|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
21-1911 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 1391.42 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 21 EYWLDKLSGDVELSRFPCDclslnNIQASKESYYCQ-----FPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKD 95
Cdd:PRK12467 241 AYWQEQLGGEHTVLELPTD-----RPRPAVPSYRGArlrvdLPQALSAGLKALAQREGVTLFMVLLASFQTLLHRYSGQS 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 96 DVVIGMPVFKQGQEETV----FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNLPLL 171
Cdd:PRK12467 316 DIRIGVPNANRNRVETErligFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAHQDLPFEQLVEALQPERSLSHSPLF 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 172 -------NTIVM-------------LDDIHCYESTDKInsDMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLYNIL 231
Cdd:PRK12467 396 qvmfnhqNTATGgrdregaqlpgltVEELSWARHTAQF--DLALDTYESAQGLWAAFTYATDLFEATTIERLATHWRNLL 473
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 232 DILMKDPNKSAMDLDVMPKTEKNQILFDFNhttrvhktlLCETVTAP----QLFEEQVKQNPNQIAIVCNGKEITYKQLN 307
Cdd:PRK12467 474 EAIVAEPRRRLGELPLLDAEERARELVRWN---------APATEYAPdcvhQLIEAQARQHPERPALVFGEQVLSYAELN 544
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 308 IKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyQNSIIKGV 387
Cdd:PRK12467 545 RQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGVRLLLT-QSHLLAQL 623
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 388 AFQGSV----INLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVL 463
Cdd:PRK12467 624 PVPAGLrslcLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIAERL--QLAADDSML 701
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 464 FSSSISFDVTIFEIFVPLVCGARMTIY-QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYfVRANQKISLNKLFVGV 542
Cdd:PRK12467 702 MVSTFAFDLGVTELFGALASGATLHLLpPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA-SRVALPRPQRALVCGG 780
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 543 EPIKTELLAKYDHLfRGNLQILNLYGPTEATVCCTSYQYeRDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEIC 622
Cdd:PRK12467 781 EALQVDLLARVRAL-GPGARLINHYGPTETTVGVSTYEL-SDEERDFGNVPIGQPLANLGLYILDHYLNPVPVGVVGELY 858
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 623 ISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETI 701
Cdd:PRK12467 859 IGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIELGEIEARLLAQPGV 938
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 702 KTAVVIQrEDESGEKYLCAYVV-------TEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPIN 774
Cdd:PRK12467 939 REAVVLA-QPGDAGLQLVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTPNGKLDRKALPKPDA 1017
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 775 N-LKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYI 853
Cdd:PRK12467 1018 SaVQATFVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLRTLFEHQTLAGFAQAV 1097
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 854 LEMEKSNYISIEPVKQQEYYLASTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQI 933
Cdd:PRK12467 1098 AAQQQGAQPALPDVDRDQPLPLSYAQERQWFLWQLEPGS-AAYHIPQALRLKGPLDIEALERSFDALVARHESLRTTFVQ 1176
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 934 LDGELVQKIEP--NVDFNIEYVHVNEKDAD----YLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSM 1007
Cdd:PRK12467 1177 EDGRTRQVIHPvgSLTLEEPLLLAADKDEAqlkvYVEAEARQPFDLEQGPLLRVGLLRLAADEHVLVLTLHHIVSDGWSM 1256
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1008 GILIKEFVELYKGN------ELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGN 1081
Cdd:PRK12467 1257 QVLVDELVALYAAYsqgqslQLPALPIQYADYAVWQRQWMDAGERARQLAYWKAQLGGEQPVLELPTDRPRPAVQSHRGA 1336
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1082 VCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLEND 1161
Cdd:PRK12467 1337 RLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGVPIANRNRAETEGLIGFFVNTQVLRAEVDGQ 1416
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1162 DEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPI-SIGELEFTPYPFKQSVSKFDL 1240
Cdd:PRK12467 1417 ASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQVMFNHQRDDHQAQaQLPGLSVESLSWESQTAQFDL 1496
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1241 SLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFNKKENSNSNYLLV 1320
Cdd:PRK12467 1497 TLDTYESSEGLQASLTYATDLFEASTIERLAGHWLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARLV 1576
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1321 HKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDT 1400
Cdd:PRK12467 1577 HQLIEDQAAATPEAVALVFGEQELTYGELNRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDP 1656
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1401 DLPKQRVEYMLTDSGCSHVLVH-----QNSIIKGIefQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPK 1475
