|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1-3146 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 2091.72 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvts 80
Cdd:PRK12467 538 LSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLL--- 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dGEAEARSRFDDIVDVHVLDISSPGDADLDEEEFAGPTR--PANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYD 158
Cdd:PRK12467 615 -TQSHLLAQLPVPAGLRSLCLDEPADLLCGYSGHNPEVAldPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERLQ 693
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 159 LTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVlgAGVGELT 238
Cdd:PRK12467 694 LAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA--SRVALPR 771
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 239 SLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVI---PIGTPTRRVSARVLDAALREVPI 315
Cdd:PRK12467 772 PQRALVCGGEALQVDLLARVRALGPGARLINHYGPTETTVGVSTYELSDEERDFgnvPIGQPLANLGLYILDHYLNPVPV 851
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 316 GVPGELYLGGVQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAA 395
Cdd:PRK12467 852 GVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEAR 931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 396 LAAAPGVLHAAAAVVDGPGGQQLVGYLAPADVD--------VDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRL 467
Cdd:PRK12467 932 LLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVAdgaehqatRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKA 1011
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 468 LPEPEIAPT--LYVPPGNADEETVAGLFAELLGVERVGVTDSFFDIGGSSLSAARIAARVSKELGVDVSVRDVFESPSVR 545
Cdd:PRK12467 1012 LPKPDASAVqaTFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLA 1091
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 546 GLVHAVS----GRGSALPSVKRIEPrperLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERH 621
Cdd:PRK12467 1092 GFAQAVAaqqqGAQPALPDVDRDQP----LPLSYAQERQWFLWQLEPGSAAYHIPQALRLKGPLDIEALERSFDALVARH 1167
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 622 EVLRTVYPSVGAAPVQ---DVLPVAVAREQLDWREADSVESLVRSTTEG---FDVSTQMPLRGRFHRDGAGLHV-ALTMH 694
Cdd:PRK12467 1168 ESLRTTFVQEDGRTRQvihPVGSLTLEEPLLLAADKDEAQLKVYVEAEArqpFDLEQGPLLRVGLLRLAADEHVlVLTLH 1247
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 695 HIAMDGQSIPVLARDLMSAYAARAEGRTGGLPVLDVQYADYALWQQSVLGDADDEtsvlgEQLSHWRRVLAGLPAVTDLP 774
Cdd:PRK12467 1248 HIVSDGWSMQVLVDELVALYAAYSQGQSLQLPALPIQYADYAVWQRQWMDAGERA-----RQLAYWKAQLGGEQPVLELP 1322
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 775 MDRPRPAVLGTAGATVTVEFDDDLADRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGM 854
Cdd:PRK12467 1323 TDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGF 1402
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 855 FVNTLLLRTQVDPGHSVGDLLGNVRTTVLDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTYTeptvNDVAGLEAS-- 932
Cdd:PRK12467 1403 FVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQ----RDDHQAQAQlp 1478
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 933 GIQAAPVDTGVVNAKFDLTVAVRARSGGtpMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDDQNTAVGDIDIVGAARA 1012
Cdd:PRK12467 1479 GLSVESLSWESQTAQFDLTLDTYESSEG--LQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAER 1556
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1013 KSV----SAPVSARTPGAMVGRGGEVEAGTlidvlaqrdlDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDV 1088
Cdd:PRK12467 1557 RQIlegwNATHTGYPLARLVHQLIEDQAAA----------TPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVL 1626
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1089 VAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDASTRARLGESSCEWVDLADLEAEAESGD 1168
Cdd:PRK12467 1627 VGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQSHLQARLPLPDGLRSLVLDQEDDWLEGY 1706
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1169 DITDTERNGSVRltNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDEpdtrILHVASPSFDASMFEMAWA 1248
Cdd:PRK12467 1707 SDSNPAVNLAPQ--NLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAYQLSAADV----VLQFTSFAFDVSVWELFWP 1780
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1249 IPAGHTLVIA-PQADFAGDALATVLERDEVTDMIITPSVL---ATVDP--ERAQYVRNLATGGEACPPELVERWSER--G 1320
Cdd:PRK12467 1781 LINGARLVIApPGAHRDPEQLIQLIERQQVTTLHFVPSMLqqlLQMDEqvEHPLSLRRVVCGGEALEVEALRPWLERlpD 1860
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1321 RRIFNCYGPTEATV----W-ATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTA 1395
Cdd:PRK12467 1861 TGLFNLYGPTETAVdvthWtCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTA 1940
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1396 VSFVADPFGEPGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVEstrgGRKHT 1475
Cdd:PRK12467 1941 ERFVADPFGTVGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQD----GANGK 2016
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1476 EVVAYLVAK----PGATIDSAAVLDEAAQHLAA----HMVPSQAIVIDEIPLTPAGKLDRAALPEPHAPEPAE-YVAPAN 1546
Cdd:PRK12467 2017 QLVAYVVPTdpglVDDDEAQVALRAILKNHLKAslpeYMVPAHLVFLARMPLTPNGKLDRKALPAPDASELQQaYVAPQS 2096
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1547 PAEDNLARIVAGLLGEERVSVTESFFALGGDSIMSIQLSSAAKAAGIHLSPREIFELKTIRAMAAAAAASGGPVALIEel 1626
Cdd:PRK12467 2097 ELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGTVSIDQ-- 2174
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1627 pGGGTGEMPLPPVTSWMIEhsEEPADFADFSQSLVFNVPASAAVADLQTVVEAVAAAHPMLTAVLTRSGDGWTmnagAGI 1706
Cdd:PRK12467 2175 -GPVTGDLPLLPIQQMFFA--DDIPERHHWNQSVLLEPREALDAELLEAALQALLVHHDALRLGFVQEDGGWS----AMH 2247
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1707 VPAVRE---------IDAEGALDPALVDAHRELlgamDPGTGSLLGTAVV-NGEGRRRLVIAIHHLGVDAVSWPILVEDL 1776
Cdd:PRK12467 2248 RAPEQErrpllwqvvVADKEELEALCEQAQRSL----DLEEGPLLRAVLAtLPDGSQRLLLVIHHLVVDGVSWRILLEDL 2323
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1777 VTAWAQLTSGRPIELRPEATTTRRIAHLLagQVHAR----AREVDYWLEQLPERPTsfGTSADRP---LHRRRDESSLTY 1849
Cdd:PRK12467 2324 QTAYRQLQGGQPVKLPAKTSAFKAWAERL--QTYAAsaalADELGYWQAQLQGAST--ELPCDHPqggLQRRHAASVTTH 2399
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1850 VVDDVAGSILTTVPQAFGSSVDDVLLGALARAVRAWqldNGIADggpVTVSTEGHGRDESIAGdegaIDLSRTVGWFTSI 1929
Cdd:PRK12467 2400 LDSEWTRRLLQEAPAAYRTQVNDLLLTALARVIARW---TGQAS---TLIQLEGHGREDLFDE----IDLTRTVGWFTSL 2469
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1930 TPLAVDASSDVVHAVKSAKDARLSRPAGGVGFGILRYNSDGEIAHR----PLPTIMYNYFGGGTAPSTETAPDDFLPVSD 2005
Cdd:PRK12467 2470 YPVKLSPTASLATSIKTIKEQLRAVPNKGLGFGVLRYLGSEAARQTlqalPVPRITFNYLGQFDGSFDAEKQALFVPSGE 2549
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2006 RpnmpssiTGAMRSPSV-----FGINISTAGREerrLEAKVTYATDALDEAAASDIARRWHDELRAVVELVDGGAEIGLS 2080
Cdd:PRK12467 2550 F-------SGAEQSEEAplgnwLSINGQVYGGE---LNLGWTFSQEMFDEATIQRLADAYAEELRALIEHCCSNDQRGVT 2619
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2081 RADVPGVEVTQDDLD---LIAQQYpgADVWPMTPLQQGLFFQadlanTVADHDAiDVYVTQTVLSLTGdVDPGRLRSALS 2157
Cdd:PRK12467 2620 PSDFPLAGLSQEQLDrlpVAVGDI--EDIYPLSPMQQGMLFH-----TLYEGGA-GDYINQMRVDVEG-LDVERFRTAWQ 2690
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2158 ELLARQRVLRSGFVRLPS-GAAVTVVPAEVTVPWSVIDLRaeDAASLDSRVEEVLATERTNPFDMAKPPLIRVVLVEHG- 2235
Cdd:PRK12467 2691 AVIDRHEILRSGFLWDGElEEPLQVVYKQARLPFSRLDWR--DRADLEQALDALAAADRQQGFDLLSAPLLRLTLVRTGe 2768
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2236 DGAELVVTNHHLLIDGWSSPLVLADLLSLYaTGQTftgsLPGTSGRdFADHARAVATADVEAGIAAWREVLAPVTEPTLV 2315
Cdd:PRK12467 2769 DRHHLIYTNHHILMDGWSGSQLLGEVLQRY-FGQP----PPAREGR-YRDYIAWLQAQDAEASEAFWKEQLAALEEPTRL 2842
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2316 APGHEPsADAPPR----DHQFSIDVKVTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRSPDIEGME 2391
Cdd:PRK12467 2843 ARALYP-APAEAVaghgAHYLHLDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQLRGAE 2921
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2392 SMVGMFINTIPAVVDVNPDATVVDVLTAVQNDKVKVLDHQQIGLPRLVAQTGLP--ALFDTLAVYESFPVNvdsvAGIDA 2469
Cdd:PRK12467 2922 QQLGLFINTLPVIASPRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWAGQGgeALFDSILVFENYPIS----EALKQ 2997
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2470 SSAGGLKLVGAKTSDATHYPLNLsASRRGAELALKLKYLPTAFAPEQVAVFADVLTGLLGAIADHPEATCAEIPLLPAEA 2549
Cdd:PRK12467 2998 GAPSGLRFGAVSSREQTNYPLTL-AVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHE 3076
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2550 AVELTPVTGGPATDPVT---LAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRS 2626
Cdd:PRK12467 3077 RRQVLHAWNATAAAYPSerlVHQLIEAQVARTPEAPALVFG-DQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERS 3155
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2627 AQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLGLS---VLASGDLPGQEFEWMrLDDDSVAAEIAAVPAgPI 2703
Cdd:PRK12467 3156 VEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTqahLLEQLPAPAGDTALT-LDRLDLNGYSENNPS-TR 3233
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2704 TDAErlgevtaaNLAYVIYTSGSTGRPKGVAVTHSGLANFAR--QESDRLNAGDNpvVLGFASPSFDASVLEYLLATVNE 2781
Cdd:PRK12467 3234 VMGE--------NLAYVIYTSGSTGKPKGVGVRHGALANHLCwiAEAYELDANDR--VLLFMSFSFDGAQERFLWTLICG 3303
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2782 GTLAYRPSEAVGGEVLERFIAEHGATHTFLTPSVLSTM----DPTAVPSLRVIAAGGEAVP---QPIVDRWAPATELHNL 2854
Cdd:PRK12467 3304 GCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFaedaGGADCASLDIYVFGGEAVPpaaFEQVKRKLKPRGLTNG 3383
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2855 YGPTETTIGITI----SSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTAN 2930
Cdd:PRK12467 3384 YGPTEAVVTVTLwkcgGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVAD 3463
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2931 PYGTAGQRMYRTGDVVRWTPDtdtgGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAY 3010
Cdd:PRK12467 3464 PFSGSGGRLYRTGDLARYRAD----GV-IEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLARDGAGGKQLVAY 3538
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3011 IVPVD-GAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVLE-AGEYVAPATGTERTIADVAAGVL 3088
Cdd:PRK12467 3539 VVPADpQGDWRETLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKgSREYVAPRSEVEQQLAAIWADVL 3618
|
3210 3220 3230 3240 3250
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 3089 NIDAglVSATSSFFELGGDSLSAARLAARLSDQLGVAVSVRDVFESGSIRALAETVGG 3146
Cdd:PRK12467 3619 GVEQ--VGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYSPL 3674
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-3142 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1924.34 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:PRK12316 2029 LSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTQR 2108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAearsRFDDIVDVHVLDISSPGD-ADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDL 159
Cdd:PRK12316 2109 HLLE----RLPLPAGVARLPLDRDAEwADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERYEL 2184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 160 TARDVFLYKAPITFDVSVREIFLPIAIGATlVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLgAGVGELTS 239
Cdd:PRK12316 2185 SPADCELQFMSFSFDGAHEQWFHPLLNGAR-VLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHA-ERDGRPPA 2262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 240 LRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDD----RVIPIGTPTRRVSARVLDAALREVPI 315
Cdd:PRK12316 2263 VRVYCFGGEAVPAASLRLAWEALRPVYLFNGYGPTEAVVTPLLWKCRPQDpcgaAYVPIGRALGNRRAYILDADLNLLAP 2342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 316 GVPGELYLGGVQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAA 395
Cdd:PRK12316 2343 GMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEAR 2422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 396 LAAAPGVLHAAAAVVDGPGGQQLVGYLAPADVDVDTVAATTAEL---LPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEPE 472
Cdd:PRK12316 2423 LQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDLLAELRAWLaarLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPD 2502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 473 IAP--TLYVPPGNADEETVAGLFAELLGVERVGVTDSFFDIGGSSLSAARIAARVSKELGVDVSVRDVFESPSVRGLVHA 550
Cdd:PRK12316 2503 VSQlrQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAAS 2582
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 551 VSGRGSALPSVKRIEPRPERLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPS 630
Cdd:PRK12316 2583 LESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESAAYHLPSALHLRGVLDQAALEQAFDALVLRHETLRTRFVE 2662
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 631 VGAAPVQDVLPVAVAREQLDWREADSVESLVRSTTE----GFDVSTQMPLRGRFHRDGAGLHV-ALTMHHIAMDGQSIPV 705
Cdd:PRK12316 2663 VGEQTRQVILPNMSLRIVLEDCAGVADAAIRQRVAEeiqrPFDLARGPLLRVRLLALDGQEHVlVITQHHIVSDGWSMQV 2742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 706 LARDLMSAYAARAEGRTGGLPVLDVQYADYALWQQSVLgdaddETSVLGEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGT 785
Cdd:PRK12316 2743 MVDELVQAYAGARRGEQPTLPPLPLQYADYAAWQRAWM-----DSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSH 2817
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 786 AGATVTVEFDDDLADRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQV 865
Cdd:PRK12316 2818 RGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFFVNTQVLRAQV 2897
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 866 DPGHSVGDLLGNVRTTVLDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTYTEptvNDVAGLEASGIQAAPVDTGVVN 945
Cdd:PRK12316 2898 DAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQS---GERAAAQLPGLHIESFAWDGAA 2974
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 946 AKFDLTVAVRARSGGtpMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDDQNTAVGDIDIVGAA---RAKSVSAPVSAR 1022
Cdd:PRK12316 2975 TQFDLALDTWESAEG--LGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEergQLLEAWNATAAE 3052
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1023 TPgamvgrggeVEAGTLIDVLAQRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLA 1102
Cdd:PRK12316 3053 YP---------LERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVG 3123
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1103 TWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGItdasTRARLGESSCEWVDLADLEAEAESGdditdTERNGSVRLT 1182
Cdd:PRK12316 3124 LLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL----SQSHLRLPLAQGVQVLDLDRGDENY-----AEANPAIRTM 3194
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1183 --NLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQ 1260
Cdd:PRK12316 3195 peNLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGD----RVLQFTTFSFDVFVEELFWPLMSGARVVLAGP 3270
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1261 ADFAGDALATVLERDEVTDMI-ITPSV----LATVDPERAQYVRNLATGGEACPPELVERWSErGRRIFNCYGPTEATVW 1335
Cdd:PRK12316 3271 EDWRDPALLVELINSEGVDVLhAYPSMlqafLEEEDAHRCTSLKRIVCGGEALPADLQQQVFA-GLPLYNLYGPTEATIT 3349
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1336 ATRSRMTAGKPVT--IGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgEPGARMYAT 1413
Cdd:PRK12316 3350 VTHWQCVEEGKDAvpIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF-VPGERLYRT 3428
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1414 GDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRggrkhteVVAYLVAKPGATIDSAA 1493
Cdd:PRK12316 3429 GDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQ-------LVAYVVPEDEAGDLREA 3501
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1494 VLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEPHAPE-PAEYVAPANPAEDNLARIVAGLLGEERVSVTESFF 1572
Cdd:PRK12316 3502 LKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALlQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFF 3581
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1573 ALGGDSIMSIQLSSAAKAAGIHLSPREIFELKTIRAMAAAAAASGGpvALIEElpGGGTGEMPLPPVTSWMIEhsEEPAD 1652
Cdd:PRK12316 3582 ELGGDSIISLQVVSRARQAGIRFTPKDLFQHQTIQGLARVARVGGG--VAVDQ--GPVSGETLLLPIQQQFFE--EPVPE 3655
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1653 FADFSQSLVFNVPASAAVADLQTVVEAVAAAHPMLTAVLTRSGDGWTMNAGAGIVPAVREIDAEGALDPALVDAHRELLG 1732
Cdd:PRK12316 3656 RHHWNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAGGWTAEHLPVELGGALLWRAELDDAEELERLGEEAQR 3735
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1733 AMDPGTGSLLGTAVVN-GEGRRRLVIAIHHLGVDAVSWPILVEDLVTAWAQLTSGRPIELRPEATTTRRIAHLLagQVHA 1811
Cdd:PRK12316 3736 SLDLADGPLLRALLATlADGSQRLLLVIHHLVVDGVSWRILLEDLQQAYQQLLQGEAPRLPAKTSSFKAWAERL--QEHA 3813
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1812 RA----REVDYWLEQLPerptsfGTSADRP-------LHRRRDESSLTYVVDDVAGSILTTVPQAFGSSVDDVLLGALAR 1880
Cdd:PRK12316 3814 RGealkAELAYWQEQLQ------GVSSELPcdhpqgaLQNRHAASVQTRLDRELTRRLLQQAPAAYRTQVNDLLLTALAR 3887
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1881 AVRAWqldNGIADggpVTVSTEGHGRDESIAGdegaIDLSRTVGWFTSITPLAVDASSDVVHAVKSAKDARLSRPAGGVG 1960
Cdd:PRK12316 3888 VVCRW---TGEAS---ALVQLEGHGREDLFAD----IDLSRTVGWFTSLFPVRLSPVEDLGASIKAIKEQLRAIPNKGIG 3957
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1961 FGILRYNSDGE----IAHRPLPTIMYNYFGGGTApSTETAPDDFLPVSDRpnmpssiTGAMRSP-SVFGINISTAGR-EE 2034
Cdd:PRK12316 3958 FGLLRYLGDEEsrrtLAGLPVPRITFNYLGQFDG-SFDEEMALFVPAGES-------AGAEQSPdAPLDNWLSLNGRvYG 4029
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2035 RRLEAKVTYATDALDEAAASDIARRWHDELRAVVELVDGGAEIGLSRADVPGVEVTQDDLD-LIAQQYPGADVWPMTPLQ 2113
Cdd:PRK12316 4030 GELSLDWTFSREMFEEATIQRLADDYAAELTALVEHCCDAERHGVTPSDFPLAGLDQARLDaLPLPLGEIEDIYPLSPMQ 4109
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2114 QGLFFqadlaNTVADHDAIDvYVTQTVLSLTGdVDPGRLRSALSELLARQRVLRSGFV-RLPSGAAVTVVPAEVTVPWSV 2192
Cdd:PRK12316 4110 QGMLF-----HSLYEQEAGD-YINQMRVDVQG-LDVERFRAAWQAALDRHDVLRSGFVwQGELGRPLQVVHKQVSLPFAE 4182
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2193 IDLRAedAASLDSRVEEVLATERTNPFDMAKPPLIRVVLVEHGDGA-ELVVTNHHLLIDGWSSPLVLADLLslyatgQTF 2271
Cdd:PRK12316 4183 LDWRG--RADLQAALDALAAAERERGFDLQRAPLLRLVLVRTAEGRhHLIYTNHHILMDGWSNSQLLGEVL------ERY 4254
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2272 TGSLPGTSGRDFADHARAVATADVEAGIAAWREVLAPVTEPTLVAPGHEPSADAPPR---DHQFSIDVKVTERLEALARN 2348
Cdd:PRK12316 4255 SGRPPAQPGGRYRDYIAWLQRQDAAASEAFWREQLAALDEPTRLAQAIARADLRSANgygEHVRELDATATARLREFART 4334
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2349 NSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRSPDIEGMESMVGMFINTIPAVVDVNPDATVVDVLTAVQNDKVKVL 2428
Cdd:PRK12316 4335 QRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAELPGIEGQIGLFINTLPVIATPRAQQSVVEWLQQVQRQNLALR 4414
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2429 DHQQIGLPRLV--AQTGLPALFDTLAVYESFPVNvdsvAGIDASSAGGLKLVGAKTSDATHYPLNLSASrRGAELALKLK 2506
Cdd:PRK12316 4415 EHEHTPLYEIQrwAGQGGEALFDSLLVFENYPVS----EALQQGAPGGLRFGEVTNHEQTNYPLTLAVG-LGETLSLQFS 4489
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2507 YLPTAFAPEQVAVFADVLTGLLGAIADHPEATCAEIPLLPAE---AAVELTPVTGGPATDPVTLAELFRAAARRAPDHVA 2583
Cdd:PRK12316 4490 YDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAeqqRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVA 4569
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2584 VVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSG 2663
Cdd:PRK12316 4570 VVFD-EEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSG 4648
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2664 AVLGLS-VLASGDLPgqefewmrldddsVAAEIAAVPAGPITDAERLGE------VTAANLAYVIYTSGSTGRPKGVAVT 2736
Cdd:PRK12316 4649 AALLLTqSHLLQRLP-------------IPDGLASLALDRDEDWEGFPAhdpavrLHPDNLAYVIYTSGSTGRPKGVAVS 4715
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2737 HSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGGEVLERFIAEHGATHTFLTPSVL 2816
Cdd:PRK12316 4716 HGSLVNHLHATGERYELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYL 4795
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2817 STMDPTA-----VPSLRVIAAGGEAVPQPIVDRW---APATELHNLYGPTETTIGITISSAmRPGDP-----VRLGGPIG 2883
Cdd:PRK12316 4796 QQLAEHAerdgePPSLRVYCFGGEAVAQASYDLAwraLKPVYLFNGYGPTETTVTVLLWKA-RDGDAcgaayMPIGTPLG 4874
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2884 GVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRMYRTGDVVRWTPDTdtgglTLEYTG 2963
Cdd:PRK12316 4875 NRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRADG-----VIDYLG 4949
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2964 RSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPVDGAVE---------VSELKAFAGGRLPAY 3034
Cdd:PRK12316 4950 RVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALAdadeaqaelRDELKAALRERLPEY 5029
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3035 MVPSSFTVIDELPLTPVGKLDKRALPEP--VLEAGEYVAPATGTERTIADVAAGVLNIDAglVSATSSFFELGGDSLSAA 3112
Cdd:PRK12316 5030 MVPAHLVFLARMPLTPNGKLDRKALPQPdaSLLQQAYVAPRSELEQQVAAIWAEVLQLER--VGLDDNFFELGGHSLLAI 5107
|
3210 3220 3230
....*....|....*....|....*....|
gi 1827387616 3113 RLAARLSDQLGVAVSVRDVFESGSIRALAE 3142
Cdd:PRK12316 5108 QVTSRIQLELGLELPLRELFQTPTLAAFVE 5137
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
4-3146 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1671.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvTSDGE 83
Cdd:PRK05691 1160 AELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLL-TQSHL 1238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 AEARSRFDDIVDVhvldisspgdaDLDEEEFAG-PTRPA-------NAAFTLFTSGSTGRPKAVVITHRGIANRLAADIE 155
Cdd:PRK05691 1239 LERLPQAEGVSAI-----------ALDSLHLDSwPSQAPglhlhgdNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQA 1307
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 156 QYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFneVLGAGVG 235
Cdd:PRK05691 1308 TYALDDSDVLMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLF--IDEPLAA 1385
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 236 ELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDD-RVIPIGTPTRRVSARVLDAALREVP 314
Cdd:PRK05691 1386 ACTSLRRLFSGGEALPAELRNRVLQRLPQVQLHNRYGPTETAINVTHWQCQAEDgERSPIGRPLGNVLCRVLDAELNLLP 1465
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 315 IGVPGELYLGGVQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEA 394
Cdd:PRK05691 1466 PGVAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQA 1545
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 395 ALAAAPGVLHAAAAVVDGPGGQQLVGYL---APADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEP 471
Cdd:PRK05691 1546 RLLAQPGVAQAAVLVREGAAGAQLVGYYtgeAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEP 1625
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 472 EIAPTLYVPPGNADEETVAGLFAELLGVERVGVTDSFFDIGGSSLSAARIAARVSKELGVDVSVRDVFESPSVRGLVHAV 551
Cdd:PRK05691 1626 VWQQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQV 1705
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 552 -----SGRGSALPSVKRIEpRPERLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRT 626
Cdd:PRK05691 1706 ariqaAGERNSQGAIARVD-RSQPVPLSYSQQRMWFLWQMEPDSPAYNVGGMARLSGVLDVDRFEAALQALILRHETLRT 1784
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 627 VYPSVGAAPVQDVlpVAVAREQLDWREADSVESLVRSTT----------EGFDVSTQMPLRGRFHRDGAGLH-VALTMHH 695
Cdd:PRK05691 1785 TFPSVDGVPVQQV--AEDSGLRMDWQDFSALPADARQQRlqqladseahQPFDLERGPLLRACLVKAAEREHyFVLTLHH 1862
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 696 IAMDGQSIPVLARDLMSAYAARAEGRTGGLPVLDVQYADYALWQQSVLgdaddETSVLGEQLSHWRRVLAGLPAVTDLPM 775
Cdd:PRK05691 1863 IVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQYLDYSVWQRQWL-----ESGERQRQLDYWKAQLGNEHPLLELPA 1937
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 776 DRPRPAVLGTAGATVTVEFDDDLADRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMF 855
Cdd:PRK05691 1938 DRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGAF 2017
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 856 VNTLLLRTQVDPGHSVGDLLGNVRTTVLDAFANDQVQFDELIEALAPERSSSHQPLAQI-------AFTYTEptvndvag 928
Cdd:PRK05691 2018 LNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVmcnvqrwEFQQSR-------- 2089
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 929 lEASGIQaapVDTGVVNA---KFDLTVAVRARSGgtPMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDDQNTAVGDID 1005
Cdd:PRK05691 2090 -QLAGMT---VEYLVNDAratKFDLNLEVTDLDG--RLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAELP 2163
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1006 IVGAARAKsvsapvsaRTPGAMVGRGGEVEAGTLIDVL--AQRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGV 1083
Cdd:PRK05691 2164 LLAAAEQQ--------QLLDSLAGEAGEARLDQTLHGLfaAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGV 2235
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1084 SPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDASTRARLGE---SSCEWVdladL 1160
Cdd:PRK05691 2236 GPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSDRALFEALGElpaGVARWC----L 2311
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1161 EAEAESGDDITDTERNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVdfVNSLAKITT-GTPEDEPDtriLHVASPSFD 1239
Cdd:PRK05691 2312 EDDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIA--MHCQAVIERfGMRADDCE---LHFYSINFD 2386
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1240 ASMFEMAWAIPAGHTLVIAPQADFAGDALATVLERDEVTDMIITPSvlatVDPERAQY---------VRNLATGGEACPP 1310
Cdd:PRK05691 2387 AASERLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPS----YGSQLAQWlagqgeqlpVRMCITGGEALTG 2462
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1311 ELVERWSE--RGRRIFNCYGPTEATVW-----ATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGL 1383
Cdd:PRK05691 2463 EHLQRIRQafAPQLFFNAYGPTETVVMplaclAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGL 2542
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1384 ARGYLGRPGQTAVSFVADPFGEPGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVV 1463
Cdd:PRK05691 2543 AQGYHDRPGLTAERFVADPFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVL 2622
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1464 GVEsTRGGRkhtEVVAYLVAKPGATIDSA------AVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPephAPE 1537
Cdd:PRK05691 2623 ALD-TPSGK---QLAGYLVSAVAGQDDEAqaalreALKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALP---APD 2695
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1538 PA----EYVAPANPAEDNLARIVAGLLGEERVSVTESFFALGGDSIMSIQLSSAAKAAGIHLSPREIFELKTIRAMAAAA 1613
Cdd:PRK05691 2696 PElnrqAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRARQLGIHFSPRDLFQHQTVQTLAAVA 2775
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1614 AASGGPVAliEElpGGGTGEMPLPPVTSWMIEhsEEPADFADFSQSLVFNVPASAAVADLQTVVEAVAAAHPMLTAVLTR 1693
Cdd:PRK05691 2776 THSEAAQA--EQ--GPLQGASGLTPIQHWFFD--SPVPQPQHWNQALLLEPRQALDPALLEQALQALVEHHDALRLRFSQ 2849
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1694 SGDGWTMNAGAG------IVPAVREIDAEGALdpaLVDAHRELlgamDPGTGSLLGTAVVNG-EGRRRLVIAIHHLGVDA 1766
Cdd:PRK05691 2850 ADGRWQAEYRAVtaqellWQVTVADFAECAAL---FADAQRSL----DLQQGPLLRALLVDGpQGQQRLLLAIHHLVVDG 2922
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1767 VSWPILVEDLVTAWAQLTSGRPIELRPEATTTRRIAHLLAGQVHARA--REVDYWLEQLPERPTSFgtSADRPL--HRRR 1842
Cdd:PRK05691 2923 VSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAGSESlrEELGWWQAQLGGPRAEL--PCDRPQggNLNR 3000
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1843 DESSLTYVVD-DVAGSILTTVPQAFGSSVDDVLLGALARAVRAWQLDNGiadggpVTVSTEGHGRDesiaGDEGAIDLSR 1921
Cdd:PRK05691 3001 HAQTVSVRLDaERTRQLLQQAPAAYRTQVNDLLLTALARVLCRWSGQPS------VLVQLEGHGRE----ALFDDIDLTR 3070
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1922 TVGWFTSITPL----AVDASSDVVHAVKSAKDARLSRPAGGVGFGILRYNSDG----EIAHRPLPTIMYNYFGggtAPST 1993
Cdd:PRK05691 3071 SVGWFTSAYPLrltpAPGDDAARGESIKAIKEQLRAVPHKGLGYGVLRYLADAavreAMAALPQAPITFNYLG---QFDQ 3147
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1994 ETAPDDFLPVSDRPNMPSSITGAmRSPSVFGINISTAGREerrLEAKVTYATDALDEAAASDIARRWHDELRAVVE--LV 2071
Cdd:PRK05691 3148 SFASDALFRPLDEPAGPAHDPDA-PLPNELSVDGQVYGGE---LVLRWTYSAERYDEQTIAELAEAYLAELQALIAhcLA 3223
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2072 DGGAeiGLSRADVPGVEVTQDDLDliAQQYPGA---DVWPMTPLQQGLFFQADLantvadHDAIDVYVTQTVLSLTGDVD 2148
Cdd:PRK05691 3224 DGAG--GLTPSDFPLAQLTQAQLD--ALPVPAAeieDVYPLTPMQEGLLLHTLL------EPGTGLYYMQDRYRINSALD 3293
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2149 PGRLRSALSELLARQRVLRSGFVRLPSGAAVTVVPAEVTVPWSVIDLRAEDAASLDSRVEEVLATERTNPFDMAKPPLIR 2228
Cdd:PRK05691 3294 PERFAQAWQAVVARHEALRASFSWNAGETMLQVIHKPGRTPIDYLDWRGLPEDGQEQRLQALHKQEREAGFDLLNQPPFH 3373
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2229 VVLVEHGDGAE-LVVTNHHLLIDGWSSPLVLADLLSLY-ATGQTFTGSLPgTSGRdFADHARAVATADVEAGIAAWREVL 2306
Cdd:PRK05691 3374 LRLIRVDEARYwFMMSNHHILIDAWCRSLLMNDFFEIYtALGEGREAQLP-VPPR-YRDYIGWLQRQDLAQARQWWQDNL 3451
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2307 APVTEPTLVapghePSADAPPRDHQFS------------IDVKVTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRTV 2374
Cdd:PRK05691 3452 RGFERPTPI-----PSDRPFLREHAGDsggmvvgdcytrLDAADGARLRELAQAHQLTVNTFAQAAWALVLRRYSGDRDV 3526
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2375 TFAETVSGRSPDIEGMESMVGMFINTIPAVV---DVNPDATVVDVLTAVQNDKVKVLDHQQIGLPRLVAQTGLPA---LF 2448
Cdd:PRK05691 3527 LFGVTVAGRPVSMPQMQRTVGLFINSIALRVqlpAAGQRCSVRQWLQGLLDSNMELREYEYLPLVAIQECSELPKgqpLF 3606
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2449 DTLAVYESFPVNV---DSVAGIDASSAGGlklvgaKTSdaTHYPLNlSASRRGAELALKLKYLPTAFAPEQVAVFADVLT 2525
Cdd:PRK05691 3607 DSLFVFENAPVEVsvlDRAQSLNASSDSG------RTH--TNFPLT-AVCYPGDDLGLHLSYDQRYFDAPTVERLLGEFK 3677
|
2650 2660 2670 2680 2690 2700 2710 2720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2526 GLLGAIADHPEATCAEIPLLPAEAAVELTPVTGGPATD-PV--TLAELFRAAARRAPDHVaVVDGAGARLTYRELDEASD 2602
Cdd:PRK05691 3678 RLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDyPLeqSYVRLFEAQVAAHPQRI-AASCLDQQWSYAELNRAAN 3756
|
2730 2740 2750 2760 2770 2780 2790 2800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2603 RLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSG-------------AVLGLS 2669
Cdd:PRK05691 3757 RLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRtpvlvcsaacreqARALLD 3836
|
2810 2820 2830 2840 2850 2860 2870 2880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2670 VLASGDLPgQEFEWMRLDDDSVAAEIAAVPAGPitdaerlgevtaANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESD 2749
Cdd:PRK05691 3837 ELGCANRP-RLLVWEEVQAGEVASHNPGIYSGP------------DNLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVP 3903
|
2890 2900 2910 2920 2930 2940 2950 2960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2750 RLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSE-AVGGEVLERFIAEHGATHTFLTPSVLSTM---DPTAVP 2825
Cdd:PRK05691 3904 YLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAiAHDPQGLLAHVQAQGITVLESVPSLIQGMlaeDRQALD 3983
|
2970 2980 2990 3000 3010 3020 3030 3040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2826 SLRVIAAGGEAVPQPIVDRWA---PATELHNLYGPTETTIGIT---ISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPV 2899
Cdd:PRK05691 3984 GLRWMLPTGEAMPPELARQWLqryPQIGLVNAYGPAECSDDVAffrVDLASTRGSYLPIGSPTDNNRLYLLDEALELVPL 4063
|
3050 3060 3070 3080 3090 3100 3110 3120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2900 GMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRMYRTGDVVRWTPDtdtgGLtLEYTGRSDDQVKLRGLRIELG 2979
Cdd:PRK05691 4064 GAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDLARRRSD----GV-LEYVGRIDHQVKIRGYRIELG 4138
|
3130 3140 3150 3160 3170 3180 3190 3200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2980 EIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPVDGAVEVSEL----KAFAGGRLPAYMVPSSFTVIDELPLTPVGKLD 3055
Cdd:PRK05691 4139 EIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVPHQTVLAQGALleriKQRLRAELPDYMVPLHWLWLDRLPLNANGKLD 4218
|
3210 3220 3230 3240 3250 3260 3270 3280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3056 KRALPEP---VLEAGEYVAPATGTERTIADVAAGVLNIDAglVSATSSFFELGGDSLSAARLAARLSDQLGVAVSVRDVF 3132
Cdd:PRK05691 4219 RKALPALdigQLQSQAYLAPRNELEQTLATIWADVLKVER--VGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAMF 4296
|
3290
....*....|....
gi 1827387616 3133 ESGSIRALAETVGG 3146
Cdd:PRK05691 4297 ECSTVEELAEYIEG 4310
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
569-3148 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1613.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 569 ERLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDV---LPVAVA 645
Cdd:PRK12316 48 ERDRLSYAQQRMWFLWQLEPQSGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVpldRPLEVE 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 646 REQLDW-----READSVESLVRSTTEGFDVSTQMPLRGRFHRDGAGLHV-ALTMHHIAMDGQSIPVLARDLMSAYAARAE 719
Cdd:PRK12316 128 FEDCSGlpeaeQEARLRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVlLLTLHHIVSDGWSMNVLIEEFSRFYSAYAT 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 720 GRTGGLPVLDVQYADYALWQQSVLGDADDEtsvlgEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVEFDDDLA 799
Cdd:PRK12316 208 GAEPGLPALPIQYADYALWQRSWLEAGEQE-----RQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALA 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 800 DRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGDLLGNVR 879
Cdd:PRK12316 283 EALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 880 TTVLDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTYtEPTVNDVAGL-EASGIQAAPVDTGVVNAKFDLTVAVRARS 958
Cdd:PRK12316 363 DTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQVMYNH-QPLVADIEALdTVAGLEFGQLEWKSRTTQFDLTLDTYEKG 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 959 GGtpMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDDQNTAVGDIDIVGAARAKSVSAPVSArtpgamVGRGGEVEAGT 1038
Cdd:PRK12316 442 GR--LHAALTYATDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNA------TAAEYPLQRGV 513
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1039 LIDVLAQRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDP 1118
Cdd:PRK12316 514 HRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDP 593
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1119 AYPADRIAYMLEDSGATVGITDASTRARLGESSCEWV---DLADLEAEAESgdditdtERNGSVRLT--NLAYLIYTSGS 1193
Cdd:PRK12316 594 EYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVldlDRPAAWLEGYS-------EENPGTELNpeNLAYVIYTSGS 666
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1194 TGRPKAVGVSHTGIvdfVNSLAKITTGTPEDEPDTrILHVASPSFDASMFEMAWAIPAGHTLVIAPQAD-FAGDALATVL 1272
Cdd:PRK12316 667 TGKPKGAGNRHRAL---SNRLCWMQQAYGLGVGDT-VLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDhRDPAKLVELI 742
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1273 ERDEVTDMIITPSVLATV----DPERAQYVRNLATGGEACPPELVERWSER--GRRIFNCYGPTEATVWATRS--RMTAG 1344
Cdd:PRK12316 743 NREGVDTLHFVPSMLQAFlqdeDVASCTSLRRIVCSGEALPADAQEQVFAKlpQAGLYNLYGPTEAAIDVTHWtcVEEGG 822
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1345 KPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEpGARMYATGDLVRVAKGGN 1424
Cdd:PRK12316 823 DSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVA-GERMYRTGDLARYRADGV 901
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1425 LEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVEstrgGRkhtEVVAYLVAKpgatiDSAAVLDEA-AQHLA 1503
Cdd:PRK12316 902 IEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVD----GK---QLVGYVVLE-----SEGGDWREAlKAHLA 969
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1504 AH----MVPSQAIVIDEIPLTPAGKLDRAALPEPHAPEP-AEYVAPANPAEDNLARIVAGLLGEERVSVTESFFALGGDS 1578
Cdd:PRK12316 970 ASlpeyMVPAQWLALERLPLTPNGKLDRKALPAPEASVAqQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDS 1049
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1579 IMSIQLSSAAKAAGIHLSPREIFELKTIRAMAAAAAAsgGPVALIEELPggGTGEMPLPPVTSWMIEhsEEPADFADFSQ 1658
Cdd:PRK12316 1050 IVSIQVVSRARQAGIQLSPRDLFQHQTIRSLALVAKA--GQATAADQGP--ASGEVALAPVQRWFFE--QAIPQRQHWNQ 1123
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1659 SLVFNVPASAAVADLQTVVEAVAAAHPMLTAVLTRSGDGWTM---NAGAGIVPAVREIDAEGALDPALVDAHRELlgamD 1735
Cdd:PRK12316 1124 SLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQayaAPQAGEVLWQRQAASEEELLALCEEAQRSL----D 1199
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1736 PGTGSLLGTAVVN-GEGRRRLVIAIHHLGVDAVSWPILVEDLVTAWAQLTSGRPielrPEATTTRRIAHLLAGQVHARAR 1814
Cdd:PRK12316 1200 LEQGPLLRALLVDmADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYADLDADLP----ARTSSYQAWARRLHEHAGARAE 1275
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1815 EVDYWLEQLPERPTSFgtSADRP---LHRRRDESSLTYVVDDVAGSILTTVPQAFGSSVDDVLLGALARAVRAWQLDngi 1891
Cdd:PRK12316 1276 ELDYWQAQLEDAPHEL--PCENPdgaLENRHERKLELRLDAERTRQLLQEAPAAYRTQVNDLLLTALARVTCRWSGQ--- 1350
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1892 adgGPVTVSTEGHGRDEsiAGDegAIDLSRTVGWFTSITPLAVDASSDVVHAVKSAKDARLSRPAGGVGFGILRYNSDGE 1971
Cdd:PRK12316 1351 ---ASVLVQLEGHGRED--LFE--DIDLSRTVGWFTSLFPVRLTPAADLGESIKAIKEQLRAVPDKGIGYGLLRYLAGEE 1423
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1972 IAHR----PLPTIMYNYFGGGTAPSTETAPddFLPVSDRpnmpssiTGAMRSPSV-----FGINISTAGREerrLEAKVT 2042
Cdd:PRK12316 1424 AAARlaalPQPRITFNYLGQFDRQFDEAAL--FVPATES-------AGAAQDPCAplanwLSIEGQVYGGE---LSLHWS 1491
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2043 YATDALDEAAASDIARRWHDELRAVVELVDGGAEIGLSRADVPGVEVTQDDLDLIAQQYPG-ADVWPMTPLQQGLFFqad 2121
Cdd:PRK12316 1492 FSREMFAEATVQRLADDYARELQALIEHCCDERNRGVTPSDFPLAGLSQAQLDALPLPAGEiADIYPLSPMQQGMLF--- 1568
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2122 laNTVADHDAIDvYVTQTVLSLTGdVDPGRLRSALSELLARQRVLRSGFVRLPSGA-AVTVVPAEVTVPWSVIDLRAEDa 2200
Cdd:PRK12316 1569 --HSLYEQEAGD-YINQLRVDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGLEqPLQVIHKQVELPFAELDWRGRE- 1643
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2201 aSLDSRVEEVLATERTNPFDMAKPPLIRVVLVEHGDGA-ELVVTNHHLLIDGWSSPLVLADLLSLYAtgqtftGSLPGTS 2279
Cdd:PRK12316 1644 -DLGQALDALAQAERQKGFDLTRAPLLRLVLVRTGEGRhHLIYTNHHILMDGWSNAQLLGEVLQRYA------GQPVAAP 1716
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2280 GRDFADHARAVATADVEAGIAAWREVLAPVTEPTLVApgHEPSADAPPR---DHQFSIDVKVTERLEALARNNSTTMATV 2356
Cdd:PRK12316 1717 GGRYRDYIAWLQRQDAAASEAFWKEQLAALEEPTRLA--QAARTEDGQVgygDHQQLLDPAQTRALAEFARAQKVTLNTL 1794
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2357 VQFAWAMFLSRLTGTRTVTFAETVSGRSPDIEGMESMVGMFINTIPAVVDVNPDATVVDVLTAVQNDKVKVLDHQQIGL- 2435
Cdd:PRK12316 1795 VQAAWLLLLQRYTGQETVAFGATVAGRPAELPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLy 1874
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2436 --PRLVAQTGlPALFDTLAVYESFPVnvdsVAGIDASSAGGLKLVGAKTSDATHYPLNLsASRRGAELALKLKYLPTAFA 2513
Cdd:PRK12316 1875 diQRWAGQGG-EALFDSLLVFENYPV----AEALKQGAPAGLVFGRVSNHEQTNYPLTL-AVTLGETLSLQYSYDRGHFD 1948
|
2010 2020 2030 2040 2050 2060 2070 2080
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2514 PEQVAVFADVLTGLLGAIADHPEATCAEIPLLPAEAAVELTPV---TGGPATDPVTLAELFRAAARRAPDHVAVVDGaGA 2590
Cdd:PRK12316 1949 AAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADwdrTPEAYPRGPGVHQRIAEQAARAPEAIAVVFG-DQ 2027
|
2090 2100 2110 2120 2130 2140 2150 2160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2591 RLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLGLS- 2669
Cdd:PRK12316 2028 HLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSGAALLLTq 2107
|
2170 2180 2190 2200 2210 2220 2230 2240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2670 --VLASGDLPgQEFEWMRLDDDsvaaeiAAVPAGPITDAERlgEVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQE 2747
Cdd:PRK12316 2108 rhLLERLPLP-AGVARLPLDRD------AEWADYPDTAPAV--QLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAA 2178
|
2250 2260 2270 2280 2290 2300 2310 2320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2748 SDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGGEVLERFIAEHGATHTFLTPSVLSTMDPTA---- 2823
Cdd:PRK12316 2179 GERYELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAerdg 2258
|
2330 2340 2350 2360 2370 2380 2390 2400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2824 -VPSLRVIAAGGEAVPQPIVDRWA---PATELHNLYGPTETTIGITISSAmRPGDP-----VRLGGPIGGVDLMVLDERL 2894
Cdd:PRK12316 2259 rPPAVRVYCFGGEAVPAASLRLAWealRPVYLFNGYGPTEAVVTPLLWKC-RPQDPcgaayVPIGRALGNRRAYILDADL 2337
|
2410 2420 2430 2440 2450 2460 2470 2480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2895 RPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRMYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGL 2974
Cdd:PRK12316 2338 NLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSASGERLYRTGDLARYRADG-----VVEYLGRIDHQVKIRGF 2412
|
2490 2500 2510 2520 2530 2540 2550 2560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2975 RIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPVDGAVEV-SELKAFAGGRLPAYMVPSSFTVIDELPLTPVGK 3053
Cdd:PRK12316 2413 RIELGEIEARLQAHPAVREAVVVAQDGASGKQLVAYVVPDDAAEDLlAELRAWLAARLPAYMVPAHWVVLERLPLNPNGK 2492
|
2570 2580 2590 2600 2610 2620 2630 2640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3054 LDKRALPEPVLEAGE--YVAPATGTERTIADVAAGVLNIDAglVSATSSFFELGGDSLSAARLAARLSDQLGVAVSVRDV 3131
Cdd:PRK12316 2493 LDRKALPKPDVSQLRqaYVAPQEGLEQRLAAIWQAVLKVEQ--VGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRIL 2570
|
2650
....*....|....*..
gi 1827387616 3132 FESGSIRALAETVGGSE 3148
Cdd:PRK12316 2571 FERPTLAAFAASLESGQ 2587
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
563-1887 |
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: 835.28 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 563 RIEPRPERLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDVLPV 642
Cdd:COG1020 10 PPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 643 AVAREQL--------DWREADSVESLVRSTTEGFDVSTQMPLRGRFHRDGAGLHVAL-TMHHIAMDGQSIPVLARDLMSA 713
Cdd:COG1020 90 VAAPLPVvvllvdleALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLLLLLLlALHHIISDGLSDGLLLAELLRL 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 714 YAARAEGRTGGLPVLDVQYADYALWQQsvlgdADDETSVLGEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVE 793
Cdd:COG1020 170 YLAAYAGAPLPLPPLPIQYADYALWQR-----EWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFR 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 794 FDDDLADRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGD 873
Cdd:COG1020 245 LPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELEGLVGFFVNTLPLRVDLSGDPSFAE 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 874 LLGNVRTTVLDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTYTEptvNDVAGLEASGIQAAPVDTGVVNAKFDLTVA 953
Cdd:COG1020 325 LLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQN---APADELELPGLTLEPLELDSGTAKFDLTLT 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 954 VRARSGGtpMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDDQNTAVGDIDIVGAA-RAKSVSAPVSARTPGAmvgrgg 1032
Cdd:COG1020 402 VVETGDG--LRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAeRQQLLAEWNATAAPYP------ 473
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1033 evEAGTLID-VLAQRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGA 1111
Cdd:COG1020 474 --ADATLHElFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGA 551
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1112 AYVPVDPAYPADRIAYMLEDSGATVGITDASTRARLGESSCEWVDLADLEAEAESGDDitdteRNGSVRLTNLAYLIYTS 1191
Cdd:COG1020 552 AYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEPATN-----PPVPVTPDDLAYVIYTS 626
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1192 GSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFA-GDALAT 1270
Cdd:COG1020 627 GSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGD----RVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRdPAALAE 702
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1271 VLERDEVTDMIITPSVLATV---DPERAQYVRNLATGGEACPPELVERWSER--GRRIFNCYGPTEATVWATRSRMTA-- 1343
Cdd:COG1020 703 LLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEALPPELVRRWRARlpGARLVNLYGPTETTVDSTYYEVTPpd 782
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1344 --GKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEPGARMYATGDLVRVAK 1421
Cdd:COG1020 783 adGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLP 862
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1422 GGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPGATIDSAAVLDEAAQH 1501
Cdd:COG1020 863 DGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDK---RLVAYVVPEAGAAAAAALLRLALALL 939
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1502 LAAHMVPSQAIVIDEIPLTPAGKLDRAALPEPHAPEPAEYVAPANPAEDNLARIVAGLLGEERVSVTESFFALGGDSIMS 1581
Cdd:COG1020 940 LPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLL 1019
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1582 IQLSSAAKAAGIHLSPREIFELKTIRAMAAAAAASGGPVALIEELPGGGtgemPLPPVTSWMIEHSEEPADFADFSQSLV 1661
Cdd:COG1020 1020 LLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAAPLAAAAA----PLPLPPLLLSLLALLLALLLLLALLAL 1095
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1662 FNVPASAAVADLQTVVEAVAAAHPMLTAVLTRSGDGWTMNAGAGIVPAVREIDAEGALDPALVDAHRELLGAM------- 1734
Cdd:COG1020 1096 LALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLRLLVALAAALALAALLALLLAAAAAAAELLaaaalll 1175
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1735 -DPGTGSLLGTAVVNGEGRRRLVIAIHHLGVDAVSWPILVEDLVTAWAQLTSGRPIELRPEATTTRRIAHLLAGQVHARA 1813
Cdd:COG1020 1176 lLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAAL 1255
|
1290 1300 1310 1320 1330 1340 1350
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 1814 REVDYWLEQLPERPTSFGTSADRPLHRRRDESSLTYVVDDVAGSILTTVPQAFGSSVDDVLLGALARAVRAWQL 1887
Cdd:COG1020 1256 AAALLALALALLALALLLLALALLLPALARARAARTARALALLLLLALLLLLALALALLLLLLLLLALLLLALL 1329
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
568-1845 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 803.22 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 568 PERLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDV---LPVAV 644
Cdd:PRK12467 47 FERIPLSYAQERQWFLWQLDPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIdasLSLTI 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 645 AREQLDWREADSVESLVRSTTEG-----FDVSTQMPLRGRFHRDGAGLHV-ALTMHHIAMDGQSIPVLARDLMSAYAARA 718
Cdd:PRK12467 127 PLDDLANEQGRARESQIEAYINEevarpFDLANGPLLRVRLLRLADDEHVlVVTLHHIISDGWSMRVLVEELVQLYSAYS 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 719 EGRTGGLPVLDVQYADYALWQQSVLGDADDEtsvlgEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVEFDDDL 798
Cdd:PRK12467 207 QGREPSLPALPIQYADYAIWQRSWLEAGERE-----RQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQAL 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 799 ADRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGDLLGNV 878
Cdd:PRK12467 282 SAGLKALAQREGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQV 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 879 RTTVLDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTY--TEPTVNDVAGLEASGIQAAPVDTGVVNAKFDLTVAVRA 956
Cdd:PRK12467 362 KRTALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHqnTATGGRDREGAQLPGLTVEELSWARHTAQFDLALDTYE 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 957 RSGGtpMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDDQNTAVGDIDIVGAArakSVSAPVSARTPGAMVGRGGEVEA 1036
Cdd:PRK12467 442 SAQG--LWAAFTYATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAE---ERARELVRWNAPATEYAPDCVHQ 516
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1037 gtLIDvlAQRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPV 1116
Cdd:PRK12467 517 --LIE--AQARQHPERPALVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1117 DPAYPADRIAYMLEDSGATVGITDASTRARLG-ESSCEWVDLADLEAEAESgdditDTERNGSVRLT--NLAYLIYTSGS 1193
Cdd:PRK12467 593 DPEYPQDRLAYMLDDSGVRLLLTQSHLLAQLPvPAGLRSLCLDEPADLLCG-----YSGHNPEVALDpdNLAYVIYTSGS 667
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1194 TGRPKAVGVSHTGIVDFVNSLAKittgTPEDEPDTRILHVASPSFDASMFEMAWAIPAGHTLVIAP-QADFAGDALATVL 1272
Cdd:PRK12467 668 TGQPKGVAISHGALANYVCVIAE----RLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPpDCARDAEAFAALM 743
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1273 ERDEVTDMIITPSVL------ATVDPERAQyvRNLATGGEACPPELVERWSERGR--RIFNCYGPTEATVWATRSRMT-- 1342
Cdd:PRK12467 744 ADQGVTVLKIVPSHLqallqaSRVALPRPQ--RALVCGGEALQVDLLARVRALGPgaRLINHYGPTETTVGVSTYELSde 821
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1343 --AGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEPGARMYATGDLVRVA 1420
Cdd:PRK12467 822 erDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYR 901
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1421 KGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVestrGGRKHTEVVAYLVakPGATIDSA---AVLDE 1497
Cdd:PRK12467 902 ADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGVREAVVLAQ----PGDAGLQLVAYLV--PAAVADGAehqATRDE 975
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1498 AAQHLAA----HMVPSQAIVIDEIPLTPAGKLDRAALPEPHA-PEPAEYVAPANPAEDNLARIVAGLLGEERVSVTESFF 1572
Cdd:PRK12467 976 LKAQLRQvlpdYMVPAHLLLLDSLPLTPNGKLDRKALPKPDAsAVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFF 1055
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1573 ALGGDSIMSIQ-LSSAAKAAGIHLSPREIFELKTIRAMAAaaaasggpvALIEELPGGGTgemPLPPVTswmiEHSEEPA 1651
Cdd:PRK12467 1056 ELGGHSLLATQvISRVRQRLGIQVPLRTLFEHQTLAGFAQ---------AVAAQQQGAQP---ALPDVD----RDQPLPL 1119
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1652 DFADFSQSLVFNV-PASAA--------------VADLQTVVEAVAAAHPMLTAVLtRSGDGWTMNA--GAGIVP-AVREI 1713
Cdd:PRK12467 1120 SYAQERQWFLWQLePGSAAyhipqalrlkgpldIEALERSFDALVARHESLRTTF-VQEDGRTRQVihPVGSLTlEEPLL 1198
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1714 DAEGALDPAL-VDAHRELLGAMDPGTGSLLGTAVVN-GEGRRRLVIAIHHLGVDAVSWPILVEDLVTAWAQLTSGR---- 1787
Cdd:PRK12467 1199 LAADKDEAQLkVYVEAEARQPFDLEQGPLLRVGLLRlAADEHVLVLTLHHIVSDGWSMQVLVDELVALYAAYSQGQslql 1278
|
1290 1300 1310 1320 1330 1340
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 1788 ---PIELRPEATTTRRiaHLLAGQvhaRAREVDYWLEQLPERPTSFGTSADRPlhRRRDES 1845
Cdd:PRK12467 1279 palPIQYADYAVWQRQ--WMDAGE---RARQLAYWKAQLGGEQPVLELPTDRP--RPAVQS 1332
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
112-1837 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 710.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 112 EEFAGPTRPANA-AFTLFTSGSTGRPKAVVITHRG-IANRLAadIEQ---YDLTARDVFLYKAPITFDVS-VREIFLPIA 185
Cdd:PRK05691 156 EAWQEPALQPDDiAFLQYTSGSTALPKGVQVSHGNlVANEQL--IRHgfgIDLNPDDVIVSWLPLYHDMGlIGGLLQPIF 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 186 IGATLVIAEPGRH-GDPVHLADLIRRHGVTVI---HFVPAMLAA-FNEVLGAGVgELTSLRLIQTGGEaltpPVARDLMV 260
Cdd:PRK05691 234 SGVPCVLMSPAYFlERPLRWLEAISEYGGTISggpDFAYRLCSErVSESALERL-DLSRWRVAYSGSE----PIRQDSLE 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 261 RLP------GTRLQN---QYGPAEASIVVTIHRVTQD-------------DRVIP--------IGTPTRRVSARVLDAA- 309
Cdd:PRK05691 309 RFAekfaacGFDPDSffaSYGLAEATLFVSGGRRGQGipaleldaealarNRAEPgtgsvlmsCGRSQPGHAVLIVDPQs 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 310 LREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVAdpfgEPGARLYRTGDRArWNRDGEIEYLGRTDFQVKLRGQRLEL 389
Cdd:PRK05691 389 LEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE----HDGRTWLRTGDLG-FLRDGELFVTGRLKDMLIVRGHNLYP 463
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 390 GEVEAALAAAPGVLH----AAAAVVDGpgGQQLVGYLA----------PADVDVDTVAATTAELLPEymRPSAWVRLD-- 453
Cdd:PRK05691 464 QDIEKTVEREVEVVRkgrvAAFAVNHQ--GEEGIGIAAeisrsvqkilPPQALIKSIRQAVAEACQE--APSVVLLLNpg 539
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 454 AMPLSRSGKVDRR---------------LLPEPEIAPTLYVP-PGNADEETVAGLFAELLGVERVGVTDSFFDIGGSSLS 517
Cdd:PRK05691 540 ALPKTSSGKLQRSacrlrladgsldsyaLFPALQAVEAAQTAaSGDELQARIAAIWCEQLKVEQVAADDHFFLLGGNSIA 619
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 518 AARIAARVSKELGVDVSVRDVFESPSVRGLVHAVS----GRGSALPSVKRIePRPERLPLSRAQRRMWFLNQFDTASGAY 593
Cdd:PRK05691 620 ATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVArqlaGGGAAQAAIARL-PRGQALPQSLAQNRLWLLWQLDPQSAAY 698
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 594 NIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDVLP---VAVAREQLDWREADSVESLVRSTTEG--- 667
Cdd:PRK05691 699 NIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAqgeFALQRIDLSDLPEAEREARAAQIREEear 778
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 668 --FDVSTQMPLRGRFHRDGAGLHVAL-TMHHIAMDGQSIPVLARDLMSAYAARAEGRTGGLPVLDVQYADYALWQQSVLG 744
Cdd:PRK05691 779 qpFDLEKGPLLRVTLVRLDDEEHQLLvTLHHIVADGWSLNILLDEFSRLYAAACQGQTAELAPLPLGYADYGAWQRQWLA 858
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 745 DADDEtsvlgEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVEFDDDLADRVDVLARSNTMTGFMVTEAAFAAT 824
Cdd:PRK05691 859 QGEAA-----RQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQAL 933
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 825 VARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGDLLGNVRTTVLDAFANDQVQFDELIEALAPER 904
Cdd:PRK05691 934 LHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQAR 1013
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 905 sssHQPLAQIAFTYTEptvNDVAGLEA-SGIQAAPVDTGVVNAKFDLTV-AVRARSGGTPMAADfiYATDLFDESTVKRF 982
Cdd:PRK05691 1014 ---EQGLFQVMFNHQQ---RDLSALRRlPGLLAEELPWHSREAKFDLQLhSEEDRNGRLTLSFD--YAAELFDAATIERL 1085
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 983 AEVYRRVLQAIVDDQNTAVGDIDIVGAARAKSVSAPVSARTPGAMVgrggeveagTLIDVL-AQRDLDPDHPALICDGTE 1061
Cdd:PRK05691 1086 AEHFLALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPCAPAQA---------WLPELLnEQARQTPERIALVWDGGS 1156
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1062 MDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDA 1141
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQS 1236
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1142 STRARLGESS-CEWVDLADLEAeaesgDDITDTERNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVDfvnSLAKITTG 1220
Cdd:PRK05691 1237 HLLERLPQAEgVSAIALDSLHL-----DSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAE---RLQWMQAT 1308
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1221 TPEDEPDTrILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFAGDA-LATVLERDEVTDMIITPSVLAT-VDPERAQ-- 1296
Cdd:PRK05691 1309 YALDDSDV-LMQKAPISFDVSVWECFWPLITGCRLVLAGPGEHRDPQrIAELVQQYGVTTLHFVPPLLQLfIDEPLAAac 1387
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1297 -YVRNLATGGEACPPELVERWSER--GRRIFNCYGPTEATVWAT--RSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQG 1371
Cdd:PRK05691 1388 tSLRRLFSGGEALPAELRNRVLQRlpQVQLHNRYGPTETAINVThwQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPG 1467
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1372 VVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEPGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVL 1451
Cdd:PRK05691 1468 VAGELCIGGAGLARGYLGRPALTAERFVPDPLGEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARL 1547
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1452 DAQPGVAQSVVVGVESTRGGRkhteVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALP 1531
Cdd:PRK05691 1548 LAQPGVAQAAVLVREGAAGAQ----LVGYYTGEAGQEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALP 1623
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1532 EPHApEPAEYVAPANPAEDNLARIVAGLLGEERVSVTESFFALGGDSIMSIQL-SSAAKAAGIHLSPREIF---ELKTIR 1607
Cdd:PRK05691 1624 EPVW-QQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIvSRTRQACDVELPLRALFeasELGAFA 1702
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1608 AMAAAAAASG-----GPVALIEElpgggtgEMPLPPVTS----WMIEHSEepadfadfSQSLVFNVpasAAVADLQTVVE 1678
Cdd:PRK05691 1703 EQVARIQAAGernsqGAIARVDR-------SQPVPLSYSqqrmWFLWQME--------PDSPAYNV---GGMARLSGVLD 1764
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1679 aVAAAHPMLTAVLTRSGDGWTMNAGAGIVPaVREIDAEG----------ALDPALVDAHRELLG------AMDPGTGSLL 1742
Cdd:PRK05691 1765 -VDRFEAALQALILRHETLRTTFPSVDGVP-VQQVAEDSglrmdwqdfsALPADARQQRLQQLAdseahqPFDLERGPLL 1842
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1743 GTAVVN-GEGRRRLVIAIHHLGVDAVSWPILVEDLVTAWAQLTSGRPIELRPEATT-------TRRiaHLLAGQvhaRAR 1814
Cdd:PRK05691 1843 RACLVKaAEREHYFVLTLHHIVTEGWAMDIFARELGALYEAFLDDRESPLEPLPVQyldysvwQRQ--WLESGE---RQR 1917
|
1850 1860
....*....|....*....|...
gi 1827387616 1815 EVDYWLEQLPERPTSFGTSADRP 1837
Cdd:PRK05691 1918 QLDYWKAQLGNEHPLLELPADRP 1940
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
2097-3148 |
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: 710.09 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2097 IAQQYPGADVWPMTPLQQGLFFQADLANTVADHDAIDVYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPSG 2176
Cdd:COG1020 1 AAAAAAAALPPAAAAAPLPLSAAQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2177 AAVTVVPAEVTVPWSVIDLRAEDAASLDSRVEEVLATERTNPFDMAKPPLIRVVLVEHGDG-AELVVTNHHLLIDGWSSP 2255
Cdd:COG1020 81 RPVQVIQPVVAAPLPVVVLLVDLEALAEAAAEAAAAAEALAPFDLLRGPLLRLLLLLLLLLlLLLLLALHHIISDGLSDG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2256 LVLADLLSLYATGQTFTGS----LPGTSGRDFADHARAVATADVEAGIAAWREVLAPVTEPTLVAPGHEPSADAPPR--D 2329
Cdd:COG1020 161 LLLAELLRLYLAAYAGAPLplppLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRgaR 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2330 HQFSIDVKVTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRSPdiEGMESMVGMFINTIPAVVDVNP 2409
Cdd:COG1020 241 VSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPR--PELEGLVGFFVNTLPLRVDLSG 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2410 DATVVDVLTAVQNDKVKVLDHQQIGLPRLVAQTGLP------ALFDTLAVYESFPVNVDSVAGIDASSAGGlklvgakTS 2483
Cdd:COG1020 319 DPSFAELLARVRETLLAAYAHQDLPFERLVEELQPErdlsrnPLFQVMFVLQNAPADELELPGLTLEPLEL-------DS 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2484 DATHYPLNLSASRRGAELALKLKYLPTAFAPEQVAVFADVLTGLLGAIADHPEATCAEIPLLPAEAAVELTPVTGGPATD 2563
Cdd:COG1020 392 GTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAP 471
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2564 ---PVTLAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTG 2640
Cdd:COG1020 472 ypaDATLHELFEAQAARTPDAVAVVFG-DQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAG 550
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2641 GAYVPIDPDYPAERVASMIEDSGAVLGLSVLASGD-LPGQEFEWMRLDDDSVAAEIAAVPAGPitdaerlgeVTAANLAY 2719
Cdd:COG1020 551 AAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAArLPELGVPVLALDALALAAEPATNPPVP---------VTPDDLAY 621
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2720 VIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAV-GGEVLE 2798
Cdd:COG1020 622 VIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARrDPAALA 701
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2799 RFIAEHGATHTFLTPSVLSTM---DPTAVPSLRVIAAGGEAVPQPIVDRWA---PATELHNLYGPTETTIGIT---ISSA 2869
Cdd:COG1020 702 ELLARHRVTVLNLTPSLLRALldaAPEALPSLRLVLVGGEALPPELVRRWRarlPGARLVNLYGPTETTVDSTyyeVTPP 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2870 MRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRMYRTGDVVRWT 2949
Cdd:COG1020 782 DADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWL 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2950 PDTdtgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG-GSVATALAAYIVPVDGA-VEVSELKAFA 3027
Cdd:COG1020 862 PDG-----NLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREdAPGDKRLVAYVVPEAGAaAAAALLRLAL 936
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3028 GGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVLEAGEYVAPATGTERTIADVAAGVLNIDAGLVSATSSFFELGGD 3107
Cdd:COG1020 937 ALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLG 1016
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|.
gi 1827387616 3108 SLSAARLAARLSDQLGVAVSVRDVFESGSIRALAETVGGSE 3148
Cdd:COG1020 1017 LLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAA 1057
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1-820 |
5.51e-178 |
|
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: 587.98 E-value: 5.51e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:COG1020 502 LTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQS 581
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRfddivDVHVLDISSPGDADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:COG1020 582 ALAARLPEL-----GVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRYGLG 656
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFnevLGAGVGELTSL 240
Cdd:COG1020 657 PGDRVLQFASLSFDASVWEIFGALLSGATLVLAPPEARRDPAALAELLARHRVTVLNLTPSLLRAL---LDAAPEALPSL 733
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 241 RLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDD---RVIPIGTPTRRVSARVLDAALREVPIGV 317
Cdd:COG1020 734 RLVLVGGEALPPELVRRWRARLPGARLVNLYGPTETTVDSTYYEVTPPDadgGSVPIGRPIANTRVYVLDAHLQPVPVGV 813
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 318 PGELYLGGVQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALA 397
Cdd:COG1020 814 PGELYIGGAGLARGYLNRPELTAERFVADPFGFPGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALL 893
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 398 AAPGVLHAAAAVV-DGPGGQQLVGYLAPADVDVDTVAATT---AELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEPEI 473
Cdd:COG1020 894 QHPGVREAVVVAReDAPGDKRLVAYVVPEAGAAAAAALLRlalALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAA 973
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 474 APTL-YVPPGNADEETVAGLFAELLGVERVGVTDSFFDIGGSSLSAARIAARVSKELGVDVSVRDVFESPSVRGLVHAVS 552
Cdd:COG1020 974 AAAAaAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAA 1053
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 553 GRGSALPSVKRIEPRPERLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVG 632
Cdd:COG1020 1054 AAAAAAAAPLAAAAAPLPLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQ 1133
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 633 AAPVQDVLPVAVA-------REQLDWREADSVESLVRSTTEGFDVSTQMPLRGRFHRDGAGLHVALTMHHIAMDGQSIPV 705
Cdd:COG1020 1134 EGPRLRLLVALAAalalaalLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1213
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 706 LARDLMSAYAARAEGRTGGLPVLDVQYADYALWQQSVLGDADDETSVLGEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGT 785
Cdd:COG1020 1214 LLLLLLLLLLLAAAAAALLALALLLALLALAALLALAALAALAAALLALALALLALALLLLALALLLPALARARAARTAR 1293
|
810 820 830
....*....|....*....|....*....|....*
gi 1827387616 786 AGATVTVEFDDDLADRVDVLARSNTMTGFMVTEAA 820
Cdd:COG1020 1294 ALALLLLLALLLLLALALALLLLLLLLLALLLLAL 1328
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
570-996 |
4.25e-166 |
|
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: 520.06 E-value: 4.25e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 570 RLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDVLPVAVAREQL 649
Cdd:cd19540 1 RIPLSFAQQRLWFLNRLDGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAAEARPDL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 650 DWR---EADSVESLVRSTTEGFDVSTQMPLRGRFHRDGAGLHV-ALTMHHIAMDGQSIPVLARDLMSAYAARAEGRTGGL 725
Cdd:cd19540 81 TVVdvtEDELAARLAEAARRGFDLTAELPLRARLFRLGPDEHVlVLVVHHIAADGWSMAPLARDLATAYAARRAGRAPDW 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 726 PVLDVQYADYALWQQSVLGDADDETSVLGEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVEFDDDLADRVDVL 805
Cdd:cd19540 161 APLPVQYADYALWQRELLGDEDDPDSLAARQLAYWRETLAGLPEELELPTDRPRPAVASYRGGTVEFTIDAELHARLAAL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 806 ARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGDLLGNVRTTVLDA 885
Cdd:cd19540 241 AREHGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 886 FANDQVQFDELIEALAPERSSSHQPLAQIAFTYTEptvNDVAGLEASGIQAAPVDTGVVNAKFDLTVAVRARSG--GTP- 962
Cdd:cd19540 321 FAHQDVPFERLVEALNPPRSTARHPLFQVMLAFQN---TAAATLELPGLTVEPVPVDTGVAKFDLSFTLTERRDadGAPa 397
|
410 420 430
....*....|....*....|....*....|....*
gi 1827387616 963 -MAADFIYATDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd19540 398 gLTGELEYATDLFDRSTAERLADRFVRVLEAVVAD 432
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
2-468 |
6.80e-166 |
|
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: 521.84 E-value: 6.80e-166
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRlVVVTSD 81
Cdd:cd17646 25 TYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPADRLAYMLADAGPA-VVLTTA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 GEAEARSRFDDIVDVHVLDISSPGDADLDEeefagPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTA 161
Cdd:cd17646 104 DLAARLPAGGDVALLGDEALAAPPATPPLV-----PPRPDNLAYVIYTSGSTGRPKGVMVTHAGIVNRLLWMQDEYPLGP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 162 RDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVlgAGVGELTSLR 241
Cdd:cd17646 179 GDRVLQKTPLSFDVSVWELFWPLVAGARLVVARPGGHRDPAYLAALIREHGVTTCHFVPSMLRVFLAE--PAAGSCASLR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 242 LIQTGGEALTPPVARDLMvRLPGTRLQNQYGPAEASIVVTIHRVT--QDDRVIPIGTPTRRVSARVLDAALREVPIGVPG 319
Cdd:cd17646 257 RVFCSGEALPPELAARFL-ALPGAELHNLYGPTEAAIDVTHWPVRgpAETPSVPIGRPVPNTRLYVLDDALRPVPVGVPG 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 320 ELYLGGVQLARGYAGRPDLTAERFVADPFGePGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAA 399
Cdd:cd17646 336 ELYLGGVQLARGYLGRPALTAERFVPDPFG-PGSRMYRTGDLARWRPDGALEFLGRSDDQVKIRGFRVEPGEIEAALAAH 414
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 400 PGVLHAAAAVVDGP-GGQQLVGYLAPA----DVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd17646 415 PAVTHAVVVARAAPaGAARLVGYVVPAagaaGPDTAALRAHLAERLPEYMVPAAFVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
2579-3059 |
4.80e-164 |
|
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: 514.77 E-value: 4.80e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2579 PDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASM 2658
Cdd:cd05930 1 PDAVAVVDG-DQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2659 IEDSGAVLglsVLasgdlpgqefewmrldddsvaaeiaavpagpitdaerlgeVTAANLAYVIYTSGSTGRPKGVAVTHS 2738
Cdd:cd05930 80 LEDSGAKL---VL----------------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2739 GLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVG-GEVLERFIAEHGATHTFLTPS--- 2814
Cdd:cd05930 117 GLVNLLLWMQEAYPLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKdPEALADLLAEEGITVLHLTPSllr 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2815 -VLSTMDPTAVPSLRVIAAGGEAVPQPIVDRWA---PATELHNLYGPTETTIGIT---ISSAMRPGDPVRLGGPIGGVDL 2887
Cdd:cd05930 197 lLLQELELAALPSLRLVLVGGEALPPDLVRRWRellPGARLVNLYGPTEATVDATyyrVPPDDEEDGRVPIGRPIPNTRV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2888 MVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGtAGQRMYRTGDVVRWTPDtdtGglTLEYTGRSDD 2967
Cdd:cd05930 277 YVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG-PGERMYRTGDLVRWLPD---G--NLEFLGRIDD 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2968 QVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATA-LAAYIVP-VDGAVEVSELKAFAGGRLPAYMVPSSFTVIDE 3045
Cdd:cd05930 351 QVKIRGYRIELGEIEAALLAHPGVREAAVVAREDGDGEKrLVAYVVPdEGGELDEEELRAHLAERLPDYMVPSAFVVLDA 430
|
490
....*....|....
gi 1827387616 3046 LPLTPVGKLDKRAL 3059
Cdd:cd05930 431 LPLTPNGKVDRKAL 444
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
2135-3145 |
9.09e-164 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 572.49 E-value: 9.09e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2135 YVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPSGAaVTVVPAEVTVPWSVIDLRAEDAASLDSRVEEVLATE 2214
Cdd:PRK12467 72 YNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGF-RQVIDASLSLTIPLDDLANEQGRARESQIEAYINEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2215 RTNPFDMAKPPLIRVVLVEHGDGAE-LVVTNHHLLIDGWSSPLVLADLLSLYAT-GQTFTGSLPG--TSGRDFADHARAV 2290
Cdd:PRK12467 151 VARPFDLANGPLLRVRLLRLADDEHvLVVTLHHIISDGWSMRVLVEELVQLYSAySQGREPSLPAlpIQYADYAIWQRSW 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2291 ATA-DVEAGIAAWREVLAPvTEPTLVAPGHEPSADAPP---RDHQFSIDVKVTERLEALARNNSTTMATVVQFAWAMFLS 2366
Cdd:PRK12467 231 LEAgERERQLAYWQEQLGG-EHTVLELPTDRPRPAVPSyrgARLRVDLPQALSAGLKALAQREGVTLFMVLLASFQTLLH 309
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2367 RLTGTRTVTFAETVSGRSPdiEGMESMVGMFINTIPAVVDVNPDATVVDVLTAVQNDKVKVLDHQQIGLPRLVA------ 2440
Cdd:PRK12467 310 RYSGQSDIRIGVPNANRNR--VETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEalqper 387
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2441 QTGLPALFDTLavyesFPVNVDSVAGID--ASSAGGLKLVGAKT-SDATHYPLNLSASRRGAELALKLKYLPTAFAPEQV 2517
Cdd:PRK12467 388 SLSHSPLFQVM-----FNHQNTATGGRDreGAQLPGLTVEELSWaRHTAQFDLALDTYESAQGLWAAFTYATDLFEATTI 462
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2518 AVFADVLTGLLGAIADHPEATCAEIPLLPAEAAVELTPVTGGPATD--PVTLAELFRAAARRAPDHVAVVDGaGARLTYR 2595
Cdd:PRK12467 463 ERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPATEyaPDCVHQLIEAQARQHPERPALVFG-EQVLSYA 541
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2596 ELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLGLS---VLA 2672
Cdd:PRK12467 542 ELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLTqshLLA 621
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2673 SGDLPgqefewmrldddsvaaeiAAVPAGPITDAERLGEVTAA----------NLAYVIYTSGSTGRPKGVAVTHSGLAN 2742
Cdd:PRK12467 622 QLPVP------------------AGLRSLCLDEPADLLCGYSGhnpevaldpdNLAYVIYTSGSTGQPKGVAISHGALAN 683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2743 FARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAV-GGEVLERFIAEHGATHTFLTPSVLSTM-- 2819
Cdd:PRK12467 684 YVCVIAERLQLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLPPDCArDAEAFAALMADQGVTVLKIVPSHLQALlq 763
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2820 DPTAVP--SLRVIAAGGEAVPQPIVDRW---APATELHNLYGPTETTIGIT---ISSAMRPGDPVRLGGPIGGVDLMVLD 2891
Cdd:PRK12467 764 ASRVALprPQRALVCGGEALQVDLLARVralGPGARLINHYGPTETTVGVStyeLSDEERDFGNVPIGQPLANLGLYILD 843
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2892 ERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRMYRTGDVVRWTPDtdtGGltLEYTGRSDDQVKL 2971
Cdd:PRK12467 844 HYLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFGADGGRLYRTGDLARYRAD---GV--IEYLGRMDHQVKI 918
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2972 RGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPVDGA------VEVSELKAFAGGRLPAYMVPSSFTVIDE 3045
Cdd:PRK12467 919 RGFRIELGEIEARLLAQPGVREAVVLAQPGDAGLQLVAYLVPAAVAdgaehqATRDELKAQLRQVLPDYMVPAHLLLLDS 998
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3046 LPLTPVGKLDKRALPEPVLEAGE--YVAPATGTERTIADVAAGVLniDAGLVSATSSFFELGGDSLSAARLAARLSDQLG 3123
Cdd:PRK12467 999 LPLTPNGKLDRKALPKPDASAVQatFVAPQTELEKRLAAIWADVL--KVERVGLTDNFFELGGHSLLATQVISRVRQRLG 1076
|
1050 1060
....*....|....*....|..
gi 1827387616 3124 VAVSVRDVFESGSIRALAETVG 3145
Cdd:PRK12467 1077 IQVPLRTLFEHQTLAGFAQAVA 1098
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
4-468 |
1.10e-162 |
|
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: 510.92 E-value: 1.10e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvtsdge 83
Cdd:cd05930 16 AELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYILEDSGAKLVL------ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 aearsrfddivdvhvldisspgdadldeeefagpTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARD 163
Cdd:cd05930 90 ----------------------------------TDPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWMQEAYPLTPGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 164 VFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAgvGELTSLRLI 243
Cdd:cd05930 136 RVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELEL--AALPSLRLV 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 244 QTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDD---RVIPIGTPTRRVSARVLDAALREVPIGVPGE 320
Cdd:cd05930 214 LVGGEALPPDLVRRWRELLPGARLVNLYGPTEATVDATYYRVPPDDeedGRVPIGRPIPNTRVYVLDENLRPVPPGVPGE 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 321 LYLGGVQLARGYAGRPDLTAERFVADPFGePGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAP 400
Cdd:cd05930 294 LYIGGAGLARGYLNRPELTAERFVPNPFG-PGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIELGEIEAALLAHP 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 401 GVLHAAA-AVVDGPGGQQLVGYLAPADVDVDTVAATTAEL---LPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd05930 373 GVREAAVvAREDGDGEKRLVAYVVPDEGGELDEEELRAHLaerLPDYMVPSAFVVLDALPLTPNGKVDRKAL 444
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1050-1530 |
7.75e-162 |
|
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: 508.22 E-value: 7.75e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDAStrarlgesscewvdladleaeaesgdditdterngsvrltNLAYLIYTSGSTGRPKAVGVSHTGIVD 1209
Cdd:cd05930 81 EDSGAKLVLTDPD----------------------------------------DLAYVIYTSGSTGKPKGVMVEHRGLVN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 FVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQAD-FAGDALATVLERDEVTDMIITPSVLA 1288
Cdd:cd05930 121 LLLWMQEAYPLTPGD----RVLQFTSFSFDVSVWEIFGALLAGATLVVLPEEVrKDPEALADLLAEEGITVLHLTPSLLR 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1289 TV----DPERAQYVRNLATGGEACPPELVERWSER--GRRIFNCYGPTEATVWAT----RSRMTAGKPVTIGKPVDGFTV 1358
Cdd:cd05930 197 LLlqelELAALPSLRLVLVGGEALPPDLVRRWRELlpGARLVNLYGPTEATVDATyyrvPPDDEEDGRVPIGRPIPNTRV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1359 RVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGePGARMYATGDLVRVAKGGNLEFAGRADHQVKIN 1438
Cdd:cd05930 277 YVLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFG-PGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIR 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1439 GQRVELGEIEAVLDAQPGVAQSVVVGVESTRGgrkHTEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIP 1518
Cdd:cd05930 356 GYRIELGEIEAALLAHPGVREAAVVAREDGDG---EKRLVAYVVPDEGGELDEEELRAHLAERLPDYMVPSAFVVLDALP 432
|
490
....*....|..
gi 1827387616 1519 LTPAGKLDRAAL 1530
Cdd:cd05930 433 LTPNGKVDRKAL 444
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
2579-3060 |
1.49e-161 |
|
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: 507.18 E-value: 1.49e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2579 PDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASM 2658
Cdd:cd17652 1 PDAPAVVFG-DETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2659 IEDSGAVLGLSvlasgdlpgqefewmrldddsvaaeiaavpagpitdaerlgevTAANLAYVIYTSGSTGRPKGVAVTHS 2738
Cdd:cd17652 80 LADARPALLLT-------------------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2739 GLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEA-VGGEVLERFIAEHGATHTFLTPSVLS 2817
Cdd:cd17652 117 GLANLAAAQIAAFDVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEElLPGEPLADLLREHRITHVTLPPAALA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2818 TMDPTAVPSLRVIAAGGEAVPQPIVDRWAPATELHNLYGPTETTIGITISSAMRPGDPVRLGGPIGGVDLMVLDERLRPV 2897
Cdd:cd17652 197 ALPPDDLPDLRTLVVAGEACPAELVDRWAPGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPV 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2898 PVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRMYRTGDVVRWTPDTDtggltLEYTGRSDDQVKLRGLRIE 2977
Cdd:cd17652 277 PPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQ-----LEFLGRADDQVKIRGFRIE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2978 LGEIEAVLAEHDAVESAVVL----GVGGSvatALAAYIVPVDG-AVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVG 3052
Cdd:cd17652 352 LGEVEAALTEHPGVAEAVVVvrddRPGDK---RLVAYVVPAPGaAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNG 428
|
....*...
gi 1827387616 3053 KLDKRALP 3060
Cdd:cd17652 429 KLDRRALP 436
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1-547 |
5.26e-159 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 531.16 E-value: 5.26e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTs 80
Cdd:PRK10252 484 FSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITT- 562
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeAEARSRFDDIVDVHVLDISSPgDADLDEEEfAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:PRK10252 563 ---ADQLPRFADVPDLTSLCYNAP-LAPQGAAP-LQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLWMQNHYPLT 637
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFnevlgagVGELT-- 238
Cdd:PRK10252 638 ADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPLAMQQFFAEYGVTTTHFVPSMLAAF-------VASLTpe 710
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 239 -------SLRLIQTGGEALtPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDD------RVIPIGTPTRRVSARV 305
Cdd:PRK10252 711 garqscaSLRQVFCSGEAL-PADLCREWQQLTGAPLHNLYGPTEAAVDVSWYPAFGEElaavrgSSVPIGYPVWNTGLRI 789
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 306 LDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFGePGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQ 385
Cdd:PRK10252 790 LDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQ 868
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 386 RLELGEVEAALAAAPGVLHAAA-------AVVDGPGGQQLVGYLAPAD---VDVDTVAATTAELLPEYMRPSAWVRLDAM 455
Cdd:PRK10252 869 RIELGEIDRAMQALPDVEQAVThacvinqAAATGGDARQLVGYLVSQSglpLDTSALQAQLRERLPPHMVPVVLLQLDQL 948
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 456 PLSRSGKVDRRLLPEPEIAP-TLYVPPGNADEETVAGLFAELLGVERVGVTDSFFDIGGSSLSAARIAARVSKELGVDVS 534
Cdd:PRK10252 949 PLSANGKLDRKALPLPELKAqVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQFARQVT 1028
|
570
....*....|...
gi 1827387616 535 VRDVFESPSVRGL 547
Cdd:PRK10252 1029 PGQVMVASTVAKL 1041
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-995 |
5.54e-154 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 541.09 E-value: 5.54e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvtS 80
Cdd:PRK12316 537 LDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLL--S 614
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRFDDIVDVHVLDISSPGDADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:PRK12316 615 QSHLGRKLPLAAGVQVLDLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLG 694
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFneVLGAGVGELTSL 240
Cdd:PRK12316 695 VGDTVLQKTPFSFDVSVWEFFWPLMSGARLVVAAPGDHRDPAKLVELINREGVDTLHFVPSMLQAF--LQDEDVASCTSL 772
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 241 RLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVT-IHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIGVPG 319
Cdd:PRK12316 773 RRIVCSGEALPADAQEQVFAKLPQAGLYNLYGPTEAAIDVThWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLG 852
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 320 ELYLGGVQLARGYAGRPDLTAERFVADPFGEpGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAA 399
Cdd:PRK12316 853 ELYLAGRGLARGYHGRPGLTAERFVPSPFVA-GERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEH 931
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 400 PGVLHAAAAVVDgpgGQQLVGYLAPADVDVDTVAATTAEL---LPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEPE--IA 474
Cdd:PRK12316 932 PWVREAAVLAVD---GKQLVGYVVLESEGGDWREALKAHLaasLPEYMVPAQWLALERLPLTPNGKLDRKALPAPEasVA 1008
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 475 PTLYVPPGNADEETVAGLFAELLGVERVGVTDSFFDIGGSSLSAARIAARvSKELGVDVSVRDVFESPSVRGLVHaVSGR 554
Cdd:PRK12316 1009 QQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSR-ARQAGIQLSPRDLFQHQTIRSLAL-VAKA 1086
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 555 GSALPSVKriEPRPERLPLSRAQRrmWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAA 634
Cdd:PRK12316 1087 GQATAADQ--GPASGEVALAPVQR--WFFEQAIPQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGG 1162
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 635 PVQDVLPvAVAREQLDWREADSVESLVRSTTEG---FDVStQMPLRGRFHRDGA--GLHVALTMHHIAMDGQSIPVLARD 709
Cdd:PRK12316 1163 WQQAYAA-PQAGEVLWQRQAASEEELLALCEEAqrsLDLE-QGPLLRALLVDMAdgSQRLLLVIHHLVVDGVSWRILLED 1240
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 710 LMSAYA---ARAEGRTGGlpvldvqyadYALWQQSVLGDAddetSVLGEQLSHWRRVLAGLPavTDLPMDRPRPAVLGTA 786
Cdd:PRK12316 1241 LQRAYAdldADLPARTSS----------YQAWARRLHEHA----GARAEELDYWQAQLEDAP--HELPCENPDGALENRH 1304
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 787 GATVTVEFDDDLADRVDVLARSNTMTgfMVTE---AAFAATVARLASTTDVVIGTPVAGRNDPA----LEELIGMFvnTL 859
Cdd:PRK12316 1305 ERKLELRLDAERTRQLLQEAPAAYRT--QVNDlllTALARVTCRWSGQASVLVQLEGHGREDLFedidLSRTVGWF--TS 1380
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 860 LLRTQVDPGHSVGDLLGNVRTTvLDAFANDQVQFDeLIEALAPE---RSSSHQPLAQIAFTYT---EPTVNDVAGLEASG 933
Cdd:PRK12316 1381 LFPVRLTPAADLGESIKAIKEQ-LRAVPDKGIGYG-LLRYLAGEeaaARLAALPQPRITFNYLgqfDRQFDEAALFVPAT 1458
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 934 IQAAPVDTGvvNAKFDLTVAVRARSGGTPMAADFIYATDLFDESTVKRFAEVYRRVLQAIVD 995
Cdd:PRK12316 1459 ESAGAAQDP--CAPLANWLSIEGQVYGGELSLHWSFSREMFAEATVQRLADDYARELQALIE 1518
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1050-1531 |
6.21e-153 |
|
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: 482.52 E-value: 6.21e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDAStrarlgesscewvdladleaeaesgdditdterngsvrltNLAYLIYTSGSTGRPKAVGVSHTGIVD 1209
Cdd:cd17652 81 ADARPALLLTTPD----------------------------------------NLAYVIYTSGSTGRPKGVVVTHRGLAN 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 FVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQAD-FAGDALATVLERDEVTDMIITPSVLA 1288
Cdd:cd17652 121 LAAAQIAAFDVGPGS----RVLQFASPSFDASVWELLMALLAGATLVLAPAEElLPGEPLADLLREHRITHVTLPPAALA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1289 TVDPERAQYVRNLATGGEACPPELVERWSeRGRRIFNCYGPTEATVWATRSRM-TAGKPVTIGKPVDGFTVRVLDGRLHE 1367
Cdd:cd17652 197 ALPPDDLPDLRTLVVAGEACPAELVDRWA-PGRRMINAYGPTETTVCATMAGPlPGGGVPPIGRPVPGTRVYVLDARLRP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1368 VPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEPGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEI 1447
Cdd:cd17652 276 VPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEV 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1448 EAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDR 1527
Cdd:cd17652 356 EAALTEHPGVAEAVVVVRDDRPGDKR---LVAYVVPAPGAAPTAAELRAHLAERLPGYMVPAAFVVLDALPLTPNGKLDR 432
|
....
gi 1827387616 1528 AALP 1531
Cdd:cd17652 433 RALP 436
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2141-3145 |
7.31e-150 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 527.04 E-value: 7.31e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2141 LSLTGDVDPGRLRSALSELLARQRVLRSGFVRlPSGAAVTVVPAEVTVPWSVIDLRAEDAASLDSRVEEVLATERTNPFD 2220
Cdd:PRK05691 704 LHLRGELDEAALRASFQRLVERHESLRTRFYE-RDGVALQRIDAQGEFALQRIDLSDLPEAEREARAAQIREEEARQPFD 782
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2221 MAKPPLIRVVLVEHGDGA-ELVVTNHHLLIDGWSSPLVLADLLSLYAT---GQTFTGSLPGTSGRDFADHARA-VATADV 2295
Cdd:PRK05691 783 LEKGPLLRVTLVRLDDEEhQLLVTLHHIVADGWSLNILLDEFSRLYAAacqGQTAELAPLPLGYADYGAWQRQwLAQGEA 862
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2296 EAGIAAWREVLAPvTEPTLVAPGHEPSA---DAPPRDHQFSIDVKVTERLEALARNNSTTMATVVQFAWAMFLSRLTGTR 2372
Cdd:PRK05691 863 ARQLAYWKAQLGD-EQPVLELATDHPRSarqAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQALLHRYSGQG 941
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2373 TVTFAETVSGRsPDIEgMESMVGMFINTIPAVVDVNPDATVVDVLTAVQNDKVKVLDHQQIGLPRLVA---QTGLPALFD 2449
Cdd:PRK05691 942 DIRIGVPNANR-PRLE-TQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEalpQAREQGLFQ 1019
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2450 TLAVYESFpvnvdsvagiDASSAGGLKLVGAKT----SDATHYPLNL-SASRRGAELALKLKYLPTAFAPEQVAVFADVL 2524
Cdd:PRK05691 1020 VMFNHQQR----------DLSALRRLPGLLAEElpwhSREAKFDLQLhSEEDRNGRLTLSFDYAAELFDAATIERLAEHF 1089
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2525 TGLLGAIADHPEATCAEIPLLPAEAAVELTPVTGGPATDP-VTLAELFRAAARRAPDHVAVVdGAGARLTYRELDEASDR 2603
Cdd:PRK05691 1090 LALLEQVCEDPQRALGDVQLLDAAERAQLAQWGQAPCAPAqAWLPELLNEQARQTPERIALV-WDGGSLDYAELHAQANR 1168
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2604 LARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLGLSVLAS-GDLPGQEfe 2682
Cdd:PRK05691 1169 LAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLTQSHLlERLPQAE-- 1246
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2683 wmrlDDDSVAAEIAAVPAGPITdAERLgEVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFAR--QESDRLNAGDnpVVL 2760
Cdd:PRK05691 1247 ----GVSAIALDSLHLDSWPSQ-APGL-HLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQwmQATYALDDSD--VLM 1318
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2761 GFASPSFDASVLEYLLATVNEGTLAYR-PSEAVGGEVLERFIAEHGATHTFLTPSVLSTM----DPTAVPSLRVIAAGGE 2835
Cdd:PRK05691 1319 QKAPISFDVSVWECFWPLITGCRLVLAgPGEHRDPQRIAELVQQYGVTTLHFVPPLLQLFidepLAAACTSLRRLFSGGE 1398
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2836 AVPQPIVDR---WAPATELHNLYGPTETTIGIT-ISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGA 2911
Cdd:PRK05691 1399 ALPAELRNRvlqRLPQVQLHNRYGPTETAINVThWQCQAEDGERSPIGRPLGNVLCRVLDAELNLLPPGVAGELCIGGAG 1478
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2912 LSRGYLDRSGLTAERFTANPYGTAGQRMYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAV 2991
Cdd:PRK05691 1479 LARGYLGRPALTAERFVPDPLGEDGARLYRTGDRARWNADG-----ALEYLGRLDQQVKLRGFRVEPEEIQARLLAQPGV 1553
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2992 ESAVVLGVGGSVATALAAYIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVLEAGEYV 3070
Cdd:PRK05691 1554 AQAAVLVREGAAGAQLVGYYTGEAGQeAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPVWQQREHV 1633
|
970 980 990 1000 1010 1020 1030
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 3071 APATGTERTIADVAAGVLNI-DAGLvsaTSSFFELGGDSLSAARLAARLSDQLGVAVSVRDVFESGSIRALAETVG 3145
Cdd:PRK05691 1634 EPRTELQQQIAAIWREVLGLpRVGL---RDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQVA 1706
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
565-1606 |
2.70e-149 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 502.65 E-value: 2.70e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 565 EPRPERLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRT--------VYPSVGAAPV 636
Cdd:PRK10252 2 EPMSQHLPLVAAQPGIWMAEKLSPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMrftedngeVWQWVDPALT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 637 QDVLPVAVAREQLD-------WREADSVESLvrsttegfDVSTQMPL-RGRFHRDGAGLHV-ALTMHHIAMDGQSIPVLA 707
Cdd:PRK10252 82 FPLPEIIDLRTQPDphaaaqaLMQADLQQDL--------RVDSGKPLvFHQLIQLGDNRWYwYQRYHHLLVDGFSFPAIT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 708 RDLMSAYAARAEGR---TGGLPVLDVQYADYALWQQSVLGDADDetsvlgeqlSHWRRVLAGLPAVTDLPmdrPRPAVLG 784
Cdd:PRK10252 154 RRIAAIYCAWLRGEptpASPFTPFADVVEEYQRYRASEAWQRDA---------AFWAEQRRQLPPPASLS---PAPLPGR 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 785 TAGAT---VTVEFDDDLADRVDVLARSNTMTGFMVteAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLL 861
Cdd:PRK10252 222 SASADilrLKLEFTDGAFRQLAAQASGVQRPDLAL--ALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPL 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 862 RTQVDPGHSVGDLLGNVRTTVLDA-----FANDQVQFDElieALAPERSSSHQPLAQIAFTYTEPtvnDVAGLEAsgiQA 936
Cdd:PRK10252 300 RVHIAAQETLPELATRLAAQLKKMrrhqrYDAEQIVRDS---GRAAGDEPLFGPVLNIKVFDYQL---DFPGVQA---QT 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 937 APVDTGVVNakfDLTVAVRARSGGTpMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDDQNTAVGDIDIVGAARAKSVS 1016
Cdd:PRK10252 371 HTLATGPVN---DLELALFPDEHGG-LSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLA 446
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1017 APVSARTPgamvgrggeVEAGTLIDVLA-QRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMER 1095
Cdd:PRK10252 447 QVNATAVE---------IPETTLSALVAqQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPR 517
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1096 SIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDASTRARL-----GESSCEWVDLADLEAEAESGDDI 1170
Cdd:PRK10252 518 SVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARPSLLITTADQLPRFadvpdLTSLCYNAPLAPQGAAPLQLSQP 597
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1171 TDTerngsvrltnlAYLIYTSGSTGRPKAVGVSHTGIvdfVNSLAKITTGTPEdEPDTRILHVASPSFDASMFEMAWAIP 1250
Cdd:PRK10252 598 HHT-----------AYIIFTSGSTGRPKGVMVGQTAI---VNRLLWMQNHYPL-TADDVVLQKTPCSFDVSVWEFFWPFI 662
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1251 AGHTLVIA-PQADFAGDALATVLERDEVTDMIITPSVL----ATVDPERA----QYVRNLATGGEACPPELVERWSER-G 1320
Cdd:PRK10252 663 AGAKLVMAePEAHRDPLAMQQFFAEYGVTTTHFVPSMLaafvASLTPEGArqscASLRQVFCSGEALPADLCREWQQLtG 742
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1321 RRIFNCYGPTEATV-------WATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQ 1393
Cdd:PRK10252 743 APLHNLYGPTEAAVdvswypaFGEELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDL 822
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1394 TAVSFVADPFGePGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRG--- 1470
Cdd:PRK10252 823 TASRFIADPFA-PGERMYRTGDVARWLDDGAVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACVINQAaat 901
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1471 GRKHTEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEPHAPEPAEYVAPANPAED 1550
Cdd:PRK10252 902 GGDARQLVGYLVSQSGLPLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTET 981
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 1551 NLARIVAGLLGEERVSVTESFFALGGDSIMSIQLSSAAKAA-GIHLSPREIFELKTI 1606
Cdd:PRK10252 982 IIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSRQfARQVTPGQVMVASTV 1038
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
2087-3144 |
1.00e-148 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 523.75 E-value: 1.00e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2087 VEVTQDDLDLIAQQYPGADVWPMTPLQQGLFFQADLANTVAdhdaidVYVTQTVLSLTGDVDPGRLRSALSELLARQRVL 2166
Cdd:PRK12316 2583 LESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPESA------AYHLPSALHLRGVLDQAALEQAFDALVLRHETL 2656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2167 RSGFVRLPSGAAVTVVPAEvtvpwSVIDLRAEDAASLDSRVEEVLATERTNPFDMAKPPLIRVVLVEHGDGAE-LVVTNH 2245
Cdd:PRK12316 2657 RTRFVEVGEQTRQVILPNM-----SLRIVLEDCAGVADAAIRQRVAEEIQRPFDLARGPLLRVRLLALDGQEHvLVITQH 2731
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2246 HLLIDGWSSPLVLADLLSLY---ATGQTFTGSLPGTSGRDFADHARA-VATADVEAGIAAWREVLAPvTEPTLVAPGHEP 2321
Cdd:PRK12316 2732 HIVSDGWSMQVMVDELVQAYagaRRGEQPTLPPLPLQYADYAAWQRAwMDSGEGARQLDYWRERLGG-EQPVLELPLDRP 2810
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2322 SADAPPRD---HQFSIDVKVTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRspDIEGMESMVGMFI 2398
Cdd:PRK12316 2811 RPALQSHRgarLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANR--NRAETERLIGFFV 2888
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2399 NTIPAVVDVNPDATVVDVLTAVQNDKVKVLDHQQIGLPRLV------AQTGLPALFDTLAVYESFPVNVDSVAGIDASSA 2472
Cdd:PRK12316 2889 NTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVealqpeRSLSHSPLFQVMYNHQSGERAAAQLPGLHIESF 2968
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2473 gglklvgAKTSDATHYPLNLSASRRGAELALKLKYLPTAFAPEQVAVFADVLTGLLGAIADHPEATCAEIPLLPAEA--- 2549
Cdd:PRK12316 2969 -------AWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEErgq 3041
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2550 AVELTPVTGGPATDPVTLAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQL 2629
Cdd:PRK12316 3042 LLEAWNATAAEYPLERGVHRLFEEQVERTPDAVALAFG-EQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEM 3120
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2630 LTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLGLSVLASGDLPGQEFEWMRLDDDSVAAEIAAVPAgpitdaerl 2709
Cdd:PRK12316 3121 VVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLSQSHLRLPLAQGVQVLDLDRGDENYAEANPAI--------- 3191
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2710 gEVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYR-P 2788
Cdd:PRK12316 3192 -RTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAYGLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAgP 3270
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2789 SEAVGGEVLERFIAEHGATHTFLTPSVLSTM----DPTAVPSLRVIAAGGEAVPQPIVDRWAPATELHNLYGPTETTIGI 2864
Cdd:PRK12316 3271 EDWRDPALLVELINSEGVDVLHAYPSMLQAFleeeDAHRCTSLKRIVCGGEALPADLQQQVFAGLPLYNLYGPTEATITV 3350
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2865 TISSAMRPG-DPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYgTAGQRMYRTG 2943
Cdd:PRK12316 3351 THWQCVEEGkDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPF-VPGERLYRTG 3429
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2944 DVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSvatALAAYIVPVDGAVEVSE- 3022
Cdd:PRK12316 3430 DLARYRADG-----VIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGR---QLVAYVVPEDEAGDLREa 3501
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3023 LKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVLEAGE--YVAPATGTERTIADVAAGVLNIDAglVSATSS 3100
Cdd:PRK12316 3502 LKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPDAALLQqdYVAPVNELERRLAAIWADVLKLEQ--VGLTDN 3579
|
1050 1060 1070 1080
....*....|....*....|....*....|....*....|....
gi 1827387616 3101 FFELGGDSLSAARLAARlSDQLGVAVSVRDVFESGSIRALAETV 3144
Cdd:PRK12316 3580 FFELGGDSIISLQVVSR-ARQAGIRFTPKDLFQHQTIQGLARVA 3622
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
2569-3059 |
7.80e-147 |
|
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: 467.14 E-value: 7.80e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2569 ELFRAAARRAPDHVAVVDgAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDP 2648
Cdd:cd17646 2 ALVAEQAARTPDAPAVVD-EGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2649 DYPAERVASMIEDSGAVLglsVLASGDLPGqefeWMRLDDDSVAAEIAAVPAGPITDAERlgEVTAANLAYVIYTSGSTG 2728
Cdd:cd17646 81 GYPADRLAYMLADAGPAV---VLTTADLAA----RLPAGGDVALLGDEALAAPPATPPLV--PPRPDNLAYVIYTSGSTG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2729 RPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAY-RPSEAVGGEVLERFIAEHGAT 2807
Cdd:cd17646 152 RPKGVMVTHAGIVNRLLWMQDEYPLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVaRPGGHRDPAYLAALIREHGVT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2808 HTFLTPSVL----STMDPTAVPSLRVIAAGGEAVPQPIVDRWA--PATELHNLYGPTETTIGIT--ISSAMRPGDPVRLG 2879
Cdd:cd17646 232 TCHFVPSMLrvflAEPAAGSCASLRRVFCSGEALPPELAARFLalPGAELHNLYGPTEAAIDVThwPVRGPAETPSVPIG 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2880 GPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGtAGQRMYRTGDVVRWTPDTdtgglTL 2959
Cdd:cd17646 312 RPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFG-PGSRMYRTGDLARWRPDG-----AL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2960 EYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG-GSVATALAAYIVPVDGAVEVS--ELKAFAGGRLPAYMV 3036
Cdd:cd17646 386 EFLGRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAaPAGAARLVGYVVPAAGAAGPDtaALRAHLAERLPEYMV 465
|
490 500
....*....|....*....|...
gi 1827387616 3037 PSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd17646 466 PAAFVVLDALPLTANGKLDRAAL 488
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
2101-3141 |
1.12e-146 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 494.56 E-value: 1.12e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2101 YPGADVWPMTPLQQGLFFqadlANTVADHDAIdvYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPSGAAVT 2180
Cdd:PRK10252 2 EPMSQHLPLVAAQPGIWM----AEKLSPLPSA--WSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2181 VVPAEVTVPWSVIDLRAEDAASLDSRVeeVLATERTNPFDMAK-PPLIRVVLVEHGDGAELVVTN-HHLLIDGWSSPLVL 2258
Cdd:PRK10252 76 VDPALTFPLPEIIDLRTQPDPHAAAQA--LMQADLQQDLRVDSgKPLVFHQLIQLGDNRWYWYQRyHHLLVDGFSFPAIT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2259 ADLLSLYAT----GQTFTGSLPGTSGRdFADHARAVATADVEAGIAAWREVLAPVTEPTLVAPGHEPSADAPPRDHQFS- 2333
Cdd:PRK10252 154 RRIAAIYCAwlrgEPTPASPFTPFADV-VEEYQRYRASEAWQRDAAFWAEQRRQLPPPASLSPAPLPGRSASADILRLKl 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2334 -IDVKVTERLEALARNNSTT-MATVVQFAWamfLSRLTGTRTVTFAETVSGR--SPDIegmeSMVGMFINTIPAVVDVNP 2409
Cdd:PRK10252 233 eFTDGAFRQLAAQASGVQRPdLALALVALW---LGRLCGRMDYAAGFIFMRRlgSAAL----TATGPVLNVLPLRVHIAA 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2410 DATVVDVLTAVQNDKVKVLDHQQIGLPRLVAQTGLPA----LFDTLAVYESFPVNVDsVAGIDAssagglklvgaKTSDA 2485
Cdd:PRK10252 306 QETLPELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAgdepLFGPVLNIKVFDYQLD-FPGVQA-----------QTHTL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2486 THYPLN-LSASRRGAE---LALKLKYLPTAFAPEQVAVFADVLTGLLGAIADHPEATCAEIPLLPAEAAVELTPVTggpA 2561
Cdd:PRK10252 374 ATGPVNdLELALFPDEhggLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQLAQVN---A 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2562 TD----PVTLAELFRAAARRAPDHVAVVDgAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVA 2637
Cdd:PRK10252 451 TAveipETTLSALVAQQAAKTPDAPALAD-ARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIV 529
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2638 KTGGAYVPIDPDYPAERVASMIEDSGAVLglsVLASGDLPGqefewmRLDD--DSVAAEIAAVPAGPitDAERLGEVTAA 2715
Cdd:PRK10252 530 EAGAAWLPLDTGYPDDRLKMMLEDARPSL---LITTADQLP------RFADvpDLTSLCYNAPLAPQ--GAAPLQLSQPH 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2716 NLAYVIYTSGSTGRPKGVAVTHSGLAN--FARQESDRLNAGDnpVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEA-V 2792
Cdd:PRK10252 599 HTAYIIFTSGSTGRPKGVMVGQTAIVNrlLWMQNHYPLTADD--VVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAhR 676
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2793 GGEVLERFIAEHGATHTFLTPSVLSTM--------DPTAVPSLRVIAAGGEAVPQPIVDRWAPAT--ELHNLYGPTETTI 2862
Cdd:PRK10252 677 DPLAMQQFFAEYGVTTTHFVPSMLAAFvasltpegARQSCASLRQVFCSGEALPADLCREWQQLTgaPLHNLYGPTEAAV 756
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2863 GITI------SSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGtAG 2936
Cdd:PRK10252 757 DVSWypafgeELAAVRGSSVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFA-PG 835
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2937 QRMYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-------GGSVATALAA 3009
Cdd:PRK10252 836 ERMYRTGDVARWLDDG-----AVEYLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVTHACvinqaaaTGGDARQLVG 910
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3010 YIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVLEAGEY-VAPATGTERTIADVAAGV 3087
Cdd:PRK10252 911 YLVSQSGLpLDTSALQAQLRERLPPHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPgRAPKTGTETIIAAAFSSL 990
|
1050 1060 1070 1080 1090
....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 3088 LNIDAglVSATSSFFELGGDSLSAARLAARLSDQLGVAVSVRDVFESGSIRALA 3141
Cdd:PRK10252 991 LGCDV--VDADADFFALGGHSLLAMKLAAQLSRQFARQVTPGQVMVASTVAKLA 1042
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
2569-3059 |
2.20e-143 |
|
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: 457.05 E-value: 2.20e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2569 ELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDP 2648
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYG-DRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2649 DYPAERVASMIEDSGAVLglsVLASGDLPGqefewmRLDDDSVAAEIAAVPAGPITDAERLGeVTAANLAYVIYTSGSTG 2728
Cdd:cd12117 80 ELPAERLAFMLADAGAKV---LLTDRSLAG------RAGGLEVAVVIDEALDAGPAGNPAVP-VSPDDLAYVMYTSGSTG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2729 RPKGVAVTHSGLANFARqESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAV-GGEVLERFIAEHGAT 2807
Cdd:cd12117 150 RPKGVAVTHRGVVRLVK-NTNYVTLGPDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVT 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2808 HTFLTPSVLSTM---DPTAVPSLRVIAAGGEAVPQPIVDRW---APATELHNLYGPTETTIgITISSAMRPGDPVR---- 2877
Cdd:cd12117 229 VLWLTAALFNQLadeDPECFAGLRELLTGGEVVSPPHVRRVlaaCPGLRLVNGYGPTENTT-FTTSHVVTELDEVAgsip 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2878 LGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGtAGQRMYRTGDVVRWTPDtdtggL 2957
Cdd:cd12117 308 IGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFG-PGERLYRTGDLARWLPD-----G 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2958 TLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAV-ESAVVLGVGGSVATALAAYIVPvDGAVEVSELKAFAGGRLPAYMV 3036
Cdd:cd12117 382 RLEFLGRIDDQVKIRGFRIELGEIEAALRAHPGVrEAVVVVREDAGGDKRLVAYVVA-EGALDAAELRAFLRERLPAYMV 460
|
490 500
....*....|....*....|...
gi 1827387616 3037 PSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd12117 461 PAAFVVLDELPLTANGKVDRRAL 483
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
570-996 |
7.30e-143 |
|
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: 452.96 E-value: 7.30e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 570 RLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDVLP---VAVAR 646
Cdd:cd19531 1 PLPLSFAQQRLWFLDQLEPGSAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPplpLPLPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 647 EQL-----DWREADsVESLVRS-TTEGFDVSTQMPLRGRFHRDGAGLHV-ALTMHHIAMDGQSIPVLARDLMSAYAARAE 719
Cdd:cd19531 81 VDLsglpeAEREAE-AQRLAREeARRPFDLARGPLLRATLLRLGEDEHVlLLTMHHIVSDGWSMGVLLRELAALYAAFLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 720 GRTGGLPVLDVQYADYALWQQSVLgdaddETSVLGEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVEFDDDLA 799
Cdd:cd19531 160 GRPSPLPPLPIQYADYAVWQREWL-----QGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAELT 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 800 DRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGDLLGNVR 879
Cdd:cd19531 235 AALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLARVR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 880 TTVLDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTYTEPtvnDVAGLEASGIQAAPVDTGVVNAKFDLTVAVRARSG 959
Cdd:cd19531 315 ETALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNA---PAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDG 391
|
410 420 430
....*....|....*....|....*....|....*..
gi 1827387616 960 GtpMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd19531 392 G--LRGSLEYNTDLFDAATIERMAGHFQTLLEAIVAD 426
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
1-757 |
6.49e-142 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 500.84 E-value: 6.49e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVts 80
Cdd:PRK12467 3121 LSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLT-- 3198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgEAEARSRFDDIVDVHVLDISSPGDADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:PRK12467 3199 --QAHLLEQLPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELD 3276
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIAePGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEvlGAGVGELTSL 240
Cdd:PRK12467 3277 ANDRVLLFMSFSFDGAQERFLWTLICGGCLVVR-DNDLWDPEELWQAIHAHRISIACFPPAYLQQFAE--DAGGADCASL 3353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 241 RLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDR----VIPIGTPTRRVSARVLDAALREVPIG 316
Cdd:PRK12467 3354 DIYVFGGEAVPPAAFEQVKRKLKPRGLTNGYGPTEAVVTVTLWKCGGDAVceapYAPIGRPVAGRSIYVLDGQLNPVPVG 3433
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 317 VPGELYLGGVQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAAL 396
Cdd:PRK12467 3434 VAGELYIGGVGLARGYHQRPSLTAERFVADPFSGSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARL 3513
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 397 AAAPGVLHAAAAVVDGPGGQQLVGYLAPADVDVD---TVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEPEI 473
Cdd:PRK12467 3514 LQHPSVREAVVLARDGAGGKQLVAYVVPADPQGDwreTLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDA 3593
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 474 APT-LYVPPGNADEETVAGLFAELLGVERVGVTDSFFDIGGSSLSAARIAARVSKELGVDVSVRDVFESPSVRGLVhAVS 552
Cdd:PRK12467 3594 KGSrEYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELA-GYS 3672
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 553 GRGSALPSVKrieprperLPLSRAQRrmwflnqfdtasgaynipaaltlagdvdetllfdSLCDVVERHEVLRTVYpsvg 632
Cdd:PRK12467 3673 PLGDVPVNLL--------LDLNRLET----------------------------------GFPALFCRHEGLGTVF---- 3706
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 633 aapvqDVLPVAVAreqldwreadsveslvrsttegfdvstqmpLRGRFHRDGaglhvaLTMHHIAMDGQSIPvlardlms 712
Cdd:PRK12467 3707 -----DYEPLAVI------------------------------LEGDRHVLG------LTCRHLLDDGWQDT-------- 3737
|
730 740 750 760
....*....|....*....|....*....|....*....|....*
gi 1827387616 713 ayaaraegrtgGLPVLDVQYADYALWQQsvlgdADDETSVLGEQL 757
Cdd:PRK12467 3738 -----------SLQAMAVQYADYILWQQ-----AKGPYGLLGWSL 3766
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
2579-3059 |
4.24e-139 |
|
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: 444.04 E-value: 4.24e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2579 PDHVAVVDGAGaRLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASM 2658
Cdd:cd12116 1 PDATAVRDDDR-SLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2659 IEDSGAVLglsVLASGDLPGqefewmRLDDDSVAAEIAaVPAGPITDAERLGEVTAANLAYVIYTSGSTGRPKGVAVTHS 2738
Cdd:cd12116 80 LEDAEPAL---VLTDDALPD------RLPAGLPVLLLA-LAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2739 GLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAV-GGEVLERFIAEHGATHTFLTPSV-- 2815
Cdd:cd12116 150 NLVNFLHSMRERLGLGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQrDPEALARLIEAHSITVMQATPATwr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2816 -LSTMDPTAVPSLRVIAaGGEAVPQPIVDRW-APATELHNLYGPTETTIGITISSAMRPGDPVRLGGPIGGVDLMVLDER 2893
Cdd:cd12116 230 mLLDAGWQGRAGLTALC-GGEALPPDLAARLlSRVGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2894 LRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRMYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRG 2973
Cdd:cd12116 309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADG-----RLEYLGRADGQVKIRG 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2974 LRIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPVDG-AVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVG 3052
Cdd:cd12116 384 HRIELGEIEAALAAHPGVAQAAVVVREDGGDRRLVAYVVLKAGaAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANG 463
|
....*..
gi 1827387616 3053 KLDKRAL 3059
Cdd:cd12116 464 KLDRKAL 470
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
2569-3062 |
2.16e-138 |
|
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: 442.92 E-value: 2.16e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2569 ELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDP 2648
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFE-DQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2649 DYPAERVASMIEDSGAVLglsVLASGDLPGQEF---EWMRLDDDSVAAEiaavpagPITDAERlgEVTAANLAYVIYTSG 2725
Cdd:cd17655 80 DYPEERIQYILEDSGADI---LLTQSHLQPPIAfigLIDLLDEDTIYHE-------ESENLEP--VSKSDDLAYVIYTSG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2726 STGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTL-AYRPSEAVGGEVLERFIAEH 2804
Cdd:cd17655 148 STGKPKGVMIEHRGVVNLVEWANKVIYQGEHLRVALFASISFDASVTEIFASLLSGNTLyIVRKETVLDGQALTQYIRQN 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2805 GATHTFLTPSVLSTMDP---TAVPSLRVIAAGGEAVPQPIVDRW----APATELHNLYGPTETTIGITI---SSAMRPGD 2874
Cdd:cd17655 228 RITIIDLTPAHLKLLDAaddSEGLSLKHLIVGGEALSTELAKKIielfGTNPTITNAYGPTETTVDASIyqyEPETDQQV 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2875 PVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYgTAGQRMYRTGDVVRWTPDTdt 2954
Cdd:cd17655 308 SVPIGKPLGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLPDG-- 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2955 gglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV---GGSVatALAAYIVPvDGAVEVSELKAFAGGRL 3031
Cdd:cd17655 385 ---NIEFLGRIDHQVKIRGYRIELGEIEARLLQHPDIKEAVVIARkdeQGQN--YLCAYIVS-EKELPVAQLREFLAREL 458
|
490 500 510
....*....|....*....|....*....|.
gi 1827387616 3032 PAYMVPSSFTVIDELPLTPVGKLDKRALPEP 3062
Cdd:cd17655 459 PDYMIPSYFIKLDEIPLTPNGKVDRKALPEP 489
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1-468 |
2.33e-138 |
|
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: 442.41 E-value: 2.33e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvtS 80
Cdd:cd12117 23 LTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFMLADAGAKVLL--T 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRfDDIVDVHVLDISSPGDAdldeEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIAnRLAADIEQYDLT 160
Cdd:cd12117 101 DRSLAGRAG-GLEVAVVIDEALDAGPA----GNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVV-RLVKNTNYVTLG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMlaaFNEVLGAGVGELTSL 240
Cdd:cd12117 175 PDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLDPDALGALIAEEGVTVLWLTAAL---FNQLADEDPECFAGL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 241 RLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRV---IPIGTPTRRVSARVLDAALREVPIGV 317
Cdd:cd12117 252 RELLTGGEVVSPPHVRRVLAACPGLRLVNGYGPTENTTFTTSHVVTELDEVagsIPIGRPIANTRVYVLDEDGRPVPPGV 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 318 PGELYLGGVQLARGYAGRPDLTAERFVADPFGePGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALA 397
Cdd:cd12117 332 PGELYVGGDGLALGYLNRPALTAERFVADPFG-PGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRGFRIELGEIEAALR 410
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 398 AAPGVLHAAAAVV-DGPGGQQLVGYLAPA-DVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd12117 411 AHPGVREAVVVVReDAGGDKRLVAYVVAEgALDAAELRAFLRERLPAYMVPAAFVVLDELPLTANGKVDRRAL 483
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
4-407 |
5.77e-138 |
|
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: 438.24 E-value: 5.77e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLAREL-TALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDG 82
Cdd:TIGR01733 3 RELDERANRLARHLrAAGGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 83 EAEARSRFDDIVDVHVLDiSSPGDADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTAR 162
Cdd:TIGR01733 83 ASRLAGLVLPVILLDPLE-LAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDPD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 163 DVFLYKAPITFDVSVREIFLPIAIGATLVIAEPG-RHGDPVHLADLIRRHGVTVIHFVPAMLAAFnevLGAGVGELTSLR 241
Cdd:TIGR01733 162 DRVLQFASLSFDASVEEIFGALLAGATLVVPPEDeERDDAALLAALIAEHPVTVLNLTPSLLALL---AAALPPALASLR 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 242 LIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDD----RVIPIGTPTRRVSARVLDAALREVPIGV 317
Cdd:TIGR01733 239 LVILGGEALTPALVDRWRARGPGARLINLYGPTETTVWSTATLVDPDDapreSPVPIGRPLANTRLYVLDDDLRPVPVGV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 318 PGELYLGGVQLARGYAGRPDLTAERFVADPF-GEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAAL 396
Cdd:TIGR01733 319 VGELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEAAL 398
|
410
....*....|.
gi 1827387616 397 AAAPGVLHAAA 407
Cdd:TIGR01733 399 LRHPGVREAVV 409
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1050-1530 |
1.13e-137 |
|
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: 440.48 E-value: 1.13e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd12117 11 PDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELPAERLAFML 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDASTRARLGESSCEWVDLADLEAEAESGDditdterNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVD 1209
Cdd:cd12117 91 ADAGAKVLLTDRSLAGRAGGLEVAVVIDEALDAGPAGNP-------AVPVSPDDLAYVMYTSGSTGRPKGVAVTHRGVVR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 FVNSLAKITTGtpedePDTRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFA-GDALATVLERDEVTDMIITPSV-- 1286
Cdd:cd12117 164 LVKNTNYVTLG-----PDDRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLLdPDALGALIAEEGVTVLWLTAALfn 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1287 -LATVDPERAQYVRNLATGGEACPPELVERWSER--GRRIFNCYGPTEATVWATRSRMTAGKPVT----IGKPVDGFTVR 1359
Cdd:cd12117 239 qLADEDPECFAGLRELLTGGEVVSPPHVRRVLAAcpGLRLVNGYGPTENTTFTTSHVVTELDEVAgsipIGRPIANTRVY 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1360 VLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGePGARMYATGDLVRVAKGGNLEFAGRADHQVKING 1439
Cdd:cd12117 319 VLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFG-PGERLYRTGDLARWLPDGRLEFLGRIDDQVKIRG 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1440 QRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPgaTIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPL 1519
Cdd:cd12117 398 FRIELGEIEAALRAHPGVREAVVVVREDAGGDK---RLVAYVVAEG--ALDAAELRAFLRERLPAYMVPAAFVVLDELPL 472
|
490
....*....|.
gi 1827387616 1520 TPAGKLDRAAL 1530
Cdd:cd12117 473 TANGKVDRRAL 483
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1050-1530 |
5.88e-137 |
|
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: 437.88 E-value: 5.88e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDASTRARLgeSSCEWVDLADLEAEAESGDditdtERNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVD 1209
Cdd:cd12116 81 EDAEPALVLTDDALPDRL--PAGLPVLLLALAAAAAAPA-----APRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVN 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 FVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAP-QADFAGDALATVLERDEVTDMIITPSV-- 1286
Cdd:cd12116 154 FLHSMRERLGLGPGD----RLLAVTTYAFDISLLELLLPLLAGARVVIAPrETQRDPEALARLIEAHSITVMQATPATwr 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1287 -LATVDPERAQYVRNLAtGGEACPPELVERWSERGRRIFNCYGPTEATVWATRSRMTAGK-PVTIGKPVDGFTVRVLDGR 1364
Cdd:cd12116 230 mLLDAGWQGRAGLTALC-GGEALPPDLAARLLSRVGSLWNLYGPTETTIWSTAARVTAAAgPIPIGRPLANTQVYVLDAA 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1365 LHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEPGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVEL 1444
Cdd:cd12116 309 LRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIEL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1445 GEIEAVLDAQPGVAQSVVVGvestRGGRKHTEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGK 1524
Cdd:cd12116 389 GEIEAALAAHPGVAQAAVVV----REDGGDRRLVAYVVLKAGAAPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGK 464
|
....*.
gi 1827387616 1525 LDRAAL 1530
Cdd:cd12116 465 LDRKAL 470
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
2571-3060 |
1.14e-136 |
|
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: 437.93 E-value: 1.14e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2571 FRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDY 2650
Cdd:cd17651 1 FERQAARTPDAPALVAE-GRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2651 PAERVASMIEDSGAVLGLsvLASGDLPGQEfewmrlDDDSVAAEIAAVPAGPITDAERLGEVTAANLAYVIYTSGSTGRP 2730
Cdd:cd17651 80 PAERLAFMLADAGPVLVL--THPALAGELA------VELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRP 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2731 KGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEA-VGGEVLERFIAEHGATHT 2809
Cdd:cd17651 152 KGVVMPHRSLANLVAWQARASSLGPGARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVrTDPPALAAWLDEQRISRV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2810 FLTPSVL------STMDPTAVPSLRVIAAGGEAVP-QPIVDRW---APATELHNLYGPTETTIGITISSAMRPG---DPV 2876
Cdd:cd17651 232 FLPTVALralaehGRPLGVRLAALRYLLTGGEQLVlTEDLREFcagLPGLRLHNHYGPTETHVVTALSLPGDPAawpAPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2877 RLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTaGQRMYRTGDVVRWTPDTdtgg 2956
Cdd:cd17651 312 PIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVP-GARMYRTGDLARWLPDG---- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2957 lTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-GGSVATALAAYIVPVDGA-VEVSELKAFAGGRLPAY 3034
Cdd:cd17651 387 -ELEFLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAReDRPGEKRLVAYVVGDPEApVDAAELRAALATHLPEY 465
|
490 500
....*....|....*....|....*.
gi 1827387616 3035 MVPSSFTVIDELPLTPVGKLDKRALP 3060
Cdd:cd17651 466 MVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1044-1530 |
4.26e-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: 436.32 E-value: 4.26e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1044 AQRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPAD 1123
Cdd:cd17646 6 EQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDPGYPAD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1124 RIAYMLEDSGATVGITDASTRARLGESSCewVDLADLEAEAESGDDITDTErngsVRLTNLAYLIYTSGSTGRPKAVGVS 1203
Cdd:cd17646 86 RLAYMLADAGPAVVLTTADLAARLPAGGD--VALLGDEALAAPPATPPLVP----PRPDNLAYVIYTSGSTGRPKGVMVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1204 HTGIvdfVNSLAKITTGTPEDePDTRILHVASPSFDASMFEMAWAIPAGHTLVIA-PQADFAGDALATVLERDEVTDMII 1282
Cdd:cd17646 160 HAGI---VNRLLWMQDEYPLG-PGDRVLQKTPLSFDVSVWELFWPLVAGARLVVArPGGHRDPAYLAALIREHGVTTCHF 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1283 TPSVL----ATVDPERAQYVRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAGK---PVTIGKPVD 1354
Cdd:cd17646 236 VPSMLrvflAEPAAGSCASLRRVFCSGEALPPELAARFLALpGAELHNLYGPTEAAIDVTHWPVRGPAetpSVPIGRPVP 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1355 GFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGePGARMYATGDLVRVAKGGNLEFAGRADHQ 1434
Cdd:cd17646 316 NTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFG-PGSRMYRTGDLARWRPDGALEFLGRSDDQ 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1435 VKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGAT-IDSAAVLDEAAQHLAAHMVPSQAIV 1513
Cdd:cd17646 395 VKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAAR---LVGYVVPAAGAAgPDTAALRAHLAERLPEYMVPAAFVV 471
|
490
....*....|....*..
gi 1827387616 1514 IDEIPLTPAGKLDRAAL 1530
Cdd:cd17646 472 LDALPLTANGKLDRAAL 488
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1-468 |
6.92e-136 |
|
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: 434.80 E-value: 6.92e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:cd12116 13 LSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYILEDAEPALVLTDD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRFDdivdvhVLDISSPGDAdLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd12116 93 ALPDRLPAGLP------VLLLALAAAA-AAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSMRERLGLG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPA---MLaafnevLGAGVGEL 237
Cdd:cd12116 166 PGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPRETQRDPEALARLIEAHSITVMQATPAtwrML------LDAGWQGR 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 238 TSLRLIqTGGEALTPPVARDLMVRlpGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIGV 317
Cdd:cd12116 240 AGLTAL-CGGEALPPDLAARLLSR--VGSLWNLYGPTETTIWSTAARVTAAAGPIPIGRPLANTQVYVLDAALRPVPPGV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 318 PGELYLGGVQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALA 397
Cdd:cd12116 317 PGELYIGGDGVAQGYLGRPALTAERFVPDPFAGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRIELGEIEAALA 396
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 398 AAPGVLHAAAAVVDGPGGQQLVGYLAPAD---VDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd12116 397 AHPGVAQAAVVVREDGGDRRLVAYVVLKAgaaPDAAALRAHLRATLPAYMVPSAFVRLDALPLTANGKLDRKAL 470
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
1-557 |
3.81e-134 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 475.99 E-value: 3.81e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:PRK12316 4577 LTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQS 4656
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeaEARSRFDDIVDVHVLDISSPGD-ADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDL 159
Cdd:PRK12316 4657 ----HLLQRLPIPDGLASLALDRDEDwEGFPAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERYEL 4732
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 160 TARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHgDPVHLADLIRRHGVTVIHFVPAMLAAFNEvlGAGV-GELT 238
Cdd:PRK12316 4733 TPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLW-DPERLYAEIHEHRVTVLVFPPVYLQQLAE--HAERdGEPP 4809
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 239 SLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDR----VIPIGTPTRRVSARVLDAALREVP 314
Cdd:PRK12316 4810 SLRVYCFGGEAVAQASYDLAWRALKPVYLFNGYGPTETTVTVLLWKARDGDAcgaaYMPIGTPLGNRSGYVLDGQLNPLP 4889
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 315 IGVPGELYLGGVQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEA 394
Cdd:PRK12316 4890 VGVAGELYLGGEGVARGYLERPALTAERFVPDPFGAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEA 4969
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 395 ALAAAPGVLHAAAAVVDGPGGQQLVGYLAPADVDVDTVAATTAEL-----------LPEYMRPSAWVRLDAMPLSRSGKV 463
Cdd:PRK12316 4970 RLREHPAVREAVVIAQEGAVGKQLVGYVVPQDPALADADEAQAELrdelkaalrerLPEYMVPAHLVFLARMPLTPNGKL 5049
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 464 DRRLLPEPE--IAPTLYVPPGNADEETVAGLFAELLGVERVGVTDSFFDIGGSSLSAARIAARVSKELGVDVSVRDVFES 541
Cdd:PRK12316 5050 DRKALPQPDasLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQT 5129
|
570
....*....|....*.
gi 1827387616 542 PSVRGLVHAVSGRGSA 557
Cdd:PRK12316 5130 PTLAAFVELAAAAGSG 5145
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1-469 |
6.20e-134 |
|
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: 428.33 E-value: 6.20e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTs 80
Cdd:cd17649 13 LSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYMLEDSGAGLLLTH- 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeaearsrfddivdvhvldisspgdadldeeefagptRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd17649 92 --------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQATAERYGLT 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGA-GVGELTS 239
Cdd:cd17649 134 PGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADELAEMVRELGVTVLDLPPAYLQQLAEEADRtGDGRPPS 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 240 LRLIQTGGEALTPPVARDLMVrlPGTRLQNQYGPAEASIVVTIHRVTQDDR----VIPIGTPTRRVSARVLDAALREVPI 315
Cdd:cd17649 214 LRLYIFGGEALSPELLRRWLK--APVRLFNAYGPTEATVTPLVWKCEAGAAragaSMPIGRPLGGRSAYILDADLNPVPV 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 316 GVPGELYLGGVQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAA 395
Cdd:cd17649 292 GVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGFRIELGEIEAA 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 396 LAAAPGVLHAAAAVVDGPGGQQLVGYLAPADV-----DVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLP 469
Cdd:cd17649 372 LLEHPGVREAAVVALDGAGGKQLVAYVVLRAAaaqpeLRAQLRTALRASLPDYMVPAHLVFLARLPLTPNGKLDRKALP 450
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
2593-2996 |
8.58e-134 |
|
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: 426.30 E-value: 8.58e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2593 TYRELDEASDRLARWLIGR-GVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLGLSVL 2671
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2672 ASGDLPGQEFEWMRLDDDSVAAEIAAVPAGPITDAERLGEvtaaNLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRL 2751
Cdd:TIGR01733 81 ALASRLAGLVLPVILLDPLELAALDDAPAPPPPDAPSGPD----DLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2752 NAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVG--GEVLERFIAEHGATHTFLTPSVLSTMDPTAVP---S 2826
Cdd:TIGR01733 157 GLDPDDRVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERddAALLAALIAEHPVTVLNLTPSLLALLAAALPPalaS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2827 LRVIAAGGEAVPQPIVDRWA---PATELHNLYGPTETTIGITISSAMRPGD----PVRLGGPIGGVDLMVLDERLRPVPV 2899
Cdd:TIGR01733 237 LRLVILGGEALTPALVDRWRargPGARLINLYGPTETTVWSTATLVDPDDApresPVPIGRPLANTRLYVLDDDLRPVPV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2900 GMPGELYVAGGALSRGYLDRSGLTAERFTANPY-GTAGQRMYRTGDVVRWTPDtdtGglTLEYTGRSDDQVKLRGLRIEL 2978
Cdd:TIGR01733 317 GVVGELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPD---G--NLEFLGRIDDQVKIRGYRIEL 391
|
410
....*....|....*...
gi 1827387616 2979 GEIEAVLAEHDAVESAVV 2996
Cdd:TIGR01733 392 GEIEAALLRHPGVREAVV 409
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2143-3148 |
3.96e-133 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 472.35 E-value: 3.96e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2143 LTGDVDPGRLRSALSELLARQRVLRSGFvrlPS--GAAVTVVPAEVTVPWSVIDLRAEDAASLDSRVEEVLATERTNPFD 2220
Cdd:PRK05691 1759 LSGVLDVDRFEAALQALILRHETLRTTF---PSvdGVPVQQVAEDSGLRMDWQDFSALPADARQQRLQQLADSEAHQPFD 1835
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2221 MAKPPLIRVVLVEHGDGAE-LVVTNHHLLIDGWSSPLVLADLLSLYatgQTFTgslpgtSGRDFADHARAVATAD----- 2294
Cdd:PRK05691 1836 LERGPLLRACLVKAAEREHyFVLTLHHIVTEGWAMDIFARELGALY---EAFL------DDRESPLEPLPVQYLDysvwq 1906
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2295 ---VEAG-----IAAWREVLApvTE-PTLVAPGHEPSAdaPPRDHQ-----FSIDVKVTERLEALARNNSTTMATVVQFA 2360
Cdd:PRK05691 1907 rqwLESGerqrqLDYWKAQLG--NEhPLLELPADRPRP--PVQSHRgelyrFDLSPELAARVRAFNAQRGLTLFMTMTAT 1982
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2361 WAMFLSRLTGTRTVTFAETVSGR-SPDIEGMesmVGMFINTIPAVVDVNPDATVVDVLTAVQNDKVKVLDHQQIGLPRLV 2439
Cdd:PRK05691 1983 LAALLYRYSGQRDLRIGAPVANRiRPESEGL---IGAFLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLV 2059
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2440 AQTGLP--ALFDTLavyesFPV--NVDSVAGIDASSAGGLKL-VGAKTSDATHYPLNLSASRRGAELALKLKYLPTAFAP 2514
Cdd:PRK05691 2060 EALQPPrsAAYNPL-----FQVmcNVQRWEFQQSRQLAGMTVeYLVNDARATKFDLNLEVTDLDGRLGCCLTYSRDLFDE 2134
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2515 EQVAVFADVLTGLLGAIADHPEATCAEIPLLPAEAAVELTPVTGGPATDPV---TLAELFRAAARRAPDHVAVVdGAGAR 2591
Cdd:PRK05691 2135 PRIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAGEARldqTLHGLFAAQAARTPQAPALT-FAGQT 2213
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2592 LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLGLS-- 2669
Cdd:PRK05691 2214 LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLLSdr 2293
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2670 --VLASGDLPGQEFEWMrLDDDSVAaeIAAVPAGPItDAERLGEvtaaNLAYVIYTSGSTGRPKGVAVTHSGLANFARQE 2747
Cdd:PRK05691 2294 alFEALGELPAGVARWC-LEDDAAA--LAAYSDAPL-PFLSLPQ----HQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAV 2365
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2748 SDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGGEVLERFIAEHGATHTFLTPSV-------LSTMD 2820
Cdd:PRK05691 2366 IERFGMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYgsqlaqwLAGQG 2445
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2821 PTAvpSLRVIAAGGEAVP----QPIVDRWAPAtELHNLYGPTETtigITISSAMRPGDPVRLGG---PIGGV----DLMV 2889
Cdd:PRK05691 2446 EQL--PVRMCITGGEALTgehlQRIRQAFAPQ-LFFNAYGPTET---VVMPLACLAPEQLEEGAasvPIGRVvgarVAYI 2519
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2890 LDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRMYRTGDVVRWTPDtdtgGLtLEYTGRSDDQV 2969
Cdd:PRK05691 2520 LDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADGGRLYRTGDLVRLRAD----GL-VEYVGRIDHQV 2594
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2970 KLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIV-PVDGAVEVSE------LKAFAGGRLPAYMVPSSFTV 3042
Cdd:PRK05691 2595 KIRGFRIELGEIESRLLEHPAVREAVVLALDTPSGKQLAGYLVsAVAGQDDEAQaalreaLKAHLKQQLPDYMVPAHLIL 2674
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3043 IDELPLTPVGKLDKRALPEPVLEAG--EYVAPATGTERTIADVAAGVLNIDAglVSATSSFFELGGDSLSAARLAARlSD 3120
Cdd:PRK05691 2675 LDSLPLTANGKLDRRALPAPDPELNrqAYQAPRSELEQQLAQIWREVLNVER--VGLGDNFFELGGDSILSIQVVSR-AR 2751
|
1050 1060
....*....|....*....|....*...
gi 1827387616 3121 QLGVAVSVRDVFESGSIRALAETVGGSE 3148
Cdd:PRK05691 2752 QLGIHFSPRDLFQHQTVQTLAAVATHSE 2779
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1045-1533 |
1.62e-132 |
|
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: 425.97 E-value: 1.62e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1045 QRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADR 1124
Cdd:cd17655 6 QAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEER 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1125 IAYMLEDSGATVGITDASTRARL-GESSCEWVDLADLEAEaesgddiTDTERNGSVRLTNLAYLIYTSGSTGRPKAVGVS 1203
Cdd:cd17655 86 IQYILEDSGADILLTQSHLQPPIaFIGLIDLLDEDTIYHE-------ESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1204 HTGIVDFVNSLAKIttgTPEDEPDtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQAD-FAGDALATVLERDEVTDMII 1282
Cdd:cd17655 159 HRGVVNLVEWANKV---IYQGEHL-RVALFASISFDASVTEIFASLLSGNTLYIVRKETvLDGQALTQYIRQNRITIIDL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1283 TPSVLATVDPERAQY---VRNLATGGEACPPELVERWSER---GRRIFNCYGPTEATVWATRSRMTAGKP----VTIGKP 1352
Cdd:cd17655 235 TPAHLKLLDAADDSEglsLKHLIVGGEALSTELAKKIIELfgtNPTITNAYGPTETTVDASIYQYEPETDqqvsVPIGKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1353 VDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgEPGARMYATGDLVRVAKGGNLEFAGRAD 1432
Cdd:cd17655 315 LGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLPDGNIEFLGRID 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1433 HQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGgrkHTEVVAYLVAKPgaTIDSAAVLDEAAQHLAAHMVPSQAI 1512
Cdd:cd17655 394 HQVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQG---QNYLCAYIVSEK--ELPVAQLREFLARELPDYMIPSYFI 468
|
490 500
....*....|....*....|.
gi 1827387616 1513 VIDEIPLTPAGKLDRAALPEP 1533
Cdd:cd17655 469 KLDEIPLTPNGKVDRKALPEP 489
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
4-469 |
4.99e-132 |
|
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: 424.83 E-value: 4.99e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvtsdGE 83
Cdd:cd17651 24 AELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAERLAFMLADAGPVLVL----TH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 AEARSRFDDIVDVHVLDISSPGDADLDEEEFAgPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARD 163
Cdd:cd17651 100 PALAGELAVELVAVTLLDQPGAAAGADAEPDP-ALDADDLAYVIYTSGSTGRPKGVVMPHRSLANLVAWQARASSLGPGA 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 164 VFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLI 243
Cdd:cd17651 179 RTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEVRTDPPALAAWLDEQRISRVFLPTVALRALAEHGRPLGVRLAALRYL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 244 QTGGEALTP-PVARDLMVRLPGTRLQNQYGPAEASiVVTIHRVTQD----DRVIPIGTPTRRVSARVLDAALREVPIGVP 318
Cdd:cd17651 259 LTGGEQLVLtEDLREFCAGLPGLRLHNHYGPTETH-VVTALSLPGDpaawPAPPPIGRPIDNTRVYVLDAALRPVPPGVP 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 319 GELYLGGVQLARGYAGRPDLTAERFVADPFGePGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAA 398
Cdd:cd17651 338 GELYIGGAGLARGYLNRPELTAERFVPDPFV-PGARMYRTGDLARWLPDGELEFLGRADDQVKIRGFRIELGEIEAALAR 416
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 399 APGVLHAAAAVV-DGPGGQQLVGYLAPADVDVDTVAATTAEL---LPEYMRPSAWVRLDAMPLSRSGKVDRRLLP 469
Cdd:cd17651 417 HPGVREAVVLAReDRPGEKRLVAYVVGDPEAPVDAAELRAALathLPEYMVPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1064-1462 |
6.72e-131 |
|
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: 417.82 E-value: 6.72e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLAR-GVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDAS 1142
Cdd:TIGR01733 2 YRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDSA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1143 TRARLGESSCEWVDLADLEaEAESGDDITDTERNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTP 1222
Cdd:TIGR01733 82 LASRLAGLVLPVILLDPLE-LAALDDAPAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLARRYGLDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1223 EDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFAGDA--LATVLERDEVTDMIITPSVLATVDPERAQY--- 1297
Cdd:TIGR01733 161 DD----RVLQFASLSFDASVEEIFGALLAGATLVVPPEDEERDDAalLAALIAEHPVTVLNLTPSLLALLAAALPPAlas 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1298 VRNLATGGEACPPELVERWSER--GRRIFNCYGPTEATVWATRSRMTAG-----KPVTIGKPVDGFTVRVLDGRLHEVPQ 1370
Cdd:TIGR01733 237 LRLVILGGEALTPALVDRWRARgpGARLINLYGPTETTVWSTATLVDPDdapreSPVPIGRPLANTRLYVLDDDLRPVPV 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1371 GVVGELYLSTAGLARGYLGRPGQTAVSFVADPF-GEPGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEA 1449
Cdd:TIGR01733 317 GVVGELYIGGPGVARGYLNRPELTAERFVPDPFaGGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELGEIEA 396
|
410
....*....|...
