR----AKdliIRGghnI--DPAAIEEALLRHPAVALAAA- 498
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 939 VTK--VRNEEQLVAYYVSKK--EVLDKDLQTYLKQKLP-PNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK07529 499 VGRpdAHAGELPVAYVQLKPgaSATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPAL 564
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
921-993 |
9.40e-07 |
|
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: 48.31 E-value: 9.40e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 497785100 921 EIQSQLLSHPSITEAivTVTKVRNE---EQLVAYYVSKK--EVLDKDLQTYLKQKLPPNLVPAYLVKMDTLPRHAHGK 993
Cdd:pfam13193 1 EVESALVSHPAVAEA--AVVGVPDElkgEAPVAFVVLKPgvELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1702-1990 |
1.40e-06 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 53.23 E-value: 1.40e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1702 PEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETKVG-QFATISFDASLWQILMALLAGATLCvvsreeQ 1780
Cdd:PRK05851 151 SGGPAVLQGTAGSTGTPRTAILSPGAVLSNLRGLNARVGLDAATDVGcSWLPLYHDMGLAFLLTAALAGAPLW------L 224
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1781 LSTKALVK---RFRDW----NVTLADLPPVVLDSI------LPE-DIPSLQTVSTGGErcPIKVA---------KRWSLD 1837
Cdd:PRK05851 225 APTTAFSAspfRWLSWlsdsRATLTAAPNFAYNLIgkyarrVSDvDLGALRVALNGGE--PVDCDgferfatamAPFGFD 302
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1838 -RNFYNVYGPTETTIATT---------WYRVSSPE--CVQDSVPIGTPVPNTEVFILDPDlNPVPMGV--IGEIYIGGVG 1903
Cdd:PRK05851 303 aGAAAPSYGLAESTCAVTvpvpgiglrVDEVTTDDgsGARRHAVLGNPIPGMEVRISPGD-GAAGVAGreIGEIEIRGAS 381
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1904 VSNGYLNRDdlnekrfiphPFREEEiLYKTGDIGkVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQ 1983
Cdd:PRK05851 382 MMSGYLGQA----------PIDPDD-WFPTGDLG-YLVDGGLVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVV 449
|
....*..
gi 497785100 1984 PLGDNQN 1990
Cdd:PRK05851 450 AVGTGEG 456
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
647-891 |
2.68e-06 |
|
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: 52.46 E-value: 2.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 647 DSSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLL-LQSLAYDFCLTTIYTSLLSGGTLFFLLKED 725
Cdd:cd17632 221 DDDPLALLIYTSGSTGTPKGAMYTERLVATFWLKVSSIQDIRPPASITLnFMPMSHIAGRISLYGTLARGGTAYFAAASD 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 726 ---------AIDPA------KVEEIVQ---GKAIDWYKITPSHLKALSSESGTKLfpRKGLiLGGE-----------ASE 776
Cdd:cd17632 301 mstlfddlaLVRPTelflvpRVCDMLFqryQAELDRRSVAGADAETLAERVKAEL--RERV-LGGRllaavcgsaplSAE 377
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 777 WSWIKEIYRNIPasckLFNHYGPSETtigvavyevtkkglsnqfsttpiGSSLSNNRIY---ILDDKLRPVP-------- 845
Cdd:cd17632 378 MKAFMESLLDLD----LHDGYGSTEA-----------------------GAVILDGVIVrppVLDYKLVDVPelgyfrtd 430
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 497785100 846 SGIP-GHIYIAGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDI 891
Cdd:cd17632 431 RPHPrGELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDV 471
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
530-937 |
3.35e-06 |
|
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: 52.04 E-value: 3.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 530 RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGGAYLPLDVESPKERIEIITQDSKLKAIIT 609
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 610 HSEYKTS--YE-GYEVP----ILYID----------QLDDF--------LLDERE----DNLNVDCDSSQLAYGIYTSGS 660