Cdd:PRK12467 1657 EYPRERLAYMIEDSGIELLLTQshlqaRLPLPDGL--RSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPK 1734
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1476 GVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQ-GEKFDVTKLVQVILEEQVTL 1554
Cdd:PRK12467 1735 GAGNRHGALVNRLCATQEAY--QLSAADVVLQFTSFAFDVSVWELFWPLINGARLVIAPpGAHRDPEQLIQLIERQQVTT 1812
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1555 SYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEATVCCTSYRYESNKEITTQN 1634
Cdd:PRK12467 1813 LHFVPSMLQQLLQMDEQVEHPLSLRRVVCGGEALEVEALRPWLERL-PDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDS 1891
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1635 VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKTGDIARWLPDGNIE 1713
Cdd:PRK12467 1892 VPIGQPIANLSTYILDASLNPVPIGVAGELYLGGVGLARGYLNRPALTAERFVADPFGTvGSRLYRTGDLARYRADGVIE 1971
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1714 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQeDEAGEKYLCAYVVTeKDIPIPE-----------VRAYLAT 1782
Cdd:PRK12467 1972 YLGRIDHQVKIRGFRIELGEIEARLREQGGVREAVVIAQ-DGANGKQLVAYVVP-TDPGLVDddeaqvalraiLKNHLKA 2049
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1783 KLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLN-TLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSL 1861
Cdd:PRK12467 2050 SLPEYMVPAHLVFLARMPLTPNGKLDRKALPAPDaSELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSI 2129
|
1930 1940 1950 1960 1970
....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1862 KGLKLFENiKRMFNVQLPLSLLFQKATIEQLSDVISRNKG---ID------SECLIPIQ 1911
Cdd:PRK12467 2130 ISIQVVSR-ARQAGIRFTPKDLFQHQTVQSLAAVAQEGDGtvsIDqgpvtgDLPLLPIQ 2187
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
76-1913 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 1208.64 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 76 LYTILLSGVKYLLSRYTDKDDV-----VIGMPVFKQGQEETV--FQNNFLLLRTQiNQEDNFKEIIYKIKETILESNEHC 148
Cdd:PRK12316 1791 LNTLVQAAWLLLLQRYTGQETVafgatVAGRPAELPGIEQQIglFINTLPVIAAP-RPDQSVADWLQEVQALNLALREHE 1869
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 149 HFPFNKLTQLLSLDGESnnlpLLNTIVMLDDIHCYESTDKiNSDMVIRF--MKNEEQ--------------LKVQVDYNS 212
Cdd:PRK12316 1870 HTPLYDIQRWAGQGGEA----LFDSLLVFENYPVAEALKQ-GAPAGLVFgrVSNHEQtnypltlavtlgetLSLQYSYDR 1944
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 213 TLYSEGLVSRIVNHLYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHT-------TRVHktllcetvtapQLFEEQV 285
Cdd:PRK12316 1945 GHFDAAAIERLDRHLLHLLEQMAEDAQAALGELALLDAGERQRILADWDRTpeayprgPGVH-----------QRIAEQA 2013
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 286 KQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVE 365
Cdd:PRK12316 2014 ARAPEAIAVVFGDQHLSYAELDSRANRLAHRLRARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLA 2093
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 366 YMLTDSGCSHVLTyQNSIIKGVAFQGSVINLM---DIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLT 442
Cdd:PRK12316 2094 YMLEDSGAALLLT-QRHLLERLPLPAGVARLPldrDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALV 2172
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 443 NFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEI 522
Cdd:PRK12316 2173 AHCQAAGERY--ELSPADCELQFMSFSFDGAHEQWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQL 2250
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 523 YDYFVRANQKISLNKLFVGVEPIKTELLAKYDHLFRGNlQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTK 602
Cdd:PRK12316 2251 AEHAERDGRPPAVRVYCFGGEAVPAASLRLAWEALRPV-YLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGNRR 2329
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 603 IYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFE-RGEKLYKTGDIARWLPDGNIEYLGRVDHQVKI 681
Cdd:PRK12316 2330 AYILDADLNLLAPGMAGELYLGGEGLARGYLNRPGLTAERFVPDPFSaSGERLYRTGDLARYRADGVVEYLGRIDHQVKI 2409
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 682 RGYRIELGEIEASLLKYETIKTAVVIQREDESGeKYLCAYVV--TEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLT 759
Cdd:PRK12316 2410 RGFRIELGEIEARLQAHPAVREAVVVAQDGASG-KQLVAYVVpdDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLN 2488
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 760 QNGKIDRKKLPQP-INNLKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIK 838
Cdd:PRK12316 2489 PNGKLDRKALPKPdVSQLRQAYVAPQEGLEQRLAAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLR 2568
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 839 SLFKFPVLVDFSKYILEMEKSNYISIEPVKQQEYYLASTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQ 918
Cdd:PRK12316 2569 ILFERPTLAAFAASLESGQTSRAPVLQKVTRVQPLPLSHAQQRQWFLWQLEPES-AAYHLPSALHLRGVLDQAALEQAFD 2647
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 919 SLIERHEILRTSFQILDGELVQKIEPNV---DFNIEYVHVNEKDADYLIHEFIS-PFDLSKPPLLRVLLLRIAEERHILV 994