gi 1827387616 1450 VLDAQPGVAQSVV 1462
Cdd:TIGR01733 397 ALLRHPGVREAVV 409
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
2569-3059 |
4.06e-129 |
|
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: 415.79 E-value: 4.06e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2569 ELFRAAARRAPDHVAVV--DGagaRLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPI 2646
Cdd:cd05918 3 DLIEERARSQPDAPAVCawDG---SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2647 DPDYPAERVASMIEDSGAVLglsVLASgdlpgqefewmrldddsvaaeiaavpagpitdaerlgevTAANLAYVIYTSGS 2726
Cdd:cd05918 80 DPSHPLQRLQEILQDTGAKV---VLTS---------------------------------------SPSDAAYVIFTSGS 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2727 TGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYrPSEAVGGEVLERFIAEHGA 2806
Cdd:cd05918 118 TGKPKGVVIEHRALSTSALAHGRALGLTSESRVLQFASYTFDVSILEIFTTLAAGGCLCI-PSEEDRLNDLAGFINRLRV 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2807 THTFLTPSVLSTMDPTAVPSLRVIAAGGEAVPQPIVDRWAPATELHNLYGPTETTIGITISSAMRPGDPVRLGGPIGGVd 2886
Cdd:cd05918 197 TWAFLTPSVARLLDPEDVPSLRTLVLGGEALTQSDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPLGAT- 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2887 LMVLDER--LRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANP------YGTAGQRMYRTGDVVRWTPDtdtGglT 2958
Cdd:cd05918 276 CWVVDPDnhDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqeGSGRGRRLYRTGDLVRYNPD---G--S 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2959 LEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV----GGSVATALAAYIVPVDGAVE--------------- 3019
Cdd:cd05918 351 LEYVGRKDTQVKIRGQRVELGEIEHHLRQSLPGAKEVVVEVvkpkDGSSSPQLVAFVVLDGSSSGsgdgdslflepsdef 430
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1827387616 3020 ---VSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05918 431 ralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1-469 |
1.14e-128 |
|
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: 412.80 E-value: 1.14e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvts 80
Cdd:cd17652 13 LTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYMLADARPALLL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeaearsrfddivdvhvldisspgdadldeeefagpTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd17652 90 -------------------------------------TTPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQIAAFDVG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEvlgagvGELTSL 240
Cdd:cd17652 133 PGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPGEPLADLLREHRITHVTLPPAALAALPP------DDLPDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 241 RLIQTGGEALTPPVARDLMvrlPGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIGVPGE 320
Cdd:cd17652 207 RTLVVAGEACPAELVDRWA---PGRRMINAYGPTETTVCATMAGPLPGGGVPPIGRPVPGTRVYVLDARLRPVPPGVPGE 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 321 LYLGGVQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAP 400
Cdd:cd17652 284 LYIAGAGLARGYLNRPGLTAERFVADPFGAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRIELGEVEAALTEHP 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 401 GVLHAAAAVV-DGPGGQQLVGYLAPADVDVDTVAATTAEL---LPEYMRPSAWVRLDAMPLSRSGKVDRRLLP 469
Cdd:cd17652 364 GVAEAVVVVRdDRPGDKRLVAYVVPAPGAAPTAAELRAHLaerLPGYMVPAAFVVLDALPLTPNGKLDRRALP 436
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
2579-3059 |
1.57e-125 |
|
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: 404.38 E-value: 1.57e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2579 PDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASM 2658
Cdd:cd17643 1 PEAVAVVDE-DRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2659 IEDSGAVLGLsvlasgdlpgqefewmrldddsvaaeiaavpagpitdaerlgeVTAANLAYVIYTSGSTGRPKGVAVTHS 2738
Cdd:cd17643 80 LADSGPSLLL-------------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2739 GLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSE-AVGGEVLERFIAEHGATHTFLTPSVLS 2817
Cdd:cd17643 117 NVLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEvARSPEDFARLLRDEGVTVLNQTPSAFY 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2818 TM------DPTAVPSLRVIAAGGEAVPQPIVDRWA-----PATELHNLYGPTETTIGITI----SSAMRPGDPVRLGGPI 2882
Cdd:cd17643 197 QLveaadrDGRDPLALRYVIFGGEALEAAMLRPWAgrfglDRPQLVNMYGITETTVHVTFrpldAADLPAAAASPIGRPL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2883 GGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRMYRTGDVVRWTPDTDtggltLEYT 2962
Cdd:cd17643 277 PGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGE-----LEYL 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2963 GRSDDQVKLRGLRIELGEIEAVLAEHDAV-ESAVVLGVGGSVATALAAYIVPVDGAVEV-SELKAFAGGRLPAYMVPSSF 3040
Cdd:cd17643 352 GRADEQVKIRGFRIELGEIEAALATHPSVrDAAVIVREDEPGDTRLVAYVVADDGAAADiAELRALLKELLPDYMVPARY 431
|
490
....*....|....*....
gi 1827387616 3041 TVIDELPLTPVGKLDKRAL 3059
Cdd:cd17643 432 VPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1044-1531 |
6.72e-125 |
|
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: 404.03 E-value: 6.72e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1044 AQRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPAD 1123
Cdd:cd17651 3 RQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYPAE 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1124 RIAYMLEDSGATVGITDASTRARLGEsscewVDLADLEAEAESGDDITDTERNGSVRLTNLAYLIYTSGSTGRPKAVGVS 1203
Cdd:cd17651 83 RLAFMLADAGPVLVLTHPALAGELAV-----ELVAVTLLDQPGAAAGADAEPDPALDADDLAYVIYTSGSTGRPKGVVMP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1204 HTGIVDFVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAP---QADFAgdALATVLERDEVTdM 1280
Cdd:cd17651 158 HRSLANLVAWQARASSLGPGA----RTLQFAGLGFDVSVQEIFSTLCAGATLVLPPeevRTDPP--ALAAWLDEQRIS-R 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1281 IITPSVL-------ATVDPERAQYVRNLATGGEACPP-ELVERW--SERGRRIFNCYGPTEATV----WATRSRMTAGKP 1346
Cdd:cd17651 231 VFLPTVAlralaehGRPLGVRLAALRYLLTGGEQLVLtEDLREFcaGLPGLRLHNHYGPTETHVvtalSLPGDPAAWPAP 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1347 VTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGePGARMYATGDLVRVAKGGNLE 1426
Cdd:cd17651 311 PPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFV-PGARMYRTGDLARWLPDGELE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1427 FAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATIDSAAVLDEAAQHLAAHM 1506
Cdd:cd17651 390 FLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKR---LVAYVVGDPEAPVDAAELRAALATHLPEYM 466
|
490 500
....*....|....*....|....*
gi 1827387616 1507 VPSQAIVIDEIPLTPAGKLDRAALP 1531
Cdd:cd17651 467 VPSAFVLLDALPLTPNGKLDRRALP 491
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1-994 |
9.73e-125 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 444.61 E-value: 9.73e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvtS 80
Cdd:PRK05691 2214 LSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGLLL--S 2291
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEA-EARSRFDDIVDVHVLDISSPGDADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDL 159
Cdd:PRK05691 2292 DRALfEALGELPAGVARWCLEDDAAALAAYSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERFGM 2371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 160 TARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHgDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLgAGVGELTS 239
Cdd:PRK05691 2372 RADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQW-GAEEICQLIREQQVSILGFTPSYGSQLAQWL-AGQGEQLP 2449
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 240 LRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEaSIVVTI-----HRVTQDDRVIPIGtptRRVSARV---LDAALR 311
Cdd:PRK05691 2450 VRMCITGGEALTGEHLQRIRQAFAPQLFFNAYGPTE-TVVMPLaclapEQLEEGAASVPIG---RVVGARVayiLDADLA 2525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 312 EVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGE 391
Cdd:PRK05691 2526 LVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAADGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGE 2605
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 392 VEAALAAAPGVLHAAAAVVDGPGGQQLVGYLAPADVDVDTVA------ATTAEL---LPEYMRPSAWVRLDAMPLSRSGK 462
Cdd:PRK05691 2606 IESRLLEHPAVREAVVLALDTPSGKQLAGYLVSAVAGQDDEAqaalreALKAHLkqqLPDYMVPAHLILLDSLPLTANGK 2685
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 463 VDRRLL--PEPEIAPTLYVPPGNADEETVAGLFAELLGVERVGVTDSFFDIGGSSLSAARIAARvSKELGVDVSVRDVFE 540
Cdd:PRK05691 2686 LDRRALpaPDPELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSR-ARQLGIHFSPRDLFQ 2764
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 541 SPSVRGLvhAVSGRGSALPSVKRiEPRPERLPLSRAQRrmWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVER 620
Cdd:PRK05691 2765 HQTVQTL--AAVATHSEAAQAEQ-GPLQGASGLTPIQH--WFFDSPVPQPQHWNQALLLEPRQALDPALLEQALQALVEH 2839
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 621 HEVLRTVYPSVGAAPVQDVLPvaVAREQLDWR----EADSVESLVRSTTEGFDVSTQMPLRGRFHRDGAGLH-VALTMHH 695
Cdd:PRK05691 2840 HDALRLRFSQADGRWQAEYRA--VTAQELLWQvtvaDFAECAALFADAQRSLDLQQGPLLRALLVDGPQGQQrLLLAIHH 2917
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 696 IAMDGQSIPVLARDLMSAYAARAEGRTGGLPVLDVQYADYALWQQSVLGdaddeTSVLGEQLSHWRRVLAGLPAvtDLPM 775
Cdd:PRK05691 2918 LVVDGVSWRVLLEDLQALYRQLSAGAEPALPAKTSAFRDWAARLQAYAG-----SESLREELGWWQAQLGGPRA--ELPC 2990
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 776 DRPRPAVLGTAGATVTVEFDddlADRVDVL------ARSNTMTGFMVTeaAFAATVARLASTTDVVIGTPVAGR----ND 845
Cdd:PRK05691 2991 DRPQGGNLNRHAQTVSVRLD---AERTRQLlqqapaAYRTQVNDLLLT--ALARVLCRWSGQPSVLVQLEGHGRealfDD 3065
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 846 PALEELIGMFVNTLLLRTQ------VDPGHSVGDLLGNVRTT--------VLDAFANDQVQfdELIEALaperssshqPL 911
Cdd:PRK05691 3066 IDLTRSVGWFTSAYPLRLTpapgddAARGESIKAIKEQLRAVphkglgygVLRYLADAAVR--EAMAAL---------PQ 3134
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 912 AQIAFTYTEPTVN--DVAGL-----EASGIQAAPvdtgvvNAKFDLTVAVRARSGGTPMAADFIYATDLFDESTVKRFAE 984
Cdd:PRK05691 3135 APITFNYLGQFDQsfASDALfrpldEPAGPAHDP------DAPLPNELSVDGQVYGGELVLRWTYSAERYDEQTIAELAE 3208
|
1050
....*....|
gi 1827387616 985 VYRRVLQAIV 994
Cdd:PRK05691 3209 AYLAELQALI 3218
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
2579-3060 |
4.81e-124 |
|
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: 399.82 E-value: 4.81e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2579 PDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASM 2658
Cdd:cd17649 1 PDAVALVFG-DQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2659 IEDSGAVLGLSVlasgdlpgqefewmrldddsvaaeiaavpagpitdaerlgevTAANLAYVIYTSGSTGRPKGVAVTHS 2738
Cdd:cd17649 80 LEDSGAGLLLTH------------------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2739 GLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGG-EVLERFIAEHGATHTFLTPSVLS 2817
Cdd:cd17649 118 PLAAHCQATAERYGLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASaDELAEMVRELGVTVLDLPPAYLQ 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2818 TM-------DPTAVPSLRVIAAGGEAVPQPIVDRWAPATE-LHNLYGPTETTIGITI----SSAMRPGDPVRLGGPIGGV 2885
Cdd:cd17649 198 QLaeeadrtGDGRPPSLRLYIFGGEALSPELLRRWLKAPVrLFNAYGPTEATVTPLVwkceAGAARAGASMPIGRPLGGR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2886 DLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRMYRTGDVVRWTPDTdtgglTLEYTGRS 2965
Cdd:cd17649 278 SAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDG-----VIEYLGRV 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2966 DDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPVDGAVE---VSELKAFAGGRLPAYMVPSSFTV 3042
Cdd:cd17649 353 DHQVKIRGFRIELGEIEAALLEHPGVREAAVVALDGAGGKQLVAYVVLRAAAAQpelRAQLRTALRASLPDYMVPAHLVF 432
|
490
....*....|....*...
gi 1827387616 3043 IDELPLTPVGKLDKRALP 3060
Cdd:cd17649 433 LARLPLTPNGKLDRKALP 450
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1050-1531 |
8.08e-123 |
|
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: 396.35 E-value: 8.08e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITdastrarlgesscewvdladleaeaESGDditdterngsvrltNLAYLIYTSGSTGRPKAVGVSHTGIVD 1209
Cdd:cd17649 81 EDSGAGLLLT-------------------------HHPR--------------QLAYVIYTSGSTGTPKGVAVSHGPLAA 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 FVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFAG-DALATVLERDEVTDMIITPS--- 1285
Cdd:cd17649 122 HCQATAERYGLTPGD----RELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASaDELAEMVRELGVTVLDLPPAylq 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1286 ----VLATVDPERAQYVRNLATGGEACPPELVERWSERGRRIFNCYGPTEATV----WATRSRMTAGKP-VTIGKPVDGF 1356
Cdd:cd17649 198 qlaeEADRTGDGRPPSLRLYIFGGEALSPELLRRWLKAPVRLFNAYGPTEATVtplvWKCEAGAARAGAsMPIGRPLGGR 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1357 TVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEPGARMYATGDLVRVAKGGNLEFAGRADHQVK 1436
Cdd:cd17649 278 SAYILDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFGAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVK 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1437 INGQRVELGEIEAVLDAQPGVAQSVVVgVESTRGGrkhTEVVAYLVAKPGATidSAAVLDEAAQHLAA----HMVPSQAI 1512
Cdd:cd17649 358 IRGFRIELGEIEAALLEHPGVREAAVV-ALDGAGG---KQLVAYVVLRAAAA--QPELRAQLRTALRAslpdYMVPAHLV 431
|
490
....*....|....*....
gi 1827387616 1513 VIDEIPLTPAGKLDRAALP 1531
Cdd:cd17649 432 FLARLPLTPNGKLDRKALP 450
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
570-997 |
1.42e-122 |
|
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: 395.09 E-value: 1.42e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 570 RLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDVLPVAVAREQL 649
Cdd:cd19538 1 EIPLSFAQRRLWFLHQLEGPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 650 DWREAD--SVESLVRSTTE-GFDVSTQMPLRGRFHRDGAGLHVA-LTMHHIAMDGQSIPVLARDLMSAYAARAEGRTGGL 725
Cdd:cd19538 81 EIKEVDeeELESEINEAVRyPFDLSEEPPFRATLFELGENEHVLlLLLHHIAADGWSLAPLTRDLSKAYRARCKGEAPEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 726 PVLDVQYADYALWQQSVLGDADDETSVLGEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVEFDDDLADRVDVL 805
Cdd:cd19538 161 APLPVQYADYALWQQELLGDESDPDSLIARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 806 ARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQV--DPghSVGDLLGNVRTTVL 883
Cdd:cd19538 241 AKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTsgNP--SFRELLERVKETNL 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 884 DAFANDQVQFDELIEALAPERSSSHQPLAQIAFTYT---EPtvndvaGLEASGIQAAPVDTGVVNAKFDLTVAVRARSG- 959
Cdd:cd19538 319 EAYEHQDIPFERLVEALNPTRSRSRHPLFQIMLALQntpQP------SLDLPGLEAKLELRTVGSAKFDLTFELREQYNd 392
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1827387616 960 GTP--MAADFIYATDLFDESTVKRFAEVYRRVLQAIVDDQ 997
Cdd:cd19538 393 GTPngIEGFIEYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1-468 |
1.68e-120 |
|
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: 389.75 E-value: 1.68e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvts 80
Cdd:cd17643 13 LTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFILADSGPSLLL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeaearsrfddivdvhvldisspgdadldeeefagpTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd17643 90 -------------------------------------TDPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAATQRWFGFN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSL 240
Cdd:cd17643 133 EDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEVARSPEDFARLLRDEGVTVLNQTPSAFYQLVEAADRDGRDPLAL 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 241 RLIQTGGEALTPPVARDLMVR--LPGTRLQNQYGPAEASIVVTIHRVTQDD----RVIPIGTPTRRVSARVLDAALREVP 314
Cdd:cd17643 213 RYVIFGGEALEAAMLRPWAGRfgLDRPQLVNMYGITETTVHVTFRPLDAADlpaaAASPIGRPLPGLRVYVLDADGRPVP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 315 IGVPGELYLGGVQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEA 394
Cdd:cd17643 293 PGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADEQVKIRGFRIELGEIEA 372
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 395 ALAAAPGVLHAAAAV-VDGPGGQQLVGYLAPAD---VDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd17643 373 ALATHPSVRDAAVIVrEDEPGDTRLVAYVVADDgaaADIAELRALLKELLPDYMVPARYVPLDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
2569-3059 |
1.07e-119 |
|
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: 386.66 E-value: 1.07e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2569 ELFRAAARRAPDHVAVvDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDP 2648
Cdd:cd17653 1 DAFERIAAAHPDAVAV-ESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2649 DYPAERVASMIEDSGAVLGLSvLASGDlpgqefewmrldddsvaaeiaavpagpitdaerlgevtaaNLAYVIYTSGSTG 2728
Cdd:cd17653 80 KLPSARIQAILRTSGATLLLT-TDSPD----------------------------------------DLAYIIFTSGSTG 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2729 RPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEavggEVLERFIAEHGATH 2808
Cdd:cd17653 119 IPKGVMVPHRGVLNYVSQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADPS----DPFAHVARTVDALM 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2809 tfLTPSVLSTMDPTAVPSLRVIAAGGEAVPQPIVDRWAPATELHNLYGPTETTIGITISSaMRPGDPVRLGGPIGGVDLM 2888
Cdd:cd17653 195 --STPSILSTLSPQDFPNLKTIFLGGEAVPPSLLDRWSPGRRLYNAYGPTECTISSTMTE-LLPGQPVTIGKPIPNSTCY 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2889 VLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTaGQRMYRTGDVVRWTPDtdtGGltLEYTGRSDDQ 2968
Cdd:cd17653 272 ILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWP-GSRMYRTGDYGRWTED---GG--LEFLGREDNQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2969 VKLRGLRIELGEIEA-VLAEHDAVESAVVLGVGGSvataLAAYIVPVDgaVEVSELKAFAGGRLPAYMVPSSFTVIDELP 3047
Cdd:cd17653 346 VKVRGFRINLEEIEEvVLQSQPEVTQAAAIVVNGR----LVAFVTPET--VDVDGLRSELAKHLPSYAVPDRIIALDSFP 419
|
490
....*....|..
gi 1827387616 3048 LTPVGKLDKRAL 3059
Cdd:cd17653 420 LTANGKVDRKAL 431
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
2567-3059 |
2.24e-119 |
|
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: 386.29 E-value: 2.24e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2567 LAELFRAAARRAPDHVAVVDGAGaRLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPI 2646
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDE-SLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2647 DPDYPAERVASMIEDSGAVLGLsvlasgdlpgqefewmrldddsvaaeiaavpagpitdaerlgeVTAANLAYVIYTSGS 2726
Cdd:cd12115 80 DPAYPPERLRFILEDAQARLVL-------------------------------------------TDPDDLAYVIYTSGS 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2727 TGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLlatvneGTLAyrpseaVGGEV--------LE 2798
Cdd:cd12115 117 TGRPKGVAIEHRNAAAFLQWAAAAFSAEELAGVLASTSICFDLSVFELF------GPLA------TGGKVvladnvlaLP 184
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2799 RFIAEHGATHTFLTPSVLSTM-DPTAVP-SLRVIAAGGEAVPQPIVDRW---APATELHNLYGPTETTIGITiSSAMRPG 2873
Cdd:cd12115 185 DLPAAAEVTLINTVPSAAAELlRHDALPaSVRVVNLAGEPLPRDLVQRLyarLQVERVVNLYGPSEDTTYST-VAPVPPG 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2874 D--PVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGtAGQRMYRTGDVVRWTPD 2951
Cdd:cd12115 264 AsgEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG-PGARLYRTGDLVRWRPD 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2952 tdtgGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVAT-ALAAYIVPVDG-AVEVSELKAFAGG 3029
Cdd:cd12115 343 ----GL-LEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGErRLVAYIVAEPGaAGLVEDLRRHLGT 417
|
490 500 510
....*....|....*....|....*....|
gi 1827387616 3030 RLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd12115 418 RLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
5-472 |
1.17e-117 |
|
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: 383.22 E-value: 1.17e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 5 EFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvtSDGEA 84
Cdd:cd17655 27 ELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDYPEERIQYILEDSGADILL--TQSHL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 85 EARSRF-DDIVDVHVLDISSPGDADLdeeefAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARD 163
Cdd:cd17655 105 QPPIAFiGLIDLLDEDTIYHEESENL-----EPVSKSDDLAYVIYTSGSTGKPKGVMIEHRGVVNLVEWANKVIYQGEHL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 164 VFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLaafNEVLGAGVGELTSLRLI 243
Cdd:cd17655 180 RVALFASISFDASVTEIFASLLSGNTLYIVRKETVLDGQALTQYIRQNRITIIDLTPAHL---KLLDAADDSEGLSLKHL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 244 QTGGEALTPPVARDLMVRL-PGTRLQNQYGPAEASIVVTIHRVTQDDRV---IPIGTPTRRVSARVLDAALREVPIGVPG 319
Cdd:cd17655 257 IVGGEALSTELAKKIIELFgTNPTITNAYGPTETTVDASIYQYEPETDQqvsVPIGKPLGNTRIYILDQYGRPQPVGVAG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 320 ELYLGGVQLARGYAGRPDLTAERFVADPFgEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAA 399
Cdd:cd17655 337 ELYIGGEGVARGYLNRPELTAEKFVDDPF-VPGERMYRTGDLARWLPDGNIEFLGRIDHQVKIRGYRIELGEIEARLLQH 415
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 400 PGVLHAAAAVV-DGPGGQQLVGYLAP-ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEPE 472
Cdd:cd17655 416 PDIKEAVVIARkDEQGQNYLCAYIVSeKELPVAQLREFLARELPDYMIPSYFIKLDEIPLTPNGKVDRKALPEPD 490
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
2566-3060 |
1.48e-117 |
|
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: 381.78 E-value: 1.48e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDgAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVP 2645
Cdd:cd17644 1 CIHQLFEEQVERTPDAVAVVF-EDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2646 IDPDYPAERVASMIEDSGavlgLSVLasgdlpgqefewmrldddsvaaeiaavpagpITDAErlgevtaaNLAYVIYTSG 2725
Cdd:cd17644 80 LDPNYPQERLTYILEDAQ----ISVL-------------------------------LTQPE--------NLAYVIYTSG 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2726 STGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAV-GGEVLERFIAEH 2804
Cdd:cd17644 117 STGKPKGVMIEHQSLVNLSHGLIKEYGITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRsSLEDFVQYIQQW 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2805 GATHTFLTPS-------VLSTMDPTAVPSLRVIAAGGEAVPQPIVDRWAPAT----ELHNLYGPTETTIGITISSAMRPG 2873
Cdd:cd17644 197 QLTVLSLPPAywhllvlELLLSTIDLPSSLRLVIVGGEAVQPELVRQWQKNVgnfiQLINVYGPTEATIAATVCRLTQLT 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2874 DP----VRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPY-GTAGQRMYRTGDVVRW 2948
Cdd:cd17644 277 ERnitsVPIGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARY 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2949 TPDTDtggltLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATA-LAAYIVP-VDGAVEVSELKAF 3026
Cdd:cd17644 357 LPDGN-----IEYLGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKrLVAYIVPhYEESPSTVELRQF 431
|
490 500 510
....*....|....*....|....*....|....
gi 1827387616 3027 AGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALP 3060
Cdd:cd17644 432 LKAKLPDYMIPSAFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1050-1530 |
6.96e-117 |
|
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: 380.73 E-value: 6.96e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPAlIC--DGtEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAY 1127
Cdd:cd05918 13 PDAPA-VCawDG-SLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1128 MLEDSGATVGITDastrarlgesscewvdladleaeaesgdditdterngsvRLTNLAYLIYTSGSTGRPKAVGVSHTGI 1207
Cdd:cd05918 91 ILQDTGAKVVLTS---------------------------------------SPSDAAYVIFTSGSTGKPKGVVIEHRAL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1208 VDFVNSLAKITTGTPedepDTRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFAGDaLATVLERDEVTDMIITPSVL 1287
Cdd:cd05918 132 STSALAHGRALGLTS----ESRVLQFASYTFDVSILEIFTTLAAGGCLCIPSEEDRLND-LAGFINRLRVTWAFLTPSVA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1288 ATVDPERAQYVRNLATGGEACPPELVERWSERgRRIFNCYGPTEATVWATRSRMTAG-KPVTIGKPVDGfTVRVLDGRLH 1366
Cdd:cd05918 207 RLLDPEDVPSLRTLVLGGEALTQSDVDTWADR-VRLINAYGPAECTIAATVSPVVPStDPRNIGRPLGA-TCWVVDPDNH 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1367 E--VPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPF------GEPGARMYATGDLVRVAKGGNLEFAGRADHQVKIN 1438
Cdd:cd05918 285 DrlVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIR 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1439 GQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKHTEVVAYLVAKPGATIDS-----------------AAVLDEAAQH 1501
Cdd:cd05918 365 GQRVELGEIEHHLRQSLPGAKEVVVEVVKPKDGSSSPQLVAFVVLDGSSSGSGdgdslflepsdefralvAELRSKLRQR 444
|
490 500
....*....|....*....|....*....
gi 1827387616 1502 LAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd05918 445 LPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1-468 |
6.99e-117 |
|
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: 380.46 E-value: 6.99e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:cd12114 13 LTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAILADAGARLVLTDG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRFDDIVDVHVLDISSPgdadldeEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd12114 93 PDAQLDVAVFDVLILDLDALAAPA-------PPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDINRRFAVG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSL 240
Cdd:cd12114 166 PDDRVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDVLEAAQALLPSL 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 241 RLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASI---VVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIGV 317
Cdd:cd12114 246 RLVLLSGDWIPLDLPARLRALAPDARLISLGGATEASIwsiYHPIDEVPPDWRSIPYGRPLANQRYRVLDPRGRDCPDWV 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 318 PGELYLGGVQLARGYAGRPDLTAERFVADPfgePGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALA 397
Cdd:cd12114 326 PGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGRRDGQVKVRGYRIELGEIEAALQ 402
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 398 AAPGVLHAAAAVVDGPGGQQLVGYLAPAD----VDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd12114 403 AHPGVARAVVVVLGDPGGKRLAAFVVPDNdgtpIAPDALRAFLAQTLPAYMIPSRVIALEALPLTANGKVDRAAL 477
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1050-1530 |
1.40e-116 |
|
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: 378.57 E-value: 1.40e-116
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDAStrarlgesscewvdladleaeaesgdditdterngsvrltNLAYLIYTSGSTGRPKAVGVSHTGivd 1209
Cdd:cd17643 81 ADSGPSLLLTDPD----------------------------------------DLAYVIYTSGSTGRPKGVVVSHAN--- 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 fVNSLAKITTGTPEDEPDTRILHVASPSFDASMFEMAWAIPAGHTLVIAPQA-DFAGDALATVLERDEVTDMIITPS--- 1285
Cdd:cd17643 118 -VLALFAATQRWFGFNEDDVWTLFHSYAFDFSVWEIWGALLHGGRLVVVPYEvARSPEDFARLLRDEGVTVLNQTPSafy 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1286 VLATVDPERAQYVRNLAT---GGEACPPELVERWSER----GRRIFNCYGPTEATVWATRSRMTA-----GKPVTIGKPV 1353
Cdd:cd17643 197 QLVEAADRDGRDPLALRYvifGGEALEAAMLRPWAGRfgldRPQLVNMYGITETTVHVTFRPLDAadlpaAAASPIGRPL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1354 DGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEPGARMYATGDLVRVAKGGNLEFAGRADH 1433
Cdd:cd17643 277 PGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGPGSRMYRTGDLARRLPDGELEYLGRADE 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1434 QVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhTEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIV 1513
Cdd:cd17643 357 QVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGD---TRLVAYVVADDGAAADIAELRALLKELLPDYMVPARYVP 433
|
490
....*....|....*..
gi 1827387616 1514 IDEIPLTPAGKLDRAAL 1530
Cdd:cd17643 434 LDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1050-1530 |
2.31e-115 |
|
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: 374.34 E-value: 2.31e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd17653 11 PDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAIL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDAStrarlgesscewvdladleaeaesGDDitdterngsvrltnLAYLIYTSGSTGRPKAVGVSHTGIVD 1209
Cdd:cd17653 91 RTSGATLLLTTDS------------------------PDD--------------LAYIIFTSGSTGIPKGVMVPHRGVLN 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 FV-NSLAKITTGtpedePDTRILHVASPSFDASMFEMAWAIPAGHTLVIA-PQADFAGDAlatvlerDEVTDMIITPSVL 1287
Cdd:cd17653 133 YVsQPPARLDVG-----PGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLAdPSDPFAHVA-------RTVDALMSTPSIL 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1288 ATVDPERAQYVRNLATGGEACPPELVERWSErGRRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHE 1367
Cdd:cd17653 201 STLSPQDFPNLKTIFLGGEAVPPSLLDRWSP-GRRLYNAYGPTECTISSTMTELLPGQPVTIGKPIPNSTCYILDADLQP 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1368 VPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgEPGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEI 1447
Cdd:cd17653 280 VPEGVVGEICISGVQVARGYLGNPALTASKFVPDPF-WPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1448 EA-VLDAQPGVAQSVVVGVESTrggrkhteVVAYLVAkpgATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLD 1526
Cdd:cd17653 359 EEvVLQSQPEVTQAAAIVVNGR--------LVAFVTP---ETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVD 427
|
....
gi 1827387616 1527 RAAL 1530
Cdd:cd17653 428 RKAL 431
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1042-1530 |
5.99e-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: 373.58 E-value: 5.99e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1042 VLAQRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYP 1121
Cdd:cd12115 5 VEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1122 ADRIAYMLEDSGATVGITDAstrarlgesscewvdladleaeaesgdditdterngsvrlTNLAYLIYTSGSTGRPKAVG 1201
Cdd:cd12115 85 PERLRFILEDAQARLVLTDP----------------------------------------DDLAYVIYTSGSTGRPKGVA 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1202 VSHTGIVDFVNSLAKITTGtpedEPDTRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFAGDALAtvleRDEVTDMI 1281
Cdd:cd12115 125 IEHRNAAAFLQWAAAAFSA----EELAGVLASTSICFDLSVFELFGPLATGGKVVLADNVLALPDLPA----AAEVTLIN 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1282 ITPSVLAT-----VDPERAQYVrNLAtgGEACPPELVERWSER--GRRIFNCYGPTEATVWATRSRMTAG--KPVTIGKP 1352
Cdd:cd12115 197 TVPSAAAEllrhdALPASVRVV-NLA--GEPLPRDLVQRLYARlqVERVVNLYGPSEDTTYSTVAPVPPGasGEVSIGRP 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1353 VDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGePGARMYATGDLVRVAKGGNLEFAGRAD 1432
Cdd:cd12115 274 LANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFG-PGARLYRTGDLVRWRPDGLLEFLGRAD 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1433 HQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAI 1512
Cdd:cd12115 353 NQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERR---LVAYIVAEPGAAGLVEDLRRHLGTRLPAYMVPSRFV 429
|
490
....*....|....*...
gi 1827387616 1513 VIDEIPLTPAGKLDRAAL 1530
Cdd:cd12115 430 RLDALPLTPNGKIDRSAL 447
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
2106-2535 |
9.01e-114 |
|
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: 369.22 E-value: 9.01e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2106 VWPMTPLQQGLFFQADLantvaDHDAiDVYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPSGAAVTVVPAE 2185
Cdd:cd19543 1 IYPLSPMQEGMLFHSLL-----DPGS-GAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQVVLKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2186 VTVPWSVIDLRAEDAASLDSRVEEVLATERTNPFDMAKPPLIRVVLVEHGDGA-ELVVTNHHLLIDGWSSPLVLADLLSL 2264
Cdd:cd19543 75 RKLPWRELDLSHLSEAEQEAELEALAEEDRERGFDLARAPLMRLTLIRLGDDRyRLVWSFHHILLDGWSLPILLKELFAI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2265 Y-ATGQTFTGSLPGTsgRDFADHARAVATADVEAGIAAWREVLAPVTEPTLVAPGHEPSADAP--PRDHQFSIDVKVTER 2341
Cdd:cd19543 155 YaALGEGQPPSLPPV--RPYRDYIAWLQRQDKEAAEAYWREYLAGFEEPTPLPKELPADADGSyePGEVSFELSAELTAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2342 LEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRSPDIEGMESMVGMFINTIPAVVDVNPDATVVDVLTAVQ 2421
Cdd:cd19543 233 LQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAELPGIETMVGLFINTLPVRVRLDPDQTVLELLKDLQ 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2422 NDKVKVLDHQQIGLPRLVAQTGLP-ALFDTLAVYESFPVnVDSVAGIDasSAGGLKLVGAKTSDATHYPLNLSASrRGAE 2500
Cdd:cd19543 313 AQQLELREHEYVPLYEIQAWSEGKqALFDHLLVFENYPV-DESLEEEQ--DEDGLRITDVSAEEQTNYPLTVVAI-PGEE 388
|
410 420 430
....*....|....*....|....*....|....*
gi 1827387616 2501 LALKLKYLPTAFAPEQVAVFADVLTGLLGAIADHP 2535
Cdd:cd19543 389 LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1-468 |
1.20e-113 |
|
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: 369.72 E-value: 1.20e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvts 80
Cdd:cd12115 25 LTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPAYPPERLRFILEDAQARLVL--- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeaearsrfddivdvhvldisspgdadldeeefagpTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd12115 102 -------------------------------------TDPDDLAYVIYTSGSTGRPKGVAIEHRNAAAFLQWAAAAFSAE 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEpgrhgDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAgvgeLTSL 240
Cdd:cd12115 145 ELAGVLASTSICFDLSVFELFGPLATGGKVVLAD-----NVLALPDLPAAAEVTLINTVPSAAAELLRHDAL----PASV 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 241 RLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVT-QDDRVIPIGTPTRRVSARVLDAALREVPIGVPG 319
Cdd:cd12115 216 RVVNLAGEPLPRDLVQRLYARLQVERVVNLYGPSEDTTYSTVAPVPpGASGEVSIGRPLANTQAYVLDRALQPVPLGVPG 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 320 ELYLGGVQLARGYAGRPDLTAERFVADPFGePGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAA 399
Cdd:cd12115 296 ELYIGGAGVARGYLGRPGLTAERFLPDPFG-PGARLYRTGDLVRWRPDGLLEFLGRADNQVKVRGFRIELGEIEAALRSI 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 400 PGVlHAAAAVV--DGPGGQQLVGYL---APADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd12115 375 PGV-REAVVVAigDAAGERRLVAYIvaePGAAGLVEDLRRHLGTRLPAYMVPSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
2579-3060 |
2.77e-113 |
|
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: 369.04 E-value: 2.77e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2579 PDHVAVVDGAgARLTYRELDEASDRLARWLIGRGVG-PERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVAS 2657
Cdd:cd17648 1 PDRVAVVYGD-KRLTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2658 MIEDSGAVLglsVLAsgdlpgqefewmrldddsvaaeiaavpagpitdaerlgevTAANLAYVIYTSGSTGRPKGVAVTH 2737
Cdd:cd17648 80 ILEDTGARV---VIT----------------------------------------NSTDLAYAIYTSGTTGKPKGVLVEH 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2738 SGLANFARQESDR--LNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGG-EVLERFIAEHGATHTFLTPS 2814
Cdd:cd17648 117 GSVVNLRTSLSERyfGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDpDRFYAYINREKVTYLSGTPS 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2815 VLSTMDPTAVPSLRVIAAGGEAVPQPIVD--RWAPATELHNLYGPTETTIgITISSAMRPGDPVR--LGGPIGGVDLMVL 2890
Cdd:cd17648 197 VLQQYDLARLPHLKRVDAAGEEFTAPVFEklRSRFAGLIINAYGPTETTV-TNHKRFFPGDQRFDksLGRPVRNTKCYVL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2891 DERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQ-------RMYRTGDVVRWTPDTDtggltLEYTG 2963
Cdd:cd17648 276 NDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQErargrnaRLYKTGDLVRWLPSGE-----LEYLG 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2964 RSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVL------GVGGSVATALAAYIVPVDGAVEVSELKAFAGGRLPAYMVP 3037
Cdd:cd17648 351 RNDFQVKIRGQRIEPGEVEAALASYPGVRECAVVakedasQAQSRIQKYLVGYYLPEPGHVPESDLLSFLRAKLPRYMVP 430
|
490 500
....*....|....*....|...
gi 1827387616 3038 SSFTVIDELPLTPVGKLDKRALP 3060
Cdd:cd17648 431 ARLVRLEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
2579-3060 |
1.86e-112 |
|
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: 367.95 E-value: 1.86e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2579 PDHVAVVDGAgARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASM 2658
Cdd:cd17656 2 PDAVAVVFEN-QKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2659 IEDSGAVLGLSVLASGDLPGQEFEWMRLDDDSVAAEiaavpagpitDAERLGEVTAAN-LAYVIYTSGSTGRPKGVAVTH 2737
Cdd:cd17656 81 MLDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQE----------DTSNIDYINNSDdLLYIIYTSGTTGKPKGVQLEH 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2738 SGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLaYRPSEAVGGEV--LERFIAEHGATHTFLTPSV 2815
Cdd:cd17656 151 KNMVNLLHFEREKTNINFSDKVLQFATCSFDVCYQEIFSTLLSGGTL-YIIREETKRDVeqLFDLVKRHNIEVVFLPVAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2816 LSTM--DPTAVPSL-----RVIAAGGE-AVPQPIVDRW-APATELHNLYGPTETTIGITISsaMRPGDPVRL----GGPI 2882
Cdd:cd17656 230 LKFIfsEREFINRFptcvkHIITAGEQlVITNEFKEMLhEHNVHLHNHYGPSETHVVTTYT--INPEAEIPElppiGKPI 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2883 GGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYgTAGQRMYRTGDVVRWTPDTDtggltLEYT 2962
Cdd:cd17656 308 SNTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGN-----IEFL 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2963 GRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATA-LAAYIVPVDgAVEVSELKAFAGGRLPAYMVPSSFT 3041
Cdd:cd17656 382 GRADHQVKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKyLCAYFVMEQ-ELNISQLREYLAKQLPEYMIPSFFV 460
|
490
....*....|....*....
gi 1827387616 3042 VIDELPLTPVGKLDKRALP 3060
Cdd:cd17656 461 PLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1-468 |
1.63e-110 |
|
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: 362.25 E-value: 1.63e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:cd05918 25 LTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPSHPLQRLQEILQDTGAKVVLTSS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeaearsrfddivdvhvldisspgdadldeeefagptrPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd05918 105 ---------------------------------------PSDAAYVIFTSGSTGKPKGVVIEHRALSTSALAHGRALGLT 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIA-EPGRHGDpvhLADLIRRHGVTVIHFVPAMLAAFNEvlgagvGELTS 239
Cdd:cd05918 146 SESRVLQFASYTFDVSILEIFTTLAAGGCLCIPsEEDRLND---LAGFINRLRVTWAFLTPSVARLLDP------EDVPS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 240 LRLIQTGGEALTPpvaRDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTrRVSARVLDAA--LREVPIGV 317
Cdd:cd05918 217 LRTLVLGGEALTQ---SDVDTWADRVRLINAYGPAECTIAATVSPVVPSTDPRNIGRPL-GATCWVVDPDnhDRLVPIGA 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 318 PGELYLGGVQLARGYAGRPDLTAERFVADPF------GEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGE 391
Cdd:cd05918 293 VGELLIEGPILARGYLNDPEKTAAAFIEDPAwlkqegSGRGRRLYRTGDLVRYNPDGSLEYVGRKDTQVKIRGQRVELGE 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 392 VEAALAAAPGVLHAAAAVV----DGPGGQQLVGYLA-----------------PADVDVDTVAATTAEL---LPEYMRPS 447
Cdd:cd05918 373 IEHHLRQSLPGAKEVVVEVvkpkDGSSSPQLVAFVVldgsssgsgdgdslflePSDEFRALVAELRSKLrqrLPSYMVPS 452
|
490 500
....*....|....*....|.
gi 1827387616 448 AWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd05918 453 VFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
5-469 |
4.99e-110 |
|
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: 360.21 E-value: 4.99e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 5 EFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvtsdgea 84
Cdd:cd17644 30 ELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYILEDAQISVLL------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 85 earsrfddivdvhvldisspgdadldeeefagpTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDV 164
Cdd:cd17644 103 ---------------------------------TQPENLAYVIYTSGSTGKPKGVMIEHQSLVNLSHGLIKEYGITSSDR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 165 FLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAF-NEVLGAGVGELTSLRLI 243
Cdd:cd17644 150 VLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRSSLEDFVQYIQQWQLTVLSLPPAYWHLLvLELLLSTIDLPSSLRLV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 244 QTGGEALTPPVARDLM-VRLPGTRLQNQYGPAEASIVVTIHRVTQDDRV----IPIGTPTRRVSARVLDAALREVPIGVP 318
Cdd:cd17644 230 IVGGEAVQPELVRQWQkNVGNFIQLINVYGPTEATIAATVCRLTQLTERnitsVPIGRPIANTQVYILDENLQPVPVGVP 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 319 GELYLGGVQLARGYAGRPDLTAERFVADPF-GEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALA 397
Cdd:cd17644 310 GELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARYLPDGNIEYLGRIDNQVKIRGFRIELGEIEAVLS 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 398 AAPGVlhAAAAVV---DGPGGQQLVGYLAPAdvdvDTVAATTAEL-------LPEYMRPSAWVRLDAMPLSRSGKVDRRL 467
Cdd:cd17644 390 QHNDV--KTAVVIvreDQPGNKRLVAYIVPH----YEESPSTVELrqflkakLPDYMIPSAFVVLEELPLTPNGKIDRRA 463
|
..
gi 1827387616 468 LP 469
Cdd:cd17644 464 LP 465
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1050-1531 |
1.94e-106 |
|
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: 349.39 E-value: 1.94e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARG-VSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYM 1128
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAeIRPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1129 LEDSGATVGITDAstrarlgesscewvdladleaeaesgdditdterngsvrlTNLAYLIYTSGSTGRPKAVGVSHTGIV 1208
Cdd:cd17648 81 LEDTGARVVITNS----------------------------------------TDLAYAIYTSGTTGKPKGVLVEHGSVV 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1209 DFVNSLAKITTGtpEDEPDTRILHVASPSFDASMFEMAWAIPAGHTLVIAPQAD-FAGDALATVLERDEVTDMIITPSVL 1287
Cdd:cd17648 121 NLRTSLSERYFG--RDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMrFDPDRFYAYINREKVTYLSGTPSVL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1288 ATVDPERAQYVRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAGKPV--TIGKPVDGFTVRVLDGR 1364
Cdd:cd17648 199 QQYDLARLPHLKRVDAAGEEFTAPVFEKLRSRfAGLIINAYGPTETTVTNHKRFFPGDQRFdkSLGRPVRNTKCYVLNDA 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1365 LHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEPG-------ARMYATGDLVRVAKGGNLEFAGRADHQVKI 1437
Cdd:cd17648 279 MKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKI 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1438 NGQRVELGEIEAVLDAQPGVAQSVVVGVE----STRGGRKHteVVAYLVAKPGaTIDSAAVLDEAAQHLAAHMVPSQAIV 1513
Cdd:cd17648 359 RGQRIEPGEVEAALASYPGVRECAVVAKEdasqAQSRIQKY--LVGYYLPEPG-HVPESDLLSFLRAKLPRYMVPARLVR 435
|
490
....*....|....*...
gi 1827387616 1514 IDEIPLTPAGKLDRAALP 1531
Cdd:cd17648 436 LEGIPVTINGKLDVRALP 453
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
2575-3059 |
2.17e-106 |
|
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: 349.24 E-value: 2.17e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2575 ARRAPDHVAVvDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAER 2654
Cdd:cd05945 1 AAANPDRPAV-VEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAER 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2655 VASMIEDSGAVLglsVLASGDlpgqefewmrldddsvaaeiaavpagpitdaerlgevtaaNLAYVIYTSGSTGRPKGVA 2734
Cdd:cd05945 80 IREILDAAKPAL---LIADGD----------------------------------------DNAYIIFTSGSTGRPKGVQ 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2735 VTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGGEV-LERFIAEHGATHTFLTP 2813
Cdd:cd05945 117 ISHDNLVSFTNWMLSDFPLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKqLFRFLAEHGITVWVSTP 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2814 SVLS------TMDPTAVPSLRVIAAGGEAVPQPIVDRW---APATELHNLYGPTETTIGIT---ISSAMRPG-DPVRLGG 2880
Cdd:cd05945 197 SFAAmcllspTFTPESLPSLRHFLFCGEVLPHKTARALqqrFPDARIYNTYGPTEATVAVTyieVTPEVLDGyDRLPIGY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2881 PIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPygtaGQRMYRTGDVVRWTPDtdtgGLtLE 2960
Cdd:cd05945 277 AKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDE----GQRAYRTGDLVRLEAD----GL-LF 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2961 YTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG-GSVATALAAYIVPVDGAVEV--SELKAFAGGRLPAYMVP 3037
Cdd:cd05945 348 YRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYkGEKVTELIAFVVPKPGAEAGltKAIKAELAERLPPYMIP 427
|
490 500
....*....|....*....|..
gi 1827387616 3038 SSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05945 428 RRFVYLDELPLNANGKIDRKAL 449
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1039-1540 |
5.13e-106 |
|
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: 347.95 E-value: 5.13e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1039 LIDVLAQR-DLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVD 1117
Cdd:COG0318 1 LADLLRRAaARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1118 PAYPADRIAYMLEDSGATVGITdastrarlgesscewvdladleaeaesgdditdterngsvrltnlAYLIYTSGSTGRP 1197
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT---------------------------------------------ALILYTSGTTGRP 115
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1198 KAVGVSHTGIVDFVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPA-GHTLVIAPqaDFAGDALATVLERDE 1276
Cdd:COG0318 116 KGVMLTHRNLLANAAAIAAALGLTPGD----VVLVALPLFHVFGLTVGLLAPLLaGATLVLLP--RFDPERVLELIERER 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1277 VTDMIITPSVLATV--DPERAQY----VRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAG--KPV 1347
Cdd:COG0318 190 VTVLFGVPTMLARLlrHPEFARYdlssLRLVVSGGAPLPPELLERFEERfGVRIVEGYGLTETSPVVTVNPEDPGerRPG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1348 TIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFvADPFgepgarmYATGDLVRVAKGGNLEF 1427
Cdd:COG0318 270 SVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDLGRLDEDGYLYI 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1428 AGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMV 1507
Cdd:COG0318 342 VGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWGE---RVVAFVVLRPGAELDAEELRAFLRERLARYKV 418
|
490 500 510
....*....|....*....|....*....|...
gi 1827387616 1508 PSQAIVIDEIPLTPAGKLDRAALPEPHAPEPAE 1540
Cdd:COG0318 419 PRRVEFVDELPRTASGKIDRRALRERYAAGALE 451
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
2579-3059 |
3.16e-105 |
|
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: 345.61 E-value: 3.16e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2579 PDHVAVVDGAgARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASM 2658
Cdd:cd17650 1 PDAIAVSDAT-RQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYM 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2659 IEDSGAVLGLSvlasgdLPGqefewmrldddsvaaeiaavpagpitdaerlgevtaaNLAYVIYTSGSTGRPKGVAVTHS 2738
Cdd:cd17650 80 LEDSGAKLLLT------QPE-------------------------------------DLAYVIYTSGTTGKPKGVMVEHR 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2739 GLANFARQESDRLNAGDNPV-VLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGGEV-LERFIAEHGATHTFLTPS-V 2815
Cdd:cd17650 117 NVAHAAHAWRREYELDSFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAaLYDLILKSRITLMESTPAlI 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2816 LSTMDPTA-----VPSLRVIAAGGEAVPQP----IVDRWAPATELHNLYGPTETTIGITISSAMRPGDP----VRLGGPI 2882
Cdd:cd17650 197 RPVMAYVYrngldLSAMRLLIVGSDGCKAQdfktLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGdsanVPIGRPL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2883 GGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGtAGQRMYRTGDVVRWTPDTdtgglTLEYT 2962
Cdd:cd17650 277 PNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFA-PGERMYRTGDLARWRADG-----NVELL 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2963 GRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVL---GVGGSvaTALAAYIVPVDgAVEVSELKAFAGGRLPAYMVPSS 3039
Cdd:cd17650 351 GRVDHQVKIRGFRIELGEIESQLARHPAIDEAVVAvreDKGGE--ARLCAYVVAAA-TLNTAELRAFLAKELPSYMIPSY 427
|
490 500
....*....|....*....|
gi 1827387616 3040 FTVIDELPLTPVGKLDKRAL 3059
Cdd:cd17650 428 YVQLDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1050-1530 |
2.06e-104 |
|
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: 343.30 E-value: 2.06e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDAstrarlgesscewvdladleaeaesgdditdterngsvrlTNLAYLIYTSGSTGRPKAVGVSHTGIVD 1209
Cdd:cd17650 81 EDSGAKLLLTQP----------------------------------------EDLAYVIYTSGTTGKPKGVMVEHRNVAH 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 FVNSLAKITTgtpEDEPDTRILHVASPSFDASMFEMAWAIPAGHTLVIAPQ-ADFAGDALATVLERDEVTDMIITPSVLA 1288
Cdd:cd17650 121 AAHAWRREYE---LDSFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICPDeVKLDPAALYDLILKSRITLMESTPALIR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1289 TV------DPERAQYVRNLATGGEACPPE----LVERWSERgRRIFNCYGPTEATVWAT-----RSRMTAGKPVTIGKPV 1353
Cdd:cd17650 198 PVmayvyrNGLDLSAMRLLIVGSDGCKAQdfktLAARFGQG-MRIINSYGVTEATIDSTyyeegRDPLGDSANVPIGRPL 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1354 DGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGePGARMYATGDLVRVAKGGNLEFAGRADH 1433
Cdd:cd17650 277 PNTAMYVLDERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFA-PGERMYRTGDLARWRADGNVELLGRVDH 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1434 QVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGgrkHTEVVAYLVakPGATIDSAAVLDEAAQHLAAHMVPSQAIV 1513
Cdd:cd17650 356 QVKIRGFRIELGEIESQLARHPAIDEAVVAVREDKGG---EARLCAYVV--AAATLNTAELRAFLAKELPSYMIPSYYVQ 430
|
490
....*....|....*..
gi 1827387616 1514 IDEIPLTPAGKLDRAAL 1530
Cdd:cd17650 431 LDALPLTPNGKVDRRAL 447
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1050-1531 |
5.79e-104 |
|
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: 342.88 E-value: 5.79e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd17644 14 PDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPNYPQERLTYIL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDAStrarlgesscewvdladleaeaesgdditdterngsvrltNLAYLIYTSGSTGRPKAVGVSHTGIVD 1209
Cdd:cd17644 94 EDAQISVLLTQPE----------------------------------------NLAYVIYTSGSTGKPKGVMIEHQSLVN 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 FVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAP-QADFAGDALATVLERDEVTDMIITPS--- 1285
Cdd:cd17644 134 LSHGLIKEYGITSSD----RVLQFASIAFDVAAEEIYVTLLSGATLVLRPeEMRSSLEDFVQYIQQWQLTVLSLPPAywh 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1286 ------VLATVD-PERAQYVrnlATGGEACPPELVERWSERGR---RIFNCYGPTEATVWATRSRMTA-----GKPVTIG 1350
Cdd:cd17644 210 llvlelLLSTIDlPSSLRLV---IVGGEAVQPELVRQWQKNVGnfiQLINVYGPTEATIAATVCRLTQlternITSVPIG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1351 KPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPF-GEPGARMYATGDLVRVAKGGNLEFAG 1429
Cdd:cd17644 287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFnSSESERLYKTGDLARYLPDGNIEYLG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1430 RADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPS 1509
Cdd:cd17644 367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKR---LVAYIVPHYEESPSTVELRQFLKAKLPDYMIPS 443
|
490 500
....*....|....*....|..
gi 1827387616 1510 QAIVIDEIPLTPAGKLDRAALP 1531
Cdd:cd17644 444 AFVVLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1-468 |
1.18e-103 |
|
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: 340.44 E-value: 1.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTs 80
Cdd:cd17653 23 LTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLPSARIQAILRTSGATLLLTT- 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeaearsrfddivdvhvldisspgdadldeeefagpTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd17653 102 -------------------------------------DSPDDLAYIIFTSGSTGIPKGVMVPHRGVLNYVSQPPARLDVG 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPgrhgdPVHLADLIRRhgVTVIHFVPAMLAAFNevlgagVGELTSL 240
Cdd:cd17653 145 PGSRVAQVLSIAFDACIGEIFSTLCNGGTLVLADP-----SDPFAHVART--VDALMSTPSILSTLS------PQDFPNL 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 241 RLIQTGGEALTPPVARDLmvrLPGTRLQNQYGPAEASIVVTIHRVTQDDRViPIGTPTRRVSARVLDAALREVPIGVPGE 320
Cdd:cd17653 212 KTIFLGGEAVPPSLLDRW---SPGRRLYNAYGPTECTISSTMTELLPGQPV-TIGKPIPNSTCYILDADLQPVPEGVVGE 287
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 321 LYLGGVQLARGYAGRPDLTAERFVADPFgEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEA-ALAAA 399
Cdd:cd17653 288 ICISGVQVARGYLGNPALTASKFVPDPF-WPGSRMYRTGDYGRWTEDGGLEFLGREDNQVKVRGFRINLEEIEEvVLQSQ 366
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 400 PGVLHAAAAVVDGpggqQLVGYLAPADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd17653 367 PEVTQAAAIVVNG----RLVAFVTPETVDVDGLRSELAKHLPSYAVPDRIIALDSFPLTANGKVDRKAL 431
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
2569-3060 |
1.18e-103 |
|
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: 340.69 E-value: 1.18e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2569 ELFRAAARRAPDHVAVVDgAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDP 2648
Cdd:cd17645 2 QLFEEQVERTPDHVAVVD-RGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2649 DYPAERVASMIEDSGAVLGLSvlasgdlpgqefewmrldddsvaaeiaavpagpitdaerlgevTAANLAYVIYTSGSTG 2728
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLT-------------------------------------------NPDDLAYVIYTSGSTG 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2729 RPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEA-VGGEVLERFIAEHGAT 2807
Cdd:cd17645 118 LPKGVMIEHHNLVNLCEWHRPYFGVTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSERrLDLDALNDYFNQEGIT 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2808 HTFLTPSVLSTMDPTAVPSLRVIAAGGEAVPQPIVDRWapatELHNLYGPTETTIGITISSAMRPGDPVRLGGPIGGVDL 2887
Cdd:cd17645 198 ISFLPTGAAEQFMQLDNQSLRVLLTGGDKLKKIERKGY----KLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRV 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2888 MVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTaGQRMYRTGDVVRWTPDtdtGGltLEYTGRSDD 2967
Cdd:cd17645 274 YILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVP-GERMYRTGDLAKFLPD---GN--IEFLGRLDQ 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2968 QVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-GGSVATALAAYIVPvDGAVEVSELKAFAGGRLPAYMVPSSFTVIDEL 3046
Cdd:cd17645 348 QVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKeDADGRKYLVAYVTA-PEEIPHEELREWLKNDLPDYMIPTYFVHLKAL 426
|
490
....*....|....
gi 1827387616 3047 PLTPVGKLDKRALP 3060
Cdd:cd17645 427 PLTANGKVDRKALP 440
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1050-1530 |
6.57e-103 |
|
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: 340.02 E-value: 6.57e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDastrarlGESSCEWVDLADLEAEAESGDDITDTERNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIvd 1209
Cdd:cd12114 81 ADAGARLVLTD-------GPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAA-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 fVNSLAKITTG---TPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFAG-DALATVLERDEVT------- 1278
Cdd:cd12114 152 -LNTILDINRRfavGPDD----RVLALSSLSFDLSVYDIFGALSAGATLVLPDEARRRDpAHWAELIERHGVTlwnsvpa 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1279 --DMIITpsvLATVDPERAQYVRNLATGGEACPPELVERWSER--GRRIFNCYGPTEATVWATRSRM----TAGKPVTIG 1350
Cdd:cd12114 227 llEMLLD---VLEAAQALLPSLRLVLLSGDWIPLDLPARLRALapDARLISLGGATEASIWSIYHPIdevpPDWRSIPYG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1351 KPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPfgePGARMYATGDLVRVAKGGNLEFAGR 1430
Cdd:cd12114 304 RPLANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDGTLEFLGR 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1431 ADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVestrGGRKHTEVVAYLVAKPGAT-IDSAAVLDEAAQHLAAHMVPS 1509
Cdd:cd12114 381 RDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVL----GDPGGKRLAAFVVPDNDGTpIAPDALRAFLAQTLPAYMIPS 456
|
490 500
....*....|....*....|.
gi 1827387616 1510 QAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd12114 457 RVIALEALPLTANGKVDRAAL 477
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
2567-3066 |
2.99e-102 |
|
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: 337.17 E-value: 2.99e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2567 LAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPI 2646
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFG-GRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2647 DPDYPAERVASMIEDSGAVLglsVLAsgdlpgqefewmrldddsvaaeiaavpagpitdaerlgevtaanlAYVIYTSGS 2726
Cdd:COG0318 80 NPRLTAEELAYILEDSGARA---LVT---------------------------------------------ALILYTSGT 111
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2727 TGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEG-TLAYRPSeaVGGEVLERFIAEHG 2805
Cdd:COG0318 112 TGRPKGVMLTHRNLLANAAAIAAALGLTPGDVVLVALPLFHVFGLTVGLLAPLLAGaTLVLLPR--FDPERVLELIERER 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2806 ATHTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRWAPAT--ELHNLYGPTETTIGITISSA-MRPGDPV 2876
Cdd:COG0318 190 VTVLFGVPTMLARLlrhpefARYDLSSLRLVVSGGAPLPPELLERFEERFgvRIVEGYGLTETSPVVTVNPEdPGERRPG 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2877 RLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFtANPYgtagqrmYRTGDVVRWTPDtdtGG 2956
Cdd:COG0318 270 SVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDLGRLDED---GY 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2957 LTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVA-TALAAYIVPVDGA-VEVSELKAFAGGRLPAY 3034
Cdd:COG0318 339 LYI--VGRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKWgERVVAFVVLRPGAeLDAEELRAFLRERLARY 416
|
490 500 510
....*....|....*....|....*....|..
gi 1827387616 3035 MVPSSFTVIDELPLTPVGKLDKRALPEPVLEA 3066
Cdd:COG0318 417 KVPRRVEFVDELPRTASGKIDRRALRERYAAG 448
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1-468 |
5.55e-102 |
|
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: 336.36 E-value: 5.55e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvts 80
Cdd:cd17650 13 LTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYMLEDSGAKLLL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeaearsrfddivdvhvldisspgdadldeeefagpTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd17650 90 -------------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAWRREYELD 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDV-FLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTS 239
Cdd:cd17650 133 SFPVrLLQMASFSFDVFAGDFARSLLNGGTLVICPDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVYRNGLDLSA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 240 LRLIQTGGEALTPPVARDLMVRL-PGTRLQNQYGPAEASIVVTIHRVTQDD----RVIPIGTPTRRVSARVLDAALREVP 314
Cdd:cd17650 213 MRLLIVGSDGCKAQDFKTLAARFgQGMRIINSYGVTEATIDSTYYEEGRDPlgdsANVPIGRPLPNTAMYVLDERLQPQP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 315 IGVPGELYLGGVQLARGYAGRPDLTAERFVADPFGePGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEA 394
Cdd:cd17650 293 VGVAGELYIGGAGVARGYLNRPELTAERFVENPFA-PGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRIELGEIES 371
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 395 ALAAAPGVLHAAAAVVDGPGGQ-QLVGYLAPAD-VDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd17650 372 QLARHPAIDEAVVAVREDKGGEaRLCAYVVAAAtLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDRRAL 447
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2-557 |
3.83e-98 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 357.17 E-value: 3.83e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSD 81
Cdd:PRK05691 3747 SYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPAQRLQRIIELSRTPVLVCSAA 3826
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 GEAEARSRFDDIVDV---HVL---DISSPGDADLDEEEFAGPTrpaNAAFTLFTSGSTGRPKAVVITHRGIANRLAADIE 155
Cdd:PRK05691 3827 CREQARALLDELGCAnrpRLLvweEVQAGEVASHNPGIYSGPD---NLAYVIYTSGSTGLPKGVMVEQRGMLNNQLSKVP 3903
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 156 QYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPA----MLAAFNEVLG 231
Cdd:PRK05691 3904 YLALSEADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQGLLAHVQAQGITVLESVPSliqgMLAEDRQALD 3983
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 232 agvgeltSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRV---TQDDRVIPIGTPTRRVSARVLDA 308
Cdd:PRK05691 3984 -------GLRWMLPTGEAMPPELARQWLQRYPQIGLVNAYGPAECSDDVAFFRVdlaSTRGSYLPIGSPTDNNRLYLLDE 4056
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 309 ALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLE 388
Cdd:PRK05691 4057 ALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFGAPGERLYRTGDLARRRSDGVLEYVGRIDHQVKIRGYRIE 4136
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 389 LGEVEAALAAAPGVLHAAAAVVDGPGGQQLVGYLAPADVDVDTVAA-------TTAElLPEYMRPSAWVRLDAMPLSRSG 461
Cdd:PRK05691 4137 LGEIEARLHEQAEVREAAVAVQEGVNGKHLVGYLVPHQTVLAQGALlerikqrLRAE-LPDYMVPLHWLWLDRLPLNANG 4215
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 462 KVDRRLLPEPEIA---PTLYVPPGNADEETVAGLFAELLGVERVGVTDSFFDIGGSSLSAARIAARVSKELGVDVSVRDV 538
Cdd:PRK05691 4216 KLDRKALPALDIGqlqSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGHSLLATQIASRVQKALQRNVPLRAM 4295
|
570
....*....|....*....
gi 1827387616 539 FESPSVRGLVHAVSGRGSA 557
Cdd:PRK05691 4296 FECSTVEELAEYIEGLAGS 4314
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1050-1530 |
1.30e-95 |
|
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: 318.04 E-value: 1.30e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd05945 5 PDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREIL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDastrarlgesscewvdladleaeaesGDDitdterngsvrltnLAYLIYTSGSTGRPKAVGVSHTGIVD 1209
Cdd:cd05945 85 DAAKPALLIAD--------------------------GDD--------------NAYIIFTSGSTGRPKGVQISHDNLVS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 FVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAP---QADFAgdALATVLERDEVTDMIITPSV 1286
Cdd:cd05945 125 FTNWMLSDFPLGPGD----VFLNQAPFSFDLSVMDLYPALASGATLVPVPrdaTADPK--QLFRFLAEHGITVWVSTPSF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1287 --LATVDPERAQyvRNLAT------GGEACPPELVERWSER--GRRIFNCYGPTEATVWATRSRMTAG-----KPVTIGK 1351
Cdd:cd05945 199 aaMCLLSPTFTP--ESLPSlrhflfCGEVLPHKTARALQQRfpDARIYNTYGPTEATVAVTYIEVTPEvldgyDRLPIGY 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1352 PVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFvadpFGEPGARMYATGDLVRVAKGGNLEFAGRA 1431
Cdd:cd05945 277 AKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAYRTGDLVRLEADGLLFYRGRL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1432 DHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVEStrgGRKHTEVVAYLVAKPGATI-DSAAVLDEAAQHLAAHMVPSQ 1510
Cdd:cd05945 353 DFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYK---GEKVTELIAFVVPKPGAEAgLTKAIKAELAERLPPYMIPRR 429
|
490 500
....*....|....*....|
gi 1827387616 1511 AIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd05945 430 FVYLDELPLNANGKIDRKAL 449
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1050-1531 |
2.75e-95 |
|
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: 318.26 E-value: 2.75e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDASTRARLGESSCEWVDLADLEAEaESGDDItdterNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVD 1209
Cdd:cd17656 82 LDSGVRVVLTQRHLKSKLSFNKSTILLEDPSISQ-EDTSNI-----DYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVN 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 FVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQA---DFagDALATVLERDEVTDMIITPSV 1286
Cdd:cd17656 156 LLHFEREKTNINFSD----KVLQFATCSFDVCYQEIFSTLLSGGTLYIIREEtkrDV--EQLFDLVKRHNIEVVFLPVAF 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1287 LATVDPER------AQYVRNLATGGE--ACPPELVERWSERGRRIFNCYGPTEATVwATRSRMTAGKPVT----IGKPVD 1354
Cdd:cd17656 230 LKFIFSERefinrfPTCVKHIITAGEqlVITNEFKEMLHEHNVHLHNHYGPSETHV-VTTYTINPEAEIPelppIGKPIS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1355 GFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgEPGARMYATGDLVRVAKGGNLEFAGRADHQ 1434
Cdd:cd17656 309 NTWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGNIEFLGRADHQ 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1435 VKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKpgATIDSAAVLDEAAQHLAAHMVPSQAIVI 1514
Cdd:cd17656 388 VKIRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEK---YLCAYFVME--QELNISQLREYLAKQLPEYMIPSFFVPL 462
|
490
....*....|....*..
gi 1827387616 1515 DEIPLTPAGKLDRAALP 1531
Cdd:cd17656 463 DQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
2579-3059 |
3.28e-95 |
|
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: 318.06 E-value: 3.28e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2579 PDHVAVVDGAGaRLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASM 2658
Cdd:cd12114 1 PDATAVICGDG-TLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2659 IEDSGAVLGLSVLASGDLPGQEFEWMRLDDDSVAAEIAAVPAGPITDAerlgevtaanLAYVIYTSGSTGRPKGVAVTHS 2738
Cdd:cd12114 80 LADAGARLVLTDGPDAQLDVAVFDVLILDLDALAAPAPPPPVDVAPDD----------LAYVIFTSGSTGTPKGVMISHR 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2739 GLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYrPSEAVGGEV--LERFIAEHGATHTFLTPSVL 2816
Cdd:cd12114 150 AALNTILDINRRFAVGPDDRVLALSSLSFDLSVYDIFGALSAGATLVL-PDEARRRDPahWAELIERHGVTLWNSVPALL 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2817 ------STMDPTAVPSLRVIAAGGEAVPQPIVDRW---APATELHNLYGPTETTIGiTISSAMRPGDP----VRLGGPIG 2883
Cdd:cd12114 229 emlldvLEAAQALLPSLRLVLLSGDWIPLDLPARLralAPDARLISLGGATEASIW-SIYHPIDEVPPdwrsIPYGRPLA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2884 GVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPygtAGQRMYRTGDVVRWTPDTdtgglTLEYTG 2963
Cdd:cd12114 308 NQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP---DGERLYRTGDLGRYRPDG-----TLEFLG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2964 RSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPVDGAVEVS--ELKAFAGGRLPAYMVPSSFT 3041
Cdd:cd12114 380 RRDGQVKVRGYRIELGEIEAALQAHPGVARAVVVVLGDPGGKRLAAFVVPDNDGTPIApdALRAFLAQTLPAYMIPSRVI 459
|
490
....*....|....*...
gi 1827387616 3042 VIDELPLTPVGKLDKRAL 3059
Cdd:cd12114 460 ALEALPLTANGKVDRAAL 477
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
4-468 |
3.85e-95 |
|
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: 316.50 E-value: 3.85e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDge 83
Cdd:cd05945 20 RELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERIREILDAAKPALLIADGD-- 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 aearsrfddivdvhvldisspgdaDLdeeefagptrpanaAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARD 163
Cdd:cd05945 98 ------------------------DN--------------AYIIFTSGSTGRPKGVQISHDNLVSFTNWMLSDFPLGPGD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 164 VFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVP------AMLAAFNEvlgagvGEL 237
Cdd:cd05945 140 VFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKQLFRFLAEHGITVWVSTPsfaamcLLSPTFTP------ESL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 238 TSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQD-----DRViPIGTPTRRVSARVLDAALRE 312
Cdd:cd05945 214 PSLRHFLFCGEVLPHKTARALQQRFPDARIYNTYGPTEATVAVTYIEVTPEvldgyDRL-PIGYAKPGAKLVILDEDGRP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 313 VPIGVPGELYLGGVQLARGYAGRPDLTAERFvadpFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEV 392
Cdd:cd05945 293 VPPGEKGELVISGPSVSKGYLNNPEKTAAAF----FPDEGQRAYRTGDLVRLEADGLLFYRGRLDFQVKLNGYRIELEEI 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 393 EAALAAAPGVlHAAAAVV--DGPGGQQLVGYLAP----ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRR 466
Cdd:cd05945 369 EAALRQVPGV-KEAVVVPkyKGEKVTELIAFVVPkpgaEAGLTKAIKAELAERLPPYMIPRRFVYLDELPLNANGKIDRK 447
|
..
gi 1827387616 467 LL 468
Cdd:cd05945 448 AL 449
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1-469 |
1.16e-94 |
|
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: 315.49 E-value: 1.16e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVG-AEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvt 79
Cdd:cd17648 13 LTYRELNERANRLAHYLLSVAEIrPDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFILEDTGARVVI-- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 80 sdgeaearsrfddivdvhvldisspgdadldeeefagpTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDL 159
Cdd:cd17648 91 --------------------------------------TNSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTSLSERYFG 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 160 TARD--VFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNevlgagVGEL 237
Cdd:cd17648 133 RDNGdeAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEMRFDPDRFYAYINREKVTYLSGTPSVLQQYD------LARL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 238 TSLRLIQTGGEALTPPVARDLMVRLPGtRLQNQYGPAEASIVVTIHRVTQDDRV-IPIGTPTRRVSARVLDAALREVPIG 316
Cdd:cd17648 207 PHLKRVDAAGEEFTAPVFEKLRSRFAG-LIINAYGPTETTVTNHKRFFPGDQRFdKSLGRPVRNTKCYVLNDAMKRVPVG 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 317 VPGELYLGGVQLARGYAGRPDLTAERFVADPFGEPG-------ARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLEL 389
Cdd:cd17648 286 AVGELYLGGDGVARGYLNRPELTAERFLPNPFQTEQerargrnARLYKTGDLVRWLPSGELEYLGRNDFQVKIRGQRIEP 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 390 GEVEAALAAAPGVLHAA------AAVVDGPGGQQLVGY--LAPADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSG 461
Cdd:cd17648 366 GEVEAALASYPGVRECAvvakedASQAQSRIQKYLVGYylPEPGHVPESDLLSFLRAKLPRYMVPARLVRLEGIPVTING 445
|
....*...
gi 1827387616 462 KVDRRLLP 469
Cdd:cd17648 446 KLDVRALP 453
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
5-469 |
6.03e-94 |
|
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: 314.41 E-value: 6.03e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 5 EFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVtsdgEA 84
Cdd:cd17656 18 ELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIMLDSGVRVVLT----QR 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 85 EARSRFDDIVDVHVLDisSPGDADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDV 164
Cdd:cd17656 94 HLKSKLSFNKSTILLE--DPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFEREKTNINFSDK 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 165 FLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQ 244
Cdd:cd17656 172 VLQFATCSFDVCYQEIFSTLLSGGTLYIIREETKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEREFINRFPTCVKHII 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 245 TGGEAL--TPPVARDLMVRlpGTRLQNQYGPAEASiVVTIHRVTQDDRVI---PIGTPTRRVSARVLDAALREVPIGVPG 319
Cdd:cd17656 252 TAGEQLviTNEFKEMLHEH--NVHLHNHYGPSETH-VVTTYTINPEAEIPelpPIGKPISNTWIYILDQEQQLQPQGIVG 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 320 ELYLGGVQLARGYAGRPDLTAERFVADPFgEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAA 399
Cdd:cd17656 329 ELYISGASVARGYLNRQELTAEKFFPDPF-DPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYRIELGEIEAQLLNH 407
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 400 PGVLHAAAAV-VDGPGGQQLVGYLAP-ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLP 469
Cdd:cd17656 408 PGVSEAVVLDkADDKGEKYLCAYFVMeQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVDRKALP 479
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
5-469 |
1.23e-90 |
|
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: 303.32 E-value: 1.23e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 5 EFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvtsdgea 84
Cdd:cd17645 28 QLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGERIAYMLADSSAKILL------- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 85 earsrfddivdvhvldisspgdadldeeefagpTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDV 164
Cdd:cd17645 101 ---------------------------------TNPDDLAYVIYTSGSTGLPKGVMIEHHNLVNLCEWHRPYFGVTPADK 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 165 FLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTvIHFVPAMLA-AFNEVlgagvgELTSLRLI 243
Cdd:cd17645 148 SLVYASFSFDASAWEIFPHLTAGAALHVVPSERRLDLDALNDYFNQEGIT-ISFLPTGAAeQFMQL------DNQSLRVL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 244 QTGGEALTPPVARdlmvrlpGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIGVPGELYL 323
Cdd:cd17645 221 LTGGDKLKKIERK-------GYKLVNNYGPTENTVVATSFEIDKPYANIPIGKPIDNTRVYILDEALQLQPIGVAGELCI 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 324 GGVQLARGYAGRPDLTAERFVADPFgEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVL 403
Cdd:cd17645 294 AGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPDGNIEFLGRLDQQVKIRGYRIEPGEIEPFLMNHPLIE 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 404 HAAA-AVVDGPGGQQLVGYL-APADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLP 469
Cdd:cd17645 373 LAAVlAKEDADGRKYLVAYVtAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALPLTANGKVDRKALP 440
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1-383 |
1.33e-90 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 302.31 E-value: 1.33e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:pfam00501 22 LTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYILEDSGAKVLITDD 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRFDDIVDVHVLDISSPGDADLDEEEFAG-------------PTRPANAAFTLFTSGSTGRPKAVVITHRGIA 147
Cdd:pfam00501 102 ALKLEELLEALGKLEVVKLVLVLDRDPVLKEEPLPEeakpadvppppppPPDPDDLAYIIYTSGTTGKPKGVMLTHRNLV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 148 NRLAA----DIEQYDLTARDVFLYKAPITFDVSVR-EIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAM 222
Cdd:pfam00501 182 ANVLSikrvRPRGFGLGPDDRVLSTLPLFHDFGLSlGLLGPLLAGATVVLPPGFPALDPAALLELIERYKVTVLYGVPTL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 223 LAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLPGTrLQNQYGPAEASIVVTIHRVTQDDRVIP--IGTPTRR 300
Cdd:pfam00501 262 LNMLLEAGAPKRALLSSLRLVLSGGAPLPPELARRFRELFGGA-LVNGYGLTETTGVVTTPLPLDEDLRSLgsVGRPLPG 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 301 VSARVLDAA-LREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADpfgepgaRLYRTGDRARWNRDGEIEYLGRTDFQ 379
Cdd:pfam00501 341 TEVKIVDDEtGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GWYRTGDLGRRDEDGYLEIVGRKKDQ 413
|
....
gi 1827387616 380 VKLR 383
Cdd:pfam00501 414 IKLG 417
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1-477 |
2.19e-90 |
|
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: 302.88 E-value: 2.19e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVts 80
Cdd:COG0318 25 LTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNPRLTAEELAYILEDSGARALVT-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeaearsrfddivdvhvldisspgdadldeeefagptrpanaAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:COG0318 103 -------------------------------------------ALILYTSGTTGRPKGVMLTHRNLLANAAAIAAALGLT 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVRE-IFLPIAIGATLVIAepgRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTS 239
Cdd:COG0318 140 PGDVVLVALPLFHVFGLTVgLLAPLLAGATLVLL---PRFDPERVLELIERERVTVLFGVPTMLARLLRHPEFARYDLSS 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 240 LRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTIHRV-TQDDRVIPIGTPTRRVSARVLDAALREVPIGVP 318
Cdd:COG0318 217 LRLVVSGGAPLPPELLERFEERF-GVRIVEGYGLTETSPVVTVNPEdPGERRPGSVGRPLPGVEVRIVDEDGRELPPGEV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 319 GELYLGGVQLARGYAGRPDLTAERFvADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAA 398
Cdd:COG0318 296 GEIVVRGPNVMKGYWNDPEATAEAF-RDGW-------LRTGDLGRLDEDGYLYIVGRKKDMIISGGENVYPAEVEEVLAA 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 399 APGVLHAAAAVVDGP-GGQQLVGYLAP---ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEPEIA 474
Cdd:COG0318 368 HPGVAEAAVVGVPDEkWGERVVAFVVLrpgAELDAEELRAFLRERLARYKVPRRVEFVDELPRTASGKIDRRALRERYAA 447
|
...
gi 1827387616 475 PTL 477
Cdd:COG0318 448 GAL 450
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
2571-2972 |
2.96e-90 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 301.15 E-value: 2.96e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2571 FRAAARRAPDHVAVVDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDY 2650
Cdd:pfam00501 1 LERQAARTPDKTALEVGEGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2651 PAERVASMIEDSGAVL----------GLSVLASGDLPGQEFEWMRLDDDSVAAEIAAVPAGPITDAERLGEVTAANLAYV 2720
Cdd:pfam00501 81 PAEELAYILEDSGAKVlitddalkleELLEALGKLEVVKLVLVLDRDPVLKEEPLPEEAKPADVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2721 IYTSGSTGRPKGVAVTHSGLANFARQ----ESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEG-TLAY-RPSEAVGG 2794
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSikrvRPRGFGLGPDDRVLSTLPLFHDFGLSLGLLGPLLAGaTVVLpPGFPALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2795 EVLERFIAEHGATHTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRWAPAT--ELHNLYGPTETTiGITI 2866
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLleagapKRALLSSLRLVLSGGAPLPPELARRFRELFggALVNGYGLTETT-GVVT 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2867 SSAMRPGDPVRL---GGPIGGVDLMVLD-ERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTAnpygtagQRMYRT 2942
Cdd:pfam00501 320 TPLPLDEDLRSLgsvGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE-------DGWYRT 392
|
410 420 430
....*....|....*....|....*....|
gi 1827387616 2943 GDVVRWTPDTdtgglTLEYTGRSDDQVKLR 2972
Cdd:pfam00501 393 GDLGRRDEDG-----YLEIVGRKKDQIKLG 417
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1045-1531 |
1.28e-88 |
|
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: 297.54 E-value: 1.28e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1045 QRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADR 1124
Cdd:cd17645 7 QVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPDYPGER 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1125 IAYMLEDSGATVGITDAStrarlgesscewvdladleaeaesgdditdterngsvrltNLAYLIYTSGSTGRPKAVGVSH 1204
Cdd:cd17645 87 IAYMLADSSAKILLTNPD----------------------------------------DLAYVIYTSGSTGLPKGVMIEH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1205 TGIVDFVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQAdfagdalaTVLERDEVTDMI--- 1281
Cdd:cd17645 127 HNLVNLCEWHRPYFGVTPAD----KSLVYASFSFDASAWEIFPHLTAGAALHVVPSE--------RRLDLDALNDYFnqe 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1282 -ITPSVLATVDPER-----AQYVRNLATGGEAcppelVERWSERGRRIFNCYGPTEATVWATRSRMTagKP---VTIGKP 1352
Cdd:cd17645 195 gITISFLPTGAAEQfmqldNQSLRVLLTGGDK-----LKKIERKGYKLVNNYGPTENTVVATSFEID--KPyanIPIGKP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1353 VDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgEPGARMYATGDLVRVAKGGNLEFAGRAD 1432
Cdd:cd17645 268 IDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPF-VPGERMYRTGDLAKFLPDGNIEFLGRLD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1433 HQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVEStRGGRKHteVVAYLVAKpgATIDSAAVLDEAAQHLAAHMVPSQAI 1512
Cdd:cd17645 347 QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKED-ADGRKY--LVAYVTAP--EEIPHEELREWLKNDLPDYMIPTYFV 421
|
490
....*....|....*....
gi 1827387616 1513 VIDEIPLTPAGKLDRAALP 1531
Cdd:cd17645 422 HLKALPLTANGKVDRKALP 440
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
570-996 |
2.00e-87 |
|
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: 293.52 E-value: 2.00e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 570 RLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVY-PSVGAAPVQDVLPVAVAReq 648
Cdd:cd19539 1 RIPLSFAQERLWFIDQGEDGGPAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLvRDDGGVPRQEILPPGPAP-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 649 LDWREADSVESLVRSTTE---------GFDVSTQMPLRGRFHRDGAGLHV-ALTMHHIAMDGQSIPVLARDLMSAYAARA 718
Cdd:cd19539 79 LEVRDLSDPDSDRERRLEellreresrGFDLDEEPPIRAVLGRFDPDDHVlVLVAHHTAFDAWSLDVFARDLAALYAARR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 719 EGRTGGLPVLDVQYADYALWQQSVLGDaddetSVLGEQLSHWRRVLAGLpAVTDLPMDRPRPAVLGTAGATVTVEFDDDL 798
Cdd:cd19539 159 KGPAAPLPELRQQYKEYAAWQREALAA-----PRAAELLDFWRRRLRGA-EPTALPTDRPRPAGFPYPGADLRFELDAEL 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 799 ADRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGDLLGNV 878
Cdd:cd19539 233 VAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARV 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 879 RTTVLDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTYTepTVNDVAGLEASGIQAAPVDTGVVNAKFDLTVAVRARS 958
Cdd:cd19539 313 RKALVDAQRHQELPFQQLVAELPVDRDAGRHPLVQIVFQVT--NAPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEG 390
|
410 420 430
....*....|....*....|....*....|....*...
gi 1827387616 959 GGtpMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd19539 391 TG--LRGSLGYATSLFDEETIQGFLADYLQVLRQLLAN 426
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
572-1010 |
3.69e-85 |
|
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: 288.08 E-value: 3.69e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 572 PLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYP-SVGAAPVQ---DVLPVAVARE 647
Cdd:pfam00668 6 PLSPAQKRMWFLEKLEPHSSAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIrQENGEPVQvilEERPFELEII 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 648 QLDWREADSVESLV-----RSTTEGFDVSTQMPLR-GRFHRDGAGLHVALTMHHIAMDGQSIPVLARDLMSAYAARAEGR 721
Cdd:pfam00668 86 DISDLSESEEEEAIeafiqRDLQSPFDLEKGPLFRaGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 722 TggLPVLDVQ-YADYALWQQSVLGDADDEtsvlgEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVEFDDDLAD 800
Cdd:pfam00668 166 P--LPLPPKTpYKDYAEWLQQYLQSEDYQ-----KDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 801 RVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGDLLGNVRT 880
Cdd:pfam00668 239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 881 TVLDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTY-------TEPTVNDVAGLEASgIQAAPVDTgvvnAKFDLTVA 953
Cdd:pfam00668 319 DLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFqnylgqdSQEEEFQLSELDLS-VSSVIEEE----AKYDLSLT 393
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 954 VRARSGGtpMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDDQNTAVGDIDIVGAA 1010
Cdd:pfam00668 394 ASERGGG--LTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDA 448
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1050-1437 |
1.69e-84 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 284.59 E-value: 1.69e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTE-MDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYM 1128
Cdd:pfam00501 9 PDKTALEVGEGRrLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRLPAEELAYI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1129 LEDSGATVGITDASTRARLGE---------SSCEWVDLADLEAE----AESGDDITDTERNGSVRLTNLAYLIYTSGSTG 1195
Cdd:pfam00501 89 LEDSGAKVLITDDALKLEELLealgklevvKLVLVLDRDPVLKEeplpEEAKPADVPPPPPPPPDPDDLAYIIYTSGTTG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1196 RPKAVGVSHTGIVDFVNSLAKITTGTPEDEPDTRILHVASPSFDASM-FEMAWAIPAGHTLVIAPQAD-FAGDALATVLE 1273
Cdd:pfam00501 169 KPKGVMLTHRNLVANVLSIKRVRPRGFGLGPDDRVLSTLPLFHDFGLsLGLLGPLLAGATVVLPPGFPaLDPAALLELIE 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1274 RDEVTDMIITPSVLATV----DPERAQY--VRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAGKP 1346
Cdd:pfam00501 249 RYKVTVLYGVPTLLNMLleagAPKRALLssLRLVLSGGAPLPPELARRFRELfGGALVNGYGLTETTGVVTTPLPLDEDL 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1347 V---TIGKPVDGFTVRVLD-GRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADpfgepgaRMYATGDLVRVAKG 1422
Cdd:pfam00501 329 RslgSVGRPLPGTEVKIVDdETGEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDED-------GWYRTGDLGRRDED 401
|
410
....*....|....*
gi 1827387616 1423 GNLEFAGRADHQVKI 1437
Cdd:pfam00501 402 GYLEIVGRKKDQIKL 416
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
2575-3063 |
3.11e-75 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 260.98 E-value: 3.11e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2575 ARRAPDHVAVvDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAER 2654
Cdd:PRK04813 12 AQTQPDFPAY-DYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVSSPAER 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2655 VASMIEDSGAVLglsVLASGDLPGQEFEWMRLDDDSVAAEIAAVPAGPITDAerlgeVTAANLAYVIYTSGSTGRPKGVA 2734
Cdd:PRK04813 91 IEMIIEVAKPSL---IIATEELPLEILGIPVITLDELKDIFATGNPYDFDHA-----VKGDDNYYIIFTSGTTGKPKGVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2735 VTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVG--GEVLERFIAEHGATHTFlT 2812
Cdd:PRK04813 163 ISHDNLVSFTNWMLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTAnfKQLFETLPQLPINVWVS-T 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2813 PSV--LSTMDPT----AVPSLRVIAAGGEAVP----QPIVDRWaPATELHNLYGPTETTIGIT---ISSAMRPGDPvRLg 2879
Cdd:PRK04813 242 PSFadMCLLDPSfneeHLPNLTHFLFCGEELPhktaKKLLERF-PSATIYNTYGPTEATVAVTsieITDEMLDQYK-RL- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2880 gPIG----GVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANpygtAGQRMYRTGDVVRWTpdtdtG 2955
Cdd:PRK04813 319 -PIGyakpDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFTF----DGQPAYHTGDAGYLE-----D 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2956 GLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV--GGSVaTALAAYIVPVDGAVE-----VSELKAFAG 3028
Cdd:PRK04813 389 GL-LFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYnkDHKV-QYLIAYVVPKEEDFErefelTKAIKKELK 466
|
490 500 510
....*....|....*....|....*....|....*
gi 1827387616 3029 GRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPV 3063
Cdd:PRK04813 467 ERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIEEV 501
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1633-2069 |
7.14e-74 |
|
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: 254.48 E-value: 7.14e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1633 EMPLPPVTSWMIEHSeePADFADFSQSLVFNVPASAAVADLQTVVEAVAAAHPMLTAVLTRSGDGWTM---NAGAGIVPA 1709
Cdd:cd19534 1 EVPLTPIQRWFFEQN--LAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQrirGDVEELFRL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1710 ----VREIDAEGALDPALVDAHRellgAMDPGTGSLLGTAVVNGEGR-RRLVIAIHHLGVDAVSWPILVEDLVTAWAQLT 1784
Cdd:cd19534 79 evvdLSSLAQAAAIEALAAEAQS----SLDLEEGPLLAAALFDGTDGgDRLLLVIHHLVVDGVSWRILLEDLEAAYEQAL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1785 SGRPIELrPEATTTRRIAHLLA--GQVHARAREVDYWLEQLPerPTSFGTSADRPlHRRRDESSLTYVVD-DVAGSILTT 1861
Cdd:cd19534 155 AGEPIPL-PSKTSFQTWAELLAeyAQSPALLEELAYWRELPA--ADYWGLPKDPE-QTYGDARTVSFTLDeEETEALLQE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1862 VPQAFGSSVDDVLLGALARAVRAWqldngiADGGPVTVSTEGHGRDESIAGdegaIDLSRTVGWFTSITP--LAVDASSD 1939
Cdd:cd19534 231 ANAAYRTEINDLLLAALALAFQDW------TGRAPPAIFLEGHGREEIDPG----LDLSRTVGWFTSMYPvvLDLEASED 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1940 VVHAVKSAKDARLSRPAGGVGFGILRY-NSDGE--IAHRPLPTIMYNYFGGGTAPSTetapDDFLPVSDRPNMPSSITGA 2016
Cdd:cd19534 301 LGDTLKRVKEQLRRIPNKGIGYGILRYlTPEGTkrLAFHPQPEISFNYLGQFDQGER----DDALFVSAVGGGGSDIGPD 376
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 2017 MRSPSVFGINISTAGreeRRLEAKVTYATDALDEAAASDIARRWHDELRAVVE 2069
Cdd:cd19534 377 TPRFALLDINAVVEG---GQLVITVSYSRNMYHEETIQQLADSYKEALEALIE 426
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
567-996 |
1.91e-72 |
|
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: 250.86 E-value: 1.91e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 567 RPERLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDVLPVAVAR 646
Cdd:cd19546 1 RPDEVPATAGQLRTWLLARLDEETRGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRILDADAAR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 647 EQLDWREADSVE---SLVRSTTEGFDVSTQMPLRGRFHRDGAGLHV-ALTMHHIAMDGQSIPVLARDLMSAYAARAEGRT 722
Cdd:cd19546 81 PELPVVPATEEElpaLLADRAAHLFDLTRETPWRCTLFALSDTEHVlLLVVHRIAADDESLDVLVRDLAAAYGARREGRA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 723 GGLPVLDVQYADYALWQQSVLGDADDETSVLGEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVEFDDDLADRV 802
Cdd:cd19546 161 PERAPLPLQFADYALWERELLAGEDDRDSLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 803 DVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDP-ALEELIGMFVNTLLLRTQVDPGHSVGDLLGNVRTT 881
Cdd:cd19546 241 MEAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDEEgDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 882 VLDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTYTEPTVNDVAGLEASGIQAAPVDTGVVNAKFDLTVAV--RARSG 959
Cdd:cd19546 321 VREARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDAPELPGLRTSPVPLGTEAMELDLSLALteRRNDD 400
|
410 420 430
....*....|....*....|....*....|....*....
gi 1827387616 960 GTP--MAADFIYATDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd19546 401 GDPdgLDGSLRYAADLFDRATAAALARRLVRVLEQVAAD 439
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
2104-2554 |
1.04e-70 |
|
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: 246.09 E-value: 1.04e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2104 ADVWPMTPLQQG-LFFQADLANTVAdhdaidvYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPSGAAVTVV 2182
Cdd:pfam00668 2 QDEYPLSPAQKRmWFLEKLEPHSSA-------YNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRQENGEPVQVI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2183 PAEVTVPWSVIDLRAEDAASLDSRVEEVLATERTNPFDMAKPPLIRVVLVEHGD-GAELVVTNHHLLIDGWSSPLVLADL 2261
Cdd:pfam00668 75 LEERPFELEIIDISDLSESEEEEAIEAFIQRDLQSPFDLEKGPLFRAGLFRIAEnRHHLLLSMHHIIVDGVSLGILLRDL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2262 LSLYAT---GQTfTGSLPGTSGRDFADHARAVAT-ADVEAGIAAWREVLAPVTEPTLVAPGHEPSADAPPRDHQFSIDV- 2336
Cdd:pfam00668 155 ADLYQQllkGEP-LPLPPKTPYKDYAEWLQQYLQsEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLd 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2337 -KVTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGR-SPDIegmESMVGMFINTIPAVVDVNPDATVV 2414
Cdd:pfam00668 234 eDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRpSPDI---ERMVGMFVNTLPLRIDPKGGKTFS 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2415 DVLTAVQNDKVKVLDHQQIGLPRLVAQTGLP------ALFDTLAVYESFPVNvDSVAGIDASSAGGLKlVGAKTSDATHY 2488
Cdd:pfam00668 311 ELIKRVQEDLLSAEPHQGYPFGDLVNDLRLPrdlsrhPLFDPMFSFQNYLGQ-DSQEEEFQLSELDLS-VSSVIEEEAKY 388
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 2489 PLNLSASRRGAELALKLKYLPTAFAPEQVAVFADVLTGLLGAIADHPEATCAEIPLLPAEAAVELT 2554
Cdd:pfam00668 389 DLSLTASERGGGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1184-1526 |
3.41e-69 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 237.57 E-value: 3.41e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1184 LAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPqaDF 1263
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGD----VFLSTLPLFHIGGLFGLLGALLAGGTVVLLP--KF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1264 AGDALATVLERDEVTDMIITPSVLATVD--PERAQY----VRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWA 1336
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLkaPESAGYdlssLRALVSGGAPLPPELLERFEEApGIKLVNGYGLTETGGTV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1337 T--RSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFvadpfgEPGarMYATG 1414
Cdd:cd04433 156 AtgPPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD------EDG--WYRTG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1415 DLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPGATIDSAAV 1494
Cdd:cd04433 228 DLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGE---RVVAVVVLRPGADLDAEEL 304
|
330 340 350
....*....|....*....|....*....|..
gi 1827387616 1495 LDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLD 1526
Cdd:cd04433 305 RAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
571-996 |
3.73e-66 |
|
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: 231.91 E-value: 3.73e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 571 LPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDVLPVAVARE--- 647
Cdd:cd19066 2 IPLSPMQRGMWFLKKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVLDKTVRFRiei 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 648 ----QLDWREADSVESLVRSTTEGFDVSTQMPLRGR-FHRDGAGLHVALTMHHIAMDGQSIPVLARDLMSAYAArAEGRT 722
Cdd:cd19066 82 idlrNLADPEARLLELIDQIQQTIYDLERGPLVRVAlFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDA-AERQK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 723 GGLPVLDVQYADYALWQQSVLGDADdetsvLGEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVEFDDDLADRV 802
Cdd:cd19066 161 PTLPPPVGSYADYAAWLEKQLESEA-----AQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 803 DVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGDLLGNVRTTV 882
Cdd:cd19066 236 REVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQS 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 883 LDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTYTepTVNDVAGLEASGIQAAPVDTGVVNAKFDLTVAVRARSGGTP 962
Cdd:cd19066 316 REAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFK--NNQQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASEDPDGDL 393
|
410 420 430
....*....|....*....|....*....|....
gi 1827387616 963 MAAdFIYATDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd19066 394 LLR-LEYSRGVYDERTIDRFAERYMTALRQLIEN 426
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
2106-2535 |
1.86e-64 |
|
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: 226.03 E-value: 1.86e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2106 VWPMTPLQQGLffqadLANTVADHDaidVYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPS-GAAVTVVPA 2184
Cdd:cd19542 1 IYPCTPMQEGM-----LLSQLRSPG---LYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVESSAeGTFLQVVLK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2185 EVTVPWSVIdlraedaasldSRVEEVLATERTNPFDM---AKPPLIRVVLVEHGDG-AELVVTNHHLLIDGWSSPLVLAD 2260
Cdd:cd19542 73 SLDPPIEEV-----------ETDEDSLDALTRDLLDDptlFGQPPHRLTLLETSSGeVYLVLRISHALYDGVSLPIILRD 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2261 LLSLYaTGQTftgSLPGTSgrdFADHARAVATADVEAGIAAWREVLA---PVTEPTLVapghePSADAPPRDHQFSIDvk 2337
Cdd:cd19542 142 LAAAY-NGQL---LPPAPP---FSDYISYLQSQSQEESLQYWRKYLQgasPCAFPSLS-----PKRPAERSLSSTRRS-- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2338 vTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRSPDIEGMESMVGMFINTIPAVVDVNPDATVVDVL 2417
Cdd:cd19542 208 -LAKLEAFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDLPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLL 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2418 TAVQNDKVKVLDHQQIGLPRLVAQTGLPA---LFDTLAVYESFPVNVDSvagidaSSAGGLKLVGAKTSDATHYPLNLSA 2494
Cdd:cd19542 287 RQLQQQYLRSLPHQHLSLREIQRALGLWPsgtLFNTLVSYQNFEASPES------ELSGSSVFELSAAEDPTEYPVAVEV 360
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1827387616 2495 SRRGAELALKLKYLPTAFAPEQVAVFADVLTGLLGAIADHP 2535
Cdd:cd19542 361 EPSGDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLANP 401
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
124-464 |
5.20e-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: 219.46 E-value: 5.20e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 124 AFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPgrhGDPVH 203
Cdd:cd04433 3 ALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPK---FDPEA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 204 LADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMvRLPGTRLQNQYGPAEASIVVTIH 283
Cdd:cd04433 80 ALELIEREKVTILLGVPTLLARLLKAPESAGYDLSSLRALVSGGAPLPPELLERFE-EAPGIKLVNGYGLTETGGTVATG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 284 RVTQDDRVIP-IGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFvadpfgEPGarLYRTGDRA 362
Cdd:cd04433 159 PPDDDARKPGsVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD------EDG--WYRTGDLG 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 363 RWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAP---ADVDVDTVAATTAE 438
Cdd:cd04433 231 RLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVvGVPDPEWGERVVAVVVLrpgADLDAEELRAHVRE 310
|
330 340
....*....|....*....|....*.
gi 1827387616 439 LLPEYMRPSAWVRLDAMPLSRSGKVD 464
Cdd:cd04433 311 RLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
2482-3144 |
1.42e-62 |
|
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: 238.04 E-value: 1.42e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2482 TSDATHYPLNLSASrrGAELALKLKYLPTAFAPEQVAVFADVLTGLLGAIADHPEATCAEIPLL-PAEAAVELTPVTG-- 2558
Cdd:TIGR03443 153 TGSTTDLTVFLTPS--SPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLItPSQKSLLPDPTKDld 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2559 -----GPATDpvtlaeLFRAAARRAPDHVAVVDGAGAR--------LTYRELDEASDRLARWLIGRGVGPERAVALAIGR 2625
Cdd:TIGR03443 231 wsgfrGAIHD------IFADNAEKHPDRTCVVETPSFLdpssktrsFTYKQINEASNILAHYLLKTGIKRGDVVMIYAYR 304
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2626 SAQLLTAIWAVAKTGGAYVPIDPDYPAER------VAS-----MIEDSGA------------------VLGLSVLASGDL 2676
Cdd:TIGR03443 305 GVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsVAKpraliVIEKAGTldqlvrdyidkelelrteIPALALQDDGSL 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2677 PGQEFEWMRLDDDSVAAEIAAVPAGPItdaerLGEVTAANLAYviyTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDN 2756
Cdd:TIGR03443 385 VGGSLEGGETDVLAPYQALKDTPTGVV-----VGPDSNPTLSF---TSGSEGIPKGVLGRHFSLAYYFPWMAKRFGLSEN 456
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2757 ------------PVVLGFASPSFDASVLeyLLATV----NEGTLAyrpseavggevleRFIAEHGATHTFLTPS---VLS 2817
Cdd:TIGR03443 457 dkftmlsgiahdPIQRDMFTPLFLGAQL--LVPTAddigTPGRLA-------------EWMAKYGATVTHLTPAmgqLLS 521
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2818 TMDPTAVPSLRVIAAGGEAVPQPIVDRW---APATELHNLYGPTETTIGI---TISSamRPGDPVRLGG-----PIG--- 2883
Cdd:TIGR03443 522 AQATTPIPSLHHAFFVGDILTKRDCLRLqtlAENVCIVNMYGTTETQRAVsyfEIPS--RSSDSTFLKNlkdvmPAGkgm 599
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2884 -GVDLMVLD--ERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQ---------------------RM 2939
Cdd:TIGR03443 600 kNVQLLVVNrnDRTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPSHwidldkennkperefwlgprdRL 679
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2940 YRTGDVVRWTPDTDtggltLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLgV--GGSVATALAAYIVPVDGA 3017
Cdd:TIGR03443 680 YRTGDLGRYLPDGN-----VECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTL-VrrDKDEEPTLVSYIVPQDKS 753
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3018 VEVSELKA---------------------------FAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVLEAGEYV 3070
Cdd:TIGR03443 754 DELEEFKSevddeessdpvvkglikyrklikdireYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQLAAV 833
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3071 AP----------ATGTERTIADVAAGVLNIDAGLVSATSSFFELGGDSLSAARLAARLSDQLGVAVSVRDVFESGSIRAL 3140
Cdd:TIGR03443 834 AKnrsasaadeeFTETEREIRDLWLELLPNRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKGF 913
|
....
gi 1827387616 3141 AETV 3144
Cdd:TIGR03443 914 AKEV 917
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1040-1530 |
6.96e-62 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 222.08 E-value: 6.96e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1040 IDVLAQRDldPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAV--GME-RSIGSVLatwGVIKSGAAYVPV 1116
Cdd:PRK04813 8 IEEFAQTQ--PDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVfgHMSpEMLATFL---GAVKAGHAYIPV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1117 DPAYPADRIAYMLEDSGATVGITDASTRarLGESSCEWVDLADLEAEAESGddiTDTERNGSVRLTNLAYLIYTSGSTGR 1196
Cdd:PRK04813 83 DVSSPAERIEMIIEVAKPSLIIATEELP--LEILGIPVITLDELKDIFATG---NPYDFDHAVKGDDNYYIIFTSGTTGK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1197 PKAVGVSHTGIVDFVNSLAKITtGTPEDEpdtRILHVASPSFDASMfeMAWAiPA---GHTLVIAPQ---ADFAgdALAT 1270
Cdd:PRK04813 158 PKGVQISHDNLVSFTNWMLEDF-ALPEGP---QFLNQAPYSFDLSV--MDLY-PTlasGGTLVALPKdmtANFK--QLFE 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1271 VLERDEVTDMIITPSV--LATVDPE-RAQYVRNLAT---GGEACP----PELVERWSERgrRIFNCYGPTEATVWATRSR 1340
Cdd:PRK04813 229 TLPQLPINVWVSTPSFadMCLLDPSfNEEHLPNLTHflfCGEELPhktaKKLLERFPSA--TIYNTYGPTEATVAVTSIE 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1341 MT-----AGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFvadpFGEPGARMYATGD 1415
Cdd:PRK04813 307 ITdemldQYKRLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF----FTFDGQPAYHTGD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1416 LVrVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVEStrgGRKHTEVVAYLVAKPG-----ATId 1490
Cdd:PRK04813 383 AG-YLEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNK---DHKVQYLIAYVVPKEEdfereFEL- 457
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1827387616 1491 SAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK04813 458 TKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
2717-3055 |
1.18e-61 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 215.61 E-value: 1.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2717 LAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEaVGGEV 2796
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNLLAAAAALAASGGLTEGDVFLSTLPLFHIGGLFGLLGALLAGGTVVLLPKF-DPEAA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2797 LERfIAEHGATHTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRW--APATELHNLYGPTETTIGITIss 2868
Cdd:cd04433 81 LEL-IEREKVTILLGVPTLLARLlkapesAGYDLSSLRALVSGGAPLPPELLERFeeAPGIKLVNGYGLTETGGTVAT-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2869 aMRPGDPVRLGGPIG----GVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFtanpygtaGQRMYRTGD 2944
Cdd:cd04433 158 -GPPDDDARKPGSVGrpvpGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVD--------EDGWYRTGD 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2945 VVRWTPDtdtGGLTleYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVAT-ALAAYIVPVDGA-VEVSE 3022
Cdd:cd04433 229 LGRLDED---GYLY--IVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGeRVVAVVVLRPGAdLDAEE 303
|
330 340 350
....*....|....*....|....*....|...
gi 1827387616 3023 LKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLD 3055
Cdd:cd04433 304 LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1050-1530 |
3.35e-61 |
|
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This subfamily of the AMP-forming adenylation family contains Escherichia coli FadD and similar prokaryotic fatty acid CoA synthetases. FadD was characterized as a long-chain fatty acid CoA synthetase. The gene fadD is regulated by the fatty acid regulatory protein FadR. Fatty acid CoA synthetase catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341259 [Multi-domain] Cd Length: 468 Bit Score: 218.97 E-value: 3.35e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd05936 13 PDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHIL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDastrarlgesscewVDLADLEAEAESgdditdTERNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVd 1209
Cdd:cd05936 93 NDSGAKALIVA--------------VSFTDLLAAGAP------LGERVALTPEDVAVLQYTSGTTGVPKGAMLTHRNLV- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 fVNSLAKITTGTPEDEPDTRILhVASPSFD--ASMFEMAWAIPAGHTLVIAPQADFAGdALATvLERDEVTDMIITPSVL 1287
Cdd:cd05936 152 -ANALQIKAWLEDLLEGDDVVL-AALPLFHvfGLTVALLLPLALGATIVLIPRFRPIG-VLKE-IRKHRVTIFPGVPTMY 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1288 ATV--DPERAQY----VRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAG-KPVTIGKPVDGFTVR 1359
Cdd:cd05936 228 IALlnAPEFKKRdfssLRLCISGGAPLPVEVAERFEELtGVPIVEGYGLTETSPVVAVNPLDGPrKPGSIGIPLPGTEVK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1360 VLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmyATGDLVRVAKGGNLEFAGRADHQVKING 1439
Cdd:cd05936 308 IVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL--------RTGDIGYMDEDGYFFIVDRKKDMIIVGG 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1440 QRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhTEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPL 1519
Cdd:cd05936 380 FNVYPREVEEVLYEHPAVAEAAVVGVPDPYSG---EAVKAFVVLKEGASLTEEEIIAFCREQLAGYKVPRQVEFRDELPK 456
|
490
....*....|.
gi 1827387616 1520 TPAGKLDRAAL 1530
Cdd:cd05936 457 SAVGKILRREL 467
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
2106-2535 |
3.63e-61 |
|
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: 216.40 E-value: 3.63e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2106 VWPMTPLQQGLFfqadlANTVADHDAidvYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPSGAAVTVVPAE 2185
Cdd:cd19545 1 IYPCTPLQEGLM-----ALTARQPGA---YVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIVQSDSGGLLQVVVKE 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2186 VTVPWsvidlraEDAASLDsrveEVLATERTNPFDmAKPPLIRVVLVEHGDGA-ELVVTNHHLLIDGWSSPLVLADLLSL 2264
Cdd:cd19545 73 SPISW-------TESTSLD----EYLEEDRAAPMG-LGGPLVRLALVEDPDTErYFVWTIHHALYDGWSLPLILRQVLAA 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2265 YATGqtftgslPGTSGRDFADHARAVATADVEAGIAAWREVLAPVTE---PTLVAPGHEPSADAPpRDHQFSIDVKVTER 2341
Cdd:cd19545 141 YQGE-------PVPQPPPFSRFVKYLRQLDDEAAAEFWRSYLAGLDPavfPPLPSSRYQPRPDAT-LEHSISLPSSASSG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2342 lealarnnsTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRSPDIEGMESMVGMFINTIPAVVDVNPDATVVDVLTAVQ 2421
Cdd:cd19545 213 ---------VTLATVLRAAWALVLSRYTGSDDVVFGVTLSGRNAPVPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQ 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2422 NDKVKVLDHQQIGLP---RLVAQTGLPALFDTLAVyesfpVNVDSVAGIDASSAGGLKLVGAKTSDATHYPLNLSASRRG 2498
Cdd:cd19545 284 KDLLDMIPFEHTGLQnirRLGPDARAACNFQTLLV-----VQPALPSSTSESLELGIEEESEDLEDFSSYGLTLECQLSG 358
|
410 420 430
....*....|....*....|....*....|....*..
gi 1827387616 2499 AELALKLKYLPTAFAPEQVAVFADVLTGLLGAIADHP 2535
Cdd:cd19545 359 SGLRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
572-997 |
4.32e-60 |
|
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: 214.24 E-value: 4.32e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 572 PLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVY--PSVGAAPVQDVLP-------- 641
Cdd:cd19532 3 PMSFGQSRFWFLQQYLEDPTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLAssplrleh 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 642 VAVAREQLDWREADSVESLVrsttegFDVSTQMPLRGRFHRDGAGLH-VALTMHHIAMDGQSIPVLARDLMSAYAARAeg 720
Cdd:cd19532 83 VQISDEAEVEEEFERLKNHV------YDLESGETMRIVLLSLSPTEHyLIFGYHHIAMDGVSFQIFLRDLERAYNGQP-- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 721 rtggLPVLDVQYADYALWQQsvlgdADDETSVLGEQLSHWRRVLAGLPAVTDL-PMDR--PRPAVLGTAGATVTVEFDDD 797
Cdd:cd19532 155 ----LLPPPLQYLDFAARQR-----QDYESGALDEDLAYWKSEFSTLPEPLPLlPFAKvkSRPPLTRYDTHTAERRLDAA 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 798 LADRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGDLLGN 877
Cdd:cd19532 226 LAARIKEASRKLRVTPFHFYLAALQVLLARLLDVDDICIGIADANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 878 VRTTVLDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTYTEPTVNDV--AGLEASGIQAAPVDTGvvnakFDLTVAVR 955
Cdd:cd19532 306 TRDKAYAALAHSRVPFDVLLDELGVPRSATHSPLFQVFINYRQGVAESRpfGDCELEGEEFEDARTP-----YDLSLDII 380
|
410 420 430 440
....*....|....*....|....*....|....*....|..
gi 1827387616 956 ARSGGTPMaADFIYATDLFDESTVKRFAEVYRRVLQAIVDDQ 997
Cdd:cd19532 381 DNPDGDCL-LTLKVQSSLYSEEDAELLLDSYVNLLEAFARDP 421
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1048-1527 |
1.22e-59 |
|
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: 213.24 E-value: 1.22e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1048 LDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAY 1127
Cdd:cd17631 7 RHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1128 MLEDSGATVGITDastrarlgesscewvdladleaeaesgdditdterngsvrltnLAYLIYTSGSTGRPKAVGVSHTGI 1207
Cdd:cd17631 87 ILADSGAKVLFDD-------------------------------------------LALLMYTSGTTGRPKGAMLTHRNL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1208 vdFVNSLAKITTGTPEdePDTRILHVAsPSFDASMFEMaWAIP---AGHTLVIAPQADfAGDALATVlERDEVTDMIITP 1284
Cdd:cd17631 124 --LWNAVNALAALDLG--PDDVLLVVA-PLFHIGGLGV-FTLPtllRGGTVVILRKFD-PETVLDLI-ERHRVTSFFLVP 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1285 SVLATV--DPERAQY----VRNLATGGEACPPELVERWSERGRRIFNCYGPTEATVWAT--RSRMTAGKPVTIGKPVDGF 1356
Cdd:cd17631 196 TMIQALlqHPRFATTdlssLRAVIYGGAPMPERLLRALQARGVKFVQGYGMTETSPGVTflSPEDHRRKLGSAGRPVFFV 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1357 TVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmyATGDLVRVAKGGNLEFAGRADHQVK 1436
Cdd:cd17631 276 EVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF--------HTGDLGRLDEDGYLYIVDRKKDMII 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1437 INGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDE 1516
Cdd:cd17631 348 SGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKWGEA---VVAVVVPRPGAELDEDELIAHCRERLARYKIPKSVEFVDA 424
|
490
....*....|.
gi 1827387616 1517 IPLTPAGKLDR 1527
Cdd:cd17631 425 LPRNATGKILK 435
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1054-1525 |
1.28e-59 |
|
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: 214.77 E-value: 1.28e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1054 ALICD--GTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLED 1131
Cdd:cd05911 1 AQIDAdtGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1132 SGATVGITDASTRARLGESSCEWVD------LADLEAEAESGDDITDTERNGSVRL---------TNLAYLIYTSGSTGR 1196
Cdd:cd05911 81 SKPKVIFTDPDGLEKVKEAAKELGPkdkiivLDDKPDGVLSIEDLLSPTLGEEDEDlppplkdgkDDTAAILYSSGTTGL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1197 PKAVGVSHTGIVdfVNSLAKITTGTPEDEPDTRILHVaSPSFDAS-MFEMAWAIPAGHTLVIAPQADFAgDALATVlERD 1275
Cdd:cd05911 161 PKGVCLSHRNLI--ANLSQVQTFLYGNDGSNDVILGF-LPLYHIYgLFTTLASLLNGATVIIMPKFDSE-LFLDLI-EKY 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1276 EVTDMIITPSVLA------TVDPERAQYVRNLATGGEACPPELVERWSERGR--RIFNCYGPTEATVWATRSRMTAGKPV 1347
Cdd:cd05911 236 KITFLYLVPPIAAalakspLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPnaTIKQGYGMTETGGILTVNPDGDDKPG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1348 TIGKPVDGFTVRVLD--GRLhEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRVAKGGNL 1425
Cdd:cd05911 316 SVGRLLPNVEAKIVDddGKD-SLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTGDIGYFDEDGYL 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1426 EFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEV-VAYLVAKPGATIDSAAVLDEAAQHLAA 1504
Cdd:cd05911 388 YIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSG----ELpRAYVVRKPGEKLTEKEVKDYVAKKVAS 463
|
490 500
....*....|....*....|....*
gi 1827387616 1505 HmvpSQ----AIVIDEIPLTPAGKL 1525
Cdd:cd05911 464 Y---KQlrggVVFVDEIPKSASGKI 485
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
2567-3059 |
1.61e-59 |
|
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: 213.96 E-value: 1.61e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2567 LAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPI 2646
Cdd:cd05936 1 LADLLEEAARRFPDKTALIFM-GRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2647 DPDYPAERVASMIEDSGAVLGLSVLAsgdlpgqeFEwmrldddSVAAEIAAVPAGPITDAErlgevtaaNLAYVIYTSGS 2726
Cdd:cd05936 80 NPLYTPRELEHILNDSGAKALIVAVS--------FT-------DLLAAGAPLGERVALTPE--------DVAVLQYTSGT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2727 TGRPKGVAVTHSGLANFARQESDRLNAGDNP--VVLGfASPSFDASVLeyllaTVNeGTLAYRpseaVGGEV--LERF-- 2800
Cdd:cd05936 137 TGVPKGAMLTHRNLVANALQIKAWLEDLLEGddVVLA-ALPLFHVFGL-----TVA-LLLPLA----LGATIvlIPRFrp 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2801 ------IAEHGATHTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRWAPAT--ELHNLYGPTETTIGITI 2866
Cdd:cd05936 206 igvlkeIRKHRVTIFPGVPTMYIALlnapefKKRDFSSLRLCISGGAPLPVEVAERFEELTgvPIVEGYGLTETSPVVAV 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2867 SSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANpygtagqrMYRTGDVV 2946
Cdd:cd05936 286 NPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDG--------WLRTGDIG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2947 RWtpDTDtGGLTLEytGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVA-TALAAYIVPVDGA-VEVSELK 3024
Cdd:cd05936 358 YM--DED-GYFFIV--DRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPYSgEAVKAFVVLKEGAsLTEEEII 432
|
490 500 510
....*....|....*....|....*....|....*
gi 1827387616 3025 AFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05936 433 AFCREQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
2571-3056 |
2.09e-59 |
|
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: 212.47 E-value: 2.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2571 FRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDY 2650
Cdd:cd17631 1 LRRRARRHPDRTALVFG-GRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2651 PAERVASMIEDSGAvlglSVLasgdlpgqefewmrLDDdsvaaeiaavpagpitdaerlgevtaanLAYVIYTSGSTGRP 2730
Cdd:cd17631 80 TPPEVAYILADSGA----KVL--------------FDD----------------------------LALLMYTSGTTGRP 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2731 KGVAVTH-SGLANFARQESDR-LNAGDNPVVLGfasPSFDASVLE-YLLATVNEGTLAYRPSEAVGGEVLeRFIAEHGAT 2807
Cdd:cd17631 114 KGAMLTHrNLLWNAVNALAALdLGPDDVLLVVA---PLFHIGGLGvFTLPTLLRGGTVVILRKFDPETVL-DLIERHRVT 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2808 HTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRW-APATELHNLYGPTETTIGITIssaMRPGDPVRL-- 2878
Cdd:cd17631 190 SFFLVPTMIQALlqhprfATTDLSSLRAVIYGGAPMPERLLRALqARGVKFVQGYGMTETSPGVTF---LSPEDHRRKlg 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2879 --GGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANpygtagqrMYRTGDVVRwtPDtDTGG 2956
Cdd:cd17631 267 saGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDG--------WFHTGDLGR--LD-EDGY 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2957 LTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG----GSVATALaayIVPVDGA-VEVSELKAFAGGRL 3031
Cdd:cd17631 336 LYI--VDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPdekwGEAVVAV---VVPRPGAeLDEDELIAHCRERL 410
|
490 500
....*....|....*....|....*
gi 1827387616 3032 PAYMVPSSFTVIDELPLTPVGKLDK 3056
Cdd:cd17631 411 ARYKIPKSVEFVDALPRNATGKILK 435
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
570-996 |
7.34e-59 |
|
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: 210.96 E-value: 7.34e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 570 RLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDVLP---VAVAR 646
Cdd:cd20483 1 PRPMSTFQRRLWFLHNFLEDKTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDdpsFHLIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 647 EQLDwREADSVESLVRSTTE----GFDVSTQMPLRGRFHRDGAGLHVALTM-HHIAMDGQSIPVLARDLMSAYAA-RAEG 720
Cdd:cd20483 81 IDLS-EAADPEAALDQLVRNlrrqELDIEEGEVIRGWLVKLPDEEFALVLAsHHIAWDRGSSKSIFEQFTALYDAlRAGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 721 RTGGLPVLDVQYADYALWQQSVLGDADDETSvlgeqLSHWRRVLAGLP-AVTDLPM-DRPRPAVLGTAGATVTVEFDDDL 798
Cdd:cd20483 160 DLATVPPPPVQYIDFTLWHNALLQSPLVQPL-----LDFWKEKLEGIPdASKLLPFaKAERPPVKDYERSTVEATLDKEL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 799 ADRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGDLLGNV 878
Cdd:cd20483 235 LARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLEST 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 879 RTTVLDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTYteptvnDVAGleasgiQAAPVDTGvvnaKFDLTvavRARS 958
Cdd:cd20483 315 KTTCLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNY------QVHG------KFPEYDTG----DFKFT---DYDH 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 959 GGTPMAADFI----------------YATDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd20483 376 YDIPTACDIAleaeedpdggldlrleFSTTLYDSADMERFLDNFVTFLTSVIRD 429
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
2569-3059 |
1.93e-58 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 213.82 E-value: 1.93e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2569 ELFRAAARRAPDHVAVV----DGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYV 2644
Cdd:COG0365 13 NCLDRHAEGRGDKVALIwegeDGEERTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHS 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2645 PIDPDYPAERVASMIEDSGAVLglsVLASGDL--PGQEFEWMRLDDDSVAA------------EIAAVPAGPITDAERL- 2709
Cdd:COG0365 93 PVFPGFGAEALADRIEDAEAKV---LITADGGlrGGKVIDLKEKVDEALEElpslehvivvgrTGADVPMEGDLDWDELl 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2710 --------GEVTAAN-LAYVIYTSGSTGRPKGVAVTHSGLANFARQESD---RLNAGDnpVVLGFASPSFdASVLEYLL- 2776
Cdd:COG0365 170 aaasaefePEPTDADdPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKyvlDLKPGD--VFWCTADIGW-ATGHSYIVy 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2777 ------ATV--NEGTLAYrPSeavgGEVLERFIAEHGATHTFLTPSVLSTM---DPTAV-----PSLRVIAAGGEAVPQP 2840
Cdd:COG0365 247 gpllngATVvlYEGRPDF-PD----PGRLWELIEKYGVTVFFTAPTAIRALmkaGDEPLkkydlSSLRLLGSAGEPLNPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2841 IVDRWAPAT--ELHNLYGPTETTiGITISSamRPGDPVR---LGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALS-- 2913
Cdd:COG0365 322 VWEWWYEAVgvPIVDGWGQTETG-GIFISN--LPGLPVKpgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGPWPGmf 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2914 RGYLDRSGLTAERFTANPYGtagqrMYRTGDVVRWTPDtdtGGLTleYTGRSDDQVKLRGLRIELGEIEAVLAEHDAV-E 2992
Cdd:COG0365 399 RGYWNDPERYRETYFGRFPG-----WYRTGDGARRDED---GYFW--ILGRSDDVINVSGHRIGTAEIESALVSHPAVaE 468
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 2993 SAVVlGV----GGSVataLAAYIVPVDGAVE----VSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:COG0365 469 AAVV-GVpdeiRGQV---VKAFVVLKPGVEPsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
2107-2535 |
8.04e-58 |
|
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: 207.69 E-value: 8.04e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2107 WPMTPLQQGLFFQADLantvadHDAIDVYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPSGAAVTVVPAEV 2186
Cdd:cd19536 2 YPLSSLQEGMLFHSLL------NPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGQPVQVVHRQA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2187 TVPWSVIDLRAEDAAslDSRVEEVLATERTNPFDMAKPPLIRVVLVEHGDGA--ELVVTNHHLLIDGWSSPLVLADLLSL 2264
Cdd:cd19536 76 QVPVTELDLTPLEEQ--LDPLRAYKEETKIRRFDLGRAPLVRAALVRKDERErfLLVISDHHSILDGWSLYLLVKEILAV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2265 Y-ATGQTFTGSLPGTSG-RDFADHARAvaTADVEAGIAAWREVLAPVTEPTLVAPgHEPSADAPPRDHQFSIDVKVTERL 2342
Cdd:cd19536 154 YnQLLEYKPLSLPPAQPyRDFVAHERA--SIQQAASERYWREYLAGATLATLPAL-SEAVGGGPEQDSELLVSVPLPVRS 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2343 EALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRSPDIEGMESMVGMFINTIPAVVDVnPDATVVDVLTAVQN 2422
Cdd:cd19536 231 RSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2423 DKVKVLDHQQIGLPRLVAQTGLPALFDTLAVYESFPVnVDSVAGIDASSAGGLKLVGAKTSdaTHYPLNLSASRRGAELA 2502
Cdd:cd19536 310 QELESLSHEQVPLADIQRCSEGEPLFDSIVNFRHFDL-DFGLPEWGSDEGMRRGLLFSEFK--SNYDVNLSVLPKQDRLE 386
|
410 420 430
....*....|....*....|....*....|...
gi 1827387616 2503 LKLKYLPTAFAPEQVAVFADVLTGLLGAIADHP 2535
Cdd:cd19536 387 LKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
2564-3067 |
1.54e-57 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 209.66 E-value: 1.54e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2564 PVTLAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAY 2643
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYFD-GRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2644 VPIDPDYPAERVASMIEDSGAVL------GLSVLAS--GDLPGQEFeWMRLDDDSVAAEIAAVP-------AGPIT-DAE 2707
Cdd:PRK06187 84 HPINIRLKPEEIAYILNDAEDRVvlvdseFVPLLAAilPQLPTVRT-VIVEGDGPAAPLAPEVGeyeellaAASDTfDFP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2708 RLGEVTAANLayvIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFAsPSF--DASVLEYLlATVNEGTL- 2784
Cdd:PRK06187 163 DIDENDAAAM---LYTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDDVYLVIV-PMFhvHAWGLPYL-ALMAGAKQv 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2785 ---AYRPSEAVggevleRFIAEHGATHTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRWA--PATELHN 2853
Cdd:PRK06187 238 iprRFDPENLL------DLIETERVTFFFAVPTIWQMLlkapraYFVDFSSLRLVIYGGAALPPALLREFKekFGIDLVQ 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2854 LYGPTETTIGITIS---SAMRPGDPVRL--GGPIGGVDLMVLDERLRPVPV--GMPGELYVAGGALSRGYLDRSGLTAER 2926
Cdd:PRK06187 312 GYGMTETSPVVSVLppeDQLPGQWTKRRsaGRPLPGVEARIVDDDGDELPPdgGEVGEIIVRGPWLMQGYWNRPEATAET 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2927 FTANpygtagqrMYRTGDVVRWTPDtdtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-----GG 3001
Cdd:PRK06187 392 IDGG--------WLHTGDVGYIDED---GYLYI--TDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVpdekwGE 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 3002 SVAtalaAYIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVLEAG 3067
Cdd:PRK06187 459 RPV----AVVVLKPGAtLDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYAEGK 521
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
2-468 |
4.81e-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: 206.17 E-value: 4.81e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSD 81
Cdd:cd17654 18 SYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNKE 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 GEAEARSRFDDivdvhvldisspgdadldEEEFAGPTrPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTA 161
Cdd:cd17654 98 LDNAPLSFTPE------------------HRHFNIRT-DECLAYVIHTSGTTGTPKIVAVPHKCILPNIQHFRSLFNITS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 162 RDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLAD-LIRRHGVTVIHFVPAMLAAF------NEVLGAgv 234
Cdd:cd17654 159 EDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADiLFKRHRITVLQATPTLFRRFgsqsikSTVLSA-- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 235 geLTSLRLIQTGGEAL-TPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREv 313
Cdd:cd17654 237 --TSSLRVLALGGEPFpSLVILSSWRGKGNRTRIFNIYGITEVSCWALAYKVPEEDSPVQLGSPLLGTVIEVRDQNGSE- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 314 pigVPGELYLGGvqLARGYagrpdltaerFVADPFGEPGARLYRTGDRARwNRDGEIEYLGRTDFQVKLRGQRLELGEVE 393
Cdd:cd17654 314 ---GTGQVFLGG--LNRVC----------ILDDEVTVPKGTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLIQ 377
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 394 AALAAAPGVLHAAAAVVDgpgGQQLVGYLAPADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd17654 378 QVIESCLGVESCAVTLSD---QQRLIAFIVGESSSSRIHKELQLTLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1049-1530 |
7.03e-57 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 209.20 E-value: 7.03e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1049 DPDHPALICDGTEMD-----YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPAD 1123
Cdd:COG0365 22 RGDKVALIWEGEDGEertltYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1124 RIAYMLEDSGATVGITDASTR--------------ARLGESSCE----------------WVDLADLEAEAESGDDITDT 1173
Cdd:COG0365 102 ALADRIEDAEAKVLITADGGLrggkvidlkekvdeALEELPSLEhvivvgrtgadvpmegDLDWDELLAAASAEFEPEPT 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1174 ERNgsvrltNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTpedEPDTRILHVASPSF---DASMFEMAWAip 1250
Cdd:COG0365 182 DAD------DPLFILYTSGTTGKPKGVVHTHGGYLVHAATTAKYVLDL---KPGDVFWCTADIGWatgHSYIVYGPLL-- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1251 AGHTLVIAPQADFAGDA--LATVLERDEVTDMIITPSVLATV----DPERAQY----VRNLATGGEACPPELVERWSER- 1319
Cdd:COG0365 251 NGATVVLYEGRPDFPDPgrLWELIEKYGVTVFFTAPTAIRALmkagDEPLKKYdlssLRLLGSAGEPLNPEVWEWWYEAv 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1320 GRRIFNCYGPTEAT-VWATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYL--STAGLARGYLGRPGQTAV 1396
Cdd:COG0365 331 GVPIVDGWGQTETGgIFISNLPGLPVKPGSMGKPVPGYDVAVVDEDGNPVPPGEEGELVIkgPWPGMFRGYWNDPERYRE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1397 SFVADPFGepgarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhTE 1476
Cdd:COG0365 411 TYFGRFPG-----WYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVVGVPDEIRG---QV 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 1477 VVAYLVAKPGATiDSAAVLDEAAQH----LAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:COG0365 483 VKAFVVLKPGVE-PSDELAKELQAHvreeLGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
571-996 |
1.52e-56 |
|
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: 203.97 E-value: 1.52e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 571 LPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRT--VYPSVGAaPVQDVLP-VAVARE 647
Cdd:cd19543 2 YPLSPMQEGMLFHSLLDPGSGAYVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTsfVWEGLGE-PLQVVLKdRKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 648 QLDWREADSVES-------LVRSTTEGFDVSTQMPLRGRFHRDGAGLHVAL-TMHHIAMDGQSIPVLARDLMSAYAARAE 719
Cdd:cd19543 81 ELDLSHLSEAEQeaelealAEEDRERGFDLARAPLMRLTLIRLGDDRYRLVwSFHHILLDGWSLPILLKELFAIYAALGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 720 GRTGGLPVlDVQYADYALWqqsvLGDADDEtsvlgEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVEFDDDLA 799
Cdd:cd19543 161 GQPPSLPP-VRPYRDYIAW----LQRQDKE-----AAEAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 800 DRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRND--PALEELIGMFVNTLLLRTQVDPGHSVGDLLGN 877
Cdd:cd19543 231 ARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGRPAelPGIETMVGLFINTLPVRVRLDPDQTVLELLKD 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 878 VRTTVLDAFANDQVQFDElIEAlapeRSSSHQPLAQIAFTYTEPTVNDVAGLEAsgiQAAPVDTGVVNAK----FDLTVA 953
Cdd:cd19543 311 LQAQQLELREHEYVPLYE-IQA----WSEGKQALFDHLLVFENYPVDESLEEEQ---DEDGLRITDVSAEeqtnYPLTVV 382
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1827387616 954 VrarSGGTPMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd19543 383 A---IPGEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAAN 422
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1050-1530 |
7.28e-56 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 202.70 E-value: 7.28e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMD----YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRI 1125
Cdd:cd17654 1 PDRPALIIDQTTSDttvsYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1126 AYMLEDSGatvgitdastrarlgesscewvdLADLEAEAESGD---DITDTERNGSVRLT-NLAYLIYTSGSTGRPKAVG 1201
Cdd:cd17654 81 LTVMKKCH-----------------------VSYLLQNKELDNaplSFTPEHRHFNIRTDeCLAYVIHTSGTTGTPKIVA 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1202 VSHTGIVDFVNSLAKITTGTPEDepdtrILHVASP-SFDASMFEMAWAIPAGHTLVIAPQADFAGDA-LATVL-ERDEVT 1278
Cdd:cd17654 138 VPHKCILPNIQHFRSLFNITSED-----ILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSkLADILfKRHRIT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1279 DMIITPSVLATVDPERAQY--------VRNLATGGEACPPELV-ERWSERGRR--IFNCYGPTEATVWATRSRMTAGK-P 1346
Cdd:cd17654 213 VLQATPTLFRRFGSQSIKStvlsatssLRVLALGGEPFPSLVIlSSWRGKGNRtrIFNIYGITEVSCWALAYKVPEEDsP 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1347 VTIGKPVDGFTVRVLDGRLHEVPqgvvGELYLstAGLARGYlgrpgqtavsFVADPFGEPGARMYATGDLVRVaKGGNLE 1426
Cdd:cd17654 293 VQLGSPLLGTVIEVRDQNGSEGT----GQVFL--GGLNRVC----------ILDDEVTVPKGTMRATGDFVTV-KDGELF 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1427 FAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRggrkhteVVAYLVAKPgatiDSAAVLDEAAQH-LAAH 1505
Cdd:cd17654 356 FLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVTLSDQQR-------LIAFIVGES----SSSRIHKELQLTlLSSH 424
|
490 500
....*....|....*....|....*
gi 1827387616 1506 MVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd17654 425 AIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
2579-3059 |
8.31e-56 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 202.70 E-value: 8.31e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2579 PDHVAV---VDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERV 2655
Cdd:cd17654 1 PDRPALiidQTTSDTTVSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2656 ASMIEDSGavlgLSVLASGDLPGQEFEWMrldddsvaaeiaavpagpITDAERLGEVTAANLAYVIYTSGSTGRPKGVAV 2735
Cdd:cd17654 81 LTVMKKCH----VSYLLQNKELDNAPLSF------------------TPEHRHFNIRTDECLAYVIHTSGTTGTPKIVAV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2736 THSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEA-VGGEVLERFIAE-HGATHTFLTP 2813
Cdd:cd17654 139 PHKCILPNIQHFRSLFNITSEDILFLTSPLTFDPSVVEIFLSLSSGATLLIVPTSVkVLPSKLADILFKrHRITVLQATP 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2814 SVL----------STMdpTAVPSLRVIAAGGEAVPQPIVDR-WAPA---TELHNLYGPTETTIGITISSAMRPGDPVRLG 2879
Cdd:cd17654 219 TLFrrfgsqsiksTVL--SATSSLRVLALGGEPFPSLVILSsWRGKgnrTRIFNIYGITEVSCWALAYKVPEEDSPVQLG 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2880 GPIGGVDLMVLDERlrpvpvGMPGELYVAGGALSRGYldrsgltaerFTANPYGTAGQRMYRTGDVVRWTPDTdtggltL 2959
Cdd:cd17654 297 SPLLGTVIEVRDQN------GSEGTGQVFLGGLNRVC----------ILDDEVTVPKGTMRATGDFVTVKDGE------L 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2960 EYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLgvgGSVATALAAYIV-PVDGAVEVSELKAFaggRLPAYMVPS 3038
Cdd:cd17654 355 FFLGRKDSQIKRRGKRINLDLIQQVIESCLGVESCAVT---LSDQQRLIAFIVgESSSSRIHKELQLT---LLSSHAIPD 428
|
490 500
....*....|....*....|.
gi 1827387616 3039 SFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd17654 429 TFVQIDKLPLTSHGKVDKSEL 449
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
50-468 |
4.55e-55 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 202.05 E-value: 4.55e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 50 GH-FVPLDEQLPVDRARYMVRTAGVRLVVVTSDgeaearsrFD-DIVDVHVLDISspgdaDLDEEEFAGPTRPANAA--- 124
Cdd:PRK04813 76 GHaYIPVDVSSPAERIEMIIEVAKPSLIIATEE--------LPlEILGIPVITLD-----ELKDIFATGNPYDFDHAvkg 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 125 ----FTLFTSGSTGRPKAVVITHrgiANRLA-AD--IEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGR 197
Cdd:PRK04813 143 ddnyYIIFTSGTTGKPKGVQISH---DNLVSfTNwmLEDFALPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDM 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 198 HGDPVHLADLIRRHGVTVIHFVPA------MLAAFNEVLgagvgeLTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQY 271
Cdd:PRK04813 220 TANFKQLFETLPQLPINVWVSTPSfadmclLDPSFNEEH------LPNLTHFLFCGEELPHKTAKKLLERFPSATIYNTY 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 272 GPAEASIVVTIHRVTQD-----DRViPIGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFvad 346
Cdd:PRK04813 294 GPTEATVAVTSIEITDEmldqyKRL-PIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAF--- 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 347 pFGEPGARLYRTGDRARWNrDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDgPGG--QQLVGYLAP 424
Cdd:PRK04813 370 -FTFDGQPAYHTGDAGYLE-DGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYN-KDHkvQYLIAYVVP 446
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 425 ADVDVDTVAATT-------AELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK04813 447 KEEDFEREFELTkaikkelKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1035-1532 |
1.11e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 201.29 E-value: 1.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1035 EAGTLIDVLAQR-DLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAY 1113
Cdd:PRK07656 3 EWMTLPELLARAaRRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1114 VPVDPAYPADRIAYMLEDSGATVGI-------TDASTRARLGE----SSCEWVDLADLEAEAESGDDI----TDTERNGS 1178
Cdd:PRK07656 83 VPLNTRYTADEAAYILARGDAKALFvlglflgVDYSATTRLPAlehvVICETEEDDPHTEKMKTFTDFlaagDPAERAPE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1179 VRLTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtRILhVASPSFDASMFEMAWAIP--AGHTLV 1256
Cdd:PRK07656 163 VDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLGLTEGD----RYL-AANPFFHVFGYKAGVNAPlmRGATIL 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1257 IAPQadFAGDALATVLERDEVTdmiitpsVLATVD---------PERAQY----VRNLATGGEACPPELVERWSERgrri 1323
Cdd:PRK07656 238 PLPV--FDPDEVFRLIETERIT-------VLPGPPtmynsllqhPDRSAEdlssLRLAVTGAASMPVALLERFESE---- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1324 FNC------YGPTEATVWAT-----RSRMTAgkPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPG 1392
Cdd:PRK07656 305 LGVdivltgYGLSEASGVTTfnrldDDRKTV--AGTIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1393 QTAVSFVADPFgepgarMYaTGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGr 1472
Cdd:PRK07656 383 ATAAAIDADGW------LH-TGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDERLG- 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 1473 khtEVV-AYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:PRK07656 455 ---EVGkAYVVLKPGAELTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1050-1535 |
2.87e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 200.03 E-value: 2.87e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:PRK06187 20 PDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYIL 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDAST-------RARL--------------GESSCEWVDLADLEAEAESGDDITDTERNgsvrltNLAYLI 1188
Cdd:PRK06187 100 NDAEDRVVLVDSEFvpllaaiLPQLptvrtvivegdgpaAPLAPEVGEYEELLAAASDTFDFPDIDEN------DAAAML 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1189 YTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtRILhVASPSFDAsmfeMAWAIP-----AGHTLVIAPQADF 1263
Cdd:PRK06187 174 YTSGTTGHPKGVVLSHRNLFLHSLAVCAWLKLSRDD----VYL-VIVPMFHV----HAWGLPylalmAGAKQVIPRRFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1264 agDALATVLERDEVTDMIITPSVLATV--DPERAQY----VRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWA 1336
Cdd:PRK06187 245 --ENLLDLIETERVTFFFAVPTIWQMLlkAPRAYFVdfssLRLVIYGGAALPPALLREFKEKfGIDLVQGYGMTETSPVV 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1337 TRSRMTAG------KPVTIGKPVDGFTVRVLDGRLHEVP--QGVVGELYLSTAGLARGYLGRPGQTAVSFVADpfgepga 1408
Cdd:PRK06187 323 SVLPPEDQlpgqwtKRRSAGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG------- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1409 rMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPGAT 1488
Cdd:PRK06187 396 -WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKWGE---RPVAVVVLKPGAT 471
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1827387616 1489 IDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEPHA 1535
Cdd:PRK06187 472 LDAKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQYA 518
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
573-809 |
7.78e-54 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 189.48 E-value: 7.78e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 573 LSRAQRRMWFLnqfDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDVLP---VAVAREQL 649
Cdd:COG4908 1 LSPAQKRFLFL---EPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPdadLPLEVVDL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 650 -----DWREADSVESLVRSTTEGFDVSTQMPLRGRFHRDGAGLHV-ALTMHHIAMDGQSIPVLARDLMSAYAARAEGRTG 723
Cdd:COG4908 78 salpePEREAELEELVAEEASRPFDLARGPLLRAALIRLGEDEHVlLLTIHHIISDGWSLGILLRELAALYAALLEGEPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 724 GLPVLDVQYADYALWQQSVLGDADdetsvLGEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVEFDDDLADRVD 803
Cdd:COG4908 158 PLPELPIQYADYAAWQRAWLQSEA-----LEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALK 232
|
....*.
gi 1827387616 804 VLARSN 809
Cdd:COG4908 233 ALAKAH 238
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1059-1531 |
4.54e-52 |
|
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: 190.97 E-value: 4.54e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1059 GTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGI 1138
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1139 TDastrarlgesscewvdladleaeaesgdditdterngsvrltnLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKIT 1218
Cdd:cd05934 81 VD-------------------------------------------PASILYTSGTTGPPKGVVITHANLTFAGYYSARRF 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1219 TGTPEDepdtrILHVASPSF--DASMFEMAWAIPAGHTLVIAPQadFAGDALATVLERDEVTDMIITPSVLATV--DPER 1294
Cdd:cd05934 118 GLGEDD-----VYLTVLPLFhiNAQAVSVLAALSVGATLVLLPR--FSASRFWSDVRRYGATVTNYLGAMLSYLlaQPPS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1295 AQYVRNL--ATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQG 1371
Cdd:cd05934 191 PDDRAHRlrAAYGAPNPPELHEEFEERfGVRLLEGYGMTETIVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1372 VVGELYLSTA---GLARGYLGRPGQTAVSFvadpfgEPGarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIE 1448
Cdd:cd05934 271 EPGELVIRGLrgwGFFKGYYNMPEATAEAM------RNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1449 AVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRA 1528
Cdd:cd05934 343 RAILRHPAVREAAVVAVPDEVGED---EVKAVVVLRPGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKA 419
|
...
gi 1827387616 1529 ALP 1531
Cdd:cd05934 420 QLR 422
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
2566-3059 |
2.36e-51 |
|
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: 191.53 E-value: 2.36e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVP 2645
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHH-DRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2646 IDPDYPAERVASMIEDSGAVL------GLSVLASGDLPGQEFEWMRLDDDSVAAEIAAVPAGPIT--------DAERLGE 2711
Cdd:TIGR03098 80 INPLLKAEQVAHILADCNVRLlvtsseRLDLLHPALPGCHDLRTLIIVGDPAHASEGHPGEEPASwpkllalgDADPPHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2712 VTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASvleyllatVNEGTLAYrpseA 2791
Cdd:TIGR03098 160 VIDSDMAAILYTSGSTGRPKGVVLSHRNLVAGAQSVATYLENRPDDRLLAVLPLSFDYG--------FNQLTTAF----Y 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2792 VGGEV----------LERFIAEHGATHTFLTPSV---LSTMD--PTAVPSLRVIAAGGEAVPQPIVDR---WAPATELHN 2853
Cdd:TIGR03098 228 VGATVvlhdyllprdVLKALEKHGITGLAAVPPLwaqLAQLDwpESAAPSLRYLTNSGGAMPRATLSRlrsFLPNARLFL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2854 LYGPTETTIGITISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPyG 2933
Cdd:TIGR03098 308 MYGLTEAFRSTYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLP-P 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2934 TAGQrMYRTGDVVrWTPDT---DTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGG-SVATALAA 3009
Cdd:TIGR03098 387 FPGE-LHLPELAV-WSGDTvrrDEEGF-LYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGVPDpTLGQAIVL 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 3010 YIVP-VDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:TIGR03098 464 VVTPpGGEELDRAALLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
2-468 |
4.29e-51 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 191.86 E-value: 4.29e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRlVVVTSD 81
Cdd:COG0365 41 TYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGFGAEALADRIEDAEAK-VLITAD 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 G------EAEARSRFDDIVD-----VHVL-------DISSPGDADLDE------EEF-AGPTRPANAAFTLFTSGSTGRP 136
Cdd:COG0365 120 GglrggkVIDLKEKVDEALEelpslEHVIvvgrtgaDVPMEGDLDWDEllaaasAEFePEPTDADDPLFILYTSGTTGKP 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 137 KAVVITHRGIANRLAADIE-QYDLTARDVFLYKAP---ITFDVSVreIFLPIAIGATLVIAEpGR--HGDPVHLADLIRR 210
Cdd:COG0365 200 KGVVHTHGGYLVHAATTAKyVLDLKPGDVFWCTADigwATGHSYI--VYGPLLNGATVVLYE-GRpdFPDPGRLWELIEK 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 211 HGVTVIHFVPAMLAAFnevLGAGVGE-----LTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAE-ASIVVTIHR 284
Cdd:COG0365 277 YGVTVFFTAPTAIRAL---MKAGDEPlkkydLSSLRLLGSAGEPLNPEVWEWWYEAV-GVPIVDGWGQTEtGGIFISNLP 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 285 VTQddrVIPiGTPTRRV---SARVLDAALREVPIGVPGELYLGG--VQLARGYAGRPDLTAERFVADPFGepgarLYRTG 359
Cdd:COG0365 353 GLP---VKP-GSMGKPVpgyDVAVVDEDGNPVPPGEEGELVIKGpwPGMFRGYWNDPERYRETYFGRFPG-----WYRTG 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 360 DRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGP---GGQQLVGYLAPADvDVDTVAATT 436
Cdd:COG0365 424 DGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAV--AEAAVVGVPdeiRGQVVKAFVVLKP-GVEPSDELA 500
|
490 500 510
....*....|....*....|....*....|....*....