Cdd:cd17641 90 EDEEQVDklLEiADRIPsvryVIYCDprgmrkyddpRLISFedvvalgrALDRRDpglyEREVAAGKGEDVAVLCTTSGT 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 661 TGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAY--DFCLTtIYTSLLSGGTLFFL-----LKED--AIDPAK 731
Cdd:cd17641 170 TGKPKLAMLSHGNFLGHCAAYLAADPLGPGDEYVSVLPLPWigEQMYS-VGQALVCGFIVNFPeepetMMEDlrEIGPTF 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 732 V-------EEI---VQGKAID--WYKitpSHLKALSSESGTKLFPR--KGLILGGEASEWSWIKE--IYRnipascKLFN 795
Cdd:cd17641 249 VllpprvwEGIaadVRARMMDatPFK---RFMFELGMKLGLRALDRgkRGRPVSLWLRLASWLADalLFR------PLRD 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 796 HYG----PSETTIGVAV-------YEVTKKGLSNQFSTTPIGSSLSNNRiyilDDKLRPVPSGIP-----------GHIY 853
Cdd:cd17641 320 RLGfsrlRSAATGGAALgpdtfrfFHAIGVPLKQLYGQTELAGAYTVHR----DGDVDPDTVGVPfpgtevridevGEIL 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 854 IAGEQVARGYLNREELTAERFMEDPFItdsrmyKTGDIGKILYTGEIQFLGRL-DGQVKIRGIRVEPEEIQSQLLSHPSI 932
Cdd:cd17641 396 VRSPGVFVGYYKNPEATAEDFDEDGWL------HTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFSPQFIENKLKFSPYI 469
|
....*
gi 497785100 933 TEAIV 937
Cdd:cd17641 470 AEAVV 474
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
655-995 |
5.06e-06 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 51.89 E-value: 5.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 655 IYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLT--TIYTsLLSGGTLFFLlkedaidPAKV 732
Cdd:PRK06814 799 LFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNALPVFHSFGLTggLVLP-LLSGVKVFLY-------PSPL 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 733 EeivqgkaidwYKITPSHLKALSSES--GTKLFpRKG---------------LILGGEAsewswIKEIYRNIPAS---CK 792
Cdd:PRK06814 871 H----------YRIIPELIYDTNATIlfGTDTF-LNGyaryahpydfrslryVFAGAEK-----VKEETRQTWMEkfgIR 934
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 793 LFNHYGPSETTIGVAVyevtKKGLSNQFSTtpIGSSLSNnriyiLDDKLRPVPsGIP--GHIYIAGEQVARGYLNREelt 870
Cdd:PRK06814 935 ILEGYGVTETAPVIAL----NTPMHNKAGT--VGRLLPG-----IEYRLEPVP-GIDegGRLFVRGPNVMLGYLRAE--- 999
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 871 AERFMEDPfitDSRMYKTGDIGKILYTGEIQFLGRLDGQVKIRGIRVE---PEEIQSQLlsHPSITEAIVTVTKVRNEEQ 947
Cdd:PRK06814 1000 NPGVLEPP---ADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISlaaVEELAAEL--WPDALHAAVSIPDARKGER 1074
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 497785100 948 LVaYYVSKKEVLDKDLQTYLKQKLPPNL-VPAYLVKMDTLPRHAHGKID 995
Cdd:PRK06814 1075 II-LLTTASDATRAAFLAHAKAAGASELmVPAEIITIDEIPLLGTGKID 1122
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1966-2034 |
6.86e-06 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 46.00 E-value: 6.86e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497785100 1966 EIESLLNLQTGVKEAIVQPLGDNQNYHTLVAYVVPHGEWEEKKI--IEELRSKLPEHMVPSIFVQMEELPR 2034
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLEEelVAHVREELGPYAVPKEVVFVDELPK 71
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1702-1988 |
7.36e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 51.22 E-value: 7.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1702 PEDIAYIIYTSGTTGTPNGVMVKHSSVMNLISATIDEFNITQETkVGQFATISF--DASLWQILMALLAGATLCVVSRee 1779
Cdd:PRK07867 151 PDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDD-VCYVSMPLFhsNAVMAGWAVALAAGASIALRRK-- 227
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1780 qLSTKALVKRFRDWNVTLADLPPVVLDSIL-----PEDIPSLQTVSTGGERCPIKVAKrwsLDRNF----YNVYGPTETT 1850
Cdd:PRK07867 228 -FSASGFLPDVRRYGATYANYVGKPLSYVLatperPDDADNPLRIVYGNEGAPGDIAR---FARRFgcvvVDGFGSTEGG 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1851 IATTWYRVSSPECvqdsvpIGTPVPNTEvfILDPD-LNPVPMGV------------IGEIY-IGGVGVSNGYLNRDDLNE 1916