Cdd:PRK12316 2648 ALVLRHETLRTRFVEVGEQTRQVILPNMslrIVLEDCAGVADAAIRQRVAEEIQrPFDLARGPLLRVRLLALDGQEHVLV 2727
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 995 VDMHHIISDGLSMGILIKEFVELYKGNE------LPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPT 1068
Cdd:PRK12316 2728 ITQHHIVSDGWSMQVMVDELVQAYAGARrgeqptLPPLPLQYADYAAWQRAWMDSGEGARQLDYWRERLGGEQPVLELPL 2807
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1069 DFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMF 1148
Cdd:PRK12316 2808 DRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQVLLHRYSGQSDIRVGVPIANRNRAETERLIGFF 2887
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1149 INTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIGELEFTP 1228
Cdd:PRK12316 2888 VNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPERSLSHSPLFQVMYNHQSGERAAAQLPGLHIES 2967
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1229 YPFKQSVSKFDLSLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFN 1308
Cdd:PRK12316 2968 FAWDGAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQNLLRGMVENPQRSVDELAMLDAEERGQLLEAWN 3047
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1309 KKENSNSNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGV 1388
Cdd:PRK12316 3048 ATAAEYPLERGVHRLFEEQVERTPDAVALAFGEQRLSYAELNRRANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAI 3127
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1389 LKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLvhQNSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTS 1468
Cdd:PRK12316 3128 LKAGGAYVPLDPEYPEERLAYMLEDSGAQLLL--SQSHLRLPLAQGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTS 3205
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1469 GSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIY-QGEKFDVTKLVQVI 1547
Cdd:PRK12316 3206 GSTGKPKGVGIRHSALSNHLCWMQQAY--GLGVGDRVLQFTTFSFDVFVEELFWPLMSGARVVLAgPEDWRDPALLVELI 3283
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1548 LEEQVTLSYIPPTLLNEIYDYfVRDNQKIVLNKLLVGVEPIKTELLAKYDhlfrGNLQILNGYGPTEATVCCTSYRYEsn 1627
Cdd:PRK12316 3284 NSEGVDVLHAYPSMLQAFLEE-EDAHRCTSLKRIVCGGEALPADLQQQVF----AGLPLYNLYGPTEATITVTHWQCV-- 3356
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1628 kEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWL 1707
Cdd:PRK12316 3357 -EEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEGLARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYR 3435
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1708 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAgekyLCAYVVTEKDIP-IPEV-RAYLATKLP 1785
Cdd:PRK12316 3436 ADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVLAVDGRQ----LVAYVVPEDEAGdLREAlKAHLKASLP 3511
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1786 HYMIPQQLIPIHNIPLTQNGKIDRSKLPKLN-TLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGL 1864
Cdd:PRK12316 3512 EYMVPAHLLFLERMPLTPNGKLDRKALPRPDaALLQQDYVAPVNELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISL 3591
|
1850 1860 1870 1880 1890
....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 1865 KLFENIkRMFNVQLPLSLLFQKATIEQLSDVISRNKG--IDSE------CLIPIQNR 1913
Cdd:PRK12316 3592 QVVSRA-RQAGIRFTPKDLFQHQTIQGLARVARVGGGvaVDQGpvsgetLLLPIQQQ 3647
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
7-1921 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 1122.95 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:PRK05691 853 QRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATLFMVLLAAFQA 932
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 87 LLSRYTDKDDVVIGMPVFKQGQEETV----FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLD 162
Cdd:PRK05691 933 LLHRYSGQGDIRIGVPNANRPRLETQglvgFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPFEQLVEALPQA 1012
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 163 GESN-----------NLPLLNTI--VMLDDIHCYESTDKINSDMvirfmKNEE----QLKVQVDYNSTLYSEGLVSRIVN 225
Cdd:PRK05691 1013 REQGlfqvmfnhqqrDLSALRRLpgLLAEELPWHSREAKFDLQL-----HSEEdrngRLTLSFDYAAELFDAATIERLAE 1087
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 226 HLYNILDILMKDPNKSAMDLDVMPKTEKNQILfdfnhtTRVHKTLLCETVTAPQLFEEQVKQNPNQIAIVCNGKEITYKQ 305
Cdd:PRK05691 1088 HFLALLEQVCEDPQRALGDVQLLDAAERAQLA------QWGQAPCAPAQAWLPELLNEQARQTPERIALVWDGGSLDYAE 1161
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 306 LNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyQNSIIK 385
Cdd:PRK05691 1162 LHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSGVELLLT-QSHLLE 1240
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 386 GV--AFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDigiTDNVL 463
Cdd:PRK05691 1241 RLpqAEGVSAIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALD---DSDVL 1317
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 464 FSSS-ISFDVTIFEIFVPLVCGARMTIY-QGEKFDVPKLVQVILEEQVT-LAYIPPTLlneiyDYFV---RANQKISLNK 537