gi 1827387616 437 AEL-------LPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:COG0365 501 KELqahvreeLGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1050-1530 |
1.21e-50 |
|
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: 189.12 E-value: 1.21e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDASTRARLG------ESSCEWVDLADLEAEAESGDDITDTERNGSVRLT-------NLAYLIYTSGSTGR 1196
Cdd:cd05959 98 EDSRARVVVVSGELAPVLAaaltksEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKpaathadDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1197 PKAVGVSHTGIVDFVNSLAKITTGTPEDEpdtRILHVASPSF-----DASMFEMAwaipAGHTLVIAPQADfAGDALATV 1271
Cdd:cd05959 178 PKGVVHLHADIYWTAELYARNVLGIREDD---VCFSAAKLFFayglgNSLTFPLS----VGATTVLMPERP-TPAAVFKR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1272 LERDEVTDMIITPSVLA--TVDPERAQY----VRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAG 1344
Cdd:cd05959 250 IRRYRPTVFFGVPTLYAamLAAPNLPSRdlssLRLCVSAGEALPAEVGERWKARfGLDILDGIGSTEMLHIFLSNRPGRV 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1345 KPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVadpfGEpgarMYATGDLVRVAKGGN 1424
Cdd:cd05959 330 RYGTTGKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ----GE----WTRTGDKYVRDDDGF 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1425 LEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGgrkHTEVVAYLVAKPGATiDSAAVLDEAAQH--- 1501
Cdd:cd05959 402 YTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDG---LTKPKAFVVLRPGYE-DSEALEEELKEFvkd 477
|
490 500 510
....*....|....*....|....*....|
gi 1827387616 1502 -LAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd05959 478 rLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
2106-2535 |
4.23e-50 |
|
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: 185.21 E-value: 4.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2106 VWPMTPLQQGLFFQADLAntvADHDAidvYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPSGAAVTVVPAE 2185
Cdd:cd19547 1 VYPLAPMQEGMLFRGLFW---PDSDA---YFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDRAEPLQYVRDD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2186 VTVPWSVIDLRAEDAASLDSRVEEVLATERTNPFDMAKPPLIRVVLVEHGDGAE-LVVTNHHLLIDGWSSPLVLADLLSL 2264
Cdd:cd19547 75 LAPPWALLDWSGEDPDRRAELLERLLADDRAAGLSLADCPLYRLTLVRLGGGRHyLLWSHHHILLDGWCLSLIWGDVFRV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2265 Y---ATGQTFTGSlPGTSGRDFADHARAvATADVEAGIAAWREVLAPVTePTlvapghePSADAPP-RDHQFSIDV---- 2336
Cdd:cd19547 155 YeelAHGREPQLS-PCRPYRDYVRWIRA-RTAQSEESERFWREYLRDLT-PS-------PFSTAPAdREGEFDTVVhefp 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2337 -KVTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRSPDIEGMESMVGMFINTIPAVVDVNPDATVVD 2415
Cdd:cd19547 225 eQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRPPELEGSEHMVGIFINTIPLRIRLDPDQTVTG 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2416 VLTAVQNDKVKVLDHQQIGLPRLVAQTGLPAL-----FDTLAVYESFPvnVDSVAGIDASsaggLKLVGAKTSDATHYPL 2490
Cdd:cd19547 305 LLETIHRDLATTAAHGHVPLAQIKSWASGERLsggrvFDNLVAFENYP--EDNLPGDDLS----IQIIDLHAQEKTEYPI 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1827387616 2491 NLSASRRgAELALKLKYLPTAFAPEQVAVFADVLTGLLGAIADHP 2535
Cdd:cd19547 379 GLIVLPL-QKLAFHFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1053-1530 |
8.65e-50 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 184.59 E-value: 8.65e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1053 PALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDS 1132
Cdd:cd05919 2 TAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDC 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1133 GATVGITDAstrarlgesscewvdladleaeaesgDDItdterngsvrltnlAYLIYTSGSTGRPKAVGVSHTGIVDFVN 1212
Cdd:cd05919 82 EARLVVTSA--------------------------DDI--------------AYLLYSSGTTGPPKGVMHAHRDPLLFAD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1213 SLAKITTG-TPEDepdtRILHVASPSFDASMFEMAW-AIPAGHTLVIAPQADFAGDALATvLERDEVTDMIITPSVLATV 1290
Cdd:cd05919 122 AMAREALGlTPGD----RVFSSAKMFFGYGLGNSLWfPLAVGASAVLNPGWPTAERVLAT-LARFRPTVLYGVPTFYANL 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1291 DPERAQY------VRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDG 1363
Cdd:cd05919 197 LDSCAGSpdalrsLRLCVSAGEALPRGLGERWMEHfGGPILDGIGATEVGHIFLSNRPGAWRLGSTGRPVPGYEIRLVDE 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1364 RLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADpfgepgarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVE 1443
Cdd:cd05919 277 EGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG--------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVS 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1444 LGEIEAVLDAQPGVAQSVVVGVESTRGGRKHTevvAYLVAKPGATIDSA---AVLDEAAQHLAAHMVPSQAIVIDEIPLT 1520
Cdd:cd05919 349 PVEVESLIIQHPAVAEAAVVAVPESTGLSRLT---AFVVLKSPAAPQESlarDIHRHLLERLSAHKVPRRIAFVDELPRT 425
|
490
....*....|
gi 1827387616 1521 PAGKLDRAAL 1530
Cdd:cd05919 426 ATGKLQRFKL 435
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
13-573 |
1.24e-49 |
|
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: 195.67 E-value: 1.24e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 13 LARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDR-----------ARYMVRTAGV--RLVVVT 79
Cdd:TIGR03443 283 LAHYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsvakprALIVIEKAGTldQLVRDY 362
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 80 SDGEAEARSRFDDI------------VDVHVLDISSPGDADLDEEE--FAGPTRPAnaafTL-FTSGSTGRPKAVVITHR 144
Cdd:TIGR03443 363 IDKELELRTEIPALalqddgslvggsLEGGETDVLAPYQALKDTPTgvVVGPDSNP----TLsFTSGSEGIPKGVLGRHF 438
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 145 GIANRLAADIEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMla 224
Cdd:TIGR03443 439 SLAYYFPWMAKRFGLSENDKFTMLSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPGRLAEWMAKYGATVTHLTPAM-- 516
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 225 afNEVLGAG-VGELTSLRLIQTGGEALTppvARDLMvRL----PGTRLQNQYGPAEASIVVTIHRV-----------TQD 288
Cdd:TIGR03443 517 --GQLLSAQaTTPIPSLHHAFFVGDILT---KRDCL-RLqtlaENVCIVNMYGTTETQRAVSYFEIpsrssdstflkNLK 590
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 289 DrVIPIGTPTRRVSARVLDAALREVPIGVP--GELYLGGVQLARGYAGRPDLTAERFVADPFGEPGA------------- 353
Cdd:TIGR03443 591 D-VMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPSHwidldkennkper 669
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 354 --------RLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVV-DGPGGQQLVGYLAP 424
Cdd:TIGR03443 670 efwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRrDKDEEPTLVSYIVP 749
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 425 AD---------VDVDTVAATTA---------EL-----------LPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEPEIAP 475
Cdd:TIGR03443 750 QDksdeleefkSEVDDEESSDPvvkglikyrKLikdireylkkkLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPDTAQ 829
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 476 TLYVPPG----------NADEETVAGLFAELL--GVERVGVTDSFFDIGGSSLSAARIAARVSKELGVDVSVRDVFESPS 543
Cdd:TIGR03443 830 LAAVAKNrsasaadeefTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPT 909
|
650 660 670
....*....|....*....|....*....|..
gi 1827387616 544 VRGLVHAVSG--RGSALPSVKRIEPRPERLPL 573
Cdd:TIGR03443 910 IKGFAKEVDRlkKGEELADEGDSEIEEEETVL 941
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1-468 |
1.20e-48 |
|
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: 182.38 E-value: 1.20e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:cd05936 25 LTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLYTPRELEHILNDSGAKALIVAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DgeaearsrFDDIVDvhvldisspgdADLDEEEFAGPTRPANAAFtLFTSGSTGRPKAVVITHRGI-ANRLAAD-IEQYD 158
Cdd:cd05936 105 S--------FTDLLA-----------AGAPLGERVALTPEDVAVL-QYTSGTTGVPKGAMLTHRNLvANALQIKaWLEDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 159 LTARDVFLYKAPI--TFDVSVrEIFLPIAIGATLVIaEPgrHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGE 236
Cdd:cd05936 165 LEGDDVVLAALPLfhVFGLTV-ALLLPLALGATIVL-IP--RFRPIGVLKEIRKHRVTIFPGVPTMYIALLNAPEFKKRD 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 237 LTSLRLIQTGGEALTPPVARDLmVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIG 316
Cdd:cd05936 241 FSSLRLCISGGAPLPVEVAERF-EELTGVPIVEGYGLTETSPVVAVNPLDGPRKPGSIGIPLPGTEVKIVDDDGEELPPG 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 317 VPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlyRTGDRARWNRDGEIEYLGR-TD------FQVKLRgqrlel 389
Cdd:cd05936 320 EVGELWVRGPQVMKGYWNRPEETAEAFVDGWL--------RTGDIGYMDEDGYFFIVDRkKDmiivggFNVYPR------ 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 390 gEVEAALAAAPGVLHAAAA-VVDGPGGQQLVGYLAPAD---VDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDR 465
Cdd:cd05936 386 -EVEEVLYEHPAVAEAAVVgVPDPYSGEAVKAFVVLKEgasLTEEEIIAFCREQLAGYKVPRQVEFRDELPKSAVGKILR 464
|
...
gi 1827387616 466 RLL 468
Cdd:cd05936 465 REL 467
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
2562-3061 |
1.88e-48 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 182.80 E-value: 1.88e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2562 TDPVTLAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGG 2641
Cdd:PRK07656 2 NEWMTLPELLARAARRFGDKEAYVFG-DQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2642 AYVPIDPDYPAERVASMIEDSGA--------VLGLSVLASGDLPGQEFEWMRLDDDSVAAEIAAVPAGPI----TDAERL 2709
Cdd:PRK07656 81 VVVPLNTRYTADEAAYILARGDAkalfvlglFLGVDYSATTRLPALEHVVICETEEDDPHTEKMKTFTDFlaagDPAERA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2710 GEVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRL--NAGDNPVVlgfASPSF-----DASVLEYLLatvNEG 2782
Cdd:PRK07656 161 PEVDPDDVADILFTSGTTGRPKGAMLTHRQLLSNAADWAEYLglTEGDRYLA---ANPFFhvfgyKAGVNAPLM---RGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2783 TLAYRPSEAVgGEVLERfIAEHGATHTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRWAPATELHNL-- 2854
Cdd:PRK07656 235 TILPLPVFDP-DEVFRL-IETERITVLPGPPTMYNSLlqhpdrSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVlt 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2855 -YGPTETTIGITISsamRPGDPVRL-----GGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFT 2928
Cdd:PRK07656 313 gYGLSEASGVTTFN---RLDDDRKTvagtiGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAID 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2929 ANPYgtagqrmYRTGDVVRWTPDtdtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG----GSVA 3004
Cdd:PRK07656 390 ADGW-------LHTGDLGRLDEE---GYLYI--VDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPderlGEVG 457
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 3005 TalaAYIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPE 3061
Cdd:PRK07656 458 K---AYVVLKPGAeLTEEELIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
2566-3059 |
2.12e-47 |
|
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: 180.34 E-value: 2.12e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGayVP 2645
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDG-ERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IP 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2646 IDPdYPAER---VASMIEDSGAVLglsVLASGDLPGqefewmrLDDDSVAAEIAA-VP----------AGPITDAERLGE 2711
Cdd:COG1021 103 VFA-LPAHRraeISHFAEQSEAVA---YIIPDRHRG-------FDYRALARELQAeVPslrhvlvvgdAGEFTSLDALLA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2712 VTAANLAYVIYTS---------GSTGRPKGVAVTHSGLANFARQESD--RLNAGDN-----PVVLGF--ASPSFDAsVLe 2773
Cdd:COG1021 172 APADLSEPRPDPDdvaffqlsgGTTGLPKLIPRTHDDYLYSVRASAEicGLDADTVylaalPAAHNFplSSPGVLG-VL- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2774 YLLATVnegTLAYRPSeavgGEVLERFIAEHGATHTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRWAP 2847
Cdd:COG1021 250 YAGGTV---VLAPDPS----PDTAFPLIERERVTVTALVPPLALLWldaaerSRYDLSSLRVLQVGGAKLSPELARRVRP 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2848 A--TELHNLYGPTETTIGITissamRPGDPVRL-----GGPIGGVD-LMVLDERLRPVPVGMPGELYVAGGALSRGYLDR 2919
Cdd:COG1021 323 AlgCTLQQVFGMAEGLVNYT-----RLDDPEEVilttqGRPISPDDeVRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRA 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2920 SGLTAERFTANPYgtagqrmYRTGDVVRWTPDTDtggltLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV 2999
Cdd:COG1021 398 PEHNARAFTPDGF-------YRTGDLVRRTPDGY-----LVVEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVVAM 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 3000 -----GGSVAtalaAYIVPVDGAVEVSELKAFAGGR-LPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:COG1021 466 pdeylGERSC----AFVVPRGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
2108-2535 |
3.56e-47 |
|
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: 176.83 E-value: 3.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2108 PMTPLQQGLFFqadLANTVADHDAIDVYVTqtvLSLTGDVDPGRLRSALSELLARQRVLRSGFVRlPSGAAVTVVPAEVT 2187
Cdd:cd19066 3 PLSPMQRGMWF---LKKLATDPSAFNVAIE---MFLTGSLDLARLKQALDAVMERHDVLRTRFCE-EAGRYEQVVLDKTV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2188 VP-WSVIDLRaeDAASLDSRVEEVLATERTNPFDMAKPPLIRVVLVEHGD-GAELVVTNHHLLIDGWSSPLVLADLLSLY 2265
Cdd:cd19066 76 RFrIEIIDLR--NLADPEARLLELIDQIQQTIYDLERGPLVRVALFRLADeRDVLVVAIHHIIVDGGSFQILFEDISSVY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2266 --ATGQTFTGSLPGTSgrdFADHARAVATA----DVEAGIAAWREVLAPVTEPTLVAPGHEPS--ADAPPRDHQFSIDVK 2337
Cdd:cd19066 154 daAERQKPTLPPPVGS---YADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPLPKAKRPSqvASYEVLTLEFFLRSE 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2338 VTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRSPDieGMESMVGMFINTIPAVVDVNPDATVVDVL 2417
Cdd:cd19066 231 ETKRLREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDE--AVEDTIGLFLNLLPLRIDTSPDATFPELL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2418 TAVQNDKVKVLDHQQIGLPRLVAQTGL------PALFDTLAVYESFPvnvdSVAGIDASSAGGLKLVgaKTSDATHYPLN 2491
Cdd:cd19066 309 KRTKEQSREAIEHQRVPFIELVRHLGVvpeapkHPLFEPVFTFKNNQ----QQLGKTGGFIFTTPVY--TSSEGTVFDLD 382
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1827387616 2492 LSAS-RRGAELALKLKYLPTAFAPEQVAVFADVLTGLLGAIADHP 2535
Cdd:cd19066 383 LEASeDPDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1069-1530 |
7.82e-47 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341246 [Multi-domain] Cd Length: 457 Bit Score: 176.48 E-value: 7.82e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1069 TRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAA----YVPVDPAYPADRIAYMLEDSGATVGITDAS-- 1142
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLADAGaa 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1143 TRARLGESSC----EWVDladleaeaesGDDITDTERNGSVRLT---NLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLA 1215
Cdd:cd05922 81 DRLRDALPASpdpgTVLD----------ADGIRAARASAPAHEVsheDLALLLYTSGSTGSPKLVRLSHQNLLANARSIA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1216 KITTGTPEDepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFaGDALATVLERDEVTDMIITPSVLA-----TV 1290
Cdd:cd05922 151 EYLGITADD----RALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVL-DDAFWEDLREHGATGLAGVPSTYAmltrlGF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1291 DPERAQYVRNLATGGEACPPELVERWSE--RGRRIFNCYGPTEATvwatrSRMT-------AGKPVTIGKPVDGFTVRVL 1361
Cdd:cd05922 226 DPAKLPSLRYLTQAGGRLPQETIARLREllPGAQVYVMYGQTEAT-----RRMTylpperiLEKPGSIGLAIPGGEFEIL 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1362 DGRLHEVPQGVVGELYLSTAGLARGYLGRPgqtavSFVADPfGEPGARMYaTGDLVRVAKGGNLEFAGRADHQVKINGQR 1441
Cdd:cd05922 301 DDDGTPTPPGEPGEIVHRGPNVMKGYWNDP-----PYRRKE-GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNR 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1442 VELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhteVVAYLVAKPGatIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTP 1521
Cdd:cd05922 374 ISPTEIEAAARSIGLIIEAAAVGLPDPLGEK----LALFVTAPDK--IDPKDVLRSLAERLPPYKVPATVRVVDELPLTA 447
|
....*....
gi 1827387616 1522 AGKLDRAAL 1530
Cdd:cd05922 448 SGKVDYAAL 456
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
768-1604 |
1.05e-46 |
|
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: 186.42 E-value: 1.05e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 768 PAVTDLPMDRPRPAVLGTAGATVTVEFDDDLAdrvdvlARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPa 847
Cdd:TIGR03443 9 PTLSVLPHDYLRPANNRLVEATYSLQLPSAEV------TAGGGSTPFIILLAAFAALVYRLTGDEDIVLGTSSNKSGRP- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 848 leeligmfvntLLLRTQVDPGHSVGDLLGNVRTTVLDAFANDQVQFDELIEAL-APERSSSHQPLAQIAFtyteptvndv 926
Cdd:TIGR03443 82 -----------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIqAAKKLERTPPLFRLAF---------- 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 927 agLEASGIQAAPVDTGVVNakfDLTVAVRarSGGTPMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDDQNTAVGDIDI 1006
Cdd:TIGR03443 141 --QDAPDNQQTTYSTGSTT---DLTVFLT--PSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSL 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1007 VGAARAKSVSAPVSARTPGAMVG-------RGGEVEAGTLIDVLAQRDLDPDHPAlicdgTEMDYDEFETRTNAIARALL 1079
Cdd:TIGR03443 214 ITPSQKSLLPDPTKDLDWSGFRGaihdifaDNAEKHPDRTCVVETPSFLDPSSKT-----RSFTYKQINEASNILAHYLL 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1080 ARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSG--ATVGITDASTRARLGESSCE---- 1153
Cdd:TIGR03443 289 KTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARQTIYLSVAKprALIVIEKAGTLDQLVRDYIDkele 368
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1154 ------WVDLAD---LEA---EAESGDDITDTERNGSVRlTNL-------AYLIYTSGSTGRPKAVGVSHTGIVDFVNSL 1214
Cdd:TIGR03443 369 lrteipALALQDdgsLVGgslEGGETDVLAPYQALKDTP-TGVvvgpdsnPTLSFTSGSEGIPKGVLGRHFSLAYYFPWM 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1215 AKiTTGTPEDEPDTRILHVASPSFDASMFemawaIPA--GHTLVIaPQADFAGDA--LATVLERDEVTDMIITPS----- 1285
Cdd:TIGR03443 448 AK-RFGLSENDKFTMLSGIAHDPIQRDMF-----TPLflGAQLLV-PTADDIGTPgrLAEWMAKYGATVTHLTPAmgqll 520
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1286 -------------------VLATVDPERAQyvrNLAtggEACppelverwsergrRIFNCYGPTEA----TVWATRSR-- 1340
Cdd:TIGR03443 521 saqattpipslhhaffvgdILTKRDCLRLQ---TLA---ENV-------------CIVNMYGTTETqravSYFEIPSRss 581
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1341 -----------MTAGKPVtigKPVDGFTVRVLDgRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEPGA- 1408
Cdd:TIGR03443 582 dstflknlkdvMPAGKGM---KNVQLLVVNRND-RTQTCGVGEVGEIYVRAGGLAEGYLGLPELNAEKFVNNWFVDPSHw 657
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1409 --------------------RMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVgVEST 1468
Cdd:TIGR03443 658 idldkennkperefwlgprdRLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTL-VRRD 736
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1469 RGGRKhtEVVAYLVAKP-GATIDSAAVLDEAA-------------------------QHLAAHMVPSQAIVIDEIPLTPA 1522
Cdd:TIGR03443 737 KDEEP--TLVSYIVPQDkSDELEEFKSEVDDEessdpvvkglikyrklikdireylkKKLPSYAIPTVIVPLKKLPLNPN 814
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1523 GKLDRAALPEPH-------APEPAEYVAPA--NPAEDNLARIVAGLLGEE--RVSVTESFFALGGDSImsiqlssaakaa 1591
Cdd:TIGR03443 815 GKVDKPALPFPDtaqlaavAKNRSASAADEefTETEREIRDLWLELLPNRpaTISPDDSFFDLGGHSI------------ 882
|
970
....*....|...
gi 1827387616 1592 gihLSPREIFELK 1604
Cdd:TIGR03443 883 ---LATRMIFELR 892
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1-465 |
1.21e-46 |
|
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: 175.49 E-value: 1.21e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVvvts 80
Cdd:cd17631 21 LTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAYILADSGAKVL---- 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeaearsrFDDIvdvhvldisspgdadldeeefagptrpanaAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd17631 97 ---------FDDL------------------------------ALLMYTSGTTGRPKGAMLTHRNLLWNAVNALAALDLG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFLP-IAIGATLVIAepgRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTS 239
Cdd:cd17631 138 PDDVLLVVAPLFHIGGLGVFTLPtLLRGGTVVIL---RKFDPETVLDLIERHRVTSFFLVPTMIQALLQHPRFATTDLSS 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 240 LRLIQTGGEALTPPVARDLMVRlpGTRLQNQYGPAEASIVVTIHRVT-QDDRVIPIGTPTRRVSARVLDAALREVPIGVP 318
Cdd:cd17631 215 LRAVIYGGAPMPERLLRALQAR--GVKFVQGYGMTETSPGVTFLSPEdHRRKLGSAGRPVFFVEVRIVDPDGREVPPGEV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 319 GELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlyRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAA 398
Cdd:cd17631 293 GEIVVRGPHVMAGYWNRPEATAAAFRDGWF--------HTGDLGRLDEDGYLYIVDRKKDMIISGGENVYPAEVEDVLYE 364
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 399 APGVlhAAAAVV---DGPGGQQLVGYLAPAD---VDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDR 465
Cdd:cd17631 365 HPAV--AEVAVIgvpDEKWGEAVVAVVVPRPgaeLDEDELIAHCRERLARYKIPKSVEFVDALPRNATGKILK 435
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
570-996 |
3.08e-46 |
|
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: 174.04 E-value: 3.08e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 570 RLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDV---LPVAVAR 646
Cdd:cd20484 1 RSPLSEGQKGLWMLQKMSPEMSAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIepsKPLSFQE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 647 EQLDWREADSVESLVRS-TTEGFDVStQMPLRgRFH---RDGAGLHVALTMHHIAMDGQSIPVLARDLMSAYAARAEGRT 722
Cdd:cd20484 81 EDISSLKESEIIAYLREkAKEPFVLE-NGPLM-RVHlfsRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQALLQGKQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 723 GGLPVLDVQYADYALWQQSVLGDADDEtsvlgEQLSHWRRVLAG-LPaVTDLPMDRPRPAVLGTAGATVTVEFDDDLADR 801
Cdd:cd20484 159 PTLASSPASYYDFVAWEQDMLAGAEGE-----EHRAYWKQQLSGtLP-ILELPADRPRSSAPSFEGQTYTRRLPSELSNQ 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 802 VDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGDLLGNVRTT 881
Cdd:cd20484 233 IKSFARSQSINLSTVFLGIFKLLLHRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLT 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 882 VLDAFANDQVQFDELIEALAPERSSSHQPLAQIAFTYTEptvndvaGLEASGIQ--AAP---------VDTGVVNAKFDL 950
Cdd:cd20484 313 VLDGLDHAAYPFPAMVRDLNIPRSQANSPVFQVAFFYQN-------FLQSTSLQqfLAEyqdvlsiefVEGIHQEGEYEL 385
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1827387616 951 TVAVRARSGGtpMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd20484 386 VLEVYEQEDR--FTLNIKYNPDLFDASTIERMMEHYVKLAEELIAN 429
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
2564-3059 |
8.85e-46 |
|
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: 174.05 E-value: 8.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2564 PVTLAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAY 2643
Cdd:cd05920 14 DEPLGDLLARSAARHPDRIAVVDG-DRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2644 VPIDPDYPAERVASMIEDSGAVLglsvLASGDlpgqefEWMRLDDDSVAAEIAAVPAGPitdaerlgevtaanlAYVIYT 2723
Cdd:cd05920 93 VLALPSHRRSELSAFCAHAEAVA----YIVPD------RHAGFDHRALARELAESIPEV---------------ALFLLS 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2724 SGSTGRPKGVAVTHSGLANFARQ--ESDRLNAGD-----NPVVLGF--ASPsfdaSVLEYLLA--TVnegTLAYRPSEav 2792
Cdd:cd05920 148 GGTTGTPKLIPRTHNDYAYNVRAsaEVCGLDQDTvylavLPAAHNFplACP----GVLGTLLAggRV---VLAPDPSP-- 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2793 gGEVLErFIAEHGATHTFLTPSVLS------TMDPTAVPSLRVIAAGGEAVPQPIVDRWAPA--TELHNLYGPTETTIGI 2864
Cdd:cd05920 219 -DAAFP-LIEREGVTVTALVPALVSlwldaaASRRADLSSLRLLQVGGARLSPALARRVPPVlgCTLQQVFGMAEGLLNY 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2865 TissamRPGDPVRL-----GGPIGGVD-LMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYgtagqr 2938
Cdd:cd05920 297 T-----RLDDPDEViihtqGRPMSPDDeIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF------ 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2939 mYRTGDVVRWTPDtdtGGLTLEytGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSV-ATALAAYIVPVDGA 3017
Cdd:cd05920 366 -YRTGDLVRRTPD---GYLVVE--GRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGERSCAFVVLRDPP 439
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 1827387616 3018 VEVSELKAFAGGR-LPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05920 440 PSAAQLRRFLRERgLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
8-468 |
1.02e-45 |
|
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: 173.40 E-value: 1.02e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 8 RRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGH----FVPLDEQLPVDRARYMVRTAGVRLVVVtsdgE 83
Cdd:cd05922 1 LGVSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLA----D 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 AEARSRFDDivdvhVLDISSPGDADLDEEEFAGPTRPANA--------AFTLFTSGSTGRPKAVVITHRGIANRLAADIE 155
Cdd:cd05922 77 AGAADRLRD-----ALPASPDPGTVLDADGIRAARASAPAhevshedlALLLYTSGSTGSPKLVRLSHQNLLANARSIAE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 156 QYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRHGDPVhlADLIRRHGVTVIHFVP---AMLAAfnevLGA 232
Cdd:cd05922 152 YLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAF--WEDLREHGATGLAGVPstyAMLTR----LGF 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 233 GVGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTI---HRVtqDDRVIPIGTPTRRVSARVLDAA 309
Cdd:cd05922 226 DPAKLPSLRYLTQAGGRLPQETIARLRELLPGAQVYVMYGQTEATRRMTYlppERI--LEKPGSIGLAIPGGEFEILDDD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 310 LREVPIGVPGELYLGGVQLARGYAGRPDLTAERfvadpfGEPGARLYrTGDRARWNRDGEIEYLGRTDFQVKLRGQRLEL 389
Cdd:cd05922 304 GTPTPPGEPGEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLH-TGDLARRDEDGFLFIVGRRDRMIKLFGNRISP 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 390 GEVEAALAAAPGVLHAAAAVVDGPGGQQLVGY-LAPADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd05922 377 TEIEAAARSIGLIIEAAAVGLPDPLGEKLALFvTAPDKIDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1060-1530 |
1.80e-45 |
|
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: 172.23 E-value: 1.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1060 TEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGIT 1139
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASALVT 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1140 DAStrarlgesscewvdladleaeaesgDDitdterngsvrltnLAYLIYTSGSTGRPKA------VGVSHTGIVDFVNS 1213
Cdd:cd05971 85 DGS-------------------------DD--------------PALIIYTSGTTGPPKGalhahrVLLGHLPGVQFPFN 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1214 LAkittgtpedepdtrilhvasPSFDASMFEMA-WA---------IPA---GHTLVIAPQADFAGDALATVLERDEVTDM 1280
Cdd:cd05971 126 LF--------------------PRDGDLYWTPAdWAwigglldvlLPSlyfGVPVLAHRMTKFDPKAALDLMSRYGVTTA 185
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1281 IITPSVL---ATVDPERAQYVRNL---ATGGEACPPELVErWSER--GRRIFNCYGPTEAT-VWATRSRMTAGKPVTIGK 1351
Cdd:cd05971 186 FLPPTALkmmRQQGEQLKHAQVKLraiATGGESLGEELLG-WAREqfGVEVNEFYGQTECNlVIGNCSALFPIKPGSMGK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1352 PVDGFTVRVLDGRLHEVPQGVVGELYLST--AGLARGYLGRPGQTAVSFVADPFgepgarmyATGDLVRVAKGGNLEFAG 1429
Cdd:cd05971 265 PIPGHRVAIVDDNGTPLPPGEVGEIAVELpdPVAFLGYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVG 336
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1430 RADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGV-ESTRGgrkhTEVVAYLVAKPGATiDSAAVLDEAAQH----LAA 1504
Cdd:cd05971 337 RDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIpDPIRG----EIVKAFVVLNPGET-PSDALAREIQELvktrLAA 411
|
490 500
....*....|....*....|....*.
gi 1827387616 1505 HMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd05971 412 HEYPREIEFVNELPRTATGKIRRREL 437
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
4-471 |
4.69e-45 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 173.06 E-value: 4.69e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAE--VAVgiqIDR-SVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:PRK06187 35 AELDERVNRLANALRALGVKKGdrVAV---FDWnSHEYLEAYFAVPKIGAVLHPINIRLKPEEIAYILNDAEDRVVLVDS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRFDDIVDV-HVLDISSPGDADLDEE--EF------AGPTRPA------NAAFTLFTSGSTGRPKAVVITHRG 145
Cdd:PRK06187 112 EFVPLLAAILPQLPTVrTVIVEGDGPAAPLAPEvgEYeellaaASDTFDFpdidenDAAAMLYTSGTTGHPKGVVLSHRN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 146 I-ANRLAAdIEQYDLTARDVFLYKAPI----TFDVSVreifLPIAIGATLVIaePGRHgDPVHLADLIRRHGVTVIHFVP 220
Cdd:PRK06187 192 LfLHSLAV-CAWLKLSRDDVYLVIVPMfhvhAWGLPY----LALMAGAKQVI--PRRF-DPENLLDLIETERVTFFFAVP 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 221 AMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTI-----HRVTQDDRVIPIG 295
Cdd:PRK06187 264 TIWQMLLKAPRAYFVDFSSLRLVIYGGAALPPALLREFKEKF-GIDLVQGYGMTETSPVVSVlppedQLPGQWTKRRSAG 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 296 TPTRRVSARVLDAALREVP--IGVPGELYLGGVQLARGYAGRPDLTAERFVADpfgepgarLYRTGDRARWNRDGEIEYL 373
Cdd:PRK06187 343 RPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEATAETIDGG--------WLHTGDVGYIDEDGYLYIT 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 374 GRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVV---DGPGGQQLVGYLAP---ADVDVDTVAATTAELLPEYMRPS 447
Cdd:PRK06187 415 DRIKDVIISGGENIYPRELEDALYGHPAV--AEVAVIgvpDEKWGERPVAVVVLkpgATLDAKELRAFLRGRLAKFKLPK 492
|
490 500
....*....|....*....|....
gi 1827387616 448 AWVRLDAMPLSRSGKVDRRLLPEP 471
Cdd:PRK06187 493 RIAFVDELPRTSVGKILKRVLREQ 516
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1038-1525 |
7.71e-45 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 172.42 E-value: 7.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1038 TLIDVL---AQRDldPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYV 1114
Cdd:PRK08316 12 TIGDILrrsARRY--PDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1115 PVDPAYPADRIAYMLEDSGATVGITDASTRAR----LGESSCEWVDLADLEAEAESGDDITD----------TERNGSVR 1180
Cdd:PRK08316 90 PVNFMLTGEELAYILDHSGARAFLVDPALAPTaeaaLALLPVDTLILSLVLGGREAPGGWLDfadwaeagsvAEPDVELA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1181 LTNLAYLIYTSGSTGRPKAVGVSHTGIV-DFVNSlakITTGtpEDEPDTRILHvASPSFD-ASM--FEMAWaIPAGHTLV 1256
Cdd:PRK08316 170 DDDLAQILYTSGTESLPKGAMLTHRALIaEYVSC---IVAG--DMSADDIPLH-ALPLYHcAQLdvFLGPY-LYVGATNV 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1257 IAPQADfAGDALATVlERDEVTDMIITPSV---------LATVD---PERAQYvrnlatGGEACPPELVERWSER--GRR 1322
Cdd:PRK08316 243 ILDAPD-PELILRTI-EAERITSFFAPPTVwisllrhpdFDTRDlssLRKGYY------GASIMPVEVLKELRERlpGLR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1323 IFNCYGPTEATVWAT--RSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVA 1400
Cdd:PRK08316 315 FYNCYGQTEIAPLATvlGPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1401 DPFgepgarmyATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAY 1480
Cdd:PRK08316 395 GWF--------HSGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEA---VTAV 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1827387616 1481 LVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKL 1525
Cdd:PRK08316 464 VVPKAGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1050-1532 |
8.31e-45 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 171.73 E-value: 8.31e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMD--YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAY 1127
Cdd:cd05926 1 PDAPALVVPGSTPAltYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1128 MLEDSGATVGITDASTRARLGES-SCEWVDLADLEAEAESGDDITDTER-------------NGSVRLTNLAYLIYTSGS 1193
Cdd:cd05926 81 YLADLGSKLVLTPKGELGPASRAaSKLGLAILELALDVGVLIRAPSAESlsnlladkknaksEGVPLPDDLALILHTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1194 TGRPKAVGVSHTGIVdfvNSLAKITTG---TPEDepdtRIL------HV-----------AS-------PSFDASMF--E 1244
Cdd:cd05926 161 TGRPKGVPLTHRNLA---ASATNITNTyklTPDD----RTLvvmplfHVhglvasllstlAAggsvvlpPRFSASTFwpD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1245 MA-----W--AIPAGHTLVIAPQADFAGDALATVlerdevtdmiitpsvlatvdperaQYVRnlaTGGEACPPELVERWS 1317
Cdd:cd05926 234 VRdynatWytAVPTIHQILLNRPEPNPESPPPKL------------------------RFIR---SCSASLPPAVLEALE 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1318 ER-GRRIFNCYGPTEATVWATRSRMTAG--KPVTIGKPVdGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQT 1394
Cdd:cd05926 287 ATfGAPVLEAYGMTEAAHQMTSNPLPPGprKPGSVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEAN 365
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1395 AVSFVADPFgepgarmYATGDLVRVAKGGNLEFAGRadhqVK--IN--GQRVELGEIEAVLDAQPGVAQSVVVGVESTRG 1470
Cdd:cd05926 366 AEAAFKDGW-------FRTGDLGYLDADGYLFLTGR----IKelINrgGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKY 434
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 1471 GRkhtEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:cd05926 435 GE---EVAAAVVLREGASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
2109-2353 |
9.84e-45 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 163.29 E-value: 9.84e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2109 MTPLQQGLFFqadlantvaDHDAIDVYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVrLPSGAAVTVVPAEVTV 2188
Cdd:COG4908 1 LSPAQKRFLF---------LEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFV-EEDGEPVQRIDPDADL 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2189 PWSVIDLRAEDAASLDSRVEEVLATERTNPFDMAKPPLIRVVLVEHG-DGAELVVTNHHLLIDGWSSPLVLADLLSLYA- 2266
Cdd:COG4908 71 PLEVVDLSALPEPEREAELEELVAEEASRPFDLARGPLLRAALIRLGeDEHVLLLTIHHIISDGWSLGILLRELAALYAa 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2267 --TGQTFTGSLPGTSGRDFADHARAVA-TADVEAGIAAWREVLAPVTEPTLVAPGHEPSADAPPR--DHQFSIDVKVTER 2341
Cdd:COG4908 151 llEGEPPPLPELPIQYADYAAWQRAWLqSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRgaTLSFTLPAELTEA 230
|
250
....*....|..
gi 1827387616 2342 LEALARNNSTTM 2353
Cdd:COG4908 231 LKALAKAHGATV 242
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1051-1530 |
1.44e-44 |
|
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: 169.39 E-value: 1.44e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1051 DHPALICDGTEMDYDEFETRTNAIARALLARGVS-PEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd05941 1 DRIAIVDDGDSITYADLVARAARLANRLLALGKDlRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVgitdastrarlgessceWVDLAdleaeaesgdditdterngsvrltnlaYLIYTSGSTGRPKAVGVSHTGIVD 1209
Cdd:cd05941 81 TDSEPSL-----------------VLDPA---------------------------LILYTSGTTGRPKGVVLTHANLAA 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1210 FVNSLAKITTGTPEDepdtRILHVAsPSFDAS--MFEMAWAIPAGHTLVIAPQADFAGDALAtvLERDEVT--------- 1278
Cdd:cd05941 117 NVRALVDAWRWTEDD----VLLHVL-PLHHVHglVNALLCPLFAGASVEFLPKFDPKEVAIS--RLMPSITvfmgvptiy 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1279 -------DMIITPSVLATVDPERAqyVRNLATGGEACPPELVERWSER-GRRIFNCYGPTEaTVWATRSRMTAG-KPVTI 1349
Cdd:cd05941 190 trllqyyEAHFTDPQFARAAAAER--LRLMVSGSAALPVPTLEEWEAItGHTLLERYGMTE-IGMALSNPLDGErRPGTV 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1350 GKPVDGFTVRVLD-GRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRVAKGGNLEFA 1428
Cdd:cd05941 267 GMPLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWIL 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1429 GR-ADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGA-TIDSAAVLDEAAQHLAAHM 1506
Cdd:cd05941 340 GRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDWGER---VVAVVVLRAGAaALSLEELKEWAKQRLAPYK 416
|
490 500
....*....|....*....|....
gi 1827387616 1507 VPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd05941 417 RPRRLILVDELPRNAMGKVNKKEL 440
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1061-1530 |
1.65e-44 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 168.81 E-value: 1.65e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1061 EMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITD 1140
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1141 AStrarlgesscewvdladleaeaesgdditdterngsvrLTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTG 1220
Cdd:cd05935 81 SE--------------------------------------LDDLALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGL 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1221 TPEDepdtrILHVASPSFDASMFE--MAWAIPAGHTLVIapQADFAGDALATVLERDEVTDMIITPSVLATV--DPERAQ 1296
Cdd:cd05935 123 TPSD-----VILACLPLFHVTGFVgsLNTAVYVGGTYVL--MARWDRETALELIEKYKVTFWTNIPTMLVDLlaTPEFKT 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1297 ----YVRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDGR-LHEVPQ 1370
Cdd:cd05935 196 rdlsSLKVLTGGGAPMPPAVAEKLLKLtGLRFVEGYGLTETMSQTHTNPPLRPKLQCLGIP*FGVDARVIDIEtGRELPP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1371 GVVGELYLSTAGLARGYLGRPGQTAVSFVADpfgePGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAV 1450
Cdd:cd05935 276 NEVGEIVVRGPQIFKGYWNRPEETEESFIEI----KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAK 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1451 LDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPG--ATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRA 1528
Cdd:cd05935 352 LYKHPAI*EVCVISVPDERVGE---EVKAFIVLRPEyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWR 428
|
..
gi 1827387616 1529 AL 1530
Cdd:cd05935 429 LL 430
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
2584-3061 |
1.89e-44 |
|
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: 170.57 E-value: 1.89e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2584 VVDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSG 2663
Cdd:cd05926 7 VVPGSTPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2664 AVLglsVLASGDLPG------QEFEWMRLD---DDSV------AAEIAAVPAGPiTDAERLGEVTAANLAYVIYTSGSTG 2728
Cdd:cd05926 87 SKL---VLTPKGELGpasraaSKLGLAILElalDVGVlirapsAESLSNLLADK-KNAKSEGVPLPDDLALILHTSGTTG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2729 RPKGVAVTHSGLANFAR--QESDRLNAGDNPVVLgfaSPSFD-----ASVLEYLLAtvnegtlayrpseavGGEVL--ER 2799
Cdd:cd05926 163 RPKGVPLTHRNLAASATniTNTYKLTPDDRTLVV---MPLFHvhglvASLLSTLAA---------------GGSVVlpPR 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2800 F--------IAEHGAT--------HTFLtpsvLSTMDPTAV---PSLRVIAAGGEAVPQPIVDRW-----APATELhnlY 2855
Cdd:cd05926 225 FsastfwpdVRDYNATwytavptiHQIL----LNRPEPNPEsppPKLRFIRSCSASLPPAVLEALeatfgAPVLEA---Y 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2856 GPTETTIGITisSAMRPGDPVRLG--GPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYg 2933
Cdd:cd05926 298 GMTEAAHQMT--SNPLPPGPRKPGsvGKPVGVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2934 tagqrmYRTGDVVRWTPDtdtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-----GGSVAtala 3008
Cdd:cd05926 375 ------FRTGDLGYLDAD---GYLFL--TGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVpdekyGEEVA---- 439
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 3009 AYIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPE 3061
Cdd:cd05926 440 AAVVLREGAsVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKVAE 493
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2589-3060 |
4.87e-44 |
|
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: 167.47 E-value: 4.87e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2589 GARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLgl 2668
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2669 svlasgdlpgqefewmrldddsvaaeiaavpagPITDaerlgevtaanLAYVIYTSGSTGRPKGVAVTHSGLANFARQES 2748
Cdd:cd05934 79 ---------------------------------VVVD-----------PASILYTSGTTGPPKGVVITHANLTFAGYYSA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2749 DRLNAGDNPVVLGFAsPSF--DASVLEYLLATVNEGTLAyrpseavggeVLERF--------IAEHGATHTFLTPSVLST 2818
Cdd:cd05934 115 RRFGLGEDDVYLTVL-PLFhiNAQAVSVLAALSVGATLV----------LLPRFsasrfwsdVRRYGATVTNYLGAMLSY 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2819 -------MDPTAVPsLRViAAGGEAVPQ---PIVDRWapATELHNLYGPTETTIGITissamRPGDPVRLGGPIG----G 2884
Cdd:cd05934 184 llaqppsPDDRAHR-LRA-AYGAPNPPElheEFEERF--GVRLLEGYGMTETIVGVI-----GPRDEPRRPGSIGrpapG 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2885 VDLMVLDERLRPVPVGMPGELYV---AGGALSRGYLDRSGLTAERFtanPYGtagqrMYRTGDVVRWTPDTDtggltLEY 2961
Cdd:cd05934 255 YEVRIVDDDGQELPAGEPGELVIrglRGWGFFKGYYNMPEATAEAM---RNG-----WFHTGDLGYRDADGF-----FYF 321
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2962 TGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVA-TALAAYIVPVDGA-VEVSELKAFAGGRLPAYMVPSS 3039
Cdd:cd05934 322 VDRKKDMIRRRGENISSAEVERAILRHPAVREAAVVAVPDEVGeDEVKAVVVLRPGEtLDPEELFAFCEGQLAYFKVPRY 401
|
490 500
....*....|....*....|.
gi 1827387616 3040 FTVIDELPLTPVGKLDKRALP 3060
Cdd:cd05934 402 IRFVDDLPKTPTEKVAKAQLR 422
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
2566-3059 |
2.29e-43 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 168.19 E-value: 2.29e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVP 2645
Cdd:PRK08316 12 TIGDILRRSARRYPDKTALVFG-DRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2646 IDPDYPAERVASMIEDSGAVL--------GLSVLASGDLPGQEFEWM-----RLDDDSVAAEIAAVPAGPITDAERlgEV 2712
Cdd:PRK08316 91 VNFMLTGEELAYILDHSGARAflvdpalaPTAEAALALLPVDTLILSlvlggREAPGGWLDFADWAEAGSVAEPDV--EL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2713 TAANLAYVIYTSGSTGRPKGVAVTHSGL-ANFARQESD-RLNAGDNPVV---LgFASPSFDASVLEYLL--ATvneGTLA 2785
Cdd:PRK08316 169 ADDDLAQILYTSGTESLPKGAMLTHRALiAEYVSCIVAgDMSADDIPLHalpL-YHCAQLDVFLGPYLYvgAT---NVIL 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2786 YRPSeavGGEVLERfIAEHGATHTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRWA---PATELHNLYG 2856
Cdd:PRK08316 245 DAPD---PELILRT-IEAERITSFFAPPTVWISLlrhpdfDTRDLSSLRKGYYGASIMPVEVLKELRerlPGLRFYNCYG 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2857 PTEttIGiTISSAMRPGDPVRLGG----PIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANpy 2932
Cdd:PRK08316 321 QTE--IA-PLATVLGPEEHLRRPGsagrPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGG-- 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2933 gtagqrMYRTGDVVRWtpdtDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSV-ATALAAYI 3011
Cdd:PRK08316 396 ------WFHSGDLGVM----DEEGY-ITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKwIEAVTAVV 464
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1827387616 3012 VPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK08316 465 VPKAGAtVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2599-3059 |
3.92e-43 |
|
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: 165.69 E-value: 3.92e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2599 EASDRLAR-WLIGRGVGPERAVALAIGRSaqllTAIW---AVAKTGGA----YVPIDPDYPAERVASMIEDSGAVLGLSV 2670
Cdd:cd05922 1 LGVSAAASaLLEAGGVRGERVVLILPNRF----TYIElsfAVAYAGGRlglvFVPLNPTLKESVLRYLVADAGGRIVLAD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2671 LASGDlpgqefewmRLDDDSVAAEIAAVPAG--PITDAERLG---EVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFAR 2745
Cdd:cd05922 77 AGAAD---------RLRDALPASPDPGTVLDadGIRAARASApahEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANAR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2746 QESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGGEVLERFiAEHGATHTFLTPSVLS-----TMD 2820
Cdd:cd05922 148 SIAEYLGITADDRALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDAFWEDL-REHGATGLAGVPSTYAmltrlGFD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2821 PTAVPSLRVIAAGGEAVPQPIVDRWA---PATELHNLYGPTETTIGITISSAMRPGD-PVRLGGPIGGVDLMVLDERLRP 2896
Cdd:cd05922 227 PAKLPSLRYLTQAGGRLPQETIARLRellPGAQVYVMYGQTEATRRMTYLPPERILEkPGSIGLAIPGGEFEILDDDGTP 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2897 VPVGMPGELYVAGGALSRGYLDRSGLTAErftanpyGTAGQRMYRTGDVVRWTPDTDtggltLEYTGRSDDQVKLRGLRI 2976
Cdd:cd05922 307 TPPGEPGEIVHRGPNVMKGYWNDPPYRRK-------EGRGGGVLHTGDLARRDEDGF-----LFIVGRRDRMIKLFGNRI 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2977 ELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPVDGaVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDK 3056
Cdd:cd05922 375 SPTEIEAAARSIGLIIEAAAVGLPDPLGEKLALFVTAPDK-IDPKDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDY 453
|
...
gi 1827387616 3057 RAL 3059
Cdd:cd05922 454 AAL 456
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
2569-3059 |
5.06e-43 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 166.78 E-value: 5.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2569 ELFRAAARRAPDHVAVVDGAGaRLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDP 2648
Cdd:cd05959 8 LVDLNLNEGRGDKTAFIDDAG-SLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2649 DYPAERVASMIEDSGAVLglsVLASGDLPGQEFEWMRLDDDSVAAEIAAVPAGPITDAERLGEVTAA------------- 2715
Cdd:cd05959 87 LLTPDDYAYYLEDSRARV---VVVSGELAPVLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELVAAeaeqlkpaathad 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2716 NLAYVIYTSGSTGRPKGVAVTHSGLA----NFARqesDRLNAGDNPVVLGfASPSFDASVL--EYLLATVNEGTLAYRPS 2789
Cdd:cd05959 164 DPAFWLYSSGSTGRPKGVVHLHADIYwtaeLYAR---NVLGIREDDVCFS-AAKLFFAYGLgnSLTFPLSVGATTVLMPE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2790 EAVGGEVLERfIAEHGATHTFLTPSVLSTMdpTAVP--------SLRVIAAGGEAVPQPIVDRWAPATELHNLYGPTETT 2861
Cdd:cd05959 240 RPTPAAVFKR-IRRYRPTVFFGVPTLYAAM--LAAPnlpsrdlsSLRLCVSAGEALPAEVGERWKARFGLDILDGIGSTE 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2862 IG-ITISSamRPGDpVRLGG---PIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANpygtagq 2937
Cdd:cd05959 317 MLhIFLSN--RPGR-VRYGTtgkPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQGE------- 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2938 rMYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVA-TALAAYIVPVDG 3016
Cdd:cd05959 387 -WTRTGDKYVRDDDG-----FYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGlTKPKAFVVLRPG 460
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1827387616 3017 ----AVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05959 461 yedsEALEEELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
2579-3062 |
6.41e-43 |
|
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: 166.54 E-value: 6.41e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2579 PDHVAVV------DGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPA 2652
Cdd:cd17647 2 PERTCVVetpslnSSKTRSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2653 ERvasmiedsgAVLGLSVLASGDLpgqefewmrldddsVAAEIAAVPAGPITDAErlgevtaanlayVIYTSGSTGRPKG 2732
Cdd:cd17647 82 AR---------QNIYLGVAKPRGL--------------IVIRAAGVVVGPDSNPT------------LSFTSGSEGIPKG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2733 VAVTHSGLANFARQESDRLNAGDN---PVVLGFASPSFDASVLEYLLAtvneGTLAYRPSEAVGG--EVLERFIAEHGAT 2807
Cdd:cd17647 127 VLGRHFSLAYYFPWMAKRFNLSENdkfTMLSGIAHDPIQRDMFTPLFL----GAQLLVPTQDDIGtpGRLAEWMAKYGAT 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2808 HTFLTPS---VLSTMDPTAVPSLRVIAAGGEAVPQPIVDRW---APATELHNLYGPTETTIGIT---ISSamRPGDPVRL 2878
Cdd:cd17647 203 VTHLTPAmgqLLTAQATTPFPKLHHAFFVGDILTKRDCLRLqtlAENVRIVNMYGTTETQRAVSyfeVPS--RSSDPTFL 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2879 ---------GGPIGGVDLMVLD--ERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQ---------- 2937
Cdd:cd17647 281 knlkdvmpaGRGMLNVQLLVVNrnDRTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDHwnyldkdnne 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2938 -----------RMYRTGDVVRWTPDTDtggltLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAV-ESAVVLGVGGSVAT 3005
Cdd:cd17647 361 pwrqfwlgprdRLYRTGDLGRYLPNGD-----CECCGRADDQVKIRGFRIELGEIDTHISQHPLVrENITLVRRDKDEEP 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3006 ALAAYIVPVDGAVE----------------------------VSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKR 3057
Cdd:cd17647 436 TLVSYIVPRFDKPDdesfaqedvpkevstdpivkgligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKP 515
|
....*
gi 1827387616 3058 ALPEP 3062
Cdd:cd17647 516 KLQFP 520
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1064-1525 |
1.05e-42 |
|
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: 163.71 E-value: 1.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDAST 1143
Cdd:cd05903 4 YSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPERF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1144 RARlgesscewvdladleAEAESGDDItdterngsvrltnlAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPE 1223
Cdd:cd05903 84 RQF---------------DPAAMPDAV--------------ALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPG 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1224 DepdtRILhVASP--SFDASMFEMAWAIPAGHTLVIapQADFAGDALATVLERDEVTDMIITP----SVLATVD--PERA 1295
Cdd:cd05903 135 D----VFL-VASPmaHQTGFVYGFTLPLLLGAPVVL--QDIWDPDKALALMREHGVTFMMGATpfltDLLNAVEeaGEPL 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1296 QYVRNLATGGEACPPELVERWSER-GRRIFNCYGPTEatVWATRSRMTAGKP----VTIGKPVDGFTVRVLDGRLHEVPQ 1370
Cdd:cd05903 208 SRLRTFVCGGATVPRSLARRAAELlGAKVCSAYGSTE--CPGAVTSITPAPEdrrlYTDGRPLPGVEIKVVDDTGATLAP 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1371 GVVGELYLSTAGLARGYLGRPGQTAvsfVADPFGepgarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAV 1450
Cdd:cd05903 286 GVEGELLSRGPSVFLGYLDRPDLTA---DAAPEG-----WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDL 357
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 1451 LDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATIDSAAV---LDeaAQHLAAHMVPSQAIVIDEIPLTPAGKL 1525
Cdd:cd05903 358 LLGHPGVIEAAVVALPDERLGER---ACAVVVTKSGALLTFDELvayLD--RQGVAKQYWPERLVHVDDLPRTPSGKV 430
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1064-1530 |
1.40e-42 |
|
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: 163.83 E-value: 1.40e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDAST 1143
Cdd:cd05969 3 FAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1144 RARlgesscewvdladleaeaesgddiTDTErngsvrltNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPE 1223
Cdd:cd05969 83 YER------------------------TDPE--------DPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1224 DepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFAGDALATVLERDEVTDMIITPSVL-----ATVDPERA--- 1295
Cdd:cd05969 131 D----IYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIrmlmkEGDELARKydl 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1296 QYVRNLATGGEACPPELVeRWSER--GRRIFNCYGPTEatvwaTRSRMTAG------KPVTIGKPVDGFTVRVLDGRLHE 1367
Cdd:cd05969 207 SSLRFIHSVGEPLNPEAI-RWGMEvfGVPIHDTWWQTE-----TGSIMIANypcmpiKPGSMGKPLPGVKAAVVDENGNE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1368 VPQGVVGELYLSTA--GLARGYLGRPGQTAVSFVADpfgepgarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELG 1445
Cdd:cd05969 281 LPPGTKGILALKPGwpSMFRGIWNDEERYKNSFIDG--------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1446 EIEAVLDAQPGVAQSVVVGVES-TRGGRkhteVVAYLVAKPGATIDSA---AVLDEAAQHLAAHMVPSQAIVIDEIPLTP 1521
Cdd:cd05969 353 EVESALMEHPAVAEAGVIGKPDpLRGEI----IKAFISLKEGFEPSDElkeEIINFVRQKLGAHVAPREIEFVDNLPKTR 428
|
....*....
gi 1827387616 1522 AGKLDRAAL 1530
Cdd:cd05969 429 SGKIMRRVL 437
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
2108-2535 |
2.81e-42 |
|
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: 162.14 E-value: 2.81e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2108 PMTPLQQGLFF--QADLANTVadhdaidvYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVrLPSGAAVTVVPAE 2185
Cdd:cd19531 3 PLSFAQQRLWFldQLEPGSAA--------YNIPGALRLRGPLDVAALERALNELVARHEALRTTFV-EVDGEPVQVILPP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2186 VTVPWSVIDLRAEDAASLDSRVEEVLATERTNPFDMAKPPLIRVVLVEHGDgAE--LVVTNHHLLIDGWSSPLVLADLLS 2263
Cdd:cd19531 74 LPLPLPVVDLSGLPEAEREAEAQRLAREEARRPFDLARGPLLRATLLRLGE-DEhvLLLTMHHIVSDGWSMGVLLRELAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2264 LYATGQTFTGS----LPgtsgRDFADHA---RAVATADV-EAGIAAWREVLA---PVTE-PTlvapghepsaDAPPRDHQ 2331
Cdd:cd19531 153 LYAAFLAGRPSplppLP----IQYADYAvwqREWLQGEVlERQLAYWREQLAgapPVLElPT----------DRPRPAVQ 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2332 --------FSIDVKVTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRS-PDIEGmesMVGMFINTIP 2402
Cdd:cd19531 219 sfrgarvrFTLPAELTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNrAELEG---LIGFFVNTLV 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2403 AVVDVNPDATVVDVLTAVQNDKVKVLDHQQigLP--RLVAQTGLP------ALFDTLAVYESFPVNVDSVAGIDASSAGg 2474
Cdd:cd19531 296 LRTDLSGDPTFRELLARVRETALEAYAHQD--LPfeKLVEALQPErdlsrsPLFQVMFVLQNAPAAALELPGLTVEPLE- 372
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 2475 lklVGAKTSdatHYPLNLSASRRGAELALKLKYlPTA-FAPEQVAVFADVLTGLLGAIADHP 2535
Cdd:cd19531 373 ---VDSGTA---KFDLTLSLTETDGGLRGSLEY-NTDlFDAATIERMAGHFQTLLEAIVADP 427
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
2583-3054 |
3.47e-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: 163.54 E-value: 3.47e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2583 AVVDGA-GARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIED 2661
Cdd:cd05911 1 AQIDADtGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2662 SGA-------------------------VLGLSVLASGDLPGQEfewmrLDDDSVAAEIAAVPAGPITDAERlgevtaan 2716
Cdd:cd05911 81 SKPkviftdpdglekvkeaakelgpkdkIIVLDDKPDGVLSIED-----LLSPTLGEEDEDLPPPLKDGKDD-------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2717 LAYVIYTSGSTGRPKGVAVTHSGL-ANFAR-QESDRLNAGDNPVVLGFaSPSFDAS-VLEYLLATVNEGTLA--YRPSEa 2791
Cdd:cd05911 148 TAAILYSSGTTGLPKGVCLSHRNLiANLSQvQTFLYGNDGSNDVILGF-LPLYHIYgLFTTLASLLNGATVIimPKFDS- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2792 vggEVLERFIAEHGATHTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRWA---PATELHNLYGPTETTI 2862
Cdd:cd05911 226 ---ELFLDLIEKYKITFLYLVPPIAAALakspllDKYDLSSLRVILSGGAPLSKELQELLAkrfPNATIKQGYGMTETGG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2863 GITISsamrPGDPVRL---GGPIGGVDLMVLDERLRP-VPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYgtagqr 2938
Cdd:cd05911 303 ILTVN----PDGDDKPgsvGRLLPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------ 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2939 mYRTGDVVRWtpdtDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATAL-AAYIVPVDGA 3017
Cdd:cd05911 373 -LHTGDIGYF----DEDGY-LYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELpRAYVVRKPGE 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1827387616 3018 VEVS-ELKAFAGGRLPAY------MVpssftVIDELPLTPVGKL 3054
Cdd:cd05911 447 KLTEkEVKDYVAKKVASYkqlrggVV-----FVDEIPKSASGKI 485
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1037-1526 |
5.27e-42 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 164.29 E-value: 5.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1037 GTLIDVLAqrDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPV 1116
Cdd:PRK07798 6 ADLFEAVA--DAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1117 DPAYPADRIAYMLEDSGATVGITDASTRARLGESScewVDLADLEAEAESGDDITDTERNGSVRLTNLA----------- 1185
Cdd:PRK07798 84 NYRYVEDELRYLLDDSDAVALVYEREFAPRVAEVL---PRLPKLRTLVVVEDGSGNDLLPGAVDYEDALaagsperdfge 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1186 ------YLIYTSGSTGRPKAV-------------GVSHtGIVDFVNSLAKITTGTPEDEPDTRIlhVASPSFDASMFEMA 1246
Cdd:PRK07798 161 rspddlYLLYTGGTTGMPKGVmwrqedifrvllgGRDF-ATGEPIEDEEELAKRAAAGPGMRRF--PAPPLMHGAGQWAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1247 W-AIPAGHTLVIAPQADFAGDALATVLERDEVTDMIIT------PSVLATVDPERAQY--VRNLATGGEACPPELVERWS 1317
Cdd:PRK07798 238 FaALFSGQTVVLLPDVRFDADEVWRTIEREKVNVITIVgdamarPLLDALEARGPYDLssLFAIASGGALFSPSVKEALL 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1318 ER--GRRIFNCYGPTEA-----TVWATRSRMTAGKPVTIGKpvdgfTVRVLDGRLHEVPQGVVGELYLSTAG-LARGYLG 1389
Cdd:PRK07798 318 ELlpNVVLTDSIGSSETgfggsGTVAKGAVHTGGPRFTIGP-----RTVVLDEDGNPVEPGSGEIGWIARRGhIPLGYYK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1390 RPGQTAVSF-VADpfgepGARMYATGDLVRVAKGGNLEFAGRADhqVKIN--GQRVELGEIEAVLDAQPGVAQSVVVGVE 1466
Cdd:PRK07798 393 DPEKTAETFpTID-----GVRYAIPGDRARVEADGTITLLGRGS--VCINtgGEKVFPEEVEEALKAHPDVADALVVGVP 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1467 STRGGRkhtEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLD 1526
Cdd:PRK07798 466 DERWGQ---EVVAVVQLREGARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
2566-3059 |
6.43e-42 |
|
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: 163.06 E-value: 6.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDGAGA-RLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYV 2644
Cdd:cd05923 2 TVFEMLRRAASRAPDACAIADPARGlRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2645 PIDPDYPAERVASMIEDS---GAVLGLSVLASGDLPGQEFEWMRLDDDsVAAEIAAVPAGPITDAERLGEVTaanlAYVI 2721
Cdd:cd05923 82 LINPRLKAAELAELIERGemtAAVIAVDAQVMDAIFQSGVRVLALSDL-VGLGEPESAGPLIEDPPREPEQP----AFVF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2722 YTSGSTGRPKGVAVTH----SGLANFARQESDRLnaGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGGEVL 2797
Cdd:cd05923 157 YTSGTTGLPKGAVIPQraaeSRVLFMSTQAGLRH--GRHNVVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADAL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2798 ErFIAEHGATHTFLTPSVL------STMDPTAVPSLRVIAAGGEAVPQPIVDRWAPA--TELHNLYGPTETTIGI----- 2864
Cdd:cd05923 235 K-LIEQERVTSLFATPTHLdalaaaAEFAGLKLSSLRHVTFAGATMPDAVLERVNQHlpGEKVNIYGTTEAMNSLymrda 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2865 TISSAMRPG--DPVRLgGPIGGVDLMVLderlrpvPVGMPGELYVAGGALS--RGYLDRSGLTAERFTanpygtagQRMY 2940
Cdd:cd05923 314 RTGTEMRPGffSEVRI-VRIGGSPDEAL-------ANGEEGELIVAAAADAafTGYLNQPEATAKKLQ--------DGWY 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2941 RTGDVVRWTPDTDtggltLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-----GGSVatalAAYIVPVD 3015
Cdd:cd05923 378 RTGDVGYVDPSGD-----VRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVaderwGQSV----TACVVPRE 448
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1827387616 3016 GAVEVSELKAFA-GGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05923 449 GTLSADELDQFCrASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1-468 |
2.50e-41 |
|
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2,3-dihydroxybenzoate (DHB) by ligation of AMP from ATP with the release of pyrophosphate. However, it can also catalyze the ATP-PPi exchange for 2,3-DHB analogs, such as salicyclic acid (o-hydrobenzoate), as well as 2,4-DHB and 2,5-DHB, but with less efficiency. Proteins in this family are the stand-alone adenylation components of non-ribosomal peptide synthases (NRPSs) involved in the biosynthesis of siderophores, which are low molecular weight iron-chelating compounds synthesized by many bacteria to aid in the acquisition of this vital trace elements. In Escherichia coli, the 2,3-dihydroxybenzoate-AMP ligase is called EntE, the adenylation component of the enterobactin NRPS system.
Pssm-ID: 341244 [Multi-domain] Cd Length: 482 Bit Score: 160.96 E-value: 2.50e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVpldEQLPVDRAR---YMVRTAGVRLVV 77
Cdd:cd05920 41 LTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPV---LALPSHRRSelsAFCAHAEAVAYI 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 78 VtsdgeAEARSRFDDIVDVHVLDISSPgdadldeeefagptrpaNAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQY 157
Cdd:cd05920 118 V-----PDRHAGFDHRALARELAESIP-----------------EVALFLLSGGTTGTPKLIPRTHNDYAYNVRASAEVC 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 158 DLTARDVFLYKAPI--TFDVSVREIFLPIAIGATLVIAEPGrhgDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVG 235
Cdd:cd05920 176 GLDQDTVYLAVLPAahNFPLACPGVLGTLLAGGRVVLAPDP---SPDAAFPLIEREGVTVTALVPALVSLWLDAAASRRA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 236 ELTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTihRVTQDDRVIpIGTPTRRVSA----RVLDAALR 311
Cdd:cd05920 253 DLSSLRLLQVGGARLSPALARRVPPVL-GCTLQQVFGMAEGLLNYT--RLDDPDEVI-IHTQGRPMSPddeiRVVDEEGN 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 312 EVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGE 391
Cdd:cd05920 329 PVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEE 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 392 VEAALAAAPGVLHAAAAVVDGPG-GQQLVGYLAPADVDVDTV---AATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRL 467
Cdd:cd05920 402 VENLLLRHPAVHDAAVVAMPDELlGERSCAFVVLRDPPPSAAqlrRFLRERGLAAYKLPDRIEFVDSLPLTAVGKIDKKA 481
|
.
gi 1827387616 468 L 468
Cdd:cd05920 482 L 482
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2-469 |
5.36e-41 |
|
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: 158.61 E-value: 5.36e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVtsd 81
Cdd:cd05934 5 TYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 geaearsrfdDIVDVhvldisspgdadldeeefagptrpanaaftLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTA 161
Cdd:cd05934 82 ----------DPASI------------------------------LYTSGTTGPPKGVVITHANLTFAGYYSARRFGLGE 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 162 RDVFLYKAPItF--DVSVREIFLPIAIGATLVIAE---PGRhgdpvhLADLIRRHGVTVIHFVPAMLAAfneVLGAGVGE 236
Cdd:cd05934 122 DDVYLTVLPL-FhiNAQAVSVLAALSVGATLVLLPrfsASR------FWSDVRRYGATVTNYLGAMLSY---LLAQPPSP 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 237 LTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEAsIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIG 316
Cdd:cd05934 192 DDRAHRLRAAYGAPNPPELHEEFEERFGVRLLEGYGMTET-IVGVIGPRDEPRRPGSIGRPAPGYEVRIVDDDGQELPAG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 317 VPGELYLGGVQ---LARGYAGRPDLTAERFvadpfgEPGarLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVE 393
Cdd:cd05934 271 EPGELVIRGLRgwgFFKGYYNMPEATAEAM------RNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVE 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 394 AALAAAPGVLHAAA-AVVDGPGGQQLVGYLA---PADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLP 469
Cdd:cd05934 343 RAILRHPAVREAAVvAVPDEVGEDEVKAVVVlrpGETLDPEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
571-996 |
6.87e-41 |
|
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike bacterial NRPS, which typically have specialized terminal thioesterase (TE) domains to cyclize peptide products, many fungal NRPSs employ a terminal condensation-like (CT) domain to produce macrocyclic peptidyl products (e.g. cyclosporine and echinocandin). Domains in this subfamily (which includes both terminal and non-terminal domains) typically have a non-canonical conserved [SN]HxxxDx(14)Y motif at their active site compared to the standard Condensation (C) domain active site motif (HHxxxD). C-domains of NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380464 [Multi-domain] Cd Length: 401 Bit Score: 157.47 E-value: 6.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 571 LPLSRAQRRMwfLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVY-PSVGAAP-VQDVLpvavAREQ 648
Cdd:cd19542 2 YPCTPMQEGM--LLSQLRSPGLYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFvESSAEGTfLQVVL----KSLD 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 649 LDWREADSVE-SLVRSTTEGFDVST---QMPLRGRFHRDGAGLH-VALTMHHIAMDGQSIPVLARDLMSAYAARAEGRTg 723
Cdd:cd19542 76 PPIEEVETDEdSLDALTRDLLDDPTlfgQPPHRLTLLETSSGEVyLVLRISHALYDGVSLPIILRDLAAAYNGQLLPPA- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 724 glpvldVQYADYA--LWQQSVLgdaddetsvlgEQLSHWRRVLAGLPAVTDlpmdrprPAVLGTAGATVTVEFDDDLADR 801
Cdd:cd19542 155 ------PPFSDYIsyLQSQSQE-----------ESLQYWRKYLQGASPCAF-------PSLSPKRPAERSLSSTRRSLAK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 802 VDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRN--DPALEELIGMFVNTLLLRTQVDPGHSVGDLLGNVR 879
Cdd:cd19542 211 LEAFCASLGVTLASLFQAAWALVLARYTGSRDVVFGYVVSGRDlpVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQ 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 880 TTVLDAFANDQVQFDELIEALapeRSSSHQPLAQIAFTYteptVNDVAGLEASGIQAAPVDTGVVNAKFDLTVAVRARSG 959
Cdd:cd19542 291 QQYLRSLPHQHLSLREIQRAL---GLWPSGTLFNTLVSY----QNFEASPESELSGSSVFELSAAEDPTEYPVAVEVEPS 363
|
410 420 430
....*....|....*....|....*....|....*..
gi 1827387616 960 GTPMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd19542 364 GDSLKVSLAYSTSVLSEEQAEELLEQFDDILEALLAN 400
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
1064-1530 |
7.23e-41 |
|
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: 158.38 E-value: 7.23e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDASt 1143
Cdd:TIGR01923 2 WQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1144 rarLGESSCEWVDLADLEAEAESgdditDTERNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPE 1223
Cdd:TIGR01923 81 ---LEEKDFQADSLDRIEAAGRY-----ETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLGFTED 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1224 DepdtRILhVASPSFDASMFEMAW-AIPAGHTLVIaPQADfagDALATVLERDEVTDMIITPSVLATVDPERA--QYVRN 1300
Cdd:TIGR01923 153 D----NWL-LSLPLYHISGLSILFrWLIEGATLRI-VDKF---NQLLEMIANERVTHISLVPTQLNRLLDEGGhnENLRK 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1301 LATGGEACPPELVERWSERGRRIFNCYGPTEA--TVWATRSRMTAGKPvTIGKPVDGFTVRVldgrlhEVP-QGVVGELY 1377
Cdd:TIGR01923 224 ILLGGSAIPAPLIEEAQQYGLPIYLSYGMTETcsQVTTATPEMLHARP-DVGRPLAGREIKI------KVDnKEGHGEIM 296
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1378 LSTAGLARGYLGR-PGQTAvsfvadpFGEPGarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPG 1456
Cdd:TIGR01923 297 VKGANLMKGYLYQgELTPA-------FEQQG--WFNTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPG 367
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 1457 VAQSVVVGVE-STRGGRKhtevVAYLVAKpgATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:TIGR01923 368 IQEAVVVPKPdAEWGQVP----VAYIVSE--SDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
2575-3059 |
1.98e-40 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 159.09 E-value: 1.98e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2575 ARRAPDHVAVV-DGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAE 2653
Cdd:PRK13391 7 AQTTPDKPAVImASTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2654 RVASMIEDSG--------AVLGLSVLASGDLPGQEfEWMRLDDD-------SVAAEIAAVPAGPITDaERLGevtaanlA 2718
Cdd:PRK13391 87 EAAYIVDDSGaralitsaAKLDVARALLKQCPGVR-HRLVLDGDgelegfvGYAEAVAGLPATPIAD-ESLG-------T 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2719 YVIYTSGSTGRPKGV--------AVTHSGLANFA------RQESDRLNagdnPVVLGFASPSFDASVLEYLLATVnegtl 2784
Cdd:PRK13391 158 DMLYSSGTTGRPKGIkrplpeqpPDTPLPLTAFLqrlwgfRSDMVYLS----PAPLYHSAPQRAVMLVIRLGGTV----- 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2785 ayrpseavggEVLERF--------IAEHGATHTFLTPSVLSTM--------DPTAVPSLRVIAAGGEAVPQPI----VDR 2844
Cdd:PRK13391 229 ----------IVMEHFdaeqylalIEEYGVTHTQLVPTMFSRMlklpeevrDKYDLSSLEVAIHAAAPCPPQVkeqmIDW 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2845 WAPAteLHNLYGPTETTIGITISSAMRPGDPVRLGGPIGGvDLMVLDERLRPVPVGMPGELYVAGGaLSRGYLDRSGLTA 2924
Cdd:PRK13391 299 WGPI--IHEYYAATEGLGFTACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEGG-RPFEYLNDPAKTA 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2925 ErfTANPYGTagqrMYRTGDVVRwtpdTDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-GGSV 3003
Cdd:PRK13391 375 E--ARHPDGT----WSTVGDIGY----VDEDGY-LYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVpNEDL 443
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3004 ATALAAYIVPVDGAVE----VSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK13391 444 GEEVKAVVQPVDGVDPgpalAAELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1039-1535 |
2.69e-40 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 158.50 E-value: 2.69e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1039 LIDVLAQRDLDPDHPAL-ICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVD 1117
Cdd:PRK07514 5 LFDALRAAFADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1118 PAYPADRIAYMLEDSGATVGITDASTR-------ARLGESSCEWVDlAD-----LEAEAESGDDITDTERNGSvrltNLA 1185
Cdd:PRK07514 85 TAYTLAELDYFIGDAEPALVVCDPANFawlskiaAAAGAPHVETLD-ADgtgslLEAAAAAPDDFETVPRGAD----DLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1186 YLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtRILHvaspsfdasmfemawAIPAGHT--LVIAPQ-AD 1262
Cdd:PRK07514 160 AILYTSGTTGRSKGAMLSHGNLLSNALTLVDYWRFTPDD----VLIH---------------ALPIFHThgLFVATNvAL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1263 FAGDAL--ATVLERDEVTDMIITPSVLATV-------------DPERAQYVRnLATGGEAcpPELVE---RWSER-GRRI 1323
Cdd:PRK07514 221 LAGASMifLPKFDPDAVLALMPRATVMMGVptfytrllqeprlTREAAAHMR-LFISGSA--PLLAEthrEFQERtGHAI 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1324 FNCYGPTEaTVWATrSRMTAGK--PVTIGKPVDGFTVRVLD---GRlhEVPQGVVGELYLSTAGLARGYLGRPGQTAVSF 1398
Cdd:PRK07514 298 LERYGMTE-TNMNT-SNPYDGErrAGTVGFPLPGVSLRVTDpetGA--ELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1399 VADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVestrggrKHTE-- 1476
Cdd:PRK07514 374 RADGF-------FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVEGEIDELPGVVESAVIGV-------PHPDfg 439
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 1477 --VVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEPHA 1535
Cdd:PRK07514 440 egVTAVVVPKPGAALDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLREQYA 500
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
2592-3059 |
2.91e-40 |
|
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: 156.85 E-value: 2.91e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2592 LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAvlglsvl 2671
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEA------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2672 asgdlpgqefewmrldddsvaaeiaavpagpitdaeRLGEVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFAR---QES 2748
Cdd:cd05919 84 ------------------------------------RLVVTSADDIAYLLYSSGTTGPPKGVMHAHRDPLLFADamaREA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2749 DRLNAGDnpVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGGEVLERFIAEHGATHTFLTPSVLSTM------DPT 2822
Cdd:cd05919 128 LGLTPGD--RVFSSAKMFFGYGLGNSLWFPLAVGASAVLNPGWPTAERVLATLARFRPTVLYGVPTFYANLldscagSPD 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2823 AVPSLRVIAAGGEAVPQPIVDRWAPATELHNLYGPTETTIGITISSAmRPGD--PVRLGGPIGGVDLMVLDERLRPVPVG 2900
Cdd:cd05919 206 ALRSLRLCVSAGEALPRGLGERWMEHFGGPILDGIGATEVGHIFLSN-RPGAwrLGSTGRPVPGYEIRLVDEEGHTIPPG 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2901 MPGELYVAGGALSRGYLDRSGLTAERFTANpygtagqrMYRTGDVVRWTPDtdtGGLTleYTGRSDDQVKLRGLRIELGE 2980
Cdd:cd05919 285 EEGDLLVRGPSAAVGYWNNPEKSRATFNGG--------WYRTGDKFCRDAD---GWYT--HAGRADDMLKVGGQWVSPVE 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2981 IEAVLAEHDAVESAVVLGV-GGSVATALAAYIVPVDGAVE----VSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLD 3055
Cdd:cd05919 352 VESLIIQHPAVAEAAVVAVpESTGLSRLTAFVVLKSPAAPqeslARDIHRHLLERLSAHKVPRRIAFVDELPRTATGKLQ 431
|
....
gi 1827387616 3056 KRAL 3059
Cdd:cd05919 432 RFKL 435
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1021-1532 |
5.05e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 158.55 E-value: 5.05e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1021 ARTPGAMVGRGgevEAGTLIDVLAQRDldPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSV 1100
Cdd:PRK07788 39 LRLAADIRRYG---PFAGLVAHAARRA--PDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFV 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1101 LATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDASTRARLGESSCE------WVDLADLEAEAESG----DDI 1170
Cdd:PRK07788 114 LALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFTDLLSALPPDlgrlraWGGNPDDDEPSGSTdetlDDL 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1171 TDTERNGSVRL--TNLAYLIYTSGSTGRPKAVGVSHTGIVDfvnSLAKITTGTPEDEPDTRILhvASPSFDA---SMFEM 1245
Cdd:PRK07788 194 IAGSSTAPLPKppKPGGIVILTSGTTGTPKGAPRPEPSPLA---PLAGLLSRVPFRAGETTLL--PAPMFHAtgwAHLTL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1246 AWAIpaGHTLVIapQADFagDALATV--LERDEVTDMIITPSVLA---TVDPE-RAQY----VRNLATGGEACPPELVER 1315
Cdd:PRK07788 269 AMAL--GSTVVL--RRRF--DPEATLedIAKHKATALVVVPVMLSrilDLGPEvLAKYdtssLKIIFVSGSALSPELATR 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1316 WSER-GRRIFNCYGPTEATvWATRSRMT--AGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPG 1392
Cdd:PRK07788 343 ALEAfGPVLYNLYGSTEVA-FATIATPEdlAEAPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTDGRD 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1393 QTAVSfvadpfgepgaRMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGR 1472
Cdd:PRK07788 422 KQIID-----------GLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQ 490
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1473 KhteVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:PRK07788 491 R---LRAFVVKAPGAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
2580-3059 |
5.15e-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: 155.91 E-value: 5.15e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2580 DHVAVVDGaGARLTYRELDEASDRLARWLIGRG-VGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASM 2658
Cdd:cd05941 1 DRIAIVDD-GDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2659 IEDSGAVLGLsvlasgdlpgqefewmrldddsvaaeiaavpagpitdaerlgevtaaNLAYVIYTSGSTGRPKGVAVTHS 2738
Cdd:cd05941 80 ITDSEPSLVL-----------------------------------------------DPALILYTSGTTGRPKGVVLTHA 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2739 GLANFAR--------QESDR--------------------LNAGDNPVVLGFASPSFDASVLEYLLATVNEGTlayrPSe 2790
Cdd:cd05941 113 NLAANVRalvdawrwTEDDVllhvlplhhvhglvnallcpLFAGASVEFLPKFDPKEVAISRLMPSITVFMGV----PT- 187
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2791 avggeVLERFIAEHGATHTFLTPSVLSTMDPtavpsLRVIAAGGEAVPQPIVDRWAPATElHNL---YGPTEttIGITIS 2867
Cdd:cd05941 188 -----IYTRLLQYYEAHFTDPQFARAAAAER-----LRLMVSGSAALPVPTLEEWEAITG-HTLlerYGMTE--IGMALS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2868 SamrPGDPVRLGGPIG----GVDLMVLD-ERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRT 2942
Cdd:cd05941 255 N---PLDGERRPGTVGmplpGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKT 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2943 GDVVRWTPDtdtGGLTLeyTGR-SDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-----GGSVatalAAYIVPVDG 3016
Cdd:cd05941 325 GDLGVVDED---GYYWI--LGRsSVDIIKSGGYKVSALEIERVLLAHPGVSECAVIGVpdpdwGERV----VAVVVLRAG 395
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1827387616 3017 AVEVS--ELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05941 396 AAALSleELKEWAKQRLAPYKRPRRLILVDELPRNAMGKVNKKEL 440
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
2560-3059 |
6.85e-40 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 157.84 E-value: 6.85e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2560 PATDPVTLAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKT 2639
Cdd:PRK06188 7 LLHSGATYGHLLVSALKRYPDRPALVLG-DTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLA 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2640 GGAYVPIDPDYPAERVASMIEDSGA--------------------VLGLS-VLASGDLPGQEfewmrldddSVAAEIAAV 2698
Cdd:PRK06188 86 GLRRTALHPLGSLDDHAYVLEDAGIstlivdpapfveralallarVPSLKhVLTLGPVPDGV---------DLLAAAAKF 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2699 PAGPITDAERLGEVtaanlAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLgFASPSFDASVLEYLLAT 2778
Cdd:PRK06188 157 GPAPLVAAALPPDI-----AGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEWPADPRFL-MCTPLSHAGGAFFLPTL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2779 VNEGTLAYRPSEAVGgEVLeRFIAEHGATHTFLTPSVL-STMD-----PTAVPSLRVIAAGGEAVpQPivDRWAPATE-- 2850
Cdd:PRK06188 231 LRGGTVIVLAKFDPA-EVL-RAIEEQRITATFLVPTMIyALLDhpdlrTRDLSSLETVYYGASPM-SP--VRLAEAIErf 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2851 ---LHNLYGPTETTIGITIssaMR-----PGDPVRL---GGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDR 2919
Cdd:PRK06188 306 gpiFAQYYGQTEAPMVITY---LRkrdhdPDDPKRLtscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNR 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2920 SGLTAERFtANPYgtagqrmYRTGDVVRwtpdTDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV 2999
Cdd:PRK06188 383 PEETAEAF-RDGW-------LHTGDVAR----EDEDGF-YYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGV 449
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 3000 -----GGSVatalAAYIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK06188 450 pdekwGEAV----TAVVVLRPGAaVDAAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1-470 |
7.38e-40 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 157.37 E-value: 7.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:PRK07656 31 LTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTRYTADEAAYILARGDAKALFVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRFDDIVDV-HVLDISSPGDADL--------------DEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRG 145
Cdd:PRK07656 111 LFLGVDYSATTRLPALeHVVICETEEDDPHtekmktftdflaagDPAERAPEVDPDDVADILFTSGTTGRPKGAMLTHRQ 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 146 IAnRLAADIEQY-DLTARD----------VFLYKAPITfdvsvreifLPIAIGATLVIAepgRHGDPVHLADLIRRHGVT 214
Cdd:PRK07656 191 LL-SNAADWAEYlGLTEGDrylaanpffhVFGYKAGVN---------APLMRGATILPL---PVFDPDEVFRLIETERIT 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 215 VIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVIP- 293
Cdd:PRK07656 258 VLPGPPTMYNSLLQHPDRSAEDLSSLRLAVTGAASMPVALLERFESELGVDIVLTGYGLSEASGVTTFNRLDDDRKTVAg 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 294 -IGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarLYrTGDRARWNRDGeieY 372
Cdd:PRK07656 338 tIGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPEATAAAIDADGW------LH-TGDLGRLDEEG---Y 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 373 LGRTD----------FQVKLRgqrlelgEVEAALAAAPGVlhAAAAVVDGPG---GQQLVGYLAP---ADVDVDTVAATT 436
Cdd:PRK07656 408 LYIVDrkkdmfivggFNVYPA-------EVEEVLYEHPAV--AEAAVIGVPDerlGEVGKAYVVLkpgAELTEEELIAYC 478
|
490 500 510
....*....|....*....|....*....|....
gi 1827387616 437 AELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPE 470
Cdd:PRK07656 479 REHLAKYKVPRSIEFLDELPKNATGKVLKRALRE 512
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1064-1530 |
1.38e-39 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 154.42 E-value: 1.38e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDASt 1143
Cdd:cd05972 3 FRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1144 rarlgesscewvdladleaeaesgdditdterngsvrltNLAYLIYTSGSTGRPKAVGVSHTGIVDFvnslaKITTGTPE 1223
Cdd:cd05972 82 ---------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGH-----IPTAAYWL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1224 D-EPDTRILHVASPS---FDASMFEMAWAipAGHTLVIAPQADFAGDALATVLERDEVTDMIITPSV---LATVDPERAQ 1296
Cdd:cd05972 118 GlRPDDIHWNIADPGwakGAWSSFFGPWL--LGATVFVYEGPRFDAERILELLERYGVTSFCGPPTAyrmLIKQDLSSYK 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1297 Y--VRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVV 1373
Cdd:cd05972 196 FshLRLVVSAGEPLNPEVIEWWRAAtGLPIRDGYGQTETGLTVGNFPDMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1374 GEL--YLSTAGLARGYLGRPGQTAVSFVADpfgepgarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVL 1451
Cdd:cd05972 276 GDIaiKLPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1452 DAQPGVAQSVVVGV-ESTRGgrkhtEVV-AYLVAKPGATiDSAAVLDEAAQH----LAAHMVPSQAIVIDEIPLTPAGKL 1525
Cdd:cd05972 348 LEHPAVAEAAVVGSpDPVRG-----EVVkAFVVLTSGYE-PSEELAEELQGHvkkvLAPYKYPREIEFVEELPKTISGKI 421
|
....*
gi 1827387616 1526 DRAAL 1530
Cdd:cd05972 422 RRVEL 426
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1-468 |
1.98e-39 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 156.46 E-value: 1.98e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGghFVPLDeQLPVDRA---RYMVRTAGVRLVV 77
Cdd:COG1021 51 LSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAG--AIPVF-ALPAHRRaeiSHFAEQSEAVAYI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 78 VtsdgeAEARSRFDD---IVDV--------HVLDISSPGD----ADLDEEEFAGP---TRPANAAFTLFTSGSTGRPKAV 139
Cdd:COG1021 128 I-----PDRHRGFDYralARELqaevpslrHVLVVGDAGEftslDALLAAPADLSeprPDPDDVAFFQLSGGTTGLPKLI 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 140 VITHRGIAN--RLAADIeqYDLTARDVFLYKAPI--TFDVSVREIFLPIAIGATLVIAEpgrHGDPVHLADLIRRHGVTV 215
Cdd:COG1021 203 PRTHDDYLYsvRASAEI--CGLDADTVYLAALPAahNFPLSSPGVLGVLYAGGTVVLAP---DPSPDTAFPLIERERVTV 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 216 IHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTihRVTQDDRVIpIG 295
Cdd:COG1021 278 TALVPPLALLWLDAAERSRYDLSSLRVLQVGGAKLSPELARRVRPAL-GCTLQQVFGMAEGLVNYT--RLDDPEEVI-LT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 296 TPTRRVSA----RVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIE 371
Cdd:COG1021 354 TQGRPISPddevRIVDEDGNPVPPGEVGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 372 YLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDgpggqQLVGYLAPADVDVDTVAATTAEL--------LPE 442
Cdd:COG1021 427 VEGRAKDQINRGGEKIAAEEVENLLLAHPAVHDAAVvAMPD-----EYLGERSCAFVVPRGEPLTLAELrrflrergLAA 501
|
490 500
....*....|....*....|....*.
gi 1827387616 443 YMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:COG1021 502 FKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
2591-3056 |
2.60e-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: 153.69 E-value: 2.60e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2591 RLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAvlglSV 2670
Cdd:cd05903 1 RLTYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKA----KV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2671 LASGDlpgqefEWMRLDddsvaaeIAAVPAGPitdaerlgevtaanlAYVIYTSGSTGRPKGVAVTHSGLANFARQESDR 2750
Cdd:cd05903 77 FVVPE------RFRQFD-------PAAMPDAV---------------ALLLFTSGTTGEPKGVMHSHNTLSASIRQYAER 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2751 LNAGDNPVVLGfASP--SFDASVLEYLLATVnEGTLA-----YRPSEAVggevleRFIAEHGATHTFLTPSVLSTM---- 2819
Cdd:cd05903 129 LGLGPGDVFLV-ASPmaHQTGFVYGFTLPLL-LGAPVvlqdiWDPDKAL------ALMREHGVTFMMGATPFLTDLlnav 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2820 --DPTAVPSLRVIAAGGEAVPQPIVDRWAPA--TELHNLYGPTETTigiTISSAMRPGDPVRL----GGPIGGVDLMVLD 2891
Cdd:cd05903 201 eeAGEPLSRLRTFVCGGATVPRSLARRAAELlgAKVCSAYGSTECP---GAVTSITPAPEDRRlytdGRPLPGVEIKVVD 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2892 ERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTanpygtagQRMYRTGDVVRWtpdTDTGGLTLeyTGRSDDQVKL 2971
Cdd:cd05903 278 DTGATLAPGVEGELLSRGPSVFLGYLDRPDLTADAAP--------EGWFRTGDLARL---DEDGYLRI--TGRSKDIIIR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2972 RGLRIELGEIEAVLAEHDAVESAVVLGVGGS-VATALAAYIVPVDGA-VEVSELKA-FAGGRLPAYMVPSSFTVIDELPL 3048
Cdd:cd05903 345 GGENIPVLEVEDLLLGHPGVIEAAVVALPDErLGERACAVVVTKSGAlLTFDELVAyLDRQGVAKQYWPERLVHVDDLPR 424
|
....*...
gi 1827387616 3049 TPVGKLDK 3056
Cdd:cd05903 425 TPSGKVQK 432
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
2140-2533 |
2.66e-39 |
|
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: 153.69 E-value: 2.66e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2140 VLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPSGAAVTVVPAEVTVPWSVIDLRAEDAAsLDSRVEEVLATERTNPF 2219
Cdd:cd19539 29 AWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGVPRQEILPPGPAPLEVRDLSDPDSD-RERRLEELLRERESRGF 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2220 DMAKPPLIRVVLVEHG-DGAELVVTNHHLLIDGWSSPLVLADLLSLYATGQTFTGS-LPGTSG--RDFADHARAVATAD- 2294
Cdd:cd19539 108 DLDEEPPIRAVLGRFDpDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAApLPELRQqyKEYAAWQREALAAPr 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2295 VEAGIAAWREVLAPVTEPTLVAPGHEPS-ADAPPRDHQFSIDVKVTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRT 2373
Cdd:cd19539 188 AAELLDFWRRRLRGAEPTALPTDRPRPAgFPYPGADLRFELDAELVAALRELAKRARSSLFMVLLAAYCVLLRRYTGQTD 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2374 VTFAETVSGRSPDieGMESMVGMFINTIPAVVDVNPDATVVDVLTAVQNDKVKVLDHQQIGLPRLVAQ------TGLPAL 2447
Cdd:cd19539 268 IVVGTPVAGRNHP--RFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPFQQLVAElpvdrdAGRHPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2448 FDTLAVYESFPVNVDSVAGidassaGGLKLVGAKTSDATHYPLNLSASRRGAELALKLKYLPTAFAPEQVAVF-ADVLTG 2526
Cdd:cd19539 346 VQIVFQVTNAPAGELELAG------GLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQGFlADYLQV 419
|
....*..
gi 1827387616 2527 LLGAIAD 2533
Cdd:cd19539 420 LRQLLAN 426
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2586-3059 |
5.04e-39 |
|
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: 152.97 E-value: 5.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2586 DGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAv 2665
Cdd:cd05971 1 KGTPEKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGA- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2666 lglSVLasgdlpgqefewmrldddsvaaeiaavpagpITDAerlgevtAANLAYVIYTSGSTGRPKGVAVTHSGLA---- 2741
Cdd:cd05971 80 ---SAL-------------------------------VTDG-------SDDPALIIYTSGTTGPPKGALHAHRVLLghlp 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2742 ------NFARQESDrlnagdnpVVLGFASPSFDASVLEYLLATVNEGT--LAYRPSEAVGGEVLErFIAEHGATHTFLTP 2813
Cdd:cd05971 119 gvqfpfNLFPRDGD--------LYWTPADWAWIGGLLDVLLPSLYFGVpvLAHRMTKFDPKAALD-LMSRYGVTTAFLPP 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2814 SVLSTM-------DPTAVpSLRVIAAGGEAVPQPIVdRWAPAT---ELHNLYGPTETTIGITISSAMRPGDPVRLGGPIG 2883
Cdd:cd05971 190 TALKMMrqqgeqlKHAQV-KLRAIATGGESLGEELL-GWAREQfgvEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2884 GVDLMVLDERLRPVPVGMPGELyvaggALSR-------GYLDRSGLTAERFtANPYgtagqrmYRTGDVVRwtpdTDTGG 2956
Cdd:cd05971 268 GHRVAIVDDNGTPLPPGEVGEI-----AVELpdpvaflGYWNNPSATEKKM-AGDW-------LLTGDLGR----KDSDG 330
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2957 LtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVAT-ALAAYIVPVDGAVE----VSELKAFAGGRL 3031
Cdd:cd05971 331 Y-FWYVGRDDDVITSSGYRIGPAEIEECLLKHPAVLMAAVVGIPDPIRGeIVKAFVVLNPGETPsdalAREIQELVKTRL 409
|
490 500
....*....|....*....|....*...
gi 1827387616 3032 PAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05971 410 AAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
13-471 |
7.89e-39 |
|
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: 154.60 E-value: 7.89e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 13 LARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDGeaearsrfdd 92
Cdd:cd17647 33 VAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPARQNIYLGVAKPRGLIVIRAA---------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 93 ivDVHVLDISSPgdadldeeefagptrpanaafTL-FTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPI 171
Cdd:cd17647 103 --GVVVGPDSNP---------------------TLsFTSGSEGIPKGVLGRHFSLAYYFPWMAKRFNLSENDKFTMLSGI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 172 TFDVSVREIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMlaafNEVLGAGVGE-LTSLRLIQTGGEAL 250
Cdd:cd17647 160 AHDPIQRDMFTPLFLGAQLLVPTQDDIGTPGRLAEWMAKYGATVTHLTPAM----GQLLTAQATTpFPKLHHAFFVGDIL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 251 TPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVT---QDDR-------VIPIGTPTRRVSARVLDAALRE--VPIGVP 318
Cdd:cd17647 236 TKRDCLRLQTLAENVRIVNMYGTTETQRAVSYFEVPsrsSDPTflknlkdVMPAGRGMLNVQLLVVNRNDRTqiCGIGEV 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 319 GELYLGGVQLARGYAGRPDLTAERFVADPFGEPGA---------------------RLYRTGDRARWNRDGEIEYLGRTD 377
Cdd:cd17647 316 GEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDHwnyldkdnnepwrqfwlgprdRLYRTGDLGRYLPNGDCECCGRAD 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 378 FQVKLRGQRLELGEVEAALAAAPGVLHAAAAV-VDGPGGQQLVGYLAP----------ADVDVDTVAATTAEL------- 439
Cdd:cd17647 396 DQVKIRGFRIELGEIDTHISQHPLVRENITLVrRDKDEEPTLVSYIVPrfdkpddesfAQEDVPKEVSTDPIVkgligyr 475
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1827387616 440 -------------LPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEP 471
Cdd:cd17647 476 klikdireflkkrLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
570-996 |
9.04e-39 |
|
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: 151.75 E-value: 9.04e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 570 RLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDVLPVA-VAREQ 648
Cdd:cd19533 1 RLPLTSAQRGVWFAEQLDPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTpVPIRH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 649 LDWREADSVESLVRSTTEGfDVSTQMPLRGRFHRDGAGLHVA-------LTMHHIAMDGQSIPVLARDLMSAYAARAEGR 721
Cdd:cd19533 81 IDLSGDPDPEGAAQQWMQE-DLRKPLPLDNDPLFRHALFTLGdnrhfwyQRVHHIVMDGFSFALFGQRVAEIYTALLKGR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 722 TGG----LPVLDV-----QYADYALWQqsvlgdaddetsvlgEQLSHWRRVLAGLPAVTDLpmdRPRPAVLGTAGATVTV 792
Cdd:cd19533 160 PAPpapfGSFLDLveeeqAYRQSERFE---------------RDRAFWTEQFEDLPEPVSL---ARRAPGRSLAFLRRTA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 793 EFDDDLADRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVG 872
Cdd:cd19533 222 ELPPELTRTLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 873 DLLGNVRTTVLDAFANDQVQFDELIEALApeRSSSHQPLAQIAFTYTE-PTVNDVAGLEAsgiQAAPVDTGVVNakfDLT 951
Cdd:cd19533 302 ELVAQVSRELRSLLRHQRYRYEDLRRDLG--LTGELHPLFGPTVNYMPfDYGLDFGGVVG---LTHNLSSGPTN---DLS 373
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 1827387616 952 VAVRARSGGTPMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd19533 374 IFVYDRDDESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAAD 418
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
2565-3066 |
1.26e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 154.81 E-value: 1.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2565 VTLAELFRAAARRAPDHVAVvDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYV 2644
Cdd:PRK06178 33 RPLTEYLRAWARERPQRPAI-IFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2645 PIDPDYPAERVASMIEDSGA--VLGLSVLA------SGDLPGQEFEWMRLDD-----------DSVAA------------ 2693
Cdd:PRK06178 112 PVSPLFREHELSYELNDAGAevLLALDQLApvveqvRAETSLRHVIVTSLADvlpaeptlplpDSLRAprlaaagaidll 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2694 -EIAAVPAGPITDAERLGEVTAANlayviYTSGSTGRPKGVAVTHSGLA-NFARQESDRLNAGDNPVVLGFAsPSF---- 2767
Cdd:PRK06178 192 pALRACTAPVPLPPPALDALAALN-----YTGGTTGMPKGCEHTQRDMVyTAAAAYAVAVVGGEDSVFLSFL-PEFwiag 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2768 -DASVLEYLLATVNEGTLAYRPSEAVggevlERFIAEHGATHTFLT-PSVLSTMDPTAV-----PSLRVIAAGG--EAVP 2838
Cdd:PRK06178 266 eNFGLLFPLFSGATLVLLARWDAVAF-----MAAVERYRVTRTVMLvDNAVELMDHPRFaeydlSSLRQVRVVSfvKKLN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2839 QPIVDRWAPATE---LHNLYGPTETTIGITISSAMRPGD------PVRLGGPIGGVDLMVLD-ERLRPVPVGMPGELYVA 2908
Cdd:PRK06178 341 PDYRQRWRALTGsvlAEAAWGMTETHTCDTFTAGFQDDDfdllsqPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVR 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2909 GGALSRGYLDRSGLTAERFTANpygtagqrMYRTGDVVRWTPDtdtgGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEH 2988
Cdd:PRK06178 421 TPSLLKGYWNKPEATAEALRDG--------WLHTGDIGKIDEQ----GF-LHYLGRRKEMLKVNGMSVFPSEVEALLGQH 487
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2989 DAVESAVVLGVG----GSVATalaAYIVPVDGA-VEVSELKAFAGGRLPAYMVPsSFTVIDELPLTPVGKLDKRALpEPV 3063
Cdd:PRK06178 488 PAVLGSAVVGRPdpdkGQVPV---AFVQLKPGAdLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL-QAL 562
|
...
gi 1827387616 3064 LEA 3066
Cdd:PRK06178 563 AEE 565
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1038-1530 |
2.46e-38 |
|
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 440644 [Multi-domain] Cd Length: 533 Bit Score: 152.99 E-value: 2.46e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1038 TLIDVLAQR-DLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAayVPV 1116
Cdd:COG1021 26 TLGDLLRRRaERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1117 DpAYPADR---IAYMLEDSGATVGITDASTR-------AR--------------LGESScEWVDLADLEAEAESGDDITd 1172
Cdd:COG1021 104 F-ALPAHRraeISHFAEQSEAVAYIIPDRHRgfdyralARelqaevpslrhvlvVGDAG-EFTSLDALLAAPADLSEPR- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1173 terngsVRLTNLAYLIYTSGSTGRPKAVGVSHTgivDFVNSL---AKITTGTpedePDTRILHV---------ASPSFDA 1240
Cdd:COG1021 181 ------PDPDDVAFFQLSGGTTGLPKLIPRTHD---DYLYSVrasAEICGLD----ADTVYLAAlpaahnfplSSPGVLG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1241 SMFemawaipAGHTLVIAPQADfAGDALATVlERDEVTDMIITPSV----LATVDPERAQY--VRNLATGGEACPPELVE 1314
Cdd:COG1021 248 VLY-------AGGTVVLAPDPS-PDTAFPLI-ERERVTVTALVPPLallwLDAAERSRYDLssLRVLQVGGAKLSPELAR 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1315 RWsergRRIFNC-----YGPTEATVWATR------SRMTagkpvTIGKPV-DGFTVRVLDGRLHEVPQGVVGELYlsTAG 1382
Cdd:COG1021 319 RV----RPALGCtlqqvFGMAEGLVNYTRlddpeeVILT-----TQGRPIsPDDEVRIVDEDGNPVPPGEVGELL--TRG 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1383 --LARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQvkIN--GQRVELGEIEAVLDAQPGVA 1458
Cdd:COG1021 388 pyTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRRTPDGYLVVEGRAKDQ--INrgGEKIAAEEVENLLLAHPAVH 458
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 1459 QSVVVGVESTRGGRKhteVVAYLVAKpGATIDSAAVLDE-AAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:COG1021 459 DAAVVAMPDEYLGER---SCAFVVPR-GEPLTLAELRRFlRERGLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
2575-3064 |
9.68e-38 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 150.34 E-value: 9.68e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2575 ARRAPDHVAVVDGA-GARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAE 2653
Cdd:PRK09088 5 ARLQPQRLAAVDLAlGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2654 RVASMIEDSGA--VLGLSVLASGdlpgqefewmRLDDDSVAAEIAAVPAGPITDAERLgevTAANLAYVIYTSGSTGRPK 2731
Cdd:PRK09088 85 ELDALLQDAEPrlLLGDDAVAAG----------RTDVEDLAAFIASADALEPADTPSI---PPERVSLILFTSGTSGQPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2732 GVAVTHSGLANFARQESdRLNAGDNPVVLGFASPSFDASVLeyllatvnegTLAYRPSEAVGGEVL----------ERFI 2801
Cdd:PRK09088 152 GVMLSERNLQQTAHNFG-VLGRVDAHSSFLCDAPMFHIIGL----------ITSVRPVLAVGGSILvsngfepkrtLGRL 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2802 AEH--GATHTFLTPSVLS------TMDPTAVPSLRVIAAGGEAVPQPIVDRW-APATELHNLYGPTE--TTIGITISSAM 2870
Cdd:PRK09088 221 GDPalGITHYFCVPQMAQafraqpGFDAAALRHLTALFTGGAPHAAEDILGWlDDGIPMVDGFGMSEagTVFGMSVDCDV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2871 RPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVRWTP 2950
Cdd:PRK09088 301 IRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIARRDA 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2951 DtdtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG----GSVATalaAYIVPVDG-AVEVSELKA 3025
Cdd:PRK09088 374 D---GFFWV--VDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMAdaqwGEVGY---LAIVPADGaPLDLERIRS 445
|
490 500 510
....*....|....*....|....*....|....*....
gi 1827387616 3026 FAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVL 3064
Cdd:PRK09088 446 HLSTRLAKYKVPKHLRLVDALPRTASGKLQKARLRDALA 484
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
2582-3068 |
1.20e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 150.44 E-value: 1.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2582 VAVVDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIED 2661
Cdd:PRK08276 2 AVIMAPSGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2662 SGA-VL-------------------GLSVLA--SGDLPGqefewmrldDDSVAAEIAAVPAGPITDaERLGevtaanlAY 2719
Cdd:PRK08276 82 SGAkVLivsaaladtaaelaaelpaGVPLLLvvAGPVPG---------FRSYEEALAAQPDTPIAD-ETAG-------AD 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2720 VIYTSGSTGRPKGVAVTHSGL------ANFARQESDRLNAGDNPVVLGfASPSFDASVLEYLLAtvnegtlayrpSEAVG 2793
Cdd:PRK08276 145 MLYSSGTTGRPKGIKRPLPGLdpdeapGMMLALLGFGMYGGPDSVYLS-PAPLYHTAPLRFGMS-----------ALALG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2794 GEV--LERFIAE--------HGATHTFLTPSVLSTMD--PTAV------PSLRVIAAGGEAVPQPI----VDRWAPAteL 2851
Cdd:PRK08276 213 GTVvvMEKFDAEealalierYRVTHSQLVPTMFVRMLklPEEVrarydvSSLRVAIHAAAPCPVEVkramIDWWGPI--I 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2852 HNLYGPTETtIGITISSAM----RPGDpvrLGGPIGGVdLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAErf 2927
Cdd:PRK08276 291 HEYYASSEG-GGVTVITSEdwlaHPGS---VGKAVLGE-VRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAA-- 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2928 tanpyGTAGQRMYRTGDV--VrwtpDTDtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-----G 3000
Cdd:PRK08276 364 -----ARNPHGWVTVGDVgyL----DED-GYLYL--TDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVpdeemG 431
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 3001 GSVAtalaAYIVPVDGA----VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVLEAGE 3068
Cdd:PRK08276 432 ERVK----AVVQPADGAdagdALAAELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWEGRQ 499
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
2566-3062 |
1.47e-37 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 151.06 E-value: 1.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDGAGArLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVP 2645
Cdd:PRK13382 44 GPTSGFAIAAQRCPDRPGLIDELGT-LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILL 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2646 IDPDYPAERVASMIEDSGAV--------LGLSVLASGDLPG--QEFEWMRLDDDSVAAEIAAVPAG-PITDAERLGEVta 2714
Cdd:PRK13382 123 LNTSFAGPALAEVVTREGVDtviydeefSATVDRALADCPQatRIVAWTDEDHDLTVEVLIAAHAGqRPEPTGRKGRV-- 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2715 anlayVIYTSGSTGRPKGVAVTHSGLANFARQESDRLN-AGDNPVVLgfASPSFDA-----SVLEYLLATVNEGTLAYRP 2788
Cdd:PRK13382 201 -----ILLTSGTTGTPKGARRSGPGGIGTLKAILDRTPwRAEEPTVI--VAPMFHAwgfsqLVLAASLACTIVTRRRFDP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2789 SEAVggevleRFIAEHGATHTFLTPSVL--------STMDPTAVPSLRVIAAGGEAVPQPIV----DRWAPAteLHNLYG 2856
Cdd:PRK13382 274 EATL------DLIDRHRATGLAVVPVMFdrimdlpaEVRNRYSGRSLRFAAASGSRMRPDVViafmDQFGDV--IYNNYN 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2857 PTETTIGITISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYldRSGLTAERFTAnpygtag 2936
Cdd:PRK13382 346 ATEAGMIATATPADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTKDFHDG------- 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2937 qrMYRTGDVVRWtpdtDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGS-VATALAAYIVPVD 3015
Cdd:PRK13382 417 --FMASGDVGYL----DENGR-LFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEqYGQRLAAFVVLKP 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1827387616 3016 GAVEVSE-LKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEP 3062
Cdd:PRK13382 490 GASATPEtLKQHVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
13-464 |
2.36e-37 |
|
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: 149.40 E-value: 2.36e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 13 LARELTALGVGAEvAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRlVVVTSDgeaearsRFDD 92
Cdd:cd05909 20 LARKLAKMTKEGE-NVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIK-TVLTSK-------QFIE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 93 IVDVHVL-DISSPGD---------------------------ADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHR 144
Cdd:cd05909 91 KLKLHHLfDVEYDARivyledlrakiskadkckaflagkfppKWLLRIFGVAPVQPDDPAVILFTSGSEGLPKGVVLSHK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 145 GIANRLAADIEQYDLTARDVFLYKAPI--TFDVSVrEIFLPIAIGATLVIaepgrHGDPVH---LADLIRRHGVTVIHFV 219
Cdd:cd05909 171 NLLANVEQITAIFDPNPEDVVFGALPFfhSFGLTG-CLWLPLLSGIKVVF-----HPNPLDykkIPELIYDKKATILLGT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 220 PAMLAAFneVLGAGVGELTSLRLIQTGGEALTPPVaRDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTR 299
Cdd:cd05909 245 PTFLRGY--ARAAHPEDFSSLRLVVAGAEKLKDTL-RQEFQEKFGIRILEGYGTTECSPVISVNTPQSPNKEGTVGRPLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 300 RVSARVLD-AALREVPIGVPGELYLGGVQLARGYAGRPDLTAErfvadpfgEPGARLYRTGDRARWNRDGEIEYLGRTDF 378
Cdd:cd05909 322 GMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSF--------AFGDGWYDTGDIGKIDGEGFLTITGRLSR 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 379 QVKLRGQRLELGEVEAALAAAPG--VLHAAAAVVDGPGGQQLVGYLAPADVDVDTV--AATTAElLPEYMRPSAWVRLDA 454
Cdd:cd05909 394 FAKIAGEMVSLEAIEDILSEILPedNEVAVVSVPDGRKGEKIVLLTTTTDTDPSSLndILKNAG-ISNLAKPSYIHQVEE 472
|
490
....*....|
gi 1827387616 455 MPLSRSGKVD 464
Cdd:cd05909 473 IPLLGTGKPD 482
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1044-1533 |
2.72e-37 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 150.29 E-value: 2.72e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1044 AQRDldPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPAD 1123
Cdd:PRK13382 53 AQRC--PDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGP 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1124 RIAYMLEDSGATVGITDASTRARLGES---------SCEWVD-----LADLEAEAESGDDITDTERNGSVrltnlayLIY 1189
Cdd:PRK13382 131 ALAEVVTREGVDTVIYDEEFSATVDRAladcpqatrIVAWTDedhdlTVEVLIAAHAGQRPEPTGRKGRV-------ILL 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1190 TSGSTGRPKavGVSHTGIVDFvNSLAKITTGTP--EDEPdtriLHVASPSFDASMF-EMAWAIPAGHTLVIapQADFAGD 1266
Cdd:PRK13382 204 TSGTTGTPK--GARRSGPGGI-GTLKAILDRTPwrAEEP----TVIVAPMFHAWGFsQLVLAASLACTIVT--RRRFDPE 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1267 ALATVLERDEVTDMIITPS----VLATVDPERAQY----VRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWAT 1337
Cdd:PRK13382 275 ATLDLIDRHRATGLAVVPVmfdrIMDLPAEVRNRYsgrsLRFAAASGSRMRPDVVIAFMDQfGDVIYNNYNATEAGMIAT 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1338 RS-RMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYlgRPGQTAvsfvadpfgEPGARMYATGDL 1416
Cdd:PRK13382 355 ATpADLRAAPDTAGRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGY--TSGSTK---------DFHDGFMASGDV 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1417 VRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATIDSAAVLD 1496
Cdd:PRK13382 424 GYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQR---LAAFVVLKPGASATPETLKQ 500
|
490 500 510
....*....|....*....|....*....|....*..
gi 1827387616 1497 EAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEP 1533
Cdd:PRK13382 501 HVRDNLANYKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1042-1532 |
3.47e-37 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 148.85 E-value: 3.47e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1042 VLAQRDLDPDHPALICDGTEMDYDEFETRTNAIARALLAR-GVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAY 1120
Cdd:PRK06839 8 IEKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1121 PADRIAYMLEDSGATV-------GITDASTRARLGESSCEWV-DLADLEAEAESGDDitdtERNGSVrltnlAYLI-YTS 1191
Cdd:PRK06839 88 TENELIFQLKDSGTTVlfvektfQNMALSMQKVSYVQRVISItSLKEIEDRKIDNFV----EKNESA-----SFIIcYTS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1192 GSTGRPK-AVGVSHTGIVDFVNSLAKITTgTPEDEPDTRIlhvasPSFDASMFEMaWAIP---AGHTLVIAPQadFAGDA 1267
Cdd:PRK06839 159 GTTGKPKgAVLTQENMFWNALNNTFAIDL-TMHDRSIVLL-----PLFHIGGIGL-FAFPtlfAGGVIIVPRK--FEPTK 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1268 LATVLERDEVTDMIITPSVLATV--DPERA----QYVRNLATGGEACPPELVERWSERGRRIFNCYGPTEA--TVWATRS 1339
Cdd:PRK06839 230 ALSMIEKHKVTVVMGVPTIHQALinCSKFEttnlQSVRWFYNGGAPCPEELMREFIDRGFLFGQGFGMTETspTVFMLSE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1340 RMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSfVADPFgepgarmYATGDLVRV 1419
Cdd:PRK06839 310 EDARRKVGSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW-------LCTGDLARV 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1420 AKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEV-VAYLVAKPGATIDSAAVLDEA 1498
Cdd:PRK06839 382 DEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWG----EIpIAFIVKKSSSVLIEKDVIEHC 457
|
490 500 510
....*....|....*....|....*....|....
gi 1827387616 1499 AQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:PRK06839 458 RLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2592-3059 |
5.28e-37 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 146.89 E-value: 5.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2592 LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLglsvl 2671
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARL----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2672 asgdlpgqefewmrldddsvaaeiaavpagPITDAERLGEVTAANLAYvIYTSGSTGRPKGVAVTHSGLANFARQESDRL 2751
Cdd:cd05973 76 ------------------------------VVTDAANRHKLDSDPFVM-MFTSGTTGLPKGVPVPLRALAAFGAYLRDAV 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2752 NAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGGEVLERFIAEHGATHTFLTPSVLSTM--DPTAVP---- 2825
Cdd:cd05973 125 DLRPEDSFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAYRLLmaAGAEVParpk 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2826 -SLRVIAAGGEAVpQPIVDRWAPA---TELHNLYGPTEttIGITISSAMRPGDPVR---LGGPIGGVDLMVLDERLRPVP 2898
Cdd:cd05973 205 gRLRRVSSAGEPL-TPEVIRWFDAalgVPIHDHYGQTE--LGMVLANHHALEHPVHagsAGRAMPGWRVAVLDDDGDELG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2899 VGMPGELyvaggALSRgylDRSGLTAER-FTANPYGTAGQRMYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIE 2977
Cdd:cd05973 282 PGEPGRL-----AIDI---ANSPLMWFRgYQLPDTPAIDGGYYLTGDTVEFDPDG-----SFSFIGRADDVITMSGYRIG 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2978 LGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPVDGAVEVS-----ELKAFAGGRLPAYMVPSSFTVIDELPLTPVG 3052
Cdd:cd05973 349 PFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVLRGGHEGTpaladELQLHVKKRLSAHAYPRTIHFVDELPKTPSG 428
|
....*..
gi 1827387616 3053 KLDKRAL 3059
Cdd:cd05973 429 KIQRFLL 435
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1049-1527 |
6.14e-37 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 148.54 E-value: 6.14e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1049 DPDHPALI--CDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIA 1126
Cdd:cd05904 18 HPSRPALIdaATGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1127 YMLEDSGATVGITDASTRARLGESSCEWVDLADLEAEAESGDDITDTERNGS-----VRLTNLAYLIYTSGSTGRPKAVG 1201
Cdd:cd05904 98 KQVKDSGAKLAFTTAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAEppvvvIKQDDVAALLYSSGTTGRSKGVM 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1202 VSHTGivdFVNSLAKITTGT-PEDEPDTRIL------HVaspsFDASMFEMAwAIPAGHTLVIAPQADFaGDALATVlER 1274
Cdd:cd05904 178 LTHRN---LIAMVAQFVAGEgSNSDSEDVFLcvlpmfHI----YGLSSFALG-LLRLGATVVVMPRFDL-EELLAAI-ER 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1275 DEVTDMIITPSVL------ATVDPERAQYVRNLATGGEACPPELVERWSER--GRRIFNCYGPTEATVWATR---SRMTA 1343
Cdd:cd05904 248 YKVTHLPVVPPIVlalvksPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKfpNVDLGQGYGMTESTGVVAMcfaPEKDR 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1344 GKPVTIGKPVDGFTVRVLD---GRLheVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRVA 1420
Cdd:cd05904 328 AKYGSVGRLVPNVEAKIVDpetGES--LPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW-------LHTGDLCYID 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1421 KGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEV-VAYLVAKPGATIDSAAVLDEAA 1499
Cdd:cd05904 399 EDGYLFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAG----EVpMAFVVRKPGSSLTEDEIMDFVA 474
|
490 500
....*....|....*....|....*...
gi 1827387616 1500 QHLAAHMVPSQAIVIDEIPLTPAGKLDR 1527
Cdd:cd05904 475 KQVAPYKKVRKVAFVDAIPKSPSGKILR 502
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1058-1536 |
7.71e-37 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 148.13 E-value: 7.71e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1058 DGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVG 1137
Cdd:PRK08276 8 SGEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1138 ITDASTRARLGESSCE-----------------WVDLADLEAeAESGDDITDtERNGSVrltnlayLIYTSGSTGRPKAV 1200
Cdd:PRK08276 88 IVSAALADTAAELAAElpagvplllvvagpvpgFRSYEEALA-AQPDTPIAD-ETAGAD-------MLYSSGTTGRPKGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1201 --GVSHTGIVDFVNSLAKITTGTPEDEPDTRILhVASPSFDA--SMFEMaWAIPAGHTLVIAPQADfAGDALATVlERDE 1276
Cdd:PRK08276 159 krPLPGLDPDEAPGMMLALLGFGMYGGPDSVYL-SPAPLYHTapLRFGM-SALALGGTVVVMEKFD-AEEALALI-ERYR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1277 VTDMIITPS----VLATVDPERAQY----VRNLATGGEACPPE----LVERWserGRRIFNCYGPTEA--TVWATrSRMT 1342
Cdd:PRK08276 235 VTHSQLVPTmfvrMLKLPEEVRARYdvssLRVAIHAAAPCPVEvkraMIDWW---GPIIHEYYASSEGggVTVIT-SEDW 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1343 AGKPVTIGKPVDGfTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVadpfgepGARMYATGDLVRVAKG 1422
Cdd:PRK08276 311 LAHPGSVGKAVLG-EVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN-------PHGWVTVGDVGYLDED 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1423 GNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPGATIDSA---AVLDEAA 1499
Cdd:PRK08276 383 GYLYLTDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGVPDEEMGE---RVKAVVQPADGADAGDAlaaELIAWLR 459
|
490 500 510
....*....|....*....|....*....|....*..
gi 1827387616 1500 QHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEPHAP 1536
Cdd:PRK08276 460 GRLAHYKCPRSIDFEDELPRTPTGKLYKRRLRDRYWE 496
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
2-468 |
1.10e-36 |
|
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate CoA ligase and 4-hydroxybenzoate-coenzyme A ligase catalyze the first activating step for benzoate and 4-hydroxybenzoate catabolic pathways, respectively. Although these two enzymes share very high sequence homology, they have their own substrate preference. The reaction proceeds via a two-step process; the first ATP-dependent step forms the substrate-AMP intermediate, while the second step forms the acyl-CoA ester, releasing the AMP. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Some bacteria can use benzoic acid or benzenoid compounds as the sole source of carbon and energy through degradation. Benzoate CoA ligase and 4-hydroxybenzoate-Coenzyme A ligase are key enzymes of this process.
Pssm-ID: 341269 [Multi-domain] Cd Length: 508 Bit Score: 147.90 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSD 81
Cdd:cd05959 31 TYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYLEDSRARVVVVSGE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 ----GEAEARSRFDDIVDVHVLDISSPGDADLDEEEF---------AGPTRPANAAFTLFTSGSTGRPKAVVITHRGI-- 146
Cdd:cd05959 111 lapvLAAALTKSEHTLVVLIVSGGAGPEAGALLLAELvaaeaeqlkPAATHADDPAFWLYSSGSTGRPKGVVHLHADIyw 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 147 -ANRLAADIeqYDLTARDVFLYKAPITFDVSV-REIFLPIAIGATLVIaEPGRHgDPVHLADLIRRHGVTVIHFVPAMLA 224
Cdd:cd05959 191 tAELYARNV--LGIREDDVCFSAAKLFFAYGLgNSLTFPLSVGATTVL-MPERP-TPAAVFKRIRRYRPTVFFGVPTLYA 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 225 AFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEAsivVTIHRVTQDDRVIPiGTPTRRV--- 301
Cdd:cd05959 267 AMLAAPNLPSRDLSSLRLCVSAGEALPAEVGERWKARF-GLDILDGIGSTEM---LHIFLSNRPGRVRY-GTTGKPVpgy 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 302 SARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVadpfGEpgarLYRTGDRARWNRDGEIEYLGRTDFQVK 381
Cdd:cd05959 342 EVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTFQ----GE----WTRTGDKYVRDDDGFYTYAGRADDMLK 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 382 LRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAPADVDVDTVAATT------AELLPEYMRPSAWVRLDA 454
Cdd:cd05959 414 VSGIWVSPFEVESALVQHPAVLEAAVvGVEDEDGLTKPKAFVVLRPGYEDSEALEEelkefvKDRLAPYKYPRWIVFVDE 493
|
490
....*....|....
gi 1827387616 455 MPLSRSGKVDRRLL 468
Cdd:cd05959 494 LPKTATGKIQRFKL 507
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
2566-3065 |
1.12e-36 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 148.36 E-value: 1.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVP 2645
Cdd:PRK06087 24 SLADYWQQTARAMPDKIAVVDNHGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2646 IDPDYPAERVASMIEDSGAV--LGLSVLASGDlPGQEFEWMRLDDDSVAAEIAAVPAGPITDAERLGEVTAAN------- 2716
Cdd:PRK06087 104 LLPSWREAELVWVLNKCQAKmfFAPTLFKQTR-PVDLILPLQNQLPQLQQIVGVDKLAPATSSLSLSQIIADYeplttai 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2717 ------LAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVV-----LGFASPSFDASVLEYLLATVNEGTLA 2785
Cdd:PRK06087 183 tthgdeLAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFmmpapLGHATGFLHGVTAPFLIGARSVLLDI 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2786 YRPSEAVGGEVLERFIAEHGAthtflTPSVLSTM-----DPTAVPSLRVIAAGGEAVPQPIV-DRWAPATELHNLYGPTE 2859
Cdd:PRK06087 263 FTPDACLALLEQQRCTCMLGA-----TPFIYDLLnllekQPADLSALRFFLCGGTTIPKKVArECQQRGIKLLSVYGSTE 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2860 TTIGITIssamRPGDPVRL-----GGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYgt 2934
Cdd:PRK06087 338 SSPHAVV----NLDDPLSRfmhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGW-- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2935 agqrmYRTGDVVRwtpdTDTGGlTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGS-VATALAAYIVP 3013
Cdd:PRK06087 412 -----YYSGDLCR----MDEAG-YIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDErLGERSCAYVVL 481
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 3014 VDG--AVEVSELKAF-AGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVLE 3065
Cdd:PRK06087 482 KAPhhSLTLEEVVAFfSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDIMR 536
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
2566-3061 |
1.28e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 148.15 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDGAGaRLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVP 2645
Cdd:PRK07788 50 PFAGLVAHAARRAPDRAALIDERG-TLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIIL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2646 IDPDYPAERVASMIEDSGAVL--------GLSVLASGDLPGQEFEWMRLDDDSVAAE--------IAAVPAGPITDAERL 2709
Cdd:PRK07788 129 LNTGFSGPQLAEVAAREGVKAlvyddeftDLLSALPPDLGRLRAWGGNPDDDEPSGStdetlddlIAGSSTAPLPKPPKP 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2710 GevtaanlAYVIYTSGSTGRPKGVAVTH-SGLANFArQESDRLNAGDNPVVLgFASPSFDA-SVLEYLLATVNEGTLAYR 2787
Cdd:PRK07788 209 G-------GIVILTSGTTGTPKGAPRPEpSPLAPLA-GLLSRVPFRAGETTL-LPAPMFHAtGWAHLTLAMALGSTVVLR 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2788 ----PSEAVggevleRFIAEHGATHTFLTPSVLSTM---DPTAVP-----SLRVIAAGGEAVPQPIVDRwapATE----- 2850
Cdd:PRK07788 280 rrfdPEATL------EDIAKHKATALVVVPVMLSRIldlGPEVLAkydtsSLKIIFVSGSALSPELATR---ALEafgpv 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2851 LHNLYGPTEttigITISSAMRPGD----PVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDrsgltaer 2926
Cdd:PRK07788 351 LYNLYGSTE----VAFATIATPEDlaeaPGTVGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD-------- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2927 fTANPYGTAGqrMYRTGDVVRWTPDtdtgGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGG-SVAT 3005
Cdd:PRK07788 419 -GRDKQIIDG--LLSSGDVGYFDED----GL-LFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDeEFGQ 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 3006 ALAAYIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPE 3061
Cdd:PRK07788 491 RLRAFVVKAPGAaLDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELRE 547
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1050-1530 |
1.57e-36 |
|
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: 146.89 E-value: 1.57e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALI--CDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAY 1127
Cdd:cd05923 15 PDACAIAdpARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1128 MLE-DSGATVGITDAS--TRARLGESSCEWV--DLADLEAEAESGDDITDTERngsvRLTNLAYLIYTSGSTGRPKAVGV 1202
Cdd:cd05923 95 LIErGEMTAAVIAVDAqvMDAIFQSGVRVLAlsDLVGLGEPESAGPLIEDPPR----EPEQPAFVFYTSGTTGLPKGAVI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1203 SHTGI---VDFVNSLAKITTGTPEdepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFAGDALATVlERDEVTD 1279
Cdd:cd05923 171 PQRAAesrVLFMSTQAGLRHGRHN-----VVLGLMPLYHVIGFFAVLVAALALDGTYVVVEEFDPADALKLI-EQERVTS 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1280 MIITPSVL------ATVDPERAQYVRNLATGGEACPPELVERWSE-RGRRIFNCYGPTEATvwaTRSRMTAGKPVTIGKP 1352
Cdd:cd05923 245 LFATPTHLdalaaaAEFAGLKLSSLRHVTFAGATMPDAVLERVNQhLPGEKVNIYGTTEAM---NSLYMRDARTGTEMRP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1353 vdGF-----TVRVLDGRLHEVPQGVVGELYLSTAGLA--RGYLGRPGQTAVSFVAdpfgepgaRMYATGDLVRVAKGGNL 1425
Cdd:cd05923 322 --GFfsevrIVRIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD--------GWYRTGDVGYVDPSGDV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1426 EFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATidSAAVLDE--AAQHLA 1503
Cdd:cd05923 392 RILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERWGQS---VTACVVPREGTL--SADELDQfcRASELA 466
|
490 500
....*....|....*....|....*..
gi 1827387616 1504 AHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd05923 467 DFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1050-1537 |
1.93e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 148.27 E-value: 1.93e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:PRK06178 47 PQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELSYEL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGIT-DA------STRARLGESSCEWVDLAD-------------LEAEAESGDDITD---TERNGSVR------ 1180
Cdd:PRK06178 127 NDAGAEVLLAlDQlapvveQVRAETSLRHVIVTSLADvlpaeptlplpdsLRAPRLAAAGAIDllpALRACTAPvplppp 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1181 -LTNLAYLIYTSGSTGRPKavGVSHTGiVDFVNSLAKITT-GTPEDEPDtrILHVASPSF--DASMFEMAWAIPAGHTLV 1256
Cdd:PRK06178 207 aLDALAALNYTGGTTGMPK--GCEHTQ-RDMVYTAAAAYAvAVVGGEDS--VFLSFLPEFwiAGENFGLLFPLFSGATLV 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1257 IAPQADfAGDALATVlERDEVTDMIITpsvlatVD--------PERAQY-VRNLATGGEAC-----PPELVERWSE-RGR 1321
Cdd:PRK06178 282 LLARWD-AVAFMAAV-ERYRVTRTVML------VDnavelmdhPRFAEYdLSSLRQVRVVSfvkklNPDYRQRWRAlTGS 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1322 RIFN-CYGPTEATvwaTRSRMTAG----------KPVTIGKPVDGFTVRVLDGRLHE-VPQGVVGELYLSTAGLARGYLG 1389
Cdd:PRK06178 354 VLAEaAWGMTETH---TCDTFTAGfqdddfdllsQPVFVGLPVPGTEFKICDFETGElLPLGAEGEIVVRTPSLLKGYWN 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1390 RPGQTAVSFVADpfgepgarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTR 1469
Cdd:PRK06178 431 KPEATAEALRDG--------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPD 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 1470 GGRkhtEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPsQAIVIDEIPLTPAGKLDRAALpEPHAPE 1537
Cdd:PRK06178 503 KGQ---VPVAFVQLKPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL-QALAEE 565
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1064-1530 |
2.54e-36 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 144.97 E-value: 2.54e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDAST 1143
Cdd:cd05973 3 FGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVTDAAN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1144 RARLGEsscewvdladleaeaesgdditdterngsvrltNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPE 1223
Cdd:cd05973 83 RHKLDS---------------------------------DPFVMMFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLRPE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1224 DepdtRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFAGDALATVLERDEVTDMIITPSV---LATVDPERAQYV-- 1298
Cdd:cd05973 130 D----SFWNAADPGWAYGLYYAITGPLALGHPTILLEGGFSVESTWRVIERLGVTNLAGSPTAyrlLMAAGAEVPARPkg 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1299 --RNLATGGEACPPELVeRWSER--GRRIFNCYGPTE-----ATVWATRSRMTAGkpvTIGKPVDGFTVRVLDGRLHEVP 1369
Cdd:cd05973 206 rlRRVSSAGEPLTPEVI-RWFDAalGVPIHDHYGQTElgmvlANHHALEHPVHAG---SAGRAMPGWRVAVLDDDGDELG 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1370 QGVVGELYLSTAGLA----RGYLGRPGQTAVsfvadpfgepgARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELG 1445
Cdd:cd05973 282 PGEPGRLAIDIANSPlmwfRGYQLPDTPAID-----------GGYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRIGPF 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1446 EIEAVLDAQPGVAQSVVVGVESTrggrKHTEVV-AYLVAKPGaTIDSAAVLDEAAQH----LAAHMVPSQAIVIDEIPLT 1520
Cdd:cd05973 351 DVESALIEHPAVAEAAVIGVPDP----ERTEVVkAFVVLRGG-HEGTPALADELQLHvkkrLSAHAYPRTIHFVDELPKT 425
|
490
....*....|
gi 1827387616 1521 PAGKLDRAAL 1530
Cdd:cd05973 426 PSGKIQRFLL 435
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1050-1525 |
3.20e-36 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 146.18 E-value: 3.20e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:PRK06145 16 PDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYIL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDASTRARLGESSCEWVDLADLEAE----AESGDDITDTErngSVRLTNLAYLIYTSGSTGRPKAVGVSHT 1205
Cdd:PRK06145 96 GDAGAKLLLVDEEFDAIVALETPKIVIDAAAQADsrrlAQGGLEIPPQA---AVAPTDLVRLMYTSGTTDRPKGVMHSYG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1206 GI----VDFVNSLAkITTgtpedepDTRILhVASPSFDASMFEMAWAIPAGHTLVIAPQADFAGDALATVLERDEVTDMI 1281
Cdd:PRK06145 173 NLhwksIDHVIALG-LTA-------SERLL-VVGPLYHVGAFDLPGIAVLWVGGTLRIHREFDPEAVLAAIERHRLTCAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1282 ITPSVLATV--DPERAQY----VRNLATGGEACPPELVERWSE--RGRRIFNCYGPTEATVWATrsRMTAGKPV----TI 1349
Cdd:PRK06145 244 MAPVMLSRVltVPDRDRFdldsLAWCIGGGEKTPESRIRDFTRvfTRARYIDAYGLTETCSGDT--LMEAGREIekigST 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1350 GKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmyATGDLVRVAKGGNLEFAG 1429
Cdd:PRK06145 322 GRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RSGDVGYLDEEGFLYLTD 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1430 RADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKHTEVVaylVAKPGATIDSAAVLDEAAQHLAAHMVPS 1509
Cdd:PRK06145 394 RKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRWGERITAVV---VLNPGATLTLEALDRHCRQRLASFKVPR 470
|
490
....*....|....*.
gi 1827387616 1510 QAIVIDEIPLTPAGKL 1525
Cdd:PRK06145 471 QLKVRDELPRNPSGKV 486
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1-463 |
3.34e-36 |
|
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: 145.82 E-value: 3.34e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:cd05911 11 LTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVIFTDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DG-----EAEARSRFDD---IVDVHVLDISSPGDADLDEEEFAGPTRPA-------NAAFTLFTSGSTGRPKAVVITHRG 145
Cdd:cd05911 91 DGlekvkEAAKELGPKDkiiVLDDKPDGVLSIEDLLSPTLGEEDEDLPPplkdgkdDTAAILYSSGTTGLPKGVCLSHRN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 146 -IAN-RLAADIEQYDLTARDVFLykAPITFDvsvrEIF-LPIAI-----GATLVIAepgRHGDPVHLADLIRRHGVTVIH 217
Cdd:cd05911 171 lIANlSQVQTFLYGNDGSNDVIL--GFLPLY----HIYgLFTTLasllnGATVIIM---PKFDSELFLDLIEKYKITFLY 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 218 FVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASiVVTIHRVTQDDRVIPIGTP 297
Cdd:cd05911 242 LVPPIAAALAKSPLLDKYDLSSLRVILSGGAPLSKELQELLAKRFPNATIKQGYGMTETG-GILTVNPDGDDKPGSVGRL 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 298 TRRVSARVLDAALRE-VPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGE------- 369
Cdd:cd05911 321 LPNVEAKIVDDDGKDsLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW-------LHTGDIGYFDEDGYlyivdrk 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 370 ---IEYLGrtdFQVKLRgqrlelgEVEAALAAAPGVLHAA--------------AAVVDGPGGQqlvgyLAPADVdVDTV 432
Cdd:cd05911 394 kelIKYKG---FQVAPA-------ELEAVLLEHPGVADAAvigipdevsgelprAYVVRKPGEK-----LTEKEV-KDYV 457
|
490 500 510
....*....|....*....|....*....|..
gi 1827387616 433 aattAELLPEYMRPSAWVR-LDAMPLSRSGKV 463
Cdd:cd05911 458 ----AKKVASYKQLRGGVVfVDEIPKSASGKI 485
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1050-1525 |
4.43e-36 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 146.64 E-value: 4.43e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLAR-GVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYM 1128
Cdd:PRK08314 24 PDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1129 LEDSGATVGITDASTRARL----GESSCEWV------------------DLADLEAEAESGDDI-----TDTERNG---- 1177
Cdd:PRK08314 104 VTDSGARVAIVGSELAPKVapavGNLRLRHVivaqysdylpaepeiavpAWLRAEPPLQALAPGgvvawKEALAAGlapp 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1178 --SVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtRILHVAsPSFDASMFE--MAWAIPAGH 1253
Cdd:PRK08314 184 phTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPES----VVLAVL-PLFHVTGMVhsMNAPIYAGA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1254 TLVIAPQADfaGDALATVLERDEVTDMIITPSVLatVD----PERAQY----VRNLATGGEACPPELVERWSER-GRRIF 1324
Cdd:PRK08314 259 TVVLMPRWD--REAAARLIERYRVTHWTNIPTMV--VDflasPGLAERdlssLRYIGGGGAAMPEAVAERLKELtGLDYV 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1325 NCYGPTEaTVWATRSR-MTAGKPVTIGKPVDGFTVRVLDGR-LHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVA-D 1401
Cdd:PRK08314 335 EGYGLTE-TMAQTHSNpPDRPKLQCLGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiD 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1402 pfgepGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYL 1481
Cdd:PRK08314 414 -----GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATPDPRRGE---TVKAVV 485
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1827387616 1482 VAKPGA--TIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKL 1525
Cdd:PRK08314 486 VLRPEArgKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
2566-3061 |
8.00e-36 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 145.97 E-value: 8.00e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVD-----GAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTG 2640
Cdd:PRK13295 25 TINDDLDACVASCPDKTAVTAvrlgtGAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIG 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2641 GAYVPIDPDYPAERVASMIEDSGAVLglsVLASGDLPGQEFEWM--RL----------------DDDSVAAEIAAVP--- 2699
Cdd:PRK13295 105 AVLNPLMPIFRERELSFMLKHAESKV---LVVPKTFRGFDHAAMarRLrpelpalrhvvvvggdGADSFEALLITPAweq 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2700 ---AGPITDAERLGevtAANLAYVIYTSGSTGRPKGVAVTH----SGLANFARqesdRLNAGDNPVVLGfASPSFDASVL 2772
Cdd:PRK13295 182 epdAPAILARLRPG---PDDVTQLIYTSGTTGEPKGVMHTAntlmANIVPYAE----RLGLGADDVILM-ASPMAHQTGF 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2773 EY--LLATVNEGTLAYR----PSEAVggevleRFIAEHGATHTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQP 2840
Cdd:PRK13295 254 MYglMMPVMLGATAVLQdiwdPARAA------ELIRTEGVTFTMASTPFLTDLtravkeSGRPVSSLRTFLCAGAPIPGA 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2841 IVDRWAPATELH--NLYGPTETTIGITIssamRPGDPVRL-----GGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALS 2913
Cdd:PRK13295 328 LVERARAALGAKivSAWGMTENGAVTLT----KLDDPDERasttdGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNF 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2914 RGYLDRSGLTaerftanpyGTAGQRMYRTGDVVRWTPDtdtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVES 2993
Cdd:PRK13295 404 GGYLKRPQLN---------GTDADGWFDTGDLARIDAD---GYIRI--SGRSKDVIIRGGENIPVVEIEALLYRHPAIAQ 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 2994 AVVLGVG----GSVAtalAAYIVPVDGA-VEVSELKAFAGG-RLPAYMVPSSFTVIDELPLTPVGKLDKRALPE 3061
Cdd:PRK13295 470 VAIVAYPderlGERA---CAFVVPRPGQsLDFEEMVEFLKAqKVAKQYIPERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
2-468 |
8.89e-36 |
|
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: 143.58 E-value: 8.89e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVA-VGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvts 80
Cdd:cd05941 13 TYADLVARAARLANRLLALGKDLRGDrVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITDSEPSLVL--- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeaearsrfddivdvhvldisspgdadldeeefagptrpaNAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd05941 90 -----------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVDAWRWT 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPItFDVS--VREIFLPIAIGATLVIAepgRHGDPVHLADLIRRHGVTVIHFVPAML--------AAFNEVL 230
Cdd:cd05941 129 EDDVLLHVLPL-HHVHglVNALLCPLFAGASVEFL---PKFDPKEVAISRLMPSITVFMGVPTIYtrllqyyeAHFTDPQ 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 231 GAGVGELTSLRLIQTGGEALTPPVARDLmVRLPGTRLQNQYGPAEASIVVTiHRVTQDDRVIPIGTPTRRVSARVLD-AA 309
Cdd:cd05941 205 FARAAAAERLRLMVSGSAALPVPTLEEW-EAITGHTLLERYGMTEIGMALS-NPLDGERRPGTVGMPLPGVQARIVDeET 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 310 LREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRT-DFQVKLRGQRLE 388
Cdd:cd05941 283 GEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEFTDDGW-------FKTGDLGVVDEDGYYWILGRSsVDIIKSGGYKVS 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 389 LGEVEAALAAAPGVlhAAAAVVDGPG---GQQLVGYLAPAD----VDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSG 461
Cdd:cd05941 356 ALEIERVLLAHPGV--SECAVIGVPDpdwGERVVAVVVLRAgaaaLSLEELKEWAKQRLAPYKRPRRLILVDELPRNAMG 433
|
....*..
gi 1827387616 462 KVDRRLL 468
Cdd:cd05941 434 KVNKKEL 440
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
2567-3075 |
1.01e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 145.18 E-value: 1.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2567 LAELFRAAARRAPDHVAVVDGAGaRLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPI 2646
Cdd:PRK07470 9 LAHFLRQAARRFPDRIALVWGDR-SWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2647 DPDYPAERVASMIEDSGAVLglsVLASGDLPGQ---------EFEWMRLDDD-----SVAAEIAAVPAGPITDAErlgeV 2712
Cdd:PRK07470 88 NFRQTPDEVAYLAEASGARA---MICHADFPEHaaavraaspDLTHVVAIGGaraglDYEALVARHLGARVANAA----V 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2713 TAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNP--VVLGFASPSFDASVleYLLATVNEG-TLAYRPS 2789
Cdd:PRK07470 161 DHDDPCWFFFTSGTTGRPKAAVLTHGQMAFVITNHLADLMPGTTEqdASLVVAPLSHGAGI--HQLCQVARGaATVLLPS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2790 EAVGGEVLERFIAEHGATHTFLTPSVLSTM--DPTAV----PSLR-VIAAGGeavPQPIVDRWAPATELHNL----YGPT 2858
Cdd:PRK07470 239 ERFDPAEVWALVERHRVTNLFTVPTILKMLveHPAVDrydhSSLRyVIYAGA---PMYRADQKRALAKLGKVlvqyFGLG 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2859 ETTIGITISSA----MRPGDPVRLGG---PIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANp 2931
Cdd:PRK07470 316 EVTGNITVLPPalhdAEDGPDARIGTcgfERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDG- 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2932 ygtagqrMYRTGDVVRwtpdTDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG----GSVATAL 3007
Cdd:PRK07470 395 -------WFRTGDLGH----LDARGF-LYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPdpvwGEVGVAV 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 3008 aayIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVLEAGEYVAPATG 3075
Cdd:PRK07470 463 ---CVARDGApVDEAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVREELEERGLLDLERAP 528
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
2108-2530 |
1.11e-35 |
|
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: 142.58 E-value: 1.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2108 PMTPLQQGLFFQADLAntvADHDAidvYVTQTVLSLTgdvDPGRLRS---ALSELLARQRVLRSGFVR--LPsgAAVTVV 2182
Cdd:cd19544 3 PLAPLQEGILFHHLLA---EEGDP---YLLRSLLAFD---SRARLDAflaALQQVIDRHDILRTAILWegLS--EPVQVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2183 PAEVTVPwsVIDLRAEDAASLDSRVEEVLATERTnPFDMAKPPLIRVVLVEHGDGAE--LVVTNHHLLIDGWSSPLVLAD 2260
Cdd:cd19544 72 WRQAELP--VEELTLDPGDDALAQLRARFDPRRY-RLDLRQAPLLRAHVAEDPANGRwlLLLLFHHLISDHTSLELLLEE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2261 LLsLYATGQTftGSLPG-TSGRDFADHARAVATAdvEAGIAAWREVLAPVTEPTlvAP---GHEPSADAPPRDHQFSIDV 2336
Cdd:cd19544 149 IQ-AILAGRA--AALPPpVPYRNFVAQARLGASQ--AEHEAFFREMLGDVDEPT--APfglLDVQGDGSDITEARLALDA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2337 KVTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAeTV-SGRSPDIEGMESMVGMFINTIPAVVDVNpDATVVD 2415
Cdd:cd19544 222 ELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFG-TVlSGRMQGGAGADRALGMFINTLPLRVRLG-GRSVRE 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2416 VLTAVQNDKVKVLDHQQIGLPrlVAQ--TGLPA---LFDTLAVYESfpvNVDSVAGIDASSAGGLKLVGAKtsDATHYPL 2490
Cdd:cd19544 300 AVRQTHARLAELLRHEHASLA--LAQrcSGVPAptpLFSALLNYRH---SAAAAAAAALAAWEGIELLGGE--ERTNYPL 372
|
410 420 430 440
....*....|....*....|....*....|....*....|.