Cdd:PRK07867 304 VAITRTPDTPPGA------LGPLPPGVA--IVDPDtGTECPPAEdadgrllnadeaIGELVnTAGPGGFEGYYNDPEADA 375
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 497785100 1917 KRFiphpfreEEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLNLQTGVKEAIVQPLGDN 1988
Cdd:PRK07867 376 ERM-------RGGVYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDP 440
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1583-1740 |
1.03e-05 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 50.75 E-value: 1.03e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1583 FLDRSY-TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDASVG 1661
Cdd:PTZ00216 116 FNETRYiTYAELWERIVNFGRGLAELGLTKGSNVAIYEETRWEWLASIYGIWSQSMVAATVYANLGEDALAYALRETECK 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1662 AIVTQTS----LEEKLSKSDLP-----YLCT-DQSQDSEDYSLLT------------KDKSYP-----EDIAYIIYTSGT 1714
Cdd:PTZ00216 196 AIVCNGKnvpnLLRLMKSGGMPnttiiYLDSlPASVDTEGCRLVAwtdvvakghsagSHHPLNipennDDLALIMYTSGT 275
|
170 180
....*....|....*....|....*.
gi 497785100 1715 TGTPNGVMVKHSSVMNLISATIDEFN 1740
Cdd:PTZ00216 276 TGDPKGVMHTHGSLTAGILALEDRLN 301
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
1586-1993 |
1.51e-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: 50.11 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1586 RSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGFLGILKCGAAYVPIDSELPLNRRDFILKDAsvGAIVT 1665
Cdd:cd17641 10 QEFTWADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYT--GARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1666 QTSLEEK------------------------LSKSDLPYLcTDQSQ--------DSEDYSLLTK--DKSYPEDIAYIIYT 1711
Cdd:cd17641 88 IAEDEEQvdklleiadripsvryviycdprgMRKYDDPRL-ISFEDvvalgralDRRDPGLYERevAAGKGEDVAVLCTT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1712 SGTTGTPNGVMVKHSSV--MNLISATIDEFNITQETkvgqfatISFDASLW---QIL---MALLAGATLCVVsrEEQLST 1783
Cdd:cd17641 167 SGTTGKPKLAMLSHGNFlgHCAAYLAADPLGPGDEY-------VSVLPLPWigeQMYsvgQALVCGFIVNFP--EEPETM 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1784 KALVK----RF-----RDWN-------VTLADLPPV--------------VLDSILPEDIPS------------------ 1815
Cdd:cd17641 238 MEDLReigpTFvllppRVWEgiaadvrARMMDATPFkrfmfelgmklglrALDRGKRGRPVSlwlrlaswladallfrpl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1816 --------LQTVSTGGERCPIKVAKRW-SLDRNFYNVYGPTETTIATTWYRVSS--PECVqdsvpiGTPVPNTEVFILDp 1884
Cdd:cd17641 318 rdrlgfsrLRSAATGGAALGPDTFRFFhAIGVPLKQLYGQTELAGAYTVHRDGDvdPDTV------GVPFPGTEVRIDE- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1885 dlnpvpmgvIGEIYIGGVGVSNGYLNRDDLNEKRFIphpfreEEILYKTGDIGKVLHDGNLEHLGRL-DHQIKVRGFRIE 1963
Cdd:cd17641 391 ---------VGEILVRSPGVFVGYYKNPEATAEDFD------EDGWLHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFS 455
|
490 500 510
....*....|....*....|....*....|
gi 497785100 1964 LGEIESLLNLQTGVKEAIVqpLGDNQNYHT 1993
Cdd:cd17641 456 PQFIENKLKFSPYIAEAVV--LGAGRPYLT 483
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
1589-1732 |
2.65e-05 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 49.43 E-value: 2.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1589 TYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSEMIFGflgiLKCGAAY----VPIDSELPLNRRDFILKDASVG--- 1661
Cdd:PLN02430 78 TYKEVYEEVLQIGSALRASGAEPGSRVGIYGSNCPQWIVA----MEACAAHslicVPLYDTLGPGAVDYIVDHAEIDfvf 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1662 ---------------------AIVTQTSL-EEKLSKSD---------LPYLCTDQSQDSEDYSlltkdkSYPEDIAYIIY 1710
Cdd:PLN02430 154 vqdkkikellepdcksakrlkAIVSFTSVtEEESDKASqigvktyswIDFLHMGKENPSETNP------PKPLDICTIMY 227
|
170 180
....*....|....*....|..