Cdd:PRK05691 1318 MQKApISFDVSVWECFWPLITGCRLVLAgPGEHRDPQRIAELVQQYGVTtLHFVPPLL-----QLFIdepLAAACTSLRR 1392
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 538 LFVGVEPIKTELLAK-YDHLfrGNLQILNLYGPTEATVCCTSYQYERDKeitTQNVPIGSPLLNTKIYILDSFHRLQPIG 616
Cdd:PRK05691 1393 LFSGGEALPAELRNRvLQRL--PQVQLHNRYGPTETAINVTHWQCQAED---GERSPIGRPLGNVLCRVLDAELNLLPPG 1467
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 617 VPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASL 695
Cdd:PRK05691 1468 VAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEEIQARL 1547
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 696 LKYETIKTAVVIQREDESGEKyLCAYVVTEK--DIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPI 773
Cdd:PRK05691 1548 LAQPGVAQAAVLVREGAAGAQ-LVGYYTGEAgqEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRALPEPV 1626
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 774 NNLKSsHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYI 853
Cdd:PRK05691 1627 WQQRE-HVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGAFAEQV 1705
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 854 LEMEKSNYIS----IEPVKQQEYYLASTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRT 929
Cdd:PRK05691 1706 ARIQAAGERNsqgaIARVDRSQPVPLSYSQQRMWFLWQMEPDS-PAYNVGGMARLSGVLDVDRFEAALQALILRHETLRT 1784
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 930 SFQILDGELVQKIEPNVDfnieyVHVNEKD----------------ADYLIHEfisPFDLSKPPLLRVLLLRIAEERHIL 993
Cdd:PRK05691 1785 TFPSVDGVPVQQVAEDSG-----LRMDWQDfsalpadarqqrlqqlADSEAHQ---PFDLERGPLLRACLVKAAEREHYF 1856
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 994 VVDMHHIISDGLSMGILIKEFVELYK----GNELP--KLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFP 1067
Cdd:PRK05691 1857 VLTLHHIVTEGWAMDIFARELGALYEafldDRESPlePLPVQYLDYSVWQRQWLESGERQRQLDYWKAQLGNEHPLLELP 1936
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1068 TDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGM 1147
Cdd:PRK05691 1937 ADRPRPPVQSHRGELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLAALLYRYSGQRDLRIGAPVANRIRPESEGLIGA 2016
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1148 FINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNmdmnpisigeleft 1227
Cdd:PRK05691 2017 FLNTQVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQPPRSAAYNPLFQVMCNVQR-------------- 2082
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1228 pYPFKQS----------------VSKFDLSLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRN 1291
Cdd:PRK05691 2083 -WEFQQSrqlagmtveylvndarATKFDLNLEVTDLDGRLGCCLTYSRDLFDEPRIARMAEHWQNLLEALLGDPQQRLAE 2161
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1292 INMLSIEEEHCIMNEFNKKENSNSNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIV 1371
Cdd:PRK05691 2162 LPLLAAAEQQQLLDSLAGEAGEARLDQTLHGLFAAQAARTPQAPALTFAGQTLSYAELDARANRLARALRERGVGPQVRV 2241
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1372 GVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCShVLVHQNSIIKGI-EFQGNVID--LMD--MSFEE 1446
Cdd:PRK05691 2242 GLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIG-LLLSDRALFEALgELPAGVARwcLEDdaAALAA 2320
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1447 EPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIY 1526
Cdd:PRK05691 2321 YSDAPLPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQAVIERF--GMRADDCELHFYSINFDAASERLLVPLLC 2398
|
1610 1620 1630 1640 1650 1660 1670 1680
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1527 GARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFRGNlQI 1606
Cdd:PRK05691 2399 GARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWLAGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQ-LF 2477
|
1690 1700 1710 1720 1730 1740 1750 1760
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1607 LNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKF 1686
Cdd:PRK05691 2478 FNAYGPTETVVMPLACLAPEQLEEGAASVPIGRVVGARVAYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERF 2557
|
1770 1780 1790 1800 1810 1820 1830 1840
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1687 IDHPFE-RGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGeKYLCAYV 1765
Cdd:PRK05691 2558 VADPFAaDGGRLYRTGDLVRLRADGLVEYVGRIDHQVKIRGFRIELGEIESRLLEHPAVREAVVLALDTPSG-KQLAGYL 2636
|
1850 1860 1870 1880 1890 1900 1910 1920
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1766 VTEKDIPIPE--------VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLN-TLGNSNYVPPRNEIDSSLID 1836
Cdd:PRK05691 2637 VSAVAGQDDEaqaalreaLKAHLKQQLPDYMVPAHLILLDSLPLTANGKLDRRALPAPDpELNRQAYQAPRSELEQQLAQ 2716
|
1930 1940 1950 1960 1970 1980 1990 2000
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1837 IWSSILGVNNIGINDNFFELGGHSLKGLKLFENiKRMFNVQLPLSLLFQKATIEQLSDVISRNKGIDSE--------CLI 1908
Cdd:PRK05691 2717 IWREVLNVERVGLGDNFFELGGDSILSIQVVSR-ARQLGIHFSPRDLFQHQTVQTLAAVATHSEAAQAEqgplqgasGLT 2795
|
2010
....*....|...