gi 1827387616 2491 NLSASRRGAELALKLKYLPtAFAPEQV-AVFADVLTGLLGA 2530
Cdd:cd19544 373 TLSVDDLGDGFSLTAQVVA-PIDAERVcAYMETALEQLVDA 412
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1050-1539 |
1.35e-35 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 145.20 E-value: 1.35e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALIC------DGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPAD 1123
Cdd:PRK13295 38 PDKTAVTAvrlgtgAPRRFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRER 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1124 RIAYMLEDSGATVGITDASTR--------ARL----------------GESSCEWVdLADLEAEAESGDD-ITDTERNGS 1178
Cdd:PRK13295 118 ELSFMLKHAESKVLVVPKTFRgfdhaamaRRLrpelpalrhvvvvggdGADSFEAL-LITPAWEQEPDAPaILARLRPGP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1179 vrlTNLAYLIYTSGSTGRPKavGVSHT------GIVDFVNSLAKittgTPEDepdtrILHVASPSFDAS--MFEMAWAIP 1250
Cdd:PRK13295 197 ---DDVTQLIYTSGTTGEPK--GVMHTantlmaNIVPYAERLGL----GADD-----VILMASPMAHQTgfMYGLMMPVM 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1251 AGHTLVIAPQADFAgdALATVLERDEVT-DMIITP--SVLATVDPERAQYVRNLAT---GGEACPPELVERWSER-GRRI 1323
Cdd:PRK13295 263 LGATAVLQDIWDPA--RAAELIRTEGVTfTMASTPflTDLTRAVKESGRPVSSLRTflcAGAPIPGALVERARAAlGAKI 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1324 FNCYGPTEATVwatrsrMTAGKP--------VTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTA 1395
Cdd:PRK13295 341 VSAWGMTENGA------VTLTKLddpderasTTDGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1396 VSfvADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKht 1475
Cdd:PRK13295 415 TD--ADGW-------FDTGDLARIDADGYIRISGRSKDVIIRGGENIPVVEIEALLYRHPAIAQVAIVAYPDERLGER-- 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 1476 eVVAYLVAKPGATIDSAAVLD-EAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEPHAPEPA 1539
Cdd:PRK13295 484 -ACAFVVPRPGQSLDFEEMVEfLKAQKVAKQYIPERLVVRDALPRTPSGKIQKFRLREMLRGEDA 547
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1060-1504 |
1.38e-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: 143.12 E-value: 1.38e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1060 TEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGIT 1139
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1140 DastrarlgesscewvDLADLeaeaesgdditdterngsvrltnlAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITT 1219
Cdd:cd05907 84 E---------------DPDDL------------------------ATIIYTSGTTGRPKGVMLSHRNILSNALALAERLP 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1220 GTPEDepdtRIL------HVaspsFDASMFEMAWaIPAGHTLVIAPQADFAGDALATVlerdEVTDMIITPSVLATV--- 1290
Cdd:cd05907 125 ATEGD----RHLsflplaHV----FERRAGLYVP-LLAGARIYFASSAETLLDDLSEV----RPTVFLAVPRVWEKVyaa 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1291 -----DPE---------RAQYVRNLATGGEACPPELVERWSERGRRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGF 1356
Cdd:cd05907 192 ikvkaVPGlkrklfdlaVGGRLRFAASGGAPLPAELLHFFRALGIPVYEGYGLTETSAVVTLNPPGDNRIGTVGKPLPGV 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1357 TVRVldgrlhevpqGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRVAKGGNLEFAGRA-DHQV 1435
Cdd:cd05907 272 EVRI----------ADDGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLHITGRKkDLII 334
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 1436 KINGQRVELGEIEAVLDAQPGVAQSVVVGvestrGGRKHteVVAyLVakpgaTIDSAAVLDEAAQHLAA 1504
Cdd:cd05907 335 TSGGKNISPEPIENALKASPLISQAVVIG-----DGRPF--LVA-LI-----VPDPEALEAWAEEHGIA 390
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
2592-3059 |
2.76e-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: 141.71 E-value: 2.76e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2592 LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAvlglsvl 2671
Cdd:cd05972 1 WSFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2672 asgdlpgqefewmrldddsvaaeiaavpAGPITDAErlgevtaaNLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRL 2751
Cdd:cd05972 74 ----------------------------KAIVTDAE--------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWL 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2752 NAGDNPVVLGFASPSFDASVLEYLLATVNEG--TLAYRPSEAVGGEVLErFIAEHGATHTFLTPSVLSTM---DPTA--V 2824
Cdd:cd05972 118 GLRPDDIHWNIADPGWAKGAWSSFFGPWLLGatVFVYEGPRFDAERILE-LLERYGVTSFCGPPTAYRMLikqDLSSykF 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2825 PSLRVIAAGGEAVPQPIVDRWAPATEL--HNLYGPTETTIGITISSAM--RPGdpvRLGGPIGGVDLMVLDERLRPVPVG 2900
Cdd:cd05972 197 SHLRLVVSAGEPLNPEVIEWWRAATGLpiRDGYGQTETGLTVGNFPDMpvKPG---SMGRPTPGYDVAIIDDDGRELPPG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2901 MPGELYVAGG--ALSRGYLDRSGLTAERFtanpygtaGQRMYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIEL 2978
Cdd:cd05972 274 EEGDIAIKLPppGLFLGYVGDPEKTEASI--------RGDYYLTGDRAYRDEDG-----YFWFVGRADDIIKSSGYRIGP 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2979 GEIEAVLAEHDAVESAVVLGVGGSVATALA-AYIVPVDGA----VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGK 3053
Cdd:cd05972 341 FEVESALLEHPAVAEAAVVGSPDPVRGEVVkAFVVLTSGYepseELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGK 420
|
....*.
gi 1827387616 3054 LDKRAL 3059
Cdd:cd05972 421 IRRVEL 426
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
4-470 |
4.01e-35 |
|
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: 141.36 E-value: 4.01e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSdge 83
Cdd:cd05903 5 SELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAKAKVFVVPE--- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 aeaRSRFDDIVDVhvldisspgdadldeeefagptrPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARD 163
Cdd:cd05903 82 ---RFRQFDPAAM-----------------------PDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLGLGPGD 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 164 VFLYKAPIT-FDVSVREIFLPIAIGATLVIAepgRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRL 242
Cdd:cd05903 136 VFLVASPMAhQTGFVYGFTLPLLLGAPVVLQ---DIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRT 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 243 IQTGGEALTPPVARDLMVRLpGTRLQNQYGPAE-ASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIGVPGEL 321
Cdd:cd05903 213 FVCGGATVPRSLARRAAELL-GAKVCSAYGSTEcPGAVTSITPAPEDRRLYTDGRPLPGVEIKVVDDTGATLAPGVEGEL 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 322 YLGGVQLARGYAGRPDLTAErfvADPFGepgarLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPG 401
Cdd:cd05903 292 LSRGPSVFLGYLDRPDLTAD---AAPEG-----WFRTGDLARLDEDGYLRITGRSKDIIIRGGENIPVLEVEDLLLGHPG 363
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 402 VLHAA-AAVVDGPGGQQLVGYL---APADVDVDTVAA-TTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPE 470
Cdd:cd05903 364 VIEAAvVALPDERLGERACAVVvtkSGALLTFDELVAyLDRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRLRE 437
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1050-1534 |
8.27e-35 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 142.43 E-value: 8.27e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVgmerSIGSVLATWGVIK----SGAAYVPVDPAYPADRI 1125
Cdd:PRK06188 26 PDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVAL----LSLNRPEVLMAIGaaqlAGLRRTALHPLGSLDDH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1126 AYMLEDSGATVGITDAS---TRAR-LGESS---------CEWVDLADLEAEAESGDDITDTERNGSvrlTNLAYLIYTSG 1192
Cdd:PRK06188 102 AYVLEDAGISTLIVDPApfvERALaLLARVpslkhvltlGPVPDGVDLLAAAAKFGPAPLVAAALP---PDIAGLAYTGG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1193 STGRPKAVGVSHTGIVDFvnslAKITTGTPEDEPDTRILHVASPSFDASMFemawAIPA---GHTLVIAPQADfAGDALA 1269
Cdd:PRK06188 179 TTGKPKGVMGTHRSIATM----AQIQLAEWEWPADPRFLMCTPLSHAGGAF----FLPTllrGGTVIVLAKFD-PAEVLR 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1270 TVlERDEVTDMIITPSVL-ATVDPERAQyVRNLAT------GGEACPPElveRWSERGRRI----FNCYGPTEA----TV 1334
Cdd:PRK06188 250 AI-EEQRITATFLVPTMIyALLDHPDLR-TRDLSSletvyyGASPMSPV---RLAEAIERFgpifAQYYGQTEApmviTY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1335 WATRSRMTA--GKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADpfgepgarMYA 1412
Cdd:PRK06188 325 LRKRDHDPDdpKRLTSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG--------WLH 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1413 TGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATIDSA 1492
Cdd:PRK06188 397 TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKWGEA---VTAVVVLRPGAAVDAA 473
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1827387616 1493 AVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEPH 1534
Cdd:PRK06188 474 ELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKALRARY 515
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
4-470 |
9.77e-35 |
|
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: 141.68 E-value: 9.77e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDGE 83
Cdd:cd05926 18 ADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTPKGEL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 ---AEARSRFDD-IVDVHVLDIS----------SPGDADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANR 149
Cdd:cd05926 98 gpaSRAASKLGLaILELALDVGVlirapsaeslSNLLADKKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLTHRNLAAS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 150 LAADIEQYDLTARDVFLYKAPItFDVS--VREIFLPIAIGATLVIaePGRHgDPVHLADLIRRHGVTVIHFVPAMLAAF- 226
Cdd:cd05926 178 ATNITNTYKLTPDDRTLVVMPL-FHVHglVASLLSTLAAGGSVVL--PPRF-SASTFWPDVRDYNATWYTAVPTIHQILl 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 227 NEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTIHRVTQDDRVI-PIGTPTRrVSARV 305
Cdd:cd05926 254 NRPEPNPESPPPKLRFIRSCSASLPPAVLEALEATF-GAPVLEAYGMTEAAHQMTSNPLPPGPRKPgSVGKPVG-VEVRI 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 306 LDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQ 385
Cdd:cd05926 332 LDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW-------FRTGDLGYLDADGYLFLTGRIKELINRGGE 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 386 RLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAP---ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSG 461
Cdd:cd05926 405 KISPLEVDGVLLSHPAVLEAVAfGVPDEKYGEEVAAAVVLregASVTEEELRAFCRKHLAAFKVPKKVYFVDELPKTATG 484
|
....*....
gi 1827387616 462 KVDRRLLPE 470
Cdd:cd05926 485 KIQRRKVAE 493
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
2566-3057 |
1.34e-34 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 141.95 E-value: 1.34e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDGAgARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVP 2645
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGD-RRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2646 IDPDYPAERVASMIEDSGAV-------LGLSVLA-SGDLPGQEFeWMRLDDDSVAAEI-------AAVPAGpitDAERLG 2710
Cdd:PRK07798 83 VNYRYVEDELRYLLDDSDAValvyereFAPRVAEvLPRLPKLRT-LVVVEDGSGNDLLpgavdyeDALAAG---SPERDF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2711 EVTAANLAYVIYTSGSTGRPKGVAVTHS-------GLANFAR--------QESDRLNAGDNPVVLGfASPSFDASVLEYL 2775
Cdd:PRK07798 159 GERSPDDLYLLYTGGTTGMPKGVMWRQEdifrvllGGRDFATgepiedeeELAKRAAAGPGMRRFP-APPLMHGAGQWAA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2776 LATVNEG--TLAYRPSEAVGGEVLeRFIAEHGATHTFLT------PSV--LSTMDPTAVPSLRVIAAGGEAVPQPIVDRW 2845
Cdd:PRK07798 238 FAALFSGqtVVLLPDVRFDADEVW-RTIEREKVNVITIVgdamarPLLdaLEARGPYDLSSLFAIASGGALFSPSVKEAL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2846 ---APATELHNLYGPTETTIGitiSSAMRPGDPVRLGGP---IGGvDLMVLDERLRPVPVGMPGELYVA-GGALSRGYLD 2918
Cdd:PRK07798 317 lelLPNVVLTDSIGSSETGFG---GSGTVAKGAVHTGGPrftIGP-RTVVLDEDGNPVEPGSGEIGWIArRGHIPLGYYK 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2919 RSGLTAERF-TANpygtaGQRMYRTGDVVRWTPDtdtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVL 2997
Cdd:PRK07798 393 DPEKTAETFpTID-----GVRYAIPGDRARVEAD---GTITL--LGRGSVCINTGGEKVFPEEVEEALKAHPDVADALVV 462
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 2998 GV-----GGSVatalAAYIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKR 3057
Cdd:PRK07798 463 GVpderwGQEV----VAVVQLREGArPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
2591-3059 |
1.78e-34 |
|
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: 139.54 E-value: 1.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2591 RLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLgLSV 2670
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKV-AVV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2671 LASgdlpgqefewmrLDDdsvaaeiaavpagpitdaerlgevtaanLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDR 2750
Cdd:cd05935 80 GSE------------LDD----------------------------LALIPYTSGTTGLPKGCMHTHFSAAANALQSAVW 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2751 LNAGDNPVVLGFAsPSFDASVLEYLLATVNEGTLAYRPSEAVGGEVLERFIAEHGATHTFLTPSVLstMDPTAVP----- 2825
Cdd:cd05935 120 TGLTPSDVILACL-PLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTML--VDLLATPefktr 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2826 ---SLRVIAAGGEAVPQPIVDRWAPATELHNL--YGPTETTIGITISSAMRPGDPVrLGGPIGGVDLMVLD-ERLRPVPV 2899
Cdd:cd05935 197 dlsSLKVLTGGGAPMPPAVAEKLLKLTGLRFVegYGLTETMSQTHTNPPLRPKLQC-LGIP*FGVDARVIDiETGRELPP 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2900 GMPGELYVAGGALSRGYLDRSGLTAERFTAnpygTAGQRMYRTGDVVRwtpdTDTGGLtLEYTGRSDDQVKLRGLRIELG 2979
Cdd:cd05935 276 NEVGEIVVRGPQIFKGYWNRPEETEESFIE----IKGRRFFRTGDLGY----MDEEGY-FFFVDRVKRMINVSGFKVWPA 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2980 EIEAVLAEHDAVESAVVLGV----GGSVATALAAYIVPVDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLD 3055
Cdd:cd05935 347 EVEAKLYKHPAI*EVCVISVpderVGEEVKAFIVLRPEYRGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKIL 426
|
....
gi 1827387616 3056 KRAL 3059
Cdd:cd05935 427 WRLL 430
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
572-996 |
1.97e-34 |
|
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: 138.47 E-value: 1.97e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 572 PLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDVLPVAVAREQLD- 650
Cdd:cd19537 3 ALSPIEREWWHKYQLSTGTSSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPPRVQRVDt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 651 ---WREADsveslvRSttegFDVSTQMPLRGRFHRDgaglHVALTMHHIAMDGQSIPVLARDLMSAYaaraegRTGGLPV 727
Cdd:cd19537 83 ldvWKEIN------RP----FDLEREDPIRVFISPD----TLLVVMSHIICDLTTLQLLLREVSAAY------NGKLLPP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 728 LDVQYADYALWQQsvlgdaddetSVLGEQLSHWRRVLAGLPaVTDLPmdrPRPAVLGTAGATVTVEFDDDLADRVDVLAR 807
Cdd:cd19537 143 VRREYLDSTAWSR----------PASPEDLDFWSEYLSGLP-LLNLP---RRTSSKSYRGTSRVFQLPGSLYRSLLQFST 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 808 SNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDP--GHSVGDLLGNVRTTVLDA 885
Cdd:cd19537 209 SSGITLHQLALAAVALALQDLSDRTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRIRFPSssDASAADFLRAVRRSSQAA 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 886 FANdQVQFDELIEALAPERSSSHQPLAQIAFTYTEPT----VNDVAGLEASGIQAapvdTGvvnAKFDLTVAVRARSGGT 961
Cdd:cd19537 289 LAH-AIPWHQLLEHLGLPPDSPNHPLFDVMVTFHDDRgvslALPIPGVEPLYTWA----EG---AKFPLMFEFTALSDDS 360
|
410 420 430
....*....|....*....|....*....|....*
gi 1827387616 962 pMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd19537 361 -LLLRLEYDTDCFSEEEIDRIESLILAALELLVEG 394
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
2566-3068 |
2.15e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 142.06 E-value: 2.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVvDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVP 2645
Cdd:PRK05605 33 TLVDLYDNAVARFGDRPAL-DFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGAVVVE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2646 IDPDYPAERVASMIEDSGA------------VLGL----------SVLASGDLPGQEFEWMRLDDDSVAAEIAAVPAGP- 2702
Cdd:PRK05605 112 HNPLYTAHELEHPFEDHGArvaivwdkvaptVERLrrttpletivSVNMIAAMPLLQRLALRLPIPALRKARAALTGPAp 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2703 -------ITDAERLG--------EVTAANLAYVIYTSGSTGRPKGVAVTHSGL-ANFARQESDRLNAGDNPVVLGFASPS 2766
Cdd:PRK05605 192 gtvpwetLVDAAIGGdgsdvshpRPTPDDVALILYTSGTTGKPKGAQLTHRNLfANAAQGKAWVPGLGDGPERVLAALPM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2767 FDAsvleYLLaTVNeGTLAYrpseAVGGE-VLerfiaehgaTHTFLTPSVLSTMD---PT---AVPSL--RVIAA----- 2832
Cdd:PRK05605 272 FHA----YGL-TLC-LTLAV----SIGGElVL---------LPAPDIDLILDAMKkhpPTwlpGVPPLyeKIAEAaeerg 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2833 -----------GGEAVPQPIVDRWAPAT--ELHNLYGPTETT---IGITISSAMRPGdpvRLGGPIGGVDLMVLD-ERL- 2894
Cdd:PRK05605 333 vdlsgvrnafsGAMALPVSTVELWEKLTggLLVEGYGLTETSpiiVGNPMSDDRRPG---YVGVPFPDTEVRIVDpEDPd 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2895 RPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANpygtagqrMYRTGDVVRWTPDtdtGGLTLeyTGRSDDQVKLRGL 2974
Cdd:PRK05605 410 ETMPDGEEGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEED---GFIRI--VDRIKELIITGGF 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2975 RIELGEIEAVLAEHDAVESAVVLGV-GGSVATALAAYIVPVDGAV-EVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVG 3052
Cdd:PRK05605 477 NVYPAEVEEVLREHPGVEDAAVVGLpREDGSEEVVAAVVLEPGAAlDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLG 556
|
570
....*....|....*.
gi 1827387616 3053 KLDKRALPEPVLEAGE 3068
Cdd:PRK05605 557 KVRRREVREELLEKLG 572
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1054-1534 |
2.54e-34 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 140.60 E-value: 2.54e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1054 ALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSG 1133
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1134 ATVGITDASTRARLGESSCEWVDLADLEAEAE-----SGDDITDTERNGSV---------------RLTNLAYLIYTSGS 1193
Cdd:PRK12406 84 ARVLIAHADLLHGLASALPAGVTVLSVPTPPEiaaayRISPALLTPPAGAIdwegwlaqqepydgpPVPQPQSMIYTSGT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1194 TGRPKAVgvshtgivdfvnslaKITTGTPED--------------EPDTRIL------HVASPSFDASmfemawAIPAGH 1253
Cdd:PRK12406 164 TGHPKGV---------------RRAAPTPEQaaaaeqmraliyglKPGIRALltgplyHSAPNAYGLR------AGRLGG 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1254 TLVIAPQadFAGDALATVLERDEVTDMIITPSV---LATVDPE-RAQY----VRNLATGGEACPPE----LVERWserGR 1321
Cdd:PRK12406 223 VLVLQPR--FDPEELLQLIERHRITHMHMVPTMfirLLKLPEEvRAKYdvssLRHVIHAAAPCPADvkraMIEWW---GP 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1322 RIFNCYGPTE--ATVWATrSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLAR-GYLGRPGQTAVSF 1398
Cdd:PRK12406 298 VIYEYYGSTEsgAVTFAT-SEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAEID 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1399 VADpfgepgarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVV 1478
Cdd:PRK12406 377 RGG--------FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEA---LM 445
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 1479 AYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEPH 1534
Cdd:PRK12406 446 AVVEPQPGATLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPY 501
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
4-468 |
3.15e-34 |
|
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: 138.77 E-value: 3.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDge 83
Cdd:cd05935 5 LELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGSE-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 aearsrFDDIvdvhvldisspgdadldeeefagptrpanaAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARD 163
Cdd:cd05935 83 ------LDDL------------------------------ALIPYTSGTTGLPKGCMHTHFSAAANALQSAVWTGLTPSD 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 164 VFLYKAPItFDVS--VREIFLPIAIGATLVIAepGRHgDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLR 241
Cdd:cd05935 127 VILACLPL-FHVTgfVGSLNTAVYVGGTYVLM--ARW-DRETALELIEKYKVTFWTNIPTMLVDLLATPEFKTRDLSSLK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 242 LIQTGGEALTPPVARDLMvRLPGTRLQNQYGPAEASIVVTIHRvTQDDRVIPIGTPTRRVSARVLDA-ALREVPIGVPGE 320
Cdd:cd05935 203 VLTGGGAPMPPAVAEKLL-KLTGLRFVEGYGLTETMSQTHTNP-PLRPKLQCLGIP*FGVDARVIDIeTGRELPPNEVGE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 321 LYLGGVQLARGYAGRPDLTAERFVADpfgePGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAP 400
Cdd:cd05935 281 IVVRGPQIFKGYWNRPEETEESFIEI----KGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAKLYKHP 356
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 401 GVLHAAA-AVVDGPGGQQLVGY--LAP---ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd05935 357 AI*EVCViSVPDERVGEEVKAFivLRPeyrGKVTEEDIIEWAREQMAAYKYPREVEFVDELPRSASGKILWRLL 430
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
2570-3059 |
4.06e-34 |
|
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: 140.07 E-value: 4.06e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2570 LFRAAARRAPDHVAV---VDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPI 2646
Cdd:cd12119 1 LLEHAARLHGDREIVsrtHEGEVHRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2647 DPDYPAERVASMI---ED-----SGAVLGLSVLASGDLPGQEfEWMRLDDDSVAAEIAAVPAG----------PITDAER 2708
Cdd:cd12119 81 NPRLFPEQIAYIInhaEDrvvfvDRDFLPLLEAIAPRLPTVE-HVVVMTDDAAMPEPAGVGVLayeellaaesPEYDWPD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2709 LGEVTAANLAYviyTSGSTGRPKGVAVTHSG--LANFARQESDRLNAGDNPVVLGFAsPSFDASV--LEYllATVNEGTL 2784
Cdd:cd12119 160 FDENTAAAICY---TSGTTGNPKGVVYSHRSlvLHAMAALLTDGLGLSESDVVLPVV-PMFHVNAwgLPY--AAAMVGAK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2785 AYRPSEAVGGEVLERFIAEHGATHTFLTPSV----LSTMD--PTAVPSLRVIAAGGEAVPQPIVDRWAPA-TELHNLYGP 2857
Cdd:cd12119 234 LVLPGPYLDPASLAELIEREGVTFAAGVPTVwqglLDHLEanGRDLSSLRRVVIGGSAVPRSLIEAFEERgVRVIHAWGM 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2858 TET-TIGI--TISSAMRPGDP-----VRL--GGPIGGVDLMVLDERLRPVPV-GMP-GELYVAGGALSRGYLDRSGlTAE 2925
Cdd:cd12119 314 TETsPLGTvaRPPSEHSNLSEdeqlaLRAkqGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDE-ESE 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2926 RFTANPYgtagqrmYRTGDVVRWTPDtdtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG----G 3001
Cdd:cd12119 393 ALTEDGW-------LRTGDVATIDED---GYLTI--TDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPhpkwG 460
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 3002 SVATALaayIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd12119 461 ERPLAV---VVLKEGAtVTAEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
2-468 |
4.78e-34 |
|
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: 138.24 E-value: 4.78e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSD 81
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVTDAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 geaearsrfddivdvhvldisspgdadldeeefagptrpaNAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTA 161
Cdd:cd05972 82 ----------------------------------------DPALIYFTSGTTGLPKGVLHTHSYPLGHIPTAAYWLGLRP 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 162 RDVFLYKAP---ITFDVSvrEIFLPIAIGATLVIAEpGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGvGELT 238
Cdd:cd05972 122 DDIHWNIADpgwAKGAWS--SFFGPWLLGATVFVYE-GPRFDAERILELLERYGVTSFCGPPTAYRMLIKQDLSS-YKFS 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 239 SLRLIQTGGEALTPPVArDLMVRLPGTRLQNQYGPAEASIVVTIHRvTQDDRVIPIGTPTRRVSARVLDAALREVPIGVP 318
Cdd:cd05972 198 HLRLVVSAGEPLNPEVI-EWWRAATGLPIRDGYGQTETGLTVGNFP-DMPVKPGSMGRPTPGYDVAIIDDDGRELPPGEE 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 319 GEL--YLGGVQLARGYAGRPDLTAERFVADpfgepgarLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAAL 396
Cdd:cd05972 276 GDIaiKLPPPGLFLGYVGDPEKTEASIRGD--------YYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVESAL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 397 AAAPGVLHAAAAVVDGPGGQQLV--------GYLaPADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd05972 348 LEHPAVAEAAVVGSPDPVRGEVVkafvvltsGYE-PSEELAEELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRVEL 426
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1-468 |
5.65e-34 |
|
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: 139.18 E-value: 5.65e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:cd05923 29 LTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAELIERGEMTAAVIAV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAeARSRFDDIVDVHVLDIsspgDADLDEEEFAGP------TRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADI 154
Cdd:cd05923 109 DAQV-MDAIFQSGVRVLALSD----LVGLGEPESAGPliedppREPEQPAFVFYTSGTTGLPKGAVIPQRAAESRVLFMS 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 155 EQYDLT--ARDVFLYKAPITFDVSVREIFL-PIAIGATLVIAepgRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLG 231
Cdd:cd05923 184 TQAGLRhgRHNVVLGLMPLYHVIGFFAVLVaALALDGTYVVV---EEFDPADALKLIEQERVTSLFATPTHLDALAAAAE 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 232 AGVGELTSLRLIQTGGEALTPPVARDLMVRLPGtRLQNQYGPAEASIVVTIHRVTQDDRVIPiGTPTRRVSARVLDAALR 311
Cdd:cd05923 261 FAGLKLSSLRHVTFAGATMPDAVLERVNQHLPG-EKVNIYGTTEAMNSLYMRDARTGTEMRP-GFFSEVRIVRIGGSPDE 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 312 EVPIGVPGELY--LGGVQLARGYAGRPDLTAERFVadpfgepgARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLEL 389
Cdd:cd05923 339 ALANGEEGELIvaAAADAAFTGYLNQPEATAKKLQ--------DGWYRTGDVGYVDPSGDVRILGRVDDMIISGGENIHP 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 390 GEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAPADVDV-----DTVAATTAelLPEYMRPSAWVRLDAMPLSRSGKV 463
Cdd:cd05923 411 SEIERVLSRHPGVTEVVViGVADERWGQSVTACVVPREGTLsadelDQFCRASE--LADFKRPRRYFFLDELPKNAMNKV 488
|
....*
gi 1827387616 464 DRRLL 468
Cdd:cd05923 489 LRRQL 493
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
2560-3061 |
5.80e-34 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 140.10 E-value: 5.80e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2560 PATdpvTLAELFRAAARRAPDHVAVVdGAGARLTYRELDEASDRLARWLIGR-GVGPERAVALAIGRSAQLLTAIWAVAK 2638
Cdd:PRK08314 8 PET---SLFHNLEVSARRYPDKTAIV-FYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2639 TGGAYVPIDPDYPAERVASMIEDSGAVLGL--SVLASGDLPGQEFEWMR----------LDDDS---------VAAEIAA 2697
Cdd:PRK08314 84 ANAVVVPVNPMNREEELAHYVTDSGARVAIvgSELAPKVAPAVGNLRLRhvivaqysdyLPAEPeiavpawlrAEPPLQA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2698 VPAG---PITDAERLG------EVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFAsPSFD 2768
Cdd:PRK08314 164 LAPGgvvAWKEALAAGlappphTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVL-PLFH 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2769 ASVLEY-LLATVNEG-TLAYRP---SEAVGgevleRFIAEHGATHTFLTPsvlsTM--DPTAVP--------SLRVIAAG 2833
Cdd:PRK08314 243 VTGMVHsMNAPIYAGaTVVLMPrwdREAAA-----RLIERYRVTHWTNIP----TMvvDFLASPglaerdlsSLRYIGGG 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2834 GEAVPQPIVDRWAPATELHNL--YGPTETTIGITISSAMRPgDPVRLGGPIGGVDLMVLD-ERLRPVPVGMPGELYVAGG 2910
Cdd:PRK08314 314 GAAMPEAVAERLKELTGLDYVegYGLTETMAQTHSNPPDRP-KLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2911 ALSRGYLDRSGLTAERFTAnpygTAGQRMYRTGDVvrwtpdtdtggltleytGRSD--------DQVK----LRGLRIEL 2978
Cdd:PRK08314 393 QVFKGYWNRPEATAEAFIE----IDGKRFFRTGDL-----------------GRMDeegyffitDRLKrminASGFKVWP 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2979 GEIEAVLAEHDAVESAVVLGV-----GGSVatalAAYIVPVD---GAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTP 3050
Cdd:PRK08314 452 AEVENLLYKHPAIQEACVIATpdprrGETV----KAVVVLRPearGKTTEEEIIAWAREHMAAYKYPRIVEFVDSLPKSG 527
|
570
....*....|.
gi 1827387616 3051 VGKLDKRALPE 3061
Cdd:PRK08314 528 SGKILWRQLQE 538
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
2560-3059 |
8.93e-34 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 139.72 E-value: 8.93e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2560 PATDPVTLAELFRAAARRAPDHVAV---VDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAV 2636
Cdd:cd05906 5 PEGAPRTLLELLLRAAERGPTKGITyidADGSEEFQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWAC 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2637 AKTGGAYVPIDP----DYPAERVASM-----IEDSGAVLGLSVLASgDLPGQEFEWMRLDDDSVAAEIAAVPAGPitdaE 2707
Cdd:cd05906 85 VLAGFVPAPLTVpptyDEPNARLRKLrhiwqLLGSPVVLTDAELVA-EFAGLETLSGLPGIRVLSIEELLDTAAD----H 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2708 RLGEVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASpsFD--ASVLEYLLATVNEGTL- 2784
Cdd:cd05906 160 DLPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLTPQDVFLNWVP--LDhvGGLVELHLRAVYLGCQq 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2785 AYRPSEAVGGEVLE--RFIAEHGATHTF--------LTPSVLSTMDPTA-VPSLRVIAAGGEAVPQPIVDRW-------- 2845
Cdd:cd05906 238 VHVPTEEILADPLRwlDLIDRYRVTITWapnfafalLNDLLEEIEDGTWdLSSLRYLVNAGEAVVAKTIRRLlrllepyg 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2846 APATELHNLYGPTETTIGITISSAMRPGDP------VRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDR 2919
Cdd:cd05906 318 LPPDAIRPAFGMTETCSGVIYSRSFPTYDHsqalefVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2920 SGLTAERFTANPYgtagqrmYRTGDVVRwtpdTDTGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV 2999
Cdd:cd05906 398 PEANAEAFTEDGW-------FRTGDLGF----LDNGNLTI--TGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAF 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 3000 G----GSVATALAAYIVPV----DGAVEVSE------LKAFagGRLPAYMVPssfTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05906 465 AvrdpGAETEELAIFFVPEydlqDALSETLRairsvvSREV--GVSPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
2547-3061 |
1.24e-33 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 139.12 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2547 AEAAVELTPVTGGPATDpVTLAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRS 2626
Cdd:PRK06155 4 LGAGLAARAVDPLPPSE-RTLPAMLARQAERYPDRPLLVFG-GTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2627 AQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVL------GLSVLAS---GDLPGQEFeWmRLDDD---SVAAE 2694
Cdd:PRK06155 82 IEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLlvveaaLLAALEAadpGDLPLPAV-W-LLDAPasvSVPAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2695 IAAVPAGPITDAERLGEVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFAsPSFDASVLEY 2774
Cdd:PRK06155 160 WSTAPLPPLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADDVLYTTL-PLFHTNALNA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2775 LL-ATVNEGTLAyrpseavggeVLERF--------IAEHGATHTFLTPSVLSTMDP-TAVPSLR---VIAAGGEAVPQPI 2841
Cdd:PRK06155 239 FFqALLAGATYV----------LEPRFsasgfwpaVRRHGATVTYLLGAMVSILLSqPARESDRahrVRVALGPGVPAAL 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2842 VD--RWAPATELHNLYGPTETT--IGITISSAmRPGDPVRLGgpiGGVDLMVLDERLRPVPVGMPGELYVAG---GALSR 2914
Cdd:PRK06155 309 HAafRERFGVDLLDGYGSTETNfvIAVTHGSQ-RPGSMGRLA---PGFEARVVDEHDQELPDGEPGELLLRAdepFAFAT 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2915 GYLDRSGLTAErftanpygtAGQRM-YRTGDVVRWTPDTDtggltLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVES 2993
Cdd:PRK06155 385 GYFGMPEKTVE---------AWRNLwFHTGDRVVRDADGW-----FRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAA 450
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2994 AVVLGVGGSVAT-ALAAYIVPVDG-AVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPE 3061
Cdd:PRK06155 451 AAVFPVPSELGEdEVMAAVVLRDGtALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1060-1530 |
1.81e-33 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes fatty acyl-CoA synthetases that can activate medium-chain to long-chain fatty acids. They catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family catalyzes the long-chain fatty acid, myristoyl acid, while another member in this family, the AlkK protein identified from Pseudomonas oleovorans, targets medium chain fatty acids. This family also includes uncharacterized FACS proteins.
Pssm-ID: 341284 [Multi-domain] Cd Length: 518 Bit Score: 138.15 E-value: 1.81e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1060 TEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGIT 1139
Cdd:cd12119 24 HRYTYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1140 DASTRARLGESSCEW--------------------VDLADLEAEAESGDDITD----TERNGSVrltnlayLIYTSGSTG 1195
Cdd:cd12119 104 DRDFLPLLEAIAPRLptvehvvvmtddaampepagVGVLAYEELLAAESPEYDwpdfDENTAAA-------ICYTSGTTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1196 RPKAVGVSHTGIVdfVNSLAKITT-GTPEDEPDTrILHVAsPSFDAsmfeMAWAIP-----AGHTLVIaPQADFAGDALA 1269
Cdd:cd12119 177 NPKGVVYSHRSLV--LHAMAALLTdGLGLSESDV-VLPVV-PMFHV----NAWGLPyaaamVGAKLVL-PGPYLDPASLA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1270 TVLERDEVTDMIITPSVLATV--DPERAQY----VRNLATGGEACPPELVERWSERGRRIFNCYGPTEATVWATRSRMTA 1343
Cdd:cd12119 248 ELIEREGVTFAAGVPTVWQGLldHLEANGRdlssLRRVVIGGSAVPRSLIEAFEERGVRVIHAWGMTETSPLGTVARPPS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1344 GKP-----------VTIGKPVDGFTVRVLDGRLHEVPQ--GVVGELYLSTAGLARGYLGRPGQTAvSFVADPFgepgarm 1410
Cdd:cd12119 328 EHSnlsedeqlalrAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDEESE-ALTEDGW------- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1411 YATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKHtevVAYLVAKPGATID 1490
Cdd:cd12119 400 LRTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGERP---LAVVVLKEGATVT 476
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1827387616 1491 SAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd12119 477 AEELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1033-1527 |
2.15e-33 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 138.98 E-value: 2.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1033 EVEAGTLIDVLAQR-DLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGA 1111
Cdd:PRK05605 28 DYGDTTLVDLYDNAvARFGDRPALDFFGATTTYAELGKQVRRAAAGLRALGVRPGDRVAIVLPNCPQHIVAFYAVLRLGA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1112 AYVPVDPAYPADRIAYMLEDSGATVGI--------------------------TDA-----------------STRARLG 1148
Cdd:PRK05605 108 VVVEHNPLYTAHELEHPFEDHGARVAIvwdkvaptverlrrttpletivsvnmIAAmpllqrlalrlpipalrKARAALT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1149 ESSCEWVDLADLEAEAESGDDITDTERngSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIvdFVNsLAKITTGTPEDEPDT 1228
Cdd:PRK05605 188 GPAPGTVPWETLVDAAIGGDGSDVSHP--RPTPDDVALILYTSGTTGKPKGAQLTHRNL--FAN-AAQGKAWVPGLGDGP 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1229 RILHVASPSFDASMFEM--AWAIPAGHTLVIAPQADFagDALATVLERDEVTDMIITPSV---LATVDPERA---QYVRN 1300
Cdd:PRK05605 263 ERVLAALPMFHAYGLTLclTLAVSIGGELVLLPAPDI--DLILDAMKKHPPTWLPGVPPLyekIAEAAEERGvdlSGVRN 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1301 LATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAG-KPVTIGKPVDGFTVRVLDGR--LHEVPQGVVGEL 1376
Cdd:PRK05605 341 AFSGAMALPVSTVELWEKLtGGLLVEGYGLTETSPIIVGNPMSDDrRPGYVGVPFPDTEVRIVDPEdpDETMPDGEEGEL 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1377 YLSTAGLARGYLGRPGQTAVSFVADpfgepgarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPG 1456
Cdd:PRK05605 421 LVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPG 492
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 1457 VAQSVVVGVESTRGGRkhtEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDR 1527
Cdd:PRK05605 493 VEDAAVVGLPREDGSE---EVVAAVVLEPGAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1027-1501 |
3.73e-33 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 138.69 E-value: 3.73e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1027 MVGRGGEVEAGTLIDVLAQR-DLDPDHPALIC--DG--TEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVL 1101
Cdd:COG1022 1 MSEFSDVPPADTLPDLLRRRaARFPDRVALREkeDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1102 ATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITD--------ASTRARL------------GESSCEWV-DLADL 1160
Cdd:COG1022 81 ADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFVEdqeqldklLEVRDELpslrhivvldprGLRDDPRLlSLDEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1161 EAE-AESGDDITDTERNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtRIL------HV 1233
Cdd:COG1022 161 LALgREVADPAELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGD----RTLsflplaHV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1234 AspsfdASMFEMAwAIPAGHTLVIAPQADFAGDALATV-----------LER--DEVTDMI------------------- 1281
Cdd:COG1022 237 F-----ERTVSYY-ALAAGATVAFAESPDTLAEDLREVkptfmlavprvWEKvyAGIQAKAeeagglkrklfrwalavgr 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1282 ---------ITPSVLatvdpERAQY------------------VRNLATGGEACPPELVERWSERGRRIFNCYGPTEATV 1334
Cdd:COG1022 311 ryararlagKSPSLL-----LRLKHaladklvfsklrealggrLRFAVSGGAALGPELARFFRALGIPVLEGYGLTETSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1335 WATRSRMTAGKPVTIGKPVDGFTVRVldgrlhevpqGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATG 1414
Cdd:COG1022 386 VITVNRPGDNRIGTVGPPLPGVEVKI----------AEDGEILVRGPNVMKGYYKNPEATAEAFDADGW-------LHTG 448
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1415 DLVRVAKGGNLEFAGRADHQVKI-NGQRVELGEIEAVLDAQPGVAQSVVVGvestrGGRKHteVVAyLVakpgaTIDSAA 1493
Cdd:COG1022 449 DIGELDEDGFLRITGRKKDLIVTsGGKNVAPQPIENALKASPLIEQAVVVG-----DGRPF--LAA-LI-----VPDFEA 515
|
....*...
gi 1827387616 1494 VLDEAAQH 1501
Cdd:COG1022 516 LGEWAEEN 523
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
2557-3049 |
5.40e-33 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 137.18 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2557 TGGPATDPVTLAELFRAAARRAPDHVAVVDGAGArLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAV 2636
Cdd:PRK06164 2 PHDAAPRADTLASLLDAHARARPDAVALIDEDRP-LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLAC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2637 AKTGGAYVPIDPDYPAERVASMIEDSGAVL----------------------------GLSVL--ASGDLPGqefewmRL 2686
Cdd:PRK06164 81 ARLGATVIAVNTRYRSHEVAHILGRGRARWlvvwpgfkgidfaailaavppdalpplrAIAVVddAADATPA------PA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2687 DDDSVAAEIAAVPAGPITDAERLGEVTAANLAYViyTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGfASPS 2766
Cdd:PRK06164 155 PGARVQLFALPDPAPPAAAGERAADPDAGALLFT--TSGTTSGPKLVLHRQATLLRHARAIARAYGYDPGAVLLA-ALPF 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2767 FDASVLEYLLATVNEG-TLAYRPseAVGGEVLERFIAEHGATHTFLTPSVLSTMDPTA-----VPSLRVI-----AAGGE 2835
Cdd:PRK06164 232 CGVFGFSTLLGALAGGaPLVCEP--VFDAARTARALRRHRVTHTFGNDEMLRRILDTAgeradFPSARLFgfasfAPALG 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2836 AVPQPIVDRWAPateLHNLYGPTETtigITISSAMRPGDPVRLGGPIGGVdLMVLDERLRPV--------PVGMPGELYV 2907
Cdd:PRK06164 310 ELAALARARGVP---LTGLYGSSEV---QALVALQPATDPVSVRIEGGGR-PASPEARVRARdpqdgallPDGESGEIEI 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2908 AGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVRWTPDtdtGGLTleYTGRSDDQVKLRGLRIELGEIEAVLAE 2987
Cdd:PRK06164 383 RAPSLMRGYLDNPDATARALTDDGY-------FRTGDLGYTRGD---GQFV--YQTRMGDSLRLGGFLVNPAEIEHALEA 450
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 2988 HDAVESAVVLGVGGSVATALAAYIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLT 3049
Cdd:PRK06164 451 LPGVAAAQVVGATRDGKTVPVAFVIPTDGAsPDEAGLMAACREALAGFKVPARVQVVEAFPVT 513
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
4-476 |
1.29e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 134.93 E-value: 1.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVvTSDGE 83
Cdd:PRK09088 26 AELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSASELDALLQDAEPRLLL-GDDAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 AEARSrfdDIVDVHVLdISSPGDADLDEEEFAGPTRPAnaaFTLFTSGSTGRPKAVVITHRgiaNRLAADIEQYDLT--- 160
Cdd:PRK09088 105 AAGRT---DVEDLAAF-IASADALEPADTPSIPPERVS---LILFTSGTSGQPKGVMLSER---NLQQTAHNFGVLGrvd 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAP----ITFDVSVREIflpIAIGATLVIA---EP----GRHGDPvhlaDLirrhGVTVIHFVPAMLAAFNEV 229
Cdd:PRK09088 175 AHSSFLCDAPmfhiIGLITSVRPV---LAVGGSILVSngfEPkrtlGRLGDP----AL----GITHYFCVPQMAQAFRAQ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 230 LGAGVGELTSLRLIQTGGealTPPVARDLMVRLP-GTRLQNQYGPAEASIV--VTIHRVTQDDRVIPIGTPTRRVSARVL 306
Cdd:PRK09088 244 PGFDAAALRHLTALFTGG---APHAAEDILGWLDdGIPMVDGFGMSEAGTVfgMSVDCDVIRAKAGAAGIPTPTVQTRVV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 307 DAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQR 386
Cdd:PRK09088 321 DDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIARRDADGFFWVVDRKKDMFISGGEN 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 387 LELGEVEAALAAAPGVLHAAA-AVVDGPGGQqlVGYLA-----PADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRS 460
Cdd:PRK09088 394 VYPAEIEAVLADHPGIRECAVvGMADAQWGE--VGYLAivpadGAPLDLERIRSHLSTRLAKYKVPKHLRLVDALPRTAS 471
|
490
....*....|....*.
gi 1827387616 461 GKVDRRLLPEPEIAPT 476
Cdd:PRK09088 472 GKLQKARLRDALAAGR 487
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
4-468 |
1.69e-32 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 135.45 E-value: 1.69e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSD-- 81
Cdd:PRK08316 40 AELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYILDHSGARAFLVDPAla 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 GEAEARSRFDDIVDVHVLDISSPGDADLDEEEF-----AGPTRPANAAFT-------LFTSGSTGRPKAVVITHRGIANR 149
Cdd:PRK08316 120 PTAEAALALLPVDTLILSLVLGGREAPGGWLDFadwaeAGSVAEPDVELAdddlaqiLYTSGTESLPKGAMLTHRALIAE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 150 LAADIEQYDLTARDVFLYKAPItFDVSVREIFL-P-IAIGATLVIAE-PgrhgDPVHLADLIRRHGVTVIhFVP-----A 221
Cdd:PRK08316 200 YVSCIVAGDMSADDIPLHALPL-YHCAQLDVFLgPyLYVGATNVILDaP----DPELILRTIEAERITSF-FAPptvwiS 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 222 ML--AAFNEVlgagvgELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVT-QDDRVIPIGTPT 298
Cdd:PRK08316 274 LLrhPDFDTR------DLSSLRKGYYGASIMPVEVLKELRERLPGLRFYNCYGQTEIAPLATVLGPEeHLRRPGSAGRPV 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 299 RRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlyRTGDRARWNRDGEIEYLGRTDF 378
Cdd:PRK08316 348 LNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRGGWF--------HSGDLGVMDEEGYITVVDRKKD 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 379 QVKLRGQRLELGEVEAALAAAPGVLHAA--------------AAVVDGPGgqqlvgylapADVDVDTVAATTAELLPEYM 444
Cdd:PRK08316 420 MIKTGGENVASREVEEALYTHPAVAEVAviglpdpkwieavtAVVVPKAG----------ATVTEDELIAHCRARLAGFK 489
|
490 500
....*....|....*....|....
gi 1827387616 445 RPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK08316 490 VPKRVIFVDELPRNPSGKILKREL 513
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
1749-2069 |
2.05e-32 |
|
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: 133.61 E-value: 2.05e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1749 GEGRRRLVIAIHHLGVDAVSWPILVEDLVTAWAQLTSGRPIELRPE---ATTTRRIAHLLAGQvhARAREVDYWLEQL-- 1823
Cdd:pfam00668 127 AENRHHLLLSMHHIIVDGVSLGILLRDLADLYQQLLKGEPLPLPPKtpyKDYAEWLQQYLQSE--DYQKDAAYWLEQLeg 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1824 PERPTSFGTSADRPLHRRRDESSLTYVVDDVAGSILTTVPQAFGSSVDDVLLGALARAVRAWqldNGiadGGPVTVSTEG 1903
Cdd:pfam00668 205 ELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGLLLSRY---TG---QDDIVVGTPG 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1904 HGRDESiagdegaiDLSRTVGWFTSITPLAVDAS-----SDVVHAVKsaKDARLSRPAGGVGFGILRYNSD--GEIAHRP 1976
Cdd:pfam00668 279 SGRPSP--------DIERMVGMFVNTLPLRIDPKggktfSELIKRVQ--EDLLSAEPHQGYPFGDLVNDLRlpRDLSRHP 348
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1977 LPTIMYNY--FGGGTAPSTETAPDDFlpvsdrpnmPSSITGAMRSPSVFGINIsTAGREERRLEAKVTYATDALDEAAAS 2054
Cdd:pfam00668 349 LFDPMFSFqnYLGQDSQEEEFQLSEL---------DLSVSSVIEEEAKYDLSL-TASERGGGLTIKIDYNTSLFDEETIE 418
|
330
....*....|....*
gi 1827387616 2055 DIARRWHDELRAVVE 2069
Cdd:pfam00668 419 RFAEHFKELLEQAIA 433
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1047-1535 |
2.19e-32 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 134.82 E-value: 2.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1047 DLDPDHPALIC--DGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADR 1124
Cdd:PRK13391 8 QTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1125 IAYMLEDSGATVGITDASTR--ARLGESSCE----------------WVDLAdlEAEAESGDDITDTERNGSVrltnlay 1186
Cdd:PRK13391 88 AAYIVDDSGARALITSAAKLdvARALLKQCPgvrhrlvldgdgelegFVGYA--EAVAGLPATPIADESLGTD------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1187 LIYTSGSTGRPKAV-------GVSH-TGIVDFVNSLAKITTGTPEDEPDTriLHVASPSFdASMFemawAIPAGHTLVIA 1258
Cdd:PRK13391 159 MLYSSGTTGRPKGIkrplpeqPPDTpLPLTAFLQRLWGFRSDMVYLSPAP--LYHSAPQR-AVML----VIRLGGTVIVM 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1259 PQADfAGDALATVlERDEVTDMIITPS----VLATVDPERAQY-VRNLATGGEA---CPPELVER----WserGRRIFNC 1326
Cdd:PRK13391 232 EHFD-AEQYLALI-EEYGVTHTQLVPTmfsrMLKLPEEVRDKYdLSSLEVAIHAaapCPPQVKEQmidwW---GPIIHEY 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1327 YGPTEAT-VWATRSRMTAGKPVTIGKPVDGfTVRVLDGRLHEVPQGVVGELYLSTaGLARGYLGRPGQTAVSFVADPfge 1405
Cdd:PRK13391 307 YAATEGLgFTACDSEEWLAHPGTVGRAMFG-DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEARHPDG--- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1406 pgaRMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKP 1485
Cdd:PRK13391 382 ---TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDLGE---EVKAVVQPVD 455
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 1486 G--ATIDSAAVLDE-AAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEPHA 1535
Cdd:PRK13391 456 GvdPGPALAAELIAfCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLLRDRYW 508
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
114-470 |
4.24e-32 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 138.13 E-value: 4.24e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 114 FAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPI--TFDVSVrEIFLPIAIGATLV 191
Cdd:PRK08633 775 YGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSSLPFfhSFGLTV-TLWLPLLEGIKVV 853
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 192 IaepgrHGDP---VHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLpGTRLQ 268
Cdd:PRK08633 854 Y-----HPDPtdaLGIAKLVAKHRATILLGTPTFLRLYLRNKKLHPLMFASLRLVVAGAEKLKPEVADAFEEKF-GIRIL 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 269 NQYGPAEASIVVTI----HRVTQDDRVI-----PIGTPTRRVSARVLDA-ALREVPIGVPGELYLGGVQLARGYAGRPDL 338
Cdd:PRK08633 928 EGYGATETSPVASVnlpdVLAADFKRQTgskegSVGMPLPGVAVRIVDPeTFEELPPGEDGLILIGGPQVMKGYLGDPEK 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 339 TAErFVADPfgePGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAA---PGVLHAAAAVVDGPGG 415
Cdd:PRK08633 1008 TAE-VIKDI---DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlggEEVVFAVTAVPDEKKG 1083
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 416 QQLVGYLAPADVDVDTVAATTAEL-LPEYMRPSAWVRLDAMPLSRSGKVDRRLLPE 470
Cdd:PRK08633 1084 EKLVVLHTCGAEDVEELKRAIKESgLPNLWKPSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
13-465 |
5.29e-32 |
|
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: 134.33 E-value: 5.29e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 13 LARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPL----DEQLPVDRAR--YMVRTAGVRLVVVTSDG---- 82
Cdd:cd05906 52 LAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGFVPAPLtvppTYDEPNARLRklRHIWQLLGSPVVLTDAElvae 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 83 --EAEARSRFDDIvDVHVLDISSPGDADLDeeefAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd05906 132 faGLETLSGLPGI-RVLSIEELLDTAADHD----LPQSRPDDLALLMLTSGSTGFPKAVPLTHRNILARSAGKIQHNGLT 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREIFL-PIAIGATLV-IAEPGRHGDPVHLADLIRRHGVTvIHFVP----AMLAAFNEVLGAGV 234
Cdd:cd05906 207 PQDVFLNWVPLDHVGGLVELHLrAVYLGCQQVhVPTEEILADPLRWLDLIDRYRVT-ITWAPnfafALLNDLLEEIEDGT 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 235 GELTSLRLIQTGGEALTPPVARDLMVRL-----PGTRLQNQYGPAEASIVVTIHRV------TQDDRVIPIGTPTRRVSA 303
Cdd:cd05906 286 WDLSSLRYLVNAGEAVVAKTIRRLLRLLepyglPPDAIRPAFGMTETCSGVIYSRSfptydhSQALEFVSLGRPIPGVSM 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 304 RVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRArWNRDGEIEYLGRTDFQVKLR 383
Cdd:cd05906 366 RIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-------FRTGDLG-FLDNGNLTITGRTKDTIIVN 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 384 GQRLELGEVEAALAAAPGVLH---AAAAVVDGPGG-QQLVGYLAPADVDVDTVAATTAE----------LLPEYMRPsaw 449
Cdd:cd05906 438 GVNYYSHEIEAAVEEVPGVEPsftAAFAVRDPGAEtEELAIFFVPEYDLQDALSETLRAirsvvsrevgVSPAYLIP--- 514
|
490
....*....|....*.
gi 1827387616 450 VRLDAMPLSRSGKVDR 465
Cdd:cd05906 515 LPKEEIPKTSLGKIQR 530
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1038-1530 |
8.54e-32 |
|
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: 132.45 E-value: 8.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1038 TLIDVLAQR-DLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPV 1116
Cdd:cd05920 16 PLGDLLARSaARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGAVPVLA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1117 DPAYPADRIAYMLEDSGATvgitdastrARLGESSCEWVDLADLEAE-AESGDDItdterngsvrltnlAYLIYTSGSTG 1195
Cdd:cd05920 96 LPSHRRSELSAFCAHAEAV---------AYIVPDRHAGFDHRALARElAESIPEV--------------ALFLLSGGTTG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1196 RPKAVGVSHTGIVDFVNSLAKITTGTPedepDTRILHV--ASPSFDASMFEMAWAIPAGHTLVIAPQADfAGDALAtVLE 1273
Cdd:cd05920 153 TPKLIPRTHNDYAYNVRASAEVCGLDQ----DTVYLAVlpAAHNFPLACPGVLGTLLAGGRVVLAPDPS-PDAAFP-LIE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1274 RDEVTDMIITPSVLATVDPERAQYVRNLAT------GGEACPPELVERWSER-GRRIFNCYGPTEATVWATR-------S 1339
Cdd:cd05920 227 REGVTVTALVPALVSLWLDAAASRRADLSSlrllqvGGARLSPALARRVPPVlGCTLQQVFGMAEGLLNYTRlddpdevI 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1340 RMTAGKPVTigkPVDgfTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRV 1419
Cdd:cd05920 307 IHTQGRPMS---PDD--EIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYRAPEHNARAFTPDGF-------YRTGDLVRR 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1420 AKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGA--TIDSAAVLDE 1497
Cdd:cd05920 375 TPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELLGER---SCAFVVLRDPPpsAAQLRRFLRE 451
|
490 500 510
....*....|....*....|....*....|...
gi 1827387616 1498 AAqhLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd05920 452 RG--LAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1186-1526 |
1.02e-31 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 129.42 E-value: 1.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1186 YLIYTSGSTGRPKAVGVSHTGIvdFVNSLAKITTGTPEDEPDTRILHVASPSFDASMFEM-----------AWAIPAGHT 1254
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEDI--FRMLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPApplmhgtgswtAFGGLLGGQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1255 LVIAPQADFAGDALATVLERDEVTDMIITPSVLAT--VDPERAQYVRNL------ATGGEACPPELVERWSER--GRRIF 1324
Cdd:cd05924 85 TVVLPDDRFDPEEVWRTIEKHKVTSMTIVGDAMARplIDALRDAGPYDLsslfaiSSGGALLSPEVKQGLLELvpNITLV 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1325 NCYGPTEATvwATRSRMTAGKPVTIGK--PVDGFTVrVLDGRLHEVPQGVVGELYLSTAGL-ARGYLGRPGQTAVSFV-A 1400
Cdd:cd05924 165 DAFGSSETG--FTGSGHSAGSGPETGPftRANPDTV-VLDDDGRVVPPGSGGVGWIARRGHiPLGYYGDEAKTAETFPeV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1401 DpfgepGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAY 1480
Cdd:cd05924 242 D-----GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPDERWGQ---EVVAV 313
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 1827387616 1481 LVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLD 1526
Cdd:cd05924 314 VQLREGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
4-468 |
1.54e-31 |
|
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: 132.37 E-value: 1.54e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDGE 83
Cdd:cd12119 29 AEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRDFL 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 ---AEARSRFDDIVDVHVLDISSPGDADLDE-----EEFAGPTRPA---------NAAFTLFTSGSTGRPKAVVITHR-- 144
Cdd:cd12119 109 pllEAIAPRLPTVEHVVVMTDDAAMPEPAGVgvlayEELLAAESPEydwpdfdenTAAAICYTSGTTGNPKGVVYSHRsl 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 145 -----GIANRLAADIEQydltaRDVFLykaPITfdvsvrEIF------LPIA---IGATLVIaePGRHGDPVHLADLIRR 210
Cdd:cd12119 189 vlhamAALLTDGLGLSE-----SDVVL---PVV------PMFhvnawgLPYAaamVGAKLVL--PGPYLDPASLAELIER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 211 HGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRlpGTRLQNQYGPAEASIVVTIHRVT---- 286
Cdd:cd12119 253 EGVTFAAGVPTVWQGLLDHLEANGRDLSSLRRVVIGGSAVPRSLIEAFEER--GVRVIHAWGMTETSPLGTVARPPsehs 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 287 ------QDDRVIPIGTPTRRVSARVLDAALREVPI--GVPGELYLGGVQLARGYAGRPDlTAERFVADPFgepgarlYRT 358
Cdd:cd12119 331 nlsedeQLALRAKQGRPVPGVELRIVDDDGRELPWdgKAVGELQVRGPWVTKSYYKNDE-ESEALTEDGW-------LRT 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 359 GDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGPGGQQ---LVGYLAP-ADVDVDTVAA 434
Cdd:cd12119 403 GDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKWGErplAVVVLKEgATVTAEELLE 482
|
490 500 510
....*....|....*....|....*....|....
gi 1827387616 435 TTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd12119 483 FLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
4-470 |
1.95e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 132.74 E-value: 1.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDGE 83
Cdd:PRK07788 78 AELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGPQLAEVAAREGVKALVYDDEFT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 AEARSRFDDIVDVHVL-------DISSPGDADLDE-----EEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLA 151
Cdd:PRK07788 158 DLLSALPPDLGRLRAWggnpdddEPSGSTDETLDDliagsSTAPLPKPPKPGGIVILTSGTTGTPKGAPRPEPSPLAPLA 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 152 ADIEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAepgRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLG 231
Cdd:PRK07788 238 GLLSRVPFRAGETTLLPAPMFHATGWAHLTLAMALGSTVVLR---RRFDPEATLEDIAKHKATALVVVPVMLSRILDLGP 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 232 AGVG--ELTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASiVVTIHRvTQDDRVIP--IGTPTRRVSARVLD 307
Cdd:PRK07788 315 EVLAkyDTSSLKIIFVSGSALSPELATRALEAF-GPVLYNLYGSTEVA-FATIAT-PEDLAEAPgtVGRPPKGVTVKILD 391
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 308 AALREVPIGVPGELYLGGVQLARGYAGrpdltaerfVADPFGEPGarLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRL 387
Cdd:PRK07788 392 ENGNEVPRGVVGRIFVGNGFPFEGYTD---------GRDKQIIDG--LLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENV 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 388 ELGEVEAALAAAPGVLHAAAAVVDGPG-GQQLVGYLAP---ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKV 463
Cdd:PRK07788 461 FPAEVEDLLAGHPDVVEAAVIGVDDEEfGQRLRAFVVKapgAALDEDAIKDYVRDNLARYKVPRDVVFLDELPRNPTGKV 540
|
....*..
gi 1827387616 464 DRRLLPE 470
Cdd:PRK07788 541 LKRELRE 547
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1023-1532 |
2.89e-31 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 132.20 E-value: 2.89e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1023 TPGAMVGRGGEVEA------GTLIDVLAQRDldPDHPALIC--DGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGME 1094
Cdd:PRK12583 1 MPQPSYYQGGGDKPlltqtiGDAFDATVARF--PDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1095 RSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDASTR-----------------ARLGESSCE---- 1153
Cdd:PRK12583 79 NCAEWLLTQFATARIGAILVNINPAYRASELEYALGQSGVRWVICADAFKtsdyhamlqellpglaeGQPGALACErlpe 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1154 --WVDL------------ADLEAEAESGDDITDTERNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITT 1219
Cdd:PRK12583 159 lrGVVSlapapppgflawHELQARGETVSREALAERQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1220 GTPEDEpdtriLHVASPSFDAsmFEMAWA----IPAGHTLVIaPQADFagDALATV--LERDEVTDMIITPSV-LATVD- 1291
Cdd:PRK12583 239 LTEHDR-----LCVPVPLYHC--FGMVLAnlgcMTVGACLVY-PNEAF--DPLATLqaVEEERCTALYGVPTMfIAELDh 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1292 PERAQY-VRNLATG---GEACPPELVERWSERGR--RIFNCYGPTEATVWATRSrmTAGKPV-----TIGKPVDGFTVRV 1360
Cdd:PRK12583 309 PQRGNFdLSSLRTGimaGAPCPIEVMRRVMDEMHmaEVQIAYGMTETSPVSLQT--TAADDLerrveTVGRTQPHLEVKV 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1361 LDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarMYaTGDLVRVAKGGNLEFAGRADHQVKINGQ 1440
Cdd:PRK12583 387 VDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW------MH-TGDLATMDEQGYVRIVGRSKDMIIRGGE 459
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1441 RVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLT 1520
Cdd:PRK12583 460 NIYPREIEEFLFTHPAVADVQVFGVPDEKYGE---EIVAWVRLHPGHAASEEELREFCKARIAHFKVPRYFRFVDEFPMT 536
|
570
....*....|..
gi 1827387616 1521 PAGKLDRAALPE 1532
Cdd:PRK12583 537 VTGKVQKFRMRE 548
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1-472 |
4.42e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 130.11 E-value: 4.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGvgaevAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:PRK07787 26 LSRSDLAGAATAVAERVAGAR-----RVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSGAQAWLGPA 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRFDdiVDVHVLDISSPGDADldeeefagptrPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:PRK07787 101 PDDPAGLPHVP--VRLHARSWHRYPEPD-----------PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEAWQWT 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPItFDVS--VREIFLPIAIGATLViaEPGRHgDPVHLADLIRRHGvTVIHFVPAM---LAAFNEVLGAgvg 235
Cdd:PRK07787 168 ADDVLVHGLPL-FHVHglVLGVLGPLRIGNRFV--HTGRP-TPEAYAQALSEGG-TLYFGVPTVwsrIAADPEAARA--- 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 236 eLTSLRLIQTGGEALTPPVARDLmVRLPGTRLQNQYGPAEASIVVTIhRVTQDDRVIPIGTPTRRVSARVLDAALREVPI 315
Cdd:PRK07787 240 -LRGARLLVSGSAALPVPVFDRL-AALTGHRPVERYGMTETLITLST-RADGERRPGWVGLPLAGVETRLVDEDGGPVPH 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 316 GVP--GELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGR--TDFqVKLRGQRLELGE 391
Cdd:PRK07787 317 DGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVAVVDPDGMHRIVGResTDL-IKSGGYRIGAGE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 392 VEAALAAAPGVlhAAAAVVDGPG---GQQLVGYLAPA-DVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRL 467
Cdd:PRK07787 389 IETALLGHPGV--REAAVVGVPDddlGQRIVAYVVGAdDVAADELIDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQ 466
|
....*
gi 1827387616 468 LPEPE 472
Cdd:PRK07787 467 LLSEG 471
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
4-468 |
4.62e-31 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 129.54 E-value: 4.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTsdge 83
Cdd:cd05969 4 AQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 aearsrfddivdvhvldisspgdadldeEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARD 163
Cdd:cd05969 80 ----------------------------EELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVLDLHPDD 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 164 VFLYKA-PITFDVSVREIFLPIAIGATLVIAEpGRHgDPVHLADLIRRHGVTVIHFVPAmlaAFNEVLGAGVG-----EL 237
Cdd:cd05969 132 IYWCTAdPGWVTGTVYGIWAPWLNGVTNVVYE-GRF-DAESWYGIIERVKVTVWYTAPT---AIRMLMKEGDElarkyDL 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 238 TSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIGV 317
Cdd:cd05969 207 SSLRFIHSVGEPLNPEAIRWGMEVF-GVPIHDTWWQTETGSIMIANYPCMPIKPGSMGKPLPGVKAAVVDENGNELPPGT 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 318 PGELYL--GGVQLARGYAGRPDLTAERFVADpfgepgarLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAA 395
Cdd:cd05969 286 KGILALkpGWPSMFRGIWNDEERYKNSFIDG--------WYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPFEVESA 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 396 LAAAPGVlhAAAAVVDGPG---GQQLVGYLA------PADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRR 466
Cdd:cd05969 358 LMEHPAV--AEAGVIGKPDplrGEIIKAFISlkegfePSDELKEEIINFVRQKLGAHVAPREIEFVDNLPKTRSGKIMRR 435
|
..
gi 1827387616 467 LL 468
Cdd:cd05969 436 VL 437
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1050-1540 |
7.19e-31 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 130.67 E-value: 7.19e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:PRK07786 31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDAS-----TRARL------------GESSCEWVDLADLEAEAESGDDITDTERNGSvrltnlAYLIYTSG 1192
Cdd:PRK07786 111 SDCGAHVVVTEAAlapvaTAVRDivpllstvvvagGSSDDSVLGYEDLLAEAGPAHAPVDIPNDSP------ALIMYTSG 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1193 STGRPKAVGVSHTGIVDfvNSLAKITTGTPEDEPDtrILHVASPSFD-ASMFEMAWAIPAGHTLVIAPQADFAGDALATV 1271
Cdd:PRK07786 185 TTGRPKGAVLTHANLTG--QAMTCLRTNGADINSD--VGFVGVPLFHiAGIGSMLPGLLLGAPTVIYPLGAFDPGQLLDV 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1272 LERDEVTDMIITP----SVLA--TVDPeRAQYVRNLATGGEACPPELVERWSER--GRRIFNCYGPTEATvwaTRSRMTA 1343
Cdd:PRK07786 261 LEAEKVTGIFLVPaqwqAVCAeqQARP-RDLALRVLSWGAAPASDTLLRQMAATfpEAQILAAFGQTEMS---PVTCMLL 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1344 GKPV-----TIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmyATGDLVR 1418
Cdd:PRK07786 337 GEDAirklgSVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF--------HSGDLVR 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1419 VAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGvestRGGRKHTEV-VAYLVAKPGATIDSAAVLDE 1497
Cdd:PRK07786 409 QDEEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIG----RADEKWGEVpVAVAAVRNDDAALTLEDLAE 484
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1827387616 1498 -AAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEPH-APEPAE 1540
Cdd:PRK07786 485 fLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRERYgACVNVE 529
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1053-1530 |
7.38e-31 |
|
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate aerobic degradation pathway by activating 2-aminobenzoate to 2-aminobenzoyl-CoA. The reaction is carried out via a two-step process; the first step is ATP-dependent and forms a 2-aminobenzoyl-AMP intermediate, and the second step forms the 2-aminobenzoyl-CoA ester and releases the AMP. 2-Aminobenzoyl-CoA is further converted to 2-amino-5-oxo-cyclohex-1-ene-1-carbonyl-CoA catalyzed by 2-aminobenzoyl-CoA monooxygenase/reductase. ABCL has been purified from cells aerobically grown with 2-aminobenzoate as sole carbon, energy, and nitrogen source, and has been characterized as a monomer.
Pssm-ID: 341268 [Multi-domain] Cd Length: 439 Bit Score: 128.75 E-value: 7.38e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1053 PALICDGTEMDYDEFETRTNAIARALLARGVS-PEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLED 1131
Cdd:cd05958 2 TCLRSPEREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDK 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1132 SGATVGITDASTRARlgesscewvdladleaeaesgDDItdterngsvrltnlAYLIYTSGSTGRPKAVGVSHTGIVDFV 1211
Cdd:cd05958 82 ARITVALCAHALTAS---------------------DDI--------------CILAFTSGTTGAPKATMHFHRDPLASA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1212 NSLAKITTGTpedEPDTRILHVASPSFDASMFEMA-WAIPAGHTLVIAPQAdfAGDALATVLERDEVTDMIITPSVLATV 1290
Cdd:cd05958 127 DRYAVNVLRL---REDDRFVGSPPLAFTFGLGGVLlFPFGVGASGVLLEEA--TPDLLLSAIARYKPTVLFTAPTAYRAM 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1291 --DPERAQY----VRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDG 1363
Cdd:cd05958 202 laHPDAAGPdlssLRKCVSAGEALPAALHRAWKEAtGIPIIDGIGSTEMFHIFISARPGDARPGATGKPVPGYEAKVVDD 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1364 RLHEVPQGVVGELYLStaglargylgrpGQTAVSFVADPfgepGARMY------ATGDLVRVAKGGNLEFAGRADHQVKI 1437
Cdd:cd05958 282 EGNPVPDGTIGRLAVR------------GPTGCRYLADK----RQRTYvqggwnITGDTYSRDPDGYFRHQGRSDDMIVS 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1438 NGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATIDSA---AVLDEAAQHLAAHMVPSQAIVI 1514
Cdd:cd05958 346 GGYNIAPPEVEDVLLQHPAVAECAVVGHPDESRGVV---VKAFVVLRPGVIPGPVlarELQDHAKAHIAPYKYPRAIEFV 422
|
490
....*....|....*.
gi 1827387616 1515 DEIPLTPAGKLDRAAL 1530
Cdd:cd05958 423 TELPRTATGKLQRFAL 438
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1038-1530 |
7.49e-31 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 130.64 E-value: 7.49e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1038 TLIDVLAQR-DLDPDHPALICD-GTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVP 1115
Cdd:PRK06087 24 SLADYWQQTaRAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1116 VDPAYPADRIAYMLEDSGATVGITDASTRARLGES----------SCEWVDLADLEAEAESGDDITDTERNG-------S 1178
Cdd:PRK06087 104 LLPSWREAELVWVLNKCQAKMFFAPTLFKQTRPVDlilplqnqlpQLQQIVGVDKLAPATSSLSLSQIIADYeplttaiT 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1179 VRLTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtrILHVASPSFDASMFEMAWAIP--AGHTLV 1256
Cdd:PRK06087 184 THGDELAAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQD-----VFMMPAPLGHATGFLHGVTAPflIGARSV 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1257 IapQADFAGDALATVLERDEVTDMI-ITPSV---LATV--DPERAQYVRNLATGGEACPPELVERWSERGRRIFNCYGPT 1330
Cdd:PRK06087 259 L--LDIFTPDACLALLEQQRCTCMLgATPFIydlLNLLekQPADLSALRFFLCGGTTIPKKVARECQQRGIKLLSVYGST 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1331 EATVWA------TRSRMTAgkpvTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFg 1404
Cdd:PRK06087 337 ESSPHAvvnlddPLSRFMH----TDGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGW- 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1405 epgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAK 1484
Cdd:PRK06087 412 ------YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKIHDACVVAMPDERLGER---SCAYVVLK 482
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1827387616 1485 PGATIDSAAVLDE--AAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK06087 483 APHHSLTLEEVVAffSRKRVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1058-1526 |
9.06e-31 |
|
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: 129.37 E-value: 9.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1058 DGTEMDYDEFETRTNAIARaLLARGVSPEDVVAVGMERSIGSVLATWGVIKSGaaYVPVDPAYPA--DRIAYMLEDSGAT 1135
Cdd:cd05909 4 LGTSLTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAglRELRACIKLAGIK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1136 VGITD-------ASTRARLGESSCEWVDLADLEAEAESGDDI----------TDTERN---GSVRLTNLAYLIYTSGSTG 1195
Cdd:cd05909 81 TVLTSkqfieklKLHHLFDVEYDARIVYLEDLRAKISKADKCkaflagkfppKWLLRIfgvAPVQPDDPAVILFTSGSEG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1196 RPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtrILHVASPSFDASMFEMAWAIP--AGHTLVIAPQ-------ADFAGD 1266
Cdd:cd05909 161 LPKGVVLSHKNLLANVEQITAIFDPNPED-----VVFGALPFFHSFGLTGCLWLPllSGIKVVFHPNpldykkiPELIYD 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1267 ALATVLerdevtdmIITPSVLA----TVDPERAQYVRNLATGGEACPPELVERWSER-GRRIFNCYGPTEAT-VWATRSR 1340
Cdd:cd05909 236 KKATIL--------LGTPTFLRgyarAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKfGIRILEGYGTTECSpVISVNTP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1341 MTAGKPVTIGKPVDGFTVRVLDGRLH-EVPQGVVGELYLSTAGLARGYLGRPGQTAVsfvadpfgEPGARMYATGDLVRV 1419
Cdd:cd05909 308 QSPNKEGTVGRPLPGMEVKIVSVETHeEVPIGEGGLLLVRGPNVMLGYLNEPELTSF--------AFGDGWYDTGDIGKI 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1420 AKGGNLEFAGRADHQVKINGQRVELGEIE-AVLDAQPGVAQSVVVGVESTRGGrkhtEVVAYLVAKPGATIDSaavLDEA 1498
Cdd:cd05909 380 DGEGFLTITGRLSRFAKIAGEMVSLEAIEdILSEILPEDNEVAVVSVPDGRKG----EKIVLLTTTTDTDPSS---LNDI 452
|
490 500 510
....*....|....*....|....*....|
gi 1827387616 1499 AQH--LAAHMVPSQAIVIDEIPLTPAGKLD 1526
Cdd:cd05909 453 LKNagISNLAKPSYIHQVEEIPLLGTGKPD 482
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
2567-3063 |
1.10e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 128.95 E-value: 1.10e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2567 LAELFRAAARRAPDHVAVVDGAGARLTYRELDEASDRLARwligrGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPI 2646
Cdd:PRK07787 1 LASLNPAAVAAAADIADAVRIGGRVLSRSDLAGAATAVAE-----RVAGARRVAVLATPTLATVLAVVGALIAGVPVVPV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2647 DPDY-PAERvASMIEDSGAVLGLsvlasGDLPGQefewmrldddsvAAEIAAVPAGPITD-AERLGEVTAANLAYVIYTS 2724
Cdd:PRK07787 76 PPDSgVAER-RHILADSGAQAWL-----GPAPDD------------PAGLPHVPVRLHARsWHRYPEPDPDAPALIVYTS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2725 GSTGRPKGVAVTHSGLANF--ARQESDRLNAGDnpvVLGFASPSFDAS--VLEYLLATVNEGTLAY--RPS-EAVGGEVl 2797
Cdd:PRK07787 138 GTTGPPKGVVLSRRAIAADldALAEAWQWTADD---VLVHGLPLFHVHglVLGVLGPLRIGNRFVHtgRPTpEAYAQAL- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2798 erfiaEHGATHTFLTPSVLSTM--DPTAVPSL---RVIAAGGEAVPQPIVDRWAPAT--ELHNLYGPTET--TIGITISS 2868
Cdd:PRK07787 214 -----SEGGTLYFGVPTVWSRIaaDPEAARALrgaRLLVSGSAALPVPVFDRLAALTghRPVERYGMTETliTLSTRADG 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2869 AMRPGdpvRLGGPIGGVDLMVLDERLRPVPVGMP--GELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVV 2946
Cdd:PRK07787 289 ERRPG---WVGLPLAGVETRLVDEDGGPVPHDGEtvGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGDVA 358
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2947 RWTPDTDtggltLEYTGR-SDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGS-VATALAAYIVPVDGAVEvSELK 3024
Cdd:PRK07787 359 VVDPDGM-----HRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDdLGQRIVAYVVGADDVAA-DELI 432
|
490 500 510
....*....|....*....|....*....|....*....
gi 1827387616 3025 AFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPV 3063
Cdd:PRK07787 433 DFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQLLSEG 471
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1060-1533 |
2.17e-30 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 128.79 E-value: 2.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1060 TEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRiaymledsgATVGIT 1139
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR---------QNIYLG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1140 DASTRARLGesscewvdLADleAEAESGDDITDTerngsvrltnlayLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKiTT 1219
Cdd:cd17647 90 VAKPRGLIV--------IRA--AGVVVGPDSNPT-------------LSFTSGSEGIPKGVLGRHFSLAYYFPWMAK-RF 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1220 GTPEDEPDTRILHVASPSFDASMFEmawAIPAGHTLVIaPQADFAG--DALATVLERDEVTDMIITPSV--LATVDP--- 1292
Cdd:cd17647 146 NLSENDKFTMLSGIAHDPIQRDMFT---PLFLGAQLLV-PTQDDIGtpGRLAEWMAKYGATVTHLTPAMgqLLTAQAttp 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1293 ----ERAQYV---------RNLATGGEACppelverwsergrRIFNCYGPTEA----TVWATRSR-------------MT 1342
Cdd:cd17647 222 fpklHHAFFVgdiltkrdcLRLQTLAENV-------------RIVNMYGTTETqravSYFEVPSRssdptflknlkdvMP 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1343 AGKPVtigKPVDGFTVRVLDgRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEPGA-------------- 1408
Cdd:cd17647 289 AGRGM---LNVQLLVVNRND-RTQICGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFVEPDHwnyldkdnnepwrq 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1409 -------RMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVgVESTRGGRKhtEVVAYL 1481
Cdd:cd17647 365 fwlgprdRLYRTGDLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITL-VRRDKDEEP--TLVSYI 441
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 1482 VAKP-----------------------GATIDSAAVLDEAAQH----LAAHMVPSQAIVIDEIPLTPAGKLDRAALPEP 1533
Cdd:cd17647 442 VPRFdkpddesfaqedvpkevstdpivKGLIGYRKLIKDIREFlkkrLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
2592-3059 |
2.73e-30 |
|
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most similar to acetyl-CoA synthetase. Acetyl-CoA synthetase (ACS) catalyzes the formation of acetyl-CoA from acetate, CoA, and ATP. Synthesis of acetyl-CoA is carried out in a two-step reaction. In the first step, the enzyme catalyzes the synthesis of acetyl-AMP intermediate from acetate and ATP. In the second step, acetyl-AMP reacts with CoA to produce acetyl-CoA. This enzyme is only present in bacteria.
Pssm-ID: 341273 [Multi-domain] Cd Length: 442 Bit Score: 127.23 E-value: 2.73e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2592 LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAvlglsvl 2671
Cdd:cd05969 1 YTFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEA------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2672 asgdlpgqefewmrldddsvaaeiaavpAGPITDAERLGEVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRL 2751
Cdd:cd05969 74 ----------------------------KVLITTEELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMIFYYFTGKYVL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2752 NAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGGEVLERFIAEHGATHTFLTPSVLSTMDPTAV------- 2824
Cdd:cd05969 126 DLHPDDIYWCTADPGWVTGTVYGIWAPWLNGVTNVVYEGRFDAESWYGIIERVKVTVWYTAPTAIRMLMKEGDelarkyd 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2825 -PSLRVIAAGGEAVpQPIVDRW---APATELHNLYGPTETTigiTISSAMRPGDPVR---LGGPIGGVDLMVLDERLRPV 2897
Cdd:cd05969 206 lSSLRFIHSVGEPL-NPEAIRWgmeVFGVPIHDTWWQTETG---SIMIANYPCMPIKpgsMGKPLPGVKAAVVDENGNEL 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2898 PVGMPGELYVAGG--ALSRGYLDRSGLTAERFTaNPYGTAGQRMYRTGDVVRWtpdtdtggltleYTGRSDDQVKLRGLR 2975
Cdd:cd05969 282 PPGTKGILALKPGwpSMFRGIWNDEERYKNSFI-DGWYLTGDLAYRDEDGYFW------------FVGRADDIIKTSGHR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2976 IELGEIEAVLAEHDAVESAVVLGVGGSV-ATALAAYIVPVDGAVEVSELK----AFAGGRLPAYMVPSSFTVIDELPLTP 3050
Cdd:cd05969 349 VGPFEVESALMEHPAVAEAGVIGKPDPLrGEIIKAFISLKEGFEPSDELKeeiiNFVRQKLGAHVAPREIEFVDNLPKTR 428
|
....*....
gi 1827387616 3051 VGKLDKRAL 3059
Cdd:cd05969 429 SGKIMRRVL 437
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1044-1532 |
2.79e-30 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 128.62 E-value: 2.79e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1044 AQRDldPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPAD 1123
Cdd:PRK07470 17 ARRF--PDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPD 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1124 RIAYMLEDSGATVGI--------TDASTRARLGESSCEWVDLADLEA--EAESGDDITDTERNGSVRLTNLAYLIYTSGS 1193
Cdd:PRK07470 95 EVAYLAEASGARAMIchadfpehAAAVRAASPDLTHVVAIGGARAGLdyEALVARHLGARVANAAVDHDDPCWFFFTSGT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1194 TGRPKAVGVSHtGIVDFV--NSLAKITTGTPEDEpdtRILHVASPSFDASMFEMAwAIPAGHTLVIAPQADFAGDALATV 1271
Cdd:PRK07470 175 TGRPKAAVLTH-GQMAFVitNHLADLMPGTTEQD---ASLVVAPLSHGAGIHQLC-QVARGAATVLLPSERFDPAEVWAL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1272 LERDEVTDMIITPSVLA--TVDPERAQY----VRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATvwatrSRMTAG 1344
Cdd:PRK07470 250 VERHRVTNLFTVPTILKmlVEHPAVDRYdhssLRYVIYAGAPMYRADQKRALAKlGKVLVQYFGLGEVT-----GNITVL 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1345 KPV-------------TIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmy 1411
Cdd:PRK07470 325 PPAlhdaedgpdarigTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF-------- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1412 ATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEV-VAYLVAKPGATID 1490
Cdd:PRK07470 397 RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVWG----EVgVAVCVARDGAPVD 472
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1827387616 1491 SAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:PRK07470 473 EAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1050-1524 |
4.36e-30 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 127.42 E-value: 4.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDAS--TRARL--GESSCEWVDLADlEAEAesgddITdterngsvrltnlayLIYTSGSTGRPKAVGVSHT 1205
Cdd:cd12118 98 RHSEAKVLFVDREfeYEDLLaeGDPDFEWIPPAD-EWDP-----IA---------------LNYTSGTTGRPKGVVYHHR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1206 GIvdFVNSLAKITTGtpEDEPDTRILHVAsPSFDASMFEMAWAIPA-GHTLVIAPQADfaGDALATVLERDEVTDMIITP 1284
Cdd:cd12118 157 GA--YLNALANILEW--EMKQHPVYLWTL-PMFHCNGWCFPWTVAAvGGTNVCLRKVD--AKAIYDLIEKHKVTHFCGAP 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1285 SVLATVDPERAQYVRNL------ATGGEACPPELVERWSERGRRIFNCYGPTE----ATV------WAT-----RSRMTA 1343
Cdd:cd12118 230 TVLNMLANAPPSDARPLphrvhvMTAGAPPPAAVLAKMEELGFDVTHVYGLTEtygpATVcawkpeWDElpteeRARLKA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1344 GKPVTIgkpVDGFTVRVLD-GRLHEVPQ-GV-VGELYLSTAGLARGYLGRPGQTAVSFvadpfgEPGarMYATGDLVRVA 1420
Cdd:cd12118 310 RQGVRY---VGLEEVDVLDpETMKPVPRdGKtIGEIVFRGNIVMKGYLKNPEATAEAF------RGG--WFHSGDLAVIH 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1421 KGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEV-VAYLVAKPGATIDSAAVLDEAA 1499
Cdd:cd12118 379 PDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKWG----EVpCAFVELKEGAKVTEEEIIAFCR 454
|
490 500
....*....|....*....|....*
gi 1827387616 1500 QHLAAHMVPSQaIVIDEIPLTPAGK 1524
Cdd:cd12118 455 EHLAGFMVPKT-VVFGELPKTSTGK 478
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1043-1527 |
6.34e-30 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 127.00 E-value: 6.34e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1043 LAQR-DLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYP 1121
Cdd:PRK03640 8 LKQRaFLTPDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1122 ADRIAYMLEDSGATVGITDASTRARLGESSCewVDLADLEAEAESGDDITDTerngsVRLTNLAYLIYTSGSTGRPKavG 1201
Cdd:PRK03640 88 REELLWQLDDAEVKCLITDDDFEAKLIPGIS--VKFAELMNGPKEEAEIQEE-----FDLDEVATIMYTSGTTGKPK--G 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1202 VSHTgivdFVNSLAK-----ITTGTPEDEpdtRILhVASPSFDASMFE-MAWAIPAGHTLVIAPQadFAGDALATVLERD 1275
Cdd:PRK03640 159 VIQT----YGNHWWSavgsaLNLGLTEDD---CWL-AAVPIFHISGLSiLMRSVIYGMRVVLVEK--FDAEKINKLLQTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1276 EVTDMIITPSVLATV--DPERAQY---VRNLATGGEACPPELVERWSERGRRIFNCYGPTEatvwaTRSRMTAGKPVTI- 1349
Cdd:PRK03640 229 GVTIISVVSTMLQRLleRLGEGTYpssFRCMLLGGGPAPKPLLEQCKEKGIPVYQSYGMTE-----TASQIVTLSPEDAl 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1350 ------GKPVDGFTVRVLDGrLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmyATGDLVRVAKGG 1423
Cdd:PRK03640 304 tklgsaGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDIGYLDEEG 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1424 NLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEV-VAYLVAkpGATIDSAAVLDEAAQHL 1502
Cdd:PRK03640 375 FLYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWG----QVpVAFVVK--SGEVTEEELRHFCEEKL 448
|
490 500
....*....|....*....|....*
gi 1827387616 1503 AAHMVPSQAIVIDEIPLTPAGKLDR 1527
Cdd:PRK03640 449 AKYKVPKRFYFVEELPRNASGKLLR 473
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1-465 |
1.22e-29 |
|
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: 125.27 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:cd05919 11 VTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARDCEARLVVTSA 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DgeaearsrfddivdvhvldisspgdadldeeefagptrpaNAAFTLFTSGSTGRPKAVVITHR---GIANRLAADIeqY 157
Cdd:cd05919 91 D----------------------------------------DIAYLLYSSGTTGPPKGVMHAHRdplLFADAMAREA--L 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 158 DLTARDVFLYKAPITFDVSV-REIFLPIAIGATLVIAePGRHgDPVHLADLIRRHGVTVIHFVPAMLAAfneVLGAGVGE 236
Cdd:cd05919 129 GLTPGDRVFSSAKMFFGYGLgNSLWFPLAVGASAVLN-PGWP-TAERVLATLARFRPTVLYGVPTFYAN---LLDSCAGS 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 237 ---LTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTIHRVTQddrvIPIGTPTRRV---SARVLDAAL 310
Cdd:cd05919 204 pdaLRSLRLCVSAGEALPRGLGERWMEHF-GGPILDGIGATEVGHIFLSNRPGA----WRLGSTGRPVpgyEIRLVDEEG 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 311 REVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADpfgepgarLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELG 390
Cdd:cd05919 279 HTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATFNGG--------WYRTGDKFCRDADGWYTHAGRADDMLKVGGQWVSPV 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 391 EVEAALAAAPGVLHAA-AAVVDGPGGQQLVGYLAPADVDVDTVA------ATTAELLPEYMRPSAWVRLDAMPLSRSGKV 463
Cdd:cd05919 351 EVESLIIQHPAVAEAAvVAVPESTGLSRLTAFVVLKSPAAPQESlardihRHLLERLSAHKVPRRIAFVDELPRTATGKL 430
|
..
gi 1827387616 464 DR 465
Cdd:cd05919 431 QR 432
|
|
| benz_CoA_lig |
TIGR02262 |
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ... |
1-470 |
1.44e-29 |
|
benzoate-CoA ligase family; Characterized members of this protein family include benzoate-CoA ligase, 4-hydroxybenzoate-CoA ligase, 2-aminobenzoate-CoA ligase, etc. Members are related to fatty acid and acetate CoA ligases.
Pssm-ID: 274059 [Multi-domain] Cd Length: 505 Bit Score: 126.11 E-value: 1.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:TIGR02262 31 LSYGELEAQVRRLAAALRRLGVKREERVLLLMLDGVDFPIAFLGAIRAGIVPVALNTLLTADDYAYMLEDSRARVVFVSG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGE---AEARSRFDDIVDVHVLDISSPGDADLDEE-------EFAGPTRPANAAFTLFTSGSTGRPKAVVITHrgianrl 150
Cdd:TIGR02262 111 ALLpviKAALGKSPHLEHRVVVGRPEAGEVQLAELlateseqFKPAATQADDPAFWLYSSGSTGMPKGVVHTH------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 151 AADIEQYDLTAR--------DVFLYKAPITFDVSV-REIFLPIAIGATLVIAepGRHGDPVHLADLIRRHGVTVIHFVP- 220
Cdd:TIGR02262 184 SNPYWTAELYARntlgiredDVCFSAAKLFFAYGLgNALTFPMSVGATTVLM--GERPTPDAVFDRLRRHQPTIFYGVPt 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 221 ---AMLAAFNEVLGAGVgeltSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEAsIVVTIHRVTQDDRVIPIGTP 297
Cdd:TIGR02262 262 lyaAMLADPNLPSEDQV----RLRLCTSAGEALPAEVGQRWQARF-GVDIVDGIGSTEM-LHIFLSNLPGDVRYGTSGKP 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 298 TRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADpfgepgarLYRTGDRARWNRDGEIEYLGRTD 377
Cdd:TIGR02262 336 VPGYRLRLVGDGGQDVADGEPGELLISGPSSATMYWNNRAKSRDTFQGE--------WTRSGDKYVRNDDGSYTYAGRTD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 378 FQVKLRGQRLELGEVEAALAAAPGVLHAA--------------AAVVDGPGGQQLvgylapadvdVDTVAATTAELLPEY 443
Cdd:TIGR02262 408 DMLKVSGIYVSPFEIESALIQHPAVLEAAvvgvadedglikpkAFVVLRPGQTAL----------ETELKEHVKDRLAPY 477
|
490 500
....*....|....*....|....*..
gi 1827387616 444 MRPSAWVRLDAMPLSRSGKVDRRLLPE 470
Cdd:TIGR02262 478 KYPRWIVFVDDLPKTATGKIQRFKLRE 504
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
2-468 |
2.01e-29 |
|
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the phenylpropanoid metabolic pathway for monolignol and flavonoid biosynthesis. It catalyzes the synthesis of hydroxycinnamate-CoA thioesters in a two-step reaction, involving the formation of hydroxycinnamate-AMP anhydride and the nucleophilic substitution of AMP by CoA. The phenylpropanoid pathway is one of the most important secondary metabolism pathways in plants and hydroxycinnamate-CoA thioesters are the precursors of lignin and other important phenylpropanoids.
Pssm-ID: 341230 [Multi-domain] Cd Length: 505 Bit Score: 125.81 E-value: 2.01e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSD 81
Cdd:cd05904 34 TYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTPAEIAKQVKDSGAKLAFTTAE 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 GEAEARSRFDDIV-----DVHVLDISSPGDADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAA--DI 154
Cdd:cd05904 114 LAEKLASLALPVVlldsaEFDSLSFSDLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIAMVAQfvAG 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 155 EQYDLTARDVFLYKAPItFDVSVREIFL--PIAIGATLVIAepgRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGA 232
Cdd:cd05904 194 EGSNSDSEDVFLCVLPM-FHIYGLSSFAlgLLRLGATVVVM---PRFDLEELLAAIERYKVTHLPVVPPIVLALVKSPIV 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 233 GVGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVIP--IGTPTRRVSARVLDAAL 310
Cdd:cd05904 270 DKYDLSSLRQIMSGAAPLGKELIEAFRAKFPNVDLGQGYGMTESTGVVAMCFAPEKDRAKYgsVGRLVPNVEAKIVDPET 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 311 REV-PIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLEL 389
Cdd:cd05904 350 GESlPPNQTGELWIRGPSIMKGYLNNPEATAATIDKEGW-------LHTGDLCYIDEDGYLFIVDRLKELIKYKGFQVAP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 390 GEVEAALAAAPGVLHAA--------------AAVVDGPGGQqlvgyLAPADVdVDTVAATTAellpEYMRPSAWVRLDAM 455
Cdd:cd05904 423 AELEALLLSHPEILDAAvipypdeeagevpmAFVVRKPGSS-----LTEDEI-MDFVAKQVA----PYKKVRKVAFVDAI 492
|
490
....*....|...
gi 1827387616 456 PLSRSGKVDRRLL 468
Cdd:cd05904 493 PKSPSGKILRKEL 505
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
2575-3059 |
2.55e-29 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 125.07 E-value: 2.55e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2575 ARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAER 2654
Cdd:PRK03640 12 AFLTPDRTAIEFE-EKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2655 VASMIEDSGAVLglsVLASGDLPGQEFEWMRLDddsvaaeIAAVPAGPITDAERLGEVTAANLAYVIYTSGSTGRPKGVA 2734
Cdd:PRK03640 91 LLWQLDDAEVKC---LITDDDFEAKLIPGISVK-------FAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2735 VTHSGlaNFARQESDRLNAG--DNPVVLGfASPSFDASVLEYLLATVNEGTLAYrpseavggeVLERFIAE--HGA--TH 2808
Cdd:PRK03640 161 QTYGN--HWWSAVGSALNLGltEDDCWLA-AVPIFHISGLSILMRSVIYGMRVV---------LVEKFDAEkiNKLlqTG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2809 TFLTPSVLSTM---------DPTAVPSLRVIAAGGEAVPQPIVDrwapATELHNL-----YGPTETTIGITissAMRPGD 2874
Cdd:PRK03640 229 GVTIISVVSTMlqrllerlgEGTYPSSFRCMLLGGGPAPKPLLE----QCKEKGIpvyqsYGMTETASQIV---TLSPED 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2875 PVR----LGGPIGGVDLMVLDErLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANpygtagqrMYRTGDVVRwtp 2950
Cdd:PRK03640 302 ALTklgsAGKPLFPCELKIEKD-GVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDG--------WFKTGDIGY--- 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2951 dTDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG----GSVAtalAAYIVpVDGAVEVSELKAF 3026
Cdd:PRK03640 370 -LDEEGF-LYVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPddkwGQVP---VAFVV-KSGEVTEEELRHF 443
|
490 500 510
....*....|....*....|....*....|...
gi 1827387616 3027 AGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK03640 444 CEEKLAKYKVPKRFYFVEELPRNASGKLLRHEL 476
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2722-3056 |
2.62e-29 |
|
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: 122.00 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2722 YTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDN-----PVvlgfasPSFDA--SVLEYlLATVNEGTLAYRPSEAVGG 2794
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQdrlciPV------PLFHCfgSVLGV-LACLTHGATMVFPSPSFDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2795 EVLERFIAEHGATHTFLTPS----VLSTMDPTAVP--SLRVIAAGGEAVPQPIVDRWAPA---TELHNLYGPTETTIGIT 2865
Cdd:cd05917 82 LAVLEAIEKEKCTALHGVPTmfiaELEHPDFDKFDlsSLRTGIMAGAPCPPELMKRVIEVmnmKDVTIAYGMTETSPVST 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2866 ISsamRPGDPVRL-----GGPIGGVDLMVLDERLRPVP-VGMPGELYVAGGALSRGYLDRSGLTAERFTanpygtaGQRM 2939
Cdd:cd05917 162 QT---RTDDSIEKrvntvGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAID-------GDGW 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2940 YRTGDVVrwTPDTDTgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-----GGSVatalAAYIVPV 3014
Cdd:cd05917 232 LHTGDLA--VMDEDG---YCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVpderyGEEV----CAWIRLK 302
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1827387616 3015 DGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDK 3056
Cdd:cd05917 303 EGAeLTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1009-1531 |
3.86e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 125.11 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1009 AARAKSVSAPVSARTPGAMV------GRGGeVEAGTLIDVLAQRDldPDHPALICDGTEMDYDEFETRTNAIARALLARG 1082
Cdd:PRK13383 5 AARALVRSGLLNPPSPRAVLrllreaSRGG-TNPYTLLAVTAARW--PGRTAIIDDDGALSYRELQRATESLARRLTRDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1083 VSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDASTRARLGESSCEWVDLADLEA 1162
Cdd:PRK13383 82 VAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHISTVVADNEFAERIAGADDAVAVIDPATA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1163 EAESGDDITDTERNGSVrltnlayLIYTSGSTGRPKAVG-----VSHTGIVDFVNSLAKITTGTPedepdtriLHVASPS 1237
Cdd:PRK13383 162 GAEESGGRPAVAAPGRI-------VLLTSGTTGKPKGVPrapqlRSAVGVWVTILDRTRLRTGSR--------ISVAMPM 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1238 FDASMFEM-AWAIPAGHTLVIAPQADFAGDALATVLERDEVtdMIITPSVLATV----DPERAQ----YVRNLATGGEAC 1308
Cdd:PRK13383 227 FHGLGLGMlMLTIALGGTVLTHRHFDAEAALAQASLHRADA--FTAVPVVLARIlelpPRVRARnplpQLRVVMSSGDRL 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1309 PPELVERWSER-GRRIFNCYGPTEATVWATRSRMT-AGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARG 1386
Cdd:PRK13383 305 DPTLGQRFMDTyGDILYNGYGSTEVGIGALATPADlRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTR 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1387 YLGRPGQTAVSfvadpfgepgaRMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVE 1466
Cdd:PRK13383 385 YTDGGGKAVVD-----------GMTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVP 453
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 1467 STRGGRKhteVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALP 1531
Cdd:PRK13383 454 DERFGHR---LAAFVVLHPGSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
2545-3061 |
4.07e-29 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 125.38 E-value: 4.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2545 LPAEAAVELTPVTGGPAtdpvtLAELFRAAARRAPDHVAVVDGAG-ARLTYRELDEASDRLARWLIGRGVGPERAVALAI 2623
Cdd:PRK05852 1 MRFMGGAAPMASDFGPR-----IADLVEVAATRLPEAPALVVTADrIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRM 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2624 GRSAQLLTAIWAVAKTGGAYVPIDPDYPaerVASMIEDSGAVLGLSVLASGDLPGQEFE----WMRLDDdSVAAEIAAVP 2699
Cdd:PRK05852 76 GSNAEFVVALLAASRADLVVVPLDPALP---IAEQRVRSQAAGARVVLIDADGPHDRAEpttrWWPLTV-NVGGDSGPSG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2700 AGPITDAERLGEVTAA---------NLAYVIYTSGSTGRPKGVAVTHSGLANFARQ--ESDRLNAGDNPVVLgfaSPSFD 2768
Cdd:PRK05852 152 GTLSVHLDAATEPTPAtstpeglrpDDAMIMFTGGTTGLPKMVPWTHANIASSVRAiiTGYRLSPRDATVAV---MPLYH 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2769 A-SVLEYLLATVNEGTLAYRPSEA-VGGEVLERFIAEHGAT--------HTFLTPSVLSTMDPTAVPSLRVI----AAGG 2834
Cdd:PRK05852 229 GhGLIAALLATLASGGAVLLPARGrFSAHTFWDDIKAVGATwytavptiHQILLERAATEPSGRKPAALRFIrscsAPLT 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2835 EAVPQPIVDRW-APATELhnlYGPTETTIGIT---ISSAMRPGDPVRLGGPIG---GVDLMVLDERLRPVPVGMPGELYV 2907
Cdd:PRK05852 309 AETAQALQTEFaAPVVCA---FGMTEATHQVTttqIEGIGQTENPVVSTGLVGrstGAQIRIVGSDGLPLPAGAVGEVWL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2908 AGGALSRGYLDRSGLTAERFTANpygtagqrMYRTGDVVRWTPDTDtggltLEYTGRSDDQVKLRGLRIELGEIEAVLAE 2987
Cdd:PRK05852 386 RGTTVVRGYLGDPTITAANFTDG--------WLRTGDLGSLSAAGD-----LSIRGRIKELINRGGEKISPERVEGVLAS 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 2988 HDAVESAVVLGVGGSV-ATALAAYIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPE 3061
Cdd:PRK05852 453 HPNVMEAAVFGVPDQLyGEAVAAVIVPRESApPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
2717-3059 |
5.07e-29 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 120.51 E-value: 5.07e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2717 LAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLgFASPSFDASVLEYLLATVNEGTLAYRPSEAvgGEV 2796
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWL-LSLPLYHVGGLAILVRSLLAGAELVLLERN--QAL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2797 LERfIAEHGATHTFLTPSVLSTM-----DPTAVPSLRVIAAGGEAVPQPIVDRWAPAT-ELHNLYGPTETTIGITISSAM 2870
Cdd:cd17630 79 AED-LAPPGVTHVSLVPTQLQRLldsgqGPAALKSLRAVLLGGAPIPPELLERAADRGiPLYTTYGMTETASQVATKRPD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2871 RPGDPvRLGGPIGGVDLMVLDerlrpvpvgmPGELYVAGGALSRGYLDrsGLTAERFTANPYgtagqrmYRTGDVVRWTP 2950
Cdd:cd17630 158 GFGRG-GVGVLLPGRELRIVE----------DGEIWVGGASLAMGYLR--GQLVPEFNEDGW-------FTTKDLGELHA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2951 DTDtggltLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGS-VATALAAYIVPvDGAVEVSELKAFAGG 3029
Cdd:cd17630 218 DGR-----LTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEeLGQRPVAVIVG-RGPADPAELRAWLKD 291
|
330 340 350
....*....|....*....|....*....|
gi 1827387616 3030 RLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd17630 292 KLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
2575-3076 |
6.44e-29 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 124.89 E-value: 6.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2575 ARRA---PDHVAVvDGAGARLTYRELDEASDRLARWLIGRGVG-PERAVALAIGRSaQLLTAIWAVAKTGGAYVPIDPDY 2650
Cdd:PRK07786 24 ARHAlmqPDAPAL-RFLGNTTTWRELDDRVAALAGALSRRGVGfGDRVLILMLNRT-EFVESVLAANMLGAIAVPVNFRL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2651 PAERVASMIEDSGA--VLGLSVLAS------GDLPGQEFEWM---RLDDDSVAAEIAAVPAGPITDAERLGEVTAAnlaY 2719
Cdd:PRK07786 102 TPPEIAFLVSDCGAhvVVTEAALAPvatavrDIVPLLSTVVVaggSSDDSVLGYEDLLAEAGPAHAPVDIPNDSPA---L 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2720 VIYTSGSTGRPKGVAVTHSGLANFArQESDRLNAGDNPVVLGF-ASPSFD----ASVLEYLL---ATVNEGTLAYRPSEA 2791
Cdd:PRK07786 179 IMYTSGTTGRPKGAVLTHANLTGQA-MTCLRTNGADINSDVGFvGVPLFHiagiGSMLPGLLlgaPTVIYPLGAFDPGQL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2792 VggEVLERfiaeHGATHTFLTPSVLSTM--DPTAVP---SLRVIAAGGEAVPQPIVDRWA---PATELHNLYGPTETTig 2863
Cdd:PRK07786 258 L--DVLEA----EKVTGIFLVPAQWQAVcaEQQARPrdlALRVLSWGAAPASDTLLRQMAatfPEAQILAAFGQTEMS-- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2864 iTISSAMRPGDPVR----LGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANpygtagqrM 2939
Cdd:PRK07786 330 -PVTCMLLGEDAIRklgsVGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGG--------W 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2940 YRTGDVVRwtpdTDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG----GSVATALAAyIVPVD 3015
Cdd:PRK07786 401 FHSGDLVR----QDEEGY-VWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRAdekwGEVPVAVAA-VRNDD 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 3016 GAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPE-----PVLEAGEYVAPATGT 3076
Cdd:PRK07786 475 AALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPAGKVLKTELRErygacVNVERRSASAGFTER 540
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1009-1532 |
7.14e-29 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 124.49 E-value: 7.14e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1009 AARAKSV-SAPVSARTPGAMVGRggeveagtlidvlaQRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPED 1087
Cdd:PRK06155 7 GLAARAVdPLPPSERTLPAMLAR--------------QAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1088 VVAVGMERSIgSVLATW-GVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDASTRARL-----GESSCEWVDLADlE 1161
Cdd:PRK06155 73 RVALMCGNRI-EFLDVFlGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALLAALeaadpGDLPLPAVWLLD-A 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1162 AEAESGDDITDTER---------NGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtrILH 1232
Cdd:PRK06155 151 PASVSVPAGWSTAPlppldapapAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQFYWWGRNSAEDLEIGADD-----VLY 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1233 VASPSFDASMFEM-AWAIPAGHTLVIAPQADFAGDALATVLERDEVTDMI--ITPSVLA--TVDPERAQYVR-NLATGGe 1306
Cdd:PRK06155 226 TTLPLFHTNALNAfFQALLAGATYVLEPRFSASGFWPAVRRHGATVTYLLgaMVSILLSqpARESDRAHRVRvALGPGV- 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1307 acPPELVERWSER-GRRIFNCYGPTEATVwATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTA---G 1382
Cdd:PRK06155 305 --PAALHAAFRERfGVDLLDGYGSTETNF-VIAVTHGSQRPGSMGRLAPGFEARVVDEHDQELPDGEPGELLLRADepfA 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1383 LARGYLGRPGQTAVSFVADPFgepgarmyATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVV 1462
Cdd:PRK06155 382 FATGYFGMPEKTVEAWRNLWF--------HTGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAV 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1463 VGVESTRGGrkhTEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:PRK06155 454 FPVPSELGE---DEVMAAVVLRDGTALEPVALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVLRE 520
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1-470 |
7.72e-29 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 124.40 E-value: 7.72e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLdeqLPVDRAR---YMVRTAGVRLVV 77
Cdd:PRK13295 56 FTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPL---MPIFRERelsFMLKHAESKVLV 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 78 VTS-----DGEAEARSRFDDIVDV-HVLDISSPGDADLdEEEFAGPTR----------------PANAAFTLFTSGSTGR 135
Cdd:PRK13295 133 VPKtfrgfDHAAMARRLRPELPALrHVVVVGGDGADSF-EALLITPAWeqepdapailarlrpgPDDVTQLIYTSGTTGE 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 136 PKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPIT----FDVSVReifLPIAIGATLVIAEPGrhgDPVHLADLIRRH 211
Cdd:PRK13295 212 PKGVMHTANTLMANIVPYAERLGLGADDVILMASPMAhqtgFMYGLM---MPVMLGATAVLQDIW---DPARAAELIRTE 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 212 GVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTIHRVTQDDRV 291
Cdd:PRK13295 286 GVTFTMASTPFLTDLTRAVKESGRPVSSLRTFLCAGAPIPGALVERARAAL-GAKIVSAWGMTENGAVTLTKLDDPDERA 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 292 IPI-GTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERfvADPFgepgarlYRTGDRARWNRDGEI 370
Cdd:PRK13295 365 STTdGCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTD--ADGW-------FDTGDLARIDADGYI 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 371 EYLGRTDfQVKLRG-QRLELGEVEAALAAAPGVlhAAAAVVDGPG---GQQLVGYLAP---ADVDVDTVAA--TTAELLP 441
Cdd:PRK13295 436 RISGRSK-DVIIRGgENIPVVEIEALLYRHPAI--AQVAIVAYPDerlGERACAFVVPrpgQSLDFEEMVEflKAQKVAK 512
|
490 500
....*....|....*....|....*....
gi 1827387616 442 EYMrPSAWVRLDAMPLSRSGKVDRRLLPE 470
Cdd:PRK13295 513 QYI-PERLVVRDALPRTPSGKIQKFRLRE 540
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
2551-3056 |
8.30e-29 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 123.56 E-value: 8.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2551 VELTPvtggpatdpvtLAELFRAAARRaPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLL 2630
Cdd:cd12118 2 VPLTP-----------LSFLERAAAVY-PDRTSIVYG-DRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMY 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2631 TAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLGL--------SVLASGDlpgQEFEWMRLDDDSvaaeiaavpaGP 2702
Cdd:cd12118 69 ELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFvdrefeyeDLLAEGD---PDFEWIPPADEW----------DP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2703 ITdaerlgevtaanlayVIYTSGSTGRPKGVAVTHSG-----LANFARQEsdrlnAGDNPVVLgFASPSFDASVLEYLLA 2777
Cdd:cd12118 136 IA---------------LNYTSGTTGRPKGVVYHHRGaylnaLANILEWE-----MKQHPVYL-WTLPMFHCNGWCFPWT 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2778 TVnegtlayrpseAVGG----------EVLERFIAEHGATHTFLTPSVLST----MDPTAVP---SLRVIAAGgeAVPQP 2840
Cdd:cd12118 195 VA-----------AVGGtnvclrkvdaKAIYDLIEKHKVTHFCGAPTVLNMlanaPPSDARPlphRVHVMTAG--APPPA 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2841 IVdrWAPATEL-----HnLYGPTETTIGITISSAMRPGDPV----------RLGGPIGGVD-LMVLD-ERLRPVP---VG 2900
Cdd:cd12118 262 AV--LAKMEELgfdvtH-VYGLTETYGPATVCAWKPEWDELpteerarlkaRQGVRYVGLEeVDVLDpETMKPVPrdgKT 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2901 MpGELYVAGGALSRGYLDRSGLTAERFTANpygtagqrMYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIELGE 2980
Cdd:cd12118 339 I-GEIVFRGNIVMKGYLKNPEATAEAFRGG--------WFHSGDLAVIHPDG-----YIEIKDRSKDIIISGGENISSVE 404
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2981 IEAVLAEHDAVESAVVLGVG----GSVATalaAYIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFtVIDELPLTPVGKLD 3055
Cdd:cd12118 405 VEGVLYKHPAVLEAAVVARPdekwGEVPC---AFVELKEGAkVTEEEIIAFCREHLAGFMVPKTV-VFGELPKTSTGKIQ 480
|
.
gi 1827387616 3056 K 3056
Cdd:cd12118 481 K 481
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
2575-3059 |
8.53e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 123.84 E-value: 8.53e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2575 ARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAER 2654
Cdd:PRK06145 12 ARRTPDRAALVYR-DQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2655 VASMIEDSGAVLGLSVLASGDLPGQEFEWMRLDDDSVA-AEIAAVPAGPITDAERLGEvtaANLAYVIYTSGSTGRPKGV 2733
Cdd:PRK06145 91 VAYILGDAGAKLLLVDEEFDAIVALETPKIVIDAAAQAdSRRLAQGGLEIPPQAAVAP---TDLVRLMYTSGTTDRPKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2734 AVTHSglaNFARQESDR-----LNAGDNPVVLGfasPSFDASVLEYL-LATVNEGTLAYRPSEAVGGEVLERfIAEHGAT 2807
Cdd:PRK06145 168 MHSYG---NLHWKSIDHvialgLTASERLLVVG---PLYHVGAFDLPgIAVLWVGGTLRIHREFDPEAVLAA-IERHRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2808 HTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIV---DRWAPATELHNLYGPTETTIGITISSAMRPGDPV-R 2877
Cdd:PRK06145 241 CAWMAPVMLSRVltvpdrDRFDLDSLAWCIGGGEKTPESRIrdfTRVFTRARYIDAYGLTETCSGDTLMEAGREIEKIgS 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2878 LGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANpygtagqrMYRTGDVVRWtpdTDTGGL 2957
Cdd:PRK06145 321 TGRALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGD--------WFRSGDVGYL---DEEGFL 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2958 TLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-GGSVATALAAYIVPVDGA-VEVSELKAFAGGRLPAYM 3035
Cdd:PRK06145 390 YL--TDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVhDDRWGERITAVVVLNPGAtLTLEALDRHCRQRLASFK 467
|
490 500
....*....|....*....|....
gi 1827387616 3036 VPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK06145 468 VPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
2566-3065 |
9.67e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 124.50 E-value: 9.67e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVV-DGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYV 2644
Cdd:PRK12583 19 TIGDAFDATVARFPDREALVvRHQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2645 PIDPDYPAERVASMIEDSG--------------------------AVLGLSVLASGDLPgqEFEWMRLDDDSVA------ 2692
Cdd:PRK12583 99 NINPAYRASELEYALGQSGvrwvicadafktsdyhamlqellpglAEGQPGALACERLP--ELRGVVSLAPAPPpgflaw 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2693 AEIAAvpAGPITDAERLGEVTAA----NLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPvVLGFASPSFD 2768
Cdd:PRK12583 177 HELQA--RGETVSREALAERQASldrdDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHD-RLCVPVPLYH 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2769 --ASVLEYLLATVNEGTLAYrPSEAVGGEVLERFIAEHGATHTFLTPSV-LSTMDPTA-----VPSLRVIAAGGEAVPQP 2840
Cdd:PRK12583 254 cfGMVLANLGCMTVGACLVY-PNEAFDPLATLQAVEEERCTALYGVPTMfIAELDHPQrgnfdLSSLRTGIMAGAPCPIE 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2841 IVDRWAP---ATELHNLYGPTETTigiTISSAMRPGDPVRL-----GGPIGGVDLMVLDERLRPVPVGMPGELYVAGGAL 2912
Cdd:PRK12583 333 VMRRVMDemhMAEVQIAYGMTETS---PVSLQTTAADDLERrvetvGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSV 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2913 SRGYLDRSGLTAERFTANPYgtagqrMYrTGDVVrwTPDTDTgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVE 2992
Cdd:PRK12583 410 MKGYWNNPEATAESIDEDGW------MH-TGDLA--TMDEQG---YVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAVA 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 2993 SAVVLGVGGS-VATALAAYIVPVDG-AVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVLE 3065
Cdd:PRK12583 478 DVQVFGVPDEkYGEEIVAWVRLHPGhAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRMREISIE 552
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
2562-3060 |
9.74e-29 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 123.95 E-value: 9.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2562 TDPVTLAELfraAARRAPDHVAVVDGAGArLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGG 2641
Cdd:PRK13383 35 TNPYTLLAV---TAARWPGRTAIIDDDGA-LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2642 AYVPIDPDYPAERVASMIEDSgavlGLSVLASGDlpgqEF-EWMRLDDDSVAAeIAAVPAGPITDAERlgEVTAANLAYV 2720
Cdd:PRK13383 111 DVVPISTEFRSDALAAALRAH----HISTVVADN----EFaERIAGADDAVAV-IDPATAGAEESGGR--PAVAAPGRIV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2721 IYTSGSTGRPKGV---AVTHSGLA-NFARQESDRLNAGDNpvvLGFASPSFDASVLEYLLATVnegtlayrpseAVGGEV 2796
Cdd:PRK13383 180 LLTSGTTGKPKGVpraPQLRSAVGvWVTILDRTRLRTGSR---ISVAMPMFHGLGLGMLMLTI-----------ALGGTV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2797 LER--FIAE--------HGATHTFLTPSVLSTM--------DPTAVPSLRVIAAGGEAVPQPIVDRWAPATE--LHNLYG 2856
Cdd:PRK13383 246 LTHrhFDAEaalaqaslHRADAFTAVPVVLARIlelpprvrARNPLPQLRVVMSSGDRLDPTLGQRFMDTYGdiLYNGYG 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2857 PTETTIGITISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGltaerftanpyGTAG 2936
Cdd:PRK13383 326 STEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNNRPVGPRVTGRIFVGGELAGTRYTDGGG-----------KAVV 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2937 QRMYRTGDVVRwtpdTDTGGlTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGS-VATALAAYIVPVD 3015
Cdd:PRK13383 395 DGMTSTGDMGY----LDNAG-RLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDErFGHRLAAFVVLHP 469
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1827387616 3016 GA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALP 3060
Cdd:PRK13383 470 GSgVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1-468 |
1.82e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 123.17 E-value: 1.82e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:PRK06188 38 LTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALHPLGSLDDHAYVLEDAGISTLIVDP 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 ----DGEAEARSRFDDIVdvHVLDIS-SPGDADL-DEEEFAGPTRPANAAFTL------FTSGSTGRPKAVVITHRGIAN 148
Cdd:PRK06188 118 apfvERALALLARVPSLK--HVLTLGpVPDGVDLlAAAAKFGPAPLVAAALPPdiaglaYTGGTTGKPKGVMGTHRSIAT 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 149 RLAADIEQYDLTARDVFLYKAPITFDVSVreIFLPIAI-GATLVIAepgRHGDPVHLADLIRRHGVTVIHFVPAMLAAFN 227
Cdd:PRK06188 196 MAQIQLAEWEWPADPRFLMCTPLSHAGGA--FFLPTLLrGGTVIVL---AKFDPAEVLRAIEEQRITATFLVPTMIYALL 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 228 EVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTI-----HRVTQDDRVIPIGTPTRRVS 302
Cdd:PRK06188 271 DHPDLRTRDLSSLETVYYGASPMSPVRLAEAIERF-GPIFAQYYGQTEAPMVITYlrkrdHDPDDPKRLTSCGRPTPGLR 349
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 303 ARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADpfgepgarLYRTGDRARWNRDGEIEYLGRTD----- 377
Cdd:PRK06188 350 VALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAFRDG--------WLHTGDVAREDEDGFYYIVDRKKdmivt 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 378 --FQVKLRgqrlelgEVEAALAAAPGVlhAAAAVVDGPGGQQlvGYLAPADVDVDTVAATTAELLPEYMR--------PS 447
Cdd:PRK06188 422 ggFNVFPR-------EVEDVLAEHPAV--AQVAVIGVPDEKW--GEAVTAVVVLRPGAAVDAAELQAHVKerkgsvhaPK 490
|
490 500
....*....|....*....|.
gi 1827387616 448 AWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK06188 491 QVDFVDSLPLTALGKPDKKAL 511
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
571-996 |
2.19e-28 |
|
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: 121.02 E-value: 2.19e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 571 LPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAA-PVQDVLP-VAVAREQ 648
Cdd:cd19536 2 YPLSSLQEGMLFHSLLNPGGSVYLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSFIEDGLGqPVQVVHRqAQVPVTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 649 LDWREADSVESLVRSTTE-----GFDVSTQMPLRGRFHRDGAGLHVALTM--HHIAMDGQSIPVLARDLMSAYAARAEGR 721
Cdd:cd19536 82 LDLTPLEEQLDPLRAYKEetkirRFDLGRAPLVRAALVRKDERERFLLVIsdHHSILDGWSLYLLVKEILAVYNQLLEYK 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 722 TGGL-PVLDvqYADYALWQQSVLGDAddetsvlgEQLSHWRRVLAGlpaVTDLPMDRPRPAVLGTAGATVTVEFDDDLAD 800
Cdd:cd19536 162 PLSLpPAQP--YRDFVAHERASIQQA--------ASERYWREYLAG---ATLATLPALSEAVGGGPEQDSELLVSVPLPV 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 801 RVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPA--LEELIGMFVNTLLLRTQVdPGHSVGDLLGNV 878
Cdd:cd19536 229 RSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGTVVHGRSEETtgAERLLGLFLNTLPLRVTL-SEETVEDLLKRA 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 879 RTTVLDAFANDQVQFDELiealapERSSSHQPLAQIAFTYTEPTVNDVAGLEASGIQAAPVDTGvVNAKFDLTVAVRARS 958
Cdd:cd19536 308 QEQELESLSHEQVPLADI------QRCSEGEPLFDSIVNFRHFDLDFGLPEWGSDEGMRRGLLF-SEFKSNYDVNLSVLP 380
|
410 420 430
....*....|....*....|....*....|....*...
gi 1827387616 959 GGTPMAADFIYATDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd19536 381 KQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATA 418
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
2-463 |
2.31e-28 |
|
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: 123.46 E-value: 2.31e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSD 81
Cdd:cd17634 86 SYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPEAVAGRIIDSSSRLLITADG 165
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 GEAEARS-----RFDDIVDV------HVL-------DISSPGDADLD---------EEEFAGPTRPANAAFTLFTSGSTG 134
Cdd:cd17634 166 GVRAGRSvplkkNVDDALNPnvtsveHVIvlkrtgsDIDWQEGRDLWwrdliakasPEHQPEAMNAEDPLFILYTSGTTG 245
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 135 RPKAVVITHRGIANRLAADIEQ-YDLTARDVFLYKAPITFDVSVRE-IFLPIAIGATLVIAEPG-RHGDPVHLADLIRRH 211
Cdd:cd17634 246 KPKGVLHTTGGYLVYAATTMKYvFDYGPGDIYWCTADVGWVTGHSYlLYGPLACGATTLLYEGVpNWPTPARMWQVVDKH 325
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 212 GVTVIHFVPAMLAAfneVLGAGVG-----ELTSLRLIQTGGEALTPPVARDLMVRLPGTR--LQNQYGPAEAS-IVVTIH 283
Cdd:cd17634 326 GVNILYTAPTAIRA---LMAAGDDaiegtDRSSLRILGSVGEPINPEAYEWYWKKIGKEKcpVVDTWWQTETGgFMITPL 402
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 284 RVTQDdrvIPIGTPTRRV---SARVLDAALREVPIGVPGELYLGGV--QLARGYAGRPDLTAERFVADPFGepgarLYRT 358
Cdd:cd17634 403 PGAIE---LKAGSATRPVfgvQPAVVDNEGHPQPGGTEGNLVITDPwpGQTRTLFGDHERFEQTYFSTFKG-----MYFS 474
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 359 GDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGP---GGQQLVGY--LAPADVDVDTVA 433
Cdd:cd17634 475 GDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKV--AEAAVVGIPhaiKGQAPYAYvvLNHGVEPSPELY 552
|
490 500 510
....*....|....*....|....*....|....
gi 1827387616 434 ATTAELLPEYMRPSAWVR----LDAMPLSRSGKV 463
Cdd:cd17634 553 AELRNWVRKEIGPLATPDvvhwVDSLPKTRSGKI 586
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1050-1525 |
3.92e-28 |
|
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: 123.07 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTE------MDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPAD 1123
Cdd:cd17634 67 GDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGFAPE 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1124 RIAYMLEDSGATVGITdASTRARLGESscewVDL---AD--LEAEAESGDDITDTERNGS-------------------- 1178
Cdd:cd17634 147 AVAGRIIDSSSRLLIT-ADGGVRAGRS----VPLkknVDdaLNPNVTSVEHVIVLKRTGSdidwqegrdlwwrdliakas 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1179 -------VRLTNLAYLIYTSGSTGRPKAVGVSHTG-IVDFVNSLAKITTGTPEDepdtrILHVASpsfdasmfEMAWAIP 1250
Cdd:cd17634 222 pehqpeaMNAEDPLFILYTSGTTGKPKGVLHTTGGyLVYAATTMKYVFDYGPGD-----IYWCTA--------DVGWVTG 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1251 ----------AGHTLVI---APQADfAGDALATVLERDEVTDMIITPSVLATVDPERAQYV--------RNLATGGEACP 1309
Cdd:cd17634 289 hsyllygplaCGATTLLyegVPNWP-TPARMWQVVDKHGVNILYTAPTAIRALMAAGDDAIegtdrsslRILGSVGEPIN 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1310 PE----LVERWSERGRRIFNCYGPTEaTVWATRSRMTAGKPVTIG---KPVDGFTVRVLDGRLHEVPQGVVGELYLSTA- 1381
Cdd:cd17634 368 PEayewYWKKIGKEKCPVVDTWWQTE-TGGFMITPLPGAIELKAGsatRPVFGVQPAVVDNEGHPQPGGTEGNLVITDPw 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1382 -GLARGYLGRPGQTAVSFVADPFGepgarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQS 1460
Cdd:cd17634 447 pGQTRTLFGDHERFEQTYFSTFKG-----MYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEA 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 1461 VVVGVestRGGRKHTEVVAYLVAKPGATiDSAAVLDE----AAQHLAAHMVPSQAIVIDEIPLTPAGKL 1525
Cdd:cd17634 522 AVVGI---PHAIKGQAPYAYVVLNHGVE-PSPELYAElrnwVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1038-1532 |
4.36e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 122.16 E-value: 4.36e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1038 TLIDVLAQRDldPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVD 1117
Cdd:PRK06164 14 SLLDAHARAR--PDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVN 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1118 PAYPADRIAYMLEDSGATVGITDASTR-----ARLGESS-------------------------CEWVDLADLEAEAESG 1167
Cdd:PRK06164 92 TRYRSHEVAHILGRGRARWLVVWPGFKgidfaAILAAVPpdalpplraiavvddaadatpapapGARVQLFALPDPAPPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1168 DDItdtERNGSVRLTNLAYLiyTSGSTGRPKAVGVSHTGIVDFVNSLAKITTgtpeDEPDTRILHVASPSFDASMFEMAW 1247
Cdd:PRK06164 172 AAG---ERAADPDAGALLFT--TSGTTSGPKLVLHRQATLLRHARAIARAYG----YDPGAVLLAALPFCGVFGFSTLLG 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1248 AIPAGHTLVIAPQADFAgdALATVLERDEVTDMIITPSVLATV---DPERAQYVRNLATGGEACPP---ELVERWSERGR 1321
Cdd:PRK06164 243 ALAGGAPLVCEPVFDAA--RTARALRRHRVTHTFGNDEMLRRIldtAGERADFPSARLFGFASFAPalgELAALARARGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1322 RIFNCYGPTEatVWATRSRMTAGKPVTI-----GKPVDG-FTVRV---LDGRLheVPQGVVGELYLSTAGLARGYLGRPG 1392
Cdd:PRK06164 321 PLTGLYGSSE--VQALVALQPATDPVSVrieggGRPASPeARVRArdpQDGAL--LPDGESGEIEIRAPSLMRGYLDNPD 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1393 QTAVSFVADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVesTRGGR 1472
Cdd:PRK06164 397 ATARALTDDGY-------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGA--TRDGK 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 1473 khTEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAG---KLDRAALPE 1532
Cdd:PRK06164 468 --TVPVAFVIPTDGASPDEAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1039-1532 |
4.49e-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: 122.22 E-value: 4.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1039 LIDVLAQRDldPDHPALI-CD--GTEMDYD--EFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAY 1113
Cdd:cd05970 22 VVDAMAKEY--PDKLALVwCDdaGEERIFTfaELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1114 VPVDPAYPADRIAYMLEDSGATVGITDA------------------STRARLGESSCE-WVDLADLEAEAEsgDDITDTE 1174
Cdd:cd05970 100 IPATHQLTAKDIVYRIESADIKMIVAIAednipeeiekaapecpskPKLVWVGDPVPEgWIDFRKLIKNAS--PDFERPT 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1175 RNGSVRLTNLAYLIYTSGSTGRPKAVgvSHtgivDFVNSLAKITTGT--PEDEPDTRILHVASPSFDASM---FEMAWAi 1249
Cdd:cd05970 178 ANSYPCGEDILLVYFSSGTTGMPKMV--EH----DFTYPLGHIVTAKywQNVREGGLHLTVADTGWGKAVwgkIYGQWI- 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1250 pAGHTLVIAPQADFAGDALATVLERDEVTDMIITPSV---LATVDPERAQY--VRNLATGGEACPPELVERWSER-GRRI 1323
Cdd:cd05970 251 -AGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPTIyrfLIREDLSRYDLssLRYCTTAGEALNPEVFNTFKEKtGIKL 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1324 FNCYGPTEATVW-ATRSRMTAgKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTA-----GLARGYLGRPGQTAVS 1397
Cdd:cd05970 330 MEGFGQTETTLTiATFPWMEP-KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIRTSkgkpvGLFGGYYKDAEKTAEV 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1398 FvADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGV-ESTRGGRKHTE 1476
Cdd:cd05970 409 W-HDGY-------YHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVpDPIRGQVVKAT 480
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 1477 VVAYLVAKPGATIDSaAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:cd05970 481 IVLAKGYEPSEELKK-ELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEIRE 535
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1189-1527 |
6.91e-28 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 117.76 E-value: 6.91e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1189 YTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtrILHVASPSFDAsmFEMAWAIPA----GHTLVIaPQADFA 1264
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQD-----RLCIPVPLFHC--FGSVLGVLAclthGATMVF-PSPSFD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1265 GDALATVLERDEVTDMIITPSVLATV--DPERAQY----VRNLATGGEACPPELVERWSER--GRRIFNCYGPTEATVWA 1336
Cdd:cd05917 81 PLAVLEAIEKEKCTALHGVPTMFIAEleHPDFDKFdlssLRTGIMAGAPCPPELMKRVIEVmnMKDVTIAYGMTETSPVS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1337 TRSRMTAG---KPVTIGKPVDGFTVRVLDGRLHEVPQ-GVVGELYLSTAGLARGYLGRPGQTAVSFVADpfgepgaRMYA 1412
Cdd:cd05917 161 TQTRTDDSiekRVNTVGRIMPHTEAKIVDPEGGIVPPvGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD-------GWLH 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1413 TGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPGATIDSA 1492
Cdd:cd05917 234 TGDLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQVVGVPDERYGE---EVCAWIRLKEGAELTEE 310
|
330 340 350
....*....|....*....|....*....|....*
gi 1827387616 1493 AVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDR 1527
Cdd:cd05917 311 DIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQK 345
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
2560-2998 |
1.18e-27 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 121.36 E-value: 1.18e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2560 PATDPVTLAELFRAAARRAPDHVAV---VDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALaIGRS------AQLl 2630
Cdd:COG1022 6 DVPPADTLPDLLRRRAARFPDRVALrekEDGIWQSLTWAEFAERVRALAAGLLALGVKPGDRVAI-LSDNrpewviADL- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2631 tAIWAVaktGGAYVPIDPDYPAERVASMIEDSGAVLglsVLASG------------DLPGQEFEW------MRLDDDSVA 2692
Cdd:COG1022 84 -AILAA---GAVTVPIYPTSSAEEVAYILNDSGAKV---LFVEDqeqldkllevrdELPSLRHIVvldprgLRDDPRLLS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2693 -AEIAAVPAGPITDAE---RLGEVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVL-------- 2760
Cdd:COG1022 157 lDELLALGREVADPAEleaRRAAVKPDDLATIIYTSGTTGRPKGVMLTHRNLLSNARALLERLPLGPGDRTLsflplahv 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2761 ----------------GFAS-------------PSFDASV---LEYLLATVNE-----GTLA---YRPSEAVGGEVLERF 2800
Cdd:COG1022 237 fertvsyyalaagatvAFAEspdtlaedlrevkPTFMLAVprvWEKVYAGIQAkaeeaGGLKrklFRWALAVGRRYARAR 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2801 IAEHG------ATHTFLTPSVLStmdptAV-----PSLRVIAAGGEAVPqPIVDRWapateLHNL-------YGPTETTI 2862
Cdd:COG1022 317 LAGKSpslllrLKHALADKLVFS-----KLrealgGRLRFAVSGGAALG-PELARF-----FRALgipvlegYGLTETSP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2863 GITISsamRPGDpVRLG--G-PIGGVDLMVLDErlrpvpvgmpGELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrm 2939
Cdd:COG1022 386 VITVN---RPGD-NRIGtvGpPLPGVEVKIAED----------GEILVRGPNVMKGYYKNPEATAEAFDADGW------- 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2940 YRTGDVVRWTPDtdtGGLTLeyTGRSDDQVKLR-GLRIELGEIEAVLAEHDAVESAVVLG 2998
Cdd:COG1022 445 LHTGDIGELDED---GFLRI--TGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVG 499
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1045-1537 |
1.32e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 119.91 E-value: 1.32e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1045 QRDLDPDHPAL--ICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPA 1122
Cdd:PRK09088 4 HARLQPQRLAAvdLALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1123 DRIAYMLEDSGATVGITDASTRArlgeSSCEWVDLADLEAEAEsGDDITDTERNGSVRLTnlaYLIYTSGSTGRPKAVGV 1202
Cdd:PRK09088 84 SELDALLQDAEPRLLLGDDAVAA----GRTDVEDLAAFIASAD-ALEPADTPSIPPERVS---LILFTSGTSGQPKGVML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1203 SHTGIVDFVNSLAKITtgtpedepdtRILHVASPSFDASMFEMAWAIPA-------GHTLVIAPQADfAGDALATVLERD 1275
Cdd:PRK09088 156 SERNLQQTAHNFGVLG----------RVDAHSSFLCDAPMFHIIGLITSvrpvlavGGSILVSNGFE-PKRTLGRLGDPA 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1276 -EVTDMIITPSVLA------TVDPERAQYVRNLATGGEACPPELVERWSERGRRIFNCYGPTEA-TVW--ATRSRMTAGK 1345
Cdd:PRK09088 225 lGITHYFCVPQMAQafraqpGFDAAALRHLTALFTGGAPHAAEDILGWLDDGIPMVDGFGMSEAgTVFgmSVDCDVIRAK 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1346 PVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRVAKGGNL 1425
Cdd:PRK09088 305 AGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAFTGDGW-------FRTGDIARRDADGFF 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1426 EFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEV-VAYLVAKPGATIDSAAVLDEAAQHLAA 1504
Cdd:PRK09088 378 WVVDRKKDMFISGGENVYPAEIEAVLADHPGIRECAVVGMADAQWG----EVgYLAIVPADGAPLDLERIRSHLSTRLAK 453
|
490 500 510
....*....|....*....|....*....|...
gi 1827387616 1505 HMVPSQAIVIDEIPLTPAGKLDRAALPEPHAPE 1537
Cdd:PRK09088 454 YKVPKHLRLVDALPRTASGKLQKARLRDALAAG 486
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
4-466 |
1.48e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 120.38 E-value: 1.48e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGG-------HFVP--LDEQLPVDRARYMV------ 68
Cdd:PRK07798 32 AELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAvpvnvnyRYVEdeLRYLLDDSDAVALVyerefa 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 69 --------RTAGVRLVVVTSDGEAEARS----RFDDIVdvhvldisSPGDADLDeeefaGPTRPANAAFTLFTSGSTGRP 136
Cdd:PRK07798 112 prvaevlpRLPKLRTLVVVEDGSGNDLLpgavDYEDAL--------AAGSPERD-----FGERSPDDLYLLYTGGTTGMP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 137 KAVVITHR--------GIANRLAADIEQYDLTARDVFLYKAPITFDVSvreiflPIAIGATL------------VIAEPG 196
Cdd:PRK07798 179 KGVMWRQEdifrvllgGRDFATGEPIEDEEELAKRAAAGPGMRRFPAP------PLMHGAGQwaafaalfsgqtVVLLPD 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 197 RHGDPVHLADLIRRHGVTVIHFV------PaMLAAFNEvlgAGVGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQ 270
Cdd:PRK07798 253 VRFDADEVWRTIEREKVNVITIVgdamarP-LLDALEA---RGPYDLSSLFAIASGGALFSPSVKEALLELLPNVVLTDS 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 271 YGPAEASIVVTIhrvTQDDRVIPIGTP--TRRVSARVLDAALREVP--IGVPGELYLGGVqLARGYAGRPDLTAERF-VA 345
Cdd:PRK07798 329 IGSSETGFGGSG---TVAKGAVHTGGPrfTIGPRTVVLDEDGNPVEpgSGEIGWIARRGH-IPLGYYKDPEKTAETFpTI 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 346 DpfgepGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGPG---GQQLVGYL 422
Cdd:PRK07798 405 D-----GVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHPDV--ADALVVGVPDerwGQEVVAVV 477
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1827387616 423 AP---ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRR 466
Cdd:PRK07798 478 QLregARPDLAELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKADYR 524
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1184-1530 |
1.53e-27 |
|
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: 116.28 E-value: 1.53e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1184 LAYLIYTSGSTGRPKAVGVS---HTGIVDFVNSLakittgTPEDEPDTRILhvASPSFDASMFEMAWA-IPAGHTLVIAP 1259
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTaanLLASAAGLHSR------LGFGGGDSWLL--SLPLYHVGGLAILVRsLLAGAELVLLE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1260 QADfagdALATVLERDEVTDMIITPSVLATV-----DPERAQYVRNLATGGEACPPELVERWSERGRRIFNCYGPTEatv 1334
Cdd:cd17630 74 RNQ----ALAEDLAPPGVTHVSLVPTQLQRLldsgqGPAALKSLRAVLLGGAPIPPELLERAADRGIPLYTTYGMTE--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1335 waTRSRMTAGKPVTIGKPVDGftvRVLDGRlhEVPQGVVGELYLSTAGLARGYLGRPGQtavsfvaDPFGEPGarMYATG 1414
Cdd:cd17630 147 --TASQVATKRPDGFGRGGVG---VLLPGR--ELRIVEDGEIWVGGASLAMGYLRGQLV-------PEFNEDG--WFTTK 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1415 DLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGAtiDSAAV 1494
Cdd:cd17630 211 DLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEELGQR---PVAVIVGRGPA--DPAEL 285
|
330 340 350
....*....|....*....|....*....|....*.
gi 1827387616 1495 LDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd17630 286 RAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1183-1525 |
1.74e-27 |
|
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: 116.45 E-value: 1.74e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1183 NLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtRILhVASPSFDASMFEMAW--AIPAGHTLViaPQ 1260
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDD----RYL-IINPFFHTFGYKAGIvaCLLTGATVV--PV 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1261 ADFAGDALATVLERDEVTDMIITPSVLATV--DPERAQY----VRNLATGGEACPPELVERW-SERG-RRIFNCYGPTEA 1332
Cdd:cd17638 74 AVFDVDAILEAIERERITVLPGPPTLFQSLldHPGRKKFdlssLRAAVTGAATVPVELVRRMrSELGfETVLTAYGLTEA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1333 TVwATRSRmTAGKPVTI----GKPVDGFTVRVLDGrlhevpqgvvGELYLSTAGLARGYLGRPGQTAVSFVADPFgepga 1408
Cdd:cd17638 154 GV-ATMCR-PGDDAETVattcGRACPGFEVRIADD----------GEVLVRGYNVMQGYLDDPEATAEAIDADGW----- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1409 rmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEV-VAYLVAKPGA 1487
Cdd:cd17638 217 --LHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMG----EVgKAFVVARPGV 290
|
330 340 350
....*....|....*....|....*....|....*...
gi 1827387616 1488 TIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKL 1525
Cdd:cd17638 291 TLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
2576-3054 |
1.86e-27 |
|
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: 120.76 E-value: 1.86e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2576 RRAPDHVAVV----DGAGAR-LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDY 2650
Cdd:cd17634 64 RENGDRTAIIyegdDTSQSRtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIGAVHSVIFGGF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2651 PAERVASMIEDSGAVLglSVLASGDL-PGQEFEWMRLDDDsvAAEIAAVPAGPITDAERLG------------------- 2710
Cdd:cd17634 144 APEAVAGRIIDSSSRL--LITADGGVrAGRSVPLKKNVDD--ALNPNVTSVEHVIVLKRTGsdidwqegrdlwwrdliak 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2711 --------EVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDR---LNAGDnpVVLGFASPSF--DASVLEYLLA 2777
Cdd:cd17634 220 aspehqpeAMNAEDPLFILYTSGTTGKPKGVLHTTGGYLVYAATTMKYvfdYGPGD--IYWCTADVGWvtGHSYLLYGPL 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2778 TVNEGTLAY--RPSEAVGGEvLERFIAEHGATHTFLTPSVLSTM---DPTAV-----PSLRVIAAGGEAV-PQPivdrWA 2846
Cdd:cd17634 298 ACGATTLLYegVPNWPTPAR-MWQVVDKHGVNILYTAPTAIRALmaaGDDAIegtdrSSLRILGSVGEPInPEA----YE 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2847 PATE--------LHNLYGPTETTIGIT----ISSAMRPGDPVRlggPIGGVDLMVLDERLRPVPVGMPGELYVAGG--AL 2912
Cdd:cd17634 373 WYWKkigkekcpVVDTWWQTETGGFMItplpGAIELKAGSATR---PVFGVQPAVVDNEGHPQPGGTEGNLVITDPwpGQ 449
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2913 SRGYLDRSgltaERFTANpYGTAGQRMYRTGDVVRwtpdTDTGGLTLeYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVE 2992
Cdd:cd17634 450 TRTLFGDH----ERFEQT-YFSTFKGMYFSGDGAR----RDEDGYYW-ITGRSDDVINVAGHRLGTAEIESVLVAHPKVA 519
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 2993 SAVVLGVGGSV-ATALAAYIV----PVDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKL 3054
Cdd:cd17634 520 EAAVVGIPHAIkGQAPYAYVVlnhgVEPSPELYAELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1049-1530 |
1.90e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 119.32 E-value: 1.90e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1049 DPDHPALICDGTEMDYDEFetrtnAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYM 1128
Cdd:PRK07787 13 ADIADAVRIGGRVLSRSDL-----AGAATAVAERVAGARRVAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHI 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1129 LEDSGATvgitdastrARLGESSCEWVDLA----DLEAEAESGDDITDTErngsvrltNLAYLIYTSGSTGRPKAVGVSH 1204
Cdd:PRK07787 88 LADSGAQ---------AWLGPAPDDPAGLPhvpvRLHARSWHRYPEPDPD--------APALIVYTSGTTGPPKGVVLSR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1205 TGIVDFVNSLAKITTGTPED----------------------EPDTRILHVASPSFDAsmfeMAWAIPAGHTLVIApqad 1262
Cdd:PRK07787 151 RAIAADLDALAEAWQWTADDvlvhglplfhvhglvlgvlgplRIGNRFVHTGRPTPEA----YAQALSEGGTLYFG---- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1263 fagdaLATVLERdeVTDmiitpsvlatvDPERAQYV---RNLATGGEACPPELVERWSER-GRRIFNCYGPTEaTVWATR 1338
Cdd:PRK07787 223 -----VPTVWSR--IAA-----------DPEAARALrgaRLLVSGSAALPVPVFDRLAALtGHRPVERYGMTE-TLITLS 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1339 SRMTAG-KPVTIGKPVDGFTVRVLDGRLHEVPQGV--VGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGD 1415
Cdd:PRK07787 284 TRADGErRPGWVGLPLAGVETRLVDEDGGPVPHDGetVGELQVRGPTLFDGYLNRPDATAAAFTADGW-------FRTGD 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1416 LVRVAKGGNLEFAGR-ADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVakPGATIDSAAV 1494
Cdd:PRK07787 357 VAVVDPDGMHRIVGReSTDLIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDLGQR---IVAYVV--GADDVAADEL 431
|
490 500 510
....*....|....*....|....*....|....*.
gi 1827387616 1495 LDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK07787 432 IDFVAQQLSVHKRPREVRFVDALPRNAMGKVLKKQL 467
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
2140-2535 |
3.20e-27 |
|
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: 117.91 E-value: 3.20e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2140 VLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPSGAAVTVVPA-EVTVPWSVIDLRAEDaasLDSRVEEVLATertnP 2218
Cdd:cd19540 29 ALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPAaEARPDLTVVDVTEDE---LAARLAEAARR----G 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2219 FDMAKPPLIRVVLVEHGDGAE-LVVTNHHLLIDGWSSPLVLADLLSLYATGqtftgslpgTSGR---------DFADHA- 2287
Cdd:cd19540 102 FDLTAELPLRARLFRLGPDEHvLVLVVHHIAADGWSMAPLARDLATAYAAR---------RAGRapdwaplpvQYADYAl 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2288 --RAV-ATADVEAGIAA-----WREVLAPVTEPtLVAPGHEP-SADAPPR--DHQFSIDVKVTERLEALARNNSTTMATV 2356
Cdd:cd19540 173 wqRELlGDEDDPDSLAArqlayWRETLAGLPEE-LELPTDRPrPAVASYRggTVEFTIDAELHARLAALAREHGATLFMV 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2357 VQFAWAMFLSRLTGTRTVTFAETVSGRspDIEGMESMVGMFINTIPAVVDVNPDATVVDVLTAVQNDKVKVLDHQQIGLP 2436
Cdd:cd19540 252 LHAALAVLLSRLGAGDDIPIGTPVAGR--GDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFAHQDVPFE 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2437 RLVAQ------TGLPALFDTLAVYESFPVNVDSVAGIDAsSAGGLKLVGAKtsdathYPLNLS------ASRRGAELALK 2504
Cdd:cd19540 330 RLVEAlnpprsTARHPLFQVMLAFQNTAAATLELPGLTV-EPVPVDTGVAK------FDLSFTlterrdADGAPAGLTGE 402
|
410 420 430
....*....|....*....|....*....|.
gi 1827387616 2505 LKYLPTAFAPEQVAVFADVLTGLLGAIADHP 2535
Cdd:cd19540 403 LEYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1046-1530 |
3.85e-27 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 120.06 E-value: 3.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1046 RDLDPDHPALICDGTEMDYDEFETRTNA-----IARA--LLAR-GVSPEDVVAVGMERSIGSVLATWGVIKSGAAyVPVD 1117
Cdd:PRK07529 35 AARHPDAPALSFLLDADPLDRPETWTYAelladVTRTanLLHSlGVGPGDVVAFLLPNLPETHFALWGGEAAGIA-NPIN 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1118 PAYPADRIAYMLEDSGATVGITDAST-RARLGESSCE------------WVDLA-----------------------DLE 1161
Cdd:PRK07529 114 PLLEPEQIAELLRAAGAKVLVTLGPFpGTDIWQKVAEvlaalpelrtvvEVDLArylpgpkrlavplirrkaharilDFD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1162 AE--AESGDDITDTERNGSVRLtnlAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtrILHVASPSF- 1238
Cdd:PRK07529 194 AElaRQPGDRLFSGRPIGPDDV---AAYFHTGGTTGMPKLAQHTHGNEVANAWLGALLLGLGPGD-----TVFCGLPLFh 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1239 -DASMFEMAWAIPAGHTLVIAPQADFAGDALA----TVLERDEVTDMIITPSVLAT-----VDPERAQYVRNLATGGEAC 1308
Cdd:PRK07529 266 vNALLVTGLAPLARGAHVVLATPQGYRGPGVIanfwKIVERYRINFLSGVPTVYAAllqvpVDGHDISSLRYALCGAAPL 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1309 PPELVERWSER-GRRIFNCYGPTEATVWATRS-RMTAGKPVTIGKPVDGFTVRVL----DGR-LHEVPQGVVGELYLSTA 1381
Cdd:PRK07529 346 PVEVFRRFEAAtGVRIVEGYGLTEATCVSSVNpPDGERRIGSVGLRLPYQRVRVVilddAGRyLRDCAVDEVGVLCIAGP 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1382 GLARGYLgRPGQTAVSFVADpfgepgaRMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSV 1461
Cdd:PRK07529 426 NVFSGYL-EAAHNKGLWLED-------GWLNTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAA 497
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 1462 VVGVESTRGGrkhtEV-VAYLVAKPGATIDSAAVLDEAAQHL---AAhmVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK07529 498 AVGRPDAHAG----ELpVAYVQLKPGASATEAELLAFARDHIaerAA--VPKHVRILDALPKTAVGKIFKPAL 564
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
4-463 |
5.44e-27 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 118.73 E-value: 5.44e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRlVVVTSDGE 83
Cdd:PRK07786 46 RELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLVSDCGAH-VVVTEAAL 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 AEARSRFDDIVDVHVLDISSPGDAD---LDEEEFAGPTRPANA---------AFTLFTSGSTGRPKAVVITHRGIANRLA 151
Cdd:PRK07786 125 APVATAVRDIVPLLSTVVVAGGSSDdsvLGYEDLLAEAGPAHApvdipndspALIMYTSGTTGRPKGAVLTHANLTGQAM 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 152 ADIEQYDL-TARDVFLYKAPITFDVSVREIFLPIAIGATLVIaEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVL 230
Cdd:PRK07786 205 TCLRTNGAdINSDVGFVGVPLFHIAGIGSMLPGLLLGAPTVI-YPLGAFDPGQLLDVLEAEKVTGIFLVPAQWQAVCAEQ 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 231 GAGVGELtSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIhrVTQDDRVIPIGT---PTRRVSARVLD 307
Cdd:PRK07786 284 QARPRDL-ALRVLSWGAAPASDTLLRQMAATFPEAQILAAFGQTEMSPVTCM--LLGEDAIRKLGSvgkVIPTVAARVVD 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 308 AALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlyRTGDRARWNRDGEIEYLGRTDFQVKLRGQRL 387
Cdd:PRK07786 361 ENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWF--------HSGDLVRQDEEGYVWVVDRKKDMIISGGENI 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 388 ELGEVEAALAAAPGVlhAAAAVVDGPG---GQQLVGYLAP----ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRS 460
Cdd:PRK07786 433 YCAEVENVLASHPDI--VEVAVIGRADekwGEVPVAVAAVrnddAALTLEDLAEFLTDRLARYKHPKALEIVDALPRNPA 510
|
...
gi 1827387616 461 GKV 463
Cdd:PRK07786 511 GKV 513
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
124-468 |
1.01e-26 |
|
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) synthetase (also known as O-succinylbenzoic acid CoA ligase) that belongs to the ANL superfamily and catalyzes the ligation of CoA to o-succinylbenzoate (OSB). It includes MenE in the bacterial menaquinone biosynthesis pathway which is a promising target for the development of novel antibacterial agents. MenE catalyzes CoA ligation via an acyl-adenylate intermediate; tight-binding inhibitors of MenE based on stable acyl-sulfonyladenosine analogs of this intermediate provide a pathway toward the development of optimized MenE inhibitors.