gi 497785100 1711 TSGTTGTPNGVMVKHSSVMNLI 1732
Cdd:PLN02430 228 TSGTSGDPKGVVLTHEAVATFV 249
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
648-718 |
3.74e-05 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 48.96 E-value: 3.74e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 497785100 648 SSQLAYGIYTSGSTGIPKGVLVEHRNLSNYIYAIQT---KLGnkPKDRYLLLQSLAYDFCLTTIYTSLLSGGTL 718
Cdd:PLN02387 249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTvvpKLG--KNDVYLAYLPLAHILELAAESVMAAVGAAI 320
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
826-996 |
4.57e-05 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 48.46 E-value: 4.57e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 826 GSSLSNNRIYILDDKLRPVPSGIPGHIYIAGEQVARGYLNREElTAERFMEDPFItdsrmyKTGDIGkILYTGEIQFLGR 905
Cdd:PRK09192 388 GKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRDEE-SQDVLAADGWL------DTGDLG-YLLDGYLYITGR 459
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 906 LDGQVKIRGIRVEPEEIQSQLLSHPSIT--EAIVTVTKVRNEEQLVAYYVSK------KEVLDKDLQTYLKQKLPPN--- 974
Cdd:PRK09192 460 AKDLIIINGRNIWPQDIEWIAEQEPELRsgDAAAFSIAQENGEKIVLLVQCRisdeerRGQLIHALAALVRSEFGVEaav 539
|
170 180
....*....|....*....|...
gi 497785100 975 -LVPAYlvkmdTLPRHAHGKIDR 996
Cdd:PRK09192 540 eLVPPH-----SLPRTSSGKLSR 557
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1702-2041 |
5.51e-05 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 48.42 E-value: 5.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1702 PEDIAYIIYTSGTTGTPNGVMVKHSsvmNLISatidefNITQETkvgqfATISFDAS--LWQIL-----MALLAGATLCV 1774
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHR---NLLA------NRAQVA-----ARIDFSPEdkVFNALpvfhsFGLTGGLVLPL 857
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1775 VSReeqlstkalVKRF-----RDWNVtladLPPVVLDS---IL---------------PEDIPSLQTVSTGGErcPIKVA 1831
Cdd:PRK06814 858 LSG---------VKVFlypspLHYRI----IPELIYDTnatILfgtdtflngyaryahPYDFRSLRYVFAGAE--KVKEE 922
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1832 KRWSLDRNF----YNVYGPTETtiattwyrvsSPecvqdSVPIGTPV---PNTEVFIL---DPDLNPVP---MGviGEIY 1898
Cdd:PRK06814 923 TRQTWMEKFgiriLEGYGVTET----------AP-----VIALNTPMhnkAGTVGRLLpgiEYRLEPVPgidEG--GRLF 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1899 IGGVGVSNGYLNRDDlnekrfiPHPFRE-EEILYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIESLLN-LQTG 1976
Cdd:PRK06814 986 VRGPNVMLGYLRAEN-------PGVLEPpADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAeLWPD 1058
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 497785100 1977 VKEAIVQpLGDNQNYHTLVAYVVPHGEWEEKKIIEELRSKLPEHMVPSIFVQMEELPRLNNKKVD 2041
Cdd:PRK06814 1059 ALHAAVS-IPDARKGERIILLTTASDATRAAFLAHAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
530-671 |
9.02e-05 |
|
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: 47.42 E-value: 9.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 530 RSYTYLQTNNRANQIARWLQKQGIGKEDFIGIQLQPCAKAIIAMLGVLKAGgaylpldVESPkerieIITQDSKLKAI-- 607
Cdd:cd05939 2 RHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIG-------VETA-----LINSNLRLESLlh 69
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497785100 608 -ITHSEYKTsyegyevpiLYIDQLDDFLLDEREDNLNVDCDS--SQLAYgIYTSGSTGIPKGVLVEH 671
Cdd:cd05939 70 cITVSKAKA---------LIFNLLDPLLTQSSTEPPSQDDVNfrDKLFY-IYTSGTTGLPKAAVIVH 126
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
889-994 |
1.69e-04 |
|
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: 46.88 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 889 GDIGKILYTGEIQFLGRLDGQVKIRGIRVEPEEIQSQLLSHPSITEAIVTVTKVRNEEQLVAYYV--SKKEVLDKDLQ-- 964
Cdd:cd05943 489 GDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVklREGVELDDELRkr 568
|
90 100 110
....*....|....*....|....*....|..