gi 446807313 1909 PIQNrtnkdsqWF 1921
Cdd:PRK05691 2796 PIQH-------WF 2801
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
917-1892 |
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: 982.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 917 FQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHVNEKD--------ADYLIHEFISPFDLSKPPLLRVLLLRIAE 988
Cdd:COG1020 61 AALLARRRRALRTRLRTRAGRPVQVIQPVVAAPLPVVVLLVDLealaeaaaEAAAAAEALAPFDLLRGPLLRLLLLLLLL 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 989 ERHILVVDMHHIISDGLSMGILIKEFVELY------KGNELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELP 1062
Cdd:COG1020 141 LLLLLLLALHHIISDGLSDGLLLAELLRLYlaayagAPLPLPPLPIQYADYALWQREWLQGEELARQLAYWRQQLAGLPP 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1063 VLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTN 1142
Cdd:COG1020 221 LLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFALLLARYSGQDDVVVGTPVAGRPRPELE 300
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1143 HMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIG 1222
Cdd:COG1020 301 GLVGFFVNTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEELQPERDLSRNPLFQVMFVLQNAPADELELP 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1223 ELEFTPYPFKQSVSKFDLSLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHC 1302
Cdd:COG1020 381 GLTLEPLELDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGHLVTLLEALAADPDQPLGDLPLLTAAERQQ 460
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1303 IMNEFNKKENSNSNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMV 1382
Cdd:COG1020 461 LLAEWNATAAPYPADATLHELFEAQAARTPDAVAVVFGDQSLTYAELNARANRLAHHLRALGVGPGDLVGVCLERSLEMV 540
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1383 IGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLA 1462
Cdd:COG1020 541 VALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARLPELGVPVLALDALALAAEPATNPPVPVTPDDLA 620
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1463 YVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIY-QGEKFDVT 1541
Cdd:COG1020 621 YVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRY--GLGPGDRVLQFASLSFDASVWEIFGALLSGATLVLApPEARRDPA 698
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1542 KLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKivLNKLLVGVEPIKTELLAKYDHLFRGnLQILNGYGPTEATVCCTS 1621
Cdd:COG1020 699 ALAELLARHRVTVLNLTPSLLRALLDAAPEALPS--LRLVLVGGEALPPELVRRWRARLPG-ARLVNLYGPTETTVDSTY 775
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1622 YRYESNkEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKT 1700
Cdd:COG1020 776 YEVTPP-DADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGGAGLARGYLNRPELTAERFVADPFGFpGARLYRT 854
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1701 GDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--EVRA 1778
Cdd:COG1020 855 GDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREAVVVAREDAPGDKRLVAYVVPEAGAAAAaaLLRL 934
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1779 YLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLNTLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGG 1858
Cdd:COG1020 935 ALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAAPPAEEEEEEAALALLLLLVVVVGDDDFFFFGGG 1014
|
970 980 990
....*....|....*....|....*....|....
gi 446807313 1859 HSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQL 1892
Cdd:COG1020 1015 LGLLLLLALARAARLLLLLLLLLLLFLAAAAAAA 1048
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
876-1890 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 813.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 876 STSQKRMFIVDQFeDGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHV 955
Cdd:PRK12467 53 SYAQERQWFLWQL-DPDSAAYNIPTALRLRGELDVSALRRAFDALVARHESLRTRFVQDEEGFRQVIDASLSLTIPLDDL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 956 NE---KDADYLIHEFIS-----PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGN------ 1021
Cdd:PRK12467 132 ANeqgRARESQIEAYINeevarPFDLANGPLLRVRLLRLADDEHVLVVTLHHIISDGWSMRVLVEELVQLYSAYsqgrep 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1022 ELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATE 1101
Cdd:PRK12467 212 SLPALPIQYADYAIWQRSWLEAGERERQLAYWQEQLGGEHTVLELPTDRPRPAVPSYRGARLRVDLPQALSAGLKALAQR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1102 TGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYEN 1181
Cdd:PRK12467 292 EGVTLFMVLLASFQTLLHRYSGQSDIRIGVPNANRNRVETERLIGFFVNTQVLKAEVDPQASFLELLQQVKRTALGAQAH 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1182 QDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNM-----DMNPISIGELEFTPYPFKQSVSKFDLSLVATEIDNNIHLKVE 1256
Cdd:PRK12467 372 QDLPFEQLVEALQPERSLSHSPLFQVMFNHQNTatggrDREGAQLPGLTVEELSWARHTAQFDLALDTYESAQGLWAAFT 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1257 YSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFNKKEnSNSNYLLVHKMFEEQVKRNPNQIA 1336
Cdd:PRK12467 452 YATDLFEATTIERLATHWRNLLEAIVAEPRRRLGELPLLDAEERARELVRWNAPA-TEYAPDCVHQLIEAQARQHPERPA 530
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1337 VVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGC 1416
Cdd:PRK12467 531 LVFGEQVLSYAELNRQANRLAHVLIAAGVGPDVLVGIAVERSIEMVVGLLAVLKAGGAYVPLDPEYPQDRLAYMLDDSGV 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1417 SHVLvHQNSIIKGIEFQGNV----IDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMY 1492
Cdd:PRK12467 611 RLLL-TQSHLLAQLPVPAGLrslcLDEPADLLCGYSGHNPEVALDPDNLAYVIYTSGSTGQPKGVAISHGALANYVCVIA 689
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1493 EDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIY-QGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYfVR 1571
Cdd:PRK12467 690 ERL--QLAADDSMLMVSTFAFDLGVTELFGALASGATLHLLpPDCARDAEAFAALMADQGVTVLKIVPSHLQALLQA-SR 766
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1572 DNQKIVLNKLLVGVEPIKTELLAKYDHLfRGNLQILNGYGPTEATVCCTSYRYeSNKEITTQNVPIGSPLLNTKIYILDS 1651
Cdd:PRK12467 767 VALPRPQRALVCGGEALQVDLLARVRAL-GPGARLINHYGPTETTVGVSTYEL-SDEERDFGNVPIGQPLANLGLYILDH 844
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1652 FHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIE 1730
Cdd:PRK12467 845 YLNPVPVGVVGELYIGGAGLARGYHRRPALTAERFVPDPFgADGGRLYRTGDLARYRADGVIEYLGRMDHQVKIRGFRIE 924
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1731 LGEIEASLLKYETIKTAVVIDQEDEAGEKyLCAYVV-------TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQ 1803
Cdd:PRK12467 925 LGEIEARLLAQPGVREAVVLAQPGDAGLQ-LVAYLVpaavadgAEHQATRDELKAQLRQVLPDYMVPAHLLLLDSLPLTP 1003
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1804 NGKIDRSKLPKL--NTLGNSnYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLS 1881
Cdd:PRK12467 1004 NGKLDRKALPKPdaSAVQAT-FVAPQTELEKRLAAIWADVLKVERVGLTDNFFELGGHSLLATQVISRVRQRLGIQVPLR 1082
|
....*....