Pssm-ID: 341285 [Multi-domain] Cd Length: 325 Bit Score: 113.97 E-value: 1.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 124 AFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPItFDVS-VREIFLPIAIGATLVIAEPGRhgdpv 202
Cdd:cd17630 3 ATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGDSWLLSLPL-YHVGgLAILVRSLLAGAELVLLERNQ----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 203 hlADLIRRH--GVTVIHFVPAMLAafnEVL--GAGVGELTSLRLIQTGGEALTPPVARDLMVRlpGTRLQNQYGPAEASI 278
Cdd:cd17630 77 --ALAEDLAppGVTHVSLVPTQLQ---RLLdsGQGPAALKSLRAVLLGGAPIPPELLERAADR--GIPLYTTYGMTETAS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 279 VVTIHRVtqddrvipiGTPTRRVSARVLDAalREVPIGVPGELYLGGVQLARGYAGRPdltaerfVADPFGEPGarLYRT 358
Cdd:cd17630 150 QVATKRP---------DGFGRGGVGVLLPG--RELRIVEDGEIWVGGASLAMGYLRGQ-------LVPEFNEDG--WFTT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 359 GDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLhaAAAVVDGPG---GQQLVGYLAPAD-VDVDTVAA 434
Cdd:cd17630 210 KDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVR--DAFVVGVPDeelGQRPVAVIVGRGpADPAELRA 287
|
330 340 350
....*....|....*....|....*....|....
gi 1827387616 435 TTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd17630 288 WLKDKLARFKLPKRIYPVPELPRTGGGKVDRRAL 321
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
2574-2999 |
1.05e-26 |
|
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: 117.34 E-value: 1.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2574 AARRAPDHVAVVDGA-GARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPA 2652
Cdd:cd05904 14 FASAHPSRPALIDAAtGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTTANPLSTP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2653 ERVASMIEDSGAVLGLSV------LASGDLP-----GQEFEWMRLDDDSVAAEIAAVPAGPITDAErlgevTAANLayvi 2721
Cdd:cd05904 94 AEIAKQVKDSGAKLAFTTaelaekLASLALPvvlldSAEFDSLSFSDLLFEADEAEPPVVVIKQDD-----VAALL---- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2722 YTSGSTGRPKGVAVTHSGL-ANFARQESDRLNAGDNPVVLGFASPSFDAsvleYLLATVNEGTLAYRpSEAVggeVLERF 2800
Cdd:cd05904 165 YSSGTTGRSKGVMLTHRNLiAMVAQFVAGEGSNSDSEDVFLCVLPMFHI----YGLSSFALGLLRLG-ATVV---VMPRF 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2801 --------IAEHGATHTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRWA---PATELHNLYGPTETTiG 2863
Cdd:cd05904 237 dleellaaIERYKVTHLPVVPPIVLALvkspivDKYDLSSLRQIMSGAAPLGKELIEAFRakfPNVDLGQGYGMTEST-G 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2864 ITISSAMRPGDPVRLGGpIG----GVDLMVLD-ERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTanpygtaGQR 2938
Cdd:cd05904 316 VVAMCFAPEKDRAKYGS-VGrlvpNVEAKIVDpETGESLPPNQTGELWIRGPSIMKGYLNNPEATAATID-------KEG 387
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 2939 MYRTGDVVRWtpdtDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV 2999
Cdd:cd05904 388 WLHTGDLCYI----DEDGY-LFIVDRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPY 443
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
2592-3059 |
1.22e-26 |
|
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: 115.52 E-value: 1.22e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2592 LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLglsvl 2671
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL----- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2672 asgdlpgqefewmrlddDSVAAeiaavpagpitdaerlgevtaanlayVIYTSGSTGRPKGVAVTHSGLANFARQESDRL 2751
Cdd:cd05912 77 -----------------DDIAT--------------------------IMYTSGTTGKPKGVQQTFGNHWWSAIGSALNL 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2752 NAGDNPVVLGfASPSFDASVLEYLLATVNEGTLAYrpseavggeVLERF--------IAEHGATHTFLTPSVLSTM---D 2820
Cdd:cd05912 114 GLTEDDNWLC-ALPLFHISGLSILMRSVIYGMTVY---------LVDKFdaeqvlhlINSGKVTIISVVPTMLQRLleiL 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2821 PTAVP-SLRVIAAGGEAVPQPIVD----RWAPateLHNLYGPTETTIGI-TISSAMRPGDPVRLGGPIGGVDLMVLDERL 2894
Cdd:cd05912 184 GEGYPnNLRCILLGGGPAPKPLLEqckeKGIP---VYQSYGMTETCSQIvTLSPEDALNKIGSAGKPLFPVELKIEDDGQ 260
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2895 RPvpvGMPGELYVAGGALSRGYLDRSGLTAERFtANPYgtagqrmYRTGDVvrwtPDTDTGGLTLEYTGRSDdqvklrgL 2974
Cdd:cd05912 261 PP---YEVGEILLKGPNVTKGYLNRPDATEESF-ENGW-------FKTGDI----GYLDEEGFLYVLDRRSD-------L 318
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2975 RIELGE------IEAVLAEHDAVESAVVLGVG----GSVATAlaaYIVpVDGAVEVSELKAFAGGRLPAYMVPSSFTVID 3044
Cdd:cd05912 319 IISGGEniypaeIEEVLLSHPAIKEAGVVGIPddkwGQVPVA---FVV-SERPISEEELIAYCSEKLAKYKVPKKIYFVD 394
|
490
....*....|....*
gi 1827387616 3045 ELPLTPVGKLDKRAL 3059
Cdd:cd05912 395 ELPRTASGKLLRHEL 409
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1-468 |
1.23e-26 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 116.08 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVts 80
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgEAEARSRFDDIVDVHvldisspgdadldeeefagptrpanaaftLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd05973 79 --DAANRHKLDSDPFVM-----------------------------MFTSGTTGLPKGVPVPLRALAAFGAYLRDAVDLR 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVF-----------LYKApitfdvsvreIFLPIAIGATLVIAEPGRHGDPVHlaDLIRRHGVTVIHFVPAmlaAFNEV 229
Cdd:cd05973 128 PEDSFwnaadpgwaygLYYA----------ITGPLALGHPTILLEGGFSVESTW--RVIERLGVTNLAGSPT---AYRLL 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 230 LGAGVGELT----SLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTIHRvtQDDRVIPIGT-----PTRR 300
Cdd:cd05973 193 MAAGAEVPArpkgRLRRVSSAGEPLTPEVIRWFDAAL-GVPIHDHYGQTELGMVLANHH--ALEHPVHAGSagramPGWR 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 301 VSarVLDAALREVPIGVPGelylggvQLARGYAGRPDLTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQV 380
Cdd:cd05973 270 VA--VLDDDGDELGPGEPG-------RLAIDIANSPLMWFRGYQLPDTPAIDGGYYLTGDTVEFDPDGSFSFIGRADDVI 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 381 KLRGQRLELGEVEAALAAAPGVLHAAAAVVDGPGGQQLVG---YLAPADVDVDTVAATTAELLPEYMRPSAWVR----LD 453
Cdd:cd05973 341 TMSGYRIGPFDVESALIEHPAVAEAAVIGVPDPERTEVVKafvVLRGGHEGTPALADELQLHVKKRLSAHAYPRtihfVD 420
|
490
....*....|....*
gi 1827387616 454 AMPLSRSGKVDRRLL 468
Cdd:cd05973 421 ELPKTPSGKIQRFLL 435
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
128-465 |
1.46e-26 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 113.91 E-value: 1.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 128 FTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPI--TFDvSVREIFLPIAIGATLVIAEPGRHGDPVHLA 205
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNNGYFIGERLGLTEQDRLCIPVPLfhCFG-SVLGVLACLTHGATMVFPSPSFDPLAVLEA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 206 dlIRRHGVTVIHFVPAMlaaFNEVLGA---GVGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTI 282
Cdd:cd05917 88 --IEKEKCTALHGVPTM---FIAELEHpdfDKFDLSSLRTGIMAGAPCPPELMKRVIEVMNMKDVTIAYGMTETSPVSTQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 283 HRV--TQDDRVIPIGTPTRRVSARVLDAALREVP-IGVPGELYLGGVQLARGYAGRPDLTAERFVADpfgepgaRLYRTG 359
Cdd:cd05917 163 TRTddSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTAEAIDGD-------GWLHTG 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 360 DRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAA-AAVVDGPGGQQLVGYLAP---ADVDVDTVAAT 435
Cdd:cd05917 236 DLAVMDEDGYCRIVGRIKDMIIRGGENIYPREIEEFLHTHPKVSDVQvVGVPDERYGEEVCAWIRLkegAELTEEDIKAY 315
|
330 340 350
....*....|....*....|....*....|.
gi 1827387616 436 TAELLPEYMRPsAWVR-LDAMPLSRSGKVDR 465
Cdd:cd05917 316 CKGKIAHYKVP-RYVFfVDEFPLTVSGKIQK 345
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1048-1530 |
1.82e-26 |
|
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: 116.32 E-value: 1.82e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1048 LDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPaDRIAY 1127
Cdd:cd05929 4 RDLDRAQVFHQRRLLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAP-RAEAC 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1128 M--------LEDSGATVGitdastrarlgesSCEWVDLADLEAEAESGDDITDTERNGSvrltnlaYLIYTSGSTGRPKA 1199
Cdd:cd05929 83 AiieikaaaLVCGLFTGG-------------GALDGLEDYEAAEGGSPETPIEDEAAGW-------KMLYSGGTTGRPKG 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1200 VGVSHTGIVDFVNSLAKITTGTPEDEpDTRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADfAGDALATVlERDEVTD 1279
Cdd:cd05929 143 IKRGLPGGPPDNDTLMAAALGFGPGA-DSVYLSPAPLYHAAPFRWSMTALFMGGTLVLMEKFD-PEEFLRLI-ERYRVTF 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1280 MIITPS----VLATVDPERAQY----VRNLATGGEACPPELVERWSE-RGRRIFNCYGPTEA--------TVWATRsrmt 1342
Cdd:cd05929 220 AQFVPTmfvrLLKLPEAVRNAYdlssLKRVIHAAAPCPPWVKEQWIDwGGPIIWEYYGGTEGqgltiingEEWLTH---- 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1343 agkPVTIGKPVDGfTVRVLDGRLHEVPQGVVGELYLSTAGlARGYLGRPGQTAVSFVADPFGepgarmyATGDLVRVAKG 1422
Cdd:cd05929 296 ---PGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWS-------TLGDVGYLDED 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1423 GNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPGA---TIDSAAVLDEAA 1499
Cdd:cd05929 364 GYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEELGQ---RVHAVVQPAPGAdagTALAEELIAFLR 440
|
490 500 510
....*....|....*....|....*....|.
gi 1827387616 1500 QHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd05929 441 DRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
2589-3059 |
1.91e-26 |
|
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: 115.65 E-value: 1.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2589 GARLTYRELDEASDRLARWLIGRGVG-PERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDsgavlg 2667
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIvPGNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDK------ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2668 lsvlasgdlpgqefewmrldddsvAAEIAAVPAGPITDAErlgevtaaNLAYVIYTSGSTGRPKGVAVTHSGLANFAR-- 2745
Cdd:cd05958 82 ------------------------ARITVALCAHALTASD--------DICILAFTSGTTGAPKATMHFHRDPLASADry 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2746 -------QESDRLnAGDNPVVLGFASpsfdASVLEYLLAtVNEGTLAYrpSEAVGGEVLErFIAEHGATHTFLTPSVLST 2818
Cdd:cd05958 130 avnvlrlREDDRF-VGSPPLAFTFGL----GGVLLFPFG-VGASGVLL--EEATPDLLLS-AIARYKPTVLFTAPTAYRA 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2819 M---DPTAVP---SLRVIAAGGEAVPQPIVDRWAPAT--ELHNLYGPTETtIGITISSamRPGD--PVRLGGPIGGVDLM 2888
Cdd:cd05958 201 MlahPDAAGPdlsSLRKCVSAGEALPAALHRAWKEATgiPIIDGIGSTEM-FHIFISA--RPGDarPGATGKPVPGYEAK 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2889 VLDERLRPVPVGMPGELYVAGGALSRGYLDRSgltAERFTANPYGTAGQRMYRTGDVVRWtpdtdtggltleYTGRSDDQ 2968
Cdd:cd05958 278 VVDDEGNPVPDGTIGRLAVRGPTGCRYLADKR---QRTYVQGGWNITGDTYSRDPDGYFR------------HQGRSDDM 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2969 VKLRGLRIELGEIEAVLAEHDAVESAVVLGV----GGSVATalaAYIVP----VDGAVEVSELKAFAGGRLPAYMVPSSF 3040
Cdd:cd05958 343 IVSGGYNIAPPEVEDVLLQHPAVAECAVVGHpdesRGVVVK---AFVVLrpgvIPGPVLARELQDHAKAHIAPYKYPRAI 419
|
490
....*....|....*....
gi 1827387616 3041 TVIDELPLTPVGKLDKRAL 3059
Cdd:cd05958 420 EFVTELPRTATGKLQRFAL 438
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
2560-3059 |
3.19e-26 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 116.66 E-value: 3.19e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2560 PATDPVTLAELFRAAARRAPDHVAVVdGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKT 2639
Cdd:PRK07059 18 DASQYPSLADLLEESFRQYADRPAFI-CMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2640 GGAYVPIDPDYPAERVASMIEDSGA---------------VLG------LSVLASGDLPGQEFEWMRLDDDSVAAeiaAV 2698
Cdd:PRK07059 97 GYVVVNVNPLYTPRELEHQLKDSGAeaivvlenfattvqqVLAktavkhVVVASMGDLLGFKGHIVNFVVRRVKK---MV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2699 PAGPITDAERLGEVTAA--------------NLAYVIYTSGSTGRPKGVAVTHSG-LANFARQES---DRLNAGDNPVVL 2760
Cdd:PRK07059 174 PAWSLPGHVRFNDALAEgarqtfkpvklgpdDVAFLQYTGGTTGVSKGATLLHRNiVANVLQMEAwlqPAFEKKPRPDQL 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2761 GF--ASPSFD--ASVLEYLLATVNEGT--LAYRPSEAVGgevlerFIAEHG--ATHTF-----LTPSVLSTMDPTAV--P 2825
Cdd:PRK07059 254 NFvcALPLYHifALTVCGLLGMRTGGRniLIPNPRDIPG------FIKELKkyQVHIFpavntLYNALLNNPDFDKLdfS 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2826 SLRVIAAGGEAVPQPIVDRWAPAT--ELHNLYGPTETTIGITISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPG 2903
Cdd:PRK07059 328 KLIVANGGGMAVQRPVAERWLEMTgcPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPG 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2904 ELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVRWTPDtdtgGLTlEYTGRSDDQVKLRGLRIELGEIEA 2983
Cdd:PRK07059 408 EICIRGPQVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDER----GYT-KIVDRKKDMILVSGFNVYPNEIEE 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 2984 VLAEHDAVESAVVLGV-GGSVATALAAYIVPVDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK07059 476 VVASHPGVLEVAAVGVpDEHSGEAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
4-468 |
4.01e-26 |
|
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: 113.98 E-value: 4.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLvvvtsdge 83
Cdd:cd05912 5 AELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL-------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 aearsrfDDIvdvhvldisspgdadldeeefagptrpanaAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARD 163
Cdd:cd05912 77 -------DDI------------------------------ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALNLGLTEDD 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 164 VFLYKAPItFDVSVREIFLPIAIGATLVIAEPgrHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGEltSLRLI 243
Cdd:cd05912 120 NWLCALPL-FHISGLSILMRSVIYGMTVYLVD--KFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPN--NLRCI 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 244 QTGGEALTPPVARDLMVRlpGTRLQNQYGPAE-ASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAalrEVPIGVPGELY 322
Cdd:cd05912 195 LLGGGPAPKPLLEQCKEK--GIPVYQSYGMTEtCSQIVTLSPEDALNKIGSAGKPLFPVELKIEDD---GQPPYEVGEIL 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 323 LGGVQLARGYAGRPDLTAERFVADPFgepgarlyRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGV 402
Cdd:cd05912 270 LKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVLLSHPAI 341
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 403 lhAAAAVVDGPG---GQQLVGYL-APADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd05912 342 --KEAGVVGIPDdkwGQVPVAFVvSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1-470 |
6.03e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.96 E-value: 6.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLAREL-TALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVT 79
Cdd:PRK06839 28 MTYKQLHEYVSKVAAYLiYELNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLTENELIFQLKDSGTTVLFVE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 80 SDGEAEARSRFDDIVDVHVLDISSPG---DADLDEEEFAGPTRPAnaaFTLFTSGSTGRPKAVVITHRGIANRLAADIEQ 156
Cdd:PRK06839 108 KTFQNMALSMQKVSYVQRVISITSLKeieDRKIDNFVEKNESASF---IICYTSGTTGKPKGAVLTQENMFWNALNNTFA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 157 YDLTARDVFLYKAPItFDVSVREIFLPIAIGATLVIAEPGRHgDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGE 236
Cdd:PRK06839 185 IDLTMHDRSIVLLPL-FHIGGIGLFAFPTLFAGGVIIVPRKF-EPTKALSMIEKHKVTVVMGVPTIHQALINCSKFETTN 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 237 LTSLRLIQTGGEALTPPVARDLMVRlpGTRLQNQYGPAEASivVTIHRVTQDD---RVIPIGTPTRRVSARVLDAALREV 313
Cdd:PRK06839 263 LQSVRWFYNGGAPCPEELMREFIDR--GFLFGQGFGMTETS--PTVFMLSEEDarrKVGSIGKPVLFCDYELIDENKNKV 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 314 PIGVPGELYLGGVQLARGYAGRPDLTAERfVADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVE 393
Cdd:PRK06839 339 EVGEVGELLIRGPNVMKEYWNRPDATEET-IQDGW-------LCTGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVE 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 394 AALAAAPGVLHAAAAVVDGPG-GQQLVGYLAP---ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLP 469
Cdd:PRK06839 411 QVINKLSDVYEVAVVGRQHVKwGEIPIAFIVKkssSVLIEKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLV 490
|
.
gi 1827387616 470 E 470
Cdd:PRK06839 491 N 491
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1074-1530 |
6.33e-26 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 117.05 E-value: 6.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1074 IARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDASTRARLGESSCe 1153
Cdd:PRK06060 43 LGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVTSDALRDRFQPSRV- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1154 wVDLADLEAEAESGDDiTDTERNGSvrlTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLA-KITTGTPEDEPdtriLH 1232
Cdd:PRK06060 122 -AEAAELMSEAARVAP-GGYEPMGG---DALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTPEDTG----LC 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1233 VASPSFDASMFEMAW-AIPAGHTLVIAPqADFAGDALATVLERDEVTDMIITPSVLATV----DPERAQYVRNLATGGEA 1307
Cdd:PRK06060 193 SARMYFAYGLGNSVWfPLATGGSAVINS-APVTPEAAAILSARFGPSVLYGVPNFFARVidscSPDSFRSLRCVVSAGEA 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1308 CPPELVERWSE--RGRRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLAR 1385
Cdd:PRK06060 272 LELGLAERLMEffGGIPILDGIGSTEVGQTFVSNRVDEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAK 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1386 GYLGRPgqtavsfvaDPFGEPGARMyATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGV 1465
Cdd:PRK06060 352 GYWNRP---------DSPVANEGWL-DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAVVAV 421
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 1466 ESTRGGrkhTEVVAYLVAKPGATIDSAAVLD---EAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK06060 422 RESTGA---STLQAFLVATSGATIDGSVMRDlhrGLLNRLSAFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
2573-3061 |
8.43e-26 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 114.57 E-value: 8.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2573 AAARRAPDHVAVVdGAGARLTYRELDEASDRLARWLIGR-GVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYP 2651
Cdd:PRK06839 10 KRAYLHPDRIAII-TEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2652 AERVASMIEDSGAVLglsVLASgdlpgQEFEWMRLD---DDSVAAEIAAVPAGPITDAERLG-EVTAANLAYVI-YTSGS 2726
Cdd:PRK06839 89 ENELIFQLKDSGTTV---LFVE-----KTFQNMALSmqkVSYVQRVISITSLKEIEDRKIDNfVEKNESASFIIcYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2727 TGRPKGVAVThsglanfarQESDRLNAGDNPVVLGFASPsfDASVLEYLLATVNEGTLAYRPSEAVGGEVLE-------- 2798
Cdd:PRK06839 161 TGKPKGAVLT---------QENMFWNALNNTFAIDLTMH--DRSIVLLPLFHIGGIGLFAFPTLFAGGVIIVprkfeptk 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2799 --RFIAEHGATHTFLTPSV------LSTMDPTAVPSLRVIAAGGEAVPQPIV----DRWAPateLHNLYGPTETTIGITI 2866
Cdd:PRK06839 230 alSMIEKHKVTVVMGVPTIhqalinCSKFETTNLQSVRWFYNGGAPCPEELMrefiDRGFL---FGQGFGMTETSPTVFM 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2867 SS----AMRPGDpvrLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAErftanpygTAGQRMYRT 2942
Cdd:PRK06839 307 LSeedaRRKVGS---IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEE--------TIQDGWLCT 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2943 GDVVRWTPDtdtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG----GSVATalaAYIVPVDGAV 3018
Cdd:PRK06839 376 GDLARVDED---GFVYI--VGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQhvkwGEIPI---AFIVKKSSSV 447
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1827387616 3019 EV-SELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPE 3061
Cdd:PRK06839 448 LIeKDVIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVN 491
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
2586-3059 |
9.46e-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: 114.35 E-value: 9.46e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2586 DGAGARLTYRELDEASDRLARwLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGgaYVPIDPDYPA--ERVASMIEDSG 2663
Cdd:cd05909 2 DTLGTSLTYRKLLTGAIALAR-KLAKMTKEGENVGVMLPPSAGGALANFALALSG--KVPVMLNYTAglRELRACIKLAG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2664 AVlglSVLAS------GDLPG-----QEFEWMRLDD----DSVAAEIAAVPAGPITDAE---RLGEVT--AANLAYVIYT 2723
Cdd:cd05909 79 IK---TVLTSkqfiekLKLHHlfdveYDARIVYLEDlrakISKADKCKAFLAGKFPPKWllrIFGVAPvqPDDPAVILFT 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2724 SGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASP--SFDASVLeyLLATVNEGTLAYRPSEAVGGEVLERFI 2801
Cdd:cd05909 156 SGSEGLPKGVVLSHKNLLANVEQITAIFDPNPEDVVFGALPFfhSFGLTGC--LWLPLLSGIKVVFHPNPLDYKKIPELI 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2802 AEHGATHTFLTPSVLS----TMDPTAVPSLRVIAAGGEAVPQPIVDRWAP--ATELHNLYGPTETTIGITISSAMRPGDP 2875
Cdd:cd05909 234 YDKKATILLGTPTFLRgyarAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEkfGIRILEGYGTTECSPVISVNTPQSPNKE 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2876 VRLGGPIGGVDLMVLD-ERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFtanpygtaGQRMYRTGDVVRWTPDtdt 2954
Cdd:cd05909 314 GTVGRPLPGMEVKIVSvETHEEVPIGEGGLLLVRGPNVMLGYLNEPELTSFAF--------GDGWYDTGDIGKIDGE--- 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2955 GGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEH--DAVESAVVLGVGGSVATALAAYIVPVDGavEVSELKAFA-GGRL 3031
Cdd:cd05909 383 GFLTI--TGRLSRFAKIAGEMVSLEAIEDILSEIlpEDNEVAVVSVPDGRKGEKIVLLTTTTDT--DPSSLNDILkNAGI 458
|
490 500
....*....|....*....|....*...
gi 1827387616 3032 PAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05909 459 SNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1050-1529 |
1.16e-25 |
|
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: 114.64 E-value: 1.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPAL--ICDGTEMD----YDEFETRTNAIARALLARGvSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPV---DPAY 1120
Cdd:cd05931 7 PDRPAYtfLDDEGGREetltYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLpppTPGR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1121 PADRIAYMLEDSGATVGITDASTRARLGE--SSCEWVDLADLEAEAESGDDITDTERNGSVRLTNLAYLIYTSGSTGRPK 1198
Cdd:cd05931 86 HAERLAAILADAGPRVVLTTAAALAAVRAfaASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGSTGTPK 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1199 AVGVSHTGIVDFVNSLAKITTGTPEDepdtrilHVAS--PSF-DASMFeMAWAIPA--GHTLVIAPQADFAGD------- 1266
Cdd:cd05931 166 GVVVTHRNLLANVRQIRRAYGLDPGD-------VVVSwlPLYhDMGLI-GGLLTPLysGGPSVLMSPAAFLRRplrwlrl 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1267 --------------ALATVLERdevtdmiITPSVLATVDPERaqyVRNLATGGEACPPELVERWSERGRR-------IFN 1325
Cdd:cd05931 238 isryratisaapnfAYDLCVRR-------VRDEDLEGLDLSS---WRVALNGAEPVRPATLRRFAEAFAPfgfrpeaFRP 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1326 CYGPTEATVWATRSRMTAGKPVTI--------------------------GKPVDGFTVRVLD-GRLHEVPQGVVGELYL 1378
Cdd:cd05931 308 SYGLAEATLFVSGGPPGTGPVVLRvdrdalagravavaaddpaarelvscGRPLPDQEVRIVDpETGRELPDGEVGEIWV 387
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1379 STAGLARGYLGRPGQTAVSFVADPfGEPGARMYATGDLVRVAkGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVA 1458
Cdd:cd05931 388 RGPSVASGYWGRPEATAETFGALA-ATDEGGWLRTGDLGFLH-DGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPAL 465
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 1459 QSVVVGVESTRGGRKHTEVVAYLVAKPGATIDSAAVLDEAAQHLA-AHMVPSQAIVI---DEIPLTPAGKLDRAA 1529
Cdd:cd05931 466 RPGCVAAFSVPDDGEERLVVVAEVERGADPADLAAIAAAIRAAVArEHGVAPADVVLvrpGSIPRTSSGKIQRRA 540
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
2-474 |
1.38e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 114.67 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLAREL-TALGV--GAEVAVGIQidRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVV 78
Cdd:PRK08314 37 SYRELLEEAERLAGYLqQECGVrkGDRVLLYMQ--NSPQFVIAYYAILRANAVVVPVNPMNREEELAHYVTDSGARVAIV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 79 TSD---------GEAEAR----SRFDDIVDVH--------------VLDISSPGDADLDEEEFAG-PTRPANA-----AF 125
Cdd:PRK08314 115 GSElapkvapavGNLRLRhvivAQYSDYLPAEpeiavpawlraeppLQALAPGGVVAWKEALAAGlAPPPHTAgpddlAV 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 126 TLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPItFDVS--VREIFLPIAIGATLVIAEpgrHGDPVH 203
Cdd:PRK08314 195 LPYTSGTTGVPKGCMHTHRTVMANAVGSVLWSNSTPESVVLAVLPL-FHVTgmVHSMNAPIYAGATVVLMP---RWDREA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 204 LADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMvRLPGTRLQNQYGPAEaSIVVTIH 283
Cdd:PRK08314 271 AARLIERYRVTHWTNIPTMVVDFLASPGLAERDLSSLRYIGGGGAAMPEAVAERLK-ELTGLDYVEGYGLTE-TMAQTHS 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 284 RVTQDDRVIPIGTPTRRVSARVLDAA-LREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVA-DpfgepGARLYRTGDR 361
Cdd:PRK08314 349 NPPDRPKLQCLGIPTFGVDARVIDPEtLEELPPGEVGEIVVHGPQVFKGYWNRPEATAEAFIEiD-----GKRFFRTGDL 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 362 ARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAPADvdvDTVAATTAELL 440
Cdd:PRK08314 424 GRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACViATPDPRRGETVKAVVVLRP---EARGKTTEEEI 500
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1827387616 441 PEYMR--------PSAWVRLDAMPLSRSGKVDRRLLPEPEIA 474
Cdd:PRK08314 501 IAWARehmaaykyPRIVEFVDSLPKSGSGKILWRQLQEQEKA 542
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1082-1530 |
1.84e-25 |
|
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: 114.10 E-value: 1.84e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1082 GVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDAS----------------TRA 1145
Cdd:cd05928 63 GLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGTIQLTAKDILYRLQASKAKCIVTSDElapevdsvasecpslkTKL 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1146 RLGESSCE-WVDLADLEAEAESGDDITDTErngsvrlTNLAYLIY-TSGSTGRPKAVGVSHT--GIVDFVNSlAKITTGT 1221
Cdd:cd05928 143 LVSEKSRDgWLNFKELLNEASTEHHCVETG-------SQEPMAIYfTSGTTGSPKMAEHSHSslGLGLKVNG-RYWLDLT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1222 PED----EPDTRILHVASpsfdASMFEmAWaiPAGHTLVIAPQADFAGDALATVLERDEVTDMIITPSV---LATVDPER 1294
Cdd:cd05928 215 ASDimwnTSDTGWIKSAW----SSLFE-PW--IQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPTVyrmLVQQDLSS 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1295 AQY--VRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQG 1371
Cdd:cd05928 288 YKFpsLQHCVTGGEPLNPEVLEKWKAQtGLDIYEGYGQTETGLICANFKGMKIKPGSMGKASPPYDVQIIDDNGNVLPPG 367
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1372 VVGELYLSTA-----GLARGYLGRPGQTAVSFVADpfgepgarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGE 1446
Cdd:cd05928 368 TEGDIGIRVKpirpfGLFSGYVDNPEKTAATIRGD--------FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1447 IEAVLDAQPGVAQSVVVGV-ESTRGgrkhtEVV-AYLV-AKPGATIDSAAVLDEAAQHL----AAHMVPSQAIVIDEIPL 1519
Cdd:cd05928 440 VESALIEHPAVVESAVVSSpDPIRG-----EVVkAFVVlAPQFLSHDPEQLTKELQQHVksvtAPYKYPRKVEFVQELPK 514
|
490
....*....|.
gi 1827387616 1520 TPAGKLDRAAL 1530
Cdd:cd05928 515 TVTGKIQRNEL 525
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
2592-3019 |
1.85e-25 |
|
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: 112.69 E-value: 1.85e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2592 LTYRELDEASDRLARWLIGRGVGPERAVAL-AIGRSAQLLT--AIWAVaktGGAYVPIDPDYPAERVASMIEDSGAVLgl 2668
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAIlSRNRPEWTIAdlAILAI---GAVPVPIYPTSSAEQIAYILNDSEAKA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2669 sVLASgdlpgqefewmrldddsvaaeiaavpagpitdaerlgevTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQES 2748
Cdd:cd05907 81 -LFVE---------------------------------------DPDDLATIIYTSGTTGRPKGVMLSHRNILSNALALA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2749 DRLNAGDNPVVLGFAsPSfdASVLE----YLLATVNEGTLAYRPSEAVGGEVLERF----------IAE--HGATHTFLT 2812
Cdd:cd05907 121 ERLPATEGDRHLSFL-PL--AHVFErragLYVPLLAGARIYFASSAETLLDDLSEVrptvflavprVWEkvYAAIKVKAV 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2813 PSVLSTMDPTAV-PSLRVIAAGGEAVPQPIVDRWAPA-TELHNLYGPTETTIGITISsamRPGDPV--RLGGPIGGVDLM 2888
Cdd:cd05907 198 PGLKRKLFDLAVgGRLRFAASGGAPLPAELLHFFRALgIPVYEGYGLTETSAVVTLN---PPGDNRigTVGKPLPGVEVR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2889 VLDErlrpvpvgmpGELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVRWTPDtdtGGLTLeyTGRSDDQ 2968
Cdd:cd05907 275 IADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDED---GFLHI--TGRKKDL 332
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 2969 VKLR-GLRIELGEIEAVLAEHDAVESAVVLGVGGSvatALAAYIVPVDGAVE 3019
Cdd:cd05907 333 IITSgGKNISPEPIENALKASPLISQAVVIGDGRP---FLVALIVPDPEALE 381
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
2566-3062 |
1.88e-25 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 114.15 E-value: 1.88e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDgAGARLTYRELDEASDRLARWLIGR-GVGPERAVALAIGRSAQLLTAIWAVAKTGGAYV 2644
Cdd:PRK12492 25 SVVEVFERSCKKFADRPAFSN-LGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2645 PIDPDYPAERVASMIEDSG--AVLGLSV---LASGDLPGQEFEWM---RLDD--------------DSVAAEIAA--VP- 2699
Cdd:PRK12492 104 NTNPLYTAREMRHQFKDSGarALVYLNMfgkLVQEVLPDTGIEYLieaKMGDllpaakgwlvntvvDKVKKMVPAyhLPq 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2700 AGPITDAERLGE--------VTAANLAYVIYTSGSTGRPKGVAVTHSGL--------ANFARQESD---RLNAGDN---- 2756
Cdd:PRK12492 184 AVPFKQALRQGRglslkpvpVGLDDIAVLQYTGGTTGLAKGAMLTHGNLvanmlqvrACLSQLGPDgqpLMKEGQEvmia 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2757 PVVLgFASPSFDASVLeYLLATVNEGTLAYRPSEaVGGEVLE----RFIAEHGATHTFLT----PSvLSTMDPTAvpsLR 2828
Cdd:PRK12492 264 PLPL-YHIYAFTANCM-CMMVSGNHNVLITNPRD-IPGFIKElgkwRFSALLGLNTLFVAlmdhPG-FKDLDFSA---LK 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2829 VIAAGGEAVPQPIVDRWAPAT--ELHNLYGPTETTigiTISSAMRPGDPVRLGG---PIGGVDLMVLDERLRPVPVGMPG 2903
Cdd:PRK12492 337 LTNSGGTALVKATAERWEQLTgcTIVEGYGLTETS---PVASTNPYGELARLGTvgiPVPGTALKVIDDDGNELPLGERG 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2904 ELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVRWTPDtdtgGLTlEYTGRSDDQVKLRGLRIELGEIEA 2983
Cdd:PRK12492 414 ELCIKGPQVMKGYWQQPEATAEALDAEGW-------FKTGDIAVIDPD----GFV-RIVDRKKDLIIVSGFNVYPNEIED 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2984 VLAEHDAVESAVVLGVGGS-VATALAAYIVPVDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEP 3062
Cdd:PRK12492 482 VVMAHPKVANCAAIGVPDErSGEAVKLFVVARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
2566-3059 |
2.73e-25 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 113.24 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVV--DGAG--ARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGG 2641
Cdd:PRK08008 8 HLRQMWDDLADVYGHKTALIfeSSGGvvRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2642 AYVPIDPDYPAERVASMIEDSGAvlGLSVLASGDLPgqEFEWMRLDDDSVAAEIAAVPAG-----PITDAERLGEVTAAN 2716
Cdd:PRK08008 88 IMVPINARLLREESAWILQNSQA--SLLVTSAQFYP--MYRQIQQEDATPLRHICLTRVAlpaddGVSSFTQLKAQQPAT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2717 LAY-----------VIYTSGSTGRPKGVAVTHSGLaNFARQESD---RLNAGDnpvVLGFASPSFDasvleyllatVNEG 2782
Cdd:PRK08008 164 LCYapplstddtaeILFTSGTTSRPKGVVITHYNL-RFAGYYSAwqcALRDDD---VYLTVMPAFH----------IDCQ 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2783 TLAYRPSEAVGGE--VLERF--------IAEHGATHTFLTPSVLST-MDPTAVPS-----LRVIA---AGGEAVPQPIVD 2843
Cdd:PRK08008 230 CTAAMAAFSAGATfvLLEKYsarafwgqVCKYRATITECIPMMIRTlMVQPPSANdrqhcLREVMfylNLSDQEKDAFEE 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2844 RWApaTELHNLYGPTETTIGItISSamRPGDPVR---LGGPIGGVDLMVLDERLRPVPVGMPGELY---VAGGALSRGYL 2917
Cdd:PRK08008 310 RFG--VRLLTSYGMTETIVGI-IGD--RPGDKRRwpsIGRPGFCYEAEIRDDHNRPLPAGEIGEICikgVPGKTIFKEYY 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2918 DRSGLTAERFTANPYGTAGQRMYRtgdvvrwtpdtDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVL 2997
Cdd:PRK08008 385 LDPKATAKVLEADGWLHTGDTGYV-----------DEEGF-FYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVV 452
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 2998 GVGGSVA-TALAAYIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK08008 453 GIKDSIRdEAIKAFVVLNEGEtLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1038-1508 |
3.15e-25 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 113.82 E-value: 3.15e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1038 TLIDVLAQR-DLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIgSVLATW-GVIKSGAAYVP 1115
Cdd:PRK08279 38 SLGDVFEEAaARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRP-EYLAAWlGLAKLGAVVAL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1116 VDPAYPADRIAYMLEDSGATVGITDA-------STRARLGESSCEWV----------DLADLEAEAESGDDITDTERNGs 1178
Cdd:PRK08279 117 LNTQQRGAVLAHSLNLVDAKHLIVGEelveafeEARADLARPPRLWVaggdtlddpeGYEDLAAAAAGAPTTNPASRSG- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1179 VRLTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtrILHVASPSFDASMFEMAW--AIPAGHTLV 1256
Cdd:PRK08279 196 VTAKDTAFYIYTSGTTGLPKAAVMSHMRWLKAMGGFGGLLRLTPDD-----VLYCCLPLYHNTGGTVAWssVLAAGATLA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1257 IAPQadFAGDALAtvlerDEVTDMIITPSV--------LATVDP---ERAQYVRnLATgGEACPPELVERWSER-G-RRI 1323
Cdd:PRK08279 271 LRRK--FSASRFW-----DDVRRYRATAFQyigelcryLLNQPPkptDRDHRLR-LMI-GNGLRPDIWDEFQQRfGiPRI 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1324 FNCYGPTEATVWAT----------RSRMTAGKPVTI-------GKPvdgftVRVLDGRLHEVPQGVVGELYLSTAGLAR- 1385
Cdd:PRK08279 342 LEFYAASEGNVGFInvfnfdgtvgRVPLWLAHPYAIvkydvdtGEP-----VRDADGRCIKVKPGEVGLLIGRITDRGPf 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1386 -GYlGRPGQTAVSFVADPFgEPGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVG 1464
Cdd:PRK08279 417 dGY-TDPEASEKKILRDVF-KKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYG 494
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1827387616 1465 VE----STRGGrkhtevVAYLVAKPGATIDSAAVLDEAAQHLAAHMVP 1508
Cdd:PRK08279 495 VEvpgtDGRAG------MAAIVLADGAEFDLAALAAHLYERLPAYAVP 536
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
13-468 |
4.49e-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: 341275 [Multi-domain] Cd Length: 439 Bit Score: 111.37 E-value: 4.49e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 13 LARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRlVVVTsdgeaearsrfdd 92
Cdd:cd05971 19 FANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGAS-ALVT------------- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 93 ivdvhvldisspgdaDLDEEEfagptrpanaAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPIT 172
Cdd:cd05971 85 ---------------DGSDDP----------ALIIYTSGTTGPPKGALHAHRVLLGHLPGVQFPFNLFPRDGDLYWTPAD 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 173 -------FDVsvreiFLPIAIGATLVIAEPGRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQT 245
Cdd:cd05971 140 wawigglLDV-----LLPSLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMRQQGEQLKHAQVKLRAIAT 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 246 GGEaltpPVARDLMV---RLPGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIGVPGELY 322
Cdd:cd05971 215 GGE----SLGEELLGwarEQFGVEVNEFYGQTECNLVIGNCSALFPIKPGSMGKPIPGHRVAIVDDNGTPLPPGEVGEIA 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 323 L---GGVQLArGYAGRPDLTAERFVADPFgepgarlyRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAA 399
Cdd:cd05971 291 VelpDPVAFL-GYWNNPSATEKKMAGDWL--------LTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGPAEIEECLLKH 361
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 400 PGVLHAAA-AVVDGPGGQQLVGY--LAPADVDVDTVAATTAEL----LPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd05971 362 PAVLMAAVvGIPDPIRGEIVKAFvvLNPGETPSDALAREIQELvktrLAAHEYPREIEFVNELPRTATGKIRRREL 437
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
119-466 |
6.10e-25 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 109.39 E-value: 6.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 119 RPANAAFTLFTSGSTGRPKAVVITH----------RGIANRLAADIEQYDLTARD----VFLYKAPITFDVSVREIFLPI 184
Cdd:cd05924 1 RSADDLYILYTGGTTGMPKGVMWRQedifrmlmggADFGTGEFTPSEDAHKAAAAaagtVMFPAPPLMHGTGSWTAFGGL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 185 AIGATLVIaePGRHGDPVHLADLIRRHGVTVIHFV-PAMLAAFNEVL-GAGVGELTSLRLIQTGGEALTPPVARDLMVRL 262
Cdd:cd05924 81 LGGQTVVL--PDDRFDPEEVWRTIEKHKVTSMTIVgDAMARPLIDALrDAGPYDLSSLFAISSGGALLSPEVKQGLLELV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 263 PGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSarVLDAALREVPIGVPGELYLG--GVqLARGYAGRPDLTA 340
Cdd:cd05924 159 PNITLVDAFGSSETGFTGSGHSAGSGPETGPFTRANPDTV--VLDDDGRVVPPGSGGVGWIArrGH-IPLGYYGDEAKTA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 341 ERFV-ADpfgepGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGPG---GQ 416
Cdd:cd05924 236 ETFPeVD-----GVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAV--YDVLVVGRPDerwGQ 308
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 417 QLVGYLA---PADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRR 466
Cdd:cd05924 309 EVVAVVQlreGAGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1-471 |
6.11e-25 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 112.54 E-value: 6.11e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:PRK13382 69 LTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPALAEVVTREGVDTVIYDE 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRFDDIVD-VHVLDISSPGDADLDE---EEFAG---PTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAAD 153
Cdd:PRK13382 149 EFSATVDRALADCPQaTRIVAWTDEDHDLTVEvliAAHAGqrpEPTGRKGRVILLTSGTTGTPKGARRSGPGGIGTLKAI 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 154 IEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAepgRHGDPVHLADLIRRHGVTVIHFVPAM----LAAFNEV 229
Cdd:PRK13382 229 LDRTPWRAEEPTVIVAPMFHAWGFSQLVLAASLACTIVTR---RRFDPEATLDLIDRHRATGLAVVPVMfdriMDLPAEV 305
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 230 LGAGVGEltSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTihrVTQDD-RVIP--IGTPTRRVSARVL 306
Cdd:PRK13382 306 RNRYSGR--SLRFAAASGSRMRPDVVIAFMDQF-GDVIYNNYNATEAGMIAT---ATPADlRAAPdtAGRPAEGTEIRIL 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 307 DAALREVPIGVPGELYLGGVQLARGY-AGRPDLTAERFVAdpfgepgarlyrTGDRARWNRDGEIEYLGRTDFQVKLRGQ 385
Cdd:PRK13382 380 DQDFREVPTGEVGTIFVRNDTQFDGYtSGSTKDFHDGFMA------------SGDVGYLDENGRLFVVGRDDEMIVSGGE 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 386 RLELGEVEAALAAAPGVLHAAAAVVDGPG-GQQLVGYLAPAD---VDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSG 461
Cdd:PRK13382 448 NVYPIEVEKTLATHPDVAEAAVIGVDDEQyGQRLAAFVVLKPgasATPETLKQHVRDNLANYKVPRDIVVLDELPRGATG 527
|
490
....*....|
gi 1827387616 462 KVDRRLLPEP 471
Cdd:PRK13382 528 KILRRELQAR 537
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
2569-3059 |
6.45e-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: 112.97 E-value: 6.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2569 ELFRAAARRAPDHVAVV----DGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYV 2644
Cdd:cd05968 65 QLLDKWLADTRTRPALRwegeDGTSRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2645 PIDPDYPAERVASMIEDSGAVLglsvLASGDL---PGQEFEWMRLDDDSVAA---------------EIAAVPAGPITDA 2706
Cdd:cd05968 145 PIFSGFGKEAAATRLQDAEAKA----LITADGftrRGREVNLKEEADKACAQcptvekvvvvrhlgnDFTPAKGRDLSYD 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2707 E-------RLGEVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQ---------ESDRLN-AGDNPVVLG----FASP 2765
Cdd:cd05968 221 EeketagdGAERTESEDPLMIIYTSGTTGKPKGTVHVHAGFPLKAAQdmyfqfdlkPGDLLTwFTDLGWMMGpwliFGGL 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2766 SFDASVLEYllatvnEGTlayrPSEAVGGEvLERFIAEHGATHTFLTPSVLSTMDPTA--------VPSLRVIAAGGEAV 2837
Cdd:cd05968 301 ILGATMVLY------DGA----PDHPKADR-LWRMVEDHEITHLGLSPTLIRALKPRGdapvnahdLSSLRVLGSTGEPW 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2838 -PQPIvdRWAPATELH------NLYGPTETTIGITISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPvGMPGELYVAGG 2910
Cdd:cd05968 370 nPEPW--NWLFETVGKgrnpiiNYSGGTEISGGILGNVLIKPIKPSSFNGPVPGMKADVLDESGKPAR-PEVGELVLLAP 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2911 --ALSRGYLDRSgltaERFTaNPYGTAGQRMYRTGDVVRWtpdtDTGGLTLeYTGRSDDQVKLRGLRIELGEIEAVLAEH 2988
Cdd:cd05968 447 wpGMTRGFWRDE----DRYL-ETYWSRFDNVWVHGDFAYY----DEEGYFY-ILGRSDDTINVAGKRVGPAEIESVLNAH 516
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 2989 DAVESAVVLGVGGSV-ATALAAYIVPVDGAVEV----SELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05968 517 PAVLESAAIGVPHPVkGEAIVCFVVLKPGVTPTealaEELMERVADELGKPLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1050-1530 |
7.51e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 111.64 E-value: 7.51e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALIC--DGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAY 1127
Cdd:PRK13390 11 PDRPAVIVaeTGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1128 MLEDSGATVGITDASTRARLGESSCEWVDLADLEAEAESGDDITDTERNGSVRLTNL---AYLIYTSGSTGRPKAV---- 1200
Cdd:PRK13390 91 IVGDSGARVLVASAALDGLAAKVGADLPLRLSFGGEIDGFGSFEAALAGAGPRLTEQpcgAVMLYSSGTTGFPKGIqpdl 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1201 ---GVSHTGivDFVNSLAKITTGTPEDEpdtrILHVASPSFDASMFEMAWAIPA-GHTLVIAPQADfAGDALATVlERDE 1276
Cdd:PRK13390 171 pgrDVDAPG--DPIVAIARAFYDISESD----IYYSSAPIYHAAPLRWCSMVHAlGGTVVLAKRFD-AQATLGHV-ERYR 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1277 VTDMIITPSVLATV----DPERAQY----VRNLATGGEACPPELVERWSE-RGRRIFNCYGPTEA---TVWATRSRMTag 1344
Cdd:PRK13390 243 ITVTQMVPTMFVRLlkldADVRTRYdvssLRAVIHAAAPCPVDVKHAMIDwLGPIVYEYYSSTEAhgmTFIDSPDWLA-- 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1345 KPVTIGKPVDGfTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVS-FVADPFgepgarMYATGDLVRVAKGG 1423
Cdd:PRK13390 321 HPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAAqHPAHPF------WTTVGDLGSVDEDG 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1424 NLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKHTEVVAYLVAKPGATIDSAAVLDEAAQHLA 1503
Cdd:PRK13390 394 YLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPEMGEQVKAVIQLVEGIRGSDELARELIDYTRSRIA 473
|
490 500
....*....|....*....|....*..
gi 1827387616 1504 AHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK13390 474 HYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1051-1530 |
8.48e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 112.16 E-value: 8.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1051 DHPALICDGTEMDYDEFETRTNAIARALLAR-GVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:PRK05677 39 DKPAFSNLGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTNPLYTAREMEHQF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITDASTrARLGE-----SSCEWV---DLADLEA------------------------EAESGDDIT-----D 1172
Cdd:PRK05677 119 NDSGAKALVCLANM-AHLAEkvlpkTGVKHVivtEVADMLPplkrllinavvkhvkkmvpayhlpQAVKFNDALakgagQ 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1173 TERNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDEPDTRI-----LHVASPSFDAsmfeMAW 1247
Cdd:PRK05677 198 PVTEANPQADDVAVLQYTGGTTGVAKGAMLTHRNLVANMLQCRALMGSNLNEGCEILIaplplYHIYAFTFHC----MAM 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1248 AIPAGHTLVIAPQADFagDALATVLERDEVTDMI-ITPSVLATVDPERaqyVRNL--------ATGGEACPPELVERWSE 1318
Cdd:PRK05677 274 MLIGNHNILISNPRDL--PAMVKELGKWKFSGFVgLNTLFVALCNNEA---FRKLdfsalkltLSGGMALQLATAERWKE 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1319 -RGRRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVS 1397
Cdd:PRK05677 349 vTGCAICEGYGMTETSPVVSVNPSQAIQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDEI 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1398 FVADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEV 1477
Cdd:PRK05677 429 LDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSG----EA 497
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 1478 V-AYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK05677 498 IkVFVVVKPGETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
2549-3059 |
1.29e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 112.36 E-value: 1.29e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2549 AAVELTPVtggPATD-PVTLAELFRAAARRAPDHVAV---VDGAGAR----LTYRELDEASDRLARWLIGRGVGPERAVA 2620
Cdd:PRK07529 11 EAIEAVPL---AARDlPASTYELLSRAAARHPDAPALsflLDADPLDrpetWTYAELLADVTRTANLLHSLGVGPGDVVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2621 LAIGRSAQLLTAIWAVAKTGGAyVPIDPDYPAERVASMIEDSGA------------------------VLGLSVLASGDL 2676
Cdd:PRK07529 88 FLLPNLPETHFALWGGEAAGIA-NPINPLLEPEQIAELLRAAGAkvlvtlgpfpgtdiwqkvaevlaaLPELRTVVEVDL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2677 PGQEFEWMRLDDDSVA-----------AEIAAVPAGPITDAERlgeVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFAR 2745
Cdd:PRK07529 167 ARYLPGPKRLAVPLIRrkaharildfdAELARQPGDRLFSGRP---IGPDDVAAYFHTGGTTGMPKLAQHTHGNEVANAW 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2746 QESDRLNAGDNPVVLgFASPSFDA-SVLEYLLATVNEGT-------LAYRpseavGGEVLERF--IAEHGATHTFLT-PS 2814
Cdd:PRK07529 244 LGALLLGLGPGDTVF-CGLPLFHVnALLVTGLAPLARGAhvvlatpQGYR-----GPGVIANFwkIVERYRINFLSGvPT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2815 VLSTM-----DPTAVPSLRVIAAGGEAVPQPIVDRWAPAT--ELHNLYGPTETTIGITISSamrPGDPVRLGG-----PI 2882
Cdd:PRK07529 318 VYAALlqvpvDGHDISSLRYALCGAAPLPVEVFRRFEAATgvRIVEGYGLTEATCVSSVNP---PDGERRIGSvglrlPY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2883 GGVDLMVLDE---RLRPVPVGMPGELYVAGGALSRGYLDrsgltaERFTANPYgtAGQRMYRTGDVVRWTPDtdtGGLTL 2959
Cdd:PRK07529 395 QRVRVVILDDagrYLRDCAVDEVGVLCIAGPNVFSGYLE------AAHNKGLW--LEDGWLNTGDLGRIDAD---GYFWL 463
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2960 eyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATAL-AAYIVPVDGA-VEVSELKAFAGGRLP---Ay 3034
Cdd:PRK07529 464 --TGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAVGRPDAHAGELpVAYVQLKPGAsATEAELLAFARDHIAeraA- 540
|
570 580
....*....|....*....|....*
gi 1827387616 3035 mVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK07529 541 -VPKHVRILDALPKTAVGKIFKPAL 564
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1-468 |
1.53e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 110.75 E-value: 1.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:PRK06145 28 ISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVAYILGDAGAKLLLVDE 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRFDDIV-DVHVLDISSPGDADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDL 159
Cdd:PRK06145 108 EFDAIVALETPKIViDAAAQADSRRLAQGGLEIPPQAAVAPTDLVRLMYTSGTTDRPKGVMHSYGNLHWKSIDHVIALGL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 160 TARDVFLYKAPItfdVSVREIFLP----IAIGATLVIAepgRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVG 235
Cdd:PRK06145 188 TASERLLVVGPL---YHVGAFDLPgiavLWVGGTLRIH---REFDPEAVLAAIERHRLTCAWMAPVMLSRVLTVPDRDRF 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 236 ELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQD-DRVIPIGTPTRRVSARVLDAALREVP 314
Cdd:PRK06145 262 DLDSLAWCIGGGEKTPESRIRDFTRVFTRARYIDAYGLTETCSGDTLMEAGREiEKIGSTGRALAHVEIRIADGAGRWLP 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 315 IGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlyRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEA 394
Cdd:PRK06145 342 PNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF--------RSGDVGYLDEEGFLYLTDRKKDMIISGGENIASSEVER 413
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 395 ALAAAPGVLHAAA-AVVDGPGGQQLVG--YLAP-ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK06145 414 VIYELPEVAEAAViGVHDDRWGERITAvvVLNPgATLTLEALDRHCRQRLASFKVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
2566-3056 |
1.59e-24 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 111.44 E-value: 1.59e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVD-GAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYV 2644
Cdd:PRK08315 17 TIGQLLDRTAARYPDREALVYrDQGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2645 PIDPDYPAERVASMIEDSGA---------------------VLGLSVLASGDLPGQEFEWMR----LDDDSVA-----AE 2694
Cdd:PRK08315 97 TINPAYRLSELEYALNQSGCkaliaadgfkdsdyvamlyelAPELATCEPGQLQSARLPELRrvifLGDEKHPgmlnfDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2695 IAAvpAGPITDAERLGEVTAANLAY-VI---YTSGSTGRPKGVAVTHSGLANFARQ--ESDRLNAGDN---PV------- 2758
Cdd:PRK08315 177 LLA--LGRAVDDAELAARQATLDPDdPIniqYTSGTTGFPKGATLTHRNILNNGYFigEAMKLTEEDRlciPVplyhcfg 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2759 -VLG------------FASPSFDAsvlEYLLATVNEgtlayrpseavggevlER----------FIAE--HGATHTFltp 2813
Cdd:PRK08315 255 mVLGnlacvthgatmvYPGEGFDP---LATLAAVEE----------------ERctalygvptmFIAEldHPDFARF--- 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2814 sVLStmdptavpSLRV-IAAGGeavPQPI------VDRWApATELHNLYGPTETTIGITISsamRPGDPVRL-----GGP 2881
Cdd:PRK08315 313 -DLS--------SLRTgIMAGS---PCPIevmkrvIDKMH-MSEVTIAYGMTETSPVSTQT---RTDDPLEKrvttvGRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2882 IGGVDLMVLD-ERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANpygtagqRMYRTGDVVrwTPDTDtGGLTLe 2960
Cdd:PRK08315 377 LPHLEVKIVDpETGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEAIDAD-------GWMHTGDLA--VMDEE-GYVNI- 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2961 yTGRSDDQVkLRGlrielG------EIEAVLAEHDAVESAVVLGV-----GgsvaTALAAYIVPVDGA-VEVSELKAFAG 3028
Cdd:PRK08315 446 -VGRIKDMI-IRG-----GeniyprEIEEFLYTHPKIQDVQVVGVpdekyG----EEVCAWIILRPGAtLTEEDVRDFCR 514
|
570 580
....*....|....*....|....*...
gi 1827387616 3029 GRLPAYMVPSSFTVIDELPLTPVGKLDK 3056
Cdd:PRK08315 515 GKIAHYKIPRYIRFVDEFPMTVTGKIQK 542
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
4-470 |
1.62e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 110.90 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSD-- 81
Cdd:PRK07470 36 REIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVAYLAEASGARAMICHADfp 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 -------------------GEAEARSRFDDIVDVHVLDISSPGDADLDEeefagptrpanAAFTLFTSGSTGRPKAVVIT 142
Cdd:PRK07470 116 ehaaavraaspdlthvvaiGGARAGLDYEALVARHLGARVANAAVDHDD-----------PCWFFFTSGTTGRPKAAVLT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 143 HRG----IANRLAADIEqyDLTARDVFLYKAPITFDVSVREIfLPIAIGATLVIAePGRHGDPVHLADLIRRHGVTVIHF 218
Cdd:PRK07470 185 HGQmafvITNHLADLMP--GTTEQDASLVVAPLSHGAGIHQL-CQVARGAATVLL-PSERFDPAEVWALVERHRVTNLFT 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 219 VPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTI-----HRVTQ--DDRV 291
Cdd:PRK07470 261 VPTILKMLVEHPAVDRYDHSSLRYVIYAGAPMYRADQKRALAKL-GKVLVQYFGLGEVTGNITVlppalHDAEDgpDARI 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 292 IPIGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlyRTGDRARWNRDGEIE 371
Cdd:PRK07470 340 GTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAFRDGWF--------RTGDLGHLDARGFLY 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 372 YLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQqlVGYL-----APADVDVDTVAATTAELLPEYMR 445
Cdd:PRK07470 412 ITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVlGVPDPVWGE--VGVAvcvarDGAPVDEAELLAWLDGKVARYKL 489
|
490 500
....*....|....*....|....*
gi 1827387616 446 PSAWVRLDAMPLSRSGKVDRRLLPE 470
Cdd:PRK07470 490 PKRFFFWDALPKSGYGKITKKMVRE 514
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
1038-1877 |
1.70e-24 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 113.72 E-value: 1.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1038 TLIDVLAQR-DLDPDHPAL--ICD----GTEMDYDEFETRTNAIARALLARGvSPEDVVAVGMERSIGSVLATWGVIKSG 1110
Cdd:PRK05691 10 TLVQALQRRaAQTPDRLALrfLADdpgeGVVLSYRDLDLRARTIAAALQARA-SFGDRAVLLFPSGPDYVAAFFGCLYAG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1111 AAYVPvdpAYPAD--------RIAYMLEDSGATVGITDASTRARL-------GESSCEWVDLADLEAEaesgddITDTER 1175
Cdd:PRK05691 89 VIAVP---AYPPEsarrhhqeRLLSIIADAEPRLLLTVADLRDSLlqmeelaAANAPELLCVDTLDPA------LAEAWQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1176 NGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIV-----------------DFVNS--------------LAKITTGTPed 1224
Cdd:PRK05691 160 EPALQPDDIAFLQYTSGSTALPKGVQVSHGNLVaneqlirhgfgidlnpdDVIVSwlplyhdmgligglLQPIFSGVP-- 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1225 epdtrILHVASPSFDASMFEMAWAIPA-GHTLVIAPqaDFAgdaLATVLERdevtdmiITPSVLATVDPERAqyvRNLAT 1303
Cdd:PRK05691 238 -----CVLMSPAYFLERPLRWLEAISEyGGTISGGP--DFA---YRLCSER-------VSESALERLDLSRW---RVAYS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1304 GGEACPPELVERWSER-------GRRIFNCYGPTEATVWATRSRMTAGKP----------------------VTIGKPVD 1354
Cdd:PRK05691 298 GSEPIRQDSLERFAEKfaacgfdPDSFFASYGLAEATLFVSGGRRGQGIPaleldaealarnraepgtgsvlMSCGRSQP 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1355 GFTVRVLD-GRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVAdpfgEPGARMYATGDLvRVAKGGNLEFAGRADH 1433
Cdd:PRK05691 378 GHAVLIVDpQSLEVLGDNRVGEIWASGPSIAHGYWRNPEASAKTFVE----HDGRTWLRTGDL-GFLRDGELFVTGRLKD 452
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1434 QVKINGQRVELGEIEAVLDAQpgvaqsvvvgVESTRGGRkhteVVAYLVAKPGAT-IDSAAVLDEAAQHL---------- 1502
Cdd:PRK05691 453 MLIVRGHNLYPQDIEKTVERE----------VEVVRKGR----VAAFAVNHQGEEgIGIAAEISRSVQKIlppqaliksi 518
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1503 ------AAHMVPSQAIVID--EIPLTPAGKLDRAA---------------LPEPHAPEPAEYVAPANPAEDNLARIVAGL 1559
Cdd:PRK05691 519 rqavaeACQEAPSVVLLLNpgALPKTSSGKLQRSAcrlrladgsldsyalFPALQAVEAAQTAASGDELQARIAAIWCEQ 598
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1560 LGEERVSVTESFFALGGDSIMSIQLSSA-AKAAGIHLSPREIFELKTIRA---MAAAAAASGGPV-ALIEELPGGGTGEM 1634
Cdd:PRK05691 599 LKVEQVAADDHFFLLGGNSIAATQVVARlRDELGIDLNLRQLFEAPTLAAfsaAVARQLAGGGAAqAAIARLPRGQALPQ 678
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1635 PLPPVTSWMIEHSEepadfadfSQSLVFNVPASAAV------ADLQTVVEAVAAAHPML-TAVLTRSGDGWTMNAGAGIV 1707
Cdd:PRK05691 679 SLAQNRLWLLWQLD--------PQSAAYNIPGGLHLrgeldeAALRASFQRLVERHESLrTRFYERDGVALQRIDAQGEF 750
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1708 PaVREIDAEGaLDPALVDA------HRELLGAMDPGTGSLLGTAVVN-GEGRRRLVIAIHHLGVDAVSWPILVEDLVTAW 1780
Cdd:PRK05691 751 A-LQRIDLSD-LPEAEREAraaqirEEEARQPFDLEKGPLLRVTLVRlDDEEHQLLVTLHHIVADGWSLNILLDEFSRLY 828
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1781 AQLTSGRPIELRPEATTTRRIAH-----LLAGQVharAREVDYWLEQLPERPTSFGTSADRP--LHRRRDESSLTYVVDD 1853
Cdd:PRK05691 829 AAACQGQTAELAPLPLGYADYGAwqrqwLAQGEA---ARQLAYWKAQLGDEQPVLELATDHPrsARQAHSAARYSLRVDA 905
|
970 980
....*....|....*....|....
gi 1827387616 1854 VAGSILTTVPQAFGSSVDDVLLGA 1877
Cdd:PRK05691 906 SLSEALRGLAQAHQATLFMVLLAA 929
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1054-1530 |
2.99e-24 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 110.16 E-value: 2.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1054 ALIC-----DGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYM 1128
Cdd:PRK08008 25 ALIFessggVVRRYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1129 LEDSGATVGITDAS-----TRARLGESSC-EWVDLADLEAEAESGddITDTERNGSVRLTNLAY-----------LIYTS 1191
Cdd:PRK08008 105 LQNSQASLLVTSAQfypmyRQIQQEDATPlRHICLTRVALPADDG--VSSFTQLKAQQPATLCYapplstddtaeILFTS 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1192 GSTGRPKAVGVSHTGIVdFVNSLAKITTGTPEDEpdtRILHVAsPSFDASmFEMAWAIPA---GHTLVIAPQAD---FAG 1265
Cdd:PRK08008 183 GTTSRPKGVVITHYNLR-FAGYYSAWQCALRDDD---VYLTVM-PAFHID-CQCTAAMAAfsaGATFVLLEKYSaraFWG 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1266 DAL---ATVlerDEVTDMIITPSVLATVDP-ERAQYVR------NLATggeacppELVERWSER-GRRIFNCYGPTEATV 1334
Cdd:PRK08008 257 QVCkyrATI---TECIPMMIRTLMVQPPSAnDRQHCLRevmfylNLSD-------QEKDAFEERfGVRLLTSYGMTETIV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1335 WATRSRMTAGK--PvTIGKPVDGFTVRVLDGRLHEVPQGVVGELYL-STAG--LARGYLGRPGQTAVSFvadpfgEPGAR 1409
Cdd:PRK08008 327 GIIGDRPGDKRrwP-SIGRPGFCYEAEIRDDHNRPLPAGEIGEICIkGVPGktIFKEYYLDPKATAKVL------EADGW 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1410 MYaTGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGV-ESTRggrkHTEVVAYLVAKPGAT 1488
Cdd:PRK08008 400 LH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIkDSIR----DEAIKAFVVLNEGET 474
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 1827387616 1489 IDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK08008 475 LSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1048-1530 |
3.26e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 109.48 E-value: 3.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1048 LDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVvAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAY 1127
Cdd:PRK07638 13 LQPNKIAIKENDRVLTYKDWFESVCKVANWLNEKESKNKTI-AILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1128 MLEDSGATVGITDASTRARLGESSCEWVDL----ADLEAEAESGDDITDTERNGsvrltnlAYLIYTSGSTGRPKAVGVS 1203
Cdd:PRK07638 92 RLAISNADMIVTERYKLNDLPDEEGRVIEIdewkRMIEKYLPTYAPIENVQNAP-------FYMGFTSGSTGKPKAFLRA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1204 HTGIVDFVNSLAKITTGTPEDepdtRILhVASpSFDASMFEMAwAIPA---GHTLVIAPQadFAGDALATVLERDEVTDM 1280
Cdd:PRK07638 165 QQSWLHSFDCNVHDFHMKRED----SVL-IAG-TLVHSLFLYG-AISTlyvGQTVHLMRK--FIPNQVLDKLETENISVM 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1281 IITPSVLATVDPERA--QYVRNLATGGEACPPELVERWSER--GRRIFNCYGPTEAT-VWATRSRMTAGKPVTIGKPVDG 1355
Cdd:PRK07638 236 YTVPTMLESLYKENRviENKMKIISSGAKWEAEAKEKIKNIfpYAKLYEFYGASELSfVTALVDEESERRPNSVGRPFHN 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1356 FTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRpgqtavsfvADPFGEPGARMYAT-GDLVRVAKGGNLEFAGRADHQ 1434
Cdd:PRK07638 316 VQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYIIG---------GVLARELNADGWMTvRDVGYEDEEGFIYIVGREKNM 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1435 VKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATIDSAAVLdeaaQHLAAHMVPSQAIVI 1514
Cdd:PRK07638 387 ILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYWGEK---PVAIIKGSATKQQLKSFCL----QRLSSFKIPKEWHFV 459
|
490
....*....|....*.
gi 1827387616 1515 DEIPLTPAGKLDRAAL 1530
Cdd:PRK07638 460 DEIPYTNSGKIARMEA 475
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1043-1505 |
4.31e-24 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 109.99 E-value: 4.31e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1043 LAQRDldPDHPALICDGT----------EMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAA 1112
Cdd:PRK09274 15 AAQER--PDQLAVAVPGGrgadgklaydELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAV 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1113 YVPVDPAYPADRIAYMLEDSG--ATVGITDASTRARLGESSCEWV---------------DLADLEAEAESGD-DITDTE 1174
Cdd:PRK09274 93 PVLVDPGMGIKNLKQCLAEAQpdAFIGIPKAHLARRLFGWGKPSVrrlvtvggrllwggtTLATLLRDGAAAPfPMADLA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1175 RngsvrlTNLAYLIYTSGSTGRPKAVGVSHTgivdfvNSLAKIT--TGTPEDEPDTRILHVAsPSFdaSMFEMAwaipAG 1252
Cdd:PRK09274 173 P------DDMAAILFTSGSTGTPKGVVYTHG------MFEAQIEalREDYGIEPGEIDLPTF-PLF--ALFGPA----LG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1253 HTLVIaPQADFAG------DALATVLERDEVTDMIITPSVLATVdperAQY----------VRNLATGGEACPPELVERW 1316
Cdd:PRK09274 234 MTSVI-PDMDPTRpatvdpAKLFAAIERYGVTNLFGSPALLERL----GRYgeangiklpsLRRVISAGAPVPIAVIERF 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1317 SE---RGRRIFNCYGPTEA----------TVWATRSRMTAGKPVTIGKPVDGFTVRVLD---------GRLHEVPQGVVG 1374
Cdd:PRK09274 309 RAmlpPDAEILTPYGATEAlpissiesreILFATRAATDNGAGICVGRPVDGVEVRIIAisdapipewDDALRLATGEIG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1375 ELYLSTAGLARGYLGRPGQTAVSFVADPFGEPGARMyatGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQ 1454
Cdd:PRK09274 389 EIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVWHRM---GDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTH 465
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 1455 PGVAQSVVVGVEstrggrKHTEVVAYLV--AKPGATIDSAAVLDEAAQHLAAH 1505
Cdd:PRK09274 466 PGVKRSALVGVG------VPGAQRPVLCveLEPGVACSKSALYQELRALAAAH 512
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1-466 |
4.68e-24 |
|
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: 109.64 E-value: 4.68e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEvAVGIQIDRSVEQVVAIHAVAMAGGHFVPL---DEQLPVDRARYMVRTAGVRLVV 77
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVGKPGD-RVLLLAPPGLDFVAAFLGCLYAGAIAVPLpppTPGRHAERLAAILADAGPRVVL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 78 VTSDGEAEAR---SRFDDIVDVHVLDISSPGDADLDEEEFAGPTrPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADI 154
Cdd:cd05931 104 TTAAALAAVRafaASRPAAGTPRLLVVDLLPDTSAADWPPPSPD-PDDIAYLQYTSGSTGTPKGVVVTHRNLLANVRQIR 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 155 EQYDLTARDVFLYKAPITFDVS-VREIFLPIAIGATLVIAEPGRH-GDPVHLADLIRRHGVTVIhFVPAMlaAFNEVLGA 232
Cdd:cd05931 183 RAYGLDPGDVVVSWLPLYHDMGlIGGLLTPLYSGGPSVLMSPAAFlRRPLRWLRLISRYRATIS-AAPNF--AYDLCVRR 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 233 GVGE------LTSLRLIQTGGEaltpPVARDLMVR---------LPGTRLQNQYGPAEASIVVTIHRVTQDDRVIPI--- 294
Cdd:cd05931 260 VRDEdlegldLSSWRVALNGAE----PVRPATLRRfaeafapfgFRPEAFRPSYGLAEATLFVSGGPPGTGPVVLRVdrd 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 295 ----------------------GTPTRRVSARVLDAA-LREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPfGEP 351
Cdd:cd05931 336 alagravavaaddpaarelvscGRPLPDQEVRIVDPEtGRELPDGEVGEIWVRGPSVASGYWGRPEATAETFGALA-ATD 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 352 GARLYRTGDRARWnRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLH---AAAAVVDGPGGQQLVgylAPADVD 428
Cdd:cd05931 415 EGGWLRTGDLGFL-HDGELYITGRLKDLIIVRGRNHYPQDIEATAEEAHPALRpgcVAAFSVPDDGEERLV---VVAEVE 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 1827387616 429 VDTVAATTAELLPEY---------MRPSA--WVRLDAMPLSRSGKVDRR 466
Cdd:cd05931 491 RGADPADLAAIAAAIraavarehgVAPADvvLVRPGSIPRTSSGKIQRR 539
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
2566-3061 |
6.04e-24 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 111.55 E-value: 6.04e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDGAGARLTYRELDEASDRLARwLIGRGVGPERAVALAIGRSAQllTAIWAVAKTGGAYVP 2645
Cdd:PRK08633 616 PLAEAWIDTAKRNWSRLAVADSTGGELSYGKALTGALALAR-LLKRELKDEENVGILLPPSVA--GALANLALLLAGKVP 692
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2646 IDPDYPAERVA--SMIEDSGAV-----------LGLSVLASGDLPGQEFEWMrlDD--------DSVAAEIAA--VPAGP 2702
Cdd:PRK08633 693 VNLNYTASEAAlkSAIEQAQIKtvitsrkflekLKNKGFDLELPENVKVIYL--EDlkakiskvDKLTALLAArlLPARL 770
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2703 ITdAERLGEVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLG----FASPSFDASVLEYLLat 2778
Cdd:PRK08633 771 LK-RLYGPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDDVILSslpfFHSFGLTVTLWLPLL-- 847
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2779 vnEGTLA---YRPSEAVGgevLERFIAEHGATHTFLTPSVLST------MDPTAVPSLRVIAAGGEAVPQPIVDRWAPAT 2849
Cdd:PRK08633 848 --EGIKVvyhPDPTDALG---IAKLVAKHRATILLGTPTFLRLylrnkkLHPLMFASLRLVVAGAEKLKPEVADAFEEKF 922
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2850 ELHNL--YGPTETT--IGITISSAMRPGDPVRLGG-------PIGGVDLMVLD-ERLRPVPVGMPGELYVAGGALSRGYL 2917
Cdd:PRK08633 923 GIRILegYGATETSpvASVNLPDVLAADFKRQTGSkegsvgmPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYL 1002
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2918 DRSGLTAERFTAnpygTAGQRMYRTGDVVRWtpDTDtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEhdavesavVL 2997
Cdd:PRK08633 1003 GDPEKTAEVIKD----IDGIGWYVTGDKGHL--DED-GFLTI--TDRYSRFAKIGGEMVPLGAVEEELAK--------AL 1065
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 2998 GVGGSVataLAAYIVP------------VDGAVEVSELK-AFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPE 3061
Cdd:PRK08633 1066 GGEEVV---FAVTAVPdekkgeklvvlhTCGAEDVEELKrAIKESGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKE 1139
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
2567-3061 |
6.99e-24 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 108.81 E-value: 6.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2567 LAELFRAAARRaPDHVAVVDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPI 2646
Cdd:PRK07514 5 LFDALRAAFAD-RDAPFIETPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2647 DPDYPAERVASMIEDSGAvlGLSVLASGDlpgqeFEWMR-------------LDDD---SVAAEIAAVPAgPITDAERlg 2710
Cdd:PRK07514 84 NTAYTLAELDYFIGDAEP--ALVVCDPAN-----FAWLSkiaaaagaphvetLDADgtgSLLEAAAAAPD-DFETVPR-- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2711 evTAANLAYVIYTSGSTGRPKGVAVTHSGLANFAR--QESDRLNAGD------------------NPVVLGFAS----PS 2766
Cdd:PRK07514 154 --GADDLAAILYTSGTTGRSKGAMLSHGNLLSNALtlVDYWRFTPDDvlihalpifhthglfvatNVALLAGASmiflPK 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2767 FDAS-VLEYL-LATVNEGTlayrPSEAVggevleRFIAEHGathtfLTPSVLSTMdptavpslRVIAAGG---------- 2834
Cdd:PRK07514 232 FDPDaVLALMpRATVMMGV----PTFYT------RLLQEPR-----LTREAAAHM--------RLFISGSapllaethre 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2835 --EAVPQPIVDRwapatelhnlYGPTETtigITISSamRPGDPVRLGGPIG----GVDLMVLD-ERLRPVPVGMPGELYV 2907
Cdd:PRK07514 289 fqERTGHAILER----------YGMTET---NMNTS--NPYDGERRAGTVGfplpGVSLRVTDpETGAELPPGEIGMIEV 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2908 AGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVRWTPDtdtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAE 2987
Cdd:PRK07514 354 KGPNVFKGYWRMPEKTAEEFRADGF-------FITGDLGKIDER---GYVHI--VGRGKDLIISGGYNVYPKEVEGEIDE 421
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2988 HDAV-ESAVVlGVG----GSVATALaayIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPE 3061
Cdd:PRK07514 422 LPGVvESAVI-GVPhpdfGEGVTAV---VVPKPGAaLDEAAILAALKGRLARFKQPKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
127-465 |
1.05e-23 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 105.42 E-value: 1.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 127 LFTSGSTGRPKAVVITHRG-IANRLAADIEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAepGRHGDPVHLA 205
Cdd:cd17635 7 IFTSGTTGEPKAVLLANKTfFAVPDILQKEGLNWVVGDVTYLPLPATHIGGLWWILTCLIHGGLCVTG--GENTTYKSLF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 206 DLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEAltpPVARDLMVRL--PGTRLQNQYGPAEASIVVTIH 283
Cdd:cd17635 85 KILTTNAVTTTCLVPTLLSKLVSELKSANATVPSLRLIGYGGSR---AIAADVRFIEatGLTNTAQVYGLSETGTALCLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 284 RVTQDDRVIPIGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlyRTGDRAR 363
Cdd:cd17635 162 TDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--------NTGDLGE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 364 WNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAA-AAVVDGPGGQQLVGYLAPADVDVDTVAA----TTAE 438
Cdd:cd17635 234 RREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECAcYEISDEEFGELVGLAVVASAELDENAIRalkhTIRR 313
|
330 340
....*....|....*....|....*..
gi 1827387616 439 LLPEYMRPSAWVRLDAMPLSRSGKVDR 465
Cdd:cd17635 314 ELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
2574-3059 |
1.19e-23 |
|
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: 107.46 E-value: 1.19e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2574 AARRAPDHVAVVDGAGaRLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAE 2653
Cdd:cd05929 1 LEARDLDRAQVFHQRR-LLLLDVYSIALNRNARAAAAEGVWIADGVYIYLINSILTVFAAAAAWKCGACPAYKSSRAPRA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2654 RVASMIEDSGAVLGLSVLASGDLPGqefewmRLDDDsvAAEIAAVPAGPItDAERLGEvtaanlaYVIYTSGSTGRPKGV 2733
Cdd:cd05929 80 EACAIIEIKAAALVCGLFTGGGALD------GLEDY--EAAEGGSPETPI-EDEAAGW-------KMLYSGGTTGRPKGI 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2734 AVTHSGlanfarqesdrlNAGDNPVVLGFA---SPSFDASvleYLL---------ATVNEGTLAyrpseaVGGEV--LER 2799
Cdd:cd05929 144 KRGLPG------------GPPDNDTLMAAAlgfGPGADSV---YLSpaplyhaapFRWSMTALF------MGGTLvlMEK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2800 FIAE--------HGATHTFLTPSVLSTMD--PTAVP------SLR-VIAAGGE---AVPQPIVDRWAPAteLHNLYGPTE 2859
Cdd:cd05929 203 FDPEeflrlierYRVTFAQFVPTMFVRLLklPEAVRnaydlsSLKrVIHAAAPcppWVKEQWIDWGGPI--IWEYYGGTE 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2860 TtIGIT-ISSAMRPGDPVRLGGPIGGvDLMVLDERLRPVPVGMPGELYVAGGAlSRGYLDRSGLTAERFTANPYGTagqr 2938
Cdd:cd05929 281 G-QGLTiINGEEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFANGP-GFEYTNDPEKTAAARNEGGWST---- 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2939 myrTGDVVRWtpDTDtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-GGSVATALAAYIVPVDGA 3017
Cdd:cd05929 354 ---LGDVGYL--DED-GYLYL--TDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVpDEELGQRVHAVVQPAPGA 425
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1827387616 3018 VE----VSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05929 426 DAgtalAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1-470 |
1.25e-23 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 108.44 E-value: 1.25e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:PRK05852 44 ISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGE---AEARSRFDDI-VDVHVLDISSPGDADLDEEEFAGPTRPANA--------AFTLFTSGSTGRPKAVVITHRGIAN 148
Cdd:PRK05852 124 DGPhdrAEPTTRWWPLtVNVGGDSGPSGGTLSVHLDAATEPTPATSTpeglrpddAMIMFTGGTTGLPKMVPWTHANIAS 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 149 RLAADIEQYDLTARDVFLYKAPITFDVSVREIFLP-IAIGATLVIAEPGRHG-----DPVHLADLIRRHGVTVIHFVPAM 222
Cdd:PRK05852 204 SVRAIITGYRLSPRDATVAVMPLYHGHGLIAALLAtLASGGAVLLPARGRFSahtfwDDIKAVGATWYTAVPTIHQILLE 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 223 LAAfNEVLGAGVgelTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTIHRVTQDDR----VIPIGTPT 298
Cdd:PRK05852 284 RAA-TEPSGRKP---AALRFIRSCSAPLTAETAQALQTEF-AAPVVCAFGMTEATHQVTTTQIEGIGQtenpVVSTGLVG 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 299 RRVSA--RVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlyRTGDRARWNRDGEIEYLGRT 376
Cdd:PRK05852 359 RSTGAqiRIVGSDGLPLPAGAVGEVWLRGTTVVRGYLGDPTITAANFTDGWL--------RTGDLGSLSAAGDLSIRGRI 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 377 DFQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAP---ADVDVDTVAATTAELLPEYMRPSAWVRL 452
Cdd:PRK05852 431 KELINRGGEKISPERVEGVLASHPNVMEAAVfGVPDQLYGEAVAAVIVPresAPPTAEELVQFCRERLAAFEIPASFQEA 510
|
490
....*....|....*...
gi 1827387616 453 DAMPLSRSGKVDRRLLPE 470
Cdd:PRK05852 511 SGLPHTAKGSLDRRAVAE 528
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
2108-2535 |
1.27e-23 |
|
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: 106.68 E-value: 1.27e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2108 PMTPLQQGLFFQADLantvadHDAIDVYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPsGAAVTVVPAEVT 2187
Cdd:cd19533 3 PLTSAQRGVWFAEQL------DPEGSIYNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEE-GEPYQWIDPYTP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2188 VPWSVIDLRAEDAAslDSRVEEVLATERTNPFDMAKPPLIRVVLVEHGDGAELVVTN-HHLLIDGWSSPLVLADLLSLY- 2265
Cdd:cd19533 76 VPIRHIDLSGDPDP--EGAAQQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRvHHIVMDGFSFALFGQRVAEIYt 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2266 --ATGQTfTGSLPGTSGRDFADHARAVATADVEAGIAA-WREVLAPVTEPTLVAP-GHEPSADAPPRDHQFSIDVkvTER 2341
Cdd:cd19533 154 alLKGRP-APPAPFGSFLDLVEEEQAYRQSERFERDRAfWTEQFEDLPEPVSLARrAPGRSLAFLRRTAELPPEL--TRT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2342 LEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRSPdiEGMESMVGMFINTIPAVVDVNPDATVVDVLTAVQ 2421
Cdd:cd19533 231 LLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLG--AAARQTPGMVANTLPLRLTVDPQQTFAELVAQVS 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2422 NDKVKVLDHQQIGLPRLVAQTGLPA----LFDTLAVYESFP--VNVDSVAGIDASSAGGLklvgakTSDAThypLNLSAS 2495
Cdd:cd19533 309 RELRSLLRHQRYRYEDLRRDLGLTGelhpLFGPTVNYMPFDygLDFGGVVGLTHNLSSGP------TNDLS---IFVYDR 379
|
410 420 430 440
....*....|....*....|....*....|....*....|
gi 1827387616 2496 RRGAELALKLKYLPTAFAPEQVAVFADVLTGLLGAIADHP 2535
Cdd:cd19533 380 DDESGLRIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
2575-3059 |
1.67e-23 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 107.40 E-value: 1.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2575 ARRAPDHVAVVDG-AGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAE 2653
Cdd:PRK13390 7 AQIAPDRPAVIVAeTGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2654 RVASMIEDSGAVL--------GLSVLASGDLPgqefewMRLD-----DDSVAAEIAAVPAGPitdaeRLGEVTAAnlAYV 2720
Cdd:PRK13390 87 EADYIVGDSGARVlvasaaldGLAAKVGADLP------LRLSfggeiDGFGSFEAALAGAGP-----RLTEQPCG--AVM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2721 IYTSGSTGRPKGVAvthsglANFARQESDRlnAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPS--EAVGGEVL- 2797
Cdd:PRK13390 154 LYSSGTTGFPKGIQ------PDLPGRDVDA--PGDPIVAIARAFYDISESDIYYSSAPIYHAAPLRWCSmvHALGGTVVl 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2798 -ERFIAEHGATHTFLTPSVLSTMDPTA----------------VPSLRVIAAGGEAVP----QPIVDRWAPAteLHNLYG 2856
Cdd:PRK13390 226 aKRFDAQATLGHVERYRITVTQMVPTMfvrllkldadvrtrydVSSLRAVIHAAAPCPvdvkHAMIDWLGPI--VYEYYS 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2857 PTETTIGITISSAMRPGDPVRLGGPIGGvDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAE-RFTANPYgta 2935
Cdd:PRK13390 304 STEAHGMTFIDSPDWLAHPGSVGRSVLG-DLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPF--- 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2936 gqrmyrtgdvvrWTPDTDTGGLT----LEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG----GSVATAL 3007
Cdd:PRK13390 380 ------------WTTVGDLGSVDedgyLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPdpemGEQVKAV 447
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 3008 AAYIVPVDGAVEVS-ELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK13390 448 IQLVEGIRGSDELArELIDYTRSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
124-468 |
2.11e-23 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 107.91 E-value: 2.11e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 124 AFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPITFDVS-VREIFLPIAIGATLVIAEpgrHGDPV 202
Cdd:PRK06087 190 AAVLFTSGTEGLPKGVMLTHNNILASERAYCARLNLTWQDVFMMPAPLGHATGfLHGVTAPFLIGARSVLLD---IFTPD 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 203 HLADLIRRHGVTVIH----FVPAMLaafNEVLGAGVgELTSLRLIQTGGEALTPPVARDLMVRlpGTRLQNQYGPAEASi 278
Cdd:PRK06087 267 ACLALLEQQRCTCMLgatpFIYDLL---NLLEKQPA-DLSALRFFLCGGTTIPKKVARECQQR--GIKLLSVYGSTESS- 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 279 vvtIHRVTQDDRVIPI-----GTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepga 353
Cdd:PRK06087 340 ---PHAVVNLDDPLSRfmhtdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTARALDEEGW----- 411
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 354 rlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGPG---GQQLVGYLAPAD-VDV 429
Cdd:PRK06087 412 --YYSGDLCRMDEAGYIKITGRKKDIIVRGGENISSREVEDILLQHPKI--HDACVVAMPDerlGERSCAYVVLKApHHS 487
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 1827387616 430 DTVAATTAEL----LPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK06087 488 LTLEEVVAFFsrkrVAKYKYPEHIVVIDKLPRTASGKIQKFLL 530
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1-447 |
2.70e-23 |
|
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: 106.14 E-value: 2.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVts 80
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIYPTSSAEQIAYILNDSEAKALFV-- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 dgeaearsrfDDIVDVHVLdisspgdadldeeefagptrpanaaftLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:cd05907 84 ----------EDPDDLATI---------------------------IYTSGTTGRPKGVMLSHRNILSNALALAERLPAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPITFDVSVREI-FLPIAIGATLVIAEPgrhgDPVHLADLiRRHGVTVIHFVPAML-AAFNEVLGAGVGELT 238
Cdd:cd05907 127 EGDRHLSFLPLAHVFERRAGlYVPLLAGARIYFASS----AETLLDDL-SEVRPTVFLAVPRVWeKVYAAIKVKAVPGLK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 239 ----------SLRLIQTGGEALTPPVARdlMVRLPGTRLQNQYGPAEASIVVTIHRVtQDDRVIPIGTPTRRVSARvlda 308
Cdd:cd05907 202 rklfdlavggRLRFAASGGAPLPAELLH--FFRALGIPVYEGYGLTETSAVVTLNPP-GDNRIGTVGKPLPGVEVR---- 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 309 alrevpIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRT-DFQVKLRGQRL 387
Cdd:cd05907 275 ------IADDGEILVRGPNVMLGYYKNPEATAEALDADGW-------LHTGDLGEIDEDGFLHITGRKkDLIITSGGKNI 341
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 388 ELGEVEAALAAAPGVlhAAAAVVdgpgGQQLVGYLAPADVDVDTVAATTAELLPEYMRPS 447
Cdd:cd05907 342 SPEPIENALKASPLI--SQAVVI----GDGRPFLVALIVPDPEALEAWAEEHGIAYTDVA 395
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2108-2534 |
2.71e-23 |
|
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: 105.81 E-value: 2.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2108 PMTPLQQGLFFqadLANTVADHDAIDVYVtqtVLSLTGDVDPGRLRSALSELLARQRVLRSGFVrlpSGA--AVTVVPAE 2185
Cdd:cd20483 3 PMSTFQRRLWF---LHNFLEDKTFLNLLL---VCHIKGKPDVNLLQKALSELVRRHEVLRTAYF---EGDdfGEQQVLDD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2186 VTVPWSVIDL--RAEDAASLDSRVEEVlateRTNPFDMAKPPLIRVVLVE-HGDGAELVVTNHHLLIDGWSSPLVLADLL 2262
Cdd:cd20483 74 PSFHLIVIDLseAADPEAALDQLVRNL----RRQELDIEEGEVIRGWLVKlPDEEFALVLASHHIAWDRGSSKSIFEQFT 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2263 SLY----ATGQTFTGSLPGTSGRDFAD-HARAVATADVEAGIAAWREVL--APVTEPTLvapghePSA--DAPPRD---- 2329
Cdd:cd20483 150 ALYdalrAGRDLATVPPPPVQYIDFTLwHNALLQSPLVQPLLDFWKEKLegIPDASKLL------PFAkaERPPVKdyer 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2330 --HQFSIDVKVTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAeTVSGRSPDIEgMESMVGMFINTIPAVVDV 2407
Cdd:cd20483 224 stVEATLDKELLARMKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIG-MVDGDRPHPD-FDDLVGFFVNMLPIRCRM 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2408 NPDATVVDVLTAVQNDKVKVLDHQQIGLPRLVAQTGLPAlfDTlavyESFP-----VNVDSVAGIDASSAGGLKLVGAKT 2482
Cdd:cd20483 302 DCDMSFDDLLESTKTTCLEAYEHSAVPFDYIVDALDVPR--ST----SHFPigqiaVNYQVHGKFPEYDTGDFKFTDYDH 375
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 2483 SDA-THYPLNLSASRRGA-ELALKLKYLPTAFAPEQVAVFADV-LTGLLGAIADH 2534
Cdd:cd20483 376 YDIpTACDIALEAEEDPDgGLDLRLEFSTTLYDSADMERFLDNfVTFLTSVIRDH 430
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
2108-2439 |
3.17e-23 |
|
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: 105.81 E-value: 3.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2108 PMTPLQQGLFFQADLANTVAdhdaidVYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRsgfvrlpsgaavTVVPAEVT 2187
Cdd:cd19538 3 PLSFAQRRLWFLHQLEGPSA------TYNIPLVIKLKGKLDVQALQQALYDVVERHESLR------------TVFPEEDG 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2188 VPWSVIdlRAEDAASLD--------SRVEEVLATERTNPFDMAKPPLIRVVLVEHGDGAE-LVVTNHHLLIDGWS-SPLv 2257
Cdd:cd19538 65 VPYQLI--LEEDEATPKleikevdeEELESEINEAVRYPFDLSEEPPFRATLFELGENEHvLLLLLHHIAADGWSlAPL- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2258 LADLLSLY---ATGQT--FTgSLPgtsgRDFADHA---------RAVATADVEAGIAAWREVLApvteptlvapgHEPSA 2323
Cdd:cd19538 142 TRDLSKAYrarCKGEApeLA-PLP----VQYADYAlwqqellgdESDPDSLIARQLAYWKKQLA-----------GLPDE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2324 DAPPRDHQ-------------FSIDVKVTERLEALARNNSTTMATVVQFAWAMFLSRLTGTRTVTFAETVSGRSPDieGM 2390
Cdd:cd19538 206 IELPTDYPrpaessyeggtltFEIDSELHQQLLQLAKDNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDD--SL 283
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1827387616 2391 ESMVGMFINTIPAVVDVNPDATVVDVLTAVQNDKVKVLDHQQIGLPRLV 2439
Cdd:cd19538 284 EDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAYEHQDIPFERLV 332
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
572-914 |
5.13e-23 |
|
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis NocB which exhibits an unusual cyclization to form beta-lactam rings in pro-nocardicin G synthesis; Nocardia uniformis NRPS NocB acts centrally in the biosynthesis of the nocardicin monocyclic beta-lactam antibiotics. Along with another NRPS NocA, it mediates an unusual cyclization to form beta-lactam rings in the synthesis of the beta-lactam-containing pentapeptide pro-nocardicin G. This small subfamily is related to DCL-type Condensation (C) domains, which catalyze condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. NRPSs catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; domains belonging to this subfamily have an HHHxxxD motif at the active site.
Pssm-ID: 380469 [Multi-domain] Cd Length: 422 Bit Score: 105.09 E-value: 5.13e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 572 PLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYP-SVGAAPVQDVLP-VAVAREQL 649
Cdd:cd19547 3 PLAPMQEGMLFRGLFWPDSDAYFNQNVLELVGGTDEDVLREAWRRVADRYEILRTGFTwRDRAEPLQYVRDdLAPPWALL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 650 DW------READSVESLV---RSTTEGFDvstQMPL-RGRFHRDGAGLHVAL-TMHHIAMDGQSIPVLARDLMSAYAARA 718
Cdd:cd19547 83 DWsgedpdRRAELLERLLaddRAAGLSLA---DCPLyRLTLVRLGGGRHYLLwSHHHILLDGWCLSLIWGDVFRVYEELA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 719 EGRTGGL-PVLdvQYADYALWQQSVLGDADdetsvlgEQLSHWRRVLAGLPAV--TDLPMDRPrpavlgTAGATVTVEFD 795
Cdd:cd19547 160 HGREPQLsPCR--PYRDYVRWIRARTAQSE-------ESERFWREYLRDLTPSpfSTAPADRE------GEFDTVVHEFP 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 796 DDLADRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRnDPAL---EELIGMFVNTLLLRTQVDPGHSVg 872
Cdd:cd19547 225 EQLTRLVNEAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGR-PPELegsEHMVGIFINTIPLRIRLDPDQTV- 302
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1827387616 873 dllgnvrTTVLDAFANDqvqfdelieaLAPERSSSHQPLAQI 914
Cdd:cd19547 303 -------TGLLETIHRD----------LATTAAHGHVPLAQI 327
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1064-1530 |
6.38e-23 |
|
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: 104.35 E-value: 6.38e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVgitdast 1143
Cdd:cd05912 4 FAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSDVKL------- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1144 rarlgesscewvdladleaeaesgDDItdterngsvrltnlAYLIYTSGSTGRPKAVgvshtgIVDFVNSLA-----KIT 1218
Cdd:cd05912 77 ------------------------DDI--------------ATIMYTSGTTGKPKGV------QQTFGNHWWsaigsALN 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1219 TGTPEDepdTRILhVASPSFDASMFE-MAWAIPAGHTLVIAPQadFAGDALATVLERDEVTDMIITPSVL---ATVDPER 1294
Cdd:cd05912 113 LGLTED---DNWL-CALPLFHISGLSiLMRSVIYGMTVYLVDK--FDAEQVLHLINSGKVTIISVVPTMLqrlLEILGEG 186
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1295 AQY-VRNLATGGEACPPELVERWSERGRRIFNCYGPTEAT--VWATRSRMTAGKPVTIGKPVDGFTVRVLDgrlHEVPQG 1371
Cdd:cd05912 187 YPNnLRCILLGGGPAPKPLLEQCKEKGIPVYQSYGMTETCsqIVTLSPEDALNKIGSAGKPLFPVELKIED---DGQPPY 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1372 VVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmyATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVL 1451
Cdd:cd05912 264 EVGEILLKGPNVTKGYLNRPDATEESFENGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPAEIEEVL 335
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1452 DAQPGVAQSVVVGVESTRGGrkhtEV-VAYLVAKpgATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd05912 336 LSHPAIKEAGVVGIPDDKWG----QVpVAFVVSE--RPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
2-468 |
6.71e-23 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 105.92 E-value: 6.71e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSD 81
Cdd:PRK08008 39 SYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVPINARLLREESAWILQNSQASLLVTSAQ 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 G-------EAEARSRFDDIVDVHVLDISSPGDADLDEE--------EFAGPTRPANAAFTLFTSGSTGRPKAVVITHrgi 146
Cdd:PRK08008 119 FypmyrqiQQEDATPLRHICLTRVALPADDGVSSFTQLkaqqpatlCYAPPLSTDDTAEILFTSGTTSRPKGVVITH--- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 147 ANRLAADIE---QYDLTARDVFLYKAP---ITFDVSVReifLPI-AIGATLVIAE--PGRHgdpvhLADLIRRHGVTVIH 217
Cdd:PRK08008 196 YNLRFAGYYsawQCALRDDDVYLTVMPafhIDCQCTAA---MAAfSAGATFVLLEkySARA-----FWGQVCKYRATITE 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 218 FVPAMLAAFnevlgagvgeltslrliqtggeALTPPVA-------RDLMVRLP-------------GTRLQNQYGPAEaS 277
Cdd:PRK08008 268 CIPMMIRTL----------------------MVQPPSAndrqhclREVMFYLNlsdqekdafeerfGVRLLTSYGMTE-T 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 278 IVVTIHRVTQDDRVIP-IGTPTRRVSARVLDAALREVPIGVPGELYLGGV---QLARGYAGRPDLTAERFvadpfgEPGA 353
Cdd:PRK08008 325 IVGIIGDRPGDKRRWPsIGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFKEYYLDPKATAKVL------EADG 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 354 RLYrTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGPGGQQLVG---YLAP-ADVDV 429
Cdd:PRK08008 399 WLH-TGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIKDSIRDEAIKafvVLNEgETLSE 477
|
490 500 510
....*....|....*....|....*....|....*....
gi 1827387616 430 DTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK08008 478 EEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1-375 |
7.67e-23 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 106.34 E-value: 7.67e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVtS 80
Cdd:COG1022 41 LTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVPIYPTSSAEEVAYILNDSGAKVLFV-E 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGE-----AEARSRFDDIVDVHVLD---------------ISSPGDADLDEEEFAGPTRPANAA--FTL-FTSGSTGRPK 137
Cdd:COG1022 120 DQEqldklLEVRDELPSLRHIVVLDprglrddprllsldeLLALGREVADPAELEARRAAVKPDdlATIiYTSGTTGRPK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 138 AVVITHRGIANRLAADIEQYDLTARDVFLykapitfdvsvreIFLP-------------IAIGATLVIAEpgrhgDPVHL 204
Cdd:COG1022 200 GVMLTHRNLLSNARALLERLPLGPGDRTL-------------SFLPlahvfertvsyyaLAAGATVAFAE-----SPDTL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 205 ADLIRRHGVTVIHFVPAML-------------------AAFNEVLGAGV--------GELTS------------------ 239
Cdd:COG1022 262 AEDLREVKPTFMLAVPRVWekvyagiqakaeeagglkrKLFRWALAVGRryararlaGKSPSlllrlkhaladklvfskl 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 240 -------LRLIQTGGEALTPPVARdlMVRLPGTRLQNQYGPAEASIVVTIHRvtqDDRVIP--IGTPTRRVsarvldaal 310
Cdd:COG1022 342 realggrLRFAVSGGAALGPELAR--FFRALGIPVLEGYGLTETSPVITVNR---PGDNRIgtVGPPLPGV--------- 407
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 311 rEVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGR 375
Cdd:COG1022 408 -EVKIAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW-------LHTGDIGELDEDGFLRITGR 464
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
2590-3013 |
9.82e-23 |
|
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: 104.75 E-value: 9.82e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2590 ARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLGLs 2669
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALV- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2670 vlasgdlpgqefewmrLDDDSvaaeiaavpagpitdaerlgevtaANLAYVIYTSGSTGRPKGVAVTHsglANFARQESd 2749
Cdd:cd17640 83 ----------------VENDS------------------------DDLATIIYTSGTTGNPKGVMLTH---ANLLHQIR- 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2750 rlnagdnpvvlgfaspsfdaSVLEYLLATVNEGTLAYRPSEAVGGEVLERFIAEHGATHTFLTPSVLS----TMDPT--- 2822
Cdd:cd17640 119 --------------------SLSDIVPPQPGDRFLSILPIWHSYERSAEYFIFACGCSQAYTSIRTLKddlkRVKPHyiv 178
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2823 AVPSL--------------------------------RVIAAGGEAVPqPIVDRWAPAT--ELHNLYGPTETTigiTISS 2868
Cdd:cd17640 179 SVPRLweslysgiqkqvsksspikqflflfflsggifKFGISGGGALP-PHVDTFFEAIgiEVLNGYGLTETS---PVVS 254
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2869 AMRPGDPVR--LGGPIGGVDLMVLDERLR-PVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDV 2945
Cdd:cd17640 255 ARRLKCNVRgsVGRPLPGTEIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDL 327
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 2946 VRWTPDTDtggltLEYTGRSDDQVKLR-GLRIELGEIEAVLAEHDAVESAVVLgvgGSVATALAAYIVP 3013
Cdd:cd17640 328 GWLTCGGE-----LVLTGRAKDTIVLSnGENVEPQPIEEALMRSPFIEQIMVV---GQDQKRLGALIVP 388
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
2564-3059 |
1.40e-22 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 105.73 E-value: 1.40e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2564 PVTLAELFRAAARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGay 2643
Cdd:PRK08279 36 KRSLGDVFEEAAARHPDRPALLFE-DQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGA-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2644 vpidpdypaerVASMIEDS--GAVLG--LSVL-----------------ASGDLPGQEFEWM--------RLDDDSVAAE 2694
Cdd:PRK08279 113 -----------VVALLNTQqrGAVLAhsLNLVdakhlivgeelveafeeARADLARPPRLWVaggdtlddPEGYEDLAAA 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2695 IAAVPAGPITDAERlgeVTAANLAYVIYTSGSTGRPKGVAVTH-------SGLANFAR-QESDRL--------NAGDNpV 2758
Cdd:PRK08279 182 AAGAPTTNPASRSG---VTAKDTAFYIYTSGTTGLPKAAVMSHmrwlkamGGFGGLLRlTPDDVLycclplyhNTGGT-V 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2759 VLGfaspsfdaSVLeyllatVNEGTLAYRPSEAVGgevleRF---IAEHGATH--------TFLTPSVLSTMDptAVPSL 2827
Cdd:PRK08279 258 AWS--------SVL------AAGATLALRRKFSAS-----RFwddVRRYRATAfqyigelcRYLLNQPPKPTD--RDHRL 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2828 RVIAAGGE------------AVPQpIVDRWApATE----LHNLYGpTETTIGITISSAMRP----------GDPVRlgGP 2881
Cdd:PRK08279 317 RLMIGNGLrpdiwdefqqrfGIPR-ILEFYA-ASEgnvgFINVFN-FDGTVGRVPLWLAHPyaivkydvdtGEPVR--DA 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2882 IGgvdlmvldeRLRPVPVGMPGELYVAGGALSR--GYLDRSGlTAERFTANPYgTAGQRMYRTGDVVRwtpdtDTGGLTL 2959
Cdd:PRK08279 392 DG---------RCIKVKPGEVGLLIGRITDRGPfdGYTDPEA-SEKKILRDVF-KKGDAWFNTGDLMR-----DDGFGHA 455
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2960 EYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV--GGSVATALAAYIVPVDGA-VEVSELKAFAGGRLPAYMV 3036
Cdd:PRK08279 456 QFVDRLGDTFRWKGENVATTEVENALSGFPGVEEAVVYGVevPGTDGRAGMAAIVLADGAeFDLAALAAHLYERLPAYAV 535
|
570 580
....*....|....*....|...
gi 1827387616 3037 PSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK08279 536 PLFVRLVPELETTGTFKYRKVDL 558
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1051-1527 |
1.62e-22 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 104.98 E-value: 1.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1051 DHPALICDGTEMD----YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIA 1126
Cdd:PRK04319 59 DKVALRYLDASRKekytYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1127 YMLEDSGATVGITDASTRARL--------------GESSCEWVDLADLEAEAESGDDITDTErngSVRLTNLAYLIYTSG 1192
Cdd:PRK04319 139 DRLEDSEAKVLITTPALLERKpaddlpslkhvllvGEDVEEGPGTLDFNALMEQASDEFDIE---WTDREDGAILHYTSG 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1193 STGRPKAVGVSHTGIVdfvnsLAKITTGTPED-EPDTRILHVASPSFDASMfemAWAIPA----GHTLVIApQADFAGDA 1267
Cdd:PRK04319 216 STGKPKGVLHVHNAML-----QHYQTGKYVLDlHEDDVYWCTADPGWVTGT---SYGIFApwlnGATNVID-GGRFSPER 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1268 LATVLERDEVTDMIITPSVL-----ATVDPeRAQY----VRNLATGGEACPPELVeRWSER--GRRIFNCYGPTEatvwa 1336
Cdd:PRK04319 287 WYRILEDYKVTVWYTAPTAIrmlmgAGDDL-VKKYdlssLRHILSVGEPLNPEVV-RWGMKvfGLPIHDNWWMTE----- 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1337 TRSRMTAG------KPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTA--GLARGYLGRPGQTAVSFVADpfgepga 1408
Cdd:PRK04319 360 TGGIMIANypamdiKPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGwpSMMRGIWNNPEKYESYFAGD------- 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1409 rMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGV-ESTRGgrkhtEVV-AYLVAKPG 1486
Cdd:PRK04319 433 -WYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKpDPVRG-----EIIkAFVALRPG 506
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1827387616 1487 ATIDSA---AVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDR 1527
Cdd:PRK04319 507 YEPSEElkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMR 550
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
2566-3059 |
2.01e-22 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 104.09 E-value: 2.01e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDGAgARLTYRELDEASDRLARWLIGRGVGPERaVALAIGRSAQLLTAIWAVAKTGGAYVP 2645
Cdd:PRK07638 2 GITKEYKKHASLQPNKIAIKEND-RVLTYKDWFESVCKVANWLNEKESKNKT-IAILLENRIEFLQLFAGAAMAGWTCVP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2646 IDPDY-PAERVASMIEDSGAVLGLSVLASGDLPGQEF------EWMRLdddsvaAEIAAVPAGPITDAERlgevtaaNLA 2718
Cdd:PRK07638 80 LDIKWkQDELKERLAISNADMIVTERYKLNDLPDEEGrvieidEWKRM------IEKYLPTYAPIENVQN-------APF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2719 YVIYTSGSTGRPKGVAVTH-SGLANFARQESD-RLNAGDNPVVLGFASPSFdasvleYLLATVNegTLAyrpseaVGGEV 2796
Cdd:PRK07638 147 YMGFTSGSTGKPKAFLRAQqSWLHSFDCNVHDfHMKREDSVLIAGTLVHSL------FLYGAIS--TLY------VGQTV 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2797 -LERFIAEHGATHTFLTP--SVLSTMdPTAVPSL-----------RVIAAGG----EAVPQpIVDRWaPATELHNLYGPT 2858
Cdd:PRK07638 213 hLMRKFIPNQVLDKLETEniSVMYTV-PTMLESLykenrvienkmKIISSGAkweaEAKEK-IKNIF-PYAKLYEFYGAS 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2859 EttigITISSAMRPGD----PVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDrsgltaerftanpygt 2934
Cdd:PRK07638 290 E----LSFVTALVDEEserrPNSVGRPFHNVQVRICNEAGEEVQKGEIGTVYVKSPQFFMGYII---------------- 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2935 aGQRMYRTGDVVRWTPDTDTGGLTLE----YTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG----GSVATA 3006
Cdd:PRK07638 350 -GGVLARELNADGWMTVRDVGYEDEEgfiyIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPdsywGEKPVA 428
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 3007 LaayivpVDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK07638 429 I------IKGSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIARMEA 475
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1066-1479 |
2.64e-22 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 104.50 E-value: 2.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1066 EFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDASTRA 1145
Cdd:PLN02860 37 EFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLLVRPVMLVTDETCSS 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1146 ---RLGESSC---EWVDLADLEAEAESGDDI----TDTERNGSVRLTNLAY--------LI-YTSGSTGRPKAVGVSHTG 1206
Cdd:PLN02860 117 wyeELQNDRLpslMWQVFLESPSSSVFIFLNsfltTEMLKQRALGTTELDYawapddavLIcFTSGTTGRPKGVTISHSA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1207 IVdfVNSLAKIT-TGTPEDEPdtrILHVAsPSFDASMFEMAWAI-PAGHTLVIAPQadFAGDALATVLERDEVTDMIITP 1284
Cdd:PLN02860 197 LI--VQSLAKIAiVGYGEDDV---YLHTA-PLCHIGGLSSALAMlMVGACHVLLPK--FDAKAALQAIKQHNVTSMITVP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1285 SVLAT-VDPERA-------QYVRNLATGGEACPPELVERWSE--RGRRIFNCYGPTEATvwATRSRMTAGKPVTIGKPVD 1354
Cdd:PLN02860 269 AMMADlISLTRKsmtwkvfPSVRKILNGGGSLSSRLLPDAKKlfPNAKLFSAYGMTEAC--SSLTFMTLHDPTLESPKQT 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1355 GFTVRVLDGRLHEVPQGV-VG------ELYL-----STAG--LARG------YLGRPGQTAVSFVADPFgepgarmYATG 1414
Cdd:PLN02860 347 LQTVNQTKSSSVHQPQGVcVGkpaphvELKIgldesSRVGriLTRGphvmlgYWGQNSETASVLSNDGW-------LDTG 419
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 1415 DLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVA 1479
Cdd:PLN02860 420 DIGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEM---VVA 481
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1183-1530 |
3.90e-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: 341266 [Multi-domain] Cd Length: 359 Bit Score: 101.02 E-value: 3.90e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1183 NLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtrILHVASPSF--DASMFEMAWAIPAGHTLVIAPQ 1260
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDD-----VLLCGLPLFhvNGSVVTLLTPLASGAHVVLAGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1261 ADFAGDALA----TVLERDEVTDMIITPSVLATV--DPERAQY--VRNLATGGEACPPELVERWSER-GRRIFNCYGPTE 1331
Cdd:cd05944 78 AGYRNPGLFdnfwKLVERYRITSLSTVPTVYAALlqVPVNADIssLRFAMSGAAPLPVELRARFEDAtGLPVVEGYGLTE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1332 ATVWATRS-RMTAGKPVTIGKPVDGFTVR--VLDGRLH---EVPQGVVGELYLSTAGLARGYLGRPGQTavsfvaDPFGE 1405
Cdd:cd05944 158 ATCLVAVNpPDGPKRPGSVGLRLPYARVRikVLDGVGRllrDCAPDEVGEICVAGPGVFGGYLYTEGNK------NAFVA 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1406 PGarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEV-VAYLVAK 1484
Cdd:cd05944 232 DG--WLNTGDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAG----ELpVAYVQLK 305
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1827387616 1485 PGATIDSAAVLDEAAQHLAAH-MVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd05944 306 PGAVVEEEELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
2569-3059 |
4.44e-22 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 103.69 E-value: 4.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2569 ELFRAAARRAPDHVAVVDgAGARLTYRELDEASDRLARWLIGR-GVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPID 2647
Cdd:PRK05677 28 AVLKQSCQRFADKPAFSN-LGKTLTYGELYKLSGAFAAWLQQHtDLKPGDRIAVQLPNVLQYPVAVFGAMRAGLIVVNTN 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2648 PDYPAERVASMIEDSGA-----VLGLSVLASGDLPGQEFEWM-------------RLDDDSVAAEIAA-VPAGPITDAER 2708
Cdd:PRK05677 107 PLYTAREMEHQFNDSGAkalvcLANMAHLAEKVLPKTGVKHVivtevadmlpplkRLLINAVVKHVKKmVPAYHLPQAVK 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2709 LGEVTA--------------ANLAYVIYTSGSTGRPKGVAVTHSGL-ANFARQES---DRLNAGDNPVVlgfaSP----- 2765
Cdd:PRK05677 187 FNDALAkgagqpvteanpqaDDVAVLQYTGGTTGVAKGAMLTHRNLvANMLQCRAlmgSNLNEGCEILI----APlplyh 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2766 --SFDASVLEYLLaTVNEGTLAYRPSEaVGGEVLE----RFIAEHGATHTFLTPSVLSTMDPTAVPSLRVIAAGGEAVPQ 2839
Cdd:PRK05677 263 iyAFTFHCMAMML-IGNHNILISNPRD-LPAMVKElgkwKFSGFVGLNTLFVALCNNEAFRKLDFSALKLTLSGGMALQL 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2840 PIVDRWAPAT--ELHNLYGPTETTIGITIS--SAMRPGDpvrLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRG 2915
Cdd:PRK05677 341 ATAERWKEVTgcAICEGYGMTETSPVVSVNpsQAIQVGT---IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKG 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2916 YLDRSGLTAERFTANPYgtagqrmYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAV 2995
Cdd:PRK05677 418 YWQRPEATDEILDSDGW-------LKTGDIALIQEDG-----YMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCA 485
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 2996 VLGV-GGSVATALAAYIVPVDG-AVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK05677 486 AIGVpDEKSGEAIKVFVVVKPGeTLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2144-2535 |
4.48e-22 |
|
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: 102.01 E-value: 4.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2144 TGDVDPGRLRSALSELLARQRVLRSGFVRlpsgaaVTVVPAEVTVPWSVIDLRAEDAASLDSrvEEVLATERTN---PFD 2220
Cdd:cd20484 33 SSKLDVEKFKQACQFVLEQHPILKSVIEE------EDGVPFQKIEPSKPLSFQEEDISSLKE--SEIIAYLREKakePFV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2221 MAKPPLIRVVLVEHGdGAE--LVVTNHHLLIDGWSSPLVLADLLSLYAT---GQTFTGSLPGTSGRDFAD-HARAVATAD 2294
Cdd:cd20484 105 LENGPLMRVHLFSRS-EQEhfVLITIHHIIFDGSSSLTLIHSLLDAYQAllqGKQPTLASSPASYYDFVAwEQDMLAGAE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2295 VEAGIAAWREVLAPvTEPTLVAPGHEPSADAPP---RDHQFSIDVKVTERLEALARNNSTTMATVVQFAWAMFLSRLTGT 2371
Cdd:cd20484 184 GEEHRAYWKQQLSG-TLPILELPADRPRSSAPSfegQTYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLLHRYTGQ 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2372 RTVTFAETVSGRSPdiEGMESMVGMFINTIPAVVDVNPDATVVDVLTAVQNDKVKVLDHQQIGLPRLVAQTGLP------ 2445
Cdd:cd20484 263 EDIIVGMPTMGRPE--ERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLNIPrsqans 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2446 ALFDTLAVYESFpvnvdsvagidaSSAGGLKLVGAKTSDATH------------YPLNLSASRRGAELALKLKYLPTAFA 2513
Cdd:cd20484 341 PVFQVAFFYQNF------------LQSTSLQQFLAEYQDVLSiefvegihqegeYELVLEVYEQEDRFTLNIKYNPDLFD 408
|
410 420
....*....|....*....|..
gi 1827387616 2514 PEQVAVFADVLTGLLGAIADHP 2535
Cdd:cd20484 409 ASTIERMMEHYVKLAEELIANP 430
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1-465 |
5.04e-22 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 103.31 E-value: 5.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDeqlPVDRAR---YMVRTAGVRLVV 77
Cdd:PRK12583 46 YTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNIN---PAYRASeleYALGQSGVRWVI 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 78 V-----TSD----------------GEAEARSRFDDIVDVHVLDISSPG----------------DADLDEEEfaGPTRP 120
Cdd:PRK12583 123 CadafkTSDyhamlqellpglaegqPGALACERLPELRGVVSLAPAPPPgflawhelqargetvsREALAERQ--ASLDR 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 121 ANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPI--TFDVsVREIFLPIAIGATLVIaePGRH 198
Cdd:PRK12583 201 DDPINIQYTSGTTGFPKGATLSHHNILNNGYFVAESLGLTEHDRLCVPVPLyhCFGM-VLANLGCMTVGACLVY--PNEA 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 199 GDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASI 278
Cdd:PRK12583 278 FDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFDLSSLRTGIMAGAPCPIEVMRRVMDEMHMAEVQIAYGMTETSP 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 279 VvtIHRVTQDD----RVIPIGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgar 354
Cdd:PRK12583 358 V--SLQTTAADdlerRVETVGRTQPHLEVKVVDPDGATVPRGEIGELCTRGYSVMKGYWNNPEATAESIDEDGW------ 429
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 355 lYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGPG---GQQLVGY--LAPADvdv 429
Cdd:PRK12583 430 -MHTGDLATMDEQGYVRIVGRSKDMIIRGGENIYPREIEEFLFTHPAV--ADVQVFGVPDekyGEEIVAWvrLHPGH--- 503
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 1827387616 430 dtvAATTAEL------------LPEYMRpsawvRLDAMPLSRSGKVDR 465
Cdd:PRK12583 504 ---AASEEELrefckariahfkVPRYFR-----FVDEFPMTVTGKVQK 543
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
5-468 |
5.37e-22 |
|
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: 103.72 E-value: 5.37e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 5 EFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLvVVTSDG-- 82
Cdd:cd05968 96 ELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKA-LITADGft 174
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 83 ----------EAEARSRFDDIVDvHVL--------DISSPGDADLDEEEFAGP------TRPANAAFTLFTSGSTGRPKA 138
Cdd:cd05968 175 rrgrevnlkeEADKACAQCPTVE-KVVvvrhlgndFTPAKGRDLSYDEEKETAgdgaerTESEDPLMIIYTSGTTGKPKG 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 139 VVITHRGIANRLAADIE-QYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAE--PGrHGDPVHLADLIRRHGVTV 215
Cdd:cd05968 254 TVHVHAGFPLKAAQDMYfQFDLKPGDLLTWFTDLGWMMGPWLIFGGLILGATMVLYDgaPD-HPKADRLWRMVEDHEITH 332
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 216 IHFVPAMLAAFNEVLGAGVG--ELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQ--NQYGPAEASIVVTIHRVTQDDRV 291
Cdd:cd05968 333 LGLSPTLIRALKPRGDAPVNahDLSSLRVLGSTGEPWNPEPWNWLFETVGKGRNPiiNYSGGTEISGGILGNVLIKPIKP 412
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 292 IPIGTPTRRVSARVLDAALREVPIGVpGELYLGG--VQLARGYAGRPDltaeRFVaDPFGEPGARLYRTGDRARWNRDGE 369
Cdd:cd05968 413 SSFNGPVPGMKADVLDESGKPARPEV-GELVLLApwPGMTRGFWRDED----RYL-ETYWSRFDNVWVHGDFAYYDEEGY 486
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 370 IEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGP-GGQQLVGY------LAPADVDVDTVAATTAELLPE 442
Cdd:cd05968 487 FYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIGVPHPvKGEAIVCFvvlkpgVTPTEALAEELMERVADELGK 566
|
490 500
....*....|....*....|....*.
gi 1827387616 443 YMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd05968 567 PLSPERILFVKDLPKTRNAKVMRRVI 592
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
2143-2445 |
7.25e-22 |
|
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: 101.38 E-value: 7.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2143 LTGDVDPGRLRSALSELLARQRVLRSGF-VRLPSGAAVTVVPAEvtvpwSVIDLRAEDAASlDSRVEEVLATERTNPFDM 2221
Cdd:cd19532 32 LTGPLDVARLERAVRAVGQRHEALRTCFfTDPEDGEPMQGVLAS-----SPLRLEHVQISD-EAEVEEEFERLKNHVYDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2222 AKPPLIRVVLVEHGDGA-ELVVTNHHLLIDGWSSPLVLADLLSLYAtGQTftgSLPGTSG-RDFADHARavatADVEAG- 2298
Cdd:cd19532 106 ESGETMRIVLLSLSPTEhYLIFGYHHIAMDGVSFQIFLRDLERAYN-GQP---LLPPPLQyLDFAARQR----QDYESGa 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2299 ----IAAWREVLAPVTE--PTLvapghePSADAPPR------DH---QFSIDVKVTERLEALARNNSttmATVVQF---A 2360
Cdd:cd19532 178 ldedLAYWKSEFSTLPEplPLL------PFAKVKSRppltryDThtaERRLDAALAARIKEASRKLR---VTPFHFylaA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2361 WAMFLSRLTGTRTVTFAETVSGRSPdiEGMESMVGMFINTIPAVVDVNPDATVVDVLTAVQnDKV-KVLDHQQIGLPRLV 2439
Cdd:cd19532 249 LQVLLARLLDVDDICIGIADANRTD--EDFMETIGFFLNLLPLRFRRDPSQTFADVLKETR-DKAyAALAHSRVPFDVLL 325
|
....*.
gi 1827387616 2440 AQTGLP 2445
Cdd:cd19532 326 DELGVP 331
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
2720-3056 |
8.18e-22 |
|
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: 99.65 E-value: 8.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2720 VIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGfASPSFDASVLEYLLATVNEGTL-----AYRPSEAVgg 2794
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLIAANLQLIHAMGLTEADVYLN-MLPLFHIAGLNLALATFHAGGAnvvmeKFDPAEAL-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2795 evleRFIAEHGATHTFLTPSVLSTM------DPTAVPSLRVIAagGEAVPQPIvDRW---APATeLHNLYGPTETTIGIT 2865
Cdd:cd17637 82 ----ELIEEEKVTLMGSFPPILSNLldaaekSGVDLSSLRHVL--GLDAPETI-QRFeetTGAT-FWSLYGQTETSGLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2866 ISSAM-RPGDPvrlGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANpygtagqrMYRTGD 2944
Cdd:cd17637 154 LSPYReRPGSA---GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG--------WHHTGD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2945 VVRWtpdtDTGGLtLEYTGRS--DDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVAT-ALAAYIVPVDGA-VEV 3020
Cdd:cd17637 223 LGRF----DEDGY-LWYAGRKpeKELIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDPKWGeGIKAVCVLKPGAtLTA 297
|
330 340 350
....*....|....*....|....*....|....*.
gi 1827387616 3021 SELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDK 3056
Cdd:cd17637 298 DELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
590-996 |
9.42e-22 |
|
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond forming Fusarium verticillioides FUM14 protein; Condensation (C) domains of nonribosomal peptide synthetases (NRPSs) typically catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. However, some C-domains have ester-bond forming activity. This subfamily includes Fusarium verticillioides FUM14 (also known as NRPS8), a bi-domain protein with an ester-bond forming NRPS C-domain, which catalyzes linkages between an aminoacyl/peptidyl-PCP donor and a hydroxyl-containing acceptor. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity. FUM14 has an altered active site motif DHTHCD instead of the typical HHxxxD motif seen in other subfamily members. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380467 [Multi-domain] Cd Length: 395 Bit Score: 100.45 E-value: 9.42e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 590 SGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVY-PSVGAAPVQdvlpVAVAREQLDWREADSVESLVRSttegf 668
Cdd:cd19545 19 PGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQ----VVVKESPISWTESTSLDEYLEE----- 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 669 DVSTQMPLRGRFHR------DGAGLHVALTMHHIAMDGQSIPVLARDLMSAYAARAEGRTgglpvldVQYADYalwqQSV 742
Cdd:cd19545 90 DRAAPMGLGGPLVRlalvedPDTERYFVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQP-------PPFSRF----VKY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 743 LGDADDETSVlgeqlSHWRRVLAGLpAVTDLPMDrPRPAVLGTAGATVTVEfdddladrvdVLARSNTMTGFMVTE---A 819
Cdd:cd19545 159 LRQLDDEAAA-----EFWRSYLAGL-DPAVFPPL-PSSRYQPRPDATLEHS----------ISLPSSASSGVTLATvlrA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 820 AFAATVARLASTTDVVIGTPVAGRNDPA--LEELIGMFVNTLLLRTQVDPGHSVGDLLGNVRTTVLDA--FANDQVQfde 895
Cdd:cd19545 222 AWALVLSRYTGSDDVVFGVTLSGRNAPVpgIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDMipFEHTGLQ--- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 896 LIEALAPErsSSHQPLAQ--IAFTYTEPTVND---VAGLEASGIQAAPVDTgvvnakFDLTVAVRARSGGtpMAADFIYA 970
Cdd:cd19545 299 NIRRLGPD--ARAACNFQtlLVVQPALPSSTSeslELGIEEESEDLEDFSS------YGLTLECQLSGSG--LRVRARYD 368
|
410 420
....*....|....*....|....*.
gi 1827387616 971 TDLFDESTVKRFAEVYRRVLQAIVDD 996
Cdd:cd19545 369 SSVISEEQVERLLDQFEHVLQQLASA 394
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1064-1464 |
1.11e-21 |
|
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: 101.67 E-value: 1.11e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDast 1143
Cdd:cd17640 8 YKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVE--- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1144 rarlgesscewvdladleaeaESGDDItdterngsvrltnlAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPE 1223
Cdd:cd17640 85 ---------------------NDSDDL--------------ATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1224 DepdtRILHVASP--SFD--ASMFEMAWAIPAGHTLVIAPQADFAgdalatvlerdevtdmIITPSVLATV--------- 1290
Cdd:cd17640 130 D----RFLSILPIwhSYErsAEYFIFACGCSQAYTSIRTLKDDLK----------------RVKPHYIVSVprlweslys 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1291 ---------DPERAQYVRNLATGGE---------ACPPELVERWSERGRRIFNCYGPTEATVWATRSRMTAGKPVTIGKP 1352
Cdd:cd17640 190 giqkqvsksSPIKQFLFLFFLSGGIfkfgisgggALPPHVDTFFEAIGIEVLNGYGLTETSPVVSARRLKCNVRGSVGRP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1353 VDGFTVRVLDGRLHEV-PQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRVAKGGNLEFAGRA 1431
Cdd:cd17640 270 LPGTEIKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLGWLTCGGELVLTGRA 342
|
410 420 430
....*....|....*....|....*....|....
gi 1827387616 1432 -DHQVKINGQRVELGEIEAVLDAQPGVAQSVVVG 1464
Cdd:cd17640 343 kDTIVLSNGENVEPQPIEEALMRSPFIEQIMVVG 376
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1050-1532 |
1.45e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 102.03 E-value: 1.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:PRK06710 38 PEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQL 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATV---------GITDASTRARLGESSCEWV-----------------DLADLEAEAESGDDI-----TDTERNGS 1178
Cdd:PRK06710 118 HDSGAKVilcldlvfpRVTNVQSATKIEHVIVTRIadflpfpknllypfvqkKQSNLVVKVSESETIhlwnsVEKEVNTG 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1179 VRL-----TNLAYLIYTSGSTGRPKAVGVSHTGIVDfvNSLAKITTGTPEDEPDTRILHVAsPSFDASMFE--MAWAIPA 1251
Cdd:PRK06710 198 VEVpcdpeNDLALLQYTGGTTGFPKGVMLTHKNLVS--NTLMGVQWLYNCKEGEEVVLGVL-PFFHVYGMTavMNLSIMQ 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1252 GHTLVIAPQADFagDALATVLERDEVTDMIITPSVLATV--DPERAQY----VRNLATGGEACPPELVERWSE-RGRRIF 1324
Cdd:PRK06710 275 GYKMVLIPKFDM--KMVFEAIKKHKVTLFPGAPTIYIALlnSPLLKEYdissIRACISGSAPLPVEVQEKFETvTGGKLV 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1325 NCYGPTEAT-------VWATRSrmtagkPVTIGKPVDGFTVRVLDGRLHEV-PQGVVGELYLSTAGLARGYLGRPGQTAv 1396
Cdd:PRK06710 353 EGYGLTESSpvthsnfLWEKRV------PGSIGVPWPDTEAMIMSLETGEAlPPGEIGEIVVKGPQIMKGYWNKPEETA- 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1397 SFVADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhte 1476
Cdd:PRK06710 426 AVLQDGW-------LHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPYRGET--- 495
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 1477 VVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:PRK06710 496 VKAFVVLKEGTECSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIE 551
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
97-468 |
1.97e-21 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 101.61 E-value: 1.97e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 97 HVLDISSPGDADLDE------EEF-AGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFL--Y 167
Cdd:PRK10946 151 VVLLLNDDGEHSLDDainhpaEDFtATPSPADEVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTPQTRYLcaL 230
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 168 KAPITFDVSVreiflPIAIGA-----TLVIA-EPGrhgdPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVG--ELTS 239
Cdd:PRK10946 231 PAAHNYPMSS-----PGALGVflaggTVVLApDPS----ATLCFPLIEKHQVNVTALVPPAVSLWLQAIAEGGSraQLAS 301
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 240 LRLIQTGGEALTPPVARdlmvRLP---GTRLQNQYGPAEAsiVVTIHRVTQDDRVIpIGTPTRRVS----ARVLDAALRE 312
Cdd:PRK10946 302 LKLLQVGGARLSETLAR----RIPaelGCQLQQVFGMAEG--LVNYTRLDDSDERI-FTTQGRPMSpddeVWVADADGNP 374
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 313 VPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEV 392
Cdd:PRK10946 375 LPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEI 447
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 393 EAALAAAPGVLHAA-AAVVDGPGGQQLVGYLAPADvDVDTVAATT---AELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK10946 448 ENLLLRHPAVIHAAlVSMEDELMGEKSCAFLVVKE-PLKAVQLRRflrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
5-465 |
3.83e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 100.24 E-value: 3.83e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 5 EFDRRVTGLARELTALGvGAEVAVGIQIDRSVE--QVVAihAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVtsdg 82
Cdd:PRK07638 31 DWFESVCKVANWLNEKE-SKNKTIAILLENRIEflQLFA--GAAMAGWTCVPLDIKWKQDELKERLAISNADMIVT---- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 83 EAEARSRFDDiVDVHVLDISS-PGDADLDEEEFAGPTRPANAAFTL-FTSGSTGRPKAVVITHRGIANRLAADIEQYDLT 160
Cdd:PRK07638 104 ERYKLNDLPD-EEGRVIEIDEwKRMIEKYLPTYAPIENVQNAPFYMgFTSGSTGKPKAFLRAQQSWLHSFDCNVHDFHMK 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARD-----------VFLYKApitfdvsVREIFlpiaIGATLVIAepgRHGDPVHLADLIRRHGVTVIHFVPAMLAAF--- 226
Cdd:PRK07638 183 REDsvliagtlvhsLFLYGA-------ISTLY----VGQTVHLM---RKFIPNQVLDKLETENISVMYTVPTMLESLyke 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 227 NEVLGagvgelTSLRLIQTGGEALTPPVARdLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVL 306
Cdd:PRK07638 249 NRVIE------NKMKIISSGAKWEAEAKEK-IKNIFPYAKLYEFYGASELSFVTALVDEESERRPNSVGRPFHNVQVRIC 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 307 DAALREVPIGVPGELYLGGVQLARGYAGRpdltaerfvADPFGEPGARLYRT-GDRARWNRDGEIEYLGRTDFQVKLRGQ 385
Cdd:PRK07638 322 NEAGEEVQKGEIGTVYVKSPQFFMGYIIG---------GVLARELNADGWMTvRDVGYEDEEGFIYIVGREKNMILFGGI 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 386 RLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLApADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVD 464
Cdd:PRK07638 393 NIFPEEIESVLHEHPAVDEIVViGVPDSYWGEKPVAIIK-GSATKQQLKSFCLQRLSSFKIPKEWHFVDEIPYTNSGKIA 471
|
.
gi 1827387616 465 R 465
Cdd:PRK07638 472 R 472
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2716-3059 |
4.46e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 97.94 E-value: 4.46e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2716 NLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLgFASPSF--DASVLEYLLAT------VNEGTLAYR 2787
Cdd:cd05944 3 DVAAYFHTGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLL-CGLPLFhvNGSVVTLLTPLasgahvVLAGPAGYR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2788 PSEAVGGevLERFIAEHGATHTFLTPSVLSTM----DPTAVPSLRVIAAGGEAVPQPIVDRWAPATELHNL--YGPTETT 2861
Cdd:cd05944 82 NPGLFDN--FWKLVERYRITSLSTVPTVYAALlqvpVNADISSLRFAMSGAAPLPVELRARFEDATGLPVVegYGLTEAT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2862 IGITISSamrPGDPVRLGG-----PIGGVDLMVLD---ERLRPVPVGMPGELYVAGGALSRGYLDRSGltaerftaNPYG 2933
Cdd:cd05944 160 CLVAVNP---PDGPKRPGSvglrlPYARVRIKVLDgvgRLLRDCAPDEVGEICVAGPGVFGGYLYTEG--------NKNA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2934 TAGQRMYRTGDVVRWTPDtdtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATAL-AAYIV 3012
Cdd:cd05944 229 FVADGWLNTGDLGRLDAD---GYLFI--TGRAKDLIIRGGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELpVAYVQ 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1827387616 3013 PVDGA-VEVSELKAFAGGRLPAYM-VPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05944 304 LKPGAvVEEEELLAWARDHVPERAaVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
97-466 |
5.55e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 100.46 E-value: 5.55e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 97 HVLDISSPGDADLDEEEFAGPTRPAnaaFTLFTSGSTGRPKAVVITHRGI-ANRLAADIEQYDLTARDVFLYKA-PI--- 171
Cdd:PRK05605 198 TLVDAAIGGDGSDVSHPRPTPDDVA---LILYTSGTTGKPKGAQLTHRNLfANAAQGKAWVPGLGDGPERVLAAlPMfha 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 172 -------TFDVSvreiflpiaIGATLV-IAEPgrhgDPVHLADLIRRHGVTvihFVPAMLAAFNEVLGA----GVgELTS 239
Cdd:PRK05605 275 ygltlclTLAVS---------IGGELVlLPAP----DIDLILDAMKKHPPT---WLPGVPPLYEKIAEAaeerGV-DLSG 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 240 LRLIQTGGEALTPPVARdLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDA--ALREVPIGV 317
Cdd:PRK05605 338 VRNAFSGAMALPVSTVE-LWEKLTGGLLVEGYGLTETSPIIVGNPMSDDRRPGYVGVPFPDTEVRIVDPedPDETMPDGE 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 318 PGELYLGGVQLARGYAGRPDLTAERFVADpfgepgarLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALA 397
Cdd:PRK05605 417 EGELLVRGPQVFKGYWNRPEETAKSFLDG--------WFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLR 488
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 398 AAPGVlhAAAAVVDGP---GGQQLVG--YLAP-ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRR 466
Cdd:PRK05605 489 EHPGV--EDAAVVGLPredGSEEVVAavVLEPgAALDPEGLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRR 561
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1187-1527 |
5.80e-21 |
|
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: 96.96 E-value: 5.80e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1187 LIYTSGSTGRPKAVGVSHTGIVdFVNSLAKITTGTPEDEPDTRIL---HVASPSFDASMFEmawaipAGHTLVIAPQadF 1263
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHGNLI-AANLQLIHAMGLTEADVYLNMLplfHIAGLNLALATFH------AGGANVVMEK--F 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1264 AGDALATVLERDEVTDMIITPSVLATVDPERAQYVRNLA-----TGGEAcpPELVERWSERGRRIFNC-YGPTEATVWAT 1337
Cdd:cd17637 76 DPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSslrhvLGLDA--PETIQRFEETTGATFWSlYGQTETSGLVT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1338 RSRMTAgKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADpfgepgarMYATGDLV 1417
Cdd:cd17637 154 LSPYRE-RPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG--------WHHTGDLG 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1418 RVAKGGNLEFAGRADHQ--VKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTrggrKHTEVV-AYLVAKPGATIDSAAV 1494
Cdd:cd17637 225 RFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDP----KWGEGIkAVCVLKPGATLTADEL 300
|
330 340 350
....*....|....*....|....*....|...