gi 497785100 965 --TYLKQKLPPNLVPAYLVKMDTLPRHAHGKI 994
Cdd:cd05943 569 irSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
589-927 |
2.63e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 46.25 E-value: 2.63e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 589 ESPKERIEiitqdsKLKAIithseyKTSYEGYEVPILyidQLDDFLLDEREDNLNVDCDSSQLAYGIYTSGSTGIPKGVL 668
Cdd:PTZ00342 259 EYDKEKLE------KIKDL------KEKAKKLGISII---LFDDMTKNKTTNYKIQNEDPDFITSIVYTSGTSGKPKGVM 323
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 669 VEHRNLSNYIY-----AIQTKLGNKPKDRYLllqSLAYDFCLTTIYTSLLSGGTL--------FF--------------- 720
Cdd:PTZ00342 324 LSNKNLYNTVVplckhSIFKKYNPKTHLSYL---PISHIYERVIAYLSFMLGGTIniwskdinYFskdiynskgnilagv 400
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 721 ----------LLKE-DAIDPAK---VEEIVQGKAIDWYKITPSHLKAL---SSESGTKLFPRKGLIL--GGEASewswiK 781
Cdd:PTZ00342 401 pkvfnriytnIMTEiNNLPPLKrflVKKILSLRKSNNNGGFSKFLEGIthiSSKIKDKVNPNLEVILngGGKLS-----P 475
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 782 EIYRNIpasCKLFN-----HYGPSETTIGVAVYEVtkkglsNQFSTTPIGSSLSNNRIYilddKLRP-----VPSGIP-G 850
Cdd:PTZ00342 476 KIAEEL---SVLLNvnyyqGYGLTETTGPIFVQHA------DDNNTESIGGPISPNTKY----KVRTwetykATDTLPkG 542
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 497785100 851 HIYIAGEQVARGYLNREELTAERFMEDPFitdsrmYKTGDIGKILYTGEIQFLGRLDGQVKIRgirvEPEEIQSQLL 927
Cdd:PTZ00342 543 ELLIKSDSIFSGYFLEKEQTKNAFTEDGY------FKTGDIVQINKNGSLTFLDRSKGLVKLS----QGEYIETDML 609
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1585-1727 |
2.88e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 45.90 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1585 DRSYTYDEVNKRANKIANQLYKMGIRRGDRVALYHERSSE----M------------IFGflG---------ILKCGAAY 1639
Cdd:PRK00174 96 SRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEaavaMlacarigavhsvVFG--GfsaealadrIIDAGAKL 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1640 VpI--DSELplnRRDFI--LKDASVGAIVTQTSLEE----KLSKSDLPYlctdqsQDSEDYSL--LTKDKSY---P---- 1702
Cdd:PRK00174 174 V-ItaDEGV---RGGKPipLKANVDEALANCPSVEKvivvRRTGGDVDW------VEGRDLWWheLVAGASDecePepmd 243
|
170 180
....*....|....*....|....*.