gi 446807313 1882 LLFQKATIE 1890
Cdd:PRK12467 1083 TLFEHQTLA 1091
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
876-1913 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 806.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 876 STSQKRMFIVDQFEDGtNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHV 955
Cdd:PRK12316 53 SYAQQRMWFLWQLEPQ-SGAYNLPSAVRLNGPLDRQALERAFASLVQRHETLRTVFPRGADDSLAQVPLDRPLEVEFEDC 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 956 NEKD--------ADYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGN------ 1021
Cdd:PRK12316 132 SGLPeaeqearlRDEAQRESLQPFDLCEGPLLRVRLLRLGEEEHVLLLTLHHIVSDGWSMNVLIEEFSRFYSAYatgaep 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1022 ELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATE 1101
Cdd:PRK12316 212 GLPALPIQYADYALWQRSWLEAGEQERQLEYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARR 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1102 TGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYEN 1181
Cdd:PRK12316 292 QGLTLFMLLLGAFNVLLHRYSGQTDIRVGVPIANRNRAEVEGLIGFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAH 371
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1182 QDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNM--DMNPIS-IGELEFTPYPFKQSVSKFDLSLVATEIDNNIHLKVEYS 1258
Cdd:PRK12316 372 QDLPFERLVEALKVERSLSHSPLFQVMYNHQPLvaDIEALDtVAGLEFGQLEWKSRTTQFDLTLDTYEKGGRLHAALTYA 451
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1259 IKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFNKKENSNSNYLLVHKMFEEQVKRNPNQIAVV 1338
Cdd:PRK12316 452 TDLFEARTVERMARHWQNLLRGMVENPQARVDELPMLDAEERGQLVEGWNATAAEYPLQRGVHRLFEEQVERTPEAPALA 531
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1339 CNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSh 1418
Cdd:PRK12316 532 FGEETLDYAELNRRANRLAHALIERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQ- 610
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1419 VLVHQNSIIKGIEFQGNV----IDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYED 1494
Cdd:PRK12316 611 LLLSQSHLGRKLPLAAGVqvldLDRPAAWLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQA 690
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1495 FSQDIGitDNVLFSSSISFDVTIFEIFVPLIYGARMTI-YQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYdYFVRDN 1573
Cdd:PRK12316 691 YGLGVG--DTVLQKTPFSFDVSVWEFFWPLMSGARLVVaAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFL-QDEDVA 767
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1574 QKIVLNKLLVGVEPIKTELLAKYDHLfRGNLQILNGYGPTEAT--VCCTSYRYESNKEittqnVPIGSPLLNTKIYILDS 1651
Cdd:PRK12316 768 SCTSLRRIVCSGEALPADAQEQVFAK-LPQAGLYNLYGPTEAAidVTHWTCVEEGGDS-----VPIGRPIANLACYILDA 841
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1652 FHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIEL 1731
Cdd:PRK12316 842 NLEPVPVGVLGELYLAGRGLARGYHGRPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIEL 921
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1732 GEIEASLLKYETIKTAVVIDQEDeageKYLCAYVVTEKDI-PIPEV-RAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:PRK12316 922 GEIEARLLEHPWVREAAVLAVDG----KQLVGYVVLESEGgDWREAlKAHLAASLPEYMVPAQWLALERLPLTPNGKLDR 997
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1810 SKLPKLN-TLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKRMfNVQLPLSLLFQKAT 1888
Cdd:PRK12316 998 KALPAPEaSVAQQGYVAPRNALERTLAAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRARQA-GIQLSPRDLFQHQT 1076
|
1050 1060 1070
....*....|....*....|....*....|...