gi 1827387616 1495 LDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDR 1527
Cdd:cd17637 301 IEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
128-468 |
5.82e-21 |
|
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: 99.09 E-value: 5.82e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 128 FTSGSTGRPKAVVITHR---GIANRLAADIeqYDLTARDVFLYKAPITFDVSVR-EIFLPIAIGATLVIAEpgrHGDPVH 203
Cdd:cd05958 104 FTSGTTGAPKATMHFHRdplASADRYAVNV--LRLREDDRFVGSPPLAFTFGLGgVLLFPFGVGASGVLLE---EATPDL 178
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 204 LADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVaRDLMVRLPGTRLQNQYGPAEAsIVVTIH 283
Cdd:cd05958 179 LLSAIARYKPTVLFTAPTAYRAMLAHPDAAGPDLSSLRKCVSAGEALPAAL-HRAWKEATGIPIIDGIGSTEM-FHIFIS 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 284 RVTQDDRVIPIGTPTRRVSARVLDAALREVPIGVPGELYLGGvqlARGYAGRPDLTAERFVADPFGEpgarlyrTGDRAR 363
Cdd:cd05958 257 ARPGDARPGATGKPVPGYEAKVVDDEGNPVPDGTIGRLAVRG---PTGCRYLADKRQRTYVQGGWNI-------TGDTYS 326
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 364 WNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGP---GGQQLVGYL------APADVDVDTVAA 434
Cdd:cd05958 327 RDPDGYFRHQGRSDDMIVSGGYNIAPPEVEDVLLQHPAV--AECAVVGHPdesRGVVVKAFVvlrpgvIPGPVLARELQD 404
|
330 340 350
....*....|....*....|....*....|....
gi 1827387616 435 TTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd05958 405 HAKAHIAPYKYPRAIEFVTELPRTATGKLQRFAL 438
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1183-1527 |
6.03e-21 |
|
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: 96.71 E-value: 6.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1183 NLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtrILHVASP-SFDASMFEMAWAIPAGHTLVIapQA 1261
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGED-----AILAPGPlSHSLFLYGAISALYLGGTFIG--QR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1262 DFAGDALATVLERDEVTDMIITPSVLA----TVDPERAqyVRNLATGGEACPPELVERWsergRRIFN------CYGPTE 1331
Cdd:cd17633 74 KFNPKSWIRKINQYNATVIYLVPTMLQalarTLEPESK--IKSIFSSGQKLFESTKKKL----KNIFPkanlieFYGTSE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1332 ATVWATRSRMTAGKPVTIGKPVDGFTVRVLDGrlhevPQGVVGELYLSTAGLARGYLGRPGQTAVSFvadpfgepgarmY 1411
Cdd:cd17633 148 LSFITYNFNQESRPPNSVGRPFPNVEIEIRNA-----DGGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------M 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1412 ATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEVVAYLVAkpGATIDS 1491
Cdd:cd17633 211 SVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFG----EIAVALYS--GDKLTY 284
|
330 340 350
....*....|....*....|....*....|....*.
gi 1827387616 1492 AAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDR 1527
Cdd:cd17633 285 KQLKRFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
2575-3020 |
6.74e-21 |
|
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: 100.01 E-value: 6.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2575 ARRAPDHVAVV-----DGAGARLTYRELDEASDRLARWLIGRGvGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPD 2649
Cdd:cd05931 3 AAARPDRPAYTflddeGGREETLTYAELDRRARAIAARLQAVG-KPGDRVLLLAPPGLDFVAAFLGCLYAGAIAVPLPPP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2650 YP---AERVASMIEDSGAVLGLSVLASGDLPgQEFEWMRLDDDSVAAEIAAVPAGPITDAERLGEVTAANLAYVIYTSGS 2726
Cdd:cd05931 82 TPgrhAERLAAILADAGPRVVLTTAAALAAV-RAFAASRPAAGTPRLLVVDLLPDTSAADWPPPSPDPDDIAYLQYTSGS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2727 TGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAY---------RPSeavggevl 2797
Cdd:cd05931 161 TGTPKGVVVTHRNLLANVRQIRRAYGLDPGDVVVSWLPLYHDMGLIGGLLTPLYSGGPSVlmspaaflrRPL-------- 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2798 eRF---IAEHGATHTF------------LTPSVLSTMDptaVPSLRVIAAGGEAVPQPIVDRWAPATELHNL-------- 2854
Cdd:cd05931 233 -RWlrlISRYRATISAapnfaydlcvrrVRDEDLEGLD---LSSWRVALNGAEPVRPATLRRFAEAFAPFGFrpeafrps 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2855 YGPTETTIGITIS--------------------SAMRPGDP-----VRLGGPIGGVDLMVLD-ERLRPVPVGMPGELYVA 2908
Cdd:cd05931 309 YGLAEATLFVSGGppgtgpvvlrvdrdalagraVAVAADDPaarelVSCGRPLPDQEVRIVDpETGRELPDGEVGEIWVR 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2909 GGALSRGYLDRSGLTAERFTANPyGTAGQRMYRTGD---VVRwtpdtdtGGLTLeyTGRSDDQVKLRGLRIELGEIEAVL 2985
Cdd:cd05931 389 GPSVASGYWGRPEATAETFGALA-ATDEGGWLRTGDlgfLHD-------GELYI--TGRLKDLIIVRGRNHYPQDIEATA 458
|
490 500 510
....*....|....*....|....*....|....*
gi 1827387616 2986 AEHDAVesavvlGVGGSVatalAAYIVPVDGAVEV 3020
Cdd:cd05931 459 EEAHPA------LRPGCV----AAFSVPDDGEERL 483
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1061-1505 |
6.86e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 99.07 E-value: 6.86e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1061 EMDYDEFETRTNAIARALLARGVSPeDVVAVGMER-SIGSVLATWGVIKSGAAYVPVDPAYpadriaymledsgatvgit 1139
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRR-GMRAVLMVPpGPDFFALTFALFKAGAVPVLIDPGM------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1140 dasTRARLGEssCewvdLADLEAEAESGDDITDTErngsvrltnlAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITT 1219
Cdd:cd05910 62 ---GRKNLKQ--C----LQEAEPDAFIGIPKADEP----------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1220 GTPEDepdtrILHVASPSFdaSMFEMAWAIPAghtlvIAPQADFAGDA------LATVLERDEVTDMIITPSVLATVDPE 1293
Cdd:cd05910 123 IRPGE-----VDLATFPLF--ALFGPALGLTS-----VIPDMDPTRPAradpqkLVGAIRQYGVSIVFGSPALLERVARY 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1294 RAQY------VRNLATGGEACPPELVERWSE---RGRRIFNCYGPTEA---------TVWATRSRMTA-GKPVTIGKPVD 1354
Cdd:cd05910 191 CAQHgitlpsLRRVLSAGAPVPIALAARLRKmlsDEAEILTPYGATEAlpvssigsrELLATTTAATSgGAGTCVGRPIP 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1355 GFTVRVLD---------GRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEPGARMyatGDLVRVAKGGNL 1425
Cdd:cd05910 271 GVRVRIIEiddepiaewDDTLELPRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEGFWHRM---GDLGYLDDEGRL 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1426 EFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVesTRGGRKHTEVVayLVAKPGATIDSAAVLDEAAQHLAAH 1505
Cdd:cd05910 348 WFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGV--GKPGCQLPVLC--VEPLPGTITPRARLEQELRALAKDY 423
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2719-3057 |
9.28e-21 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 97.07 E-value: 9.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2719 YVIYTSGSTGRPKGVAVTHS-------GLANFARQE------SDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLA 2785
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEdifrmlmGGADFGTGEftpsedAHKAAAAAAGTVMFPAPPLMHGTGSWTAFGGLLGGQTV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2786 YRPSEAVGGEVLERFIAEHGATHTFLT------PSV--LSTMDPTAVPSLRVIAAGGEAVPQPIVDRW---APATELHNL 2854
Cdd:cd05924 87 VLPDDRFDPEEVWRTIEKHKVTSMTIVgdamarPLIdaLRDAGPYDLSSLFAISSGGALLSPEVKQGLlelVPNITLVDA 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2855 YGPTETTIGITISSAMRPGD--PVRLGGPiggvDLMVLDERLRPVPVGMPGELYVA-GGALSRGYLDRSGLTAERF-TAN 2930
Cdd:cd05924 167 FGSSETGFTGSGHSAGSGPEtgPFTRANP----DTVVLDDDGRVVPPGSGGVGWIArRGHIPLGYYGDEAKTAETFpEVD 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2931 pygtaGQRMYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-----GGSVAT 3005
Cdd:cd05924 243 -----GVRYAVPGDRATVEADG-----TVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRpderwGQEVVA 312
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 3006 alaayIVPVDGAVEVS--ELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKR 3057
Cdd:cd05924 313 -----VVQLREGAGVDleELREHCRTRIARYKLPKQVVFVDEIERSPAGKADYR 361
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
128-465 |
1.70e-20 |
|
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: 95.55 E-value: 1.70e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 128 FTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAepgRHGDPVHLADL 207
Cdd:cd17633 7 FTSGTTGLPKAYYRSERSWIESFVCNEDLFNISGEDAILAPGPLSHSLFLYGAISALYLGGTFIGQ---RKFNPKSWIRK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 208 IRRHGVTVIHFVPAMLAAFNEVLGAgvgeLTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVvTIHRVTQ 287
Cdd:cd17633 84 INQYNATVIYLVPTMLQALARTLEP----ESKIKSIFSSGQKLFESTKKKLKNIFPKANLIEFYGTSELSFI-TYNFNQE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 288 DDRVIPIGTPTRRVSARVLDAALREVpigvpGELYLGGVQLARGYAGRPDLTAERFvadpfgepgarlYRTGDRARWNRD 367
Cdd:cd17633 159 SRPPNSVGRPFPNVEIEIRNADGGEI-----GKIFVKSEMVFSGYVRGGFSNPDGW------------MSVGDIGYVDEE 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 368 GEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAPADVDVDTVAATTAELLPEYMRP 446
Cdd:cd17633 222 GYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVvGIPDARFGEIAVALYSGDKLTYKQLKRFLKQKLSRYEIP 301
|
330
....*....|....*....
gi 1827387616 447 SAWVRLDAMPLSRSGKVDR 465
Cdd:cd17633 302 KKIIFVDSLPYTSSGKIAR 320
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1-461 |
2.10e-20 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 98.28 E-value: 2.10e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQ---------LPVDRARYMVRTA 71
Cdd:PRK06164 36 LSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRyrshevahiLGRGRARWLVVWP 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 72 GVR---LVVVTSDGEAEARSRFDDIVDVHVLDISSPGDADLDEEE-FAGPTRPANAA--------------FTlfTSGST 133
Cdd:PRK06164 116 GFKgidFAAILAAVPPDALPPLRAIAVVDDAADATPAPAPGARVQlFALPDPAPPAAageraadpdagallFT--TSGTT 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 134 GRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGrhgDPVHLADLIRRHGV 213
Cdd:PRK06164 194 SGPKLVLHRQATLLRHARAIARAYGYDPGAVLLAALPFCGVFGFSTLLGALAGGAPLVCEPVF---DAARTARALRRHRV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 214 TVIHFVPAMLAAFNEVLGAGvGELTSLRLIqtgGEALTPPVARDLM--VRLPGTRLQNQYGPAEASIVVTIHRVTQD--D 289
Cdd:PRK06164 271 THTFGNDEMLRRILDTAGER-ADFPSARLF---GFASFAPALGELAalARARGVPLTGLYGSSEVQALVALQPATDPvsV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 290 RVIPIGTPTR---RVSAR-VLDAALreVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWN 365
Cdd:PRK06164 347 RIEGGGRPASpeaRVRARdPQDGAL--LPDGESGEIEIRAPSLMRGYLDNPDATARALTDDGY-------FRTGDLGYTR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 366 RDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGPGGQQLVGYLAPAD---VDVDTVAATTAELLPE 442
Cdd:PRK06164 418 GDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRDGKTVPVAFVIPTDgasPDEAGLMAACREALAG 497
|
490
....*....|....*....
gi 1827387616 443 YMRPSAWVRLDAMPLSRSG 461
Cdd:PRK06164 498 FKVPARVQVVEAFPVTESA 516
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1187-1526 |
2.24e-20 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 95.06 E-value: 2.24e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1187 LIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITtgtpEDEPDTRILhVASPSFD-ASMFEMAWAIPAGHTLVIAPQADFAG 1265
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQ----AIDEGTVFL-NSGPLFHiGTLMFTLATFHAGGTNVFVRRVDAEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1266 daLATVLERDEVTDMIITPSVLATVDPERAQYVRNLAT--------GGEACPPELVERWSERGRRifncYGPTEATVWAT 1337
Cdd:cd17636 80 --VLELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSlrsspaapEWNDMATVDTSPWGRKPGG----YGQTEVMGLAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1338 RSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVadpfgepgARMYATGDLV 1417
Cdd:cd17636 154 FAALGGGAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR--------GGWHHTNDLG 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1418 RVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPGATIDSAAVLDE 1497
Cdd:cd17636 226 RREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQ---SVKAIVVLKPGASVTEAELIEH 302
|
330 340
....*....|....*....|....*....
gi 1827387616 1498 AAQHLAAHMVPSQAIVIDEIPLTPAGKLD 1526
Cdd:cd17636 303 CRARIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
2591-3062 |
2.74e-20 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 97.46 E-value: 2.74e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2591 RLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGA-VL--- 2666
Cdd:PRK12406 11 RRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGArVLiah 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2667 -------------GLSVLaSGDLPGQEFEWMRLDDDSvaaeiAAVPAGPITDAERLGE------VTAANLAYVIYTSGST 2727
Cdd:PRK12406 91 adllhglasalpaGVTVL-SVPTPPEIAAAYRISPAL-----LTPPAGAIDWEGWLAQqepydgPPVPQPQSMIYTSGTT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2728 GRPKGV---AVTHSGLANFARQEsdRLNAGDNP-VVLGFASPSFDASVLEYllatvneGTLAYRPSEAVggeVLE-RF-- 2800
Cdd:PRK12406 165 GHPKGVrraAPTPEQAAAAEQMR--ALIYGLKPgIRALLTGPLYHSAPNAY-------GLRAGRLGGVL---VLQpRFdp 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2801 ------IAEHGATHTFLTPSVLST-MD-PTAV------PSLRVIAAGGEAVPQPI----VDRWAPAteLHNLYGPTETTI 2862
Cdd:PRK12406 233 eellqlIERHRITHMHMVPTMFIRlLKlPEEVrakydvSSLRHVIHAAAPCPADVkramIEWWGPV--IYEYYGSTESGA 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2863 GITISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYV--AGGAL--------SRGYLDRSGLTaerftanpy 2932
Cdd:PRK12406 311 VTFATSEDALSHPGTVGKAAPGAELRFVDEDGRPLPQGEIGEIYSriAGNPDftyhnkpeKRAEIDRGGFI--------- 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2933 gTAGQRMYRTGDVVRWTPDtdtggltleytgRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGS-VATALAAYI 3011
Cdd:PRK12406 382 -TSGDVGYLDADGYLFLCD------------RKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAeFGEALMAVV 448
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 3012 VPVDGA-VEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEP 3062
Cdd:PRK12406 449 EPQPGAtLDEADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1-468 |
3.15e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 97.34 E-value: 3.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:PRK03640 28 VTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQLDDAEVKCLITDD 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAE----ARSRFDDIVDVHVLDISSPGDADLDEeefagptrpanAAFTLFTSGSTGRPKAVVITHrgiANRLAADI-- 154
Cdd:PRK03640 108 DFEAKlipgISVKFAELMNGPKEEAEIQEEFDLDE-----------VATIMYTSGTTGKPKGVIQTY---GNHWWSAVgs 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 155 -EQYDLTARDVFLYKAPItFDVSVREIFLPIAI-GATLVIAEpgrHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGA 232
Cdd:PRK03640 174 aLNLGLTEDDCWLAAVPI-FHISGLSILMRSVIyGMRVVLVE---KFDAEKINKLLQTGGVTIISVVSTMLQRLLERLGE 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 233 GvGELTSLRLIQTGGEaltpPVARDLM--VRLPGTRLQNQYGPAE-ASIVVTIhrvTQDDRVIPIGT---PTRRVSARVL 306
Cdd:PRK03640 250 G-TYPSSFRCMLLGGG----PAPKPLLeqCKEKGIPVYQSYGMTEtASQIVTL---SPEDALTKLGSagkPLFPCELKIE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 307 DaALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlyRTGDRARWNRDGEIEYLGRTDFQVKLRGQR 386
Cdd:PRK03640 322 K-DGVVVPPFEEGEIVVKGPNVTKGYLNREDATRETFQDGWF--------KTGDIGYLDEEGFLYVLDRRSDLIISGGEN 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 387 LELGEVEAALAAAPGVlhAAAAVV---DGPGGQQLVGYL-APADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGK 462
Cdd:PRK03640 393 IYPAEIEEVLLSHPGV--AEAGVVgvpDDKWGQVPVAFVvKSGEVTEEELRHFCEEKLAKYKVPKRFYFVEELPRNASGK 470
|
....*.
gi 1827387616 463 VDRRLL 468
Cdd:PRK03640 471 LLRHEL 476
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
2566-3059 |
4.09e-20 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 97.43 E-value: 4.09e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVVDgAGARLTYRELDEASDRLARWLiGRGVGPERA--VALAIGRSAQLLTAIWAVAKTGGAY 2643
Cdd:PRK08974 24 SLVDMFEQAVARYADQPAFIN-MGEVMTFRKLEERSRAFAAYL-QNGLGLKKGdrVALMMPNLLQYPIALFGILRAGMIV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2644 VPIDPDYPAERVASMIEDSGA--VLGLSVLASG------DLPGQEFEWMRLDD----------DSVAAEIAA-VPAGPIT 2704
Cdd:PRK08974 102 VNVNPLYTPRELEHQLNDSGAkaIVIVSNFAHTlekvvfKTPVKHVILTRMGDqlstakgtlvNFVVKYIKRlVPKYHLP 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2705 DA----------ERLG----EVTAANLAYVIYTSGSTGRPKGVAVTHSG-LANFARQE---SDRLNAGDNPVVLgfASPs 2766
Cdd:PRK08974 182 DAisfrsalhkgRRMQyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQAKaayGPLLHPGKELVVT--ALP- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2767 fdasvLEYLLA-TVN---------EGTLAYRPSEaVGGEVLE----RFIAEHGATHTFltPSVLSTMDPTAV--PSLRVI 2830
Cdd:PRK08974 259 -----LYHIFAlTVNcllfielggQNLLITNPRD-IPGFVKElkkyPFTAITGVNTLF--NALLNNEEFQELdfSSLKLS 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2831 AAGGEAVPQPIVDRWAPATELHNL--YGPTETTIGITISsamrPGDPVRLGGPIG----GVDLMVLDERLRPVPVGMPGE 2904
Cdd:PRK08974 331 VGGGMAVQQAVAERWVKLTGQYLLegYGLTECSPLVSVN----PYDLDYYSGSIGlpvpSTEIKLVDDDGNEVPPGEPGE 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2905 LYVAGGALSRGYLDRSGLTAERFTanpygtagQRMYRTGDVVRwtpdTDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAV 2984
Cdd:PRK08974 407 LWVKGPQVMLGYWQRPEATDEVIK--------DGWLATGDIAV----MDEEGF-LRIVDRKKDMILVSGFNVYPNEIEDV 473
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 2985 LAEHDAVESAVVLGVGGSVA-TALAAYIVPVDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK08974 474 VMLHPKVLEVAAVGVPSEVSgEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1058-1530 |
4.55e-20 |
|
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) synthesizing toxins and antitumor agents; The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPSs that synthesize toxins and antitumor agents; for example, TubE for Tubulysine, CrpA for cryptophycin, TdiA for terrequinone A, KtzG for kutzneride, and Vlm1/Vlm2 for Valinomycin. Nonribosomal peptide synthetases are large multifunctional enzymes which synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341232 [Multi-domain] Cd Length: 540 Bit Score: 97.35 E-value: 4.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1058 DGTE--MDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSG--AAYVPVDPAY--PADRIAYmLED 1131
Cdd:cd05906 34 DGSEefQSYQDLLEDARRLAAGLRQLGLRPGDSVILQFDDNEDFIPAFWACVLAGfvPAPLTVPPTYdePNARLRK-LRH 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1132 SGATVG----ITDASTRARLGESSCEWVDLADLEAEAESGDDiTDTERNG-SVRLTNLAYLIYTSGSTGRPKAVGVSHTG 1206
Cdd:cd05906 113 IWQLLGspvvLTDAELVAEFAGLETLSGLPGIRVLSIEELLD-TAADHDLpQSRPDDLALLMLTSGSTGFPKAVPLTHRN 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1207 IVDfvNSLAKITTGtpEDEPDTRIL------HVASpsfdASMFEMAwAIPAGHTLVIAPQADFAGDALATV--LERDEVT 1278
Cdd:cd05906 192 ILA--RSAGKIQHN--GLTPQDVFLnwvpldHVGG----LVELHLR-AVYLGCQQVHVPTEEILADPLRWLdlIDRYRVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1279 dmiIT--P----SVLATVDPERAQY------VRNLATGGEACPPE----LVERWSERGRRIF----------NCYGPTEA 1332
Cdd:cd05906 263 ---ITwaPnfafALLNDLLEEIEDGtwdlssLRYLVNAGEAVVAKtirrLLRLLEPYGLPPDairpafgmteTCSGVIYS 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1333 TVWATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYA 1412
Cdd:cd05906 340 RSFPTYDHSQALEFVSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTEDGW-------FR 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1413 TGDLVRVaKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVeSTRGGRKHTEVVAyLVAKPGATIDSA 1492
Cdd:cd05906 413 TGDLGFL-DNGNLTITGRTKDTIIVNGVNYYSHEIEAAVEEVPGVEPSFTAAF-AVRDPGAETEELA-IFFVPEYDLQDA 489
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1827387616 1493 --AVLDEAAQHLAAHMVPSQAIVI----DEIPLTPAGKLDRAAL 1530
Cdd:cd05906 490 lsETLRAIRSVVSREVGVSPAYLIplpkEEIPKTSLGKIQRSKL 533
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
2720-3055 |
5.68e-20 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 93.91 E-value: 5.68e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2720 VIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGfASPSFDASVLEYLLAT-VNEGTLAYRPseAVGGEVLE 2798
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLN-SGPLFHIGTLMFTLATfHAGGTNVFVR--RVDAEEVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2799 RFIAEHGATHTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRWAPATELHnLYGPTETTiGITISSAMRP 2872
Cdd:cd17636 82 ELIEAERCTHAFLLPPTIDQIvelnadGLYDLSSLRSSPAAPEWNDMATVDTSPWGRKPG-GYGQTEVM-GLATFAALGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2873 GDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTAnpygtagqRMYRTGDVVRWTPDT 2952
Cdd:cd17636 160 GAIGGAGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG--------GWHHTNDLGRREPDG 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2953 dtgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSV-ATALAAYIVPVDGA-VEVSELKAFAGGR 3030
Cdd:cd17636 232 -----SLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRwAQSVKAIVVLKPGAsVTEAELIEHCRAR 306
|
330 340
....*....|....*....|....*
gi 1827387616 3031 LPAYMVPSSFTVIDELPLTPVGKLD 3055
Cdd:cd17636 307 IASYKKPKSVEFADALPRTAGGADD 331
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
107-439 |
7.16e-20 |
|
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: 95.61 E-value: 7.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 107 ADLDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPITfdvsvrEIFLPiAI 186
Cdd:cd05910 71 QEAEPDAFIGIPKADEPAAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDLATFPLF------ALFGP-AL 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 187 GATLVIAE-----PGRhGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVR 261
Cdd:cd05910 144 GLTSVIPDmdptrPAR-ADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLPSLRRVLSAGAPVPIALAARLRKM 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 262 L-PGTRLQNQYGPAEASIVVTI---------HRVTQDDRVIPIGTPTRRVSARVLDA---------ALREVPIGVPGELY 322
Cdd:cd05910 223 LsDEAEILTPYGATEALPVSSIgsrellattTAATSGGAGTCVGRPIPGVRVRIIEIddepiaewdDTLELPRGEIGEIT 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 323 LGGVQLARGYAGRPDLTAERFVADPfgePGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGV 402
Cdd:cd05910 303 VTGPTVTPTYVNRPVATALAKIDDN---SEGFWHRMGDLGYLDDEGRLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGV 379
|
330 340 350
....*....|....*....|....*....|....*..
gi 1827387616 403 LHAAAAVVDGPGGQQLVGYLAPADVDVDTVAATTAEL 439
Cdd:cd05910 380 RRSALVGVGKPGCQLPVLCVEPLPGTITPRARLEQEL 416
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
2703-3059 |
8.81e-20 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 93.96 E-value: 8.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2703 ITDAERLGEVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLnAGDNPVVLgfASPSFDASVLEYLLATVNEG 2782
Cdd:PRK07824 23 LRDALRVGEPIDDDVALVVATSGTTGTPKGAMLTAAALTASADATHDRL-GGPGQWLL--ALPAHHIAGLQVLVRSVIAG 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2783 T--LAYRPSEAVGGEVLERFIAEHGA--THTFLTPSVLSTM--DPTAVPSLRVIAA---GGEAVPQPIVDRWAPA-TELH 2852
Cdd:PRK07824 100 SepVELDVSAGFDPTALPRAVAELGGgrRYTSLVPMQLAKAldDPAATAALAELDAvlvGGGPAPAPVLDAAAAAgINVV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2853 NLYGPTETTigitissamrpGDPVRLGGPIGGVDLMVLDERLrpvpvgmpgelYVAGGALSRGYldRSGLTAERFtANPy 2932
Cdd:PRK07824 180 RTYGMSETS-----------GGCVYDGVPLDGVRVRVEDGRI-----------ALGGPTLAKGY--RNPVDPDPF-AEP- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2933 gtagqrmyrtgdvvRWTPDTDTGGLT---LEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-----GGSVA 3004
Cdd:PRK07824 234 --------------GWFRTDDLGALDdgvLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLpddrlGQRVV 299
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 3005 talAAYIVPVDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK07824 300 ---AAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
2573-3058 |
9.38e-20 |
|
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: 96.03 E-value: 9.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2573 AAARRAPDHVAVV--DGAGAR--LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVP--- 2645
Cdd:cd05970 25 AMAKEYPDKLALVwcDDAGEEriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPath 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2646 ---------------------IDPDYPAERVASMIEDSGAVLGLsVLASGDLPGQEFEWMRLDDDsvAAEIAAVPAGPit 2704
Cdd:cd05970 105 qltakdivyriesadikmivaIAEDNIPEEIEKAAPECPSKPKL-VWVGDPVPEGWIDFRKLIKN--ASPDFERPTAN-- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2705 dAERLGEvtaaNLAYVIYTSGSTGRPKGVA------VTHSGLANFARqesdrlNAGDNPVVLGFASPSFDASVLEYLLAT 2778
Cdd:cd05970 180 -SYPCGE----DILLVYFSSGTTGMPKMVEhdftypLGHIVTAKYWQ------NVREGGLHLTVADTGWGKAVWGKIYGQ 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2779 VNEGT--LAYRPSEAVGGEVLERfIAEHGAT--------HTFLTPSVLSTMDptaVPSLRVIAAGGEAVPQPIVDRWAPA 2848
Cdd:cd05970 249 WIAGAavFVYDYDKFDPKALLEK-LSKYGVTtfcapptiYRFLIREDLSRYD---LSSLRYCTTAGEALNPEVFNTFKEK 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2849 T--ELHNLYGPTETTIGITISSAMRPgDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYV--AGG---ALSRGYLDRSG 2921
Cdd:cd05970 325 TgiKLMEGFGQTETTLTIATFPWMEP-KPGSMGKPAPGYEIDLIDREGRSCEAGEEGEIVIrtSKGkpvGLFGGYYKDAE 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2922 LTAERFTANpygtagqrMYRTGDVVrWTpdtDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGG 3001
Cdd:cd05970 404 KTAEVWHDG--------YYHTGDAA-WM---DEDGY-LWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPD 470
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 3002 SV-ATALAAYIVPVDG--AVEV--SELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLdKRA 3058
Cdd:cd05970 471 PIrGQVVKATIVLAKGyePSEElkKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKI-RRV 531
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
117-474 |
9.45e-20 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 97.09 E-value: 9.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 117 PTRPANAAFTLFTSGSTGRPKAVVITHrgiaNRLAADIEQY----DLTARDVFLYKAPI--TFDVSVrEIFLPIAIGATL 190
Cdd:PRK08043 361 KQQPEDAALILFTSGSEGHPKGVVHSH----KSLLANVEQIktiaDFTPNDRFMSALPLfhSFGLTV-GLFTPLLTGAEV 435
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 191 VIaepgrHGDPVH---LADLIRRHGVTVIHFVPAMLAAFNEVlgAGVGELTSLRLIQTGGEALTPPVARDLMVRLpGTRL 267
Cdd:PRK08043 436 FL-----YPSPLHyriVPELVYDRNCTVLFGTSTFLGNYARF--ANPYDFARLRYVVAGAEKLQESTKQLWQDKF-GLRI 507
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 268 QNQYGPAEASIVVTIHrvtqddrvIPIGTPTRRVsARVL---DAALREVP-IGVPGELYLGGVQLARGY--AGRPDLTAE 341
Cdd:PRK08043 508 LEGYGVTECAPVVSIN--------VPMAAKPGTV-GRILpgmDARLLSVPgIEQGGRLQLKGPNIMNGYlrVEKPGVLEV 578
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 342 RFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEA-ALAAAPGVLHAAAAVVDGPGGQQLVG 420
Cdd:PRK08043 579 PTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQlALGVSPDKQHATAIKSDASKGEALVL 658
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 421 YLAPADVDVDTVAATTAEL-LPEYMRPSAWVRLDAMPLSRSGKVD----RRLLPEPEIA 474
Cdd:PRK08043 659 FTTDSELTREKLQQYAREHgVPELAVPRDIRYLKQLPLLGSGKPDfvtlKSMVDEPEQH 717
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1019-1527 |
1.14e-19 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 96.41 E-value: 1.14e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1019 VSARTPGAMVGRGGEVeagTLIDVLAQRDL--DPDHPALICDGTE-----MDYDEFETRTNAIARALLARGVSPEDVVAV 1091
Cdd:cd05968 45 LSGGKPWAAWFVGGRM---NIVEQLLDKWLadTRTRPALRWEGEDgtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGI 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1092 GMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGIT-DASTR----------ARLGESSCEWVDL--- 1157
Cdd:cd05968 122 YLPMIPEIVPAFLAVARIGGIVVPIFSGFGKEAAATRLQDAEAKALITaDGFTRrgrevnlkeeADKACAQCPTVEKvvv 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1158 ---ADLEAEAESGDDITDTERNGS--VRLTNLA-----YLIYTSGSTGRPKAVGVSHTGIvdfvNSLAKITTGTPED-EP 1226
Cdd:cd05968 202 vrhLGNDFTPAKGRDLSYDEEKETagDGAERTEsedplMIIYTSGTTGKPKGTVHVHAGF----PLKAAQDMYFQFDlKP 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1227 DTRILHVASPSFDASMFEMAWAIPAGHTLVI---APQADFAgDALATVLERDEVTDMIITPSVLATVDPERAQYV----- 1298
Cdd:cd05968 278 GDLLTWFTDLGWMMGPWLIFGGLILGATMVLydgAPDHPKA-DRLWRMVEDHEITHLGLSPTLIRALKPRGDAPVnahdl 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1299 ---RNLATGGEACPPE----LVERWSERGRRIFNCYGPTEatvwatrsrMTAG----------KPVTIGKPVDGFTVRVL 1361
Cdd:cd05968 357 sslRVLGSTGEPWNPEpwnwLFETVGKGRNPIINYSGGTE---------ISGGilgnvlikpiKPSSFNGPVPGMKADVL 427
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1362 DGRLHEVPqGVVGELYLSTA--GLARGYLGRPGQtavsfVADPFGEPGARMYATGDLVRVAKGGNLEFAGRADHQVKING 1439
Cdd:cd05968 428 DESGKPAR-PEVGELVLLAPwpGMTRGFWRDEDR-----YLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAG 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1440 QRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhTEVVAYLVAKPGATiDSAAVLDEAAQHLAAHM----VPSQAIVID 1515
Cdd:cd05968 502 KRVGPAEIESVLNAHPAVLESAAIGVPHPVKG---EAIVCFVVLKPGVT-PTEALAEELMERVADELgkplSPERILFVK 577
|
570
....*....|..
gi 1827387616 1516 EIPLTPAGKLDR 1527
Cdd:cd05968 578 DLPKTRNAKVMR 589
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
42-468 |
1.19e-19 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 95.82 E-value: 1.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 42 IHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVrlVVVTSDGEAEarsrfddiVDVHVLDISSPGDADLDEEEFAgptrPA 121
Cdd:PLN02246 114 IAKQAKASGAKLIITQSCYVDKLKGLAEDDGV--TVVTIDDPPE--------GCLHFSELTQADENELPEVEIS----PD 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 122 NAAFTLFTSGSTGRPKAVVITHRG----IANRLAADIEQYDLTARDVFLYKAPITFDVSVREIFL-PIAIGATLVIAepg 196
Cdd:PLN02246 180 DVVALPYSSGTTGLPKGVMLTHKGlvtsVAQQVDGENPNLYFHSDDVILCVLPMFHIYSLNSVLLcGLRVGAAILIM--- 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 197 RHGDPVHLADLIRRHGVTVIHFVPAMLAAF--NEVLGAgvGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPA 274
Cdd:PLN02246 257 PKFEIGALLELIQRHKVTIAPFVPPIVLAIakSPVVEK--YDLSSIRMVLSGAAPLGKELEDAFRAKLPNAVLGQGYGMT 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 275 EASIVVTIHRVTQDDrVIPI-----GTPTRRVSARVLDAALRE-VPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPF 348
Cdd:PLN02246 335 EAGPVLAMCLAFAKE-PFPVksgscGTVVRNAELKIVDPETGAsLPRNQPGEICIRGPQIMKGYLNDPEATANTIDKDGW 413
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 349 gepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVV---DGPGGQQLVGYLAPA 425
Cdd:PLN02246 414 -------LHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSI--ADAAVVpmkDEVAGEVPVAFVVRS 484
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1827387616 426 ---DVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PLN02246 485 ngsEITEDEIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1-469 |
1.63e-19 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 95.45 E-value: 1.63e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRlVVVTS 80
Cdd:PRK13383 61 LSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAALRAHHIS-TVVAD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRFDDivDVHVLDISSPGdadlDEEEFAGPTRPANAAFTLFTSGSTGRPKAV-----VITHRGIANRLaadIE 155
Cdd:PRK13383 140 NEFAERIAGADD--AVAVIDPATAG----AEESGGRPAVAAPGRIVLLTSGTTGKPKGVprapqLRSAVGVWVTI---LD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 156 QYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAepgRHGDP---VHLADLIRRHGVTVihfVPAMLAAFNEVLGA 232
Cdd:PRK13383 211 RTRLRTGSRISVAMPMFHGLGLGMLMLTIALGGTVLTH---RHFDAeaaLAQASLHRADAFTA---VPVVLARILELPPR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 233 --GVGELTSLRLIQTGGEALTPPVARDLMvRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAAL 310
Cdd:PRK13383 285 vrARNPLPQLRVVMSSGDRLDPTLGQRFM-DTYGDILYNGYGSTEVGIGALATPADLRDAPETVGKPVAGCPVRILDRNN 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 311 REVPIGVPGELYLGGVQLARGYAGrpdlTAERFVADPfgepgarLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELG 390
Cdd:PRK13383 364 RPVGPRVTGRIFVGGELAGTRYTD----GGGKAVVDG-------MTSTGDMGYLDNAGRLFIVGREDDMIISGGENVYPR 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 391 EVEAALAAAPGVL-HAAAAVVDGPGGQQLVGYLAP---ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRR 466
Cdd:PRK13383 433 AVENALAAHPAVAdNAVIGVPDERFGHRLAAFVVLhpgSGVDAAQLRDYLKDRVSRFEQPRDINIVSSIPRNPTGKVLRK 512
|
...
gi 1827387616 467 LLP 469
Cdd:PRK13383 513 ELP 515
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
2566-3059 |
1.71e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 95.71 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVvDGAGARLTYRELDEASDRLARWLIGR-GVGPERAVALAIGRSAQLLTAIWAVAKTGGAYV 2644
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAY-HSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2645 PIDPDYPAERVASMIEDSGAvlglSVLASGDLPGQEFEWMrLDDDSVAAEIAA------------------------VPA 2700
Cdd:PRK08751 105 NVNPLYTPRELKHQLIDSGA----SVLVVIDNFGTTVQQV-IADTPVKQVITTglgdmlgfpkaalvnfvvkyvkklVPE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2701 GPITDAERLGEVTAA--------------NLAYVIYTSGSTGRPKGVAVTHSGL-ANFAR-----QESDRLNAGDNPVVl 2760
Cdd:PRK08751 180 YRINGAIRFREALALgrkhsmptlqiepdDIAFLQYTGGTTGVAKGAMLTHRNLvANMQQahqwlAGTGKLEEGCEVVI- 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2761 gfaspsfDASVLEYLLATVNEGT----------LAYRPSEaVGGEVLE----RFIAEHGATHTFltPSVLST--MDPTAV 2824
Cdd:PRK08751 259 -------TALPLYHIFALTANGLvfmkiggcnhLISNPRD-MPGFVKElkktRFTAFTGVNTLF--NGLLNTpgFDQIDF 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2825 PSLRVIAAGGEAVPQPIVDRWAPAT--ELHNLYGPTETTIGITISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMP 2902
Cdd:PRK08751 329 SSLKMTLGGGMAVQRSVAERWKQVTglTLVEAYGLTETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2903 GELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVRwtpdTDTGGLtLEYTGRSDDQVKLRGLRIELGEIE 2982
Cdd:PRK08751 409 GELCIKGPQVMKGYWKRPEETAKVMDADGW-------LHTGDIAR----MDEQGF-VYIVDRKKDMILVSGFNVYPNEIE 476
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 2983 AVLAEHDAVESAVVLGVGGSVA-TALAAYIVPVDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK08751 477 DVIAMMPGVLEVAAVGVPDEKSgEIVKVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1050-1524 |
1.76e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 95.65 E-value: 1.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALI-CD-GTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAY 1127
Cdd:PRK08315 30 PDREALVyRDqGLRWTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTINPAYRLSELEY 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1128 MLEDSGATVGITDASTR-------------------------ARL----------GESSCEWVDLADLEAEAESGDDITD 1172
Cdd:PRK08315 110 ALNQSGCKALIAADGFKdsdyvamlyelapelatcepgqlqsARLpelrrviflgDEKHPGMLNFDELLALGRAVDDAEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1173 TERNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVD---FVNSLAKITtgtPEDepdtRI-LHVasP---SFDASMFEM 1245
Cdd:PRK08315 190 AARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNngyFIGEAMKLT---EED----RLcIPV--PlyhCFGMVLGNL 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1246 AwAIPAGHTLVIAPQADFAGDALATVleRDE-------VTDMIItpSVLAtvDPERAQY-VRNLATG---GEACPPELVE 1314
Cdd:PRK08315 261 A-CVTHGATMVYPGEGFDPLATLAAV--EEErctalygVPTMFI--AELD--HPDFARFdLSSLRTGimaGSPCPIEVMK 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1315 RWSER--GRRIFNCYGPTEATVWATRSRMTAgkPV-----TIGKPVDGFTVRVLD---GRlhEVPQGVVGELylstagLA 1384
Cdd:PRK08315 334 RVIDKmhMSEVTIAYGMTETSPVSTQTRTDD--PLekrvtTVGRALPHLEVKIVDpetGE--TVPRGEQGEL------CT 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1385 RGY---LG---RPGQTAVSFVADPFgepgarMYaTGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVA 1458
Cdd:PRK08315 404 RGYsvmKGywnDPEKTAEAIDADGW------MH-TGDLAVMDEEGYVNIVGRIKDMIIRGGENIYPREIEEFLYTHPKIQ 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 1459 QSVVVGVESTRGGRkhtEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGK 1524
Cdd:PRK08315 477 DVQVVGVPDEKYGE---EVCAWIILRPGATLTEEDVRDFCRGKIAHYKIPRYIRFVDEFPMTVTGK 539
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
120-468 |
2.20e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 95.09 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 120 PANAAFTLFTSGSTGRPKAVVITHRGIAnrlaADIEQYDLTARDVFLYKAPITFDVSV-----REIF-------LPIAIG 187
Cdd:PRK07059 203 PDDVAFLQYTGGTTGVSKGATLLHRNIV----ANVLQMEAWLQPAFEKKPRPDQLNFVcalplYHIFaltvcglLGMRTG 278
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 188 AT-LVIAepgrhgDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGA-GVGEL--TSLRLIQTGGEALTPPVARDlMVRLP 263
Cdd:PRK07059 279 GRnILIP------NPRDIPGFIKELKKYQVHIFPAVNTLYNALLNNpDFDKLdfSKLIVANGGGMAVQRPVAER-WLEMT 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 264 GTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERF 343
Cdd:PRK07059 352 GCPITEGYGLSETSPVATCNPVDATEFSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDETAKVM 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 344 VADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYL 422
Cdd:PRK07059 432 TADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAvGVPDEHSGEAVKLFV 504
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1827387616 423 APADVDV--DTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK07059 505 VKKDPALteEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1062-1508 |
2.91e-19 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 93.96 E-value: 2.91e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1062 MDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDA 1141
Cdd:cd05940 4 LTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLVVDA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1142 strarlgesscewvdladleaeaesgdditdterngsvrltnlAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGT 1221
Cdd:cd05940 84 -------------------------------------------ALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGAL 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1222 PEDepdtrILHVASPSFDASMFEMAWA--IPAGHTLVIAPQ---ADFAGDALAtvlERDEVTDMI--ITPSVLAT--VDP 1292
Cdd:cd05940 121 PSD-----VLYTCLPLYHSTALIVGWSacLASGATLVIRKKfsaSNFWDDIRK---YQATIFQYIgeLCRYLLNQppKPT 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1293 ERAQYVRnlATGGEACPPELVERWSERGR--RIFNCYGPTEATVWATRsrmTAGKPVTIGK----PVDGFTVRVL----- 1361
Cdd:cd05940 193 ERKHKVR--MIFGNGLRPDIWEEFKERFGvpRIAEFYAATEGNSGFIN---FFGKPGAIGRnpslLRKVAPLALVkydle 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1362 --------DGRLHEVPQGVVGELYLSTAGLAR--GYLGrPGQTAVSFVADPFgEPGARMYATGDLVRVAKGGNLEFAGRA 1431
Cdd:cd05940 268 sgepirdaEGRCIKVPRGEPGLLISRINPLEPfdGYTD-PAATEKKILRDVF-KKGDAWFNTGDLMRLDGEGFWYFVDRL 345
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 1432 DHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTR-GGRKHtevVAYLVAKPGATIDSAAVLDEAAQHLAAHMVP 1508
Cdd:cd05940 346 GDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVQVPGtDGRAG---MAAIVLQPNEEFDLSALAAHLEKNLPGYARP 420
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
117-468 |
3.59e-19 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 94.52 E-value: 3.59e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 117 PTRPANAAFTLFTSGSTGRPKAVVITHRGianrLAADIE--------QYDLTARD-VFLYKAPItFDVSVREIFLP--IA 185
Cdd:PLN02574 194 VIKQDDVAAIMYSSGTTGASKGVVLTHRN----LIAMVElfvrfeasQYEYPGSDnVYLAALPM-FHIYGLSLFVVglLS 268
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 186 IGATLVIAepgRHGDPVHLADLIRRHGVTVIHFVPAMLAAF-NEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLPG 264
Cdd:PLN02574 269 LGSTIVVM---RRFDASDMVKVIDRFKVTHFPVVPPILMALtKKAKGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTLPH 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 265 TRLQNQYGPAEASIVVTIHRVT-QDDRVIPIGTPTRRVSARVLD---AALreVPIGVPGELYLGGVQLARGYAGRPDLTA 340
Cdd:PLN02574 346 VDFIQGYGMTESTAVGTRGFNTeKLSKYSSVGLLAPNMQAKVVDwstGCL--LPPGNCGELWIQGPGVMKGYLNNPKATQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 341 ERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAA-AAVVDGPGGQQLV 419
Cdd:PLN02574 424 STIDKDGW-------LRTGDIAYFDEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAvTAVPDKECGEIPV 496
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 420 GY--------LAPADVdVDTVAATTAellpEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PLN02574 497 AFvvrrqgstLSQEAV-INYVAKQVA----PYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1050-1466 |
4.95e-19 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 93.01 E-value: 4.95e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPAD------ 1123
Cdd:PRK09029 17 PQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPlleell 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1124 -----RIAYMLEDSGATVGITDASTRARLGESSCEWvdladleaeaesgdditdterngsvRLTNLAYLIYTSGSTGRPK 1198
Cdd:PRK09029 97 psltlDFALVLEGENTFSALTSLHLQLVEGAHAVAW-------------------------QPQRLATMTLTSGSTGLPK 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1199 AvgVSHT---------GIVDFVNSLAKittgtpedepDTRILHVasPSFDASMFEMAWA-IPAGHTLVIAPQADFAgDAL 1268
Cdd:PRK09029 152 A--AVHTaqahlasaeGVLSLMPFTAQ----------DSWLLSL--PLFHVSGQGIVWRwLYAGATLVVRDKQPLE-QAL 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1269 ATV---------LER--DEVTDMIITPSVLatvdperaqyvrnlaTGGEACPPELVERWSERGRRIFNCYGPTEA--TVW 1335
Cdd:PRK09029 217 AGCthaslvptqLWRllDNRSEPLSLKAVL---------------LGGAAIPVELTEQAEQQGIRCWCGYGLTEMasTVC 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1336 ATRSRMTAGkpvtIGKPVDGFTVRVLDgrlhevpqgvvGELYLSTAGLARGYLgRPGQTaVSFVadpfGEPGarMYATGD 1415
Cdd:PRK09029 282 AKRADGLAG----VGSPLPGREVKLVD-----------GEIWLRGASLALGYW-RQGQL-VPLV----NDEG--WFATRD 338
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 1416 LVRVAkGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVE 1466
Cdd:PRK09029 339 RGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVA 388
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1051-1533 |
5.12e-19 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 94.12 E-value: 5.12e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1051 DHPALICDGTEMDYDEFETRTNAIARALLAR-GVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:PRK12492 39 DRPAFSNLGVTLSYAELERHSAAFAAYLQQHtDLVPGDRIAVQMPNVLQYPIAVFGALRAGLIVVNTNPLYTAREMRHQF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGAT----VGITDASTRARLGESSCEW---VDLADLEAEAESG--DDITDTE-------------------RNG---- 1177
Cdd:PRK12492 119 KDSGARalvyLNMFGKLVQEVLPDTGIEYlieAKMGDLLPAAKGWlvNTVVDKVkkmvpayhlpqavpfkqalRQGrgls 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1178 ----SVRLTNLAYLIYTSGSTGRPKAVGVSHTGIV-DFVNSLAKITTGTPEDEPDTR----ILHVASPSFDASMFE---M 1245
Cdd:PRK12492 199 lkpvPVGLDDIAVLQYTGGTTGLAKGAMLTHGNLVaNMLQVRACLSQLGPDGQPLMKegqeVMIAPLPLYHIYAFTancM 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1246 AWAIPAGHTLVIAPQADFAGdaLATVLERDEVTDMI-ITPSVLATVD-PERAQY----VRNLATGGEACPPELVERWSE- 1318
Cdd:PRK12492 279 CMMVSGNHNVLITNPRDIPG--FIKELGKWRFSALLgLNTLFVALMDhPGFKDLdfsaLKLTNSGGTALVKATAERWEQl 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1319 RGRRIFNCYGPTEAT-VWATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVS 1397
Cdd:PRK12492 357 TGCTIVEGYGLTETSpVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEA 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1398 FVADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteV 1477
Cdd:PRK12492 437 LDAEGW-------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDERSGEA---V 506
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 1478 VAYLVAK-PGATIDSAAVLdeAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEP 1533
Cdd:PRK12492 507 KLFVVARdPGLSVEELKAY--CKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1176-1526 |
6.29e-19 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 94.99 E-value: 6.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1176 NGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtRILHVAsPSFDASMFEMAWAIPA--GH 1253
Cdd:PRK08633 776 GPTFKPDDTATIIFSSGSEGEPKGVMLSHHNILSNIEQISDVFNLRNDD----VILSSL-PFFHSFGLTVTLWLPLleGI 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1254 TLVIAPQ-ADfaGDALATVLERDEVTDMIITPSVLAT------VDPERAQYVRNLATGGEACPPELVERWSER-GRRIFN 1325
Cdd:PRK08633 851 KVVYHPDpTD--ALGIAKLVAKHRATILLGTPTFLRLylrnkkLHPLMFASLRLVVAGAEKLKPEVADAFEEKfGIRILE 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1326 CYGPTEATVWATRS----------RMTAGKPVTIGKPVDGFTVRVLD-GRLHEVPQGVVGELYLSTAGLARGYLGRPGQT 1394
Cdd:PRK08633 929 GYGATETSPVASVNlpdvlaadfkRQTGSKEGSVGMPLPGVAVRIVDpETFEELPPGEDGLILIGGPQVMKGYLGDPEKT 1008
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1395 AvSFVADPfgePGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIE----AVLDAQPGVAqsVVVGVESTRG 1470
Cdd:PRK08633 1009 A-EVIKDI---DGIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEeelaKALGGEEVVF--AVTAVPDEKK 1082
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 1471 GrkhtEVVAYLVAKPgaTIDSAAVLDE-AAQHLAAHMVPSQAIVIDEIPLTPAGKLD 1526
Cdd:PRK08633 1083 G----EKLVVLHTCG--AEDVEELKRAiKESGLPNLWKPSRYFKVEALPLLGSGKLD 1133
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
2564-3145 |
7.44e-19 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 95.24 E-value: 7.44e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2564 PVTLAELFRAAARRAPDHVAV-----VDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALaIGRSAQLLTAIWAVAK 2638
Cdd:PRK05691 8 PLTLVQALQRRAAQTPDRLALrfladDPGEGVVLSYRDLDLRARTIAAALQARASFGDRAVLL-FPSGPDYVAAFFGCLY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2639 TGGAYVPIDPDYPA-----ERVASMIEDSGAVLGLSVLASGDlPGQEFEWMRLDDdsvAAEIAAVPAGPITDAERLGE-- 2711
Cdd:PRK05691 87 AGVIAVPAYPPESArrhhqERLLSIIADAEPRLLLTVADLRD-SLLQMEELAAAN---APELLCVDTLDPALAEAWQEpa 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2712 VTAANLAYVIYTSGSTGRPKGVAVTHSGL-AN--FARQeSDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRP 2788
Cdd:PRK05691 163 LQPDDIAFLQYTSGSTALPKGVQVSHGNLvANeqLIRH-GFGIDLNPDDVIVSWLPLYHDMGLIGGLLQPIFSGVPCVLM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2789 SEAVggeVLER------FIAEHGAT------------HTFLTPSVLSTMDptaVPSLRVIAAGGEAVPQPIVDRWAP--- 2847
Cdd:PRK05691 242 SPAY---FLERplrwleAISEYGGTisggpdfayrlcSERVSESALERLD---LSRWRVAYSGSEPIRQDSLERFAEkfa 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2848 -----ATELHNLYGPTETTIGITIS------SAMR------------PGDPVRL---GGPIGGVDLMVLD-ERLRPVPVG 2900
Cdd:PRK05691 316 acgfdPDSFFASYGLAEATLFVSGGrrgqgiPALEldaealarnraePGTGSVLmscGRSQPGHAVLIVDpQSLEVLGDN 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2901 MPGELYVAGGALSRGYLDRSGLTAERFTANpygtAGQRMYRTGDVvrwtpdtdtGGL---TLEYTGRSDDQVKLRGLRIE 2977
Cdd:PRK05691 396 RVGEIWASGPSIAHGYWRNPEASAKTFVEH----DGRTWLRTGDL---------GFLrdgELFVTGRLKDMLIVRGHNLY 462
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2978 LGEIEAVlaehdaVESAVVLGVGGSVatalAAYIVPVDG------AVEVSE-----------LKAFAGGRLPAYM-VPSS 3039
Cdd:PRK05691 463 PQDIEKT------VEREVEVVRKGRV----AAFAVNHQGeegigiAAEISRsvqkilppqalIKSIRQAVAEACQeAPSV 532
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3040 FTVID--ELPLTPVGKLdKRALPEPVLEAGEYVA----PATGTERTIADVAAG-------------VLNIDAglVSATSS 3100
Cdd:PRK05691 533 VLLLNpgALPKTSSGKL-QRSACRLRLADGSLDSyalfPALQAVEAAQTAASGdelqariaaiwceQLKVEQ--VAADDH 609
|
650 660 670 680
....*....|....*....|....*....|....*....|....*
gi 1827387616 3101 FFELGGDSLSAARLAARLSDQLGVAVSVRDVFESGSIRALAETVG 3145
Cdd:PRK05691 610 FFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVA 654
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1050-1530 |
9.88e-19 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 93.16 E-value: 9.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:PRK07059 37 ADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNPLYTPRELEHQL 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGA-----------TVGITDASTR------ARLGE-----------------------SSCEWVDLADLEAEAE---- 1165
Cdd:PRK07059 117 KDSGAeaivvlenfatTVQQVLAKTAvkhvvvASMGDllgfkghivnfvvrrvkkmvpawSLPGHVRFNDALAEGArqtf 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1166 -----SGDDItdterngsvrltnlAYLIYTSGSTGRPKAVGVSHTGIVDFV--NSLAKITTGTPEDEPDTRILHVASPSF 1238
Cdd:PRK07059 197 kpvklGPDDV--------------AFLQYTGGTTGVSKGATLLHRNIVANVlqMEAWLQPAFEKKPRPDQLNFVCALPLY 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1239 D------ASMFEMAwaiPAGHTLVIAPQADFAGdaLATVLERDEVTdmiITPSV-------LATVDPERAQYVRNLAT-- 1303
Cdd:PRK07059 263 HifaltvCGLLGMR---TGGRNILIPNPRDIPG--FIKELKKYQVH---IFPAVntlynalLNNPDFDKLDFSKLIVAng 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1304 GGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSRMTAGK-PVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTA 1381
Cdd:PRK07059 335 GGMAVQRPVAERWLEMtGCPITEGYGLSETSPVATCNPVDATEfSGTIGLPLPSTEVSIRDDDGNDLPLGEPGEICIRGP 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1382 GLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSV 1461
Cdd:PRK07059 415 QVMAGYWNRPDETAKVMTADGF-------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEEVVASHPGVLEVA 487
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 1462 VVGVESTRGGrkhtEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK07059 488 AVGVPDEHSG----EAVKLFVVKKDPALTEEDVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
127-463 |
1.22e-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: 89.87 E-value: 1.22e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 127 LFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPITFDVSVREIFLPIAI-GATLViaePGRHGDPVHLA 205
Cdd:cd17638 6 MFTSGTTGRSKGVMCAHRQTLRAAAAWADCADLTEDDRYLIINPFFHTFGYKAGIVACLLtGATVV---PVAVFDVDAIL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 206 DLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEAsIVVTIHRv 285
Cdd:cd17638 83 EAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVLTAYGLTEA-GVATMCR- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 286 tQDDRVIPIGTPTRRVSARVldaalrEVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWN 365
Cdd:cd17638 161 -PGDDAETVATTCGRACPGF------EVRIADDGEVLVRGYNVMQGYLDDPEATAEAIDADGW-------LHTGDVGELD 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 366 RDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVD----GPGGQQLVGYLAPADVDVDTVAATTAELLP 441
Cdd:cd17638 227 ERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPdermGEVGKAFVVARPGVTLTEEDVIAWCRERLA 306
|
330 340
....*....|....*....|..
gi 1827387616 442 EYMRPSAWVRLDAMPLSRSGKV 463
Cdd:cd17638 307 NYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
2592-3142 |
1.30e-18 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 93.17 E-value: 1.30e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2592 LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLglsVL 2671
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPAL---VV 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2672 ASGDLpgqefewmrldDDSVAAEIAAVPAGPITDAERLGE-----VTAANLAYVIYTSGSTGRPKGVAVTHSGLANFAR- 2745
Cdd:PRK06060 108 TSDAL-----------RDRFQPSRVAEAAELMSEAARVAPggyepMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDa 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2746 --QESDRLNAGDnpVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGGEVLERFIAEHGATHTFLTPS----VLSTM 2819
Cdd:PRK06060 177 mcRKALRLTPED--TGLCSARMYFAYGLGNSVWFPLATGGSAVINSAPVTPEAAAILSARFGPSVLYGVPNffarVIDSC 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2820 DPTAVPSLRVIAAGGEAVPQPIVDRwapATELHN----LYGPTETTIGIT-ISSAMRPGDPVRLGGPIGGVDLMVLDERL 2894
Cdd:PRK06060 255 SPDSFRSLRCVVSAGEALELGLAER---LMEFFGgipiLDGIGSTEVGQTfVSNRVDEWRLGTLGRVLPPYEIRVVAPDG 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2895 RPVPVGMPGELYVAGGALSRGYLDRSgltaerftaNPYGTAGQRMyRTGDVVRWTPDtdtGGLTleYTGRSDDQVKLRGL 2974
Cdd:PRK06060 332 TTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWL-DTRDRVCIDSD---GWVT--YRCRADDTEVIGGV 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2975 RIELGEIEAVLAEHDAVESAVVLGVGGSV-ATALAAYIVP-----VDGAVeVSELKAFAGGRLPAYMVPSSFTVIDELPL 3048
Cdd:PRK06060 397 NVDPREVERLIIEDEAVAEAAVVAVRESTgASTLQAFLVAtsgatIDGSV-MRDLHRGLLNRLSAFKVPHRFAVVDRLPR 475
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3049 TPVGKLDKRAL-----PEPVLE------------------AGEYVAPATGT----------------ERTIADVAAG--- 3086
Cdd:PRK06060 476 TPNGKLVRGALrkqspTKPIWElsltepgsgvraqrddlsASNMTIAGGNDggatlrerlvalrqerQRLVVDAVCAeaa 555
|
570 580 590 600 610
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 3087 --VLNIDAGLVSATSSFFELGGDSLSAARLAARLSDQLGVAVSVRDVFESGSIRALAE 3142
Cdd:PRK06060 556 kmLGEPDPWSVDQDLAFSELGFDSQMTVTLCKRLAAVTGLRLPETVGWDYGSISGLAQ 613
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1015-1532 |
1.83e-18 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 92.26 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1015 VSAPVSARTPGAMVGRGgeveAGTLIDVLAQRDldPDHPALIC--DGTEMDYDEFETRTNAIARALLARGVSPEDVVAVG 1092
Cdd:PRK05852 1 MRFMGGAAPMASDFGPR----IADLVEVAATRL--PEAPALVVtaDRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALR 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1093 MERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDASTRARLGESSCEWVDLA------DLEAEAES 1166
Cdd:PRK05852 75 MGSNAEFVVALLAASRADLVVVPLDPALPIAEQRVRSQAAGARVVLIDADGPHDRAEPTTRWWPLTvnvggdSGPSGGTL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1167 GDDITDTERNGSVRLTNL------AYLIYTSGSTGRPKAVGVSHTGIVDFVNSlakITTGTPEDEPDTRIlhVASPSFDA 1240
Cdd:PRK05852 155 SVHLDAATEPTPATSTPEglrpddAMIMFTGGTTGLPKMVPWTHANIASSVRA---IITGYRLSPRDATV--AVMPLYHG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1241 S--MFEMAWAIPAGHTLVIAPQADFAGDALATVLERDEVTDMIITPSV----LATVDPERAQYVRNLATGGEACPPELVE 1314
Cdd:PRK05852 230 HglIAALLATLASGGAVLLPARGRFSAHTFWDDIKAVGATWYTAVPTIhqilLERAATEPSGRKPAALRFIRSCSAPLTA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1315 RWSERGRRIFNC-----YGPTEATVWATRSRMTAG----KPVTIGKPVD---GFTVRVLDGRLHEVPQGVVGELYLSTAG 1382
Cdd:PRK05852 310 ETAQALQTEFAApvvcaFGMTEATHQVTTTQIEGIgqteNPVVSTGLVGrstGAQIRIVGSDGLPLPAGAVGEVWLRGTT 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1383 LARGYLGRPGQTAVSFVADPFgepgarmyATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVV 1462
Cdd:PRK05852 390 VVRGYLGDPTITAANFTDGWL--------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAV 461
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1463 VGVESTRGGRkhtEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:PRK05852 462 FGVPDQLYGE---AVAAVIVPRESAPPTAEELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1-439 |
2.03e-18 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 92.42 E-value: 2.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVV----AIHA---VA--------MAGGH-------------F 52
Cdd:PRK12582 81 VTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALmtlaAMQAgvpAApvspayslMSHDHaklkhlfdlvkprV 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 53 VPLDEQLPVDRARYMVRTAGVRLVVVTSDGEAEARSRFDDIVdvhvldiSSPGDADLdEEEFAGPTrPANAAFTLFTSGS 132
Cdd:PRK12582 161 VFAQSGAPFARALAALDLLDVTVVHVTGPGEGIASIAFADLA-------ATPPTAAV-AAAIAAIT-PDTVAKYLFTSGS 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 133 TGRPKAVVITHRGIANRLAAdieQYDLTARD------VFLYKAPITFDVSVREIFLPIAI-GATLVIAE----PGRHGDP 201
Cdd:PRK12582 232 TGMPKAVINTQRMMCANIAM---QEQLRPREpdppppVSLDWMPWNHTMGGNANFNGLLWgGGTLYIDDgkplPGMFEET 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 202 VHladLIRRHGVTVIHFVPAMLAAF------NEVLGAGVgeLTSLRLIQTGGEALTPPV---ARDLMVRLPGTR--LQNQ 270
Cdd:PRK12582 309 IR---NLREISPTVYGNVPAGYAMLaeamekDDALRRSF--FKNLRLMAYGGATLSDDLyerMQALAVRTTGHRipFYTG 383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 271 YGPAEAS-IVVTIHRVTqdDRVIPIGTPTRRVsarvldaALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFg 349
Cdd:PRK12582 384 YGATETApTTTGTHWDT--ERVGLIGLPLPGV-------ELKLAPVGDKYEVRVKGPNVTPGYHKDPELTAAAFDEEGF- 453
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 350 epgarlYRTGDRARW--NRDGE--IEYLGRTDFQVKL-RGQRLELGEVEA-ALAAAPGVLHaaAAVVDG----------- 412
Cdd:PRK12582 454 ------YRLGDAARFvdPDDPEkgLIFDGRVAEDFKLsTGTWVSVGTLRPdAVAACSPVIH--DAVVAGqdrafigllaw 525
|
490 500 510
....*....|....*....|....*....|
gi 1827387616 413 ---PGGQQLVGYLAPADVDVDTVAATTAEL 439
Cdd:PRK12582 526 pnpAACRQLAGDPDAAPEDVVKHPAVLAIL 555
|
|
| NRPS-para261 |
TIGR01720 |
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately ... |
1942-2097 |
2.35e-18 |
|
non-ribosomal peptide synthase domain TIGR01720; This domain appears to be located immediately downstream from a condensation domain (pfam00668), and is followed primarily by the end of the molecule or another condensation domain (in a few cases it is followed by pfam00501, an AMP-binding module). The converse is not true, pfam00668 domains are not always followed by this domain. This implicates this domain in possible post-condensation modification events. This model is 171 amino acids long and contains three very highly conserved regions. At the N-terminus is a nearly invariant lysine (position 11) followed by xxxRxxPxxGxGYG in which the proline and the first glycine are invariant. This is followed approximately 22 residues later by the motif FNYLG. Near the C-terminus of the domain is the sequence TxSD where the serine and aspartate are nearly invariant.
Pssm-ID: 273774 [Multi-domain] Cd Length: 153 Bit Score: 84.25 E-value: 2.35e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1942 HAVKSAKDARLSRPAGGVGFGILRY--NSDGEIAHRPLPTIMYNYFGGGTAPSTEtapDDFLPVSDRPNmpSSITGAMRS 2019
Cdd:TIGR01720 4 RLIKAVKEQLRRIPNKGVGYGVLRYltEPEEKLAASPQPEISFNYLGQFDADSND---ELFQPSSYSPG--EAISPESPR 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 2020 PSVFGINistAGREERRLEAKVTYATDALDEAAASDIARRWHDELRAVVELVDGGAEIGLSRADVPGVEVTQDDLDLI 2097
Cdd:TIGR01720 79 PYALEIN---AMIEDGELTLTWSYPTQLFSEDTIEQLADRFKEALEALIAHCAGKEGGGLTPSDFSLKDLTQDELDEL 153
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1050-1530 |
3.15e-18 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 91.65 E-value: 3.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARAL-----LARGvspeDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADR 1124
Cdd:PRK08974 37 ADQPAFINMGEVMTFRKLEERSRAFAAYLqnglgLKKG----DRVALMMPNLLQYPIALFGILRAGMIVVNVNPLYTPRE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1125 IAYMLEDSGAT--VGITD-ASTRARLGESSC-EWVDLADLeaeaesGDDITDTER---NGSVRL---------------- 1181
Cdd:PRK08974 113 LEHQLNDSGAKaiVIVSNfAHTLEKVVFKTPvKHVILTRM------GDQLSTAKGtlvNFVVKYikrlvpkyhlpdaisf 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1182 -------------------TNLAYLIYTSGSTGRPKAVGVSHTGIVdfVNSLAKITTGTPEDEPDTRIL-------HVAS 1235
Cdd:PRK08974 187 rsalhkgrrmqyvkpelvpEDLAFLQYTGGTTGVAKGAMLTHRNML--ANLEQAKAAYGPLLHPGKELVvtalplyHIFA 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1236 PSFDASMF-EMAwaipaGHTLVIAPQADFagDALATVLERDEVTDMIITPSVL-ATVDPERAQYV-----RNLATGGEAC 1308
Cdd:PRK08974 265 LTVNCLLFiELG-----GQNLLITNPRDI--PGFVKELKKYPFTAITGVNTLFnALLNNEEFQELdfsslKLSVGGGMAV 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1309 PPELVERWSE-RGRRIFNCYGPTEAtvwatrSRMTAGKPV-------TIGKPVDGFTVRVLDGRLHEVPQGVVGELYLST 1380
Cdd:PRK08974 338 QQAVAERWVKlTGQYLLEGYGLTEC------SPLVSVNPYdldyysgSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKG 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1381 AGLARGYLGRPGQTAvSFVADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQS 1460
Cdd:PRK08974 412 PQVMLGYWQRPEATD-EVIKDGW-------LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEV 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1461 VVVGVESTRGGrkhtEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK08974 484 AAVGVPSEVSG----EAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
127-468 |
3.23e-18 |
|
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: 91.61 E-value: 3.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 127 LFTSGSTGRPKAVVITHRGIANRLAADIEQ-YDLTARDVFLYKAPITFDVSVREI-FLPIAIGATLVIAE--PGRHGDPV 202
Cdd:cd05967 236 LYTSGTTGKPKGVVRDNGGHAVALNWSMRNiYGIKPGDVWWAASDVGWVVGHSYIvYGPLLHGATTVLYEgkPVGTPDPG 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 203 HLADLIRRHGVTVIHFVPAMLAAF-----NEVLGAGVgELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNqYGPAEAS 277
Cdd:cd05967 316 AFWRVIEKYQVNALFTAPTAIRAIrkedpDGKYIKKY-DLSSLRTLFLAGERLDPPTLEWAENTLGVPVIDH-WWQTETG 393
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 278 IVVTIHRVTQDDRVIPIGTPTRRV---SARVLDAALREVPIGVPGELYLGGvQLARGYAGRPDLTAERFVADPFGE-PGa 353
Cdd:cd05967 394 WPITANPVGLEPLPIKAGSPGKPVpgyQVQVLDEDGEPVGPNELGNIVIKL-PLPPGCLLTLWKNDERFKKLYLSKfPG- 471
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 354 rLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAPadvdVDTV 432
Cdd:cd05967 472 -YYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAVvGVRDELKGQVPLGLVVL----KEGV 546
|
330 340 350 360
....*....|....*....|....*....|....*....|....*..
gi 1827387616 433 AATTAELLPEYMR-------PSAWVRL----DAMPLSRSGKVDRRLL 468
Cdd:cd05967 547 KITAEELEKELVAlvreqigPVAAFRLvifvKRLPKTRSGKILRRTL 593
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1059-1532 |
4.06e-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: 91.05 E-value: 4.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1059 GTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATV-- 1136
Cdd:cd17642 42 GVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISKPTIvf 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1137 --------------------GITDASTRARLGESSCewvDLADLEAEAESGDDITDTERNGSVRLTNLAYLIYTSGSTGR 1196
Cdd:cd17642 122 cskkglqkvlnvqkklkiikTIIILDSKEDYKGYQC---LYTFITQNLPPGFNEYDFKPPSFDRDEQVALIMNSSGSTGL 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1197 PKAVGVSHTGIVDFVNSLAKITTGTpEDEPDTRILHVAsPSFDA-SMFEMAWAIPAGHTLVIAPQadFAGDALATVLERD 1275
Cdd:cd17642 199 PKGVQLTHKNIVARFSHARDPIFGN-QIIPDTAILTVI-PFHHGfGMFTTLGYLICGFRVVLMYK--FEEELFLRSLQDY 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1276 EVTDMIITPSVLA------TVDPERAQYVRNLATGGEACPPELVERWSERGRRIF--NCYGPTEATVWATRSRMTAGKPV 1347
Cdd:cd17642 275 KVQSALLVPTLFAffakstLVDKYDLSNLHEIASGGAPLSKEVGEAVAKRFKLPGirQGYGLTETTSAILITPEGDDKPG 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1348 TIGKPVDGFTVRVLD---GRLHEVPQgvVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRVAKGGN 1424
Cdd:cd17642 355 AVGKVVPFFYAKVVDldtGKTLGPNE--RGELCVKGPMIMKGYVNNPEATKALIDKDGW-------LHSGDIAYYDEDGH 425
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1425 LEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKHTEVVaylVAKPGATIDSAAVLD-EAAQHLA 1503
Cdd:cd17642 426 FFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVV---VLEAGKTMTEKEVMDyVASQVST 502
|
490 500
....*....|....*....|....*....
gi 1827387616 1504 AHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:cd17642 503 AKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1064-1463 |
5.00e-18 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 89.93 E-value: 5.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLARGVSPEDVVAVgmerSIGSVLATW----GVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGIT 1139
Cdd:cd05974 3 FAEMSARSSRVANFLRSIGVGRGDRILL----MLGNVVELWeamlAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1140 DASTRArlgesscewvdladleaeaesgDDITdterngsvrltnlaYLIYTSGSTGRPKAVGVSHTGI-VDFVNSLAKIT 1218
Cdd:cd05974 79 DENTHA----------------------DDPM--------------LLYFTSGTTSKPKLVEHTHRSYpVGHLSTMYWIG 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1219 TgtpedEPDTRILHVASPSFDA---SMFEMAWAipAGHTLVIAPQADFAGDALATVLERDEVTDMIITPSV---LATVDP 1292
Cdd:cd05974 123 L-----KPGDVHWNISSPGWAKhawSCFFAPWN--AGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPTVwrmLIQQDL 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1293 ERAQY-VRNLATGGEACPPELVER----WserGRRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHE 1367
Cdd:cd05974 196 ASFDVkLREVVGAGEPLNPEVIEQvrraW---GLTIRDGYGQTETTALVGNSPGQPVKAGSMGRPLPGYRVALLDPDGAP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1368 VPQGVVGeLYLST---AGLARGYLGRPGQTAvsfvadpfGEPGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVEL 1444
Cdd:cd05974 273 ATEGEVA-LDLGDtrpVGLMKGYAGDPDKTA--------HAMRGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISP 343
|
410
....*....|....*....
gi 1827387616 1445 GEIEAVLDAQPGVAQSVVV 1463
Cdd:cd05974 344 FELESVLIEHPAVAEAAVV 362
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
1036-1530 |
5.03e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 90.51 E-value: 5.03e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1036 AGTLIDVLAQRdLDPDHPALICDGTEMDYDEFETRTNAIA---RALLARGVSPEdvVAVGMERSIGSVLATWGVIKSGAA 1112
Cdd:PRK07867 4 APTVAELLLPL-AEDDDRGLYFEDSFTSWREHIRGSAARAaalRARLDPTRPPH--VGVLLDNTPEFSLLLGAAALSGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1113 YVPVDPAYPADRIAYMLEDSGATVGITDASTRARLGE----------SSCEWVDLADLEAEAEsgdditdtERNGSVRLT 1182
Cdd:PRK07867 81 PVGLNPTRRGAALARDIAHADCQLVLTESAHAELLDGldpgvrvinvDSPAWADELAAHRDAE--------PPFRVADPD 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1183 NLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtrILHVASPSF--DASMFEMAWAIPAGHTLVI--- 1257
Cdd:PRK07867 153 DLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDD-----VCYVSMPLFhsNAVMAGWAVALAAGASIALrrk 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1258 --------------APQADFAGDALATVLERDEVtdmiitpsvlatvdPERAQYVRNLATGGEACPPElVERWSER-GRR 1322
Cdd:PRK07867 228 fsasgflpdvrrygATYANYVGKPLSYVLATPER--------------PDDADNPLRIVYGNEGAPGD-IARFARRfGCV 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1323 IFNCYGPTEATVWATRSRMTagKPVTIGKPVDGFTVRVLDGRlHEVPQGV------------VGELYLST-AGLARGYLG 1389
Cdd:PRK07867 293 VVDGFGSTEGGVAITRTPDT--PPGALGPLPPGVAIVDPDTG-TECPPAEdadgrllnadeaIGELVNTAgPGGFEGYYN 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1390 RPGQTAvsfvadpfgepgARM----YATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGV 1465
Cdd:PRK07867 370 DPEADA------------ERMrggvYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAV 437
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 1466 -ESTRGGRkhteVVAYLVAKPGATIDSAAV---LDEAAQhLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK07867 438 pDPVVGDQ----VMAALVLAPGAKFDPDAFaefLAAQPD-LGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1358-1607 |
5.47e-18 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 87.50 E-value: 5.47e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1358 VRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGEPGARMYATGDLVRVAKGGNLEFAGRADHQVKI 1437
Cdd:COG3433 25 VQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGRQADDLRLLLRRGLGPGGGLERLVQ 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1438 NGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKHTEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEI 1517
Cdd:COG3433 105 QVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAAALAALDKVPPDVVAASAVVALDAL 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1518 PLTPAGKLDRAALPEPHAPEPAEYVAPANPAEDN-----LARIVAGLLGE--ERVSVTESFFALGGDSIMSIQLSSAAKA 1590
Cdd:COG3433 185 LLLALKVVARAAPALAAAEALLAAASPAPALETAlteeeLRADVAELLGVdpEEIDPDDNLFDLGLDSIRLMQLVERWRK 264
|
250
....*....|....*..
gi 1827387616 1591 AGIHLSPREIFELKTIR 1607
Cdd:COG3433 265 AGLDVSFADLAEHPTLA 281
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
1064-1532 |
5.97e-18 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 90.58 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLARGVSPEDVVAVgMERSIGSVLATW-GVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITD-- 1140
Cdd:PRK06018 42 YAQIHDRALKVSQALDRDGIKLGDRVAT-IAWNTWRHLEAWyGIMGIGAICHTVNPRLFPEQIAWIINHAEDRVVITDlt 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1141 -----ASTRARLgESSCEWVDLADLE-------AEAESGDDITDtERNGSVRLTNL-----AYLIYTSGSTGRPKAVGVS 1203
Cdd:PRK06018 121 fvpilEKIADKL-PSVERYVVLTDAAhmpqttlKNAVAYEEWIA-EADGDFAWKTFdentaAGMCYTSGTTGDPKGVLYS 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1204 HTGivdfvNSLAKITTGTPE----DEPDTrILHVAsPSFDASMFEMAWAIPAGHTLVIAPQADFAGDALATVLERDEVTD 1279
Cdd:PRK06018 199 HRS-----NVLHALMANNGDalgtSAADT-MLPVV-PLFHANSWGIAFSAPSMGTKLVMPGAKLDGASVYELLDTEKVTF 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1280 MIITPSV----LATVDPERAQ--YVRNLATGGEACPPELVERWSERGRRIFNCYGPTEATVWATRSRMTAG--------- 1344
Cdd:PRK06018 272 TAGVPTVwlmlLQYMEKEGLKlpHLKMVVCGGSAMPRSMIKAFEDMGVEVRHAWGMTEMSPLGTLAALKPPfsklpgdar 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1345 --KPVTIGKPVDGFTVRVLDGRLHEVPQG--VVGELYLSTAGLARGYLGRPGQTavsFVADPFgepgarmYATGDLVRVA 1420
Cdd:PRK06018 352 ldVLQKQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYRVDGEI---LDDDGF-------FDTGDVATID 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1421 KGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKHTEVVaylVAKPGATIDSAAVLDEAAQ 1500
Cdd:PRK06018 422 AYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGVYHPKWDERPLLIV---QLKPGETATREEILKYMDG 498
|
490 500 510
....*....|....*....|....*....|..
gi 1827387616 1501 HLAAHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:PRK06018 499 KIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
4-472 |
6.06e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 90.49 E-value: 6.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDeqlPVDRA---RYMVRTAGVRlVVVTS 80
Cdd:PRK06178 62 AELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVS---PLFREhelSYELNDAGAE-VLLAL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAE------ARSRFDDIVDVHVLD------------------ISSPGDADLDEEEFAGPTRPANAAFTL-------FT 129
Cdd:PRK06178 138 DQLAPvveqvrAETSLRHVIVTSLADvlpaeptlplpdslraprLAAAGAIDLLPALRACTAPVPLPPPALdalaalnYT 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 130 SGSTGRPKAVVITHRGI-----ANRLAADIEQYDltarDVFLYKAPItFDVSVRE--IFLPIAIGATLVIAEpgrHGDPV 202
Cdd:PRK06178 218 GGTTGMPKGCEHTQRDMvytaaAAYAVAVVGGED----SVFLSFLPE-FWIAGENfgLLFPLFSGATLVLLA---RWDAV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 203 HLADLIRRHGVTVIhfvpAMLA-AFNEVL---GAGVGELTSLRliQTGGEALTPPVARDLMVR---LPGTRL-QNQYGPA 274
Cdd:PRK06178 290 AFMAAVERYRVTRT----VMLVdNAVELMdhpRFAEYDLSSLR--QVRVVSFVKKLNPDYRQRwraLTGSVLaEAAWGMT 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 275 EASIVVTIHRVTQDD------RVIPIGTPTRRVSARVLDAALRE-VPIGVPGELYLGGVQLARGYAGRPDLTAERFVADp 347
Cdd:PRK06178 364 ETHTCDTFTAGFQDDdfdllsQPVFVGLPVPGTEFKICDFETGElLPLGAEGEIVVRTPSLLKGYWNKPEATAEALRDG- 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 348 fgepgarLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLhaAAAVV---DGPGGQQLVGY--L 422
Cdd:PRK06178 443 -------WLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVL--GSAVVgrpDPDKGQVPVAFvqL 513
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 423 AP-ADVDVDTVAATTAELLPEYMRPSAWVrLDAMPLSRSGKVDR-RLLPEPE 472
Cdd:PRK06178 514 KPgADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKqDLQALAE 564
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
4-470 |
6.15e-18 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 90.59 E-value: 6.15e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDGE 83
Cdd:PRK06155 50 AEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTALRGPQLEHILRNSGARLLVVEAALL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 AEARS---RFDDIVDVHVLDISSPGDAD----------LDEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRG--IAN 148
Cdd:PRK06155 130 AALEAadpGDLPLPAVWLLDAPASVSVPagwstaplppLDAPAPAAAVQPGDTAAILYTSGTTGPSKGVCCPHAQfyWWG 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 149 RLAAdiEQYDLTARDVFLYKAPItFDVSVREIFLPIAI-GATLVIaepGRHGDPVHLADLIRRHGVTVIHFVPAMLaafn 227
Cdd:PRK06155 210 RNSA--EDLEIGADDVLYTTLPL-FHTNALNAFFQALLaGATYVL---EPRFSASGFWPAVRRHGATVTYLLGAMV---- 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 228 evlgagvgeltSLRLIQTGGE---------ALTPPVARDLMVRLP---GTRLQNQYGPAEASIVvtIHRVTQDDRVIPIG 295
Cdd:PRK06155 280 -----------SILLSQPAREsdrahrvrvALGPGVPAALHAAFRerfGVDLLDGYGSTETNFV--IAVTHGSQRPGSMG 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 296 TPTRRVSARVLDAALREVPIGVPGELYLGGVQ---LARGYAGRPDLTAERFVADPFgepgarlyRTGDRARWNRDGEIEY 372
Cdd:PRK06155 347 RLAPGFEARVVDEHDQELPDGEPGELLLRADEpfaFATGYFGMPEKTVEAWRNLWF--------HTGDRVVRDADGWFRF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 373 LGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAPAD---VDVDTVAATTAELLPEYMRPSA 448
Cdd:PRK06155 419 VDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVfPVPSELGEDEVMAAVVLRDgtaLEPVALVRHCEPRLAYFAVPRY 498
|
490 500
....*....|....*....|..
gi 1827387616 449 WVRLDAMPLSRSGKVDRRLLPE 470
Cdd:PRK06155 499 VEFVAALPKTENGKVQKFVLRE 520
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1304-1530 |
7.29e-18 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 88.18 E-value: 7.29e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1304 GGEACPPELVERWSERGRRIFNCYGPTEatvwatrsrmTAGKPVTIGKPVDGFTVRVLDGRLHevpqgvvgelyLSTAGL 1383
Cdd:PRK07824 159 GGGPAPAPVLDAAAAAGINVVRTYGMSE----------TSGGCVYDGVPLDGVRVRVEDGRIA-----------LGGPTL 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1384 ARGYLGRPgqtavsfVADPFGEPGarMYATGDLVRVAKGgNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVV 1463
Cdd:PRK07824 218 AKGYRNPV-------DPDPFAEPG--WFRTDDLGALDDG-VLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVF 287
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 1464 GVESTRGGRKhteVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK07824 288 GLPDDRLGQR---VVAAVVGDGGPAPTLEALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
236-474 |
8.02e-18 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 90.21 E-value: 8.02e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 236 ELTSLRLIQTGGEALTPPVArDLMVRLPGTRLQNQYGPAEASIVVTIHRVtQDDRVIPIGTPTRRVSARVLDAALREVPI 315
Cdd:PRK05677 324 DFSALKLTLSGGMALQLATA-ERWKEVTGCAICEGYGMTETSPVVSVNPS-QAIQVGTIGIPVPSTLCKVIDDDGNELPL 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 316 GVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAA 395
Cdd:PRK05677 402 GEVGELCVKGPQVMKGYWQRPEATDEILDSDGW-------LKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDV 474
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 396 LAAAPGVLHAAA-AVVDGPGGQQLVGYLAP---ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEP 471
Cdd:PRK05677 475 LAALPGVLQCAAiGVPDEKSGEAIKVFVVVkpgETLTKEQVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRRELRDE 554
|
...
gi 1827387616 472 EIA 474
Cdd:PRK05677 555 ELK 557
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1-474 |
8.96e-18 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 89.76 E-value: 8.96e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:PRK12406 12 RSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSGARVLIAHA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 DGEAEARSRFDDivDVHVLDISSP------------------GDADLDE-----EEFAGPTRPANAAFtLFTSGSTGRPK 137
Cdd:PRK12406 92 DLLHGLASALPA--GVTVLSVPTPpeiaaayrispalltppaGAIDWEGwlaqqEPYDGPPVPQPQSM-IYTSGTTGHPK 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 138 AV-----VITHRGIANRLAADIEQYDLTARDVF---LY-KAPITFDVSVreiflpIAIGATLVIaEPgrHGDPVHLADLI 208
Cdd:PRK12406 169 GVrraapTPEQAAAAEQMRALIYGLKPGIRALLtgpLYhSAPNAYGLRA------GRLGGVLVL-QP--RFDPEELLQLI 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 209 RRHGVTVIHFVPAMLAAFNEvLGAGVGE---LTSLRLIqTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTihrV 285
Cdd:PRK12406 240 ERHRITHMHMVPTMFIRLLK-LPEEVRAkydVSSLRHV-IHAAAPCPADVKRAMIEWWGPVIYEYYGSTESGAVTF---A 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 286 TQDDRVIPIGT---PTRRVSARVLDAALREVPIGVPGELYlggvqlARgYAGRPDLTAErfvadpfGEPGARlyRTGDRA 362
Cdd:PRK12406 315 TSEDALSHPGTvgkAAPGAELRFVDEDGRPLPQGEIGEIY------SR-IAGNPDFTYH-------NKPEKR--AEIDRG 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 363 RWNRDGEIEYLGRTDF---------QVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAP---ADVDV 429
Cdd:PRK12406 379 GFITSGDVGYLDADGYlflcdrkrdMVISGGVNIYPAEIEAVLHAVPGVHDCAVfGIPDAEFGEALMAVVEPqpgATLDE 458
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 1827387616 430 DTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEPEIA 474
Cdd:PRK12406 459 ADIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDPYWA 503
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
2716-3056 |
9.19e-18 |
|
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, as well as long-chain fatty acid-CoA ligase VraA, all of which are as yet to be characterized. These proteins belong to the adenylate-forming enzymes which catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain
Pssm-ID: 341288 [Multi-domain] Cd Length: 320 Bit Score: 87.08 E-value: 9.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2716 NLAYVIYTSGSTGRPKGVAVTH-SGLANFARQESD-RLNAGDNPVVLGFASPSFDasvLEYLLATVNEGTLAYRPSEAVG 2793
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSErSWIESFVCNEDLfNISGEDAILAPGPLSHSLF---LYGAISALYLGGTFIGQRKFNP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2794 GEVLeRFIAEHGATHTFLTPSVLSTMDPTAVP--SLRVIAAGGEAVPQPI---VDRWAPATELHNLYGPTETTIgITISS 2868
Cdd:cd17633 78 KSWI-RKINQYNATVIYLVPTMLQALARTLEPesKIKSIFSSGQKLFESTkkkLKNIFPKANLIEFYGTSELSF-ITYNF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2869 AMRPGDPVRLGGPIGGVDLmvldeRLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFtanpygtagqrmYRTGDVVRW 2948
Cdd:cd17633 156 NQESRPPNSVGRPFPNVEI-----EIRNADGGEIGKIFVKSEMVFSGYVRGGFSNPDGW------------MSVGDIGYV 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2949 TPDtdtGGLTLEytGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPVDGAVEvSELKAFAG 3028
Cdd:cd17633 219 DEE---GYLYLV--GRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVALYSGDKLTY-KQLKRFLK 292
|
330 340
....*....|....*....|....*...
gi 1827387616 3029 GRLPAYMVPSSFTVIDELPLTPVGKLDK 3056
Cdd:cd17633 293 QKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
4-468 |
9.36e-18 |
|
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This family includes fatty acyl-CoA synthetases that can activate medium to long-chain fatty acids. These enzymes catalyze the ATP-dependent acylation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters. The fatty acyl-CoA synthetase from Thermus thermophiles in this family has been shown to catalyze the long-chain fatty acid, myristoyl acid. Also included in this family are acyl activating enzymes from Arabidopsis, which contains a large number of proteins from this family with up to 63 different genes, many of which are uncharacterized.
Pssm-ID: 341283 [Multi-domain] Cd Length: 486 Bit Score: 89.67 E-value: 9.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDGE 83
Cdd:cd12118 33 RQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFILRHSEAKVLFVDREFE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 AEArsrfddivdvhVLDISSPGdadldeeefAGPTRPANA--AFTL-FTSGSTGRPKAVVITHRGIA-NRLAADIEqYDL 159
Cdd:cd12118 113 YED-----------LLAEGDPD---------FEWIPPADEwdPIALnYTSGTTGRPKGVVYHHRGAYlNALANILE-WEM 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 160 TARDVFLYKAPI------TFdvsvreIFLPIAIGATLVIAepgRHGDPVHLADLIRRHGVTviHF-----VPAMLAAFNE 228
Cdd:cd12118 172 KQHPVYLWTLPMfhcngwCF------PWTVAAVGGTNVCL---RKVDAKAIYDLIEKHKVT--HFcgaptVLNMLANAPP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 229 vlgAGVGELTSLRLIQTGGeALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTI-------HRVTQDDRVipigtptrRV 301
Cdd:cd12118 241 ---SDARPLPHRVHVMTAG-APPPAAVLAKMEEL-GFDVTHVYGLTETYGPATVcawkpewDELPTEERA--------RL 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 302 SAR------------VLDAalrEVPIGVP------GELYLGGVQLARGYAGRPDLTAERFvadpfgEPGarLYRTGDRAR 363
Cdd:cd12118 308 KARqgvryvgleevdVLDP---ETMKPVPrdgktiGEIVFRGNIVMKGYLKNPEATAEAF------RGG--WFHSGDLAV 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 364 WNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLhaAAAVVDGPG---GQQLVGYLA---PADVDVDTVAATTA 437
Cdd:cd12118 377 IHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVL--EAAVVARPDekwGEVPCAFVElkeGAKVTEEEIIAFCR 454
|
490 500 510
....*....|....*....|....*....|.
gi 1827387616 438 ELLPEYMRPSAWVRLDaMPLSRSGKVDRRLL 468
Cdd:cd12118 455 EHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1050-1530 |
1.07e-17 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 89.90 E-value: 1.07e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALI--CDGTEMDYDEFETRTNAIARALLAR-GVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIA 1126
Cdd:PLN02574 53 NGDTALIdsSTGFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNPSSSLGEIK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1127 YMLEDSGATVGITDASTRARLGE------SSCEWVDLADLEAEAESGDDI----TDTERNGSVRLTNLAYLIYTSGSTGR 1196
Cdd:PLN02574 133 KRVVDCSVGLAFTSPENVEKLSPlgvpviGVPENYDFDSKRIEFPKFYELikedFDFVPKPVIKQDDVAAIMYSSGTTGA 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1197 PKAVGVSHTGIVDFVNSLAKITTGTPEDEPDTRILHVASPSFDA---SMFEMAwAIPAGHTLVIAPQADfAGDALaTVLE 1273
Cdd:PLN02574 213 SKGVVLTHRNLIAMVELFVRFEASQYEYPGSDNVYLAALPMFHIyglSLFVVG-LLSLGSTIVVMRRFD-ASDMV-KVID 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1274 RDEVTDMIITPSVLA----TVDPERAQYVRNL---ATGGEACPPELVERWSERGRRI--FNCYGPTEATVWATRSRMTA- 1343
Cdd:PLN02574 290 RFKVTHFPVVPPILMaltkKAKGVCGEVLKSLkqvSCGAAPLSGKFIQDFVQTLPHVdfIQGYGMTESTAVGTRGFNTEk 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1344 -GKPVTIGKPVDGFTVRVLD---GRLheVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRV 1419
Cdd:PLN02574 370 lSKYSSVGLLAPNMQAKVVDwstGCL--LPPGNCGELWIQGPGVMKGYLNNPKATQSTIDKDGW-------LRTGDIAYF 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1420 AKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEV-VAYLVAKPGATIDSAAVLDEA 1498
Cdd:PLN02574 441 DEDGYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECG----EIpVAFVVRRQGSTLSQEAVINYV 516
|
490 500 510
....*....|....*....|....*....|..
gi 1827387616 1499 AQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PLN02574 517 AKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
2590-3000 |
1.22e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 88.67 E-value: 1.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2590 ARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDsgavlgls 2669
Cdd:cd05910 1 SRLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQE-------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2670 vlasgdlpgqefewmrldddsvaaeiaAVPAGPItdaerlGEVTAANLAYVIYTSGSTGRPKGVAVTHSglaNFARQ--- 2746
Cdd:cd05910 73 ---------------------------AEPDAFI------GIPKADEPAAILFTSGSTGTPKGVVYRHG---TFAAQida 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2747 --------ESDRLNAGDNPV-----VLGFAS--PSFDASvleyllatvnegtlayRPSEAVGGEVLErFIAEHGATHTFL 2811
Cdd:cd05910 117 lrqlygirPGEVDLATFPLFalfgpALGLTSviPDMDPT----------------RPARADPQKLVG-AIRQYGVSIVFG 179
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2812 TPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVDRW----APATELHNLYGPTE----TTIG-----ITISSAMRP 2872
Cdd:cd05910 180 SPALLERVarycaqHGITLPSLRRVLSAGAPVPIALAARLrkmlSDEAEILTPYGATEalpvSSIGsrellATTTAATSG 259
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2873 GDPVRLGGPIGGVDLMVL----------DERLRpVPVGMPGELYVAGGALSRGYLDRSGLTAerfTANPYGTAGQRMYRT 2942
Cdd:cd05910 260 GAGTCVGRPIPGVRVRIIeiddepiaewDDTLE-LPRGEIGEITVTGPTVTPTYVNRPVATA---LAKIDDNSEGFWHRM 335
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 2943 GDVVRWtpdtDTGGlTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG 3000
Cdd:cd05910 336 GDLGYL----DDEG-RLWFCGRKAHRVITTGGTLYTEPVERVFNTHPGVRRSALVGVG 388
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
127-464 |
1.58e-17 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 86.59 E-value: 1.58e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 127 LFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPItFDVSVREIFLPI-AIGATLVIAepgRHGDPVHLA 205
Cdd:cd17636 6 IYTAAFSGRPNGALLSHQALLAQALVLAVLQAIDEGTVFLNSGPL-FHIGTLMFTLATfHAGGTNVFV---RRVDAEEVL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 206 DLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGE------ALTPPVARDLMvrlpgtrlqnQYGPAEASIV 279
Cdd:cd17636 82 ELIEAERCTHAFLLPPTIDQIVELNADGLYDLSSLRSSPAAPEwndmatVDTSPWGRKPG----------GYGQTEVMGL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 280 VTIHRVTQDDRVIpIGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVadpfgepgARLYRTG 359
Cdd:cd17636 152 ATFAALGGGAIGG-AGRPSPLVQVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTR--------GGWHHTN 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 360 DRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGPGGQQLVGYLApadVDVDTVAATTAEL 439
Cdd:cd17636 223 DLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIV---VLKPGASVTEAEL 299
|
330 340 350
....*....|....*....|....*....|..
gi 1827387616 440 -------LPEYMRPSAWVRLDAMPLSRSGKVD 464
Cdd:cd17636 300 iehcrarIASYKKPKSVEFADALPRTAGGADD 331
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
2561-3027 |
1.76e-17 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 89.19 E-value: 1.76e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2561 ATDPVTLAELFRAAARRAPDHVAVVDGAG---------ARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLT 2631
Cdd:PRK09274 2 MASMANIARHLPRAAQERPDQLAVAVPGGrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFA 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2632 AIWAVAKTGGAYVPIDPDYPAERVASMIEDSG--AVLG--LSVLASgdlpgqefEWMRLDDDSV-------------AAE 2694
Cdd:PRK09274 82 LTFALFKAGAVPVLVDPGMGIKNLKQCLAEAQpdAFIGipKAHLAR--------RLFGWGKPSVrrlvtvggrllwgGTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2695 IAAVPAGPITDAERLGEVTAANLAYVIYTSGSTGRPKGVAVTHSglaNFARQ-----ESDRLNAGD------------NP 2757
Cdd:PRK09274 154 LATLLRDGAAAPFPMADLAPDDMAAILFTSGSTGTPKGVVYTHG---MFEAQiealrEDYGIEPGEidlptfplfalfGP 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2758 VvLGFAS--PSFDASvleyllatvnegtlayRPSeAVGGEVLERFIAEHGATHTFLTPSVLSTM------DPTAVPSLRV 2829
Cdd:PRK09274 231 A-LGMTSviPDMDPT----------------RPA-TVDPAKLFAAIERYGVTNLFGSPALLERLgrygeaNGIKLPSLRR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2830 IAAGGEAVPQPIVDRW----APATELHNLYGPTE----TTIG-----ITISSAMRPGDPVRLGGPIGGVDLMVLD----- 2891
Cdd:PRK09274 293 VISAGAPVPIAVIERFramlPPDAEILTPYGATEalpiSSIEsreilFATRAATDNGAGICVGRPVDGVEVRIIAisdap 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2892 ----ERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRMyrtGDVVRWtpdtDTGGLtLEYTGRSDD 2967
Cdd:PRK09274 373 ipewDDALRLATGEIGEIVVAGPMVTRSYYNRPEATRLAKIPDGQGDVWHRM---GDLGYL----DAQGR-LWFCGRKAH 444
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 2968 QVKLRGLRIELGEIEAVLAEHDAV-ESAVVL-GVGGSVATAL----AAYIVPVDGAVEvSELKAFA 3027
Cdd:PRK09274 445 RVETAGGTLYTIPCERIFNTHPGVkRSALVGvGVPGAQRPVLcvelEPGVACSKSALY-QELRALA 509
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
2564-3061 |
1.79e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 89.00 E-value: 1.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2564 PVTLAELFRAAARRAPDHVAV---VDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTG 2640
Cdd:PRK07008 9 PLLISSLIAHAARHAGDTEIVsrrVEGDIHRYTYRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2641 GAYVPIDPDYPAERVASMI---EDSGAVLGLSVLA-----SGDLPGQEfEWMRLDDDsvaaeiAAVPAGPI--------T 2704
Cdd:PRK07008 89 AVCHTINPRLFPEQIAYIVnhaEDRYVLFDLTFLPlvdalAPQCPNVK-GWVAMTDA------AHLPAGSTpllcyetlV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2705 DAE-------RLGEVTAANLAYviyTSGSTGRPKGVAVTH--SGLANFARQESD--RLNAGDN--PVVlgfasPSF--DA 2769
Cdd:PRK07008 162 GAQdgdydwpRFDENQASSLCY---TSGTTGNPKGALYSHrsTVLHAYGAALPDamGLSARDAvlPVV-----PMFhvNA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2770 SVLEYLLATVneGTLAYRPSEAVGGEVLERFIAEHGATHTFLTPSV----LSTMDPTAV--PSLRVIAAGGEAVPQPIVD 2843
Cdd:PRK07008 234 WGLPYSAPLT--GAKLVLPGPDLDGKSLYELIEAERVTFSAGVPTVwlglLNHMREAGLrfSTLRRTVIGGSACPPAMIR 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2844 RWAPA--TELHNLYGPTE-----TTIGITISSAMRPGDPVR-----LGGPIGGVDLMVLDERLRPVPV-GMP-GELYVAG 2909
Cdd:PRK07008 312 TFEDEygVEVIHAWGMTEmsplgTLCKLKWKHSQLPLDEQRkllekQGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRG 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2910 GALSRGYL--DRSGLTAERFTanpygtagqrmyrTGDVVrwTPDTDTgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAE 2987
Cdd:PRK07008 392 PWVIDRYFrgDASPLVDGWFP-------------TGDVA--TIDADG---FMQITDRSKDVIKSGGEWISSIDIENVAVA 453
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 2988 HDAVESAVVLGVGGSVATALAAYIVPVDGAVEVS--ELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPE 3061
Cdd:PRK07008 454 HPAVAEAACIACAHPKWDERPLLVVVKRPGAEVTreELLAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1059-1527 |
2.20e-17 |
|
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: 88.27 E-value: 2.20e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1059 GTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGI 1138
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1139 TdastrarlgesscewvdladleaeaesgddiTDTErngsvrltNLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKIT 1218
Cdd:cd05914 85 V-------------------------------SDED--------DVALINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVV 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1219 TGTPEDepdtRILhvaspsfdaSMFEMAWAIPAGHTLVIAPQAD----FAGD---ALATVLERDEVTDMIITPSVLATVD 1291
Cdd:cd05914 126 LLGKGD----KIL---------SILPLHHIYPLTFTLLLPLLNGahvvFLDKipsAKIIALAFAQVTPTLGVPVPLVIEK 192
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1292 ---------------------PERAQYVRNLA----------------TGGEACPPELVERWSERGRRIFNCYGPTEATV 1334
Cdd:cd05914 193 ifkmdiipkltlkkfkfklakKINNRKIRKLAfkkvheafggnikefvIGGAKINPDVEEFLRTIGFPYTIGYGMTETAP 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1335 WATRSRMTAGKPVTIGKPVDGFTVRVLDgrlhEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATG 1414
Cdd:cd05914 273 IISYSPPNRIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW-------FHTG 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1415 DLVRVAKGGNLEFAGRADHQ-VKINGQRVELGEIEAVLDAQPGVAQSVVVgvestrggRKHTEVVAYLVAKPGATIDSA- 1492
Cdd:cd05914 342 DLGKIDAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVV--------VQEKKLVALAYIDPDFLDVKAl 413
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 1827387616 1493 -----------AVLDEAAQHLAAH-MVPSQAIVIDEIPLTPAGKLDR 1527
Cdd:cd05914 414 kqrniidaikwEVRDKVNQKVPNYkKISKVKIVKEEFEKTPKGKIKR 460
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
2564-3008 |
2.44e-17 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 88.95 E-value: 2.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2564 PVTLAELFRAAARRAPDHVAVV-----DGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAK 2638
Cdd:PRK12582 48 PRSIPHLLAKWAAEAPDRPWLAqrepgHGQWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQ 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2639 TGGAYVPIDPDYpaervaSMIEDSGAVL---------GLSVLASGDLPGQEFEWMRLDDDSV-----------AAEIAAV 2698
Cdd:PRK12582 128 AGVPAAPVSPAY------SLMSHDHAKLkhlfdlvkpRVVFAQSGAPFARALAALDLLDVTVvhvtgpgegiaSIAFADL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2699 PAGPITD--AERLGEVTAANLAYVIYTSGSTGRPKGVAVTHSGL-ANFARQESDRLNAGDNPVvlgfaspsfdASVLEYL 2775
Cdd:PRK12582 202 AATPPTAavAAAIAAITPDTVAKYLFTSGSTGMPKAVINTQRMMcANIAMQEQLRPREPDPPP----------PVSLDWM 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2776 -------------LATVNEGTLAYRPSEAVGGEVLE--RFIAEHGATHTFLTPSVLSTM------DPTAVPS----LRVI 2830
Cdd:PRK12582 272 pwnhtmggnanfnGLLWGGGTLYIDDGKPLPGMFEEtiRNLREISPTVYGNVPAGYAMLaeamekDDALRRSffknLRLM 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2831 AAGGEAVPQPIVDRW---APATELHNL-----YGPTETTiGITISSAMRPGDPVRLGGPIGGVDLMVlderlrpVPVGMP 2902
Cdd:PRK12582 352 AYGGATLSDDLYERMqalAVRTTGHRIpfytgYGATETA-PTTTGTHWDTERVGLIGLPLPGVELKL-------APVGDK 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2903 GELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVRWTpDTDTGGLTLEYTGRSDDQVKL-RGLRIELGE- 2980
Cdd:PRK12582 424 YEVRVKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAARFV-DPDDPEKGLIFDGRVAEDFKLsTGTWVSVGTl 495
|
490 500
....*....|....*....|....*....
gi 1827387616 2981 -IEAVLAEHDAVESAVVLGVGGSVATALA 3008
Cdd:PRK12582 496 rPDAVAACSPVIHDAVVAGQDRAFIGLLA 524
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
127-465 |
2.47e-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: 86.17 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 127 LFTSGSTGRPKAVVITHRGIanrLAADIE---QYDLTARDVFLYKAPItFDVSvrEIFLPIAI---GATLVIAEpgrHGD 200
Cdd:cd17637 6 IHTAAVAGRPRGAVLSHGNL---IAANLQlihAMGLTEADVYLNMLPL-FHIA--GLNLALATfhaGGANVVME---KFD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 201 PVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIqTGGEalTPPVARDLMVRLPGTrLQNQYGPAEASIVV 280
Cdd:cd17637 77 PAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHV-LGLD--APETIQRFEETTGAT-FWSLYGQTETSGLV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 281 TIHRVtqDDRVIPIGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADpfgepgarLYRTGD 360
Cdd:cd17637 153 TLSPY--RERPGSAGRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTAYTFRNG--------WHHTGD 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 361 RARWNRDGEIEYLGRTDFQ--VKLRGQRLELGEVEAALAAAPGVlhaAAAVVDG-PG-----GQQLVGYLAP-ADVDVDT 431
Cdd:cd17637 223 LGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAI---AEVCVIGvPDpkwgeGIKAVCVLKPgATLTADE 299
|
330 340 350
....*....|....*....|....*....|....
gi 1827387616 432 VAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDR 465
Cdd:cd17637 300 LIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
2581-3074 |
3.91e-17 |
|
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: 88.14 E-value: 3.91e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2581 HVAVVDGAGARLTYRELDEASDRLARWLIGRGVG------------PERAVA-LAIGRsaqlLTAIWAVAKTGGAyvpid 2647
Cdd:cd05967 72 YDSPVTGTERTYTYAELLDEVSRLAGVLRKLGVVkgdrviiympmiPEAAIAmLACAR----IGAIHSVVFGGFA----- 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2648 pdypAERVASMIEDSGAVLGLSvlASGDL-PGQEFEWMRLDDDSVA--------------AEIAAVPAGPITD------- 2705
Cdd:cd05967 143 ----AKELASRIDDAKPKLIVT--ASCGIePGKVVPYKPLLDKALElsghkphhvlvlnrPQVPADLTKPGRDldwsell 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2706 --AERLGEVT--AANLAYVIYTSGSTGRPKGVAVTHSGLA---NFARQESDRLNAGDnpvVLGFASP-------SFdaSV 2771
Cdd:cd05967 217 akAEPVDCVPvaATDPLYILYTSGTTGKPKGVVRDNGGHAvalNWSMRNIYGIKPGD---VWWAASDvgwvvghSY--IV 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2772 LEYLLATVNegTLAY--RPSEAVGGEVLERFIAEHGATHTFLTPS---VLSTMDPTA-------VPSLRVIAAGGE---- 2835
Cdd:cd05967 292 YGPLLHGAT--TVLYegKPVGTPDPGAFWRVIEKYQVNALFTAPTairAIRKEDPDGkyikkydLSSLRTLFLAGErldp 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2836 --------AVPQPIVDRWapatelhnlyGPTETTIGITISS------AMRPGDPvrlGGPIGGVDLMVLDERLRPVPVGM 2901
Cdd:cd05967 370 ptlewaenTLGVPVIDHW----------WQTETGWPITANPvgleplPIKAGSP---GKPVPGYQVQVLDEDGEPVGPNE 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2902 PGELYVAG----GALSRGYLDRsgltaERFTaNPYGTAGQRMYRTGDvvrWTPDTDTGGLTLeyTGRSDDQVKLRGLRIE 2977
Cdd:cd05967 437 LGNIVIKLplppGCLLTLWKND-----ERFK-KLYLSKFPGYYDTGD---AGYKDEDGYLFI--MGRTDDVINVAGHRLS 505
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2978 LGEIEAVLAEHDAVESAVVLGV----GGSVATALAayiVPVDGAVEV-----SELKAFAGGRLPAYMVPSSFTVIDELPL 3048
Cdd:cd05967 506 TGEMEESVLSHPAVAECAVVGVrdelKGQVPLGLV---VLKEGVKITaeeleKELVALVREQIGPVAAFRLVIFVKRLPK 582
|
570 580
....*....|....*....|....*.
gi 1827387616 3049 TPVGKLDKRALPEpVLEAGEYVAPAT 3074
Cdd:cd05967 583 TRSGKILRRTLRK-IADGEDYTIPST 607
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
4-471 |
3.99e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 87.65 E-value: 3.99e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDGE 83
Cdd:PRK08276 15 GELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSAALA 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 AEARSRFDDI----VDVHVLDISSPGDADLDEEEFAGPTRP----ANAAFTLFTSGSTGRPKAVV--ITHRGI----ANR 149
Cdd:PRK08276 95 DTAAELAAELpagvPLLLVVAGPVPGFRSYEEALAAQPDTPiadeTAGADMLYSSGTTGRPKGIKrpLPGLDPdeapGMM 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 150 LAADIEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEpgrHGDPVHLADLIRRHGVTVIHFVPAM----LAA 225
Cdd:PRK08276 175 LALLGFGMYGGPDSVYLSPAPLYHTAPLRFGMSALALGGTVVVME---KFDAEEALALIERYRVTHSQLVPTMfvrmLKL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 226 FNEVLGAgvGELTSLRLIQTGGEALTPPVARDlMVRLPGTRLQNQYGPAEASIVVTIhrvTQDDRVIPIGTPTRRVSA-- 303
Cdd:PRK08276 252 PEEVRAR--YDVSSLRVAIHAAAPCPVEVKRA-MIDWWGPIIHEYYASSEGGGVTVI---TSEDWLAHPGSVGKAVLGev 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 304 RVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVadpfgepGARLYRTGDRARWNRDGeieYLGRTD---FQV 380
Cdd:PRK08276 326 RILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKTAAARN-------PHGWVTVGDVGYLDEDG---YLYLTDrksDMI 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 381 KLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAPADvDVDTVAATTAEL-------LPEYMRPSAWVRL 452
Cdd:PRK08276 396 ISGGVNIYPQEIENLLVTHPKVADVAVfGVPDEEMGERVKAVVQPAD-GADAGDALAAELiawlrgrLAHYKCPRSIDFE 474
|
490
....*....|....*....
gi 1827387616 453 DAMPLSRSGKVDRRLLPEP 471
Cdd:PRK08276 475 DELPRTPTGKLYKRRLRDR 493
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
2-413 |
4.27e-17 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 87.93 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTagVRLVVVTSD 81
Cdd:PLN02860 34 TGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYRWSFEEAKSAMLL--VRPVMLVTD 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 GEAEA---RSRFDDI--VDVHVL-----DISSPGDAD-----------LDEEEFAGPTRPANAAFTLFTSGSTGRPKAVV 140
Cdd:PLN02860 112 ETCSSwyeELQNDRLpsLMWQVFlespsSSVFIFLNSflttemlkqraLGTTELDYAWAPDDAVLICFTSGTTGRPKGVT 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 141 ITHRGIANRLAADIEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAePGRHGDPVhlADLIRRHGVTVIHFVP 220
Cdd:PLN02860 192 ISHSALIVQSLAKIAIVGYGEDDVYLHTAPLCHIGGLSSALAMLMVGACHVLL-PKFDAKAA--LQAIKQHNVTSMITVP 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 221 AMLAAFNEV--LGAGVGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEA--SIV-VTIHRVTQDDRVIPIG 295
Cdd:PLN02860 269 AMMADLISLtrKSMTWKVFPSVRKILNGGGSLSSRLLPDAKKLFPNAKLFSAYGMTEAcsSLTfMTLHDPTLESPKQTLQ 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 296 TPTRRVSARV---------LDAALREVPIGVPGELYLGGVqLARG------YAGRPDLTAERFVADPFGEpgarlyrTGD 360
Cdd:PLN02860 349 TVNQTKSSSVhqpqgvcvgKPAPHVELKIGLDESSRVGRI-LTRGphvmlgYWGQNSETASVLSNDGWLD-------TGD 420
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 361 RARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGP 413
Cdd:PLN02860 421 IGWIDKAGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGV--ASVVVVGVP 471
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
2716-3001 |
4.30e-17 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 87.95 E-value: 4.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2716 NLAYVIYTSGSTGRPKGVAVTHSGLanFARQES--DRLNAGDNPVVLGFASP----SFDASVLEYLLATVNEgTLAYRPS 2789
Cdd:PRK06334 184 DVAVILFTSGTEKLPKGVPLTHANL--LANQRAclKFFSPKEDDVMMSFLPPfhayGFNSCTLFPLLSGVPV-VFAYNPL 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2790 EAvggEVLERFIAEHGATHTFLTPSVLSTMDPTA------VPSLRVIAAGGEAVPQPI---VDRWAPATELHNLYGPTET 2860
Cdd:PRK06334 261 YP---KKIVEMIDEAKVTFLGSTPVFFDYILKTAkkqescLPSLRFVVIGGDAFKDSLyqeALKTFPHIQLRQGYGTTEC 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2861 TIGITISSAMRPGDPVRLGGPIGGVDLMVLDERLR-PVPVGMPGELYVAGGALSRGYLdrsgltAERFTANPYGTAGQRM 2939
Cdd:PRK06334 338 SPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYL------GEDFGQGFVELGGETW 411
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 2940 YRTGDVVRWTPDtdtGGLTLEytGRSDDQVKLRGLRIELGEIEAVLAEH------DAVESAVVLGVGG 3001
Cdd:PRK06334 412 YVTGDLGYVDRH---GELFLK--GRLSRFVKIGAEMVSLEALESILMEGfgqnaaDHAGPLVVCGLPG 474
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
2716-3056 |
6.75e-17 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 84.86 E-value: 6.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2716 NLAYVIYTSGSTGRPKGVAVTHSGLANFARQESD--RLNAGDNPVVLG--FASPSFDASVLEYLL--ATVNEGTLaYRPS 2789
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTLRAAAAWADcaDLTEDDRYLIINpfFHTFGYKAGIVACLLtgATVVPVAV-FDVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2790 EAVGGEVLERFIAEHGATHTFLTPSVLSTMDPTAVPSLRVIAAGGEAVPQPIVDRWAPATELHNL---YGPTETTIGiTI 2866
Cdd:cd17638 80 AILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVTGAATVPVELVRRMRSELGFETVltaYGLTEAGVA-TM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2867 SsamRPGDPVRL-----GGPIGGVDLMVLDerlrpvpvgmPGELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYR 2941
Cdd:cd17638 159 C---RPGDDAETvattcGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATAEAIDADGW-------LH 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2942 TGDVVRWtpdTDTGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG----GSVATalaAYIVPVDG- 3016
Cdd:cd17638 219 TGDVGEL---DERGYLRI--TDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPdermGEVGK---AFVVARPGv 290
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1827387616 3017 AVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDK 3056
Cdd:cd17638 291 TLTEEDVIAWCRERLANYKVPRFVRFLDELPRNASGKVMK 330
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
275-554 |
7.06e-17 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 84.03 E-value: 7.06e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 275 EASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFGEPGAR 354
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPAQPGR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 355 LYRTGDRARWNRDGEIEYL--GRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGPGGQQLVGYLAPADVDVDTV 432
Cdd:COG3433 81 QADDLRLLLRRGLGPGGGLerLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 433 AATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEPEIAPTL--YVPPGNADE-----ETVAGLFAELLGV--ERVG 503
Cdd:COG3433 161 ALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALlaAASPAPALEtalteEELRADVAELLGVdpEEID 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 504 VTDSFFDIGGSSLSAARIAARVsKELGVDVSVRDVFESPSVRGLVHAVSGR 554
Cdd:COG3433 241 PDDNLFDLGLDSIRLMQLVERW-RKAGLDVSFADLAEHPTLAAWWALLAAA 290
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
2564-3059 |
7.54e-17 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 86.97 E-value: 7.54e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2564 PVTLAELFRA-------------AARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLL 2630
Cdd:PRK10946 9 PEEFARRYREkgywqdlpltdilTRHAASDAIAVICG-ERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFY 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2631 TAIWAVAKTGgaYVPIDPDY---------------PAERVAS----------MIEDSGAVLG--LSVLASGDLPGQEFew 2683
Cdd:PRK10946 88 ITFFALLKLG--VAPVNALFshqrselnayasqiePALLIADrqhalfsdddFLNTLVAEHSslRVVLLLNDDGEHSL-- 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2684 mrldDDSVAAEIAAVPAGPiTDAerlGEVtaanlAYVIYTSGSTGRPKGVAVTHSGLANFARQESD--RLNAGDN----- 2756
Cdd:PRK10946 164 ----DDAINHPAEDFTATP-SPA---DEV-----AFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEicGFTPQTRylcal 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2757 PVVLGFASPSFDASVLEYLLATVnegTLAYRPSEAVGGEVLERfiaeHGATHTFLTPSVLS-----TMDPT---AVPSLR 2828
Cdd:PRK10946 231 PAAHNYPMSSPGALGVFLAGGTV---VLAPDPSATLCFPLIEK----HQVNVTALVPPAVSlwlqaIAEGGsraQLASLK 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2829 VIAAGGEAVPQPIVDRwAPAT---ELHNLYGPTE----------------TTIGITISsamrPGDPVRlggpiggvdlmV 2889
Cdd:PRK10946 304 LLQVGGARLSETLARR-IPAElgcQLQQVFGMAEglvnytrlddsderifTTQGRPMS----PDDEVW-----------V 367
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2890 LDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVRWTPDtdtGGLTLEytGRSDDQV 2969
Cdd:PRK10946 368 ADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASAFDANGF-------YCSGDLVSIDPD---GYITVV--GREKDQI 435
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2970 KLRGLRIELGEIEAVLAEHDAV-ESAVVlgvggSVATAL-----AAYIVPVDgAVEVSELKAFAGGRLPA-YMVPSSFTV 3042
Cdd:PRK10946 436 NRGGEKIAAEEIENLLLRHPAViHAALV-----SMEDELmgeksCAFLVVKE-PLKAVQLRRFLREQGIAeFKLPDRVEC 509
|
570
....*....|....*..
gi 1827387616 3043 IDELPLTPVGKLDKRAL 3059
Cdd:PRK10946 510 VDSLPLTAVGKVDKKQL 526
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1051-1536 |
1.28e-16 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 86.47 E-value: 1.28e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1051 DHPALICDGTEMDYDEFETRTNAIARALLAR-GVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:PRK08751 40 DRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNVNPLYTPRELKHQL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATV-------GITDASTRARLGESSCEWVDLADLEAEAESG----------DDITDTERNGSVRLT---------- 1182
Cdd:PRK08751 120 IDSGASVlvvidnfGTTVQQVIADTPVKQVITTGLGDMLGFPKAAlvnfvvkyvkKLVPEYRINGAIRFRealalgrkhs 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1183 ---------NLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDEPDTRILHVASPS---FDASMFEMAWAIP 1250
Cdd:PRK08751 200 mptlqiepdDIAFLQYTGGTTGVAKGAMLTHRNLVANMQQAHQWLAGTGKLEEGCEVVITALPLyhiFALTANGLVFMKI 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1251 AGHTLVIAPQADFAGdaLATVLERDEVT----------DMIITPSvLATVDperAQYVRNLATGGEACPPELVERWSE-R 1319
Cdd:PRK08751 280 GGCNHLISNPRDMPG--FVKELKKTRFTaftgvntlfnGLLNTPG-FDQID---FSSLKMTLGGGMAVQRSVAERWKQvT 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1320 GRRIFNCYGPTEATVWATRSRMTAGK-PVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSF 1398
Cdd:PRK08751 354 GLTLVEAYGLTETSPAACINPLTLKEyNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVM 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1399 VADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEVV 1478
Cdd:PRK08751 434 DADGW-------LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEVAAVGVPDEKSG----EIV 502
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 1479 AYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPEPHAP 1536
Cdd:PRK08751 503 KVVIVKKDPALTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRRELRDAAKA 560
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
125-468 |
1.39e-16 |
|
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: 86.46 E-value: 1.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 125 FTLFTSGSTGRPKAVVITHRGianrlaadieqYDLTARDVFLYkapiTFDVSVREIFL-----------------PIAIG 187
Cdd:cd05966 235 FILYTSGSTGKPKGVVHTTGG-----------YLLYAATTFKY----VFDYHPDDIYWctadigwitghsyivygPLANG 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 188 ATLVIAE-------PGRHgdpvhlADLIRRHGVTVIHFVPAMLAAFnevLGAGVG-----ELTSLRLIQTGGEALTPPVA 255
Cdd:cd05966 300 ATTVMFEgtptypdPGRY------WDIVEKHKVTIFYTAPTAIRAL---MKFGDEwvkkhDLSSLRVLGSVGEPINPEAW 370
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 256 RdlmvrlpgtRLQNQYGPAEASIVVTI-------HRVTQddrvIPIGTPTRR---------VSARVLDAALREVPIGVPG 319
Cdd:cd05966 371 M---------WYYEVIGKERCPIVDTWwqtetggIMITP----LPGATPLKPgsatrpffgIEPAILDEEGNEVEGEVEG 437
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 320 EL-----YLGgvqLARGYAGRPdltaERFVADPFGE-PGarLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVE 393
Cdd:cd05966 438 YLvikrpWPG---MARTIYGDH----ERYEDTYFSKfPG--YYFTGDGARRDEDGYYWITGRVDDVINVSGHRLGTAEVE 508
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 394 AALAAAPGVlhAAAAVVDGP---GGQQLVGYL------APADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVD 464
Cdd:cd05966 509 SALVAHPAV--AEAAVVGRPhdiKGEAIYAFVtlkdgeEPSDELRKELRKHVRKEIGPIATPDKIQFVPGLPKTRSGKIM 586
|
....
gi 1827387616 465 RRLL 468
Cdd:cd05966 587 RRIL 590
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
2561-3059 |
1.96e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 85.50 E-value: 1.96e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2561 ATDPVTLAELFRAaarRAPDHVAVVDGAGARLTYRELDEASDRLARWLIGR-GVGPERAVALAIGRSAQLLTAIWAVAKT 2639
Cdd:PRK07867 1 TSSAPTVAELLLP---LAEDDDRGLYFEDSFTSWREHIRGSAARAAALRARlDPTRPPHVGVLLDNTPEFSLLLGAAALS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2640 GGAYVPIDPDYPAERVASMIE--DSGAVL---GLSVLASGDLPGQEFewmrLDDDSVA-AEIAAVPAGPITDAerlGEVT 2713
Cdd:PRK07867 78 GIVPVGLNPTRRGAALARDIAhaDCQLVLtesAHAELLDGLDPGVRV----INVDSPAwADELAAHRDAEPPF---RVAD 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2714 AANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLgFASPSF--DASVLEYLLATVNEGTLAYRPSEA 2791
Cdd:PRK07867 151 PDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCY-VSMPLFhsNAVMAGWAVALAAGASIALRRKFS 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2792 VGGevlerFIA---EHGATHTFLTPSVLSTMDPT------AVPSLRvIAAGGEAVPqPIVDRWAP--ATELHNLYGPTET 2860
Cdd:PRK07867 230 ASG-----FLPdvrRYGATYANYVGKPLSYVLATperpddADNPLR-IVYGNEGAP-GDIARFARrfGCVVVDGFGSTEG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2861 TIGITISSAMRPGDpvrLGGPIGGVDlmVLD-ERLRPVPVGMP------------GELY-VAGGALSRGYLDRSGLTAER 2926
Cdd:PRK07867 303 GVAITRTPDTPPGA---LGPLPPGVA--IVDpDTGTECPPAEDadgrllnadeaiGELVnTAGPGGFEGYYNDPEADAER 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2927 FTANpygtagqrMYRTGDVVRwtpdTDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVA-T 3005
Cdd:PRK07867 378 MRGG--------VYWSGDLAY----RDADGY-AYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDPVVgD 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 3006 ALAAYIVPVDGAV-EVSELKAFAGGR--LPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK07867 445 QVMAALVLAPGAKfDPDAFAEFLAAQpdLGPKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
1670-1870 |
2.07e-16 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 81.62 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1670 VADLQTVVEAVAAAHPMLTAVLTRSGDGWTMNAGAGIVPAVREIDAEGALDPALVDAHRELLGA-----MDPGTGSLLGT 1744
Cdd:COG4908 32 VEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVDLSALPEPEREAELEELVAEeasrpFDLARGPLLRA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1745 AVVNGEGRR-RLVIAIHHLGVDAVSWPILVEDLVTAWAQLTSGRPIELRPEATTTRRIAHLLAG--QVHARAREVDYWLE 1821
Cdd:COG4908 112 ALIRLGEDEhVLLLTIHHIISDGWSLGILLRELAALYAALLEGEPPPLPELPIQYADYAAWQRAwlQSEALEKQLEYWRQ 191
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 1822 QL--PERPTSFGTSADRPLHRRRDESSLTYVVDDVAGSILTTVPQAFGSSV 1870
Cdd:COG4908 192 QLagAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAKAHGATV 242
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
2720-3056 |
2.63e-16 |
|
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: 83.08 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2720 VIYTSGSTGRPKGVAVTHSGLanFARQE---SDRLNAGDNPVVLGFASPSFDASVLeYLLATVNEGTLAYRPSEAVGGEV 2796
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTF--FAVPDilqKEGLNWVVGDVTYLPLPATHIGGLW-WILTCLIHGGLCVTGGENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2797 LERFIAEHGATHTFLTPSVLS-----TMDPTA-VPSLRVIAAGGEavpQPIVDR-----WAPATELHNLYGPTETTIGIT 2865
Cdd:cd17635 83 LFKILTTNAVTTTCLVPTLLSklvseLKSANAtVPSLRLIGYGGS---RAIAADvrfieATGLTNTAQVYGLSETGTALC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2866 ISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTanpygtagQRMYRTGDV 2945
Cdd:cd17635 160 LPTDDDSIEINAVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLI--------DGWVNTGDL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2946 VRwtpdTDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATAL-AAYIV--PVDGAVEVSE 3022
Cdd:cd17635 232 GE----RREDGF-LFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFGELvGLAVVasAELDENAIRA 306
|
330 340 350
....*....|....*....|....*....|....
gi 1827387616 3023 LKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDK 3056
Cdd:cd17635 307 LKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
103-468 |
2.73e-16 |
|
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes the formation of bile acid-CoA conjugates in a two-step reaction: the formation of a bile acid-AMP molecule as an intermediate, followed by the formation of a bile acid-CoA. This ligase requires a bile acid with a free carboxyl group, ATP, Mg2+, and CoA for synthesis of the final bile acid-CoA conjugate. The bile acid-CoA ligation is believed to be the initial step in the bile acid 7alpha-dehydroxylation pathway in the intestinal bacterium Eubacterium sp.