gi 497785100 1703 -EDIAYIIYTSGTTGTPNGVMvkHSS 1727
Cdd:PRK00174 244 aEDPLFILYTSGSTGKPKGVL--HTT 267
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
656-959 |
5.04e-04 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 45.09 E-value: 5.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 656 YTSGSTGIPKGVLVEHRNL-SNYI-YAIQTKLGnkPKDRYLLLQSLAYDFCLTTIYTSLLSGGTLFFL------LKED-- 725
Cdd:PLN02736 228 YTSGTTGTPKGVVLTHGNLiANVAgSSLSTKFY--PSDVHISYLPLAHIYERVNQIVMLHYGVAVGFYqgdnlkLMDDla 305
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 726 AIDP-------------------------------------AKVEEIVQGKAID--WYKITPSHLKAlssesgtKLFPRK 766
Cdd:PLN02736 306 ALRPtifcsvprlynriydgitnavkesgglkerlfnaaynAKKQALENGKNPSpmWDRLVFNKIKA-------KLGGRV 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 767 GLILGGEASEWSWIKEIYRnIPASCKLFNHYGPSETTigvAVYEVTKKGlsnQFSTTPIGSSLSNNRI---------YIL 837
Cdd:PLN02736 379 RFMSSGASPLSPDVMEFLR-ICFGGRVLEGYGMTETS---CVISGMDEG---DNLSGHVGSPNPACEVklvdvpemnYTS 451
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 838 DDKlrPVPSgipGHIYIAGEQVARGYLNREELTAERFMEDPFItdsrmyKTGDIGKILYTGEIQFLGRLDGQVKI-RGIR 916
Cdd:PLN02736 452 EDQ--PYPR---GEICVRGPIIFKGYYKDEVQTREVIDEDGWL------HTGDIGLWLPGGRLKIIDRKKNIFKLaQGEY 520
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 497785100 917 VEPEEIQSQLLSHPSITEAIVTVTKVRNeeQLVAYYVSKKEVL 959
Cdd:PLN02736 521 IAPEKIENVYAKCKFVAQCFVYGDSLNS--SLVAVVVVDPEVL 561
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
1702-1950 |
7.21e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 44.71 E-value: 7.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1702 PEDIAYIIYTSGTTGTPNGVMVKHSSVMNLI-----SATIDEFNITQETkvgQFATIS--FDASLwqILMALLAGATLCV 1774
Cdd:PTZ00342 303 PDFITSIVYTSGTSGKPKGVMLSNKNLYNTVvplckHSIFKKYNPKTHL---SYLPIShiYERVI--AYLSFMLGGTINI 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1775 VSR------EEQLSTKALV-----KRF-RDWNVTLAD---LPPV----------------------VLDSI------LPE 1811
Cdd:PTZ00342 378 WSKdinyfsKDIYNSKGNIlagvpKVFnRIYTNIMTEinnLPPLkrflvkkilslrksnnnggfskFLEGIthisskIKD 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1812 DI-PSLQTVSTGGERCPIKVAKRWS--LDRNFYNVYGPTETT--IATTWYRVSSPECvqdsvpIGTPV-PNTEVFILD-- 1883
Cdd:PTZ00342 458 KVnPNLEVILNGGGKLSPKIAEELSvlLNVNYYQGYGLTETTgpIFVQHADDNNTES------IGGPIsPNTKYKVRTwe 531
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497785100 1884 ----PDLNPVpmgviGEIYIGGVGVSNGYLNRDDLNEKRFIphpfreEEILYKTGDIGKVLHDGNLEHLGR 1950
Cdd:PTZ00342 532 tykaTDTLPK-----GELLIKSDSIFSGYFLEKEQTKNAFT------EDGYFKTGDIVQINKNGSLTFLDR 591
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
861-999 |
1.33e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 43.86 E-value: 1.33e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 861 RGYLNREELTAERFMEDpfitdsrMYKTGDIGKILYTGEIQFLGRldgqvkiRG--IRVEPEE-----IQSQLLSHPSIT 933
Cdd:PRK13388 364 EGYYNNPEATAERMRHG-------MYWSGDLAYRDADGWIYFAGR-------TAdwMRVDGENlsaapIERILLRHPAIN 429