gi 446807313 1889 IEQLSDVISRNKGIDSE--------CLIPIQNR 1913
Cdd:PRK12316 1077 IRSLALVAKAGQATAADqgpasgevALAPVQRW 1109
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
412-1898 |
0e+00 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 761.25 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 412 TMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGiTDNVLFSssisfdvtifeiFVPL------VCGA 485
Cdd:PRK05691 162 ALQPDDIAFLQYTSGSTALPKGVQVSHGNLVANEQLIRHGFGIDLN-PDDVIVS------------WLPLyhdmglIGGL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 486 RMTIYQGekfdVPklvQVILEEQVTLAYiPPTLLNEIYDY-----------FVRANQKISLNKL-----------FVGVE 543
Cdd:PRK05691 229 LQPIFSG----VP---CVLMSPAYFLER-PLRWLEAISEYggtisggpdfaYRLCSERVSESALerldlsrwrvaYSGSE 300
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 544 PIKTELLAKYDHLFRG----NLQILNLYGPTEATVCCTSYQ-------YERDKEITTQNVPI---GSPLLNT-------K 602
Cdd:PRK05691 301 PIRQDSLERFAEKFAAcgfdPDSFFASYGLAEATLFVSGGRrgqgipaLELDAEALARNRAEpgtGSVLMSCgrsqpghA 380
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 603 IYILDSfHRLQPIG--VPGEICISGIGLARGYINRKELTADKFIDHPferGEKLYKTGDIArWLPDGNIEYLGRVDHQVK 680
Cdd:PRK05691 381 VLIVDP-QSLEVLGdnRVGEIWASGPSIAHGYWRNPEASAKTFVEHD---GRTWLRTGDLG-FLRDGELFVTGRLKDMLI 455
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 681 IRGYRIELGEIEasllkyetiKTavvIQREDESGEK-YLCAYVVT---EKDIPIP-EVRAYLATKLP------------- 742
Cdd:PRK05691 456 VRGHNLYPQDIE---------KT---VEREVEVVRKgRVAAFAVNhqgEEGIGIAaEISRSVQKILPpqaliksirqava 523
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 743 --YYMIPQQIISIQ--NIPLTQNGKIDRK---------------KLPQPINNLKSSHLEPTNSTERKLVEIWKDVLGIQR 803
Cdd:PRK05691 524 eaCQEAPSVVLLLNpgALPKTSSGKLQRSacrlrladgsldsyaLFPALQAVEAAQTAASGDELQARIAAIWCEQLKVEQ 603
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 804 IGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYILEMEKSNYIS---IEPVKQQEYYLASTSQK 880
Cdd:PRK05691 604 VAADDHFFLLGGNSIAATQVVARLRDELGIDLNLRQLFEAPTLAAFSAAVARQLAGGGAAqaaIARLPRGQALPQSLAQN 683
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 881 RMFIVDQFeDGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHVN---- 956
Cdd:PRK05691 684 RLWLLWQL-DPQSAAYNIPGGLHLRGELDEAALRASFQRLVERHESLRTRFYERDGVALQRIDAQGEFALQRIDLSdlpe 762
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 957 -EKDADYLI---HEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY------KGNELPKL 1026
Cdd:PRK05691 763 aEREARAAQireEEARQPFDLEKGPLLRVTLVRLDDEEHQLLVTLHHIVADGWSLNILLDEFSRLYaaacqgQTAELAPL 842
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1027 RVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTP 1106
Cdd:PRK05691 843 PLGYADYGAWQRQWLAQGEAARQLAYWKAQLGDEQPVLELATDHPRSARQAHSAARYSLRVDASLSEALRGLAQAHQATL 922
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1107 YMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPF 1186
Cdd:PRK05691 923 FMVLLAAFQALLHRYSGQGDIRIGVPNANRPRLETQGLVGFFINTQVLRAQLDGRLPFTALLAQVRQATLGAQAHQDLPF 1002
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1187 EELLEGLDLHRDTSrnpLFDTMFVFQNMDMNPI-SIGELEFTPYPFKQSVSKFDLSLVATEiDNN--IHLKVEYSIKLFK 1263
Cdd:PRK05691 1003 EQLVEALPQAREQG---LFQVMFNHQQRDLSALrRLPGLLAEELPWHSREAKFDLQLHSEE-DRNgrLTLSFDYAAELFD 1078
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1264 AETIERLMVHFTNIVEEVTNNPRVRLRNINMLSiEEEHCIMNEFNKKENSNSNYLLVhKMFEEQVKRNPNQIAVVCNEKG 1343
Cdd:PRK05691 1079 AATIERLAEHFLALLEQVCEDPQRALGDVQLLD-AAERAQLAQWGQAPCAPAQAWLP-ELLNEQARQTPERIALVWDGGS 1156
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcSHVLVHQ 1423
Cdd:PRK05691 1157 LDYAELHAQANRLAHYLRDKGVGPDVCVAIAAERSPQLLVGLLAILKAGGAYVPLDPDYPAERLAYMLADSG-VELLLTQ 1235
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 NSIIKGIEFQGNV--IDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDigi 1501
Cdd:PRK05691 1236 SHLLERLPQAEGVsaIALDSLHLDSWPSQAPGLHLHGDNLAYVIYTSGSTGQPKGVGNTHAALAERLQWMQATYALD--- 1312
|
1210 1220 1230 1240 1250 1260 1270 1280
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1502 TDNVLFSSS-ISFDVTIFEIFVPLIYGARMTIY-QGEKFDVTKLVQVILEEQVT-LSYIPPTLlneiyDYFVRD---NQK 1575
Cdd:PRK05691 1313 DSDVLMQKApISFDVSVWECFWPLITGCRLVLAgPGEHRDPQRIAELVQQYGVTtLHFVPPLL-----QLFIDEplaAAC 1387
|
1290 1300 1310 1320 1330 1340 1350 1360
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1576 IVLNKLLVGVEPIKTELLAK-YDHLfrGNLQILNGYGPTEATVCCTSYRYESNKeitTQNVPIGSPLLNTKIYILDSFHR 1654
Cdd:PRK05691 1388 TSLRRLFSGGEALPAELRNRvLQRL--PQVQLHNRYGPTETAINVTHWQCQAED---GERSPIGRPLGNVLCRVLDAELN 1462
|
1370 1380 1390 1400 1410 1420 1430 1440
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1655 IQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGE 1733
Cdd:PRK05691 1463 LLPPGVAGELCIGGAGLARGYLGRPALTAERFVPDPLgEDGARLYRTGDRARWNADGALEYLGRLDQQVKLRGFRVEPEE 1542
|
1450 1460 1470 1480 1490 1500 1510 1520
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1734 IEASLLKYETIKTAVVIDQEDEAGEKyLCAYVVTEK--DIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSK 1811
Cdd:PRK05691 1543 IQARLLAQPGVAQAAVLVREGAAGAQ-LVGYYTGEAgqEAEAERLKAALAAELPEYMVPAQLIRLDQMPLGPSGKLDRRA 1621
|
1530 1540 1550 1560 1570 1580 1590 1600
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1812 LPkLNTLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQ 1891
Cdd:PRK05691 1622 LP-EPVWQQREHVEPRTELQQQIAAIWREVLGLPRVGLRDDFFALGGHSLLATQIVSRTRQACDVELPLRALFEASELGA 1700
|
....*..