Pssm-ID: 341252 [Multi-domain] Cd Length: 473 Bit Score: 84.74 E-value: 2.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 103 SPGDADLDEEEFAGPTRP----ANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDL---TARDVFLYKAPITFDV 175
Cdd:cd05929 103 LDGLEDYEAAEGGSPETPiedeAAGWKMLYSGGTTGRPKGIKRGLPGGPPDNDTLMAAALGfgpGADSVYLSPAPLYHAA 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 176 SVREIFLPIAIGATLVIAEpgrHGDPVHLADLIRRHGVTVIHFVPAM----LAAFNEVLGAGvgELTSLR-LIQTGgeAL 250
Cdd:cd05929 183 PFRWSMTALFMGGTLVLME---KFDPEEFLRLIERYRVTFAQFVPTMfvrlLKLPEAVRNAY--DLSSLKrVIHAA--AP 255
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 251 TPPVARDLMVRLPGTRLQNQYGPAEASIVVTIhrvTQDDRVIPIGTPTRRVSARV--LDAALREVPIGVPGELYLGGVQl 328
Cdd:cd05929 256 CPPWVKEQWIDWGGPIIWEYYGGTEGQGLTII---NGEEWLTHPGSVGRAVLGKVhiLDEDGNEVPPGEIGEVYFANGP- 331
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 329 ARGYAGRPDLTAERFVADPFgepgarlyRT-GDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA 407
Cdd:cd05929 332 GFEYTNDPEKTAAARNEGGW--------STlGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAV 403
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 408 -AVVDGPGGQQLVGYLAPADvDVDTVAATTAEL-------LPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:cd05929 404 vGVPDEELGQRVHAVVQPAP-GADAGTALAEELiaflrdrLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1-470 |
4.20e-16 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 84.54 E-value: 4.20e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGV--GAEVAVgiQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVV 78
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVkpGDRVAV--QVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVC 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 79 TSDGEAEARSRFDDIVDVHVLDISSPGDADLDEEEFAGPTRPANAAFT-------LFTSGSTGRPKAVVITHRGIANRLA 151
Cdd:PRK07514 107 DPANFAWLSKIAAAAGAPHVETLDADGTGSLLEAAAAAPDDFETVPRGaddlaaiLYTSGTTGRSKGAMLSHGNLLSNAL 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 152 ADIEQYDLTARDVFLYKAPItFDVSvreiFLPIAIGATLV-----IAEPGRhgDPVHLADLIRRhgVTVIHFVPA----M 222
Cdd:PRK07514 187 TLVDYWRFTPDDVLIHALPI-FHTH----GLFVATNVALLagasmIFLPKF--DPDAVLALMPR--ATVMMGVPTfytrL 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 223 LA--AFNEVLGAGVgeltslRLIQTGGEALTPPVARDLMVRlPGTRLQNQYGPAEAsIVVTIHRVTQDDRVIPIGTPTRR 300
Cdd:PRK07514 258 LQepRLTREAAAHM------RLFISGSAPLLAETHREFQER-TGHAILERYGMTET-NMNTSNPYDGERRAGTVGFPLPG 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 301 VSARVLD-AALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQ 379
Cdd:PRK07514 330 VSLRVTDpETGAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEFRADGF-------FITGDLGKIDERGYVHIVGRGKDL 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 380 VKLRGQRLELGEVEAALAAAPGVLHAA--------------AAVVDGPGgqqlvgylapADVDVDTVAATTAELLPEYMR 445
Cdd:PRK07514 403 IISGGYNVYPKEVEGEIDELPGVVESAvigvphpdfgegvtAVVVPKPG----------AALDEAAILAALKGRLARFKQ 472
|
490 500
....*....|....*....|....*
gi 1827387616 446 PSAWVRLDAMPLSRSGKVDRRLLPE 470
Cdd:PRK07514 473 PKRVFFVDELPRNTMGKVQKNLLRE 497
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
28-468 |
4.57e-16 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 84.69 E-value: 4.57e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 28 VGIQIDRSVEQVVAIHAVAMAGGHFVPLDeqlPVDRARYM---VRTAGVRLVVVtsdgEAEARSRFD--DIVDVHVLDIS 102
Cdd:PRK13388 55 VGVLLGNTPEMLFWLAAAALGGYVLVGLN---TTRRGAALaadIRRADCQLLVT----DAEHRPLLDglDLPGVRVLDVD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 103 SPGDAD-LDEEEFAGPTRPANAAFT---LFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPITFDVSVR 178
Cdd:PRK13388 128 TPAYAElVAAAGALTPHREVDAMDPfmlIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDDVCYVSMPLFHSNAVM 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 179 EIFLP-IAIGATlvIAEPGRHGDPVHLADlIRRHGVTVIHFVPAMLA---AFNEVLGAGVGELTslrlIQTGGEAltPPV 254
Cdd:PRK13388 208 AGWAPaVASGAA--VALPAKFSASGFLDD-VRRYGATYFNYVGKPLAyilATPERPDDADNPLR----VAFGNEA--SPR 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 255 ARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQ-------DDRVIPIGTPTRRVSAR-VLDAALREV-PIGVPGELY-LG 324
Cdd:PRK13388 279 DIAEFSRRFGCQVEDGYGSSEGAVIVVREPGTPpgsigrgAPGVAIYNPETLTECAVaRFDAHGALLnADEAIGELVnTA 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 325 GVQLARGYAGRPDLTAERFvadpfgepgaR--LYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGV 402
Cdd:PRK13388 359 GAGFFEGYYNNPEATAERM----------RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAI 428
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 403 LHAAA-AVVDGPGGQQLVGYLAPADVDVDTVAATTAEL-----LPEYMRPSaWVRL-DAMPLSRSGKVDRRLL 468
Cdd:PRK13388 429 NRVAVyAVPDERVGDQVMAALVLRDGATFDPDAFAAFLaaqpdLGTKAWPR-YVRIaADLPSTATNKVLKREL 500
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1184-1532 |
6.07e-16 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 83.69 E-value: 6.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1184 LAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtRILHVASPSFDASM--FEMAWAIpAGHTLVIAPQA 1261
Cdd:cd05908 108 LAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKD----RILSWMPLTHDMGLiaFHLAPLI-AGMNQYLMPTR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1262 DFAGDALATVLERDEVTDMIIT-PS-----VLATVDPERAQ-----YVRNLATGGEACPPELVE----RWSERGRR---I 1323
Cdd:cd05908 183 LFIRRPILWLKKASEHKATIVSsPNfgykyFLKTLKPEKANdwdlsSIRMILNGAEPIDYELCHefldHMSKYGLKrnaI 262
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1324 FNCYGPTEATVWAT--------------RSRMTAGKP--------------VTIGKPVDGFTVRVLDGRLHEVPQGVVGE 1375
Cdd:cd05908 263 LPVYGLAEASVGASlpkaqspfktitlgRRHVTHGEPepevdkkdsecltfVEVGKPIDETDIRICDEDNKILPDGYIGH 342
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1376 LYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRVAKgGNLEFAGRADHQVKINGQRVELGEIEAVLDAQP 1455
Cdd:cd05908 343 IQIRGKNVTPGYYNNPEATAKVFTDDGW-------LKTGDLGFIRN-GRLVITGREKDIIFVNGQNVYPHDIERIAEELE 414
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1456 GV--AQSVVVGVESTRggRKHTEVVAYLVAKpgATIDSAAVLdeaAQHLAAHMVP------SQAIVIDEIPLTPAGKLDR 1527
Cdd:cd05908 415 GVelGRVVACGVNNSN--TRNEEIFCFIEHR--KSEDDFYPL---GKKIKKHLNKrggwqiNEVLPIRRIPKTTSGKVKR 487
|
....*
gi 1827387616 1528 AALPE 1532
Cdd:cd05908 488 YELAQ 492
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
1064-1532 |
6.11e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 83.99 E-value: 6.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDaST 1143
Cdd:PRK07008 42 YRDCERRAKQLAQALAALGVEPGDRVGTLAWNGYRHLEAYYGVSGSGAVCHTINPRLFPEQIAYIVNHAEDRYVLFD-LT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1144 RARLGES---SCE----WVDLAD---LEA------------EAESGD-DITDTERNGSvrltnlAYLIYTSGSTGRPKAV 1200
Cdd:PRK07008 121 FLPLVDAlapQCPnvkgWVAMTDaahLPAgstpllcyetlvGAQDGDyDWPRFDENQA------SSLCYTSGTTGNPKGA 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1201 GVSHTGIV--DFVNSLAKITTGTPEDEpdtrILHVAsPSFDASmfemAWAIPAGHTLVIA----PQADFAGDALATVLER 1274
Cdd:PRK07008 195 LYSHRSTVlhAYGAALPDAMGLSARDA----VLPVV-PMFHVN----AWGLPYSAPLTGAklvlPGPDLDGKSLYELIEA 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1275 DEVTDMIITPSV----LATVDPERAQY--VRNLATGGEACPPELVERWS-ERGRRIFNCYGPTEATVWATRSRMTA---G 1344
Cdd:PRK07008 266 ERVTFSAGVPTVwlglLNHMREAGLRFstLRRTVIGGSACPPAMIRTFEdEYGVEVIHAWGMTEMSPLGTLCKLKWkhsQ 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1345 KPVTI--------GKPVDGFTVRVLDGRLHEVP-QGVV-GELYLSTAGLARGYLGRPGQTAVsfvadpfgepgARMYATG 1414
Cdd:PRK07008 346 LPLDEqrkllekqGRVIYGVDMKIVGDDGRELPwDGKAfGDLQVRGPWVIDRYFRGDASPLV-----------DGWFPTG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1415 DLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKHTEVVaylVAKPGATIDSAAV 1494
Cdd:PRK07008 415 DVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACIACAHPKWDERPLLVV---VKRPGAEVTREEL 491
|
490 500 510
....*....|....*....|....*....|....*...
gi 1827387616 1495 LDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:PRK07008 492 LAFYEGKVAKWWIPDDVVFVDAIPHTATGKLQKLKLRE 529
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
572-994 |
6.26e-16 |
|
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: 83.07 E-value: 6.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 572 PLSRAQRrmWFLNQFDTASGAYNIPAALTLAGDVDETLLFDSLCDVVERHEVLRTVYPSVGAAPVQDVLPVA---VAREQ 648
Cdd:cd19534 3 PLTPIQR--WFFEQNLAGRHHFNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVeelFRLEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 649 LDWREADS---VESLVRSTTEGFDVsTQMPL--RGRFHRDGAGLHVALTMHHIAMDGQSIPVLARDLMSAYAARAEGRTG 723
Cdd:cd19534 81 VDLSSLAQaaaIEALAAEAQSSLDL-EEGPLlaAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYEQALAGEPI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 724 GLPvLDVQYADYALWQQSVLGDADDEtsvlgEQLSHWRRVLAglPAVTDLPMDRPRpavlgTAGATVTVEFDDDLADRVD 803
Cdd:cd19534 160 PLP-SKTSFQTWAELLAEYAQSPALL-----EELAYWRELPA--ADYWGLPKDPEQ-----TYGDARTVSFTLDEEETEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 804 VLARSNTMTGfmvTE------AAFAATVARLASTTDVVIGTPVAGRnDPALEEL-----IGMFvnTLL--LRTQVDPGHS 870
Cdd:cd19534 227 LLQEANAAYR---TEindlllAALALAFQDWTGRAPPAIFLEGHGR-EEIDPGLdlsrtVGWF--TSMypVVLDLEASED 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 871 VGDLLGNVRTTvLDAFANDQVQFDELIEALAPERSS-SHQPLAQIAFTYTEPTVNDVAGlEASGIQAAPVDTGVVNAK-- 947
Cdd:cd19534 301 LGDTLKRVKEQ-LRRIPNKGIGYGILRYLTPEGTKRlAFHPQPEISFNYLGQFDQGERD-DALFVSAVGGGGSDIGPDtp 378
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 948 ----FDLTVAVrarSGGTpMAADFIYATDLFDESTVKRFAEVYRRVLQAIV 994
Cdd:cd19534 379 rfalLDINAVV---EGGQ-LVITVSYSRNMYHEETIQQLADSYKEALEALI 425
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
2561-3061 |
7.29e-16 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 83.93 E-value: 7.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2561 ATDPVTLAELFRAAARRAPDHVAVvDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTG 2640
Cdd:PRK06710 20 SYDIQPLHKYVEQMASRYPEKKAL-HFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2641 GAYVPIDPDYPAERVASMIEDSGAVLGLSVlasgdlpgqEFEWMRLDDDSVAAEIAAVPAGPITD--------------- 2705
Cdd:PRK06710 99 GIVVQTNPLYTERELEYQLHDSGAKVILCL---------DLVFPRVTNVQSATKIEHVIVTRIADflpfpknllypfvqk 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2706 --------------------AERlgEVTAA---------NLAYVIYTSGSTGRPKGVAVTHSGLAN---------FARQE 2747
Cdd:PRK06710 170 kqsnlvvkvsesetihlwnsVEK--EVNTGvevpcdpenDLALLQYTGGTTGFPKGVMLTHKNLVSntlmgvqwlYNCKE 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2748 SDRLNAGDNPV--VLGFASpSFDASVLE-YLLATVNEGTLAYrPSEAVGGEVLERFIAEHGATHTFLTPSVLSTMDptaV 2824
Cdd:PRK06710 248 GEEVVLGVLPFfhVYGMTA-VMNLSIMQgYKMVLIPKFDMKM-VFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYD---I 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2825 PSLRVIAAGGEAVPQPIVDRWAPAT--ELHNLYGPTETTiGITISSAM-RPGDPVRLGGPIGGVDLMVLD----ERLRPv 2897
Cdd:PRK06710 323 SSIRACISGSAPLPVEVQEKFETVTggKLVEGYGLTESS-PVTHSNFLwEKRVPGSIGVPWPDTEAMIMSletgEALPP- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2898 pvGMPGELYVAGGALSRGYLDRSGLTAerftanpyGTAGQRMYRTGDVVRwtpdTDTGGLtLEYTGRSDDQVKLRGLRIE 2977
Cdd:PRK06710 401 --GEIGEIVVKGPQIMKGYWNKPEETA--------AVLQDGWLHTGDVGY----MDEDGF-FYVKDRKKDMIVASGFNVY 465
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2978 LGEIEAVLAEHDAVESAVVLGVGGSV-ATALAAYIVPVDGAV-EVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLD 3055
Cdd:PRK06710 466 PREVEEVLYEHEKVQEVVTIGVPDPYrGETVKAFVVLKEGTEcSEEELNQFARKYLAAYKVPKVYEFRDELPKTTVGKIL 545
|
....*.
gi 1827387616 3056 KRALPE 3061
Cdd:PRK06710 546 RRVLIE 551
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1050-1532 |
8.58e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 83.84 E-value: 8.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVgMERSIGSVL-ATWGVIKSGAAYVPVDPAYPADRIAYM 1128
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAV-LLPNIPAMVeAHFGVPMAGAVLNTLNTRLDAASIAFM 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1129 LEDSGATVGITD----ASTRARLGESSCEW---VDLADleAEAESGDDITDTERNGSVRLTNLAY-------------LI 1188
Cdd:PRK08162 111 LRHGEAKVLIVDtefaEVAREALALLPGPKplvIDVDD--PEYPGGRFIGALDYEAFLASGDPDFawtlpadewdaiaLN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1189 YTSGSTGRPKAVGVSHTGIvdFVNSLAKITTGtpeDEPDTRILHVASPSFDASMFEMAWAIPA-GHTLVIAPQADfaGDA 1267
Cdd:PRK08162 189 YTSGTTGNPKGVVYHHRGA--YLNALSNILAW---GMPKHPVYLWTLPMFHCNGWCFPWTVAArAGTNVCLRKVD--PKL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1268 LATVLERDEVTDMIITPSVLATVDPERAQYVRNLA------TGGEACPPELVERWSERGRRIFNCYGPTE----ATV--- 1334
Cdd:PRK08162 262 IFDLIREHGVTHYCGAPIVLSALINAPAEWRAGIDhpvhamVAGAAPPAAVIAKMEEIGFDLTHVYGLTEtygpATVcaw 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1335 ---WAT-----RSRMTAGKPVTIgKPVDGftVRVLDGR-LHEVPQG--VVGELYLSTAGLARGYLGRPGQTAVSFVADPF 1403
Cdd:PRK08162 342 qpeWDAlpldeRAQLKARQGVRY-PLQEG--VTVLDPDtMQPVPADgeTIGEIMFRGNIVMKGYLKNPKATEEAFAGGWF 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1404 gepgarmyATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEV-VAYLV 1482
Cdd:PRK08162 419 --------HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWG----EVpCAFVE 486
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1483 AKPGATIDSAAVLDEAAQHLAAHMVPSqAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:PRK08162 487 LKDGASATEEEIIAHCREHLAGFKVPK-AVVFGELPKTSTGKIQKFVLRE 535
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
2564-3059 |
1.21e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 83.15 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2564 PVTLAELFRAaaRRAPDHVAVVDGaGARLTYRELDEASDRLARWLIG--RGVGPERaVALAIGRSAQLLTAIWAVAKTGG 2641
Cdd:PRK13388 2 RDTIAQLLRD--RAGDDTIAVRYG-DRTWTWREVLAEAAARAAALIAlaDPDRPLH-VGVLLGNTPEMLFWLAAAALGGY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2642 AYVPIDPDYPAERVASMIE--DSGAVL----GLSVLASGDLPGQEFewMRLDDDSVAAEIAAVPagpitDAERLGEVTAA 2715
Cdd:PRK13388 78 VLVGLNTTRRGAALAADIRraDCQLLVtdaeHRPLLDGLDLPGVRV--LDVDTPAYAELVAAAG-----ALTPHREVDAM 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2716 NLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDR--LNAGDnpvVLGFASPSF--DASVLEYLLATVNEGTLAYRPSEA 2791
Cdd:PRK13388 151 DPFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERfgLTRDD---VCYVSMPLFhsNAVMAGWAPAVASGAAVALPAKFS 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2792 VGGEVLErfIAEHGAthTFLT------PSVLST--MDPTAVPSLRViAAGGEAVPQPI---VDRWapATELHNLYGPTET 2860
Cdd:PRK13388 228 ASGFLDD--VRRYGA--TYFNyvgkplAYILATpeRPDDADNPLRV-AFGNEASPRDIaefSRRF--GCQVEDGYGSSEG 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2861 TIGITISSAMRPGDpvrLGGPIGGVdlMVLD-ERLRPVPVGM-------------PGELY-VAGGALSRGYLDRSGLTAE 2925
Cdd:PRK13388 301 AVIVVREPGTPPGS---IGRGAPGV--AIYNpETLTECAVARfdahgallnadeaIGELVnTAGAGFFEGYYNNPEATAE 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2926 RFTANpygtagqrMYRTGDVVRwtpdTDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV-GGSVA 3004
Cdd:PRK13388 376 RMRHG--------MYWSGDLAY----RDADGW-IYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVpDERVG 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 3005 TALAAYIVPVDGA-VEVSELKAFAGGR--LPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK13388 443 DQVMAALVLRDGAtFDPDAFAAFLAAQpdLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
2589-3049 |
1.30e-15 |
|
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: 82.40 E-value: 1.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2589 GARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGayvpidpdypaerVASMIED--SGAVL 2666
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGA-------------VAALINYnlRGESL 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2667 GLSVLASGDLpgqefewmrldddsvaaeiaavpagpitdaerlgeVTAANLAYVIYTSGSTGRPKGVAVTHSGLANFAR- 2745
Cdd:cd05940 68 AHCLNVSSAK-----------------------------------HLVVDAALYIYTSGTTGLPKAAIISHRRAWRGGAf 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2746 -QESDRLNAGDnpvVLGFASPSFDASVLEYLLATV--NEGTLAYRpseavggevlERFIAEHgathtFLTPSVlsTMDPT 2822
Cdd:cd05940 113 fAGSGGALPSD---VLYTCLPLYHSTALIVGWSAClaSGATLVIR----------KKFSASN-----FWDDIR--KYQAT 172
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2823 AVPSLrviaagGE------AVPQPIVDR----------------WAPATELHNL------YGPTETTIGIT-----ISSA 2869
Cdd:cd05940 173 IFQYI------GElcryllNQPPKPTERkhkvrmifgnglrpdiWEEFKERFGVpriaefYAATEGNSGFInffgkPGAI 246
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2870 MRPGDPVRLGGPIGGVDLMVLDERL--------RPVPVGMPGELYVAGGALSR--GYLDRSglTAERFTANPYGTAGQRM 2939
Cdd:cd05940 247 GRNPSLLRKVAPLALVKYDLESGEPirdaegrcIKVPRGEPGLLISRINPLEPfdGYTDPA--ATEKKILRDVFKKGDAW 324
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2940 YRTGDVVRWtpdtDTGGLTlEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV--GGSVATA-LAAYIVPVDG 3016
Cdd:cd05940 325 FNTGDLMRL----DGEGFW-YFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVqvPGTDGRAgMAAIVLQPNE 399
|
490 500 510
....*....|....*....|....*....|...
gi 1827387616 3017 AVEVSELKAFAGGRLPAYMVPSSFTVIDELPLT 3049
Cdd:cd05940 400 EFDLSALAAHLEKNLPGYARPLFLRLQPEMEIT 432
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
101-470 |
1.32e-15 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 82.96 E-value: 1.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 101 ISSPGDADLDEEEFAGPT--RPANAAFTLFTSGSTGRPKAVVITHRGIANRLAadieqydlTARDVFLYKAPI--TFDVS 176
Cdd:cd17642 162 ITQNLPPGFNEYDFKPPSfdRDEQVALIMNSSGSTGLPKGVQLTHKNIVARFS--------HARDPIFGNQIIpdTAILT 233
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 177 VREIFLPIAIGATLVIAEPG-------RHGDPVHLADLiRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEA 249
Cdd:cd17642 234 VIPFHHGFGMFTTLGYLICGfrvvlmyKFEEELFLRSL-QDYKVQSALLVPTLFAFFAKSTLVDKYDLSNLHEIASGGAP 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 250 LTPPVARDLMVR--LPGTRlqNQYGPAEASIVVTIHRVTqDDRVIPIGTPTRRVSARVLDAALREVpIGV--PGELYLGG 325
Cdd:cd17642 313 LSKEVGEAVAKRfkLPGIR--QGYGLTETTSAILITPEG-DDKPGAVGKVVPFFYAKVVDLDTGKT-LGPneRGELCVKG 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 326 VQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHA 405
Cdd:cd17642 389 PMIMKGYVNNPEATKALIDKDGW-------LHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDA 461
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 406 AAAVVDGPGGqqlvGYLAPADVDVDTVAATTAELLPEYM----RPSAWVR-----LDAMPLSRSGKVDRRLLPE 470
Cdd:cd17642 462 GVAGIPDEDA----GELPAAVVVLEAGKTMTEKEVMDYVasqvSTAKRLRggvkfVDEVPKGLTGKIDRRKIRE 531
|
|
| PRK13388 |
PRK13388 |
acyl-CoA synthetase; Provisional |
1038-1530 |
1.73e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237374 [Multi-domain] Cd Length: 540 Bit Score: 82.77 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1038 TLIDVLAQRdLDPDHPALICDGTEMDYDEFetRTNAIARALLARGVSPEDV---VAVGMERSIGSVLATWGVIKSGAAYV 1114
Cdd:PRK13388 4 TIAQLLRDR-AGDDTIAVRYGDRTWTWREV--LAEAAARAAALIALADPDRplhVGVLLGNTPEMLFWLAAAALGGYVLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1115 PVDPAYPADRIAYMLEDSGATVGITDASTRARLGE-----------SSCEWVDLADLEAEAESGDDITDTerngsvrltN 1183
Cdd:PRK13388 81 GLNTTRRGAALAADIRRADCQLLVTDAEHRPLLDGldlpgvrvldvDTPAYAELVAAAGALTPHREVDAM---------D 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1184 LAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtrILHVASPSF--DASMFEMAWAIPAGHTLVIAPQa 1261
Cdd:PRK13388 152 PFMLIFTSGTTGAPKAVRCSHGRLAFAGRALTERFGLTRDD-----VCYVSMPLFhsNAVMAGWAPAVASGAAVALPAK- 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1262 dFAGDALATVLERDEVTDMIITPSVLATV--DPERAQYVRN---LATGGEAcPPELVERWSER-GRRIFNCYGPTEATVW 1335
Cdd:PRK13388 226 -FSASGFLDDVRRYGATYFNYVGKPLAYIlaTPERPDDADNplrVAFGNEA-SPRDIAEFSRRfGCQVEDGYGSSEGAVI 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1336 ATRSRMTAgkPVTIGKPVDGftVRVLD---------------GRLHEvPQGVVGELyLSTAGLAR--GYLGRPGQTAVSF 1398
Cdd:PRK13388 304 VVREPGTP--PGSIGRGAPG--VAIYNpetltecavarfdahGALLN-ADEAIGEL-VNTAGAGFfeGYYNNPEATAERM 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1399 vadpfgepgaR--MYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhTE 1476
Cdd:PRK13388 378 ----------RhgMYWSGDLAYRDADGWIYFAGRTADWMRVDGENLSAAPIERILLRHPAINRVAVYAVPDERVG---DQ 444
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 1477 VVAYLVAKPGATIDSAAVLD--EAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK13388 445 VMAALVLRDGATFDPDAFAAflAAQPDLGTKAWPRYVRIAADLPSTATNKVLKREL 500
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1154-1530 |
2.14e-15 |
|
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: 82.75 E-value: 2.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1154 WVDLADLEAEAESGDDITdterngsVRLTNLAYLIYTSGSTGRPKAVgVSHTG--IVDFVNSLAKITTGTPEDEpdtril 1231
Cdd:cd05967 209 DLDWSELLAKAEPVDCVP-------VAATDPLYILYTSGTTGKPKGV-VRDNGghAVALNWSMRNIYGIKPGDV------ 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1232 hvaspSFDASmfEMAWAIpaGHTLVI-------APQADFAG------DALA--TVLERDEVTDMIITPSVLATV--DPER 1294
Cdd:cd05967 275 -----WWAAS--DVGWVV--GHSYIVygpllhgATTVLYEGkpvgtpDPGAfwRVIEKYQVNALFTAPTAIRAIrkEDPD 345
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1295 AQYV--------RNLATGGEACPPELVErWSER--GRRIFNCYGPTEaTVWATRSR-----MTAGKPVTIGKPVDGFTVR 1359
Cdd:cd05967 346 GKYIkkydlsslRTLFLAGERLDPPTLE-WAENtlGVPVIDHWWQTE-TGWPITANpvglePLPIKAGSPGKPVPGYQVQ 423
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1360 VLDGRLHEVPQGVVGELYLSTAgLARGYLGRPGQTAVSFVADPFGE-PGarMYATGDLVRVAKGGNLEFAGRADHQVKIN 1438
Cdd:cd05967 424 VLDEDGEPVGPNELGNIVIKLP-LPPGCLLTLWKNDERFKKLYLSKfPG--YYDTGDAGYKDEDGYLFIMGRTDDVINVA 500
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1439 GQRVELGEIEAVLDAQPGVAQSVVVGVE-STRGGRkhteVVAYLVAKPGATIDSAAVLDEAAQH----LAAHMVPSQAIV 1513
Cdd:cd05967 501 GHRLSTGEMEESVLSHPAVAECAVVGVRdELKGQV----PLGLVVLKEGVKITAEELEKELVALvreqIGPVAAFRLVIF 576
|
410
....*....|....*..
gi 1827387616 1514 IDEIPLTPAGKLDRAAL 1530
Cdd:cd05967 577 VKRLPKTRSGKILRRTL 593
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
4-468 |
2.28e-15 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 82.05 E-value: 2.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDGE 83
Cdd:PRK13391 28 RELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPAEAAYIVDDSGARALITSAAKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 AEARSRFDDIVDV-HVLDISSPGDAD----LDEEEFAGPTRPANAAFT----LFTSGSTGRPKAV--------VITHRGI 146
Cdd:PRK13391 108 DVARALLKQCPGVrHRLVLDGDGELEgfvgYAEAVAGLPATPIADESLgtdmLYSSGTTGRPKGIkrplpeqpPDTPLPL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 147 ANRLAadiEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEpgrHGDPVHLADLIRRHGVTVIHFVPAM---- 222
Cdd:PRK13391 188 TAFLQ---RLWGFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVME---HFDAEQYLALIEEYGVTHTQLVPTMfsrm 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 223 LAAFNEVLGAgvGELTSLRlIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTI-------HRVTQdDRVIpIG 295
Cdd:PRK13391 262 LKLPEEVRDK--YDLSSLE-VAIHAAAPCPPQVKEQMIDWWGPIIHEYYAATEGLGFTACdseewlaHPGTV-GRAM-FG 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 296 TPtrrvsaRVLDAALREVPIGVPGELYL-GGVQLArgYAGRPDLTAERFVADPfgepgaRLYRTGDRARWNRDGeieYLG 374
Cdd:PRK13391 337 DL------HILDDDGAELPPGEPGTIWFeGGRPFE--YLNDPAKTAEARHPDG------TWSTVGDIGYVDEDG---YLY 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 375 RTD---FQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAPADvDVDTVAATTAELLpEYMR----- 445
Cdd:PRK13391 400 LTDraaFMIISGGVNIYPQEAENLLITHPKVADAAVfGVPNEDLGEEVKAVVQPVD-GVDPGPALAAELI-AFCRqrlsr 477
|
490 500
....*....|....*....|....*.
gi 1827387616 446 ---PSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK13391 478 qkcPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
1642-2069 |
2.30e-15 |
|
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: 81.30 E-value: 2.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1642 WMIEHSEEPADFadFSQSLVFNVPASAAVADLQTVVEAVAAAHPMLTAVLTR-SGDGWTMNAGAGIVPAVREIDAEGALD 1720
Cdd:cd19066 12 WFLKKLATDPSA--FNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEeAGRYEQVVLDKTVRFRIEIIDLRNLAD 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1721 PalvDAH-RELLGAM-----DPGTGSLLGTA-VVNGEGRRRLVIAIHHLGVDAVSWPILVEDLVTAWAQLTSGRPIELRP 1793
Cdd:cd19066 90 P---EARlLELIDQIqqtiyDLERGPLVRVAlFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAAERQKPTLPPP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1794 eatTTRRIAHLLAGQVH----ARAREVDYWLEQLPERPTSFGTSADRPLHRRRDESSLT--YVVDDVAGSILTTVPQAFG 1867
Cdd:cd19066 167 ---VGSYADYAAWLEKQleseAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTleFFLRSEETKRLREVARESG 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1868 SSVDDVLLGALARAVRAWQldngiaDGGPVTVSTEGHGRDESiagdegaiDLSRTVGWFTSITPLAVDASSDVV---HAV 1944
Cdd:cd19066 244 TTPTQLLLAAFALALKRLT------ASIDVVIGLTFLNRPDE--------AVEDTIGLFLNLLPLRIDTSPDATfpeLLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1945 KSAKDARLSRPAGGVGFGIL--RYNSDGEIAHRPLPTIMYNYFGGGtapstetAPDDFLPVSdRPNMPssiTGAMRSPSV 2022
Cdd:cd19066 310 RTKEQSREAIEHQRVPFIELvrHLGVVPEAPKHPLFEPVFTFKNNQ-------QQLGKTGGF-IFTTP---VYTSSEGTV 378
|
410 420 430 440
....*....|....*....|....*....|....*....|....*..
gi 1827387616 2023 FGINISTAGREERRLEAKVTYATDALDEAAASDIARRWHDELRAVVE 2069
Cdd:cd19066 379 FDLDLEASEDPDGDLLLRLEYSRGVYDERTIDRFAERYMTALRQLIE 425
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
2580-3059 |
2.54e-15 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 82.25 E-value: 2.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2580 DHVAV--VDGAGAR-LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVA 2656
Cdd:PRK04319 59 DKVALryLDASRKEkYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVR 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2657 SMIEDSGAVLGLSVLA------SGDLPgqEFEWMRLDDDSVAAEiaavpaGPITDAERLGE----------VTAANLAYV 2720
Cdd:PRK04319 139 DRLEDSEAKVLITTPAllerkpADDLP--SLKHVLLVGEDVEEG------PGTLDFNALMEqasdefdiewTDREDGAIL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2721 IYTSGSTGRPKGV------AVTHSGLANFAR--QESDR---------------------LNAGDNPVVLGFASPSFDASV 2771
Cdd:PRK04319 211 HYTSGSTGKPKGVlhvhnaMLQHYQTGKYVLdlHEDDVywctadpgwvtgtsygifapwLNGATNVIDGGRFSPERWYRI 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2772 LEYLLATV--NEGTlAYRPSEAVGGEVLERFiaehgathtfltpsvlstmdptAVPSLRVIAAGGEAVpQPIVDRWAPAT 2849
Cdd:PRK04319 291 LEDYKVTVwyTAPT-AIRMLMGAGDDLVKKY----------------------DLSSLRHILSVGEPL-NPEVVRWGMKV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2850 ---ELHNLYGPTETTiGITISS--AM--RPGDpvrLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGG--ALSRGYLDRS 2920
Cdd:PRK04319 347 fglPIHDNWWMTETG-GIMIANypAMdiKPGS---MGKPLPGIEAAIVDDQGNELPPNRMGNLAIKKGwpSMMRGIWNNP 422
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2921 gltaERFtaNPYGTAGqrMYRTGDVVR-------WtpdtdtggltleYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVES 2993
Cdd:PRK04319 423 ----EKY--ESYFAGD--WYVSGDSAYmdedgyfW------------FQGRVDDVIKTSGERVGPFEVESKLMEHPAVAE 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 2994 AVVLGVGGSVATAL-AAYIVPVDGaVEVS-----ELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK04319 483 AGVIGKPDPVRGEIiKAFVALRPG-YEPSeelkeEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVL 553
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
4-463 |
2.67e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 82.31 E-value: 2.67e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAvAMAGGHFVPLDEQLPVDRARYMVRTAGVRlVVVTSDGE 83
Cdd:PRK07529 62 AELLADVTRTANLLHSLGVGPGDVVAFLLPNLPETHFALWG-GEAAGIANPINPLLEPEQIAELLRAAGAK-VLVTLGPF 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 ---------AEARSR---FDDIVDVHVLDISSP---------------GDADLDEE---------EFAGPTRPANAAFTL 127
Cdd:PRK07529 140 pgtdiwqkvAEVLAAlpeLRTVVEVDLARYLPGpkrlavplirrkahaRILDFDAElarqpgdrlFSGRPIGPDDVAAYF 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 128 FTSGSTGRPKAVVITHRG-IANRLAADiEQYDLTARDVFLYKAPItFDV--SVREIFLPIAIGATLVIAEP-GRHGDPV- 202
Cdd:PRK07529 220 HTGGTTGMPKLAQHTHGNeVANAWLGA-LLLGLGPGDTVFCGLPL-FHVnaLLVTGLAPLARGAHVVLATPqGYRGPGVi 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 203 -HLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVgELTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVT 281
Cdd:PRK07529 298 aNFWKIVERYRINFLSGVPTVYAALLQVPVDGH-DISSLRYALCGAAPLPVEVFRRFEAAT-GVRIVEGYGLTEATCVSS 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 282 IHRVTQDDRVIPIGT--PTRRVSARVLDAA---LREVPIGVPGELYLGGVQLARGYagrpdlTAERFVADPFGEPgaRLY 356
Cdd:PRK07529 376 VNPPDGERRIGSVGLrlPYQRVRVVILDDAgryLRDCAVDEVGVLCIAGPNVFSGY------LEAAHNKGLWLED--GWL 447
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 357 RTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYlapadVDVDTVAAT 435
Cdd:PRK07529 448 NTGDLGRIDADGYFWLTGRAKDLIIRGGHNIDPAAIEEALLRHPAVALAAAvGRPDAHAGELPVAY-----VQLKPGASA 522
|
490 500 510
....*....|....*....|....*....|....*..
gi 1827387616 436 TAELLPEYMR---------PSAWVRLDAMPLSRSGKV 463
Cdd:PRK07529 523 TEAELLAFARdhiaeraavPKHVRILDALPKTAVGKI 559
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2108-2534 |
3.56e-15 |
|
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: 80.76 E-value: 3.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2108 PMTPLQQgLFFQADLANTvaDHdaidvYVTQTVLSLTGDVDPGRLRSALSELLARQRVLRSGFVRlPSGAAVTVVPAEVT 2187
Cdd:cd19534 3 PLTPIQR-WFFEQNLAGR--HH-----FNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRR-EDGGWQQRIRGDVE 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2188 vpwSVIDLRAEDAASLDSRVE-EVLATERTNPFDMAKPPLIRVVLVE-HGDGAELVVTNHHLLIDGWSSPLVLADLLSLY 2265
Cdd:cd19534 74 ---ELFRLEVVDLSSLAQAAAiEALAAEAQSSLDLEEGPLLAAALFDgTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2266 ATGQ-TFTGSLP-GTSGRDFADHARAVAT-ADVEAGIAAWREVLAPVTEPtlvAPGHEPSADAPPRDHQFSIDVKVTERL 2342
Cdd:cd19534 151 EQALaGEPIPLPsKTSFQTWAELLAEYAQsPALLEELAYWRELPAADYWG---LPKDPEQTYGDARTVSFTLDEEETEAL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2343 --EALARNNsTTMATVVQFAWAMFLSRLTGTRTVtfaeTVS----GRSPDIEGMESM--VGMFINTIPAVVDVNPDATVV 2414
Cdd:cd19534 228 lqEANAAYR-TEINDLLLAALALAFQDWTGRAPP----AIFleghGREEIDPGLDLSrtVGWFTSMYPVVLDLEASEDLG 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2415 DVLTAVqNDKVKVLDHQQI--GLPRLVAQTGLPALFDTLAVYESF--------PVNVDSVAGIDASSAGglKLVGAKTsd 2484
Cdd:cd19534 303 DTLKRV-KEQLRRIPNKGIgyGILRYLTPEGTKRLAFHPQPEISFnylgqfdqGERDDALFVSAVGGGG--SDIGPDT-- 377
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2485 ATHYPLNLSASRRGAELALKLKYLPTAFAPEQVAVFADVLTGLLGAIADH 2534
Cdd:cd19534 378 PRFALLDINAVVEGGQLVITVSYSRNMYHEETIQQLADSYKEALEALIEH 427
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
129-465 |
5.24e-15 |
|
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: 79.45 E-value: 5.24e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 129 TSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPItFDV--SVREIFLPIAIGATLVIAEPGRHGDPVHLAD 206
Cdd:cd05944 10 TGGTTGTPKLAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPL-FHVngSVVTLLTPLASGAHVVLAGPAGYRNPGLFDN 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 207 ---LIRRHGVTVIHFVPAMLAAFNEVlgAGVGELTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTIH 283
Cdd:cd05944 89 fwkLVERYRITSLSTVPTVYAALLQV--PVNADISSLRFAMSGAAPLPVELRARFEDAT-GLPVVEGYGLTEATCLVAVN 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 284 RVTQDDRVIPIG--TPTRRVSARVLDAALREV-PIGVP--GELYLGGVQLARGYagrpdlTAERFVADPFGEPGarLYRT 358
Cdd:cd05944 166 PPDGPKRPGSVGlrLPYARVRIKVLDGVGRLLrDCAPDevGEICVAGPGVFGGY------LYTEGNKNAFVADG--WLNT 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 359 GDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGP---GGQQLVGY--LAP-ADVDVDTV 432
Cdd:cd05944 238 GDLGRLDADGYLFITGRAKDLIIRGGHNIDPALIEEALLRHPAV--AFAGAVGQPdahAGELPVAYvqLKPgAVVEEEEL 315
|
330 340 350
....*....|....*....|....*....|....
gi 1827387616 433 AATTAELLPEYMR-PSAWVRLDAMPLSRSGKVDR 465
Cdd:cd05944 316 LAWARDHVPERAAvPKHIEVLEELPVTAVGKVFK 349
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1061-1527 |
1.16e-14 |
|
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: 1.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1061 EMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGAT---VG 1137
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKalfVG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1138 ITD--ASTRARLGES--SC------------EWVDLADLEAEAEsGDDITDTERngsvrltnLAYLIYTSGSTGRPKavG 1201
Cdd:cd05932 86 KLDdwKAMAPGVPEGliSIslpppsaancqyQWDDLIAQHPPLE-ERPTRFPEQ--------LATLIYTSGTTGQPK--G 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1202 VSHTgivdfVNSLAKITTGTPED---EPDTRIL------HVASPSFdasmFEMAWAIpAGHTLVIAPQAD-FAGDalatv 1271
Cdd:cd05932 155 VMLT-----FGSFAWAAQAGIEHigtEENDRMLsylplaHVTERVF----VEGGSLY-GGVLVAFAESLDtFVED----- 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1272 LERDEVTDMIITP--------SVLATVDPERAQ-----------------------YVRNLATGGEACPPELVERWSERG 1320
Cdd:cd05932 220 VQRARPTLFFSVPrlwtkfqqGVQDKIPQQKLNlllkipvvnslvkrkvlkglgldQCRLAGCGSAPVPPALLEWYRSLG 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1321 RRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDGrlhevpqgvvGELYLSTAGLARGYLGRPGQTAVSFVA 1400
Cdd:cd05932 300 LNILEAYGMTENFAYSHLNYPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTA 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1401 DPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKIN-GQRVELGEIEAVLDAQPGVAQSVVVGVESTR---------G 1470
Cdd:cd05932 370 DGF-------LRTGDKGELDADGNLTITGRVKDIFKTSkGKYVAPAPIENKLAEHDRVEMVCVIGSGLPAplalvvlseE 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 1471 GRKHTEVVAY--LVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDR 1527
Cdd:cd05932 443 ARLRADAFARaeLEASLRAHLARVNSTLDSHEQLAGIVVVKDPWSIDNGILTPTLKIKR 501
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
2592-3054 |
1.27e-14 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 79.15 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2592 LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVlglsvl 2671
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAV------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2672 asgdlpgqefewmrldddsvaaeIAAVPagpitdaerlgEVTAANLAYVIY-TSGSTGRPKGVAVTHSG--LANFARQES 2748
Cdd:cd05974 75 -----------------------YAAVD-----------ENTHADDPMLLYfTSGTTSKPKLVEHTHRSypVGHLSTMYW 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2749 DRLNAGDnpVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEA-VGGEVLERFIAEHGATHTFLTPSVLSTMDPTAVPSL 2827
Cdd:cd05974 121 IGLKPGD--VHWNISSPGWAKHAWSCFFAPWNAGATVFLFNYArFDAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASF 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2828 RV----IAAGGEAVPQPIVD--RWAPATELHNLYGPTETTIGITISsamrPGDPVR---LGGPIGGVDLMVLDERLRPVP 2898
Cdd:cd05974 199 DVklreVVGAGEPLNPEVIEqvRRAWGLTIRDGYGQTETTALVGNS----PGQPVKagsMGRPLPGYRVALLDPDGAPAT 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2899 vgmPGELYVAGGA-----LSRGYLDRSGLTAerftanpyGTAGQRMYRTGDVVRWTPDtdtGGLTleYTGRSDDQVKLRG 2973
Cdd:cd05974 275 ---EGEVALDLGDtrpvgLMKGYAGDPDKTA--------HAMRGGYYRTGDIAMRDED---GYLT--YVGRADDVFKSSD 338
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2974 LRIELGEIEAVLAEHDAVESAVVLGVGGSVATAL-AAYIVPVDGAVEVSELK----AFAGGRLPAYMVPSSFTvIDELPL 3048
Cdd:cd05974 339 YRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVpKAFIVLRAGYEPSPETAleifRFSRERLAPYKRIRRLE-FAELPK 417
|
....*.
gi 1827387616 3049 TPVGKL 3054
Cdd:cd05974 418 TISGKI 423
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
236-471 |
1.32e-14 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 79.87 E-value: 1.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 236 ELTSLRLIQTGGEALTPPVArDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPI 315
Cdd:PRK12492 331 DFSALKLTNSGGTALVKATA-ERWEQLTGCTIVEGYGLTETSPVASTNPYGELARLGTVGIPVPGTALKVIDDDGNELPL 409
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 316 GVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAA 395
Cdd:PRK12492 410 GERGELCIKGPQVMKGYWQQPEATAEALDAEGW-------FKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDV 482
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 396 LAAAPGVLHAAA-AVVDGPGGQQLVGYLAPAD--VDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEP 471
Cdd:PRK12492 483 VMAHPKVANCAAiGVPDERSGEAVKLFVVARDpgLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRRELRDI 561
|
|
| PRK12582 |
PRK12582 |
acyl-CoA synthetase; Provisional |
1043-1463 |
1.39e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237144 [Multi-domain] Cd Length: 624 Bit Score: 80.09 E-value: 1.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1043 LAQRDldPDHPalicDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPA 1122
Cdd:PRK12582 68 LAQRE--PGHG----QWRKVTYGEAKRAVDALAQALLDLGLDPGRPVMILSGNSIEHALMTLAAMQAGVPAAPVSPAYSL 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1123 -----DRIAYMLE---------DSGATVgitdASTRARLGESSCEWVdLADLEAEAESG---DDITDTERNGSV-----R 1180
Cdd:PRK12582 142 mshdhAKLKHLFDlvkprvvfaQSGAPF----ARALAALDLLDVTVV-HVTGPGEGIASiafADLAATPPTAAVaaaiaA 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1181 LT--NLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDEPDTrilhvaspsfdaSMFEMAW----------- 1247
Cdd:PRK12582 217 ITpdTVAKYLFTSGSTGMPKAVINTQRMMCANIAMQEQLRPREPDPPPPV------------SLDWMPWnhtmggnanfn 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1248 -AIPAGHTLVIAPQADFAGDALATVLERDEvtdmiITPSVLATV-------------DPE-RAQYVRNLAT---GGEACP 1309
Cdd:PRK12582 285 gLLWGGGTLYIDDGKPLPGMFEETIRNLRE-----ISPTVYGNVpagyamlaeamekDDAlRRSFFKNLRLmayGGATLS 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1310 PELVERW-----SERGRRI--FNCYGPTEA------TVWATRsrmtagKPVTIGKPVDGFTVRVldgrlheVPQGVVGEL 1376
Cdd:PRK12582 360 DDLYERMqalavRTTGHRIpfYTGYGATETaptttgTHWDTE------RVGLIGLPLPGVELKL-------APVGDKYEV 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1377 YLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRV------AKGgnLEFAGRADHQVKI-NGQRVELGEIEA 1449
Cdd:PRK12582 427 RVKGPNVTPGYHKDPELTAAAFDEEGF-------YRLGDAARFvdpddpEKG--LIFDGRVAEDFKLsTGTWVSVGTLRP 497
|
490
....*....|....*
gi 1827387616 1450 -VLDAQPGVAQSVVV 1463
Cdd:PRK12582 498 dAVAACSPVIHDAVV 512
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
2564-3061 |
1.48e-14 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 79.80 E-value: 1.48e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2564 PVTLAELFRAAARRAPDHVAV---VDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTG 2640
Cdd:PRK06018 9 PLLCHRIIDHAARIHGNREVVtrsVEGPIVRTTYAQIHDRALKVSQALDRDGIKLGDRVATIAWNTWRHLEAWYGIMGIG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2641 GAYVPIDPDYPAERVASMI---EDSGAVLGLSVLA-----SGDLPGQEfEWMRLDDDSVAAEIA---AVPAGPITDAER- 2708
Cdd:PRK06018 89 AICHTVNPRLFPEQIAWIInhaEDRVVITDLTFVPilekiADKLPSVE-RYVVLTDAAHMPQTTlknAVAYEEWIAEADg 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2709 ------LGEVTAANLAYviyTSGSTGRPKGVAVTHSG--LANFARQESDRLNAGDNPVVLGFAsPSFDASVLEYLLATVN 2780
Cdd:PRK06018 168 dfawktFDENTAAGMCY---TSGTTGDPKGVLYSHRSnvLHALMANNGDALGTSAADTMLPVV-PLFHANSWGIAFSAPS 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2781 EGTLAYRPSEAVGGEVLERFIAEHGATHTFLTPSV----LSTMDPT--AVPSLRVIAAGGEAVPQPIVDRWAP-ATELHN 2853
Cdd:PRK06018 244 MGTKLVMPGAKLDGASVYELLDTEKVTFTAGVPTVwlmlLQYMEKEglKLPHLKMVVCGGSAMPRSMIKAFEDmGVEVRH 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2854 LYGPTETTIGITISS-----AMRPGDP-----VRLGGPIGGVDLMVLDERLRPVPVG--MPGELYVAGGALSRGYL--DR 2919
Cdd:PRK06018 324 AWGMTEMSPLGTLAAlkppfSKLPGDArldvlQKQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYYrvDG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2920 SGLTAERFtanpygtagqrmYRTGDVVrwtpDTDTGGlTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV 2999
Cdd:PRK06018 404 EILDDDGF------------FDTGDVA----TIDAYG-YMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIGV 466
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 3000 GGSVATALAAYIVPVDGAVEVS--ELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPE 3061
Cdd:PRK06018 467 YHPKWDERPLLIVQLKPGETATreEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTALRE 530
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
2575-3008 |
1.78e-14 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 79.40 E-value: 1.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2575 ARRAPDHVAVVDGAGA----RLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDY 2650
Cdd:cd05921 5 ARQAPDRTWLAEREGNggwrRVTYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAY 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2651 PA-----ERVASMIE--DSGAV-----------------LGLSVLASGDLPGqefewmrlDDDSVA-AEIAAVPAGPITD 2705
Cdd:cd05921 85 SLmsqdlAKLKHLFEllKPGLVfaqdaapfaralaaifpLGTPLVVSRNAVA--------GRGAISfAELAATPPTAAVD 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2706 AERlGEVTAANLAYVIYTSGSTGRPKGVAVTHSGL-ANFARQESDR-LNAGDNPVVLGFA--SPSFDASVlEYLLATVNE 2781
Cdd:cd05921 157 AAF-AAVGPDTVAKFLFTSGSTGLPKAVINTQRMLcANQAMLEQTYpFFGEEPPVLVDWLpwNHTFGGNH-NFNLVLYNG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2782 GTL---AYRPSEAVGGEVLeRFIAEHGATHTFLTPSVLSTM------DPTAVPS----LRVIAAGGEAVPQPIVDRW--- 2845
Cdd:cd05921 235 GTLyidDGKPMPGGFEETL-RNLREISPTVYFNVPAGWEMLvaalekDEALRRRffkrLKLMFYAGAGLSQDVWDRLqal 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2846 APATELHNL-----YGPTETTIGITISS--AMRPGDpvrLGGPIGGVDLmvlderlRPVPVGMPGELYVAGGALSRGYLD 2918
Cdd:cd05921 314 AVATVGERIpmmagLGATETAPTATFTHwpTERSGL---IGLPAPGTEL-------KLVPSGGKYEVRVKGPNVTPGYWR 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2919 RSGLTAERFTANPYgtagqrmYRTGDVVRWT-PDTDTGGLTleYTGRSDDQVKLR-GLRIELGEI--EAVLAEHDAVESA 2994
Cdd:cd05921 384 QPELTAQAFDEEGF-------YCLGDAAKLAdPDDPAKGLV--FDGRVAEDFKLAsGTWVSVGPLraRAVAACAPLVHDA 454
|
490
....*....|....
gi 1827387616 2995 VVLGVGGSVATALA 3008
Cdd:cd05921 455 VVAGEDRAEVGALV 468
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
4-465 |
2.31e-14 |
|
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: 79.08 E-value: 2.31e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDG- 82
Cdd:cd05970 51 AELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDn 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 83 -----EAEARSRFDDIVDVHVLDISSPGDADLDEE------EFAGPTRPANA-----AFTLFTSGSTGRPKAVVITHRGI 146
Cdd:cd05970 131 ipeeiEKAAPECPSKPKLVWVGDPVPEGWIDFRKLiknaspDFERPTANSYPcgediLLVYFSSGTTGMPKMVEHDFTYP 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 147 ANRLAADIEQYDLTARDVFLYKAPITFDVSV-REIFLPIAIGATLVIAEPGRHgDPVHLADLIRRHGVTVIHFVPAMlaa 225
Cdd:cd05970 211 LGHIVTAKYWQNVREGGLHLTVADTGWGKAVwGKIYGQWIAGAAVFVYDYDKF-DPKALLEKLSKYGVTTFCAPPTI--- 286
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 226 FNEVLGAGVG--ELTSLRLIQTGGEALTPPVARDLMvRLPGTRLQNQYGPAEasIVVTIHRVT-QDDRVIPIGTPTRRVS 302
Cdd:cd05970 287 YRFLIREDLSryDLSSLRYCTTAGEALNPEVFNTFK-EKTGIKLMEGFGQTE--TTLTIATFPwMEPKPGSMGKPAPGYE 363
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 303 ARVLDAALREVPIGVPGELYLG-----GVQLARGYAGRPDLTAERFvADPFgepgarlYRTGDRARWNRDGEIEYLGRTD 377
Cdd:cd05970 364 IDLIDREGRSCEAGEEGEIVIRtskgkPVGLFGGYYKDAEKTAEVW-HDGY-------YHTGDAAWMDEDGYLWFVGRTD 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 378 FQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGPGGQQLV--------GYLAPADVD---VDTVAATTAellpEYMRP 446
Cdd:cd05970 436 DLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVkativlakGYEPSEELKkelQDHVKKVTA----PYKYP 511
|
490
....*....|....*....
gi 1827387616 447 SAWVRLDAMPLSRSGKVDR 465
Cdd:cd05970 512 RIVEFVDELPKTISGKIRR 530
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
76-468 |
5.16e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 78.01 E-value: 5.16e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 76 VVVTSDgEAEARSRFDDIVDV-HVLDISSPGDA-----DLDE------EEF-AGPTRPANAAFTLFTSGSTGRPKAVVIT 142
Cdd:PRK04319 148 VLITTP-ALLERKPADDLPSLkHVLLVGEDVEEgpgtlDFNAlmeqasDEFdIEWTDREDGAILHYTSGSTGKPKGVLHV 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 143 HRgianrlaADIEQY-------DLTARDVFLYKA-PITFDVSVREIFLPIAIGATLVIAEpGRHgDPVHLADLIRRHGVT 214
Cdd:PRK04319 227 HN-------AMLQHYqtgkyvlDLHEDDVYWCTAdPGWVTGTSYGIFAPWLNGATNVIDG-GRF-SPERWYRILEDYKVT 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 215 VIHFVPamlAAFNEVLGAGVG-----ELTSLRLIQTGGEALTPPVARDLMvRLPGTRLQNQYGPAEASIVVTIHRVTQDD 289
Cdd:PRK04319 298 VWYTAP---TAIRMLMGAGDDlvkkyDLSSLRHILSVGEPLNPEVVRWGM-KVFGLPIHDNWWMTETGGIMIANYPAMDI 373
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 290 RVIPIGTPTRRVSARVLDAALREVPIGVPGELYL--GGVQLARGYAGRPDLTAERFVADpfgepgarLYRTGDRARWNRD 367
Cdd:PRK04319 374 KPGSMGKPLPGIEAAIVDDQGNELPPNRMGNLAIkkGWPSMMRGIWNNPEKYESYFAGD--------WYVSGDSAYMDED 445
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 368 GEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGPggQQLVGYLAPADVDVDTVAATTAELLPEYMrps 447
Cdd:PRK04319 446 GYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAV--AEAGVIGKP--DPVRGEIIKAFVALRPGYEPSEELKEEIR--- 518
|
410 420 430
....*....|....*....|....*....|....*
gi 1827387616 448 AWVR--------------LDAMPLSRSGKVDRRLL 468
Cdd:PRK04319 519 GFVKkglgahaapreiefKDKLPKTRSGKIMRRVL 553
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
4-402 |
6.03e-14 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 77.73 E-value: 6.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLP-VDRARYMVRTA------GVRLV 76
Cdd:PRK07768 33 GEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPrTDLAVWAEDTLrvigmiGAKAV 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 77 VVTSDGEAEARSRFDDIVDVHVLdisspgdADLDEEEFAGP--TRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADI 154
Cdd:PRK07768 113 VVGEPFLAAAPVLEEKGIRVLTV-------ADLLAADPIDPveTGEDDLALMQLTSGSTGSPKAVQITHGNLYANAEAMF 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 155 E--QYDLtARDVFLYKAPITFDVS-VREIFLPIAIGATLVIAEPGRH-GDPVHLADLIRRHGVTVI---HFVPAMLAafn 227
Cdd:PRK07768 186 VaaEFDV-ETDVMVSWLPLFHDMGmVGFLTVPMYFGAELVKVTPMDFlRDPLLWAELISKYRGTMTaapNFAYALLA--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 228 EVLGAGVGE----LTSLRLIQTGGEALTPPVARDLMVR-----LPGTRLQNQYGPAEASIVVTIHRV------------- 285
Cdd:PRK07768 262 RRLRRQAKPgafdLSSLRFALNGAEPIDPADVEDLLDAgarfgLRPEAILPAYGMAEATLAVSFSPCgaglvvdevdadl 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 286 -TQDDRVIP-----------IGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYagrpdLTAERFVA--DPFGep 351
Cdd:PRK07768 342 lAALRRAVPatkgntrrlatLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGY-----LTMDGFIPaqDADG-- 414
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 352 garLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGV 402
Cdd:PRK07768 415 ---WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGV 462
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
2555-3061 |
6.33e-14 |
|
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: 77.57 E-value: 6.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2555 PVTggPATDPVTLAELFRAAARRA--PDHVAVVDG-AGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLT 2631
Cdd:cd17642 7 PFY--PLEDGTAGEQLHKAMKRYAsvPGTIAFTDAhTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2632 AIWAVAKTGGAYVPIDPDY-------------PA---------ERVASMIEDSGAVLGLSVLASG-DLPG-QEFE-WMRL 2686
Cdd:cd17642 85 PVIAGLFIGVGVAPTNDIYnereldhslniskPTivfcskkglQKVLNVQKKLKIIKTIIILDSKeDYKGyQCLYtFITQ 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2687 DDDSVAAEIAAVPagPITDAERlgevtaaNLAYVIYTSGSTGRPKGVAVTHSGL-ANFARQESDRLNAGDNP-VVLGFAS 2764
Cdd:cd17642 165 NLPPGFNEYDFKP--PSFDRDE-------QVALIMNSSGSTGLPKGVQLTHKNIvARFSHARDPIFGNQIIPdTAILTVI 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2765 PSFDASVLEYLLATVNEG---TLAYRPSEavggEVLERFIAEHGATHTFLTPSVLS------TMDPTAVPSLRVIAAGGE 2835
Cdd:cd17642 236 PFHHGFGMFTTLGYLICGfrvVLMYKFEE----ELFLRSLQDYKVQSALLVPTLFAffakstLVDKYDLSNLHEIASGGA 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2836 AVPQPIVDRWAPATELHNL---YGPTETTIGITISSA--MRPGDpvrLGGPIGGVDLMVLD-ERLRPVPVGMPGELYVAG 2909
Cdd:cd17642 312 PLSKEVGEAVAKRFKLPGIrqgYGLTETTSAILITPEgdDKPGA---VGKVVPFFYAKVVDlDTGKTLGPNERGELCVKG 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2910 GALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVRWtpDTDTGGLTLEytgRSDDQVKLRGLRIELGEIEAVLAEHD 2989
Cdd:cd17642 389 PMIMKGYVNNPEATKALIDKDGW-------LHSGDIAYY--DEDGHFFIVD---RLKSLIKYKGYQVPPAELESILLQHP 456
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 2990 AVESAVVLGVGGSVATALAAYIVPVDGAVEVSE---LKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPE 3061
Cdd:cd17642 457 KIFDAGVAGIPDEDAGELPAAVVVLEAGKTMTEkevMDYVASQVSTAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
2717-3034 |
6.98e-14 |
|
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: 77.26 E-value: 6.98e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2717 LAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLN--AGDNPVVLGFAsPSfdASVLEYLL--------ATVNEG---T 2783
Cdd:cd17639 90 LACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPelLGPDDRYLAYL-PL--AHIFELAAenvclyrgGTIGYGsprT 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2784 L-------------AYRPSEAVG-GEVLER----------------------------FIAEHGATHTFLTPSVLSTMDP 2821
Cdd:cd17639 167 LtdkskrgckgdltEFKPTLMVGvPAIWDTirkgvlaklnpmgglkrtlfwtayqsklKALKEGPGTPLLDELVFKKVRA 246
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2822 TAVPSLRVIAAGGEAVpqpivdrwAPAT-ELHNL--------YGPTETTIGITISsamRPGD--PVRLGGPIGGVDLMVL 2890
Cdd:cd17639 247 ALGGRLRYMLSGGAPL--------SADTqEFLNIvlcpviqgYGLTETCAGGTVQ---DPGDleTGRVGPPLPCCEIKLV 315
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2891 D-ERLRPVP-VGMP-GELYVAGGALSRGYLDRSGLTAERFTanpygtaGQRMYRTGDVVRWTPDTdtgglTLEYTGRSDD 2967
Cdd:cd17639 316 DwEEGGYSTdKPPPrGEILIRGPNVFKGYYKNPEKTKEAFD-------GDGWFHTGDIGEFHPDG-----TLKIIDRKKD 383
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 2968 QVKLR-GLRIELGEIEAVLAEHDAVESAVVLGVggSVATALAAYIVPVDGAVEV-SELKAFAGGRLPAY 3034
Cdd:cd17639 384 LVKLQnGEYIALEKLESIYRSNPLVNNICVYAD--PDKSYPVAIVVPNEKHLTKlAEKHGVINSEWEEL 450
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
120-468 |
7.32e-14 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 77.61 E-value: 7.32e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 120 PANAAFTLFTSGSTGRPKAVVITHRG-IANRLAAdiEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEPGRH 198
Cdd:PRK08751 207 PDDIAFLQYTGGTTGVAKGAMLTHRNlVANMQQA--HQWLAGTGKLEEGCEVVITALPLYHIFALTANGLVFMKIGGCNH 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 199 --GDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGA-GVGEL--TSLRLIQTGGEALTPPVARDLMvRLPGTRLQNQYGP 273
Cdd:PRK08751 285 liSNPRDMPGFVKELKKTRFTAFTGVNTLFNGLLNTpGFDQIdfSSLKMTLGGGMAVQRSVAERWK-QVTGLTLVEAYGL 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 274 AEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepga 353
Cdd:PRK08751 364 TETSPAACINPLTLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIGELCIKGPQVMKGYWKRPEETAKVMDADGW----- 438
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 354 rlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLH-AAAAVVDGPGGQQLVGYLAPAD--VDVD 430
Cdd:PRK08751 439 --LHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMPGVLEvAAVGVPDEKSGEIVKVVIVKKDpaLTAE 516
|
330 340 350
....*....|....*....|....*....|....*...
gi 1827387616 431 TVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK08751 517 DVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
3078-3139 |
9.38e-14 |
|
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: 67.97 E-value: 9.38e-14
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 3078 RTIADVAAGVLNIDAGLVSATSSFFELGGDSLSAARLAARLSDQLGVAVSVRDVFESGSIRA 3139
Cdd:pfam00550 1 ERLRELLAEVLGVPAEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
28-468 |
1.03e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 77.03 E-value: 1.03e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 28 VGIQIDRSVEQVVAIHAVAMAGGHFVPLDeqlPVDRARYMVRT---AGVRLVVVtsdgEAEARSRFDDIV-DVHVLDISS 103
Cdd:PRK07867 57 VGVLLDNTPEFSLLLGAAALSGIVPVGLN---PTRRGAALARDiahADCQLVLT----ESAHAELLDGLDpGVRVINVDS 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 104 PGDADL-----DEEEFAGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPITFDVSVR 178
Cdd:PRK07867 130 PAWADElaahrDAEPPFRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRFGLGPDDVCYVSMPLFHSNAVM 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 179 EIFLP-IAIGATLVIaePGRHGDPVHLADlIRRHGVTVIHFVPAMLAAfneVLGAgvGEL-----TSLRlIQTGGEALTP 252
Cdd:PRK07867 210 AGWAVaLAAGASIAL--RRKFSASGFLPD-VRRYGATYANYVGKPLSY---VLAT--PERpddadNPLR-IVYGNEGAPG 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 253 PVARdlMVRLPGTRLQNQYGPAEASIVVT---------IHRVTQDDRVIPIGTPTRRVSArVLDAALREVPIGVPGELY- 322
Cdd:PRK07867 281 DIAR--FARRFGCVVVDGFGSTEGGVAITrtpdtppgaLGPLPPGVAIVDPDTGTECPPA-EDADGRLLNADEAIGELVn 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 323 LGGVQLARGYAGRPDLTAERFVADpfgepgarLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGV 402
Cdd:PRK07867 358 TAGPGGFEGYYNDPEADAERMRGG--------VYWSGDLAYRDADGYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDA 429
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 403 LHAAA-AVVDGPGGQQLVGYLAPADvDVDTVAATTAELLPEY--MRPSAW---VRL-DAMPLSRSGKVDRRLL 468
Cdd:PRK07867 430 TEVAVyAVPDPVVGDQVMAALVLAP-GAKFDPDAFAEFLAAQpdLGPKQWpsyVRVcAELPRTATFKVLKRQL 501
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
2574-3068 |
1.12e-13 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 76.91 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2574 AARRAPDHVAVVDGAgARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAE 2653
Cdd:PRK08162 27 AAEVYPDRPAVIHGD-RRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2654 RVASMIEDSGAVLGLSVLASGDLPGQEFEWM-RLDDDSVAAEIAAVPAGPI---TDAERLGEVTAANLAYVI-------- 2721
Cdd:PRK08162 106 SIAFMLRHGEAKVLIVDTEFAEVAREALALLpGPKPLVIDVDDPEYPGGRFigaLDYEAFLASGDPDFAWTLpadewdai 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2722 ---YTSGSTGRPKGVAVTHSGLAnfarqesdrLNAGDN---------PVVL---------GFASPSFDAsvleyLLATVN 2780
Cdd:PRK08162 186 alnYTSGTTGNPKGVVYHHRGAY---------LNALSNilawgmpkhPVYLwtlpmfhcnGWCFPWTVA-----ARAGTN 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2781 EGTLAYRPseavgGEVLErFIAEHGATHTFLTPSVLSTM-----DPTAVPSLRVIAAGGEAVPQPIVDRWAPAT--ELHN 2853
Cdd:PRK08162 252 VCLRKVDP-----KLIFD-LIREHGVTHYCGAPIVLSALinapaEWRAGIDHPVHAMVAGAAPPAAVIAKMEEIgfDLTH 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2854 LYGPTETTIGITIS------SAMRPGDPVRLGGPiGGV------DLMVLD-ERLRPVPVG--MPGELYVAGGALSRGYLD 2918
Cdd:PRK08162 326 VYGLTETYGPATVCawqpewDALPLDERAQLKAR-QGVryplqeGVTVLDpDTMQPVPADgeTIGEIMFRGNIVMKGYLK 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2919 RSGLTAERFtanpygtAGQrMYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVlg 2998
Cdd:PRK08162 405 NPKATEEAF-------AGG-WFHTGDLAVLHPDG-----YIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVLVAAV-- 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 2999 vggsVATALA-------AYIVPVDGA-VEVSELKAFAGGRLPAYMVPSSFtVIDELPLTPVGKLDKRALPEPVLEAGE 3068
Cdd:PRK08162 470 ----VAKPDPkwgevpcAFVELKDGAsATEEEIIAHCREHLAGFKVPKAV-VFGELPKTSTGKIQKFVLREQAKSLKA 542
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1035-1532 |
1.21e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 76.94 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1035 EAGTLID-VLAQRDLDPDHPALI--CDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGA 1111
Cdd:PLN02330 26 DKLTLPDfVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1112 AYVPVDPAYPADRIAYMLEDSGATVGITDASTRAR----------LGESSCE----WVDLADleaeaeSGDDITDTERNG 1177
Cdd:PLN02330 106 VFSGANPTALESEIKKQAEAAGAKLIVTNDTNYGKvkglglpvivLGEEKIEgavnWKELLE------AADRAGDTSDNE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1178 SVRLTNLAYLIYTSGSTGRPKAVGVSHTGIVdfVNSLAKITTGTPEdepdtRILHVASPSFdasmfemawaIPAGHTLVI 1257
Cdd:PLN02330 180 EILQTDLCALPFSSGTTGISKGVMLTHRNLV--ANLCSSLFSVGPE-----MIGQVVTLGL----------IPFFHIYGI 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1258 ApqadfaGDALATVLERDEVTDM---------------------IITPSVLATV-DPERAQY------VRNLATGGEACP 1309
Cdd:PLN02330 243 T------GICCATLRNKGKVVVMsrfelrtflnalitqevsfapIVPPIILNLVkNPIVEEFdlsklkLQAIMTAAAPLA 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1310 PELVERWSER--GRRIFNCYGPTEATVWAtrsrMTAGKPV---------TIGKPVDGFTVRVLD---GRlhEVPQGVVGE 1375
Cdd:PLN02330 317 PELLTAFEAKfpGVQVQEAYGLTEHSCIT----LTHGDPEkghgiakknSVGFILPNLEVKFIDpdtGR--SLPKNTPGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1376 LYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQP 1455
Cdd:PLN02330 391 LCVRSQCVMQGYYNNKEETDRTIDEDGW-------LHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHP 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 1456 GVAQSVVVGVESTRGGrkhtEV-VAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALPE 1532
Cdd:PLN02330 464 SVEDAAVVPLPDEEAG----EIpAACVVINPKAKESEEDILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKE 537
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1187-1527 |
1.29e-13 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 74.99 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1187 LIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDEPDTRILHVaspSFDASMFEMAWAIPAGHTLVIApqADFAG- 1265
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTFFAVPDILQKEGLNWVVGDVTYLPLPA---THIGGLWWILTCLIHGGLCVTG--GENTTy 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1266 DALATVLERDEVTDMIITPSVLATVDPERA---QYVR--NLATGGEACPPELVERWSE--RGRRIFNCYGPTEAT----V 1334
Cdd:cd17635 81 KSLFKILTTNAVTTTCLVPTLLSKLVSELKsanATVPslRLIGYGGSRAIAADVRFIEatGLTNTAQVYGLSETGtalcL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1335 WATRSRMTAGkpvTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmyATG 1414
Cdd:cd17635 161 PTDDDSIEIN---AVGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV--------NTG 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1415 DLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtEVVAYLVAKPGATIDSA-- 1492
Cdd:cd17635 230 DLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEFG----ELVGLAVVASAELDENAir 305
|
330 340 350
....*....|....*....|....*....|....*
gi 1827387616 1493 AVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDR 1527
Cdd:cd17635 306 ALKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
124-475 |
1.29e-13 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 76.63 E-value: 1.29e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 124 AFTLFTSGSTGRPKAVVITHRG-IANRLAAD-------IEQYDLTARDVFLYKapiTFDVSVrEIFLPIAIGAT-LVIAE 194
Cdd:PRK08974 209 AFLQYTGGTTGVAKGAMLTHRNmLANLEQAKaaygpllHPGKELVVTALPLYH---IFALTV-NCLLFIELGGQnLLITN 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 195 PgRhgDPVHLADLIRRHGVTVIHFVPAMLAA------FNEVlgagvgELTSLRLIQTGGEALTPPVArDLMVRLPGTRLQ 268
Cdd:PRK08974 285 P-R--DIPGFVKELKKYPFTAITGVNTLFNAllnneeFQEL------DFSSLKLSVGGGMAVQQAVA-ERWVKLTGQYLL 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 269 NQYGPAEASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAErFVADPF 348
Cdd:PRK08974 355 EGYGLTECSPLVSVNPYDLDYYSGSIGLPVPSTEIKLVDDDGNEVPPGEPGELWVKGPQVMLGYWQRPEATDE-VIKDGW 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 349 gepgarlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAPADV 427
Cdd:PRK08974 434 -------LATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEDVVMLHPKVLEVAAvGVPSEVSGEAVKIFVVKKDP 506
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1827387616 428 DV--DTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEPEIAP 475
Cdd:PRK08974 507 SLteEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRRELRDEARAK 556
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
2591-3059 |
1.40e-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: 76.83 E-value: 1.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2591 RLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGA------ 2664
Cdd:cd05966 84 TITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGAVHSVVFAGFSAESLADRINDAQCklvita 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2665 --------VLGLSVLASGDL----------------------PGQEFEWmrldDDSVAAEIAAVPAGPItDAErlgevta 2714
Cdd:cd05966 164 dggyrggkVIPLKEIVDEALekcpsvekvlvvkrtggevpmtEGRDLWW----HDLMAKQSPECEPEWM-DSE------- 231
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2715 aNLAYVIYTSGSTGRPKGVAVTHSGLANFAR---------QESDRL-NAGD------------NPVVLGfaspsfdASVL 2772
Cdd:cd05966 232 -DPLFILYTSGSTGKPKGVVHTTGGYLLYAAttfkyvfdyHPDDIYwCTADigwitghsyivyGPLANG-------ATTV 303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2773 EYllatvnEGTLAYrPSEAVGGEVLERfiaeHGATHtFLTPsvlstmdPTAV----------------PSLRVIAAGGEA 2836
Cdd:cd05966 304 MF------EGTPTY-PDPGRYWDIVEK----HKVTI-FYTA-------PTAIralmkfgdewvkkhdlSSLRVLGSVGEP 364
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2837 V-PQ--------------PIVDRWapatelhnlyGPTETTiGITISS-----AMRPGDPVRlggPIGGVDLMVLDERLRP 2896
Cdd:cd05966 365 InPEawmwyyevigkercPIVDTW----------WQTETG-GIMITPlpgatPLKPGSATR---PFFGIEPAILDEEGNE 430
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2897 VPVGMPGELYVAG---GALSRGYLDRsgltaERFTaNPYGTAGQRMYRTGDVVRWTPDtdtGGLTLeyTGRSDDQVKLRG 2973
Cdd:cd05966 431 VEGEVEGYLVIKRpwpGMARTIYGDH-----ERYE-DTYFSKFPGYYFTGDGARRDED---GYYWI--TGRVDDVINVSG 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2974 LRIELGEIEAVLAEHDAV-ESAVVlGVGGSVAT-ALAAYIVPVDGAVE----VSELKAFAGGRLPAYMVPSSFTVIDELP 3047
Cdd:cd05966 500 HRLGTAEVESALVAHPAVaEAAVV-GRPHDIKGeAIYAFVTLKDGEEPsdelRKELRKHVRKEIGPIATPDKIQFVPGLP 578
|
570
....*....|..
gi 1827387616 3048 LTPVGKLDKRAL 3059
Cdd:cd05966 579 KTRSGKIMRRIL 590
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1446-1524 |
1.47e-13 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 67.95 E-value: 1.47e-13
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 1446 EIEAVLDAQPGVAQSVVVGVESTRGGRkhtEVVAYLVAKPGATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGK 1524
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGE---APVAFVVLKPGVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
2592-3033 |
1.82e-13 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 75.97 E-value: 1.82e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2592 LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAvlglSVL 2671
Cdd:cd05932 7 FTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSES----KAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2672 ASGDLpgqefewmrlddDSVAAEIAAVPAGPIT------DAER--------------LGEVT---AANLAYVIYTSGSTG 2728
Cdd:cd05932 83 FVGKL------------DDWKAMAPGVPEGLISislpppSAANcqyqwddliaqhppLEERPtrfPEQLATLIYTSGTTG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2729 RPKGVAVTHSGLANFARQESDRLNAGDNPvvlgfaspsfdaSVLEYL-LATVNEGTLAYRPSEAVG-----GEVLERFIA 2802
Cdd:cd05932 151 QPKGVMLTFGSFAWAAQAGIEHIGTEEND------------RMLSYLpLAHVTERVFVEGGSLYGGvlvafAESLDTFVE 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2803 E---HGATHTFLTP--------SVLSTMDPTAVPSL-----------------------RVIAAGGEAVPQPIVDrW--A 2846
Cdd:cd05932 219 DvqrARPTLFFSVPrlwtkfqqGVQDKIPQQKLNLLlkipvvnslvkrkvlkglgldqcRLAGCGSAPVPPALLE-WyrS 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2847 PATELHNLYGPTETtigITISSAMRPGDPVR--LGGPIGGVDLMVLDErlrpvpvgmpGELYVAGGALSRGYLDRSGLTA 2924
Cdd:cd05932 298 LGLNILEAYGMTEN---FAYSHLNYPGRDKIgtVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATA 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2925 ERFTANPYgtagqrmYRTGDVVRWTPDtdtGGLTLeyTGRSDDQVKL-RGLRIELGEIEAVLAEHDAVESAVVLGVGGSV 3003
Cdd:cd05932 365 EAFTADGF-------LRTGDKGELDAD---GNLTI--TGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVIGSGLPA 432
|
490 500 510
....*....|....*....|....*....|
gi 1827387616 3004 ATALAayivpVDGAVEVSELKAFAGGRLPA 3033
Cdd:cd05932 433 PLALV-----VLSEEARLRADAFARAELEA 457
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
4-446 |
1.92e-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: 75.47 E-value: 1.92e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGghfvpldeqlpvdrarymvrtAGVRLVVVTSDGE 83
Cdd:cd05940 7 AELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIG---------------------AVAALINYNLRGE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 AEArsrfddivdvHVLDISSPGDADLDeeefagptrpanAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARD 163
Cdd:cd05940 66 SLA----------HCLNVSSAKHLVVD------------AALYIYTSGTTGLPKAAIISHRRAWRGGAFFAGSGGALPSD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 164 VFLYKAPITFDVSVreIFLP---IAIGATLVIaepGRHGDPVHLADLIRRHGVTVIHFVpamlaafnevlgagvGELT-- 238
Cdd:cd05940 124 VLYTCLPLYHSTAL--IVGWsacLASGATLVI---RKKFSASNFWDDIRKYQATIFQYI---------------GELCry 183
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 239 -------------SLRLIQtgGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVT--------------IHRVTQDDRV 291
Cdd:cd05940 184 llnqppkpterkhKVRMIF--GNGLRPDIWEEFKERFGVPRIAEFYAATEGNSGFInffgkpgaigrnpsLLRKVAPLAL 261
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 292 IPI----GTPTRRVSARVldaalREVPIGVPGEL--YLGGVQLARGYAGrPDLTAERFVADPFgEPGARLYRTGDRARWN 365
Cdd:cd05940 262 VKYdlesGEPIRDAEGRC-----IKVPRGEPGLLisRINPLEPFDGYTD-PAATEKKILRDVF-KKGDAWFNTGDLMRLD 334
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 366 RDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVV-----DGPGGQQLVGYLAPADVDVDTVAATTAELL 440
Cdd:cd05940 335 GEGFWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYGVqvpgtDGRAGMAAIVLQPNEEFDLSALAAHLEKNL 414
|
....*.
gi 1827387616 441 PEYMRP 446
Cdd:cd05940 415 PGYARP 420
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
4-400 |
2.05e-13 |
|
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: 75.86 E-value: 2.05e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDGe 83
Cdd:cd17640 9 KDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESVALVVENDS- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 aearsrfDDIvdvhvldisspgdadldeeefagptrpanaAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARD 163
Cdd:cd17640 88 -------DDL------------------------------ATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPGD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 164 VFLYKAPI--TFDVSVrEIFLpIAIGATLViaepgrHGDPVHLADLIRRHGVTVIHFVPAMLAAFNE------------- 228
Cdd:cd17640 131 RFLSILPIwhSYERSA-EYFI-FACGCSQA------YTSIRTLKDDLKRVKPHYIVSVPRLWESLYSgiqkqvsksspik 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 229 --VLGAGV--GELtslRLIQTGGEALTPPVarDLMVRLPGTRLQNQYGPAEASIVVTIHRVtqdDRVI--PIGTPTRRVS 302
Cdd:cd17640 203 qfLFLFFLsgGIF---KFGISGGGALPPHV--DTFFEAIGIEVLNGYGLTETSPVVSARRL---KCNVrgSVGRPLPGTE 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 303 ARVLDAALREV-PIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRT-DFQV 380
Cdd:cd17640 275 IKIVDPEGNVVlPPGEKGIVWVRGPQVMKGYYKNPEATSKVLDSDGW-------FNTGDLGWLTCGGELVLTGRAkDTIV 347
|
410 420
....*....|....*....|
gi 1827387616 381 KLRGQRLELGEVEAALAAAP 400
Cdd:cd17640 348 LSNGENVEPQPIEEALMRSP 367
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
2570-3066 |
2.06e-13 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 75.99 E-value: 2.06e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2570 LFRAAARRApdHVAVVDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPD 2649
Cdd:PLN02860 13 LTRLATLRG--NAVVTISGNRRRTGHEFVDGVLSLAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNYR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2650 YPAERVASMIE---------DSGAVLGLSVLASGDLPgqEFEW-MRLDDDSVAAEIAAVPAGPITDAERLGEVTA----- 2714
Cdd:PLN02860 91 WSFEEAKSAMLlvrpvmlvtDETCSSWYEELQNDRLP--SLMWqVFLESPSSSVFIFLNSFLTTEMLKQRALGTTeldya 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2715 ---ANLAYVIYTSGSTGRPKGVAVTHSG-----LANFA---RQESD-------------------RLNAGDNPVVLgfas 2764
Cdd:PLN02860 169 wapDDAVLICFTSGTTGRPKGVTISHSAlivqsLAKIAivgYGEDDvylhtaplchigglssalaMLMVGACHVLL---- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2765 PSFDASVleyllatvnegtlayrpseavggeVLErFIAEHGATHTFLTPSVL--------STMDPTAVPSLRVIAAGGEA 2836
Cdd:PLN02860 245 PKFDAKA------------------------ALQ-AIKQHNVTSMITVPAMMadlisltrKSMTWKVFPSVRKILNGGGS 299
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2837 VPQPIVD---RWAPATELHNLYGPTET----------------------TIGITISSAMRPGDPVRLGGPIGGVDLMV-L 2890
Cdd:PLN02860 300 LSSRLLPdakKLFPNAKLFSAYGMTEAcssltfmtlhdptlespkqtlqTVNQTKSSSVHQPQGVCVGKPAPHVELKIgL 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2891 DERLRpvpvgmPGELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDvVRWTpdTDTGGLTLeyTGRSDDQVK 2970
Cdd:PLN02860 380 DESSR------VGRILTRGPHVMLGYWGQNSETASVLSNDGW-------LDTGD-IGWI--DKAGNLWL--IGRSNDRIK 441
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2971 LRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPV-DGAVEVSELKAFAGG----------------RLPA 3033
Cdd:PLN02860 442 TGGENVYPEEVEAVLSQHPGVASVVVVGVPDSRLTEMVVACVRLrDGWIWSDNEKENAKKnltlssetlrhhcrekNLSR 521
|
570 580 590
....*....|....*....|....*....|....
gi 1827387616 3034 YMVPSSFTVI-DELPLTPVGKLDKRALPEPVLEA 3066
Cdd:PLN02860 522 FKIPKLFVQWrKPFPLTTTGKIRRDEVRREVLSH 555
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
125-468 |
2.23e-13 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 76.33 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 125 FTLFTSGSTGRPKAVVITHRGIANRLAadieqydLTARDVFLYKAPITF----DVS-------VreIFLPIAIGATLVIA 193
Cdd:PRK00174 249 FILYTSGSTGKPKGVLHTTGGYLVYAA-------MTMKYVFDYKDGDVYwctaDVGwvtghsyI--VYGPLANGATTLMF 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 194 E-------PGRHGDpvhladLIRRHGVTVIHFVPAMLAAFnevLGAGVGE-----LTSLRLIQTGGEALTPP-------- 253
Cdd:PRK00174 320 EgvpnypdPGRFWE------VIDKHKVTIFYTAPTAIRAL---MKEGDEHpkkydLSSLRLLGSVGEPINPEawewyykv 390
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 254 VARDlmvRLPgtrlqnqygpaeasIVVTI-------HRVTQDDRVIPI--GTPTRR---VSARVLDAALREVPIGVPGEL 321
Cdd:PRK00174 391 VGGE---RCP--------------IVDTWwqtetggIMITPLPGATPLkpGSATRPlpgIQPAVVDEEGNPLEGGEGGNL 453
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 322 YL-----GgvqLARGYAGRPdltaERFVADPFGE-PGarLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAA 395
Cdd:PRK00174 454 VIkdpwpG---MMRTIYGDH----ERFVKTYFSTfKG--MYFTGDGARRDEDGYYWITGRVDDVLNVSGHRLGTAEIESA 524
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 396 LAAAPGVlhAAAAVVDGP---GGQQLVGYlapadVDVDTVAATTAELLPEyMRpsAWVR--------------LDAMPLS 458
Cdd:PRK00174 525 LVAHPKV--AEAAVVGRPddiKGQGIYAF-----VTLKGGEEPSDELRKE-LR--NWVRkeigpiakpdviqfAPGLPKT 594
|
410
....*....|
gi 1827387616 459 RSGKVDRRLL 468
Cdd:PRK00174 595 RSGKIMRRIL 604
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
119-464 |
2.40e-13 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 76.54 E-value: 2.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 119 RPANAAFTLFTSGSTGRPKAVVITHRGI-ANR--LAADIeqyDLTARDvflykapITFDVsvreifLPI--AIGATLVIA 193
Cdd:PRK06814 791 DPDDPAVILFTSGSEGTPKGVVLSHRNLlANRaqVAARI---DFSPED-------KVFNA------LPVfhSFGLTGGLV 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 194 EPGRHGDPVHL----------ADLIRRHGVTVIHFVPAMLAAFNEVlgAGVGELTSLRLIQTGGEALTPPVARDLMVRLp 263
Cdd:PRK06814 855 LPLLSGVKVFLypsplhyriiPELIYDTNATILFGTDTFLNGYARY--AHPYDFRSLRYVFAGAEKVKEETRQTWMEKF- 931
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 264 GTRLQNQYGPAEASivvtihrvtqddRVIPIGTPTRRVSARV------LDAALREVPiGVP--GELYLGGVQLARGYagr 335
Cdd:PRK06814 932 GIRILEGYGVTETA------------PVIALNTPMHNKAGTVgrllpgIEYRLEPVP-GIDegGRLFVRGPNVMLGY--- 995
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 336 pdLTAER-FVADPfgePGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAA-PGVLHAAAAVVDGP 413
Cdd:PRK06814 996 --LRAENpGVLEP---PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELwPDALHAAVSIPDAR 1070
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 414 GGQQLVGYLAPADVDVDTVAA-TTAELLPEYMRPSAWVRLDAMPLSRSGKVD 464
Cdd:PRK06814 1071 KGERIILLTTASDATRAAFLAhAKAAGASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
1-468 |
3.08e-13 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 75.43 E-value: 3.08e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTS 80
Cdd:PRK13390 25 VSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADYIVGDSGARVLVASA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 81 ---------DGEAEARSRFDDIVDvhvldisspGDADLDEE-EFAGP--TRPANAAFTLFTSGSTGRPKavvithrGIAN 148
Cdd:PRK13390 105 aldglaakvGADLPLRLSFGGEID---------GFGSFEAAlAGAGPrlTEQPCGAVMLYSSGTTGFPK-------GIQP 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 149 RLAA-DIEQ------------YDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAepgRHGDPVHLADLIRRHGVTV 215
Cdd:PRK13390 169 DLPGrDVDApgdpivaiarafYDISESDIYYSSAPIYHAAPLRWCSMVHALGGTVVLA---KRFDAQATLGHVERYRITV 245
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 216 IHFVPAMLAAFNEvLGAGVG---ELTSLRLIqTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIhrvTQDDRVI 292
Cdd:PRK13390 246 TQMVPTMFVRLLK-LDADVRtryDVSSLRAV-IHAAAPCPVDVKHAMIDWLGPIVYEYYSSTEAHGMTFI---DSPDWLA 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 293 PIGTPTRRV--SARVLDAALREVPIGVPGELYLGGVQLARGYAGRPDLTAE-RFVADPFgepgarLYRTGDRARWNRDGE 369
Cdd:PRK13390 321 HPGSVGRSVlgDLHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPF------WTTVGDLGSVDEDGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 370 IEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGP--GGQ-----QLVGYLAPADVDVDTVAATTAELLPE 442
Cdd:PRK13390 395 LYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDPemGEQvkaviQLVEGIRGSDELARELIDYTRSRIAH 474
|
490 500
....*....|....*....|....*.
gi 1827387616 443 YMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK13390 475 YKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
2861-3144 |
3.78e-13 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 72.86 E-value: 3.78e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2861 TIGITISSAMRPGDPVRLGGPIGGVDLMVLdeRLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRmY 2940
Cdd:COG3433 1 IAIATPPPAPPTPDEPPPVIPPAIVQARAL--LLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYPA-Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2941 RTGDVVRWTPDTDTGGLTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPVDGAVEV 3020
Cdd:COG3433 78 PGRQADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAALDGLA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3021 SELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALP--EPVLEAGEYVAPATGTERT-----IADVAAGVLNIDAG 3093
Cdd:COG3433 158 AAAALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPalAAAEALLAAASPAPALETAlteeeLRADVAELLGVDPE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 3094 LVSATSSFFELGGDSLSAARLAARLSdQLGVAVSVRDVFESGSIRALAETV 3144
Cdd:COG3433 238 EIDPDDNLFDLGLDSIRLMQLVERWR-KAGLDVSFADLAEHPTLAAWWALL 287
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
2141-2535 |
4.28e-13 |
|
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: 74.44 E-value: 4.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2141 LSLTGDVDPGRLRSALSELLARQRVLRSGFvrlpSGAAVTVVPAEVTVPWSVIDLRAEDAAslDSRVEEVLATERTNPFD 2220
Cdd:cd19546 33 LRLRGRLDRDALEAALGDVAARHEILRTTF----PGDGGDVHQRILDADAARPELPVVPAT--EEELPALLADRAAHLFD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2221 MAKPPLIRVVLVEHGDGAE-LVVTNHHLLIDGWSSPLVLADLLSLYatGQTFTGSLPGTS--GRDFADHA-------RAV 2290
Cdd:cd19546 107 LTRETPWRCTLFALSDTEHvLLLVVHRIAADDESLDVLVRDLAAAY--GARREGRAPERAplPLQFADYAlwerellAGE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2291 ATADVEAG--IAAWREVLAPVtEPTLVAPGHEPSADAPPRDH---QFSIDVKVTERLEALARNNSTTMATVVQFAWAMFL 2365
Cdd:cd19546 185 DDRDSLIGdqIAYWRDALAGA-PDELELPTDRPRPVLPSRRAgavPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2366 SRLTGTRTVTFAeTVSGRSPDIEGMESMVGMFINTIPAVVDVNPDATVVDVLTAVQNDKVKVLDHQQIGLPRLVAQTGLP 2445
Cdd:cd19546 264 TRLGAGTDVTVG-TVLPRDDEEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELLALP 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2446 ALFDTLAVYE-SFPVNVDSVAGIDASSAGGLK--LVGAKTsDATHYPLNLSAS-RRGAE-----LALKLKYLPTAFAPEQ 2516
Cdd:cd19546 343 PSADRHPVFQvALDVRDDDNDPWDAPELPGLRtsPVPLGT-EAMELDLSLALTeRRNDDgdpdgLDGSLRYAADLFDRAT 421
|
410
....*....|....*....
gi 1827387616 2517 VAVFADVLTGLLGAIADHP 2535
Cdd:cd19546 422 AAALARRLVRVLEQVAADP 440
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
123-468 |
4.99e-13 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 75.07 E-value: 4.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 123 AAFTLFTSGSTGRPKAVVITHRGIANRLAADI-EQYDLTARDVFLYKAPITFDVSV-REIFLPIAIGATLVIAEPgrhgd 200
Cdd:PRK06060 147 LAYATYTSGTTGPPKAAIHRHADPLTFVDAMCrKALRLTPEDTGLCSARMYFAYGLgNSVWFPLATGGSAVINSA----- 221
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 201 PVH---LADLIRRHGVTVIHFVPAMlaaFNEVLGA-GVGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEA 276
Cdd:PRK06060 222 PVTpeaAAILSARFGPSVLYGVPNF---FARVIDScSPDSFRSLRCVVSAGEALELGLAERLMEFFGGIPILDGIGSTEV 298
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 277 SIVVTIHRVtQDDRVIPIGTPTRRVSARVLDAALREVPIGVPGELYLGGVQLARGYAGRPdltaerfvaDPFGEPGARLy 356
Cdd:PRK06060 299 GQTFVSNRV-DEWRLGTLGRVLPPYEIRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRP---------DSPVANEGWL- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 357 RTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAA-AAVVDGPGGQQLVGYLAPAD---VDVDTV 432
Cdd:PRK06060 368 DTRDRVCIDSDGWVTYRCRADDTEVIGGVNVDPREVERLIIEDEAVAEAAvVAVRESTGASTLQAFLVATSgatIDGSVM 447
|
330 340 350
....*....|....*....|....*....|....*....
gi 1827387616 433 AATTAELLPE---YMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK06060 448 RDLHRGLLNRlsaFKVPHRFAVVDRLPRTPNGKLVRGAL 486
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1039-1530 |
5.17e-13 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 74.64 E-value: 5.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1039 LIDVLAqRDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVgmerSIGSV----LATWGVIKSGAAyv 1114
Cdd:PRK10946 27 LTDILT-RHAASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALV----QLGNVaefyITFFALLKLGVA-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1115 PVDP----------AYpADRI--AYMLEDSGATVGITDASTRARLGESSCEWVDLADLEAEAESGDDITDTERNGSVRLT 1182
Cdd:PRK10946 100 PVNAlfshqrselnAY-ASQIepALLIADRQHALFSDDDFLNTLVAEHSSLRVVLLLNDDGEHSLDDAINHPAEDFTATP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1183 N----LAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPedepDTRILhVASPSfdASMFEMA-----WAIPAGH 1253
Cdd:PRK10946 179 SpadeVAFFQLSGGSTGTPKLIPRTHNDYYYSVRRSVEICGFTP----QTRYL-CALPA--AHNYPMSspgalGVFLAGG 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1254 TLVIAPqadfagDALAT----VLERDEVTDMIITPSVL-----ATVDPERAQYVRNL---ATGGEacppelveRWSER-G 1320
Cdd:PRK10946 252 TVVLAP------DPSATlcfpLIEKHQVNVTALVPPAVslwlqAIAEGGSRAQLASLkllQVGGA--------RLSETlA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1321 RRI---FNC-----YGPTEATVWATRSR-------MTAGKPVTigkPVDgfTVRVLDGRLHEVPQGVVGELYLSTAGLAR 1385
Cdd:PRK10946 318 RRIpaeLGCqlqqvFGMAEGLVNYTRLDdsderifTTQGRPMS---PDD--EVWVADADGNPLPQGEVGRLMTRGPYTFR 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1386 GYLGRPGQTAVSFVADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGV 1465
Cdd:PRK10946 393 GYYKSPQHNASAFDANGF-------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSM 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 1466 ESTRGGRKHtevVAYLVAK-PGATIDSAAVLDEaaQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK10946 466 EDELMGEKS---CAFLVVKePLKAVQLRRFLRE--QGIAEFKLPDRVECVDSLPLTAVGKVDKKQL 526
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
2560-3065 |
6.09e-13 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 74.63 E-value: 6.09e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2560 PATDPVTLAELFRAAARRAPDHVAVVDGA-GARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAK 2638
Cdd:PLN02330 23 PVPDKLTLPDFVLQDAELYADKVAFVEAVtGKAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2639 TGGAYVPIDPDYPAERVASMIEDSGAVLGLS-VLASGDLPGQEFEWMRLDDDSVAAEI-------AAVPAGPITDAErlg 2710
Cdd:PLN02330 103 AGGVFSGANPTALESEIKKQAEAAGAKLIVTnDTNYGKVKGLGLPVIVLGEEKIEGAVnwkelleAADRAGDTSDNE--- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2711 EVTAANLAYVIYTSGSTGRPKGVAVTHSGL-ANFArqeSDRLNAGDNPV----VLGFAsPSFDA-SVLEYLLATV-NEGT 2783
Cdd:PLN02330 180 EILQTDLCALPFSSGTTGISKGVMLTHRNLvANLC---SSLFSVGPEMIgqvvTLGLI-PFFHIyGITGICCATLrNKGK 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2784 LAyrpseAVGGEVLERF---IAEHGATHTFLTPSVLSTM---------DPTAVPSLRVIAAGGEAVPQPIV--DRWAPAT 2849
Cdd:PLN02330 256 VV-----VMSRFELRTFlnaLITQEVSFAPIVPPIILNLvknpiveefDLSKLKLQAIMTAAAPLAPELLTafEAKFPGV 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2850 ELHNLYGPTETTIgITISSamrpGDPVR---------LGGPIGGVDLMVLD-ERLRPVPVGMPGELYVAGGALSRGYLDR 2919
Cdd:PLN02330 331 QVQEAYGLTEHSC-ITLTH----GDPEKghgiakknsVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNN 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2920 SGLTAERFTANPYgtagqrmYRTGDVVRWTPDTDtggltLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV 2999
Cdd:PLN02330 406 KEETDRTIDEDGW-------LHTGDIGYIDDDGD-----IFIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPL 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 3000 GGSVATALAAYIVPVDGAVEVSE--LKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALPEPVLE 3065
Cdd:PLN02330 474 PDEEAGEIPAACVVINPKAKESEedILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKMLS 541
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
1066-1529 |
7.38e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 74.26 E-value: 7.38e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1066 EFETRTNAIARALLARGVSPEDVVAV--GMERSIG-SVLATWgviKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDAS 1142
Cdd:PRK07768 34 EVHERARRIAGGLAAAGVGPGDAVAVlaGAPVEIApTAQGLW---MRGASLTMLHQPTPRTDLAVWAEDTLRVIGMIGAK 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1143 T----------RARLGESSCEWVDLADLEAeAESGDDITDTERNgsvrltnLAYLIYTSGSTGRPKAVGVSHTgivDFVN 1212
Cdd:PRK07768 111 AvvvgepflaaAPVLEEKGIRVLTVADLLA-ADPIDPVETGEDD-------LALMQLTSGSTGSPKAVQITHG---NLYA 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1213 SLAKITTGTPEDEPDTRILHVASPSFDASMFEmAWAIP--AGHTLVIAPQADFAGDAL--ATVLERDEVTdMIITP---- 1284
Cdd:PRK07768 180 NAEAMFVAAEFDVETDVMVSWLPLFHDMGMVG-FLTVPmyFGAELVKVTPMDFLRDPLlwAELISKYRGT-MTAAPnfay 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1285 SVLA---TVDPERAQY----VRNLATGGEACPPELVERWSERGRR-------IFNCYGPTEATVWATRSRMTAG------ 1344
Cdd:PRK07768 258 ALLArrlRRQAKPGAFdlssLRFALNGAEPIDPADVEDLLDAGARfglrpeaILPAYGMAEATLAVSFSPCGAGlvvdev 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1345 ---------------KP-----VTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLgrpgqTAVSFVA--DP 1402
Cdd:PRK07768 338 dadllaalrravpatKGntrrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYL-----TMDGFIPaqDA 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1403 FGepgarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKHTEVVAylv 1482
Cdd:PRK07768 413 DG-----WLDTGDLGYLTEEGEVVVCGRVKDVIIMAGRNIYPTDIERAAARVEGVRPGNAVAVRLDAGHSREGFAVA--- 484
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1483 akpgatIDSAAVLDEAA----QHLAAHMV-------PSQAIVID--EIPLTPAGKLDRAA 1529
Cdd:PRK07768 485 ------VESNAFEDPAEvrriRHQVAHEVvaevgvrPRNVVVLGpgSIPKTPSGKLRRAN 538
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
2146-2430 |
9.13e-13 |
|
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the Condensation-domain family; Cyc (heterocyclization) domains catalyze two separate reactions in the creation of heterocyclized peptide products in nonribosomal peptide synthesis: amide bond formation followed by intramolecular cyclodehydration between a Cys, Ser, or Thr side chain and a carbonyl carbon on the peptide backbone to form a thiazoline, oxazoline, or methyloxazoline ring. Cyc-domains are homologous to standard NRPS Condensation (C) domains. C-domains typically have a conserved HHxxxD motif at the active site; Cyc-domains have an alternative, conserved DxxxxD active site motif, mutation of the aspartate residues in this motif can abolish or diminish condensation activity. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains such as the LCL-type which catalyzes peptide bond formation between two L-amino acids, the DCL-type which links an L-amino acid to the D-amino acid at the end of a growing peptide, starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and Cyc-domains. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain.
Pssm-ID: 380458 [Multi-domain] Cd Length: 423 Bit Score: 73.29 E-value: 9.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2146 DVDPGRLRSALSELLARQRVLRSGFvrLPSGaaVTVVPAEVTVP-WSVIDLRAEDAASLDSRVEEV---LATERtnpFDM 2221
Cdd:cd19535 36 DLDPDRLERAWNKLIARHPMLRAVF--LDDG--TQQILPEVPWYgITVHDLRGLSEEEAEAALEELrerLSHRV---LDV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2222 AKPPLIRVVLVEHGDGAELVVTNHHLLI-DGWSSPLVLADLLSLYATGQTftgSLPgTSGRDFAD---HARAVATADVEA 2297
Cdd:cd19535 109 ERGPLFDIRLSLLPEGRTRLHLSIDLLVaDALSLQILLRELAALYEDPGE---PLP-PLELSFRDyllAEQALRETAYER 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2298 GIAAWREVLapvtePTLvapghePSADAPP--------RDHQFS-----IDVKVTERLEALARNNSTTMATVVQFAWAMF 2364
Cdd:cd19535 185 ARAYWQERL-----PTL------PPAPQLPlakdpeeiKEPRFTrrehrLSAEQWQRLKERARQHGVTPSMVLLTAYAEV 253
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 2365 LSRLTGTRTVTFAETVSGRSPDIEGMESMVGMFINTIPAVVDVNPDATVVDVLTAVQNDKVKVLDH 2430
Cdd:cd19535 254 LARWSGQPRFLLNLTLFNRLPLHPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDH 319
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
118-418 |
9.14e-13 |
|
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: 73.37 E-value: 9.14e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 118 TRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFL-YKAPITFDVSVREIFLPIAIGATLVIAEPG 196
Cdd:cd05974 82 THADDPMLLYFTSGTTSKPKLVEHTHRSYPVGHLSTMYWIGLKPGDVHWnISSPGWAKHAWSCFFAPWNAGATVFLFNYA 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 197 RHgDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGelTSLRLIQTGGEALTPPVArDLMVRLPGTRLQNQYGPAEA 276
Cdd:cd05974 162 RF-DAKRVLAALVRYGVTTLCAPPTVWRMLIQQDLASFD--VKLREVVGAGEPLNPEVI-EQVRRAWGLTIRDGYGQTET 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 277 SIVVTiHRVTQDDRVIPIGTPTRRVSARVLDAALREVPigvPGELYLG-----GVQLARGYAGRPDLTAERFvadpfgep 351
Cdd:cd05974 238 TALVG-NSPGQPVKAGSMGRPLPGYRVALLDPDGAPAT---EGEVALDlgdtrPVGLMKGYAGDPDKTAHAM-------- 305
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 352 GARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGPGGQQL 418
Cdd:cd05974 306 RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSSDYRISPFELESVLIEHPAV--AEAAVVPSPDPVRL 370
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
124-375 |
9.86e-13 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 73.68 E-value: 9.86e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 124 AFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPITFDVSVreiflpIAIGATLVIAepGRHGDPVH 203
Cdd:cd05908 109 AFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGL------IAFHLAPLIA--GMNQYLMP 180
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 204 LADLIRR----------HGVTVI---HFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQ-- 268
Cdd:cd05908 181 TRLFIRRpilwlkkaseHKATIVsspNFGYKYFLKTLKPEKANDWDLSSIRMILNGAEPIDYELCHEFLDHMSKYGLKrn 260
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 269 ---NQYGPAEASI------------VVTIHR-----------VTQDD----RVIPIGTPTRRVSARVLDAALREVPIGVP 318
Cdd:cd05908 261 ailPVYGLAEASVgaslpkaqspfkTITLGRrhvthgepepeVDKKDseclTFVEVGKPIDETDIRICDEDNKILPDGYI 340
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 319 GELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRArWNRDGEIEYLGR 375
Cdd:cd05908 341 GHIQIRGKNVTPGYYNNPEATAKVFTDDGW-------LKTGDLG-FIRNGRLVITGR 389
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
487-545 |
1.81e-12 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 64.51 E-value: 1.81e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 487 ETVAGLFAELLGV--ERVGVTDSFFDIGGSSLSAARIAARVSKELGVDVSVRDVFESPSVR 545
Cdd:pfam00550 1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLA 61
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
117-440 |
1.95e-12 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 73.01 E-value: 1.95e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 117 PTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYkapiTFDVSVreiFLPIAIGATLVIAE-- 194
Cdd:PRK09274 170 DLAPDDMAAILFTSGSTGTPKGVVYTHGMFEAQIEALREDYGIEPGEIDLP----TFPLFA---LFGPALGMTSVIPDmd 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 195 PGRHG--DPVHLADLIRRHGVTVIHFVPAMLaafNEVLGAGVGE---LTSLRLIQTGGealtPPVARDLMVRL-----PG 264
Cdd:PRK09274 243 PTRPAtvDPAKLFAAIERYGVTNLFGSPALL---ERLGRYGEANgikLPSLRRVISAG----APVPIAVIERFramlpPD 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 265 TRLQNQYGPAEASIVVTI---------HRVTQDDRVIPIGTPTRRVSARVL---DAAL------REVPIGVPGELYLGGV 326
Cdd:PRK09274 316 AEILTPYGATEALPISSIesreilfatRAATDNGAGICVGRPVDGVEVRIIaisDAPIpewddaLRLATGEIGEIVVAGP 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 327 QLARGYAGRPDLTAERFVADPfgEPGARlYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAA 406
Cdd:PRK09274 396 MVTRSYYNRPEATRLAKIPDG--QGDVW-HRMGDLGYLDAQGRLWFCGRKAHRVETAGGTLYTIPCERIFNTHPGVKRSA 472
|
330 340 350
....*....|....*....|....*....|....
gi 1827387616 407 AAVVDGPGGQQLVGYLAPADVDVDTVAATTAELL 440
Cdd:PRK09274 473 LVGVGVPGAQRPVLCVELEPGVACSKSALYQELR 506
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
3071-3144 |
2.06e-12 |
|
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the Pathway/BioSystem: Fatty acid biosynthesis
Pssm-ID: 440006 [Multi-domain] Cd Length: 80 Bit Score: 64.87 E-value: 2.06e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 3071 APATGTERTIADVAAGVLNIDAGLVSATSSFF-ELGGDSLSAARLAARLSDQLGVAVSVRDVFESGSIRALAETV 3144
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVDPEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYL 75
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
2564-2948 |
2.68e-12 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 72.60 E-value: 2.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2564 PVTLAELFRAAARRAPDHVAVV----DGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRS---AQL-LTAIWA 2635
Cdd:PRK08180 38 PRRLTDRLVHWAQEAPDRVFLAergaDGGWRRLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSiehALLaLAAMYA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2636 vaktGGAYVPIDPDYPA-----ERVASMIEdsgaVL--GLSVLASGDLPGQEFEWMRLDDDSVAAEIAAVPAGPIT---- 2704
Cdd:PRK08180 118 ----GVPYAPVSPAYSLvsqdfGKLRHVLE----LLtpGLVFADDGAAFARALAAVVPADVEVVAVRGAVPGRAATpfaa 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2705 --DAERLGEVTAAN-------LAYVIYTSGSTGRPKGVAVTHSGL-ANFA--RQESDRLnAGDNPVVLGFA--SPSFDAS 2770
Cdd:PRK08180 190 llATPPTAAVDAAHaavgpdtIAKFLFTSGSTGLPKAVINTHRMLcANQQmlAQTFPFL-AEEPPVLVDWLpwNHTFGGN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2771 -VLEYLLAtvNEGTLaY----RPSEAVGGEVLERfiaehgathtfltpsvLSTMDPTA---VPS---------------- 2826
Cdd:PRK08180 269 hNLGIVLY--NGGTL-YiddgKPTPGGFDETLRN----------------LREISPTVyfnVPKgwemlvpalerdaalr 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2827 ------LRVIAAGGEAVPQPIVDRWAPATELH--------NLYGPTETTIGITISS--AMRPGDpvrLGGPIGGVDlmvl 2890
Cdd:PRK08180 330 rrffsrLKLLFYAGAALSQDVWDRLDRVAEATcgerirmmTGLGMTETAPSATFTTgpLSRAGN---IGLPAPGCE---- 402
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 2891 derLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVRW 2948
Cdd:PRK08180 403 ---VKLVPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEEGY-------YRSGDAVRF 450
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
2980-3053 |
3.13e-12 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 64.10 E-value: 3.13e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 2980 EIEAVLAEHDAVESAVVLGVGGSV-ATALAAYIVPVDGAVEVS-ELKAFAGGRLPAYMVPSSFTVIDELPLTPVGK 3053
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELkGEAPVAFVVLKPGVELLEeELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1050-1530 |
3.89e-12 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 71.94 E-value: 3.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALI--CDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAY 1127
Cdd:PLN02246 37 SDRPCLIdgATGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEIAK 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1128 MLEDSGATVGITDAStrarlgessceWVD-LADLEAEaesgDDIT----DTERNGSVRLTNL------------------ 1184
Cdd:PLN02246 117 QAKASGAKLIITQSC-----------YVDkLKGLAED----DGVTvvtiDDPPEGCLHFSELtqadenelpeveispddv 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1185 AYLIYTSGSTGRPKAVGVSHTGIvdfVNSLAKITTG-------TPEDepdtRILHVaspsfdASMFE-------MAWAIP 1250
Cdd:PLN02246 182 VALPYSSGTTGLPKGVMLTHKGL---VTSVAQQVDGenpnlyfHSDD----VILCV------LPMFHiyslnsvLLCGLR 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1251 AGHTLVIAPQADFAgdALATVLERDEVT-DMIITPSVLATV-DPERAQY----VRNLATGGEACPPELVERWSER--GRR 1322
Cdd:PLN02246 249 VGAAILIMPKFEIG--ALLELIQRHKVTiAPFVPPIVLAIAkSPVVEKYdlssIRMVLSGAAPLGKELEDAFRAKlpNAV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1323 IFNCYGPTEATVWATRSRMTAGKPVTI-----GKPVDGFTVRVLDGRLHE-VPQGVVGELYLSTAGLARGYLGRPGQTAV 1396
Cdd:PLN02246 327 LGQGYGMTEAGPVLAMCLAFAKEPFPVksgscGTVVRNAELKIVDPETGAsLPRNQPGEICIRGPQIMKGYLNDPEATAN 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1397 SFVADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhtE 1476
Cdd:PLN02246 407 TIDKDGW-------LHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAG----E 475
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 1477 V-VAYLVAKPGATIDSaavlDEAAQHLAAHMVPSQAI----VIDEIPLTPAGKLDRAAL 1530
Cdd:PLN02246 476 VpVAFVVRSNGSEITE----DEIKQFVAKQVVFYKRIhkvfFVDSIPKAPSGKILRKDL 530
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
2-429 |
4.67e-12 |
|
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: 71.32 E-value: 4.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTsd 81
Cdd:cd05914 9 TYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS-- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 82 geaearsrfddivdvhvldisspgdadlDEEEFAgptrpanaaFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYDLTA 161
Cdd:cd05914 87 ----------------------------DEDDVA---------LINYTSGTTGNSKGVMLTYRNIVSNVDGVKEVVLLGK 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 162 RDVFL------YKAPITFDvsvreIFLPIAIGATLVIAEPgrhgDPVHLADLIRRHGVTVIHFVPAML------------ 223
Cdd:cd05914 130 GDKILsilplhHIYPLTFT-----LLLPLLNGAHVVFLDK----IPSAKIIALAFAQVTPTLGVPVPLviekifkmdiip 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 224 ----------------------AAFNEVLGAGVGeltSLRLIQTGGEALTPPVARDLmvRLPGTRLQNQYGPAEASIVVT 281
Cdd:cd05914 201 kltlkkfkfklakkinnrkirkLAFKKVHEAFGG---NIKEFVIGGAKINPDVEEFL--RTIGFPYTIGYGMTETAPIIS 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 282 IHRvTQDDRVIPIGTPTRRVSARVLDaalrEVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDR 361
Cdd:cd05914 276 YSP-PNRIRLGSAGKVIDGVEVRIDS----PDPATGEGEIIVRGPNVMKGYYKNPEATAEAFDKDGW-------FHTGDL 343
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 362 ARWNRDGEIEYLGRT-DFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGPGgqQLVGYLAPADVDV 429
Cdd:cd05914 344 GKIDAEGYLYIRGRKkEMIVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKL--VALAYIDPDFLDV 410
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
2562-3073 |
6.06e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 71.92 E-value: 6.06e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2562 TDPVTLAELFRAAARRAPDHVAVVDGAGARLTYRELDEASDRLARwLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGg 2641
Cdd:PRK06814 629 YDRTLFEALIEAAKIHGFKKLAVEDPVNGPLTYRKLLTGAFVLGR-KLKKNTPPGENVGVMLPNANGAAVTFFALQSAG- 706
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2642 ayvpidpdypaeRVASMIE-DSGAVlglSVLASGDLPG-------QEF-EWMRLDDdsVAAEIAA---------VPAGpI 2703
Cdd:PRK06814 707 ------------RVPAMINfSAGIA---NILSACKAAQvktvltsRAFiEKARLGP--LIEALEFgiriiyledVRAQ-I 768
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2704 TDAERLGEVTAANL-------------AYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLG----FASPS 2766
Cdd:PRK06814 769 GLADKIKGLLAGRFplvyfcnrdpddpAVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPEDKVFNalpvFHSFG 848
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2767 FDASVLEYLLATVN----EGTLAYRpseavggeVLERFIAEHGATHTFLTPSVLSTMDPTAVP----SLRVIAAGGEAVP 2838
Cdd:PRK06814 849 LTGGLVLPLLSGVKvflyPSPLHYR--------IIPELIYDTNATILFGTDTFLNGYARYAHPydfrSLRYVFAGAEKVK 920
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2839 QPIVDRWAPATELHNL--YGPTETTIGITISSAM--RPGDPVRLggpiggvdLMVLDERLRPVP-VGMPGELYVAGGALS 2913
Cdd:PRK06814 921 EETRQTWMEKFGIRILegYGVTETAPVIALNTPMhnKAGTVGRL--------LPGIEYRLEPVPgIDEGGRLFVRGPNVM 992
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2914 RGYLDrsgltaerfTANP--YGTAGQRMYRTGDVVrwTPDTDtGGLTLEytGRSDDQVKLRGLRIELGEIEAVLAE--HD 2989
Cdd:PRK06814 993 LGYLR---------AENPgvLEPPADGWYDTGDIV--TIDEE-GFITIK--GRAKRFAKIAGEMISLAAVEELAAElwPD 1058
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2990 AVESAV-----------VLGVGGSVATAlaayivpvdgavevSELKAFAGGR-LPAYMVPSSFTVIDELPLTPVGKLDKR 3057
Cdd:PRK06814 1059 ALHAAVsipdarkgeriILLTTASDATR--------------AAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKIDYV 1124
|
570
....*....|....*.
gi 1827387616 3058 ALPEPVLEAGEYVAPA 3073
Cdd:PRK06814 1125 AVTKLAEEAAAKPEAA 1140
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
4-414 |
7.77e-12 |
|
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase, most of which are as yet uncharacterized. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341296 [Multi-domain] Cd Length: 569 Bit Score: 70.91 E-value: 7.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVtSDGE 83
Cdd:cd17641 15 ADYADRVRAFALGLLALGVGRGDVVAILGDNRPEWVWAELAAQAIGALSLGIYQDSMAEEVAYLLNYTGARVVIA-EDEE 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 --------------------AEAR--SRFDDIVDVHVLDISSPGDA------DLDEEEFAGpTRPANAAFTLFTSGSTGR 135
Cdd:cd17641 94 qvdklleiadripsvryviyCDPRgmRKYDDPRLISFEDVVALGRAldrrdpGLYEREVAA-GKGEDVAVLCTTSGTTGK 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 136 PKAVVITHRGI----ANRLAAD------------------------------------IEQYDLTARDV------FLYKA 169
Cdd:cd17641 173 PKLAMLSHGNFlghcAAYLAADplgpgdeyvsvlplpwigeqmysvgqalvcgfivnfPEEPETMMEDLreigptFVLLP 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 170 PITF-----DVSVR--------EIFLPIAIGATLVIAEPGRHGDPVHLADLIRRHgvtviHFVPAMLAAFNEVLGagvge 236
Cdd:cd17641 253 PRVWegiaaDVRARmmdatpfkRFMFELGMKLGLRALDRGKRGRPVSLWLRLASW-----LADALLFRPLRDRLG----- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 237 LTSLRLIQTGGEALTPPVARdlMVRLPGTRLQNQYGPAEASIVVTIHRvtqDDRVIP--IGTPTRRVSARVLDAalrevp 314
Cdd:cd17641 323 FSRLRSAATGGAALGPDTFR--FFHAIGVPLKQLYGQTELAGAYTVHR---DGDVDPdtVGVPFPGTEVRIDEV------ 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 315 igvpGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGR-TDFQVKLRGQRLELGEVE 393
Cdd:cd17641 392 ----GEILVRSPGVFVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRaKDVGTTSDGTRFSPQFIE 460
|
490 500
....*....|....*....|.
gi 1827387616 394 AALAAAPGVlhaAAAVVDGPG 414
Cdd:cd17641 461 NKLKFSPYI---AEAVVLGAG 478
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1062-1527 |
1.05e-11 |
|
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: 70.32 E-value: 1.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1062 MDYDEFETRTNAIARALLARGVSPEDVVAVGMERSigsvlATWGVIKSGAAyvpvdpaypadriaymledsgaTVGITDA 1141
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETR-----AEWLITALGCW----------------------SQNIPIV 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1142 STRARLGESscewvDLADLEAEAESGDDITDTERNGsvrltnLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGT 1221
Cdd:cd17639 59 TVYATLGED-----ALIHSLNETECSAIFTDGKPDD------LACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPEL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1222 PEdePDTRIL------HVASpsFDASMFEMAWAIPAGH----TLVIAPQADFAGD----------ALATVLERdevtdmi 1281
Cdd:cd17639 128 LG--PDDRYLaylplaHIFE--LAAENVCLYRGGTIGYgsprTLTDKSKRGCKGDltefkptlmvGVPAIWDT------- 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1282 ITPSVLATVDP---------------ERAQY------------------------VRNLATGGEACPPELVERWSERGRR 1322
Cdd:cd17639 197 IRKGVLAKLNPmgglkrtlfwtayqsKLKALkegpgtplldelvfkkvraalggrLRYMLSGGAPLSADTQEFLNIVLCP 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1323 IFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDgrlheVPQGVV--------GELYLSTAGLARGYLGRPGQT 1394
Cdd:cd17639 277 VIQGYGLTETCAGGTVQDPGDLETGRVGPPLPCCEIKLVD-----WEEGGYstdkppprGEILIRGPNVFKGYYKNPEKT 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1395 AVSFVADpfgepgaRMYATGDLVRVAKGGNLEFAGRADHQVKI-NGQRVELGEIEAVLDAQPGVAQSVVVGVEStrggrk 1473
Cdd:cd17639 352 KEAFDGD-------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLqNGEYIALEKLESIYRSNPLVNNICVYADPD------ 418
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1474 HTEVVAYLV-------------AKPGATIDS--------AAVLDE-----AAQHLAAHMVPsQAIVIDEIP-------LT 1520
Cdd:cd17639 419 KSYPVAIVVpnekhltklaekhGVINSEWEElcedkklqKAVLKSlaetaRAAGLEKFEIP-QGVVLLDEEwtpenglVT 497
|
....*..
gi 1827387616 1521 PAGKLDR 1527
Cdd:cd17639 498 AAQKLKR 504
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
2559-3025 |
1.14e-11 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 70.56 E-value: 1.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2559 GPATDPVTLAELFRAAARRAPdhvavvdgagarLTYREL-DEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVA 2637
Cdd:cd17632 47 ELVTDPATGRTTLRLLPRFET------------ITYAELwERVGAVAAAHDPEQPVRPGDFVAVLGFTSPDYATVDLALT 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2638 KTGGAYVPIDPDYPAERVASMIEDSG----AV------LGLSVLASGDLPGQ--------EFEWMRLDDDSVAAEIAAVP 2699
Cdd:cd17632 115 RLGAVSVPLQAGASAAQLAPILAETEprllAVsaehldLAVEAVLEGGTPPRlvvfdhrpEVDAHRAALESARERLAAVG 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2700 AGPITDAERLGEVTAAN-------------LAYVIYTSGSTGRPKGVAVTHSGLANFARQeSDRLNAGDNP--VVLGFAS 2764
Cdd:cd17632 195 IPVTTLTLIAVRGRDLPpaplfrpepdddpLALLIYTSGSTGTPKGAMYTERLVATFWLK-VSSIQDIRPPasITLNFMP 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2765 PSFDASVLeYLLATVNEGTLAY-----------------RPSEA-----VGGEVLERFIAEHGATHTflTPSVLSTMDPT 2822
Cdd:cd17632 274 MSHIAGRI-SLYGTLARGGTAYfaaasdmstlfddlalvRPTELflvprVCDMLFQRYQAELDRRSV--AGADAETLAER 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2823 AVPSLRVIAAGGE---AV--PQPIVDR------WAPATELHNLYGPTETTIGITISSAMRPGdpvrlggpiggvdlmVLD 2891
Cdd:cd17632 351 VKAELRERVLGGRllaAVcgSAPLSAEmkafmeSLLDLDLHDGYGSTEAGAVILDGVIVRPP---------------VLD 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2892 ERLRPVP------VGMP---GELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVrwtpdTDTGGLTLEYT 2962
Cdd:cd17632 416 YKLVDVPelgyfrTDRPhprGELLVKTDTLFPGYYKRPEVTAEVFDEDGF-------YRTGDVM-----AELGPDRLVYV 483
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 2963 GRSDDQVKL-RGLRIELGEIEAVLAEHDAVESAVVLgvGGSVATALAAYIVPVDGAVE---VSELKA 3025
Cdd:cd17632 484 DRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVY--GNSERAYLLAVVVPTQDALAgedTARLRA 548
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
2713-3059 |
1.28e-11 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 70.19 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2713 TAANLAYVIY-TSGSTGRPKGVAVTHS----GLANFAR-----QESDRL-NAGDNPVVLGFASPSFD-----ASVLEYLL 2776
Cdd:cd05928 171 TGSQEPMAIYfTSGTTGSPKMAEHSHSslglGLKVNGRywldlTASDIMwNTSDTGWIKSAWSSLFEpwiqgACVFVHHL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2777 ATVNEGTLAyrpseavggEVLERFiaehgATHTFLTPSVLSTM----DPTAV--PSLRVIAAGGEAVPQPIVDRWAPAT- 2849
Cdd:cd05928 251 PRFDPLVIL---------KTLSSY-----PITTFCGAPTVYRMlvqqDLSSYkfPSLQHCVTGGEPLNPEVLEKWKAQTg 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2850 -ELHNLYGPTETTIGITISSAM--RPGDpvrLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGG-----ALSRGYLDRSG 2921
Cdd:cd05928 317 lDIYEGYGQTETGLICANFKGMkiKPGS---MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRVKpirpfGLFSGYVDNPE 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2922 LTAERFTANPYGTaGQRMYRTGDVVRWtpdtdtggltleYTGRSDDQVKLRGLRIELGEIEAVLAEHDAV-ESAVVLG-- 2998
Cdd:cd05928 394 KTAATIRGDFYLT-GDRGIMDEDGYFW------------FMGRADDVINSSGYRIGPFEVESALIEHPAVvESAVVSSpd 460
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 2999 -VGGSVATA---LAAYIVPVDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05928 461 pIRGEVVKAfvvLAPQFLSHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1-402 |
1.37e-11 |
|
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: 69.94 E-value: 1.37e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGghfvpldeqlpvdrarymvrtagvrLVVVT- 79
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN-------------------------IPIVTv 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 80 --SDGEaearsrfDDIVdvHVLD-------ISSPGDADLdeeefagptrpanaAFTLFTSGSTGRPKAVVITHRGIANRL 150
Cdd:cd17639 61 yaTLGE-------DALI--HSLNetecsaiFTDGKPDDL--------------ACIMYTSGSTGNPKGVMLTHGNLVAGI 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 151 AA--DIEQYDLTARDVFLYKAPIT--FDVSVREIFLpiAIGATLVIAEP---------GRHGD-----PVHLA------D 206
Cdd:cd17639 118 AGlgDRVPELLGPDDRYLAYLPLAhiFELAAENVCL--YRGGTIGYGSPrtltdkskrGCKGDltefkPTLMVgvpaiwD 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 207 LIRRhgvTVIHFVPAM---------------LAA---------FNEVLGAGVGELTS--LRLIQTGGEALTPPVARDLMV 260
Cdd:cd17639 196 TIRK---GVLAKLNPMgglkrtlfwtayqskLKAlkegpgtplLDELVFKKVRAALGgrLRYMLSGGAPLSADTQEFLNI 272
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 261 RLpGTRLQNqYGPAEASIVVTIHRVTQ--DDRVipiGTPTRRVSARVLDAA-LREVPIGVP--GELYLGGVQLARGYAGR 335
Cdd:cd17639 273 VL-CPVIQG-YGLTETCAGGTVQDPGDleTGRV---GPPLPCCEIKLVDWEeGGYSTDKPPprGEILIRGPNVFKGYYKN 347
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 336 PDLTAERFVADpfgepgaRLYRTGDRARWNRDGEIEYLGRTDFQVKLR-GQRLELGEVEAALAAAPGV 402
Cdd:cd17639 348 PEKTKEAFDGD-------GWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLV 408
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
486-554 |
1.75e-11 |
|
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: 62.18 E-value: 1.75e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 486 EETVAGLFAELLGV--ERVGVTDSFF-DIGGSSLSAARIAARVSKELGVDVSVRDVFESPSVRGLVHAVSGR 554
Cdd:COG0236 7 EERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEK 78
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
4-468 |
2.94e-11 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 69.04 E-value: 2.94e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLAREL-TALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTA----------- 71
Cdd:PRK05620 42 AAIGARAAALAHALhDELGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAedevivadprl 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 72 ------------GVRLVVVTSDGEAeARSRFDDIVDVHVLDIsspgDADLDEE--EFAGPTRPANAAFTL-FTSGSTGRP 136
Cdd:PRK05620 122 aeqlgeilkecpCVRAVVFIGPSDA-DSAAAHMPEGIKVYSY----EALLDGRstVYDWPELDETTAAAIcYSTGTTGAP 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 137 KAVVITHRGI----ANRLAADieQYDLTARDVFLYKAPItfdVSVREIFLPIAI---GATLVIaePGRHGDPVHLADLIR 209
Cdd:PRK05620 197 KGVVYSHRSLylqsLSLRTTD--SLAVTHGESFLCCVPI---YHVLSWGVPLAAfmsGTPLVF--PGPDLSAPTLAKIIA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 210 RHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALtPPVARDLMVRLPGTRLQNQYGPAEASIVVTI------- 282
Cdd:PRK05620 270 TAMPRVAHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAV-PPILIKAWEERYGVDVVHVWGMTETSPVGTVarppsgv 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 283 -------HRVTQDDrvIPIGTPTRRVS-ARVLDAALREvpigvPGELYLGGVQLARGY----AGRPDLTAERFVADPFGE 350
Cdd:PRK05620 349 sgearwaYRVSQGR--FPASLEYRIVNdGQVMESTDRN-----EGEIQVRGNWVTASYyhspTEEGGGAASTFRGEDVED 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 351 PGARL-----YRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA-AVVDGPGGQQ--LVGYL 422
Cdd:PRK05620 422 ANDRFtadgwLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAViGYPDDKWGERplAVTVL 501
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 423 APadvDVDTVAATTAEL-------LPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK05620 502 AP---GIEPTRETAERLrdqlrdrLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
1041-1529 |
3.22e-11 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 69.00 E-value: 3.22e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1041 DVLAQRDLDPDHPALICdGTEMDYDEFETRTNAIArALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPV-DPA 1119
Cdd:PRK12476 49 DTVAYRYLDHSHSAAGC-AVELTWTQLGVRLRAVG-ARLQQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPE 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1120 YP--ADRIAYMLEDSGATVGITDASTRARLGESscewvdLADLEAEAESG----DDITDTERNGSVRLT----NLAYLIY 1189
Cdd:PRK12476 127 LPghAERLDTALRDAEPTVVLTTTAAAEAVEGF------LRNLPRLRRPRviaiDAIPDSAGESFVPVEldtdDVSHLQY 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1190 TSGSTGRPKAVGVSHTGIVdfVNSLAKITTGTPEDePDTR------------ILHVASPS--------FDASMF------ 1243
Cdd:PRK12476 201 TSGSTRPPVGVEITHRAVG--TNLVQMILSIDLLD-RNTHgvswlplyhdmgLSMIGFPAvygghstlMSPTAFvrrpqr 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1244 ---EMAWAIPAGHTLVIAPQADFAGDALATVLERDEVTD-----MII--TPSVLATVDperaqyVRNLATGGEACPPELV 1313
Cdd:PRK12476 278 wikALSEGSRTGRVVTAAPNFAYEWAAQRGLPAEGDDIDlsnvvLIIgsEPVSIDAVT------TFNKAFAPYGLPRTAF 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1314 ErwsergrrifNCYGPTEAT--------------VWATRSRMTAGKPVTIGKPVDGFTVRVLDGRL-------------- 1365
Cdd:PRK12476 352 K----------PSYGIAEATlfvatiapdaepsvVYLDREQLGAGRAVRVAADAPNAVAHVSCGQVarsqwavivdpdtg 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1366 HEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVAD-----PFG------EPGARMYATGDLvRVAKGGNLEFAGRADHQ 1434
Cdd:PRK12476 422 AELPDGEVGEIWLHGDNIGRGYWGRPEETERTFGAKlqsrlAEGshadgaADDGTWLRTGDL-GVYLDGELYITGRIADL 500
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1435 VKINGQRVELGEIEA-VLDAQPGVAQSVVVGVESTRGGRKHTEVVAYLV-----AKPGATIDS--AAVLDEAAQHLA-AH 1505
Cdd:PRK12476 501 IVIDGRNHYPQDIEAtVAEASPMVRRGYVTAFTVPAEDNERLVIVAERAagtsrADPAPAIDAirAAVSRRHGLAVAdVR 580
|
570 580
....*....|....*....|....
gi 1827387616 1506 MVPSQAivideIPLTPAGKLDRAA 1529
Cdd:PRK12476 581 LVPAGA-----IPRTTSGKLARRA 599
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
2722-3067 |
4.45e-11 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 68.72 E-value: 4.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2722 YTSGSTGRPKGVAVTHSGLanfarqesdRLNAGDNPVVLG--------FASPSFDAS--VLEYLLATVNEGTLAYRPSEA 2791
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRGA---------YLMALSNALIWGmnegavylWTLPMFHCNgwCFTWTLAALCGTNICLRQVTA 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2792 VGgevLERFIAEHGATHTFLTPSVLSTM-----DPTAVPSLRVI---AAGgeAVPQPIV--------DRWAPATELHNLY 2855
Cdd:PLN02479 273 KA---IYSAIANYGVTHFCAAPVVLNTIvnapkSETILPLPRVVhvmTAG--AAPPPSVlfamsekgFRVTHTYGLSETY 347
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2856 GPTETTIGITISSAMRPGDPVRLGGP-----IGGVDLMVLDER-LRPVPV--GMPGELYVAGGALSRGYLDRSGLTAERF 2927
Cdd:PLN02479 348 GPSTVCAWKPEWDSLPPEEQARLNARqgvryIGLEGLDVVDTKtMKPVPAdgKTMGEIVMRGNMVMKGYLKNPKANEEAF 427
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2928 tANPYgtagqrmYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAV-ESAVVLGVGGSVATA 3006
Cdd:PLN02479 428 -ANGW-------FHSGDLGVKHPDG-----YIEIKDRSKDIIISGGENISSLEVENVVYTHPAVlEASVVARPDERWGES 494
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 3007 LAAYIVPVDGAVEVSE------LKAFAGGRLPAYMVPSSfTVIDELPLTPVGKLDKRALPEPVLEAG 3067
Cdd:PLN02479 495 PCAFVTLKPGVDKSDEaalaedIMKFCRERLPAYWVPKS-VVFGPLPKTATGKIQKHVLRAKAKEMG 560
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1185-1530 |
4.48e-11 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 69.22 E-value: 4.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1185 AYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtrILHVASPSFDASMFEMAWAIP--AGHTLV------ 1256
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHRNLLANRAQVAARIDFSPED-----KVFNALPVFHSFGLTGGLVLPllSGVKVFlypspl 870
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1257 ---IAPQADFAGDAlatvlerdevTDMIITPSVLA----TVDPERAQYVRNLATGGEACPPELVERWSER-GRRIFNCYG 1328
Cdd:PRK06814 871 hyrIIPELIYDTNA----------TILFGTDTFLNgyarYAHPYDFRSLRYVFAGAEKVKEETRQTWMEKfGIRILEGYG 940
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1329 PTE-ATVWATRSRMtAGKPVTIGKPVDGftvrvLDGRLHEVP---QGvvGELYLSTAGLARGYL--GRPGqtavsfVADP 1402
Cdd:PRK06814 941 VTEtAPVIALNTPM-HNKAGTVGRLLPG-----IEYRLEPVPgidEG--GRLFVRGPNVMLGYLraENPG------VLEP 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1403 fgePGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEA-VLDAQPGvAQSVVVGVESTRGGrkhtEVVAYL 1481
Cdd:PRK06814 1007 ---PADGWYDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEElAAELWPD-ALHAAVSIPDARKG----ERIILL 1078
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1482 VAKPGATidSAAVLDEAAQHLAAH-MVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK06814 1079 TTASDAT--RAAFLAHAKAAGASElMVPAEIITIDEIPLLGTGKIDYVAV 1126
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
128-413 |
7.52e-11 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 67.88 E-value: 7.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 128 FTSGSTGRPKAVVITHRGIANRLAADIEQY-DLTARDVFLYKAPITFDVS-VREIFLPIAIGATLVIAEPGRHgDPVHLA 205
Cdd:cd05928 181 FTSGTTGSPKMAEHSHSSLGLGLKVNGRYWlDLTASDIMWNTSDTGWIKSaWSSLFEPWIQGACVFVHHLPRF-DPLVIL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 206 DLIRRHGVTVIHFVPAmlaAFNEVLGAGVG--ELTSLRLIQTGGEALTPPVaRDLMVRLPGTRLQNQYGPAEasiVVTIH 283
Cdd:cd05928 260 KTLSSYPITTFCGAPT---VYRMLVQQDLSsyKFPSLQHCVTGGEPLNPEV-LEKWKAQTGLDIYEGYGQTE---TGLIC 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 284 RVTQDDRVIP--IGTPTRRVSARVLDAALREVPIGVPGELylgGVQLA--------RGYAGRPDLTAERFVADpfgepga 353
Cdd:cd05928 333 ANFKGMKIKPgsMGKASPPYDVQIIDDNGNVLPPGTEGDI---GIRVKpirpfglfSGYVDNPEKTAATIRGD------- 402
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 354 rLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGP 413
Cdd:cd05928 403 -FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAV--VESAVVSSP 459
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
604-917 |
9.49e-11 |
|
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: 67.13 E-value: 9.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 604 DVDETLLFDSLCDVVERHEVLRTVY-----------PSVGAAPVQD---VLPVAVAREQLDWREADSVESLVRSTTEGFD 669
Cdd:cd19535 36 DLDPDRLERAWNKLIARHPMLRAVFlddgtqqilpeVPWYGITVHDlrgLSEEEAEAALEELRERLSHRVLDVERGPLFD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 670 VS-TQMPlRGRfHRdgagLHVALTMhhIAMDGQSIPVLARDLMSAYAARAEgrtgGLPVLDVQYADYALWQQsvlgdADD 748
Cdd:cd19535 116 IRlSLLP-EGR-TR----LHLSIDL--LVADALSLQILLRELAALYEDPGE----PLPPLELSFRDYLLAEQ-----ALR 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 749 ETSVLGEQlSHWRRVLAGLPAVTDLPMdRPRPAVLGTAGAT-VTVEFDDDLADRVDVLARSNTMTGFMVTEAAFAATVAR 827
Cdd:cd19535 179 ETAYERAR-AYWQERLPTLPPAPQLPL-AKDPEEIKEPRFTrREHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLAR 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 828 LASTTDVVIGTPVAGRND--PALEELIGMFVNTLLLRTQVDPGHSVGDLLGNVRTTVLDAFAN-DQVQFDELIEALApeR 904
Cdd:cd19535 257 WSGQPRFLLNLTLFNRLPlhPDVNDVVGDFTSLLLLEVDGSEGQSFLERARRLQQQLWEDLDHsSYSGVVVVRRLLR--R 334
|
330
....*....|...
gi 1827387616 905 SSSHQPLAQIAFT 917
Cdd:cd19535 335 RGGQPVLAPVVFT 347
|
|
| PRK07768 |
PRK07768 |
long-chain-fatty-acid--CoA ligase; Validated |
2587-2921 |
1.37e-10 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236091 [Multi-domain] Cd Length: 545 Bit Score: 66.94 E-value: 1.37e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2587 GAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYP----------AERVA 2656
Cdd:PRK07768 25 DAPVRHTWGEVHERARRIAGGLAAAGVGPGDAVAVLAGAPVEIAPTAQGLWMRGASLTMLHQPTPrtdlavwaedTLRVI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2657 SMIEDSGAVLGLSVLASGDLPGQEFEWMRLDDDSVAAEiaavPAGPItdaerlgEVTAANLAYVIYTSGSTGRPKGVAVT 2736
Cdd:PRK07768 105 GMIGAKAVVVGEPFLAAAPVLEEKGIRVLTVADLLAAD----PIDPV-------ETGEDDLALMQLTSGSTGSPKAVQIT 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2737 HSGLANFARQESDRLNAG-DNPVVLGFASPSFDASVLEYLLATVNEG--TLAYRPSEAVGGEVL-ERFIAEHGATHTF-- 2810
Cdd:PRK07768 174 HGNLYANAEAMFVAAEFDvETDVMVSWLPLFHDMGMVGFLTVPMYFGaeLVKVTPMDFLRDPLLwAELISKYRGTMTAap 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2811 -----LTPSVLSTMDPTA---VPSLRVIAAGGEAVPQPIVDRWAPATELHNL--------YGPTETTIGITIS------- 2867
Cdd:PRK07768 254 nfayaLLARRLRRQAKPGafdLSSLRFALNGAEPIDPADVEDLLDAGARFGLrpeailpaYGMAEATLAVSFSpcgaglv 333
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 2868 ---------SAMRPGDP---------VRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSG 2921
Cdd:PRK07768 334 vdevdadllAALRRAVPatkgntrrlATLGPPLPGLEVRVVDEDGQVLPPRGVGVIELRGESVTPGYLTMDG 405
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1050-1530 |
1.58e-10 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 66.79 E-value: 1.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1050 PDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYML 1129
Cdd:PLN02479 34 PTRKSVVHGSVRYTWAQTYQRCRRLASALAKRSIGPGSTVAVIAPNIPAMYEAHFGVPMAGAVVNCVNIRLNAPTIAFLL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1130 EDSGATVGITD-------------------ASTRARL----GESSCEWVDLAD------LEAEA--ESGDDITD----TE 1174
Cdd:PLN02479 114 EHSKSEVVMVDqefftlaeealkilaekkkSSFKPPLliviGDPTCDPKSLQYalgkgaIEYEKflETGDPEFAwkppAD 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1175 RNGSVRLTnlayliYTSGSTGRPKAVGVSHTGIvdFVNSLAK-ITTGTPEDEPDTRILhvasPSFDASMFEMAWAIPA-G 1252
Cdd:PLN02479 194 EWQSIALG------YTSGTTASPKGVVLHHRGA--YLMALSNaLIWGMNEGAVYLWTL----PMFHCNGWCFTWTLAAlC 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1253 HTLVIAPQAdfAGDALATVLERDEVTDMIITPSVLATV----DPERA---QYVRNLATGGEACPPELVERWSERGRRIFN 1325
Cdd:PLN02479 262 GTNICLRQV--TAKAIYSAIANYGVTHFCAAPVVLNTIvnapKSETIlplPRVVHVMTAGAAPPPSVLFAMSEKGFRVTH 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1326 CYGPTE----ATVWA-----------TRSRMTAGKPVT-IGkpVDGFTVrVLDGRLHEVPQ--GVVGELYLSTAGLARGY 1387
Cdd:PLN02479 340 TYGLSEtygpSTVCAwkpewdslppeEQARLNARQGVRyIG--LEGLDV-VDTKTMKPVPAdgKTMGEIVMRGNMVMKGY 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1388 LGRPGQTAVSFVADpfgepgarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVES 1467
Cdd:PLN02479 417 LKNPKANEEAFANG--------WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVARPD 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 1468 TRGGRKHtevVAYLVAKPGA-TIDSAAVLDEAAQ----HLAAHMVPsQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PLN02479 489 ERWGESP---CAFVTLKPGVdKSDEAALAEDIMKfcreRLPAYWVP-KSVVFGPLPKTATGKIQKHVL 552
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1038-1416 |
1.97e-10 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 66.50 E-value: 1.97e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1038 TLIDVLAQR-DLDPDHPALicdgTEMDYD-------------EFETRTNAIARALLARGvSPEDVVAVGMERSIGSVLAT 1103
Cdd:PRK05850 2 SVPSLLRERaSLQPDDAAF----TFIDYEqdpagvaetltwsQLYRRTLNVAEELRRHG-STGDRAVILAPQGLEYIVAF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1104 WGVIKSGAAYVPVDPAYPA---DRIAYMLEDSGATVGITDASTRARLGESSCEW----------VDLADLEAEAESGDDI 1170
Cdd:PRK05850 77 LGALQAGLIAVPLSVPQGGahdERVSAVLRDTSPSVVLTTSAVVDDVTEYVAPQpgqsappvieVDLLDLDSPRGSDARP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1171 TDterngsvrLTNLAYLIYTSGSTGRPKAVGVSHTG-IVDFVNSLAKITTGTPEDEPDTR--------------ILHVAS 1235
Cdd:PRK05850 157 RD--------LPSTAYLQYTSGSTRTPAGVMVSHRNvIANFEQLMSDYFGDTGGVPPPDTtvvswlpfyhdmglVLGVCA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1236 PSFDAS----MFEMAW-AIPAG--HTLVIAPQA-----DFAGDaLATVLERDEvtDMiitpsvlATVDPERaqyVRNLAT 1303
Cdd:PRK05850 229 PILGGCpavlTSPVAFlQRPARwmQLLASNPHAfsaapNFAFE-LAVRKTSDD--DM-------AGLDLGG---VLGIIS 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1304 GGEACPPELVERWSERGRRiFN--------CYGPTEATVW------------------------ATRSRMTAGKP-VTIG 1350
Cdd:PRK05850 296 GSERVHPATLKRFADRFAP-FNlretairpSYGLAEATVYvatrepgqppesvrfdyeklsaghAKRCETGGGTPlVSYG 374
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1827387616 1351 KPvDGFTVRVLDGRLH-EVPQGVVGELYLSTAGLARGYLGRPGQTAVSF---VADPF-GEPGARMYATGDL 1416
Cdd:PRK05850 375 SP-RSPTVRIVDPDTCiECPAGTVGEIWVHGDNVAAGYWQKPEETERTFgatLVDPSpGTPEGPWLRTGDL 444
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
2-452 |
1.98e-10 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 66.44 E-value: 1.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVV--- 78
Cdd:PRK08279 64 SYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQRGAVLAHSLNLVDAKHLIVgee 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 79 TSDGEAEARSRFDDIVDVHVLD----ISSPGDADLDEEEFAGPTRPANA---------AFTLFTSGSTGRPKAVVITHRG 145
Cdd:PRK08279 144 LVEAFEEARADLARPPRLWVAGgdtlDDPEGYEDLAAAAAGAPTTNPASrsgvtakdtAFYIYTSGTTGLPKAAVMSHMR 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 146 IANRLAADIEQYDLTARDVfLYkapitfdvsvreIFLP--------------IAIGATLVIaepGRHGDPVHLADLIRRH 211
Cdd:PRK08279 224 WLKAMGGFGGLLRLTPDDV-LY------------CCLPlyhntggtvawssvLAAGATLAL---RRKFSASRFWDDVRRY 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 212 GVTVIHFvpamlaafnevlgagVGELT---------------SLRLIQtgGEALTPPVARDLMVRLPGTRLQNQYGPAEA 276
Cdd:PRK08279 288 RATAFQY---------------IGELCryllnqppkptdrdhRLRLMI--GNGLRPDIWDEFQQRFGIPRILEFYAASEG 350
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 277 SIVV--------TIHRVTQDDRViPI---------GTPTRrvsarvlDAA--LREVPIGVPGELyLGGV-QLAR--GYAg 334
Cdd:PRK08279 351 NVGFinvfnfdgTVGRVPLWLAH-PYaivkydvdtGEPVR-------DADgrCIKVKPGEVGLL-IGRItDRGPfdGYT- 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 335 RPDLTAERFVADPFgEPGARLYRTGDRARWNRDGEIEY---LGRTdFQVKlrGQRLELGEVEAALAAAPGVLHAAAAVVD 411
Cdd:PRK08279 421 DPEASEKKILRDVF-KKGDAWFNTGDLMRDDGFGHAQFvdrLGDT-FRWK--GENVATTEVENALSGFPGVEEAVVYGVE 496
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 1827387616 412 GPG-----GQQLVGYLAPADVDVDTVAATTAELLPEYMRPsAWVRL 452
Cdd:PRK08279 497 VPGtdgraGMAAIVLADGAEFDLAALAAHLYERLPAYAVP-LFVRL 541
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
1061-1530 |
2.17e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 66.34 E-value: 2.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1061 EMDYDEFETRTNAIARALLAR-GVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGIT 1139
Cdd:PRK05620 38 QTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEDEVIVA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1140 DASTRARLGE--SSCEWV---------DLADLEAEAESGDDITDTERNGSVRLT----------NLAYLIYTSGSTGRPK 1198
Cdd:PRK05620 118 DPRLAEQLGEilKECPCVravvfigpsDADSAAAHMPEGIKVYSYEALLDGRSTvydwpeldetTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1199 AVGVSHTGIvdFVNSLAKITTGTPEDEPDTRIL------HVASpsfdasmfemaWAIP-----AGHTLVIaPQADFAGDA 1267
Cdd:PRK05620 198 GVVYSHRSL--YLQSLSLRTTDSLAVTHGESFLccvpiyHVLS-----------WGVPlaafmSGTPLVF-PGPDLSAPT 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1268 LATVLERDE------VTDMIITPSVLATVDPERAQYVRNLATGGEACPPELVERWSER-GRRIFNCYGPTEATVWATRSR 1340
Cdd:PRK05620 264 LAKIIATAMprvahgVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEERyGVDVVHVWGMTETSPVGTVAR 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1341 MTAGKP--------VTIGKPVDGFTVRVL-DGRL---HEVPQG--------VVGELYLSTAGLARGYLGRPGQTAVSFVA 1400
Cdd:PRK05620 344 PPSGVSgearwayrVSQGRFPASLEYRIVnDGQVmesTDRNEGeiqvrgnwVTASYYHSPTEEGGGAASTFRGEDVEDAN 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1401 DPFGEPGarMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKHTEVVay 1480
Cdd:PRK05620 424 DRFTADG--WLRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKWGERPLAVT-- 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 1481 lVAKPGA--TIDSAAVL-DEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK05620 500 -VLAPGIepTRETAERLrDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
28-370 |
2.27e-10 |
|
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: 66.08 E-value: 2.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 28 VGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDGEAEArsrFDDIVDVhvldisspGDA 107
Cdd:cd05927 35 VGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFCDAGVKVYS---LEEFEKL--------GKK 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 108 DLDEEEfagPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQydltardVFLYKAPITFDVSVReiFLPIA-- 185
Cdd:cd05927 104 NKVPPP---PPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKI-------LEILNKINPTDVYIS--YLPLAhi 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 186 ---IGATLVIAEPGR----HGDPVHLADLIRRHGVTVIHFVPAML-----AAFNEVLGAG--------------VGELTS 239
Cdd:cd05927 172 ferVVEALFLYHGAKigfySGDIRLLLDDIKALKPTVFPGVPRVLnriydKIFNKVQAKGplkrklfnfalnykLAELRS 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 240 ------------------------LRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTIhrVTQDDRVI-PI 294
Cdd:cd05927 252 gvvraspfwdklvfnkikqalggnVRLMLTGSAPLSPEVLEFLRVAL-GCPVLEGYGQTECTAGATL--TLPGDTSVgHV 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 295 GTPTRRVSARVLDA------ALREVPigvPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDG 368
Cdd:cd05927 329 GGPLPCAEVKLVDVpemnydAKDPNP---RGEVCIRGPNVFSGYYKDPEKTAEALDEDGW-------LHTGDIGEWLPNG 398
|
..
gi 1827387616 369 EI 370
Cdd:cd05927 399 TL 400
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
2140-2421 |
2.54e-10 |
|
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: 65.28 E-value: 2.54e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2140 VLSLTGDVDPGRLRSALSELLARQRVLRSGFVRLPSGAAVTVVPAEVTVPW-SVIDLRAEdaasldsrveevlaterTN- 2217
Cdd:cd19537 29 ACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSSSPPRVQRvDTLDVWKE-----------------INr 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2218 PFDMAKPPLIRVVLvehgDGAELVVTNHHllidgwssplVLADLLSLYA----TGQTFTGSLPGTSGRDFADHARAVATA 2293
Cdd:cd19537 92 PFDLEREDPIRVFI----SPDTLLVVMSH----------IICDLTTLQLllreVSAAYNGKLLPPVRREYLDSTAWSRPA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2294 DVEAgIAAWREVLAPVteptlvapghePSADAPPRD---------HQFSIDVKVTERLEALARNNSTTM-----ATVvqf 2359
Cdd:cd19537 158 SPED-LDFWSEYLSGL-----------PLLNLPRRTssksyrgtsRVFQLPGSLYRSLLQFSTSSGITLhqlalAAV--- 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 2360 awAMFLSRLTGTRTVTFAETVSGRSPDIEgmESMVGMFINTIPAVV--DVNPDATVVDVLTAVQ 2421
Cdd:cd19537 223 --ALALQDLSDRTDIVLGAPYLNRTSEED--METVGLFLEPLPIRIrfPSSSDASAADFLRAVR 282
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
2593-3059 |
2.82e-10 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 65.53 E-value: 2.82e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2593 TYRELDEASDRLARWLIG-RGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIEDSGAVLGLSvl 2671
Cdd:cd05937 7 TYSETYDLVLRYAHWLHDdLGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFINYNLSGDPLIHCLKLSGSRFVIV-- 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2672 asgdlpgqefewmrlDDDSVAAeiaavpagpitdaerlgevtaanlayVIYTSGSTGRPKGVAVTHSGLANFARQESDRL 2751
Cdd:cd05937 85 ---------------DPDDPAI--------------------------LIYTSGTTGLPKAAAISWRRTLVTSNLLSHDL 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2752 NAgDNPVVLGFASPSFDASVleYLLATVNE----GTLAYRPSEAVggevlERF---IAEHGATHTF----LTPSVLSTmd 2820
Cdd:cd05937 124 NL-KNGDRTYTCMPLYHGTA--AFLGACNClmsgGTLALSRKFSA-----SQFwkdVRDSGATIIQyvgeLCRYLLST-- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2821 PtavPSL-----RVIAAGGEAVPQPIVDRWAP---ATELHNLYGPTETTIGITISSAmrpGD----PVRLGGPI------ 2882
Cdd:cd05937 194 P---PSPydrdhKVRVAWGNGLRPDIWERFRErfnVPEIGEFYAATEGVFALTNHNV---GDfgagAIGHHGLIrrwkfe 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2883 GGVDLMVLDER-----LRP-------VPVGMPGELYVAGGALSR----GYLDRSGLTAERFTANPYgTAGQRMYRTGDVV 2946
Cdd:cd05937 268 NQVVLVKMDPEtddpiRDPktgfcvrAPVGEPGEMLGRVPFKNReafqGYLHNEDATESKLVRDVF-RKGDIYFRTGDLL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2947 RWtpdtDTGGLtLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV--------GGSVATAL---AAYIVPVD 3015
Cdd:cd05937 347 RQ----DADGR-WYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYGVkvpghdgrAGCAAITLeesSAVPTEFT 421
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 1827387616 3016 gaveVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:cd05937 422 ----KSLLASLARKNLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
9-463 |
5.12e-10 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 65.04 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 9 RVTGLARELTALGVGAEVAVGIqIDRSVEQVVAIH-AVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDGEAEAR 87
Cdd:PLN03102 48 RCCRLAASLISLNITKNDVVSV-LAPNTPAMYEMHfAVPMAGAVLNPINTRLDATSIAAILRHAKPKILFVDRSFEPLAR 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 88 ------SRFDDIVDVHVL---DISSPGDADLDEEEFAG------PTRPANAAFTL-----------FTSGSTGRPKAVVI 141
Cdd:PLN03102 127 evlhllSSEDSNLNLPVIfihEIDFPKRPSSEELDYECliqrgePTPSLVARMFRiqdehdpislnYTSGTTADPKGVVI 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 142 THRGIANRLAADIEQYDLTARDVFLYKAPI------TFDVSVreiflpIAIGATLVIAepgRHGDPVHLADLIRRHGVTV 215
Cdd:PLN03102 207 SHRGAYLSTLSAIIGWEMGTCPVYLWTLPMfhcngwTFTWGT------AARGGTSVCM---RHVTAPEIYKNIEMHNVTH 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 216 IHFVPAMlaaFNEVLGAGVGEL---TSLRLIQTGGEalTPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVI 292
Cdd:PLN03102 278 MCCVPTV---FNILLKGNSLDLsprSGPVHVLTGGS--PPPAALVKKVQRLGFQVMHAYGLTEATGPVLFCEWQDEWNRL 352
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 293 PIGTPTR---RVSARVL-----DAALREVPIGVP------GELYLGGVQLARGYAGRPDLTAERFVADpfgepgarLYRT 358
Cdd:PLN03102 353 PENQQMElkaRQGVSILgladvDVKNKETQESVPrdgktmGEIVIKGSSIMKGYLKNPKATSEAFKHG--------WLNT 424
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 359 GDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGPG-GQQLVGYLA------PADVDVDT 431
Cdd:PLN03102 425 GDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTwGETPCAFVVlekgetTKEDRVDK 504
|
490 500 510
....*....|....*....|....*....|....*....
gi 1827387616 432 VAATTAEL-------LPEYMRPSAWVRLDAMPLSRSGKV 463
Cdd:PLN03102 505 LVTRERDLieycrenLPHFMCPRKVVFLQELPKNGNGKI 543
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
617-879 |
5.67e-10 |
|
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: 64.38 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 617 VVERHEVLRTVYPSVG-AAPVQDV-----LPVavarEQLDWREADSVESLVRSTTEG----FDVsTQMPL-RGRFHRDGA 685
Cdd:cd19544 48 VIDRHDILRTAILWEGlSEPVQVVwrqaeLPV----EELTLDPGDDALAQLRARFDPrryrLDL-RQAPLlRAHVAEDPA 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 686 G--LHVALTMHHIAMDGQSIPVLARDLmsayAARAEGRTGGLPVLdVQYADYALWQQSVLGDADDETsvlgeqlsHWRRV 763
Cdd:cd19544 123 NgrWLLLLLFHHLISDHTSLELLLEEI----QAILAGRAAALPPP-VPYRNFVAQARLGASQAEHEA--------FFREM 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 764 LAG-----LP-AVTDLPMDrprpavlGTAGATVTVEFDDDLADRVDVLARSNTMTGFMVTEAAFAATVARLASTTDVVIG 837
Cdd:cd19544 190 LGDvdeptAPfGLLDVQGD-------GSDITEARLALDAELAQRLRAQARRLGVSPASLFHLAWALVLARCSGRDDVVFG 262
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1827387616 838 TPVAGR--NDPALEELIGMFVNTLLLRTQVDpGHSVGDLLGNVR 879
Cdd:cd19544 263 TVLSGRmqGGAGADRALGMFINTLPLRVRLG-GRSVREAVRQTH 305
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
2572-3124 |
8.12e-10 |
|
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: 64.72 E-value: 8.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2572 RAAARRAPDHVAVVDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYP 2651
Cdd:COG3319 7 AAAAAAAAAAAAAAAAAAAALAAAAAAAAAAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALAL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2652 AERVASMIEDSGAVLGLSVLASGDLPGQEFEW--MRLDDDSVAAEIAAVPAGPITDAERLGEVTAANLAYVIYTSGSTGR 2729
Cdd:COG3319 87 ALAAAAAALLLAALALLLALLAALALALLALLlaALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2730 PKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEGTLAYRPSEAVGGEVLERFIAEHGATHT 2809
Cdd:COG3319 167 VLAALLALLLAALLALALALAALLLLALAAALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAA 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2810 FLTPSVLSTMDPTAVPSLRVIAAGGEAVPQPIVDRWAPATELHNLYGPTETTIGITISSAMRPGDPVRLGGPIGGVDLMV 2889
Cdd:COG3319 247 LLLLLALALLLLLALLLLLGLLALLLALLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2890 LDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYGTAGQRMYRTGDVVRWTPDTDtGGLTLEYTGRSDDQV 2969
Cdd:COG3319 327 LLVLLVLLLPLLLGVGGGGGGGGGGGGAGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRL-GGGLLLGLGRLRLQR 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2970 KLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVPVDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLT 3049
Cdd:COG3319 406 LRRGLREELEEAEAALAEAAAVAAAVAAAAAAAAAAAALAAAVVAAAALAAAALLLLLLLLLLPPPLPPALLLLLLLLLL 485
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 3050 PVGKLDKRALPEPVLEAGEYVAPATGTERTIADVAAGVLNIDAGLVSATSSFFEL------------------------- 3104
Cdd:COG3319 486 LLLAALLLAAAAPAAAAAAAAAPAPAAALELALALLLLLLLGLGLVGDDDDFFGGgggsllallllllllalllrlllll 565
|
570 580 590 600 610 620
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 3105 ---------------------------------------------GGDSLSAARLAARLSDQLGV 3124
Cdd:COG3319 566 alllaptlaalaaalaaaaaaaalsplvplraggsgpplfcvhpaGGNVLCYRPLARALGPDRPV 630
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
2709-3059 |
9.05e-10 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 64.42 E-value: 9.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2709 LGEVTAANLAYviyTSGSTGRPKGVAVTHSGLAnfarQESDRLNAGDN-------------PV--VLGFASPsfdasvle 2773
Cdd:PRK05620 178 LDETTAAAICY---STGTTGAPKGVVYSHRSLY----LQSLSLRTTDSlavthgesflccvPIyhVLSWGVP-------- 242
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2774 ylLATVNEGTLAYRPSEAVGGEVLERFIAE------HGATHTFLTPSVLSTMDPTAVPSLRVIAAGGEAVPQPIVDRWAP 2847
Cdd:PRK05620 243 --LAAFMSGTPLVFPGPDLSAPTLAKIIATamprvaHGVPTLWIQLMVHYLKNPPERMSLQEIYVGGSAVPPILIKAWEE 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2848 --ATELHNLYGPTETTigiTISSAMRPgdPVRLGG-------------PIGGVDLMVLDERLRPVPVGMPGELYVAGGAL 2912
Cdd:PRK05620 321 ryGVDVVHVWGMTETS---PVGTVARP--PSGVSGearwayrvsqgrfPASLEYRIVNDGQVMESTDRNEGEIQVRGNWV 395
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2913 SRGYL----DRSGLTAERFTANPYGTAGQRM-----YRTGDVVRWTPDtdtGGLTLEytGRSDDQVKLRGLRIELGEIEA 2983
Cdd:PRK05620 396 TASYYhsptEEGGGAASTFRGEDVEDANDRFtadgwLRTGDVGSVTRD---GFLTIH--DRARDVIRSGGEWIYSAQLEN 470
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2984 VLAEHDAVESAVVLGVGGS-------VATALAAYIVPVDGAVEvsELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDK 3056
Cdd:PRK05620 471 YIMAAPEVVECAVIGYPDDkwgerplAVTVLAPGIEPTRETAE--RLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDK 548
|
...