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 497785100 934 EAIV-TVTKVRNEEQLVAYYVSKKEV-LDKD-LQTYL--KQKLPPNLVPAYLVKMDTLPRHAHGKIDRKAL 999
Cdd:PRK13388 430 RVAVyAVPDERVGDQVMAALVLRDGAtFDPDaFAAFLaaQPDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
49-364 |
1.88e-03 |
|
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: 43.19 E-value: 1.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 49 YPLSSIQKQIWFMSQLNPE-----LPIynehLIKINLSGKVN--IEALkksfEQIVNRHQILRmrvkqT----EDSIE-- 115
Cdd:cd19544 2 YPLAPLQEGILFHHLLAEEgdpylLRS----LLAFDSRARLDafLAAL----QQVIDRHDILR-----TailwEGLSEpv 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 116 QVITKSEP-TIQFLSLRGISGEEQQeiLSEYCRkEANYPYRLEQENLIRMSIIELSES-SYSVLFSRHHILSDGWSASIL 193
Cdd:cd19544 69 QVVWRQAElPVEELTLDPGDDALAQ--LRARFD-PRRYRLDLRQAPLLRAHVAEDPANgRWLLLLLFHHLISDHTSLELL 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 194 LSELERFynmysQNGEinpeqsQEELT--IQYHDY---ALWQEKLLTSEnlekglEYWKEKLeGDL--PMLSIG--GITQ 264
Cdd:cd19544 146 LEEIQAI-----LAGR------AAALPppVPYRNFvaqARLGASQAEHE------AFFREML-GDVdePTAPFGllDVQG 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 265 EGTGVgSEYNFKIPNILTDKLRKLAEEQKVSLYSVWLAIYKIVISKYTQETDLAVGTPIAGR--NIRETRNVIGPFINTV 342
Cdd:cd19544 208 DGSDI-TEARLALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRmqGGAGADRALGMFINTL 286
|
330 340
....*....|....*....|..
gi 497785100 343 VIRTKAeQNLSVIEYLQQVHET 364
Cdd:cd19544 287 PLRVRL-GGRSVREAVRQTHAR 307
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
655-719 |
2.56e-03 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 42.78 E-value: 2.56e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 655 IYTSGSTGIPKGVLVEHRNLSNYIYAIQTKLGNKPKDRYLLLQSLAYDFCLTT-IYTSLLSGGTLF 719
Cdd:PRK08043 371 LFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPNDRFMSALPLFHSFGLTVgLFTPLLTGAEVF 436
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1692-1969 |
2.77e-03 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 42.81 E-value: 2.77e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1692 YSLLTKDKSYPediAYIIYTSGTTGTPNGVMVKHSSvmNLISATIDEFNITQETKVGQFAT------ISFDASLWqilmA 1765
Cdd:PTZ00237 246 YEYVPVESSHP---LYILYTSGTTGNSKAVVRSNGP--HLVGLKYYWRSIIEKDIPTVVFShssigwVSFHGFLY----G 316
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1766 LLAGATLCVVSREEQLSTKALVKRFrdWNV-------TLADLPPVV--LDSILPE--------DIPSLQTVSTGGE--RC 1826
Cdd:PTZ00237 317 SLSLGNTFVMFEGGIIKNKHIEDDL--WNTiekhkvtHTLTLPKTIryLIKTDPEatiirskyDLSNLKEIWCGGEviEE 394
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 497785100 1827 PIKVAKRWSLDRNFYNVYGPTETTIaTTWYRVSSPECVQDSVpiGTPVPNTEVFILDPDLNPVPMGVIGEIYIG---GVG 1903
Cdd:PTZ00237 395 SIPEYIENKLKIKSSRGYGQTEIGI-TYLYCYGHINIPYNAT--GVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPS 471
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 497785100 1904 VSNGYLNRDDLNEKRFIPHPFreeeiLYKTGDIGKVLHDGNLEHLGRLDHQIKVRGFRIELGEIES 1969
Cdd:PTZ00237 472 FATTFYKNDEKFKQLFSKFPG-----YYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIET 532
|
|
| |