gi 1827387616 3057 RAL 3059
Cdd:PRK05620 549 KDL 551
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1061-1530 |
1.02e-09 |
|
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: 63.99 E-value: 1.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1061 EMDYDEFETRTNAI--ARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGI 1138
Cdd:cd05915 22 VHRTTYAEVYQRARrlMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDKVLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1139 TDASTRARLGESSCEWVDLADLEAEAESGDDITDTERNGS--------VRLTNLAYLIYTSGSTGRPKAVGVSHTGIvdF 1210
Cdd:cd05915 102 FDPNLLPLVEAIRGELKTVQHFVVMDEKAPEGYLAYEEALgeeadpvrVPERAACGMAYTTGTTGLPKGVVYSHRAL--V 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1211 VNSLAKITTGTPEDEPdTRILHVASPSFDASMFEMAWAIPAGHTLVIAPQADFAGDALATVLERDEVTDMIITPSVLATV 1290
Cdd:cd05915 180 LHSLAASLVDGTALSE-KDVVLPVVPMFHVNAWCLPYAATLVGAKQVLPGPRLDPASLVELFDGEGVTFTAGVPTVWLAL 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1291 DPERAQYVRNL-----ATGGEACPPELVERWSERGR-RIFNCYGPTE------ATVW-----------ATRSRMTAG--- 1344
Cdd:cd05915 259 ADYLESTGHRLktlrrLVVGGSAAPRSLIARFERMGvEVRQGYGLTEtspvvvQNFVkshleslseeeKLTLKAKTGlpi 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1345 --------KPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGylgrpgqtavsfvadpfgepgaRMYATGDL 1416
Cdd:cd05915 339 plvrlrvaDEEGRPVPKDGKALGEVQLKGPWITGGYYGNEEATRSALTPD----------------------GFFRTGDI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1417 VRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGvestRGGRKHTEVVAYLVAKPGATIDSAAVLD 1496
Cdd:cd05915 397 AVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVA----IPHPKWQERPLAVVVPRGEKPTPEELNE 472
|
490 500 510
....*....|....*....|....*....|....*
gi 1827387616 1497 EAAQHLA-AHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:cd05915 473 HLLKAGFaKWQLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1342-1527 |
1.07e-09 |
|
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: 64.12 E-value: 1.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1342 TAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTA--GLARGYLGRPGQtavsFVADPFGE-PGarMYATGDLVR 1418
Cdd:cd05966 405 TPLKPGSATRPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHER----YEDTYFSKfPG--YYFTGDGAR 478
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1419 VAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATIdSAAVLDEA 1498
Cdd:cd05966 479 RDEDGYYWITGRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEA---IYAFVTLKDGEEP-SDELRKEL 554
|
170 180 190
....*....|....*....|....*....|...
gi 1827387616 1499 AQH----LAAHMVPSQAIVIDEIPLTPAGKLDR 1527
Cdd:cd05966 555 RKHvrkeIGPIATPDKIQFVPGLPKTRSGKIMR 587
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
2592-2919 |
1.55e-09 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 63.49 E-value: 1.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2592 LTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDpdYPA---------ERVASMIEDS 2662
Cdd:PRK09192 50 LPYQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPLP--LPMgfggresyiAQLRGMLASA 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2663 GAVLGLSVLASGDLPGQEFEWMRLDDDSVAAEIAAVPAGPITdaerLGEVTAANLAYVIYTSGSTGRPKGVAVTH-SGLA 2741
Cdd:PRK09192 128 QPAAIITPDELLPWVNEATHGNPLLHVLSHAWFKALPEADVA----LPRPTPDDIAYLQYSSGSTRFPRGVIITHrALMA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2742 NFARQESDRLN--AGDNPV----------VLGF--------------ASPSFDASVLEYL-LATVNEGTLAYRPSeaVGG 2794
Cdd:PRK09192 204 NLRAISHDGLKvrPGDRCVswlpfyhdmgLVGFlltpvatqlsvdylPTRDFARRPLQWLdLISRNRGTISYSPP--FGY 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2795 EVLERFIAEhgATHTFLTPSvlstmdptavpSLRVIAAGGEAVPQPI----VDRWAPA----TELHNLYGPTETTIGITI 2866
Cdd:PRK09192 282 ELCARRVNS--KDLAELDLS-----------CWRVAGIGADMIRPDVlhqfAEAFAPAgfddKAFMPSYGLAEATLAVSF 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2867 SS--------------------AMRPGDP-------VRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDR 2919
Cdd:PRK09192 349 SPlgsgivveevdrdrleyqgkAVAPGAEtrrvrtfVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYFRD 428
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
2703-3000 |
1.56e-09 |
|
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: 63.28 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2703 ITDAERLGEVtAANLAYVIYTSGSTGRPKGVAVTHSGLANFARQESDRLNAGDNPVVLGFASPSFDASVLEYLLATVNEG 2782
Cdd:cd05908 95 ITEEEVLCEL-ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILNSTEWKTKDRILSWMPLTHDMGLIAFHLAPLIAG 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2783 TLAY---------RPSEAVggevleRFIAEHGATHT----FLTPSVLSTMDPTA-----VPSLRVIAAGGEAVPQPIVDR 2844
Cdd:cd05908 174 MNQYlmptrlfirRPILWL------KKASEHKATIVsspnFGYKYFLKTLKPEKandwdLSSIRMILNGAEPIDYELCHE 247
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2845 WAPATELHNL--------YGPTETTIGITISSAMRP-------------GDP--------------VRLGGPIGGVDLMV 2889
Cdd:cd05908 248 FLDHMSKYGLkrnailpvYGLAEASVGASLPKAQSPfktitlgrrhvthGEPepevdkkdsecltfVEVGKPIDETDIRI 327
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2890 LDERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDV--VRwtpdtdTGGLTLeyTGRSDD 2967
Cdd:cd05908 328 CDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTDDGW-------LKTGDLgfIR------NGRLVI--TGREKD 392
|
330 340 350
....*....|....*....|....*....|...
gi 1827387616 2968 QVKLRGLRIELGEIEAVLAEHDAVESAVVLGVG 3000
Cdd:cd05908 393 IIFVNGQNVYPHDIERIAEELEGVELGRVVACG 425
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1064-1511 |
1.96e-09 |
|
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: 63.08 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLA-RGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGITDAS 1142
Cdd:cd05938 8 YRDVDRRSNQAARALLAhAGLRPGDTVALLLGNEPAFLWIWLGLAKLGCPVAFLNTNIRSKSLLHCFRCCGAKVLVVAPE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1143 TRARL------------------GESSCEWVDlADLEAEAESGDDITDTERNGSVRLTNLAYLIYTSGSTGRPKAVGVSH 1204
Cdd:cd05938 88 LQEAVeevlpalradgvsvwylsHTSNTEGVI-SLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLPKAARISH 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1205 TGIV--DFVNSLAKITTgtpEDepdtrILHVASPSF--DASMFEMAWAIPAGHTLVIAPQadFAGDALATVLERDEVTDM 1280
Cdd:cd05938 167 LRVLqcSGFLSLCGVTA---DD-----VIYITLPLYhsSGFLLGIGGCIELGATCVLKPK--FSASQFWDDCRKHNVTVI 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1281 iitpsvlatvdperaQYVrnlatgGEAC------PPELVER----------------WSERGRR-----IFNCYGPTEAT 1333
Cdd:cd05938 237 ---------------QYI------GELLrylcnqPQSPNDRdhkvrlaignglradvWREFLRRfgpirIREFYGSTEGN 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1334 VwatrSRMT-AGKPVTIGK---------PVD--------GFTVRVLDGRLHEVPQGVVGELYLSTAGLA--RGYLGRPGQ 1393
Cdd:cd05938 296 I----GFFNyTGKIGAVGRvsylykllfPFElikfdvekEEPVRDAQGFCIPVAKGEPGLLVAKITQQSpfLGYAGDKEQ 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1394 TAVSFVADPFgEPGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVesTRGGRK 1473
Cdd:cd05938 372 TEKKLLRDVF-KKGDVYFNTGDLLVQDQQNFLYFHDRVGDTFRWKGENVATTEVADVLGLLDFLQEVNVYGV--TVPGHE 448
|
490 500 510
....*....|....*....|....*....|....*...
gi 1827387616 1474 HTEVVAYLVAKPGATIDsaavLDEAAQHLaAHMVPSQA 1511
Cdd:cd05938 449 GRIGMAAVKLKPGHEFD----GKKLYQHV-REYLPAYA 481
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
128-470 |
1.96e-09 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 63.07 E-value: 1.96e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 128 FTSGSTGRPKAVVITHRGIANRLAADIEQY--DLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAEpGRHGDPVHLA 205
Cdd:PLN02330 191 FSSGTTGISKGVMLTHRNLVANLCSSLFSVgpEMIGQVVTLGLIPFFHIYGITGICCATLRNKGKVVVM-SRFELRTFLN 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 206 DLIRrHGVTVIHFVPAMLaaFNEVLGAGVGE--LTSLRL--IQTGGEALTPPVARDLMVRLPGTRLQNQYGPAEASIVVT 281
Cdd:PLN02330 270 ALIT-QEVSFAPIVPPII--LNLVKNPIVEEfdLSKLKLqaIMTAAAPLAPELLTAFEAKFPGVQVQEAYGLTEHSCITL 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 282 IHRVTQDDRVI----PIGTPTRRVSARVLDAAL-REVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlY 356
Cdd:PLN02330 347 THGDPEKGHGIakknSVGFILPNLEVKFIDPDTgRSLPKNTPGELCVRSQCVMQGYYNNKEETDRTIDEDGW-------L 419
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 357 RTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVVDGPggQQLVGYLAPADVDVDTVAATT 436
Cdd:PLN02330 420 HTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPSV--EDAAVVPLP--DEEAGEIPAACVVINPKAKES 495
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 1827387616 437 AELLPEYMRPSAW----VR----LDAMPLSRSGKVDRRLLPE 470
Cdd:PLN02330 496 EEDILNFVAANVAhykkVRvvqfVDSIPKSLSGKIMRRLLKE 537
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
2723-2993 |
2.09e-09 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 62.86 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2723 TSGSTGRPKGVAVTHSGLANFARQESdRL--NAGDNP---VVLGFAspsfdasvleYLLATVneGTLAYRPSEAVGGEVL 2797
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLDRWAELFA-RSlrAAGVRPgdrVQNAFG----------YGLFTG--GLGLHYGAERLGATVI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2798 -------ER---FIAEHGATHTFLTPSVLSTM---------DPTAvPSLRVIAAGGEAVPQP----IVDRWApaTELHNL 2854
Cdd:COG1541 158 pagggntERqlrLMQDFGPTVLVGTPSYLLYLaevaeeegiDPRD-LSLKKGIFGGEPWSEEmrkeIEERWG--IKAYDI 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2855 YGPTETTIGITISSAMRPGdpvrlggpiggvdlMVLDERL-----------RPVPVGMPGELYVaggalsrgyldrSGLT 2923
Cdd:COG1541 235 YGLTEVGPGVAYECEAQDG--------------LHIWEDHflveiidpetgEPVPEGEEGELVV------------TTLT 288
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 2924 AE-----RftanpygtagqrmYRTGDVVRWTPDTDTGGLT---LEY-TGRSDDQVKLRGLRIELGEIEAVLAEHDAVES 2993
Cdd:COG1541 289 KEampliR-------------YRTGDLTRLLPEPCPCGRThprIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVGP 354
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
24-466 |
2.28e-09 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 63.04 E-value: 2.28e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 24 AEVAVGIQIDRSvEQVVAIHAVA-MAGGHFVP----LDEQ-----------LPVDRA-RYMVRTAGvRLVvvtsDGEAEA 86
Cdd:PRK10524 144 ASHSLAARIDDA-KPVLIVSADAgSRGGKVVPykplLDEAialaqhkprhvLLVDRGlAPMARVAG-RDV----DYATLR 217
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 87 RSRFDDIVDVHVLDISSPgdadldeeefagptrpanaAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQ-YDLTARDVF 165
Cdd:PRK10524 218 AQHLGARVPVEWLESNEP-------------------SYILYTSGTTGKPKGVQRDTGGYAVALATSMDTiFGGKAGETF 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 166 LYKAPITFDVSVREI-FLPIAIGATLVIAEpgrhGDPVH-----LADLIRRHGVTVIHFVPA---MLAAFNEVLgAGVGE 236
Cdd:PRK10524 279 FCASDIGWVVGHSYIvYAPLLAGMATIMYE----GLPTRpdagiWWRIVEKYKVNRMFSAPTairVLKKQDPAL-LRKHD 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 237 LTSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASI-VVTIHRvTQDDRVIPIGTPTRRV---SARVLDAALRE 312
Cdd:PRK10524 354 LSSLRALFLAGEPLDEPTASWISEAL-GVPVIDNYWQTETGWpILAIAR-GVEDRPTRLGSPGVPMygyNVKLLNEVTGE 431
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 313 VP-------IGVPGELYLGGVQLARGyagrpdlTAERFVADPFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQ 385
Cdd:PRK10524 432 PCgpnekgvLVIEGPLPPGCMQTVWG-------DDDRFVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVAGH 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 386 RLELGEVEAALAAAPGVlhAAAAVV---DGPGGQQLVGYLAPADVDVDTVAATTAELLPEYM-----------RPSAWVR 451
Cdd:PRK10524 505 RLGTREIEESISSHPAV--AEVAVVgvkDALKGQVAVAFVVPKDSDSLADREARLALEKEIMalvdsqlgavaRPARVWF 582
|
490
....*....|....*
gi 1827387616 452 LDAMPLSRSGKVDRR 466
Cdd:PRK10524 583 VSALPKTRSGKLLRR 597
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
2713-3013 |
2.49e-09 |
|
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: 63.00 E-value: 2.49e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2713 TAANLAYVIYTSGSTGRPKGVAVTH----SGLANFARQESDRLNAGDNPVVLGFASPS--FDASVLEYLLA--------- 2777
Cdd:cd05927 112 KPEDLATICYTSGTTGNPKGVMLTHgnivSNVAGVFKILEILNKINPTDVYISYLPLAhiFERVVEALFLYhgakigfys 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2778 ----TVNEGTLAYRPS-------------EAVGGEV-----LERFI-------------AEHGATHTFLTPSVLSTMDPT 2822
Cdd:cd05927 192 gdirLLLDDIKALKPTvfpgvprvlnriyDKIFNKVqakgpLKRKLfnfalnyklaelrSGVVRASPFWDKLVFNKIKQA 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2823 AVPSLRVIAAGGEAVPQPIVD--RWAPATELHNLYGPTETTIGITISsamRPGDPV--RLGGPIGGVDLmvldeRLRPVP 2898
Cdd:cd05927 272 LGGNVRLMLTGSAPLSPEVLEflRVALGCPVLEGYGQTECTAGATLT---LPGDTSvgHVGGPLPCAEV-----KLVDVP 343
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2899 -----VGMP---GELYVAGGALSRGYLDRSGLTAERFTANPYgtagqrmYRTGDVVRWTPDtdtGGLTLeyTGRSDDQVK 2970
Cdd:cd05927 344 emnydAKDPnprGEVCIRGPNVFSGYYKDPEKTAEALDEDGW-------LHTGDIGEWLPN---GTLKI--IDRKKNIFK 411
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 1827387616 2971 L-RGLRIELGEIEAVLAEHDAVESAVVLgvGGSVATALAAYIVP 3013
Cdd:cd05927 412 LsQGEYVAPEKIENIYARSPFVAQIFVY--GDSLKSFLVAIVVP 453
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
2556-3053 |
2.65e-09 |
|
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: 63.06 E-value: 2.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2556 VTGGPATDPV-----TL--AE--LFRAAARRAPDHVAVVDGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRS 2626
Cdd:cd05943 54 VSGRIMPGARwfpgaRLnyAEnlLRHADADDPAAIYAAEDGERTEVTWAELRRRVARLAAALRALGVKPGDRVAGYLPNI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2627 AQLLTAIWAVAKTGGAYVPIDPDYPAERVA---SMIE------DSGAV---------------------LGLSVLASGDL 2676
Cdd:cd05943 134 PEAVVAMLATASIGAIWSSCSPDFGVPGVLdrfGQIEpkvlfaVDAYTyngkrhdvrekvaelvkglpsLLAVVVVPYTV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2677 PGQEFEWMRLDDDSVAAEIAAVPAGPITDAERLGevtAANLAYVIYTSGSTGRPKGVAVTHSG-----LANFARQeSDrL 2751
Cdd:cd05943 214 AAGQPDLSKIAKALTLEDFLATGAAGELEFEPLP---FDHPLYILYSSGTTGLPKCIVHGAGGtllqhLKEHILH-CD-L 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2752 NAGD-------------NPVVLGFASpsfDASVLEYllatvnEGTLAYRPseavgGEVLERFIAEHGATH-----TFLTP 2813
Cdd:cd05943 289 RPGDrlfyyttcgwmmwNWLVSGLAV---GATIVLY------DGSPFYPD-----TNALWDLADEEGITVfgtsaKYLDA 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2814 SVLSTMDPTAV---PSLRVIAAGGEAVPQP----IVDRWAPATELHNLYGPTETtigITISSAMRPGDPVRLG---GPIG 2883
Cdd:cd05943 355 LEKAGLKPAEThdlSSLRTILSTGSPLKPEsfdyVYDHIKPDVLLASISGGTDI---ISCFVGGNPLLPVYRGeiqCRGL 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2884 GVDLMVLDERLRPVpVGMPGELYVAGGALSR-----GYLDRSGLTAERFTANPygtagqRMYRTGDVVRWTPDtdtGGLT 2958
Cdd:cd05943 432 GMAVEAFDEEGKPV-WGEKGELVCTKPFPSMpvgfwNDPDGSRYRAAYFAKYP------GVWAHGDWIEITPR---GGVV 501
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2959 LeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGV---GGSVATALaaYIVPVDGAVEVSEL-----KAFAGGR 3030
Cdd:cd05943 502 I--LGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQewkDGDERVIL--FVKLREGVELDDELrkrirSTIRSAL 577
|
570 580
....*....|....*....|...
gi 1827387616 3031 LPAYmVPSSFTVIDELPLTPVGK 3053
Cdd:cd05943 578 SPRH-VPAKIIAVPDIPRTLSGK 599
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1184-1465 |
3.69e-09 |
|
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: 62.06 E-value: 3.69e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1184 LAYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDEpdtriLHVASPSFDASMFEMAWA--IPAGHTLVIAPQ- 1260
Cdd:cd05937 89 PAILIYTSGTTGLPKAAAISWRRTLVTSNLLSHDLNLKNGDR-----TYTCMPLYHGTAAFLGACncLMSGGTLALSRKf 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1261 --ADFAGDALAT----VLERDEVTDMIItpSVLATVDpERAQYVRnLATGgEACPPELVERWSERgrriFNC------YG 1328
Cdd:cd05937 164 saSQFWKDVRDSgatiIQYVGELCRYLL--STPPSPY-DRDHKVR-VAWG-NGLRPDIWERFRER----FNVpeigefYA 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1329 PTEATVWAT---RSRMTAGK-----------------PVTIG--------KPVDGFTVRVLDGRlhevPQGVVGELYLST 1380
Cdd:cd05937 235 ATEGVFALTnhnVGDFGAGAighhglirrwkfenqvvLVKMDpetddpirDPKTGFCVRAPVGE----PGEMLGRVPFKN 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1381 AGLARGYLGRPGQTAVSFVADPFgEPGARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQS 1460
Cdd:cd05937 311 REAFQGYLHNEDATESKLVRDVF-RKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEA 389
|
....*
gi 1827387616 1461 VVVGV 1465
Cdd:cd05937 390 NVYGV 394
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
1185-1535 |
4.13e-09 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 62.42 E-value: 4.13e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1185 AYLIYTSGSTGRPKAVGVSHTGIVDFVNSLAKITTGTPEDepdtRILHvASPSFDASMFEMAWAIP--AGHTLVIAPQAD 1262
Cdd:PRK08043 368 ALILFTSGSEGHPKGVVHSHKSLLANVEQIKTIADFTPND----RFMS-ALPLFHSFGLTVGLFTPllTGAEVFLYPSPL 442
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1263 FAGDALATVLERDeVTDMIITPSVLATV-------DPERAQYVrnlATGGEACPPELVERWSER-GRRIFNCYGPTE-AT 1333
Cdd:PRK08043 443 HYRIVPELVYDRN-CTVLFGTSTFLGNYarfanpyDFARLRYV---VAGAEKLQESTKQLWQDKfGLRILEGYGVTEcAP 518
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1334 VWATRSRMtAGKPVTIGKPVDGftvrvLDGRLHEVP---QGvvGELYLSTAGLARGYL--GRPGQTAVSFVADPFGEPGA 1408
Cdd:PRK08043 519 VVSINVPM-AAKPGTVGRILPG-----MDARLLSVPgieQG--GRLQLKGPNIMNGYLrvEKPGVLEVPTAENARGEMER 590
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1409 RMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAV-LDAQPGVAQSVVVGVESTRGgrkhTEVVAYlvakpga 1487
Cdd:PRK08043 591 GWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLaLGVSPDKQHATAIKSDASKG----EALVLF------- 659
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 1488 TIDSAAVLDEAAQHLAAHMVPSQAI-----VIDEIPLTPAGKLDRAAL------PEPHA 1535
Cdd:PRK08043 660 TTDSELTREKLQQYAREHGVPELAVprdirYLKQLPLLGSGKPDFVTLksmvdePEQHD 718
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
4-413 |
4.46e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 61.89 E-value: 4.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVtsDGE 83
Cdd:PRK08162 47 AETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFMLRHGEAKVLIV--DTE 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 -----AEARSRFD--DIVDVHVLDISSPGDA---DLDEEEFA-------GPTRPANA--AFTL-FTSGSTGRPKAVVITH 143
Cdd:PRK08162 125 faevaREALALLPgpKPLVIDVDDPEYPGGRfigALDYEAFLasgdpdfAWTLPADEwdAIALnYTSGTTGNPKGVVYHH 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 144 RGIANRLAADIEQYDLTARDVFLYKAPI------TFDVSVreiflpIAIGATLVIAepgRHGDPVHLADLIRRHGVTviH 217
Cdd:PRK08162 205 RGAYLNALSNILAWGMPKHPVYLWTLPMfhcngwCFPWTV------AARAGTNVCL---RKVDPKLIFDLIREHGVT--H 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 218 F-----VPAMLAAFNEVLGAGVGELTSlrlIQTGGEAltPPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVTQDDRVI 292
Cdd:PRK08162 274 YcgapiVLSALINAPAEWRAGIDHPVH---AMVAGAA--PPAAVIAKMEEIGFDLTHVYGLTETYGPATVCAWQPEWDAL 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 293 PIGTPTRRVS-----------ARVLDAA-LREVP-----IgvpGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarl 355
Cdd:PRK08162 349 PLDERAQLKArqgvryplqegVTVLDPDtMQPVPadgetI---GEIMFRGNIVMKGYLKNPKATEEAFAGGWF------- 418
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 356 yRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLhaAAAVVDGP 413
Cdd:PRK08162 419 -HTGDLAVLHPDGYIKIKDRSKDIIISGGENISSIEVEDVLYRHPAVL--VAAVVAKP 473
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
3080-3142 |
4.68e-09 |
|
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: 55.72 E-value: 4.68e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 3080 IADVAAGVLNIDAG-LVSATSSFFELGGDSLSAARLAARLSDQLGVAVSVRDVFESGSIRALAE 3142
Cdd:smart00823 17 VREQVAAVLGHAAAeAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAE 80
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
2-363 |
4.84e-09 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 62.06 E-value: 4.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPV-----DRARYMVRTAGVRLV 76
Cdd:cd05921 27 TYAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLmsqdlAKLKHLFELLKPGLV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 77 VVtSDGEAEARSrFDDIVDVHVLDISSPGDAD----------------LDEEEFAGPTRPANAAFTLFTSGSTGRPKAVV 140
Cdd:cd05921 107 FA-QDAAPFARA-LAAIFPLGTPLVVSRNAVAgrgaisfaelaatpptAAVDAAFAAVGPDTVAKFLFTSGSTGLPKAVI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 141 ITHRGIANRLAADIEQYDLTARD--VFLYKAPITFDVSVREIFLPIAI-GATLVIAE----PGRHGDPVhlaDLIRRHGV 213
Cdd:cd05921 185 NTQRMLCANQAMLEQTYPFFGEEppVLVDWLPWNHTFGGNHNFNLVLYnGGTLYIDDgkpmPGGFEETL---RNLREISP 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 214 TVIHFVPA---MLAAF---NEVLGAGVgeLTSLRLIQTGGEALTPPV---ARDLMVRLPGTRLQ--NQYGPAEASIVVT- 281
Cdd:cd05921 262 TVYFNVPAgweMLVAAlekDEALRRRF--FKRLKLMFYAGAGLSQDVwdrLQALAVATVGERIPmmAGLGATETAPTATf 339
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 282 IHRVTqdDRVIPIGTPTRRVsarvldaALREVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDR 361
Cdd:cd05921 340 THWPT--ERSGLIGLPAPGT-------ELKLVPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF-------YCLGDA 403
|
..
gi 1827387616 362 AR 363
Cdd:cd05921 404 AK 405
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
120-468 |
6.46e-09 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 61.37 E-value: 6.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 120 PANAAFTLFTSGSTGRPKAVVITHRG-IANRLAAdIEQYDLTARDVFLYKAP----ITFDVSVreiFLPIAIGATLVIAE 194
Cdd:PRK06334 182 PEDVAVILFTSGTEKLPKGVPLTHANlLANQRAC-LKFFSPKEDDVMMSFLPpfhaYGFNSCT---LFPLLSGVPVVFAY 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 195 PGRHgdPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQYGPA 274
Cdd:PRK06334 258 NPLY--PKKIVEMIDEAKVTFLGSTPVFFDYILKTAKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIQLRQGYGTT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 275 EASIVVTIHRVTQDDRVIPIGTPTRRVSARVLDAALR-EVPIGVPGELYLGGVQLARGYAGrpdltaerfvADP---FGE 350
Cdd:PRK06334 336 ECSPVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLG----------EDFgqgFVE 405
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 351 -PGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALA---AAPGVLHAAAAVVDG-PGGQQLVGYLAPA 425
Cdd:PRK06334 406 lGGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILMegfGQNAADHAGPLVVCGlPGEKVRLCLFTTF 485
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 1827387616 426 DVDVDTV-----AATTAELlpeyMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK06334 486 PTSISEVndilkNSKTSSI----LKISYHHQVESIPMLGTGKPDYCSL 529
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
4-472 |
6.73e-09 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 61.59 E-value: 6.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLV-----VV 78
Cdd:PRK06710 53 SVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVIlcldlVF 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 79 TSDGEAEARSRFDDIVDVHVLD-ISSPGDA--------------------------DLDEEEFAG---PTRPAN-AAFTL 127
Cdd:PRK06710 133 PRVTNVQSATKIEHVIVTRIADfLPFPKNLlypfvqkkqsnlvvkvsesetihlwnSVEKEVNTGvevPCDPENdLALLQ 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 128 FTSGSTGRPKAVVITHRG-IANRLAADIEQYD-LTARDVFLYKAPITFDVSVREIF-LPIAIGATLVIAEpgrHGDPVHL 204
Cdd:PRK06710 213 YTGGTTGFPKGVMLTHKNlVSNTLMGVQWLYNcKEGEEVVLGVLPFFHVYGMTAVMnLSIMQGYKMVLIP---KFDMKMV 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 205 ADLIRRHGVTVIHFVPAM-LAAFNEVLGAGVgELTSLRLIQTGGEALtPPVARDLMVRLPGTRLQNQYGPAEASIVVtiH 283
Cdd:PRK06710 290 FEAIKKHKVTLFPGAPTIyIALLNSPLLKEY-DISSIRACISGSAPL-PVEVQEKFETVTGGKLVEGYGLTESSPVT--H 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 284 RVTQDDRVIP--IGTPTRRVSARVLDAALREV-PIGVPGELYLGGVQLARGYAGRPDLTAErFVADPFgepgarlYRTGD 360
Cdd:PRK06710 366 SNFLWEKRVPgsIGVPWPDTEAMIMSLETGEAlPPGEIGEIVVKGPQIMKGYWNKPEETAA-VLQDGW-------LHTGD 437
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 361 RARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGP-GGQQLVGYLAPADVDV---DTVAATT 436
Cdd:PRK06710 438 VGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEKVQEVVTIGVPDPyRGETVKAFVVLKEGTEcseEELNQFA 517
|
490 500 510
....*....|....*....|....*....|....*.
gi 1827387616 437 AELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEPE 472
Cdd:PRK06710 518 RKYLAAYKVPKVYEFRDELPKTTVGKILRRVLIEEE 553
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
2719-3059 |
7.39e-09 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 61.50 E-value: 7.39e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2719 YVIYTSGSTGRPKGVAVTHSGLAnFARQESDRLNAGDNPVVLGFASPSFDASV---------LEYLLATV-NEGtLAYRP 2788
Cdd:PRK10524 237 YILYTSGTTGKPKGVQRDTGGYA-VALATSMDTIFGGKAGETFFCASDIGWVVghsyivyapLLAGMATImYEG-LPTRP 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2789 SEAVGGEVLERfiaeHGATHTFLTPS---VLSTMDPTA-----VPSLRVIAAGGE------------AVPQPIVDRwapa 2848
Cdd:PRK10524 315 DAGIWWRIVEK----YKVNRMFSAPTairVLKKQDPALlrkhdLSSLRALFLAGEpldeptaswiseALGVPVIDN---- 386
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2849 telhnlYGPTETtiGITISSAMRPGD--PVRLGGP---IGGVDLMVLDERL-RPVPVGMPGELYVAG----GALSRGYLD 2918
Cdd:PRK10524 387 ------YWQTET--GWPILAIARGVEdrPTRLGSPgvpMYGYNVKLLNEVTgEPCGPNEKGVLVIEGplppGCMQTVWGD 458
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2919 RsgltaERFTANPYGTAGQRMYRTGDvvrWTPDTDTGGLTLeyTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLG 2998
Cdd:PRK10524 459 D-----DRFVKTYWSLFGRQVYSTFD---WGIRDADGYYFI--LGRTDDVINVAGHRLGTREIEESISSHPAVAEVAVVG 528
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 2999 VG----GSVATALAayiVPVDGAVEVSELKAFA---------GGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK10524 529 VKdalkGQVAVAFV---VPKDSDSLADREARLAlekeimalvDSQLGAVARPARVWFVSALPKTRSGKLLRRAI 599
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1061-1513 |
8.37e-09 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 61.43 E-value: 8.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1061 EMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAY---PAD--RIAYMLE----- 1130
Cdd:PRK08180 69 RLTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAYslvSQDfgKLRHVLElltpg 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1131 ----DSGA----------TVGITDASTRARLGESSCewVDLADLEAEAESGDDitdTERNGSVRLTNLAYLIYTSGSTGR 1196
Cdd:PRK08180 149 lvfaDDGAafaralaavvPADVEVVAVRGAVPGRAA--TPFAALLATPPTAAV---DAAHAAVGPDTIAKFLFTSGSTGL 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1197 PKAVGVSHTGIVdfVNSLAKITT-GTPEDEPdTRILHVA--SPSFDASM-FEMAWA------------IPAG--HTL--- 1255
Cdd:PRK08180 224 PKAVINTHRMLC--ANQQMLAQTfPFLAEEP-PVLVDWLpwNHTFGGNHnLGIVLYnggtlyiddgkpTPGGfdETLrnl 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1256 -VIAPQADF---AG-DALATVLERDEvtdmiitpsVLATVDPERaqyVRNLATGGEACPPEL---VERWSER--GRRIFN 1325
Cdd:PRK08180 301 rEISPTVYFnvpKGwEMLVPALERDA---------ALRRRFFSR---LKLLFYAGAALSQDVwdrLDRVAEAtcGERIRM 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1326 C--YGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVldgrlheVPQGvvGELYLSTAG--LARGYLGRPGQTAVSFVAD 1401
Cdd:PRK08180 369 MtgLGMTETAPSATFTTGPLSRAGNIGLPAPGCEVKL-------VPVG--GKLEVRVKGpnVTPGYWRAPELTAEAFDEE 439
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1402 PFgepgarmYATGDLVRVA------KGgnLEFAGRADHQVKI-NGQRVELGEIEA-VLDAQPGVAQSVVVgvestrGGRK 1473
Cdd:PRK08180 440 GY-------YRSGDAVRFVdpadpeRG--LMFDGRIAEDFKLsSGTWVSVGPLRArAVSAGAPLVQDVVI------TGHD 504
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 1827387616 1474 HTEVVAYLVAKPGAtidSAAVLDEAAQHLAAHMVPSQAIV 1513
Cdd:PRK08180 505 RDEIGLLVFPNLDA---CRRLAGLLADASLAEVLAHPAVR 541
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1187-1530 |
8.68e-09 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 61.19 E-value: 8.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1187 LIYTSGSTGRPKAVGVSHTGIvdFVNSLAKITTGTPEDEPdtrILHVASPSFDASMFEMAWAIPA-GHT-----LVIAPQ 1260
Cdd:PLN03102 191 LNYTSGTTADPKGVVISHRGA--YLSTLSAIIGWEMGTCP---VYLWTLPMFHCNGWTFTWGTAArGGTsvcmrHVTAPE 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1261 adfagdaLATVLERDEVTDMIITPSVL-------ATVDPERAQYVRNLaTGGEACPPELVERWSERGRRIFNCYGPTEAT 1333
Cdd:PLN03102 266 -------IYKNIEMHNVTHMCCVPTVFnillkgnSLDLSPRSGPVHVL-TGGSPPPAALVKKVQRLGFQVMHAYGLTEAT 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1334 ------VWATR-SRMTAGKPVTIG--KPVDGFTVRVLDGR----LHEVPQG--VVGELYLSTAGLARGYLGRPGQTAVSF 1398
Cdd:PLN03102 338 gpvlfcEWQDEwNRLPENQQMELKarQGVSILGLADVDVKnketQESVPRDgkTMGEIVIKGSSIMKGYLKNPKATSEAF 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1399 VADPFGepgarmyaTGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKHtevV 1478
Cdd:PLN03102 418 KHGWLN--------TGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYPKVLETAVVAMPHPTWGETP---C 486
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 1479 AYLVAKPGATIDSAAV----------LDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PLN03102 487 AFVVLEKGETTKEDRVdklvtrerdlIEYCRENLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
1407-1531 |
9.90e-09 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 60.44 E-value: 9.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1407 GARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVV-GVESTRGGRkhteVVAYLVAKp 1485
Cdd:PRK08308 289 GDKEIFTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYrGKDPVAGER----VKAKVISH- 363
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1827387616 1486 gATIDSAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKLDRAALP 1531
Cdd:PRK08308 364 -EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| LC_FACS_bac1 |
cd17641 |
bacterial long-chain fatty acid CoA synthetase; The members of this family are bacterial ... |
1061-1464 |
1.46e-08 |
|
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: 60.51 E-value: 1.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1061 EMDYDEFETRTNAIARALLARGVSPEDVVAV-GMERS--IGSVLATWGViksGAAYVPVDPAYPADRIAYMLEDSGATVG 1137
Cdd:cd17641 11 EFTWADYADRVRAFALGLLALGVGRGDVVAIlGDNRPewVWAELAAQAI---GALSLGIYQDSMAEEVAYLLNYTGARVV 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1138 IT-DASTRARLGE-----SSCEWV-----------------DLADLEAEAESGDDITDTERNGSVRLT---NLAYLIYTS 1191
Cdd:cd17641 88 IAeDEEQVDKLLEiadriPSVRYViycdprgmrkyddprliSFEDVVALGRALDRRDPGLYEREVAAGkgeDVAVLCTTS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1192 GSTGRPKAVGVSHTG----------------------------IVDFVNSLAK-ITTGT----PEdEPDT---------- 1228
Cdd:cd17641 168 GTTGKPKLAMLSHGNflghcaaylaadplgpgdeyvsvlplpwIGEQMYSVGQaLVCGFivnfPE-EPETmmedlreigp 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1229 -----------------RILHVASPSFDASMFEmaWAIPAGHtlviapqadfagDALATVLERDEVTDMIITPSVLA--- 1288
Cdd:cd17641 247 tfvllpprvwegiaadvRARMMDATPFKRFMFE--LGMKLGL------------RALDRGKRGRPVSLWLRLASWLAdal 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1289 TVDPERAQ----YVRNLATGGEACPPELVERWSERGRRIFNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVLDgr 1364
Cdd:cd17641 313 LFRPLRDRlgfsRLRSAATGGAALGPDTFRFFHAIGVPLKQLYGQTELAGAYTVHRDGDVDPDTVGVPFPGTEVRIDE-- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1365 lhevpqgvVGELYLSTAGLARGYLGRPGQTAVSFVADPFgepgarmYATGDLVRVAKGGNLEFAGRA-DHQVKINGQRVE 1443
Cdd:cd17641 391 --------VGEILVRSPGVFVGYYKNPEATAEDFDEDGW-------LHTGDAGYFKENGHLVVIDRAkDVGTTSDGTRFS 455
|
490 500
....*....|....*....|.
gi 1827387616 1444 LGEIEAVLDAQPGVAQSVVVG 1464
Cdd:cd17641 456 PQFIENKLKFSPYIAEAVVLG 476
|
|
| PRK07008 |
PRK07008 |
long-chain-fatty-acid--CoA ligase; Validated |
113-470 |
2.35e-08 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235908 [Multi-domain] Cd Length: 539 Bit Score: 59.72 E-value: 2.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 113 EFAGPTRPANAAFTL-FTSGSTGRPKAVVITHRG--IANRLAADIEQYDLTARDVFLYKAPItFDVSVREIFLPIAI-GA 188
Cdd:PRK07008 167 DYDWPRFDENQASSLcYTSGTTGNPKGALYSHRStvLHAYGAALPDAMGLSARDAVLPVVPM-FHVNAWGLPYSAPLtGA 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 189 TLVIaePGRHGDPVHLADLIRRHGVTVIHFVPAM-LAAFNEVLGAGVgELTSLRLIQTGGEALTPPVARDLMVRLpGTRL 267
Cdd:PRK07008 246 KLVL--PGPDLDGKSLYELIEAERVTFSAGVPTVwLGLLNHMREAGL-RFSTLRRTVIGGSACPPAMIRTFEDEY-GVEV 321
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 268 QNQYGPAEASIVVTIHRVTQDDRVIPI----------GTPTRRVSARVLDAALREVPI-GVP-GELYLGGVQLARGYAGR 335
Cdd:PRK07008 322 IHAWGMTEMSPLGTLCKLKWKHSQLPLdeqrkllekqGRVIYGVDMKIVGDDGRELPWdGKAfGDLQVRGPWVIDRYFRG 401
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 336 PdltaerfvADPFGEpgaRLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAA-------- 407
Cdd:PRK07008 402 D--------ASPLVD---GWFPTGDVATIDADGFMQITDRSKDVIKSGGEWISSIDIENVAVAHPAVAEAACiacahpkw 470
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 408 ------AVVDGPGgqqlvgylapADVdvdtvaaTTAELLPEYMRPSA-W------VRLDAMPLSRSGKVDRRLLPE 470
Cdd:PRK07008 471 derpllVVVKRPG----------AEV-------TREELLAFYEGKVAkWwipddvVFVDAIPHTATGKLQKLKLRE 529
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1552-1607 |
2.47e-08 |
|
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: 52.57 E-value: 2.47e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 1552 LARIVAGLLG--EERVSVTESFFALGGDSIMSIQLSSAAKAA-GIHLSPREIFELKTIR 1607
Cdd:pfam00550 3 LRELLAEVLGvpAEEIDPDTDLFDLGLDSLLAVELIARLEEEfGVEIPPSDLFEHPTLA 61
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
319-468 |
2.82e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 58.90 E-value: 2.82e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 319 GELYLGGVQLARGYAGRPDltaerfvADPFGEPGarLYRTGDRARWNrDGEIEYLGRTDFQVKLRGQRLELGEVEAALAA 398
Cdd:PRK07824 208 GRIALGGPTLAKGYRNPVD-------PDPFAEPG--WFRTDDLGALD-DGVLTVLGRADDAISTGGLTVLPQVVEAALAT 277
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 399 APGVlhAAAAVVDGPG---GQQLVGYLAPADVDVDTVAATTAEL---LPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK07824 278 HPAV--ADCAVFGLPDdrlGQRVVAAVVGDGGPAPTLEALRAHVartLDRTAAPRELHVVDELPRRGIGKVDRRAL 351
|
|
| FCS |
cd05921 |
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl ... |
1064-1464 |
3.10e-08 |
|
Feruloyl-CoA synthetase (FCS); Feruloyl-CoA synthetase is an essential enzyme in the feruloyl acid degradation pathway and enables some proteobacteria to grow on media containing feruloyl acid as the sole carbon source. It catalyzes the transfer of CoA to the carboxyl group of ferulic acid, which then forms feruloyl-CoA in the presence of ATP and Mg2. The resulting feruloyl-CoA is further degraded to vanillin and acetyl-CoA. Feruloyl-CoA synthetase (FCS) is a subfamily of the adenylate-forming enzymes superfamily.
Pssm-ID: 341245 [Multi-domain] Cd Length: 561 Bit Score: 59.37 E-value: 3.10e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPA-----DRIAYMLE-------- 1130
Cdd:cd05921 28 YAEALRQVRAIAQGLLDLGLSAERPLLILSGNSIEHALMALAAMYAGVPAAPVSPAYSLmsqdlAKLKHLFEllkpglvf 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1131 --------DSGATVGITD----ASTRARLGESSCEWVDLADLEAEAESgdditdTERNGSVRLTNLAYLIYTSGSTGRPK 1198
Cdd:cd05921 108 aqdaapfaRALAAIFPLGtplvVSRNAVAGRGAISFAELAATPPTAAV------DAAFAAVGPDTVAKFLFTSGSTGLPK 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1199 AVGVSHTGIVdfVNSLAKITTGTPEDEPDTRILHVA--SPSFDASM-FEM------AWAIPAGHTLV------------I 1257
Cdd:cd05921 182 AVINTQRMLC--ANQAMLEQTYPFFGEEPPVLVDWLpwNHTFGGNHnFNLvlynggTLYIDDGKPMPggfeetlrnlreI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1258 APQADF---AG-DALATVLERDEVTdmiitpsvlatvdpeRAQYVRNL---ATGGEACPPELVERWSE-----RGRRI-- 1323
Cdd:cd05921 260 SPTVYFnvpAGwEMLVAALEKDEAL---------------RRRFFKRLklmFYAGAGLSQDVWDRLQAlavatVGERIpm 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1324 FNCYGPTEATVWATRSRMTAGKPVTIGKPVDGFTVRVldgrlheVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPF 1403
Cdd:cd05921 325 MAGLGATETAPTATFTHWPTERSGLIGLPAPGTELKL-------VPSGGKYEVRVKGPNVTPGYWRQPELTAQAFDEEGF 397
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1404 gepgarmYATGDLVRVA------KGgnLEFAGRADHQVKIN-GQRVELGEI--EAVLDAQPGVAQSVVVG 1464
Cdd:cd05921 398 -------YCLGDAAKLAdpddpaKG--LVFDGRVAEDFKLAsGTWVSVGPLraRAVAACAPLVHDAVVAG 458
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
4-468 |
3.13e-08 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 59.11 E-value: 3.13e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVVTSDGE 83
Cdd:PRK09029 32 QQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEELLPSLTLDFALVLEGEN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 84 AearsrFDDIVDVHVLDISSPGDADLDeeefagPTRPAnaafTL-FTSGSTGRPKAVVITHRG-IANrlAADI-EQYDLT 160
Cdd:PRK09029 112 T-----FSALTSLHLQLVEGAHAVAWQ------PQRLA----TMtLTSGSTGLPKAAVHTAQAhLAS--AEGVlSLMPFT 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 161 ARDVFLYKAPItFDVSVREIF---LpiAIGATLVIaepgrhGDPVHLADLIRrhGVTVIHFVPAMLaafnEVLGAGVGEL 237
Cdd:PRK09029 175 AQDSWLLSLPL-FHVSGQGIVwrwL--YAGATLVV------RDKQPLEQALA--GCTHASLVPTQL----WRLLDNRSEP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 238 TSLRLIQTGGEALtpPVARDLMVRLPGTRLQNQYGPAEASIVVTIHRVtqdDRVIPIGTPTrrvsarvldaALREVPIgV 317
Cdd:PRK09029 240 LSLKAVLLGGAAI--PVELTEQAEQQGIRCWCGYGLTEMASTVCAKRA---DGLAGVGSPL----------PGREVKL-V 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 318 PGELYLGGVQLARGY--AGRP-DLTAERfvadpfGepgarLYRTGDRARWNrDGEIEYLGRTDFQVKLRGQRLELGEVEA 394
Cdd:PRK09029 304 DGEIWLRGASLALGYwrQGQLvPLVNDE------G-----WFATRDRGEWQ-NGELTILGRLDNLFFSGGEGIQPEEIER 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 395 ALAAAPGVLHA-AAAVVDGPGGQQlvgylaPADVdVDTVAATTAELLPEYM--------RPSAWVRLDAMpLSRSG-KVD 464
Cdd:PRK09029 372 VINQHPLVQQVfVVPVADAEFGQR------PVAV-VESDSEAAVVNLAEWLqdklarfqQPVAYYLLPPE-LKNGGiKIS 443
|
....
gi 1827387616 465 RRLL 468
Cdd:PRK09029 444 RQAL 447
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1064-1529 |
4.19e-08 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 58.86 E-value: 4.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1064 YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAayVPVDPAYPA---------DRIAYMLEDSGA 1134
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGL--VPVPLPLPMgfggresyiAQLRGMLASAQP 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1135 TVGIT---------DASTRARLGESscewVDLADLEAEAESGDDITDTERNgsvrltNLAYLIYTSGSTGRPKAVGVSHT 1205
Cdd:PRK09192 130 AAIITpdellpwvnEATHGNPLLHV----LSHAWFKALPEADVALPRPTPD------DIAYLQYSSGSTRFPRGVIITHR 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1206 GIvdfVNSLAKITTGTPEDEPDTRILhvaspsfdasmfemAWaIPAGHT-----LVIAPQA-----------DFAGDALA 1269
Cdd:PRK09192 200 AL---MANLRAISHDGLKVRPGDRCV--------------SW-LPFYHDmglvgFLLTPVAtqlsvdylptrDFARRPLQ 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1270 --TVLERDEVTdMIITPSV-------------LATVDPERAqyvRNLATGGEACPPEL----VERWSERG--RRIF-NCY 1327
Cdd:PRK09192 262 wlDLISRNRGT-ISYSPPFgyelcarrvnskdLAELDLSCW---RVAGIGADMIRPDVlhqfAEAFAPAGfdDKAFmPSY 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1328 GPTEATVWAT--------------RSRMTAGKP--------------VTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLS 1379
Cdd:PRK09192 338 GLAEATLAVSfsplgsgivveevdRDRLEYQGKavapgaetrrvrtfVNCGKALPGHEIEIRNEAGMPLPERVVGHICVR 417
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1380 TAGLARGYLGRPgQTAVSFVADPFGEpgarmyaTGDLVRVAkGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGV-A 1458
Cdd:PRK09192 418 GPSLMSGYFRDE-ESQDVLAADGWLD-------TGDLGYLL-DGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELrS 488
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 1459 QSVVVGVESTRGGRKhteVVAYLVAKPGATIDSAAVLDEAAQHL-AAHMVPSQAIVI--DEIPLTPAGKLDRAA 1529
Cdd:PRK09192 489 GDAAAFSIAQENGEK---IVLLVQCRISDEERRGQLIHALAALVrSEFGVEAAVELVppHSLPRTSSGKLSRAK 559
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
128-375 |
4.40e-08 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 59.05 E-value: 4.40e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 128 FTSGSTGRPKAVVITHRGIAN--RLAAdiEQYDLTARD-----VFLYK---------APITFdvsvreiflpiaiGATLV 191
Cdd:PRK08315 206 YTSGTTGFPKGATLTHRNILNngYFIG--EAMKLTEEDrlcipVPLYHcfgmvlgnlACVTH-------------GATMV 270
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 192 IaePGRHGDPVHLADLIRRHGVTVIHFVPAMLAA------FNEVlgagvgELTSLRliqTGGEALTP---PVARDLMVRL 262
Cdd:PRK08315 271 Y--PGEGFDPLATLAAVEEERCTALYGVPTMFIAeldhpdFARF------DLSSLR---TGIMAGSPcpiEVMKRVIDKM 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 263 PGTRLQNQYGPAEASIVVTIHRVtqDD----RVIPIGTPTRRVSARVLDAAL-REVPIGVPGELYLGGVQLARGYAGRPD 337
Cdd:PRK08315 340 HMSEVTIAYGMTETSPVSTQTRT--DDplekRVTTVGRALPHLEVKIVDPETgETVPRGEQGELCTRGYSVMKGYWNDPE 417
|
250 260 270
....*....|....*....|....*....|....*...
gi 1827387616 338 LTAErfVADPfgepgARLYRTGDRARWNRDGEIEYLGR 375
Cdd:PRK08315 418 KTAE--AIDA-----DGWMHTGDLAVMDEEGYVNIVGR 448
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
2934-3060 |
4.47e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 58.51 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2934 TAGQRMYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATALAAYIVP 3013
Cdd:PRK08308 287 KMGDKEIFTKDLGYKSERG-----TLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVI 361
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1827387616 3014 VDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRALP 3060
Cdd:PRK08308 362 SHEEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1543-1607 |
5.97e-08 |
|
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: 52.16 E-value: 5.97e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 1543 APANPAEDNLARIVAGLLG--EERVSVTESFFA-LGGDSIMSIQLSSAAKAA-GIHLSPREIFELKTIR 1607
Cdd:COG0236 1 MPREELEERLAEIIAEVLGvdPEEITPDDSFFEdLGLDSLDAVELIAALEEEfGIELPDTELFEYPTVA 69
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1346-1524 |
7.42e-08 |
|
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: 58.44 E-value: 7.42e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1346 PVTIG---KPVDGFTVRVLDGRLHEVPqGVVGELYLstaglARGYLGRPgqtaVSFVADPFGE----------PGarMYA 1412
Cdd:cd05943 420 PVYRGeiqCRGLGMAVEAFDEEGKPVW-GEKGELVC-----TKPFPSMP----VGFWNDPDGSryraayfakyPG--VWA 487
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1413 TGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhTEVVAYLVAKPGATIDSA 1492
Cdd:cd05943 488 HGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGD---ERVILFVKLREGVELDDE 564
|
170 180 190
....*....|....*....|....*....|....*
gi 1827387616 1493 ---AVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGK 1524
Cdd:cd05943 565 lrkRIRSTIRSALSPRHVPAKIIAVPDIPRTLSGK 599
|
|
| PRK08180 |
PRK08180 |
feruloyl-CoA synthase; Reviewed |
1-364 |
8.08e-08 |
|
feruloyl-CoA synthase; Reviewed
Pssm-ID: 236175 [Multi-domain] Cd Length: 614 Bit Score: 57.97 E-value: 8.08e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQ---LPVDRA--RYMVRTAGVRL 75
Cdd:PRK08180 70 LTYAEALERVRAIAQALLDRGLSAERPLMILSGNSIEHALLALAAMYAGVPYAPVSPAyslVSQDFGklRHVLELLTPGL 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 76 VVVtSDGEAEARSrFDDIVDVHVLDISS----PGDADLDEEEFAGPTRPAN--AAF----------TLFTSGSTGRPKAV 139
Cdd:PRK08180 150 VFA-DDGAAFARA-LAAVVPADVEVVAVrgavPGRAATPFAALLATPPTAAvdAAHaavgpdtiakFLFTSGSTGLPKAV 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 140 VITHRgianRLAADIEQYDLTARDvFLYKAPITFDvsvreiFLP--------------IAIGATLVIAE----PGRhgdp 201
Cdd:PRK08180 228 INTHR----MLCANQQMLAQTFPF-LAEEPPVLVD------WLPwnhtfggnhnlgivLYNGGTLYIDDgkptPGG---- 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 202 vhLADLIR--RHGVTVIHF-VPA---MLAAF---NEVLGAGVgeLTSLRLIQTGGEALTPPVARDLM---VRLPGTRLQ- 268
Cdd:PRK08180 293 --FDETLRnlREISPTVYFnVPKgweMLVPAlerDAALRRRF--FSRLKLLFYAGAALSQDVWDRLDrvaEATCGERIRm 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 269 -NQYGPAEASIVVT-IHRvtQDDRVIPIGTPTRRVSARVldaalreVPIGVPGELYLGGVQLARGYAGRPDLTAERFVAD 346
Cdd:PRK08180 369 mTGLGMTETAPSATfTTG--PLSRAGNIGLPAPGCEVKL-------VPVGGKLEVRVKGPNVTPGYWRAPELTAEAFDEE 439
|
410
....*....|....*...
gi 1827387616 347 PFgepgarlYRTGDRARW 364
Cdd:PRK08180 440 GY-------YRSGDAVRF 450
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1042-1530 |
8.92e-08 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 57.71 E-value: 8.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1042 VLAQRDLDPDHPALI-CDGT-EMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPA 1119
Cdd:PRK05857 20 VFEQARQQPEAIALRrCDGTsALRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1120 YPADRIAYMLEdsgatvgITDAST-----RARLGESSCEWVDLADLEAEAESGDDITDTERNGSVRL--TNLAY------ 1186
Cdd:PRK05857 100 LPIAAIERFCQ-------ITDPAAalvapGSKMASSAVPEALHSIPVIAVDIAAVTRESEHSLDAASlaGNADQgsedpl 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1187 -LIYTSGSTGRPKAVGVSHTGI-----------VDFVNSLAKITTGTPedEPDTRIlhvaspsfdASMFEMAWAIPAGHT 1254
Cdd:PRK05857 173 aMIFTSGTTGEPKAVLLANRTFfavpdilqkegLNWVTWVVGETTYSP--LPATHI---------GGLWWILTCLMHGGL 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1255 LVIAPQadfAGDALATVLERDEVTDMIITPSVL----------ATVDPEraqyVRNLATGGEACPPELVERWSERGRRIF 1324
Cdd:PRK05857 242 CVTGGE---NTTSLLEILTTNAVATTCLVPTLLsklvselksaNATVPS----LRLVGYGGSRAIAADVRFIEATGVRTA 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1325 NCYGPTEATVWA--------TRSRMTAGkpvTIGKPVDGFTVRVL--DGRLHEVPQGV----VGELYLSTAGLARGYLGR 1390
Cdd:PRK05857 315 QVYGLSETGCTAlclptddgSIVKIEAG---AVGRPYPGVDVYLAatDGIGPTAPGAGpsasFGTLWIKSPANMLGYWNN 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1391 PGQTAvSFVADPFgepgarmYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRG 1470
Cdd:PRK05857 392 PERTA-EVLIDGW-------VNTGDLLERREDGFFYIKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEF 463
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 1471 GrkhteVVAYLVAKPGATIDSAAVLdEAAQHLAAH--------MVPSQAIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK05857 464 G-----ALVGLAVVASAELDESAAR-ALKHTIAARfrresepmARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
61-405 |
1.13e-07 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 57.82 E-value: 1.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 61 VDRARYMvRTAGVRLVVVTSDGEAEARSRFDDivdVHVLDISSPGDADLdeeefagpTRPANAAFTLFTSGSTGRPKAVV 140
Cdd:PLN02387 202 VKRVIYM-DDEGVDSDSSLSGSSNWTVSSFSE---VEKLGKENPVDPDL--------PSPNDIAVIMYTSGSTGLPKGVM 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 141 ITHRGIANRLAADIEQY-DLTARDVFLykapitfdvsvreIFLPIA----IGATLVIAEPGR---HGDPVHLADL---IR 209
Cdd:PLN02387 270 MTHGNIVATVAGVMTVVpKLGKNDVYL-------------AYLPLAhileLAAESVMAAVGAaigYGSPLTLTDTsnkIK 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 210 RH--------GVTVIHFVPAML-----------------------AAFNEVLGA------GVGELTSL------------ 240
Cdd:PLN02387 337 KGtkgdasalKPTLMTAVPAILdrvrdgvrkkvdakgglakklfdIAYKRRLAAiegswfGAWGLEKLlwdalvfkkira 416
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 241 ------RLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTIHRVtqDDrvipigTPTRRVSARVLDAALREV- 313
Cdd:PLN02387 417 vlggriRFMLSGGAPLSGDTQRFINICL-GAPIGQGYGLTETCAGATFSEW--DD------TSVGRVGPPLPCCYVKLVs 487
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 314 -PIG--------VP-GELYLGGVQLARGYAGRPDLTAERFVADpfgEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLR 383
Cdd:PLN02387 488 wEEGgylisdkpMPrGEIVIGGPSVTLGYFKNQEKTDEVYKVD---ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQ 564
|
410 420
....*....|....*....|....*..
gi 1827387616 384 -GQRLELGEVEAALAAAPGV----LHA 405
Cdd:PLN02387 565 hGEYVSLGKVEAALSVSPYVdnimVHA 591
|
|
| prpE |
PRK10524 |
propionyl-CoA synthetase; Provisional |
1043-1530 |
1.26e-07 |
|
propionyl-CoA synthetase; Provisional
Pssm-ID: 182517 [Multi-domain] Cd Length: 629 Bit Score: 57.65 E-value: 1.26e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1043 LAQRdldPDHPALICDGTEMD------YDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPV 1116
Cdd:PRK10524 63 LAKR---PEQLALIAVSTETDeertytFRQLHDEVNRMAAMLRSLGVQRGDRVLIYMPMIAEAAFAMLACARIGAIHSVV 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1117 DPAYPADRIAYMLEDSGATVGIT-DASTRA--------------RLGESSCEWVDLAD---LEAEAESGDDI---TDTER 1175
Cdd:PRK10524 140 FGGFASHSLAARIDDAKPVLIVSaDAGSRGgkvvpykplldeaiALAQHKPRHVLLVDrglAPMARVAGRDVdyaTLRAQ 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1176 NGSVRL-------TNLAYLIYTSGSTGRPKAVgVSHTG--IVDFVNSLAKITTGTPEDepdtrilhvaspsfdaSMF--- 1243
Cdd:PRK10524 220 HLGARVpvewlesNEPSYILYTSGTTGKPKGV-QRDTGgyAVALATSMDTIFGGKAGE----------------TFFcas 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1244 EMAWAIpaGHTLVI-APQadFAGdaLATVL-----------------ERDEVTDMIITPS---VLATVDPER-AQY---- 1297
Cdd:PRK10524 283 DIGWVV--GHSYIVyAPL--LAG--MATIMyeglptrpdagiwwrivEKYKVNRMFSAPTairVLKKQDPALlRKHdlss 356
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1298 VRNLATGGEacpP--ELVERW--SERGRRIFNCYGPTEaTVW-----ATRSRMTAGKPVTIGKPVDGFTVRVLDGRLHEV 1368
Cdd:PRK10524 357 LRALFLAGE---PldEPTASWisEALGVPVIDNYWQTE-TGWpilaiARGVEDRPTRLGSPGVPMYGYNVKLLNEVTGEP 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1369 PQ----GVVGelylstaglARGYLgRPG--QTA----VSFVADPFGEPGARMYATGDLVRVAKGGNLEFAGRADHQVKIN 1438
Cdd:PRK10524 433 CGpnekGVLV---------IEGPL-PPGcmQTVwgddDRFVKTYWSLFGRQVYSTFDWGIRDADGYYFILGRTDDVINVA 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1439 GQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVAKPGATIDS--------AAVLDEAAQHLAAHMVPSQ 1510
Cdd:PRK10524 503 GHRLGTREIEESISSHPAVAEVAVVGVKDALKGQV---AVAFVVPKDSDSLADrearlaleKEIMALVDSQLGAVARPAR 579
|
570 580
....*....|....*....|
gi 1827387616 1511 AIVIDEIPLTPAGKLDRAAL 1530
Cdd:PRK10524 580 VWFVSALPKTRSGKLLRRAI 599
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
1642-1950 |
1.33e-07 |
|
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: 57.00 E-value: 1.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1642 WMIEHSEEPAdfADFSQSLVFNVPASAAVADLQTVVEAVAAAHPMLTAVLTRSGDG----WTMNAGAGIVPAVREIDAEG 1717
Cdd:cd19539 12 WFIDQGEDGG--PAYNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDGGvprqEILPPGPAPLEVRDLSDPDS 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1718 ALDPALVDAHRELLGAMDPGTGSLLGTAVV--NGEGRRRLVIAIHHLGVDAVSWPILVEDLVTAWAQLTSGRPIELRPEA 1795
Cdd:cd19539 90 DRERRLEELLRERESRGFDLDEEPPIRAVLgrFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRKGPAAPLPELR 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1796 TTTRRIA-----HLLAGQVharAREVDYWLEQLPE-RPTSFGTSADRPLHRRRDESSLTYVVDDVAGSILTTVPQAFGSS 1869
Cdd:cd19539 170 QQYKEYAawqreALAAPRA---AELLDFWRRRLRGaEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAKRARSS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1870 VDDVLLGALARAVRAW--QLDngiadggpVTVSTEGHGRDESiagdegaiDLSRTVGWFTSITPLAVDASS-----DVVH 1942
Cdd:cd19539 247 LFMVLLAAYCVLLRRYtgQTD--------IVVGTPVAGRNHP--------RFESTVGFFVNLLPLRVDVSDcatfrDLIA 310
|
....*....
gi 1827387616 1943 AV-KSAKDA 1950
Cdd:cd19539 311 RVrKALVDA 319
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
2716-3059 |
1.36e-07 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 57.16 E-value: 1.36e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2716 NLAYVIYTSGSTGRPKGVAVTHSGLAN----FARQESDRLNAGDNPVVLGFASPSFDAsvleYLLATVNEGTLA------ 2785
Cdd:PLN02574 199 DVAAIMYSSGTTGASKGVVLTHRNLIAmvelFVRFEASQYEYPGSDNVYLAALPMFHI----YGLSLFVVGLLSlgstiv 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2786 ----YRPSEAVggEVLERFiaehGATHTFLTPSVLSTMDPTAVP-------SLRVIAAGGEAVPQPIVDRWA---PATEL 2851
Cdd:PLN02574 275 vmrrFDASDMV--KVIDRF----KVTHFPVVPPILMALTKKAKGvcgevlkSLKQVSCGAAPLSGKFIQDFVqtlPHVDF 348
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2852 HNLYGPTETTIGITI---SSAMRPGDPVRLGGPigGVDLMVLD-ERLRPVPVGMPGELYVAGGALSRGYLDRSGLTAERF 2927
Cdd:PLN02574 349 IQGYGMTESTAVGTRgfnTEKLSKYSSVGLLAP--NMQAKVVDwSTGCLLPPGNCGELWIQGPGVMKGYLNNPKATQSTI 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2928 TANPYgtagqrmYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGSVATAL 3007
Cdd:PLN02574 427 DKDGW-------LRTGDIAYFDEDG-----YLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEI 494
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 3008 -AAYIVPVDG-AVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PLN02574 495 pVAFVVRRQGsTLSQEAVINYVAKQVAPYKKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
5-466 |
1.54e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 57.06 E-value: 1.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 5 EFDRRVTGLARELTALGVGAEV-AVGIQIDR--------------SVEQVVAIHAVAMAGGHFVPL-DEQLP--VDRARY 66
Cdd:PRK12476 57 DHSHSAAGCAVELTWTQLGVRLrAVGARLQQvagpgdrvailapqGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDT 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 67 MVRTAGVRLVVVTSDGEAEARSRFDDIVDV---HVLDISSPGDADldEEEFAGPTRPANA-AFTLFTSGSTGRPKAVVIT 142
Cdd:PRK12476 137 ALRDAEPTVVLTTTAAAEAVEGFLRNLPRLrrpRVIAIDAIPDSA--GESFVPVELDTDDvSHLQYTSGSTRPPVGVEIT 214
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 143 HRGIANRLAADIEQYDLTARDVF-LYKAPITFDVSVREIFLPIAIGATLVIAEPgrhgdpvhlADLIRRHGVTV------ 215
Cdd:PRK12476 215 HRAVGTNLVQMILSIDLLDRNTHgVSWLPLYHDMGLSMIGFPAVYGGHSTLMSP---------TAFVRRPQRWIkalseg 285
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 216 IHFVPAMLAAFNEVLgagvgELTSLRLIQTGGEAL----------TPPVARDLMVR---------LPGTRLQNQYGPAEA 276
Cdd:PRK12476 286 SRTGRVVTAAPNFAY-----EWAAQRGLPAEGDDIdlsnvvliigSEPVSIDAVTTfnkafapygLPRTAFKPSYGIAEA 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 277 SIVV-TIH---------------------RVTQD-DRVIP---IGTPTRRVSARVLDAAL-REVPIGVPGELYLGGVQLA 329
Cdd:PRK12476 361 TLFVaTIApdaepsvvyldreqlgagravRVAADaPNAVAhvsCGQVARSQWAVIVDPDTgAELPDGEVGEIWLHGDNIG 440
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 330 RGYAGRPDLTAERFVAD-----PFG------EPGARLYRTGDRARWnRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAA 398
Cdd:PRK12476 441 RGYWGRPEETERTFGAKlqsrlAEGshadgaADDGTWLRTGDLGVY-LDGELYITGRIADLIVIDGRNHYPQDIEATVAE 519
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 399 APGVL---HAAAAVVDGPGGQQLV--GYLAPADVDVD---TVAATTAELLPEYMRPSAWVRL---DAMPLSRSGKVDRR 466
Cdd:PRK12476 520 ASPMVrrgYVTAFTVPAEDNERLVivAERAAGTSRADpapAIDAIRAAVSRRHGLAVADVRLvpaGAIPRTTSGKLARR 598
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
1-468 |
1.75e-07 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 56.94 E-value: 1.75e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1 MSRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLP---VDRARYMVRTAGVrlvV 77
Cdd:PRK05857 42 LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGAIAVMADGNLPiaaIERFCQITDPAAA---L 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 78 VTSDGEAEARSRFDDIVDVHVLDISSPGDA-----DLDEEEFAG-PTRPANAAFTL-FTSGSTGRPKAVVITHR---GIA 147
Cdd:PRK05857 119 VAPGSKMASSAVPEALHSIPVIAVDIAAVTresehSLDAASLAGnADQGSEDPLAMiFTSGTTGEPKAVLLANRtffAVP 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 148 NRLAAD-IEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIAepGRHGdpVHLADLIRRHGVTVIHFVPAMLAAF 226
Cdd:PRK05857 199 DILQKEgLNWVTWVVGETTYSPLPATHIGGLWWILTCLMHGGLCVTG--GENT--TSLLEILTTNAVATTCLVPTLLSKL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 227 NEVLGAGVGELTSLRLIQTGGealTPPVARDL-MVRLPGTRLQNQYGPAEASIVV--------TIHRVTQDdrviPIGTP 297
Cdd:PRK05857 275 VSELKSANATVPSLRLVGYGG---SRAIAADVrFIEATGVRTAQVYGLSETGCTAlclptddgSIVKIEAG----AVGRP 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 298 TRRVSARVLDA--ALREVPIGVP----GELYLGGVQLARGYAGRPDLTAErFVADPFgepgarlYRTGDRARWNRDGEIE 371
Cdd:PRK05857 348 YPGVDVYLAATdgIGPTAPGAGPsasfGTLWIKSPANMLGYWNNPERTAE-VLIDGW-------VNTGDLLERREDGFFY 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 372 YLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGPGGQQLVGY--LAPADVDVDTVAATTAELLPEY------ 443
Cdd:PRK05857 420 IKGRSSEMIICGGVNIAPDEVDRIAEGVSGVREAACYEIPDEEFGALVGLavVASAELDESAARALKHTIAARFrresep 499
|
490 500
....*....|....*....|....*.
gi 1827387616 444 -MRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PRK05857 500 mARPSTIVIVTDIPRTQSGKVMRASL 525
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
2587-3059 |
1.83e-07 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 57.21 E-value: 1.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2587 GAGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERVASMIED----- 2661
Cdd:PLN02654 116 GFDASLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSAESLAQRIVDckpkv 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2662 ----SGAVLGLSVLASGDLPGQEFEWMRLDDDSVAAEIA------------------------AVPAGPIT-DAERlgeV 2712
Cdd:PLN02654 196 vitcNAVKRGPKTINLKDIVDAALDESAKNGVSVGICLTyenqlamkredtkwqegrdvwwqdVVPNYPTKcEVEW---V 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2713 TAANLAYVIYTSGSTGRPKGVAVTHSGLA---------NFARQESD-RLNAGDNPVVLGFASPSFdASVLEYLLATVNEG 2782
Cdd:PLN02654 273 DAEDPLFLLYTSGSTGKPKGVLHTTGGYMvytattfkyAFDYKPTDvYWCTADCGWITGHSYVTY-GPMLNGATVLVFEG 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2783 TLAYrPSEAVGGEVLERFIAEHGATHTFLTPSVLSTMDPTAV----PSLRVIAAGGEAVpQPIVDRWapateLHNLYGPT 2858
Cdd:PLN02654 352 APNY-PDSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTrhsrKSLRVLGSVGEPI-NPSAWRW-----FFNVVGDS 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2859 ETTIG------------ITISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAG---GALSRGYLDRSGLT 2923
Cdd:PLN02654 425 RCPISdtwwqtetggfmITPLPGAWPQKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVKKswpGAFRTLYGDHERYE 504
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2924 AERFTANP-YGTAGQRMYRTGDVVRWtpdtdtggltleYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVESAVVLGVGGS 3002
Cdd:PLN02654 505 TTYFKPFAgYYFSGDGCSRDKDGYYW------------LTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHE 572
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 3003 V-ATALAAYIVPVDGAVEVSELKA----FAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PLN02654 573 VkGQGIYAFVTLVEGVPYSEELRKslilTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
5-409 |
2.85e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 56.28 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 5 EFDRRVTGLARELTALGVGAEV-AVGIQI-------DR-------SVEQVVAIHAVAMAGGHFVPL-DEQLP--VDRARy 66
Cdd:PRK07769 44 DFSTERDGVARDLTWSQFGARNrAVGARLqqvtkpgDRvailapqNLDYLIAFFGALYAGRIAVPLfDPAEPghVGRLH- 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 67 MVRTAGVRLVVVTSDGEAEARSRF--------------DDIVDVHVLDISSPGDADLDeeefagptrpaNAAFTLFTSGS 132
Cdd:PRK07769 123 AVLDDCTPSAILTTTDSAEGVRKFfrarpakerprviaVDAVPDEVGATWVPPEANED-----------TIAYLQYTSGS 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 133 TGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPITFDVSVREIFLPIAIGATLVIA-------EPGRHgdpvhLA 205
Cdd:PRK07769 192 TRIPAGVQITHLNLPTNVLQVIDALEGQEGDRGVSWLPFFHDMGLITVLLPALLGHYITFMspaafvrRPGRW-----IR 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 206 DLIRRHGVTVIHFVPAMLAAFNEVLGAGV---GE----LTSLRLIQTGGEALTPPVARDLM-----VRLPGTRLQNQYGP 273
Cdd:PRK07769 267 ELARKPGGTGGTFSAAPNFAFEHAAARGLpkdGEppldLSNVKGLLNGSEPVSPASMRKFNeafapYGLPPTAIKPSYGM 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 274 AEASIVVTIHRVTQDDRVI---------------PIGTPTR--RVS---------ARVLDA-ALREVPIGVPGELYLGGV 326
Cdd:PRK07769 347 AEATLFVSTTPMDEEPTVIyvdrdelnagrfvevPADAPNAvaQVSagkvgvsewAVIVDPeTASELPDGQIGEIWLHGN 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 327 QLARGYAGRPDLTAERF---VADPFGE-------PGARLYRTGDRARWnRDGEIEYLGRTDFQVKLRG-----QRLELGE 391
Cdd:PRK07769 427 NIGTGYWGKPEETAATFqniLKSRLSEshaegapDDALWVRTGDYGVY-FDGELYITGRVKDLVIIDGrnhypQDLEYTA 505
|
490
....*....|....*...
gi 1827387616 392 VEAALAAAPGVLhAAAAV 409
Cdd:PRK07769 506 QEATKALRTGYV-AAFSV 522
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
1284-1532 |
3.04e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 55.77 E-value: 3.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1284 PSVLATVDPERAQYVRNLAT---GGEACPPELVERWSERGRRIFNCYGPTEatvwatrsrmTAGKPVTIgKPVDGFTVRV 1360
Cdd:PRK07445 215 PTQLQRLLQLRPQWLAQFRTillGGAPAWPSLLEQARQLQLRLAPTYGMTE----------TASQIATL-KPDDFLAGNN 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1361 LDGRL--H---EVPQGVVGELYLSTAGLARGYLgrpgqtavsfvadPFGEPGARMYATGDLVRVAKGGNLEFAGRADHQV 1435
Cdd:PRK07445 284 SSGQVlpHaqiTIPANQTGNITIQAQSLALGYY-------------PQILDSQGIFETDDLGYLDAQGYLHILGRNSQKI 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1436 KINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKhteVVAYLVakPGATIDSAAVLDEA-AQHLAAHMVPSQAIVI 1514
Cdd:PRK07445 351 ITGGENVYPAEVEAAILATGLVQDVCVLGLPDPHWGEV---VTAIYV--PKDPSISLEELKTAiKDQLSPFKQPKHWIPV 425
|
250
....*....|....*...
gi 1827387616 1515 DEIPLTPAGKLDRAALPE 1532
Cdd:PRK07445 426 PQLPRNPQGKINRQQLQQ 443
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
1635-2069 |
3.60e-07 |
|
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: 56.40 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1635 PLPPVTSWMIEHSEEPADFADFSQSLVFNVPASAAVADLQTVVEAVAAAHPMLTAVLTRSGDGWTMNAGAGIVPAVREID 1714
Cdd:COG1020 23 AQQRLWLLLLLLLGSAAYNLALALLLLGLLLVAALLLLAALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVD 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1715 AEG-ALDPALVDAHRELLGAMDPGTGSLL-GTAVVNGEGRRRLVIAIHHLGVDAVSWPILVEDLVTAWAQLTSGRPIELR 1792
Cdd:COG1020 103 LEAlAEAAAEAAAAAEALAPFDLLRGPLLrLLLLLLLLLLLLLLLALHHIISDGLSDGLLLAELLRLYLAAYAGAPLPLP 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1793 PEATT--TRRIAHLLAGQVHARAREVDYWLEQLPERPTSFGTSADRPLHRRRDES--SLTYVVDDVAGSILTTVPQAFGS 1868
Cdd:COG1020 183 PLPIQyaDYALWQREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRgaRVSFRLPAELTAALRALARRHGV 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1869 SVDDVLLGALARAVRAWqldNGIADggpVTVSTEGHGRDESiagdegaiDLSRTVGWFTSITPLAVDAS-----SDVVHA 1943
Cdd:COG1020 263 TLFMVLLAAFALLLARY---SGQDD---VVVGTPVAGRPRP--------ELEGLVGFFVNTLPLRVDLSgdpsfAELLAR 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1944 VKSAKDARLSRPAggVGFGILR--YNSDGEIAHRPLPTIMYNYfgggtapstETAPDDFLpvsDRPNMPSSITGAMRSPS 2021
Cdd:COG1020 329 VRETLLAAYAHQD--LPFERLVeeLQPERDLSRNPLFQVMFVL---------QNAPADEL---ELPGLTLEPLELDSGTA 394
|
410 420 430 440
....*....|....*....|....*....|....*....|....*...
gi 1827387616 2022 VFGINISTAGREERrLEAKVTYATDALDEAAASDIARRWHDELRAVVE 2069
Cdd:COG1020 395 KFDLTLTVVETGDG-LRLTLEYNTDLFDAATIERMAGHLVTLLEALAA 441
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
2575-2742 |
4.16e-07 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 55.65 E-value: 4.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2575 ARRAPDHVAVVDGaGARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAER 2654
Cdd:PRK09029 13 AQVRPQAIALRLN-DEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPL 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2655 VASMIEDSGAVLGlsvlasgdLPGQEFEWMRLDDDSVAAEIAAVPAGPItDAERlgevtaanLAYVIYTSGSTGRPKGVA 2734
Cdd:PRK09029 92 LEELLPSLTLDFA--------LVLEGENTFSALTSLHLQLVEGAHAVAW-QPQR--------LATMTLTSGSTGLPKAAV 154
|
....*....
gi 1827387616 2735 VTHSG-LAN 2742
Cdd:PRK09029 155 HTAQAhLAS 163
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
2686-2996 |
6.76e-07 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 55.12 E-value: 6.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2686 LDDDSVAAEIAAVPAG-----PITDAERLGEVT--------AANLAYVIYTSGSTGRPKGVAVTHSG-LANFARQESDRL 2751
Cdd:PLN02387 208 MDDEGVDSDSSLSGSSnwtvsSFSEVEKLGKENpvdpdlpsPNDIAVIMYTSGSTGLPKGVMMTHGNiVATVAGVMTVVP 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2752 NAGDNPVVLGFAsPSfdASVLEylLATvnEGTLAyrpseAVGGEVlerfiaEHGATHTFL---------TPSVLSTMDPT 2822
Cdd:PLN02387 288 KLGKNDVYLAYL-PL--AHILE--LAA--ESVMA-----AVGAAI------GYGSPLTLTdtsnkikkgTKGDASALKPT 349
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2823 ---AVPSL----------RVIAAGG--------------EAVPQPIVDRWAPATELHNL--------------------- 2854
Cdd:PLN02387 350 lmtAVPAIldrvrdgvrkKVDAKGGlakklfdiaykrrlAAIEGSWFGAWGLEKLLWDAlvfkkiravlggrirfmlsgg 429
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2855 ----------------------YGPTETTIGITIS-----SAMRPGDPVrlggPIGGVDLMVLDE---RLRPVPvgMP-G 2903
Cdd:PLN02387 430 aplsgdtqrfiniclgapigqgYGLTETCAGATFSewddtSVGRVGPPL----PCCYVKLVSWEEggyLISDKP--MPrG 503
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2904 ELYVAGGALSRGYLDRSGLTAERFTANPYGTagqRMYRTGDVVRWTPDTdtgglTLEYTGRSDDQVKLR-GLRIELGEIE 2982
Cdd:PLN02387 504 EIVIGGPSVTLGYFKNQEKTDEVYKVDERGM---RWFYTGDIGQFHPDG-----CLEIIDRKKDIVKLQhGEYVSLGKVE 575
|
410
....*....|....
gi 1827387616 2983 AVLAEHDAVESAVV 2996
Cdd:PLN02387 576 AALSVSPYVDNIMV 589
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
128-474 |
7.01e-07 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 54.66 E-value: 7.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 128 FTSGSTGRPKAVVITHRGIANRLAADIEQYDLTARDVFLYKAPITFDVSVreiflpiaIGATLVIAEPGR------HGDP 201
Cdd:PRK08308 108 YSSGTTGEPKLIRRSWTEIDREIEAYNEALNCEQDETPIVACPVTHSYGL--------ICGVLAALTRGSkpviitNKNP 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 202 VHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVgeltSLRLIQTGGEALTPPVARDLMVRlpGTRLQNQYGPAEASIVVT 281
Cdd:PRK08308 180 KFALNILRNTPQHILYAVPLMLHILGRLLPGTF----QFHAVMTSGTPLPEAWFYKLRER--TTYMMQQYGCSEAGCVSI 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 282 IHRVTQDDRvipIGTPTRRVSarvLDAALREvpiGVPGELYLggvqlargyagrpdltaerfvadpfgEPGARLYRTGDR 361
Cdd:PRK08308 254 CPDMKSHLD---LGNPLPHVS---VSAGSDE---NAPEEIVV--------------------------KMGDKEIFTKDL 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 362 ARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGPGGQQLVGYLAPADVDVDTVAATT--AEL 439
Cdd:PRK08308 299 GYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPVAGERVKAKVISHEEIDPVQLREwcIQH 378
|
330 340 350
....*....|....*....|....*....|....*
gi 1827387616 440 LPEYMRPSAWVRLDAMPLSRSGKVDRRLLPEPEIA 474
Cdd:PRK08308 379 LAPYQVPHEIESVTEIPKNANGKVSRKLLELGEVT 413
|
|
| PaaK |
COG1541 |
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and ... |
129-416 |
7.30e-07 |
|
Phenylacetate-coenzyme A ligase PaaK, adenylate-forming domain family [Coenzyme transport and metabolism];
Pssm-ID: 441150 [Multi-domain] Cd Length: 423 Bit Score: 54.38 E-value: 7.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 129 TSGSTGRPKAVVITHRGI---ANRLAADIEQYDLTARDVF-------LYKAPITFDVSVReiflpiAIGATLViaePGRH 198
Cdd:COG1541 91 SSGTTGKPTVVGYTRKDLdrwAELFARSLRAAGVRPGDRVqnafgygLFTGGLGLHYGAE------RLGATVI---PAGG 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 199 GDPVHLADLIRRHGVTVIHFVPAMLAAFNEVL---GAGVGELtSLRLIQTGGEALTPPVaRDLMVRLPGTRLQNQYGPAE 275
Cdd:COG1541 162 GNTERQLRLMQDFGPTVLVGTPSYLLYLAEVAeeeGIDPRDL-SLKKGIFGGEPWSEEM-RKEIEERWGIKAYDIYGLTE 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 276 ASIVVTI--------HrVTQDDRVIPIGTP-TRRVsarvldaalreVPIGVPGELYLGGvqlargyagrpdLTAE----- 341
Cdd:COG1541 240 VGPGVAYeceaqdglH-IWEDHFLVEIIDPeTGEP-----------VPEGEEGELVVTT------------LTKEampli 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 342 RfvadpfgepgarlYRTGDRARWNRDGE--------IEY-LGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDG 412
Cdd:COG1541 296 R-------------YRTGDLTRLLPEPCpcgrthprIGRiLGRADDMLIIRGVNVFPSQIEEVLLRIPEVGPEYQIVVDR 362
|
....
gi 1827387616 413 PGGQ 416
Cdd:COG1541 363 EGGL 366
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
1661-2059 |
7.82e-07 |
|
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: 54.23 E-value: 7.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1661 VFNVPASAAVADLQTVVEAVAAAHPML-TAVLTRSGDGWTMnagaGIV-----PAVREI-DAEGALDPALVDAHRELLGA 1733
Cdd:cd19542 27 VFDLDSSVDVERLRNAWRQLVQRHDILrTVFVESSAEGTFL----QVVlksldPPIEEVeTDEDSLDALTRDLLDDPTLF 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1734 MDPGTgSLlgTAVVNGEGRRRLVIAIHHLGVDAVSWPILVEDLvtawAQLTSGRPIelrPEATTTRRIAHLLAGQVHARA 1813
Cdd:cd19542 103 GQPPH-RL--TLLETSSGEVYLVLRISHALYDGVSLPIILRDL----AAAYNGQLL---PPAPPFSDYISYLQSQSQEES 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1814 RevDYWLEQL-PERPTSFGTSADRPLHRRRDESSltyvvdDVAGSILTTVPQAFGSSVDDVLLGALARAVRAW-QLDNgi 1891
Cdd:cd19542 173 L--QYWRKYLqGASPCAFPSLSPKRPAERSLSST------RRSLAKLEAFCASLGVTLASLFQAAWALVLARYtGSRD-- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1892 adggpVTVSTEGHGRDESIAGdegaIDlsRTVGWFTSITPLAVD-----ASSDVVHAVKSAKDArlSRPAGGVGFG-ILR 1965
Cdd:cd19542 243 -----VVFGYVVSGRDLPVPG----ID--DIVGPCINTLPVRVKldpdwTVLDLLRQLQQQYLR--SLPHQHLSLReIQR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1966 ynSDGEIAHRPLPTIMYNYFGGGTAPSTETAPDDFLpvsdrpnmpSSITGAMRSPSVFGINISTAGREerrLEAKVTYAT 2045
Cdd:cd19542 310 --ALGLWPSGTLFNTLVSYQNFEASPESELSGSSVF---------ELSAAEDPTEYPVAVEVEPSGDS---LKVSLAYST 375
|
410
....*....|....
gi 1827387616 2046 DALDEAAASDIARR 2059
Cdd:cd19542 376 SVLSEEQAEELLEQ 389
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
26-402 |
8.56e-07 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 54.77 E-value: 8.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 26 VAVGIQIDRSVEQVVAIhaVAMAGGHFVPLD-EQLPVDRARYMVRTAGVRLVV--------VTSDGEAEARSRFDDI--- 93
Cdd:cd17632 119 VSVPLQAGASAAQLAPI--LAETEPRLLAVSaEHLDLAVEAVLEGGTPPRLVVfdhrpevdAHRAALESARERLAAVgip 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 94 VDVHVLDISSPGDADLDEEEFAGPTRPANAAFtLFTSGSTGRPKAVVITHRGIANR-LAADIEQYDLTARDVFLYKAPIT 172
Cdd:cd17632 197 VTTLTLIAVRGRDLPPAPLFRPEPDDDPLALL-IYTSGSTGTPKGAMYTERLVATFwLKVSSIQDIRPPASITLNFMPMS 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 173 FDVSVREIFLPIAIGAT---------------LVIAEPGRHGDPVHLADLI-RRHGVTVIHFVPAmlAAFNEVLGAGVGe 236
Cdd:cd17632 276 HIAGRISLYGTLARGGTayfaaasdmstlfddLALVRPTELFLVPRVCDMLfQRYQAELDRRSVA--GADAETLAERVK- 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 237 lTSLRLIQTGGEALT-----PPVARDL---MVRLPGTRLQNQYGPAEASIVVTihrvtqDDRVipigtptrrVSARVLDA 308
Cdd:cd17632 353 -AELRERVLGGRLLAavcgsAPLSAEMkafMESLLDLDLHDGYGSTEAGAVIL------DGVI---------VRPPVLDY 416
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 309 ALREVP-IGV--------PGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGD-RARWNRDgEIEYLGRTDF 378
Cdd:cd17632 417 KLVDVPeLGYfrtdrphpRGELLVKTDTLFPGYYKRPEVTAEVFDEDGF-------YRTGDvMAELGPD-RLVYVDRRNN 488
|
410 420
....*....|....*....|....*
gi 1827387616 379 QVKL-RGQRLELGEVEAALAAAPGV 402
Cdd:cd17632 489 VLKLsQGEFVTVARLEAVFAASPLV 513
|
|
| PLN03051 |
PLN03051 |
acyl-activating enzyme; Provisional |
2720-3028 |
8.96e-07 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215552 [Multi-domain] Cd Length: 499 Bit Score: 54.44 E-value: 8.96e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2720 VIYTSGSTGRPKGVAVTHS--------GLANFARQESDRLNAgdnPVVLGFASpsfdASVLEYlLATVNEGTLAYRPSEA 2791
Cdd:PLN03051 124 ILFSSGTTGEPKAIPWTHLsplrcasdGWAHMDIQPGDVVCW---PTNLGWMM----GPWLLY-SAFLNGATLALYGGAP 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2792 VGGEVLErFIAEHGATHTFLTPSVLST--------MDPTAVPSLRVIAAGGEAvPQPIVDRW--------APATElhnLY 2855
Cdd:PLN03051 196 LGRGFGK-FVQDAGVTVLGLVPSIVKAwrhtgafaMEGLDWSKLRVFASTGEA-SAVDDVLWlssvrgyyKPVIE---YC 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2856 GPTETTIGITISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSgLTAER----FTANP 2931
Cdd:PLN03051 271 GGTELASGYISSTLLQPQAPGAFSTASLGTRFVLLNDNGVPYPDDQPCVGEVALAPPMLGASDRL-LNADHdkvyYKGMP 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2932 -YGTAGQRMYRTGDVVRWTPdtdtgGLTLEYTGRSDDQVKLRGLRIELGEIEAVLAEHDAvesavvlgvggSVATALAAY 3010
Cdd:PLN03051 350 mYGSKGMPLRRHGDIMKRTP-----GGYFCVQGRADDTMNLGGIKTSSVEIERACDRAVA-----------GIAETAAVG 413
|
330
....*....|....*...
gi 1827387616 3011 IVPVDGAVEVSELKAFAG 3028
Cdd:PLN03051 414 VAPPDGGPELLVIFLVLG 431
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
391-462 |
9.42e-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: 48.69 E-value: 9.42e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 391 EVEAALAAAPGVLHAAA-AVVDGPGGQQLVGYLAP---ADVDVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGK 462
Cdd:pfam13193 1 EVESALVSHPAVAEAAVvGVPDELKGEAPVAFVVLkpgVELLEEELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
1749-2057 |
1.48e-06 |
|
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: 53.61 E-value: 1.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1749 GEGRRRLVIAIHHLGVDAVSWPILVEDLVTAWAQLTSGRPIELRPEATTTRRIAHLLAgqVHARAREVDYWLEQLPE--- 1825
Cdd:cd19536 123 ERERFLLVISDHHSILDGWSLYLLVKEILAVYNQLLEYKPLSLPPAQPYRDFVAHERA--SIQQAASERYWREYLAGatl 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1826 RPTSFGTSADRPLHRRRDEssltYVVDDVAGSILTTVPQAFGSSVDDVLLGALARAVRAWQldngiaDGGPVTVSTEGHG 1905
Cdd:cd19536 201 ATLPALSEAVGGGPEQDSE----LLVSVPLPVRSRSLAKRSGIPLSTLLLAAWALVLSRHS------GSDDVVFGTVVHG 270
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1906 RDESIAGDEgaidlsRTVGWFTSITPLAVDAS----SDVVHAVKSAKDARLSRPAGGVgfGILRYNSDGEiahrPLPTIM 1981
Cdd:cd19536 271 RSEETTGAE------RLLGLFLNTLPLRVTLSeetvEDLLKRAQEQELESLSHEQVPL--ADIQRCSEGE----PLFDSI 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1982 YNY------FGGGTAPSTETAPDDFLPVSDRPNMPssitgamrspsvfgINISTAGREErRLEAKVTYATDALDEAAASD 2055
Cdd:cd19536 339 VNFrhfdldFGLPEWGSDEGMRRGLLFSEFKSNYD--------------VNLSVLPKQD-RLELKLAYNSQVLDEEQAQR 403
|
..
gi 1827387616 2056 IA 2057
Cdd:cd19536 404 LA 405
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
486-554 |
2.18e-06 |
|
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the prosthetic group of acyl carrier proteins (ACP) in some multienzyme complexes where it serves as a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups.
Pssm-ID: 214834 [Multi-domain] Cd Length: 86 Bit Score: 48.02 E-value: 2.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 486 EETVAGLFAELLGV---ERVGVTDSFFDIGGSSLSAARIAARVSKELGVDVSVRDVFESPSVRGLVHAVSGR 554
Cdd:smart00823 14 LDLVREQVAAVLGHaaaEAIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAEHLAAE 85
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1183-1451 |
2.19e-06 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 53.28 E-value: 2.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1183 NLAYLIYTSGSTGRPKAVGVSHTGIVDfvNSLAKITTGTPEdEPDTRILHVasPSFDASMFEMAWAIP--AGHTLVIA-- 1258
Cdd:PRK06334 184 DVAVILFTSGTEKLPKGVPLTHANLLA--NQRACLKFFSPK-EDDVMMSFL--PPFHAYGFNSCTLFPllSGVPVVFAyn 258
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1259 ---PQ--ADFAGDALATVLERDEV-TDMIITPsvlATVDPERAQYVRNLATGGEACPPELVERWSERGRRI--FNCYGPT 1330
Cdd:PRK06334 259 plyPKkiVEMIDEAKVTFLGSTPVfFDYILKT---AKKQESCLPSLRFVVIGGDAFKDSLYQEALKTFPHIqlRQGYGTT 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1331 EAT-VWATRSRMTAGKPVTIGKPVDGFTVRVLDGRLH-EVPQGVVGELYLSTAGLARGYLGR-PGQTAVSFvadpfgePG 1407
Cdd:PRK06334 336 ECSpVITINTVNSPKHESCVGMPIRGMDVLIVSEETKvPVSSGETGLVLTRGTSLFSGYLGEdFGQGFVEL-------GG 408
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1827387616 1408 ARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVL 1451
Cdd:PRK06334 409 ETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESIL 452
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
2903-3061 |
2.98e-06 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 52.69 E-value: 2.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2903 GELYVAGGALSRGYLdrsgltaerftanPYGTAGQRMYRTGDVVRWtpdtDTGGlTLEYTGRSDDQVKLRGLRIELGEIE 2982
Cdd:PRK07445 302 GNITIQAQSLALGYY-------------PQILDSQGIFETDDLGYL----DAQG-YLHILGRNSQKIITGGENVYPAEVE 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2983 AVLAEHDAVESAVVLGVG----GSVATALAayiVPVDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRA 3058
Cdd:PRK07445 364 AAILATGLVQDVCVLGLPdphwGEVVTAIY---VPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQ 440
|
...
gi 1827387616 3059 LPE 3061
Cdd:PRK07445 441 LQQ 443
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
2577-3059 |
3.13e-06 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 52.68 E-value: 3.13e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2577 RAPDHVAVVDGA-GARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGGAYVPIDPDYPAERV 2655
Cdd:PLN02246 35 EFSDRPCLIDGAtGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVTTTANPFYTPAEI 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2656 ASMIEDSGAVL------------------GLSVLASGDLPGQ--EFEWMRLDDDSVAAEIAAVPAGPITdaerlgevtaa 2715
Cdd:PLN02246 115 AKQAKASGAKLiitqscyvdklkglaeddGVTVVTIDDPPEGclHFSELTQADENELPEVEISPDDVVA----------- 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2716 nlayVIYTSGSTGRPKGVAVTHSGLANFARQESDrlnaGDNP--------VVLGFAsPSFDASVLE-YLLATVNEG-TLA 2785
Cdd:PLN02246 184 ----LPYSSGTTGLPKGVMLTHKGLVTSVAQQVD----GENPnlyfhsddVILCVL-PMFHIYSLNsVLLCGLRVGaAIL 254
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2786 YRPSEAVgGEVLErFIAEHGAT-HTFLTPSVLS-----TMDPTAVPSLRVIAAGgeAVP-----QPIVDRWAPATELHNL 2854
Cdd:PLN02246 255 IMPKFEI-GALLE-LIQRHKVTiAPFVPPIVLAiakspVVEKYDLSSIRMVLSG--AAPlgkelEDAFRAKLPNAVLGQG 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2855 YGPTE--TTIGITISSAMRPGdPVRlGGPIGGV----DLMVLD-ERLRPVPVGMPGELYVAGGALSRGYLDrsgltaerf 2927
Cdd:PLN02246 331 YGMTEagPVLAMCLAFAKEPF-PVK-SGSCGTVvrnaELKIVDpETGASLPRNQPGEICIRGPQIMKGYLN--------- 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2928 taNPYGTAgqrmyRTGDVVRWTPDTDTGgltleYTGRSD-----DQV----KLRGLRIELGEIEAVLAEHDAVESAVVLG 2998
Cdd:PLN02246 400 --DPEATA-----NTIDKDGWLHTGDIG-----YIDDDDelfivDRLkeliKYKGFQVAPAELEALLISHPSIADAAVVP 467
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1827387616 2999 VGGSVATAL-AAYIVPVDGAvEVSE--LKAFAGGRLPAYMVPSSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PLN02246 468 MKDEVAGEVpVAFVVRSNGS-EITEdeIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
312-446 |
3.83e-06 |
|
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: 52.43 E-value: 3.83e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 312 EVPIGVPGE----LYLGGVQLARGYAGRPDLTAERFVADPFgEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRL 387
Cdd:cd05937 293 RAPVGEPGEmlgrVPFKNREAFQGYLHNEDATESKLVRDVF-RKGDIYFRTGDLLRQDADGRWYFLDRLGDTFRWKSENV 371
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 388 ELGEVEAALAAAPGVLHAAAAVVDGPGGQQLVGYLA---------PADVDVDTVAATTAELLPEYMRP 446
Cdd:cd05937 372 STTEVADVLGAHPDIAEANVYGVKVPGHDGRAGCAAitleessavPTEFTKSLLASLARKNLPSYAVP 439
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
125-468 |
3.95e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 52.59 E-value: 3.95e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 125 FTLFTSGSTGRPKAVVITHRGIANRLAADIEQ-YDLTARDVFLYKAP---ITFDVSVreIFLPIAIGATLVIAEPG-RHG 199
Cdd:PLN02654 279 FLLYTSGSTGKPKGVLHTTGGYMVYTATTFKYaFDYKPTDVYWCTADcgwITGHSYV--TYGPMLNGATVLVFEGApNYP 356
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 200 DPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELT--SLRLIQTGGEALTPPVAR-------DLMVRLPGTRLQNQ 270
Cdd:PLN02654 357 DSGRCWDIVDKYKVTIFYTAPTLVRSLMRDGDEYVTRHSrkSLRVLGSVGEPINPSAWRwffnvvgDSRCPISDTWWQTE 436
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 271 YGpaeaSIVVTihrvtqddrVIPIGTPTRRVSAR-----VLDAALREVPIGVPGEL--YL-------GGVQLARGYAGRP 336
Cdd:PLN02654 437 TG----GFMIT---------PLPGAWPQKPGSATfpffgVQPVIVDEKGKEIEGECsgYLcvkkswpGAFRTLYGDHERY 503
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 337 DLTaerfvadpFGEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVVDGP-GG 415
Cdd:PLN02654 504 ETT--------YFKPFAGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAEAAVVGIEHEvKG 575
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 416 QQLVGYLA-----PADVDV-DTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLL 468
Cdd:PLN02654 576 QGIYAFVTlvegvPYSEELrKSLILTVRNQIGAFAAPDKIHWAPGLPKTRSGKIMRRIL 634
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
8-360 |
3.99e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 52.64 E-value: 3.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 8 RRVTGLARELTALGVGAEVAVgIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPV---DRARYMVRTAGVRLVVVTSDGEA 84
Cdd:PRK05850 43 RRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGahdERVSAVLRDTSPSVVLTTSAVVD 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 85 EARSRFDD--------IVDVHVLDISSPGDADLDEEEfagptrPANAAFTLFTSGSTGRPKAVVITHRGianrLAADIEQ 156
Cdd:PRK05850 122 DVTEYVAPqpgqsappVIEVDLLDLDSPRGSDARPRD------LPSTAYLQYTSGSTRTPAGVMVSHRN----VIANFEQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 157 ydlTARDVFLYKA----PITFDVS----------VREIFLPIAIGATLVIAEPgrhgdpvhLADLIRrhgvtvihfvPA- 221
Cdd:PRK05850 192 ---LMSDYFGDTGgvppPDTTVVSwlpfyhdmglVLGVCAPILGGCPAVLTSP--------VAFLQR----------PAr 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 222 ---MLA------------AFNEVLG-------AGVgELTSLRLIQTGGEALTPPVARDLMVR-----LPGTRLQNQYGPA 274
Cdd:PRK05850 251 wmqLLAsnphafsaapnfAFELAVRktsdddmAGL-DLGGVLGIISGSERVHPATLKRFADRfapfnLRETAIRPSYGLA 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 275 EASIVVTIHRVTQDDRVI---------------PIGTPTRRVS--------ARVLDA-ALREVPIGVPGELYLGGVQLAR 330
Cdd:PRK05850 330 EATVYVATREPGQPPESVrfdyeklsaghakrcETGGGTPLVSygsprsptVRIVDPdTCIECPAGTVGEIWVHGDNVAA 409
|
410 420 430
....*....|....*....|....*....|....
gi 1827387616 331 GYAGRPDLTAERF---VADPF-GEPGARLYRTGD 360
Cdd:PRK05850 410 GYWQKPEETERTFgatLVDPSpGTPEGPWLRTGD 443
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
13-375 |
4.80e-06 |
|
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: 52.09 E-value: 4.80e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 13 LARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLDEQLPVDRARYMVRTAGVRLVVV--TSDGEAEARSRF 90
Cdd:cd05932 19 LAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgkLDDWKAMAPGVP 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 91 DDIVDVhvldISSPGDADLDEEEF------------AGPTRPANAAFTLFTSGSTGRPKAVVITHRGIANRLAADIEQYD 158
Cdd:cd05932 99 EGLISI----SLPPPSAANCQYQWddliaqhppleeRPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFAWAAQAGIEHIG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 159 LTARDVFLYKAPITFDVSVREIFLPIAIGATLV-IAEpgrhGDPVHLADLiRRHGVTVIHFVPAMLAAFNE--------- 228
Cdd:cd05932 175 TEENDRMLSYLPLAHVTERVFVEGGSLYGGVLVaFAE----SLDTFVEDV-QRARPTLFFSVPRLWTKFQQgvqdkipqq 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 229 ---------VLGAGVGE--LTSLRLIQT----GGEALTPPVARDLMVRLpGTRLQNQYGPAEASIVVTIHRvTQDDRVIP 293
Cdd:cd05932 250 klnlllkipVVNSLVKRkvLKGLGLDQCrlagCGSAPVPPALLEWYRSL-GLNILEAYGMTENFAYSHLNY-PGRDKIGT 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 294 IGTPTRRVsarvldaalrEVPIGVPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYL 373
Cdd:cd05932 328 VGNAGPGV----------EVRISEDGEILVRSPALMMGYYKDPEATAEAFTADGF-------LRTGDKGELDADGNLTIT 390
|
..
gi 1827387616 374 GR 375
Cdd:cd05932 391 GR 392
|
|
| PaaK |
cd05913 |
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic ... |
2723-2993 |
9.12e-06 |
|
Phenylacetate-CoA ligase (also known as PaaK); PaaK catalyzes the first step in the aromatic degradation pathway, by converting phenylacetic acid (PA) into phenylacetyl-CoA (PA-CoA). Phenylacetate-CoA ligase has been found in proteobacteria as well as gram positive prokaryotes. The enzyme is specifically induced after aerobic growth in a chemically defined medium containing PA or phenylalanine (Phe) as the sole carbon source. PaaKs are members of the adenylate-forming enzyme (AFE) family. However, sequence comparison reveals divergent features of PaaK with respect to the superfamily, including a novel N-terminal sequence.
Pssm-ID: 341239 [Multi-domain] Cd Length: 425 Bit Score: 51.09 E-value: 9.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2723 TSGSTGRPKGVAVTHSGLANFARQES-------------------DRLNAGDNPVVLGfaspsfdasvLEYLLATVnegt 2783
Cdd:cd05913 86 SSGTTGKPTVVGYTKNDLDVWAELVArcldaagvtpgdrvqnaygYGLFTGGLGFHYG----------AERLGALV---- 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2784 layrpsEAVGGEVLER---FIAEHGATHTFLTPSVLSTM---------DPTAVpSLRVIAAGGEAVPQP----IVDRWAp 2847
Cdd:cd05913 152 ------IPAGGGNTERqlqLIKDFGPTVLCCTPSYALYLaeeaeeegiDPREL-SLKVGIFGAEPWTEEmrkrIERRLG- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2848 aTELHNLYGPTETT-IGITISSAMRPGdpvrlggpIGGVDLMVL-----DERLRPVPVGMPGELYVAGgalsrgyLDRSG 2921
Cdd:cd05913 224 -IKAYDIYGLTEIIgPGVAFECEEKDG--------LHIWEDHFIpeiidPETGEPVPPGEVGELVFTT-------LTKEA 287
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1827387616 2922 LTAERftanpygtagqrmYRTGDVVRWTPDTDTGGLTL----EYTGRSDDQVKLRGLRIELGEIEAVLAEHDAVES 2993
Cdd:cd05913 288 MPLIR-------------YRTRDITRLLPGPCPCGRTHrridRITGRSDDMLIIRGVNVFPSQIEDVLLKIPGLGP 350
|
|
| PRK09294 |
PRK09294 |
phthiocerol/phthiodiolone dimycocerosyl transferase; |
2134-2412 |
9.32e-06 |
|
phthiocerol/phthiodiolone dimycocerosyl transferase;
Pssm-ID: 181765 [Multi-domain] Cd Length: 416 Bit Score: 50.86 E-value: 9.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2134 VYVTQTVLsLTGDVDPGRLRSALSELLARQRVLRSGFVRLPSGAAvTVVPAEVTVPWsvidlraedAASLDSRVEEVLAT 2213
Cdd:PRK09294 22 AFTGYTAH-LRGVLDIDALSDAFDALLRAHPVLAAHLEQDSDGGW-ELVADDLLHPG---------IVVVDGDAARPLPE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2214 ERTNPFDMakppLIRVVLVEHGDGAELVVTNHHLLIDGWSSPLVLADLLSLYATGQTfTGSLPGT-------SGRDFADH 2286
Cdd:PRK09294 91 LQLDQGVS----LLALDVVPDDGGARVTLYIHHSIADAHHSASLLDELWSRYTDVVT-TGDPGPIrpqpapqSLEAVLAQ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2287 --ARAVATADVEAGIAAWREVLAPVTEPTlvAPGHEPSADAPPRDHQFSIDVKVTERLEALARNNSTTMATVVQFAWAMF 2364
Cdd:PRK09294 166 rgIRRQALSGAERFMPAMYAYELPPTPTA--AVLAKPGLPQAVPVTRCRLSKAQTSSLAAFGRRHRLTVNALVSAAILLA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 2365 LSRLTGTRTVT--FAETVSGR---SPDIEGMESMVGMFINTIPAVVDVNPDAT 2412
Cdd:PRK09294 244 EWQLRRTPHVPlpYVYPVDLRfrlTPPVAATEGTNLLGAATYLAEIGPDTDIV 296
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
353-470 |
3.10e-05 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 49.61 E-value: 3.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 353 ARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVlhAAAAVV---DGPGGQQLVGYLAPAD--V 427
Cdd:PRK07445 323 QGIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILATGLV--QDVCVLglpDPHWGEVVTAIYVPKDpsI 400
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 1827387616 428 DVDTVAATTAELLPEYMRPSAWVRLDAMPLSRSGKVDRRLLPE 470
Cdd:PRK07445 401 SLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
2566-2743 |
3.92e-05 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 49.17 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2566 TLAELFRAAARRAPDHVAVV--------DGAGARLTYRELDEASDRLARWLIGRGVGPERAVALAiGRSAQLLTAIWAVA 2637
Cdd:PRK05850 2 SVPSLLRERASLQPDDAAFTfidyeqdpAGVAETLTWSQLYRRTLNVAEELRRHGSTGDRAVILA-PQGLEYIVAFLGAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2638 KTGGAYVPIDPDYPA---ERVASMIEDSGAVLglsVLASGDLPGQEFEWMRLDDDSVAAEIAAV-------PAGPitdae 2707
Cdd:PRK05850 81 QAGLIAVPLSVPQGGahdERVSAVLRDTSPSV---VLTTSAVVDDVTEYVAPQPGQSAPPVIEVdlldldsPRGS----- 152
|
170 180 190
....*....|....*....|....*....|....*..
gi 1827387616 2708 RLGEVTAANLAYVIYTSGSTGRPKGVAVTHSGL-ANF 2743
Cdd:PRK05850 153 DARPRDLPSTAYLQYTSGSTRTPAGVMVSHRNViANF 189
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
96-252 |
4.12e-05 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 49.41 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 96 VHVLDISSPGDADLDEEEFAGPTRPANAAFT----------LFTSGSTGRPKAVVITHRGI------ANRLaadieQYDL 159
Cdd:PRK03584 228 LGPAAAAAALPGALLWEDFLAPAEAAELEFEpvpfdhplwiLYSSGTTGLPKCIVHGHGGIllehlkELGL-----HCDL 302
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 160 TARDVFLYkapIT--------FDVSVreiflpIAIGATLVIAE--PGrHGDPVHLADLIRRHGVTVIHFVPAMLAAfneV 229
Cdd:PRK03584 303 GPGDRFFW---YTtcgwmmwnWLVSG------LLVGATLVLYDgsPF-YPDPNVLWDLAAEEGVTVFGTSAKYLDA---C 369
|
170 180
....*....|....*....|....*...
gi 1827387616 230 LGAGV-----GELTSLRLIQTGGEALTP 252
Cdd:PRK03584 370 EKAGLvpgetHDLSALRTIGSTGSPLPP 397
|
|
| PRK05857 |
PRK05857 |
fatty acid--CoA ligase; |
2564-2860 |
4.85e-05 |
|
fatty acid--CoA ligase;
Pssm-ID: 180293 [Multi-domain] Cd Length: 540 Bit Score: 48.85 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2564 PVTLAELFRAAARRAPDHVAV--VDGAGArLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLTAIWAVAKTGG 2641
Cdd:PRK05857 13 PSTVLDRVFEQARQQPEAIALrrCDGTSA-LRYRELVAEVGGLAADLRAQSVSRGSRVLVISDNGPETYLSVLACAKLGA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2642 AYVPIDPDYPAERVA--SMIEDSGAVLglsvLASGDlpgqefewmRLDDDSVAAEIAAVPAGPITDAERLGEVT------ 2713
Cdd:PRK05857 92 IAVMADGNLPIAAIErfCQITDPAAAL----VAPGS---------KMASSAVPEALHSIPVIAVDIAAVTRESEhsldaa 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2714 --AANLAY-------VIYTSGSTGRPKGVAV---THSGLANFARQESdrLNAGDNPVVLGFASPSFDASV--LEYLLATV 2779
Cdd:PRK05857 159 slAGNADQgsedplaMIFTSGTTGEPKAVLLanrTFFAVPDILQKEG--LNWVTWVVGETTYSPLPATHIggLWWILTCL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2780 NEGTLAYRPSEAvGGEVLERFIAEHGAThTFLTPSVLSTM------DPTAVPSLRVIAAGGEAVPQPIVdRWAPATELH- 2852
Cdd:PRK05857 237 MHGGLCVTGGEN-TTSLLEILTTNAVAT-TCLVPTLLSKLvselksANATVPSLRLVGYGGSRAIAADV-RFIEATGVRt 313
|
....*....
gi 1827387616 2853 -NLYGPTET 2860
Cdd:PRK05857 314 aQVYGLSET 322
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
2-252 |
5.10e-05 |
|
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: 49.19 E-value: 5.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2 SRAEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGG----------------HFVPLDEQL--PVDR 63
Cdd:cd05943 100 TWAELRRRVARLAAALRALGVKPGDRVAGYLPNIPEAVVAMLATASIGAiwsscspdfgvpgvldRFGQIEPKVlfAVDA 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 64 ARYMVRTAGVRLVVvtsdgeAEARSRFDDIVD-VHVLDISSPGDADLDE-------EEFAGPTRPANAAFT--------- 126
Cdd:cd05943 180 YTYNGKRHDVREKV------AELVKGLPSLLAvVVVPYTVAAGQPDLSKiakaltlEDFLATGAAGELEFEplpfdhply 253
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 127 -LFTSGSTGRPKAVVITHRGI-ANRLAADIEQYDLTARDVFLYKAPIT-----FDVSvreiflPIAIGATLVI--AEPGr 197
Cdd:cd05943 254 iLYSSGTTGLPKCIVHGAGGTlLQHLKEHILHCDLRPGDRLFYYTTCGwmmwnWLVS------GLAVGATIVLydGSPF- 326
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1827387616 198 HGDPVHLADLIRRHGVTVIHFVPAMLAAFNE--VLGAGVGELTSLRLIQTGGEALTP 252
Cdd:cd05943 327 YPDTNALWDLADEEGITVFGTSAKYLDALEKagLKPAETHDLSSLRTILSTGSPLKP 383
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
1673-1827 |
7.91e-05 |
|
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: 47.87 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1673 LQTVVEAVAAAHPMLTAVLTRSGDGWTMNAGAgiVPAVREIDAEGaLDPALVDAH----RELLGA--MDPGTGSLLGTAV 1746
Cdd:cd19535 42 LERAWNKLIARHPMLRAVFLDDGTQQILPEVP--WYGITVHDLRG-LSEEEAEAAleelRERLSHrvLDVERGPLFDIRL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1747 VN-GEGRRRLVIAIHHLGVDAVSWPILVEDlvtaWAQLTSGRPIELRPEATTTRR-IAHLLAGQVHARAREVDYWLEQLP 1824
Cdd:cd19535 119 SLlPEGRTRLHLSIDLLVADALSLQILLRE----LAALYEDPGEPLPPLELSFRDyLLAEQALRETAYERARAYWQERLP 194
|
...
gi 1827387616 1825 ERP 1827
Cdd:cd19535 195 TLP 197
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
1634-2069 |
1.11e-04 |
|
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor; The DCL-type Condensation (C) domain catalyzes the condensation between a D-aminoacyl/peptidyl-PCP donor and a L-aminoacyl-PCP acceptor. This domain is D-specific for the peptidyl donor and L-specific for the aminoacyl acceptor ((D)C(L)); this is in contrast with the standard LCL domains which catalyze peptide bond formation between two L-amino acids, and the restriction of ribosomes to use only L-amino acids. C domains of nonribosomal peptide synthetases (NRPSs) catalyze peptide bond formation within (usually) large multi-modular enzymatic complexes. NRPS can use a large variety of acyl monomers (approximately 500 different possible monomer substrates as opposed to the 20 standard amino acids in ribosomal protein synthesis) to construct bioactive secondary metabolites of 2 to 18 units long (with various activities such as antibiotic, antifungal, antitumor and immunosuppression). There are various subtypes of C-domains in addition to the LCL- and DCL-types such as starter C-domains which acylate the first amino acid with a beta-hydroxy carboxylic acid, and heterocyclization (Cyc) domains which catalyze both peptide bond formation and cyclization of Cys, Ser, or Thr residues. Typically, an NRPS module consists of an adenylation domain, a peptidyl carrier protein (PCP) domain (also known as thiolation (T) domain) and a C-domain. NRPS modules may also include specialized domains such as the terminal-module thioesterase (Te) domain that releases the product via hydrolysis or macrocyclization and any of various C-domain family members such as the epimerization (E) domain, the ester-bond forming C-domain, dual E/C (epimerization and condensation) domains, and the X-domain. C-domains typically have a conserved HHxxxD motif at the active site; mutations in this motif can abolish or diminish condensation activity.
Pssm-ID: 380465 [Multi-domain] Cd Length: 423 Bit Score: 47.58 E-value: 1.11e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1634 MPLPPVTSWMIEHS-EEPADFADFSQSlVFNVPASAAVADLQTVVEAVAAAHPMLTAVLTRSGDGWTMNagagIVPA--- 1709
Cdd:cd19543 2 YPLSPMQEGMLFHSlLDPGSGAYVEQM-VITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEGLGEPLQ----VVLKdrk 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1710 --VREIDAEGaLDPALVDAH-RELLGA-----MDPGTGSLLGTAVVN-GEGRRRLVIAIHHLGVDAVSWPILVEDLVTAW 1780
Cdd:cd19543 77 lpWRELDLSH-LSEAEQEAElEALAEEdrergFDLARAPLMRLTLIRlGDDRYRLVWSFHHILLDGWSLPILLKELFAIY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1781 AQLTSGRPIELRPEATTTRRIAhLLAGQVHARARevDYWLEQLP--ERPTSFGTSADRPLHRRRDESSLTYVVDDVAGSI 1858
Cdd:cd19543 156 AALGEGQPPSLPPVRPYRDYIA-WLQRQDKEAAE--AYWREYLAgfEEPTPLPKELPADADGSYEPGEVSFELSAELTAR 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1859 LTTVPQAFGSSVDDVLLGA----LARAvrawqldNGIAD---GgpVTVSteghGRDESIAGDEgaidlsRTVGWFTSITP 1931
Cdd:cd19543 233 LQELARQHGVTLNTVVQGAwallLSRY-------SGRDDvvfG--TTVS----GRPAELPGIE------TMVGLFINTLP 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1932 LAVDASSD--VVHAVKSAKDARL-SRPAGGVGFGILRYNSDGeiaHRPL-PTIMY--NYfgggtapstetaPDDFLPVSD 2005
Cdd:cd19543 294 VRVRLDPDqtVLELLKDLQAQQLeLREHEYVPLYEIQAWSEG---KQALfDHLLVfeNY------------PVDESLEEE 358
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1827387616 2006 RPNMPSSITG-AMRSPSVFGINISTAGREErrLEAKVTYATDALDEAAASDIARRWHDELRAVVE 2069
Cdd:cd19543 359 QDEDGLRITDvSAEEQTNYPLTVVAIPGEE--LTIKLSYDAEVFDEATIERLLGHLRRVLEQVAA 421
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1186-1466 |
1.28e-04 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 47.58 E-value: 1.28e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1186 YLIYTSGSTGRPKavGVSHTgivdfvnslakitTGTPEDEPDTRILHvaspSFDASMFEMAWAIP-----AGHTLVI--- 1257
Cdd:PLN02654 279 FLLYTSGSTGKPK--GVLHT-------------TGGYMVYTATTFKY----AFDYKPTDVYWCTAdcgwiTGHSYVTygp 339
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1258 ------------APQADFAGDALATVlERDEVTDMIITPSVLATVDPERAQYV--------RNLATGGEACPPElVERWs 1317
Cdd:PLN02654 340 mlngatvlvfegAPNYPDSGRCWDIV-DKYKVTIFYTAPTLVRSLMRDGDEYVtrhsrkslRVLGSVGEPINPS-AWRW- 416
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1318 ergrrIFNCYG----PTEATVWATRsrmTAG------------KPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYL--S 1379
Cdd:PLN02654 417 -----FFNVVGdsrcPISDTWWQTE---TGGfmitplpgawpqKPGSATFPFFGVQPVIVDEKGKEIEGECSGYLCVkkS 488
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1380 TAGLARGYLGRPGQTAVSFVAdPFgepgARMYATGDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQ 1459
Cdd:PLN02654 489 WPGAFRTLYGDHERYETTYFK-PF----AGYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEVESALVSHPQCAE 563
|
....*..
gi 1827387616 1460 SVVVGVE 1466
Cdd:PLN02654 564 AAVVGIE 570
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
238-382 |
2.74e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 46.64 E-value: 2.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 238 TSLRLIQTGGEALTPPVARDLMVRLpGTRLQNQYGPAEAS--IVVTIHRvtqDDRVIPIG---TPTRRVSARVLDA--AL 310
Cdd:PTZ00342 461 PNLEVILNGGGKLSPKIAEELSVLL-NVNYYQGYGLTETTgpIFVQHAD---DNNTESIGgpiSPNTKYKVRTWETykAT 536
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1827387616 311 REVPigvPGELYLGGVQLARGYAGRPDLTAERFVADPFgepgarlYRTGDRARWNRDGEIEYLGRTDFQVKL 382
Cdd:PTZ00342 537 DTLP---KGELLIKSDSIFSGYFLEKEQTKNAFTEDGY-------FKTGDIVQINKNGSLTFLDRSKGLVKL 598
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
117-402 |
3.45e-04 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 46.35 E-value: 3.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 117 PTRPANAAFTLFTSGSTGRPKAVVITHRGIANRL-AADI--EQYD--LTARDVFLYKAPIT--FDVSVREIFLpiAIGAT 189
Cdd:PLN02430 216 PPKPLDICTIMYTSGTSGDPKGVVLTHEAVATFVrGVDLfmEQFEdkMTHDDVYLSFLPLAhiLDRMIEEYFF--RKGAS 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 190 LVIaepgRHGDPVHLADLIRRHGVTVIHFVPAMLAAFNEVLGAGVGELT------------------------------- 238
Cdd:PLN02430 294 VGY----YHGDLNALRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNprrrlifnalykyklawmnrgyshkkaspma 369
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 239 --------------SLRLIQTGGEALTPPVARDLMVRLPGTRLQNqYGPAEASIVVTIhrvTQDDRVIPIGTPTrrVSAR 304
Cdd:PLN02430 370 dflafrkvkaklggRLRLLISGGAPLSTEIEEFLRVTSCAFVVQG-YGLTETLGPTTL---GFPDEMCMLGTVG--APAV 443
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 305 VLDAALREV------PIGVP--GELYLGGVQLARGYAGRPDLTAErFVADPFgepgarlYRTGDRARWNRDGEIEYLGRT 376
Cdd:PLN02430 444 YNELRLEEVpemgydPLGEPprGEICVRGKCLFSGYYKNPELTEE-VMKDGW-------FHTGDIGEILPNGVLKIIDRK 515
|
330 340
....*....|....*....|....*..
gi 1827387616 377 DFQVKL-RGQRLELGEVEAALAAAPGV 402
Cdd:PLN02430 516 KNLIKLsQGEYVALEYLENVYGQNPIV 542
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
2591-3059 |
5.49e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 45.52 E-value: 5.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2591 RLTYRELDEASDRLARWLIGRGVG------------PERAVA-LAIGRsaqlLTAIWAVAKTGgayvpidpdYPAERVAS 2657
Cdd:PRK00174 98 KITYRELHREVCRFANALKSLGVKkgdrvaiympmiPEAAVAmLACAR----IGAVHSVVFGG---------FSAEALAD 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2658 MIEDSGAVL----------GLSV---------LASGDL---------PGQEFEWMRLDD----DSVAAEIAAVPAGPItD 2705
Cdd:PRK00174 165 RIIDAGAKLvitadegvrgGKPIplkanvdeaLANCPSvekvivvrrTGGDVDWVEGRDlwwhELVAGASDECEPEPM-D 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2706 AErlgevtaaNLAYVIYTSGSTGRPKGV-----------AVTHSGLanFARQESDRL--NA------GDNPVVLGfasP- 2765
Cdd:PRK00174 244 AE--------DPLFILYTSGSTGKPKGVlhttggylvyaAMTMKYV--FDYKDGDVYwcTAdvgwvtGHSYIVYG---Pl 310
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2766 SFDASVLEYllatvnEGTLAYrPSEAVGGEVLERfiaeHGAThTFLTPsvlstmdPTAVPSLrvIAAGGEAVPQ------ 2839
Cdd:PRK00174 311 ANGATTLMF------EGVPNY-PDPGRFWEVIDK----HKVT-IFYTA-------PTAIRAL--MKEGDEHPKKydlssl 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2840 ---------------------------PIVDRWapatelhnlyGPTETTiGITIS-----SAMRPGDPVRlggPIGGVDL 2887
Cdd:PRK00174 370 rllgsvgepinpeawewyykvvggercPIVDTW----------WQTETG-GIMITplpgaTPLKPGSATR---PLPGIQP 435
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2888 MVLDERLRPVPVGMPGELYVAGG--ALSRG-YLDRsgltaERFTANPYGT-AGqrMYRTGDVVRWtpDTDtGGLTLeyTG 2963
Cdd:PRK00174 436 AVVDEEGNPLEGGEGGNLVIKDPwpGMMRTiYGDH-----ERFVKTYFSTfKG--MYFTGDGARR--DED-GYYWI--TG 503
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2964 RSDDQVKLRGLRIELGEIEAVLAEHDAV-ESAVVlGVGGSV-ATALAAYIVPVDGAVE----VSELKAFAGGRLPAYMVP 3037
Cdd:PRK00174 504 RVDDVLNVSGHRLGTAEIESALVAHPKVaEAAVV-GRPDDIkGQGIYAFVTLKGGEEPsdelRKELRNWVRKEIGPIAKP 582
|
570 580
....*....|....*....|..
gi 1827387616 3038 SSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PRK00174 583 DVIQFAPGLPKTRSGKIMRRIL 604
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1342-1527 |
5.92e-04 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 45.52 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1342 TAGKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTA--GLARGYLGRPGQtavsFVADPFGE-PGarMYATGDLVR 1418
Cdd:PRK00174 419 TPLKPGSATRPLPGIQPAVVDEEGNPLEGGEGGNLVIKDPwpGMMRTIYGDHER----FVKTYFSTfKG--MYFTGDGAR 492
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1419 VAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGV-ESTRGgrkhTEVVAYLVAKPGATIDsaavlDE 1497
Cdd:PRK00174 493 RDEDGYYWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRpDDIKG----QGIYAFVTLKGGEEPS-----DE 563
|
170 180 190
....*....|....*....|....*....|....*...
gi 1827387616 1498 AAQHLAAHMV--------PSQAIVIDEIPLTPAGKLDR 1527
Cdd:PRK00174 564 LRKELRNWVRkeigpiakPDVIQFAPGLPKTRSGKIMR 601
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
331-446 |
6.12e-04 |
|
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. At least five copies of FATPs are identified in mammalian cells. This family includes FATP4, FATP1, and homologous proteins. Each FATP has unique patterns of tissue distribution. FATP4 is mainly expressed in the brain, testis, colon and kidney. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341262 [Multi-domain] Cd Length: 474 Bit Score: 45.11 E-value: 6.12e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 331 GYAGRPDlTAERFVADPFgEPGARLYRTGDRARWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVLHAAAAVV 410
Cdd:cd05939 328 GYVNEGA-TNKKIARDVF-KKGDSAFLSGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYGV 405
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 1827387616 411 DGPGGQQLVGYLAPAD----VDVDTVAATTAELLPEYMRP 446
Cdd:cd05939 406 EVPGVEGRAGMAAIVDperkVDLDRFSAVLAKSLPPYARP 445
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1062-1222 |
8.02e-04 |
|
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: 44.90 E-value: 8.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1062 MDYDEFETRTNAIARALLARGV--SPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVGIT 1139
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGkpAPASFVGIYSINRPEWIISELACYAYSLVTVPLYDTLGPEAIEYILNHAEISIVFC 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1140 DAStrarlgesscewVDLADLEaeaesgdDITDTERNGSVRLT-----NLAYLIYTSGSTGRPKAVGVSHTGIVDFVNSL 1214
Cdd:cd05927 86 DAG------------VKVYSLE-------EFEKLGKKNKVPPPppkpeDLATICYTSGTTGNPKGVMLTHGNIVSNVAGV 146
|
....*...
gi 1827387616 1215 AKITTGTP 1222
Cdd:cd05927 147 FKILEILN 154
|
|
| PRK05851 |
PRK05851 |
long-chain-fatty acid--ACP ligase MbtM; |
1349-1529 |
8.38e-04 |
|
long-chain-fatty acid--ACP ligase MbtM;
Pssm-ID: 180289 [Multi-domain] Cd Length: 525 Bit Score: 44.76 E-value: 8.38e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1349 IGKPVDGFTVRVLDGrlhEVPQGV----VGELYLSTAGLARGYLGrpgqtavsfvADPfGEPGArMYATGDLVRVAKGGn 1424
Cdd:PRK05851 347 LGNPIPGMEVRISPG---DGAAGVagreIGEIEIRGASMMSGYLG----------QAP-IDPDD-WFPTGDLGYLVDGG- 410
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1425 LEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGRKHTEVVAYLVAKPgatiDSAAVLDEAAQHLAA 1504
Cdd:PRK05851 411 LVVCGRAKELITVAGRNIFPTEIERVAAQVRGVREGAVVAVGTGEGSARPGLVIAAEFRGP----DEAGARSEVVQRVAS 486
|
170 180
....*....|....*....|....*....
gi 1827387616 1505 H--MVPSQAIVID--EIPLTPAGKLDRAA 1529
Cdd:PRK05851 487 EcgVVPSDVVFVApgSLPRTSSGKLRRLA 515
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1549-1607 |
1.11e-03 |
|
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: 40.31 E-value: 1.11e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1827387616 1549 EDNLARIVAGLLG---EERVSVTESFFALGGDSIMSIQLSSA-AKAAGIHLSPREIFELKTIR 1607
Cdd:smart00823 14 LDLVREQVAAVLGhaaAEAIDPDRPFRDLGLDSLMAVELRNRlEAATGLRLPATLVFDHPTPA 76
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
2589-3059 |
1.17e-03 |
|
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: 44.34 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2589 GARLTYRELDEASDRLARWLIGRGVGPERAVALAIGRSAQLLtAIW-AVAKTGGAYVPIDPDYPAERVASMIEDSGAVlg 2667
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFV-ALWlGLAKIGVETALINSNLRLESLLHCITVSKAK-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2668 lSVLasgdlpgqefewMRLDDDSVAAEIAAVPAGPITDAErlgevtaANLAYvIYTSGSTGRPKGVAVTHS--------G 2739
Cdd:cd05939 78 -ALI------------FNLLDPLLTQSSTEPPSQDDVNFR-------DKLFY-IYTSGTTGLPKAAVIVHSryyriaagA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2740 LANFARQESDRL--------NAGD-----NPVVLG--------FASPSF-------DASVLEY-------LLATvnegtl 2784
Cdd:cd05939 137 YYAFGMRPEDVVydclplyhSAGGimgvgQALLHGstvvirkkFSASNFwddcvkyNCTIVQYigeicryLLAQ------ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2785 AYRPSE-------AVGG--------EVLERF----IAE-HGATHTfltPSVLSTMDPtavpslRVIAAGgeavpqpIVDR 2844
Cdd:cd05939 211 PPSEEEqkhnvrlAVGNglrpqiweQFVRRFgipqIGEfYGATEG---NSSLVNIDN------HVGACG-------FNSR 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2845 WapateLHNLYgptettigitissamrpgdPVRL-------GGPIGGVDLMVLdeRLRPvpvGMPGELY---VAGGALSR 2914
Cdd:cd05939 275 I-----LPSVY-------------------PIRLikvdedtGELIRDSDGLCI--PCQP---GEPGLLVgkiIQNDPLRR 325
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2915 --GYLDRsGLTAERFTANPYgTAGQRMY------------------RTGDVVRWtpdtdtggltleytgrsddqvklRGL 2974
Cdd:cd05939 326 fdGYVNE-GATNKKIARDVF-KKGDSAFlsgdvlvmdelgylyfkdRTGDTFRW-----------------------KGE 380
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2975 RIELGEIEAVLAEHDAVESAVVLGV--GGSVATALAAYIVPVDGAVEVSELKAFAGGRLPAYMVPSSFTVIDELPLTPVG 3052
Cdd:cd05939 381 NVSTTEVEGILSNVLGLEDVVVYGVevPGVEGRAGMAAIVDPERKVDLDRFSAVLAKSLPPYARPQFIRLLPEVDKTGTF 460
|
....*..
gi 1827387616 3053 KLDKRAL 3059
Cdd:cd05939 461 KLQKTDL 467
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
1669-1840 |
1.80e-03 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 44.26 E-value: 1.80e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1669 AVADLQTVVEAVAAAHPMLTAVLTRSGDGWTMNAGAGIVPAVREIDAEGALDP---ALVDAHRELLGAMDPGTGSLLGTA 1745
Cdd:PRK10252 44 APLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLPEIIDLRTQPDPhaaAQALMQADLQQDLRVDSGKPLVFH 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1746 V--VNGEGRRRLVIAIHHLGVDAVSWPILVEDLVTAWAQLTSGRPielrPEATTTRRIAHLLA-----GQVHARAREVDY 1818
Cdd:PRK10252 124 QliQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAWLRGEP----TPASPFTPFADVVEeyqryRASEAWQRDAAF 199
|
170 180
....*....|....*....|..
gi 1827387616 1819 WLEQLPERPTSFGTSADRPLHR 1840
Cdd:PRK10252 200 WAEQRRQLPPPASLSPAPLPGR 221
|
|
| PRK03584 |
PRK03584 |
acetoacetate--CoA ligase; |
1414-1525 |
2.05e-03 |
|
acetoacetate--CoA ligase;
Pssm-ID: 235134 [Multi-domain] Cd Length: 655 Bit Score: 43.63 E-value: 2.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1414 GDLVRVAKGGNLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVESTRGGrkhTEVVAYLVAKPGATID--- 1490
Cdd:PRK03584 503 GDWIEITEHGGVVIYGRSDATLNRGGVRIGTAEIYRQVEALPEVLDSLVIGQEWPDGD---VRMPLFVVLAEGVTLDdal 579
|
90 100 110
....*....|....*....|....*....|....*
gi 1827387616 1491 SAAVLDEAAQHLAAHMVPSQAIVIDEIPLTPAGKL 1525
Cdd:PRK03584 580 RARIRTTIRTNLSPRHVPDKIIAVPDIPRTLSGKK 614
|
|
| PksD |
COG3321 |
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites ... |
566-1124 |
2.08e-03 |
|
Acyl transferase domain in polyketide synthase (PKS) enzymes [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442550 [Multi-domain] Cd Length: 1386 Bit Score: 44.09 E-value: 2.08e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 566 PRPERLPLSRAQRRMWFLNQFDTASGAYNIPAALTLAGDVDETLLfdslcdvverhevlrtvypSVGAAPVQDVLPVAVA 645
Cdd:COG3321 858 RRRVPLPTYPFQREDAAAALLAAALAAALAAAAALGALLLAALAA-------------------ALAAALLALAAAAAAA 918
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 646 REQLDWREADSVESLVRSTTEGFDVSTQMPLRGRFHRDGAGLHVALTMHHIAMDGQSIPVLARDLMSAYAARAEGRTGGL 725
Cdd:COG3321 919 LALAAAALAALLALVALAAAAAALLALAAAAAAAAAALAAAEAGALLLLAAAAAAAAAAAAAAAAAAAAAAAAAAAALAA 998
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 726 PVLDVQYADYALWQQSVLGDADDETSVLGEQLSHWRRVLAGLPAVTDLPMDRPRPAVLGTAGATVTVEFDDDLADRVDVL 805
Cdd:COG3321 999 AAALALLAAAALLLAAAAAAAALLALAALLAAAAAALAAAAAAAAAAAALAALAAAAAAAAALALALAALLLLAALAELA 1078
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 806 ARSNTMTGFMVTEAAFAATVARLASTTDVVIGTPVAGRNDPALEELIGMFVNTLLLRTQVDPGHSVGDLLGNVRTTVLDA 885
Cdd:COG3321 1079 LAAAALALAAALAAAALALALAALAAALLLLALLAALALAAAAAALLALAALLAAAAAAAALAAAAAAAAALALAAAAAA 1158
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 886 FANDQVQFDELIEALAPERSSSHQPLAqiaftyteptvndvAGLEASGIQAAPVDTGVVNAKFDLTVAVRARSGGTPMAA 965
Cdd:COG3321 1159 LAAALAAALLAAAALLLALALALAAAL--------------AAALAGLAALLLAALLAALLAALLALALAALAAAAAALL 1224
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 966 DFIYATDLFDESTVKRFAEVYRRVLQAIVDDQNTAVGDIDIVGAARAKSVSAPVSARTPGAMVGRGGEVEAGTLIDVLAQ 1045
Cdd:COG3321 1225 AAAAAAAALALLALAAAAAAVAALAAAAAALLAALAALALLAAAAGLAALAAAAAAAAAALALAAAAAAAAAALAALLAA 1304
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1827387616 1046 RDLDPDHPALICDGTEMDYDEFETRTNAIARALLARGVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADR 1124
Cdd:COG3321 1305 AAAAAAAAAAAAAAAALAAALLAAALAALAAAVAAALALAAAAAAAAAAAAAAAAAAALAAAAGAAAAAAALALAALAA 1383
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
1165-1208 |
2.25e-03 |
|
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: 43.50 E-value: 2.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 1827387616 1165 ESGDDITDTE---RNGSVRLTNLAYLIYTSGSTGRPKAVGVSHTGIV 1208
Cdd:cd05933 130 ELGRSIPDEQldaIISSQKPNQCCTLIYTSGTTGMPKGVMLSHDNIT 176
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
4-419 |
3.39e-03 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 43.07 E-value: 3.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 4 AEFDRRVTGLARELTALGVGAEVAVGIQIDRSVEQVVAIHAVAMAGGHFVPLdeQLP---------VDRARYMVRTAGVR 74
Cdd:PRK09192 53 QTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLVPVPL--PLPmgfggresyIAQLRGMLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 75 LVVVTSDGE---AEARSRFDDivdVHVLdisSPGDADLDEE---EFAGPTrPANAAFTLFTSGSTGRPKAVVITHRGIAN 148
Cdd:PRK09192 131 AIITPDELLpwvNEATHGNPL---LHVL---SHAWFKALPEadvALPRPT-PDDIAYLQYSSGSTRFPRGVIITHRALMA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 149 RLAAdIEQYDLTARD----------------VFLYKAPITFDVSVReiFLPIaigatlviaepgrhGD----PVHLADLI 208
Cdd:PRK09192 204 NLRA-ISHDGLKVRPgdrcvswlpfyhdmglVGFLLTPVATQLSVD--YLPT--------------RDfarrPLQWLDLI 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 209 RRHGVTvIHFVP-------------AMLAAFNevlgagvgeLTSLRLIQTGGEALTPPVARDLMVRLPGTRLQNQ----- 270
Cdd:PRK09192 267 SRNRGT-ISYSPpfgyelcarrvnsKDLAELD---------LSCWRVAGIGADMIRPDVLHQFAEAFAPAGFDDKafmps 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 271 YGPAEASIVVTI--------------HRVTQDDRVIPIGTPTRRVSA-------------RVLDAALREVPIGVPGELYL 323
Cdd:PRK09192 337 YGLAEATLAVSFsplgsgivveevdrDRLEYQGKAVAPGAETRRVRTfvncgkalpgheiEIRNEAGMPLPERVVGHICV 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 324 GGVQLARGYAGRPDlTAERFVADPFGEpgarlyrTGDRArWNRDGEIEYLGRTDFQVKLRGQRLELGEVEAALAAAPGVL 403
Cdd:PRK09192 417 RGPSLMSGYFRDEE-SQDVLAADGWLD-------TGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELR 487
|
490
....*....|....*...
gi 1827387616 404 H--AAAAVVDGPGGQQLV 419
Cdd:PRK09192 488 SgdAAAFSIAQENGEKIV 505
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
1059-1289 |
3.55e-03 |
|
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: 43.11 E-value: 3.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1059 GTEMDYDEFETRTNAIARALLAR-GVSPEDVVAVGMERSIGSVLATWGVIKSGAAYVPVDPAYPADRIAYMLEDSGATVG 1137
Cdd:cd05905 12 ATTLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQQLGFLLGTCKVRVA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1138 IT------DASTRARLGESSCE------WVDLADLEAEAESGDDIT-DTERNGSVRLTNLAYLIYTSGSTGRPKAVGVSH 1204
Cdd:cd05905 92 LTveaclkGLPKKLLKSKTAAEiakkkgWPKILDFVKIPKSKRSKLkKWGPHPPTRDGDTAYIEYSFSSDGSLSGVAVSH 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1205 TGIVDFVNSLaKITTGTPEDEPdtrILHVASPSFDASMfeMAWA---IPAGHTLVIAPQADFAGDALA--TVLERDEVTD 1279
Cdd:cd05905 172 SSLLAHCRAL-KEACELYESRP---LVTVLDFKSGLGL--WHGCllsVYSGHHTILIPPELMKTNPLLwlQTLSQYKVRD 245
|
250
....*....|
gi 1827387616 1280 MIITPSVLAT 1289
Cdd:cd05905 246 AYVKLRTLHW 255
|
|
| PRK07868 |
PRK07868 |
acyl-CoA synthetase; Validated |
1344-1542 |
3.82e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236121 [Multi-domain] Cd Length: 994 Bit Score: 43.17 E-value: 3.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1344 GKPVTIGKPVDGFTVRVLDGRLHEVPQGVVGELYLSTAGLARGYLGRPGQTAVSFVADPFGePGARMYATGDLVRVAKGG 1423
Cdd:PRK07868 772 GRPLPGAGRVELAAYDPEHDLILEDDRGFVRRAEVNEVGVLLARARGPIDPTASVKRGVFA-PADTWISTEYLFRRDDDG 850
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1424 NLEFAGRADHQVKINGQRVELGEIEAVLDAQPGVAQSVVVGVEStrggRKHTEVVAYLVAKPGATIdSAAVLDEAAQHLA 1503
Cdd:PRK07868 851 DYWLVDRRGSVIRTARGPVYTEPVTDALGRIGGVDLAVTYGVEV----GGRQLAVAAVTLRPGAAI-TAADLTEALASLP 925
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1827387616 1504 AHMVPSQAIVIDEIPLTP-----AGKLDRAALPEPHA------PEPAEYV 1542
Cdd:PRK07868 926 VGLGPDIVHVVPEIPLSAtyrptVSALRAAGIPKPGRqawyfdPETNRYR 975
|
|
| PLN03052 |
PLN03052 |
acetate--CoA ligase; Provisional |
2856-3059 |
4.89e-03 |
|
acetate--CoA ligase; Provisional
Pssm-ID: 215553 [Multi-domain] Cd Length: 728 Bit Score: 42.76 E-value: 4.89e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2856 GPTETTIGITISSAMRPGDPVRLGGPIGGVDLMVLDERLRPVPVGMPGELYVAGGALSRGYLDRSgLTAERFTANPYGTA 2935
Cdd:PLN03052 505 GGTELGGGFVTGSLLQPQAFAAFSTPAMGCKLFILDDSGNPYPDDAPCTGELALFPLMFGASSTL-LNADHYKVYFKGMP 583
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1827387616 2936 ---GQRMYRTGDVVRWTPdtdtGGLTLEYtGRSDDQVKLRGLRIELGEIEAVL-AEHDAV-ESAVVlGV----GGSVATA 3006
Cdd:PLN03052 584 vfnGKILRRHGDIFERTS----GGYYRAH-GRADDTMNLGGIKVSSVEIERVCnAADESVlETAAI-GVpppgGGPEQLV 657
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1827387616 3007 LAAYIVPVDGA-VEVSELKAFAGGRLPAYMVP----SSFTVIDELPLTPVGKLDKRAL 3059
Cdd:PLN03052 658 IAAVLKDPPGSnPDLNELKKIFNSAIQKKLNPlfkvSAVVIVPSFPRTASNKVMRRVL 715
|
|
|