gi 446807313 1892 LSDVISR 1898
Cdd:PRK05691 1701 FAEQVAR 1707
|
|
| EntF |
COG1020 |
EntF, seryl-AMP synthase component of non-ribosomal peptide synthetase [Secondary metabolites ... |
7-1018 |
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: 760.93 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:COG1020 195 QREWLQGEELARQLAYWRQQLAGLPPLLELPTDRPRPAVQSYRGARVSFRLPAELTAALRALARRHGVTLFMVLLAAFAL 274
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 87 LLSRYTDKDDVVIGMPVFKQGQEET-------VfqnNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLL 159
Cdd:COG1020 275 LLARYSGQDDVVVGTPVAGRPRPELeglvgffV---NTLPLRVDLSGDPSFAELLARVRETLLAAYAHQDLPFERLVEEL 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 160 SLDGESNNLPLLNTIVMLD------------DIHCYE-STDKINSDMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNH 226
Cdd:COG1020 352 QPERDLSRNPLFQVMFVLQnapadelelpglTLEPLElDSGTAKFDLTLTVVETGDGLRLTLEYNTDLFDAATIERMAGH 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 227 LYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTTRVHKtllcETVTAPQLFEEQVKQNPNQIAIVCNGKEITYKQL 306
Cdd:COG1020 432 LVTLLEALAADPDQPLGDLPLLTAAERQQLLAEWNATAAPYP----ADATLHELFEAQAARTPDAVAVVFGDQSLTYAEL 507
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 307 NIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSIIKG 386
Cdd:COG1020 508 NARANRLAHHLRALGVGPGDLVGVCLERSLEMVVALLAVLKAGAAYVPLDPAYPAERLAYMLEDAGARLVLTQSALAARL 587
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 387 VAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSS 466
Cdd:COG1020 588 PELGVPVLALDALALAAEPATNPPVPVTPDDLAYVIYTSGSTGRPKGVMVEHRALVNLLAWMQRRY--GLGPGDRVLQFA 665
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 467 SISFDVTIFEIFVPLVCGARMTIY-QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQkiSLNKLFVGVEPI 545
Cdd:COG1020 666 SLSFDASVWEIFGALLSGATLVLApPEARRDPAALAELLARHRVTVLNLTPSLLRALLDAAPEALP--SLRLVLVGGEAL 743
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 546 KTELLAKYDHLFRGnLQILNLYGPTEATVCCTSYQYERDkEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISG 625
Cdd:COG1020 744 PPELVRRWRARLPG-ARLVNLYGPTETTVDSTYYEVTPP-DADGGSVPIGRPIANTRVYVLDAHLQPVPVGVPGELYIGG 821
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 626 IGLARGYINRKELTADKFIDHPFER-GEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTA 704
Cdd:COG1020 822 AGLARGYLNRPELTAERFVADPFGFpGARLYRTGDLARWLPDGNLEFLGRADDQVKIRGFRIELGEIEAALLQHPGVREA 901
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 705 VVIQREDESGEKYLCAYVVTEKDIPIP--EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSSHLE 782
Cdd:COG1020 902 VVVAREDAPGDKRLVAYVVPEAGAAAAaaLLRLALALLLPPYMVPAAVVLLLPLPLTGNGKLDRLALPAPAAAAAAAAAA 981
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 783 PTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYILEMEKSNYI 862
Cdd:COG1020 982 PPAEEEEEEAALALLLLLVVVVGDDDFFFFGGGLGLLLLLALARAARLLLLLLLLLLLFLAAAAAAAAAAAAAAAAAAAA 1061
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 863 SIEPVKQQEyYLASTSQKRMFIVDQFEDGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQ-- 940
Cdd:COG1020 1062 PLAAAAAPL-PLPPLLLSLLALLLALLLLLALLALLALLLLLLLLLLLLALLLLLALLLALLAALRARRAVRQEGPRLrl 1140
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 941 ----KIEPNVDFNIEYVHVNEKDADYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVE 1016
Cdd:COG1020 1141 lvalAAALALAALLALLLAAAAAAAELLAAAALLLLLALLLLALLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL 1220
|
..
gi 446807313 1017 LY 1018
Cdd:COG1020 1221 LL 1222
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
866-2046 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 706.15 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 866 PVKQQE----YYLASTSQKRMFivDQFEDGTNTTYNMPTILKVEG-DIckDKFENIFQSLIERHEILRTSFqILDGELVQ 940
Cdd:PRK12467 2637 PVAVGDiediYPLSPMQQGMLF--HTLYEGGAGDYINQMRVDVEGlDV--ERFRTAWQAVIDRHEILRSGF-LWDGELEE 2711
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 941 KIE--------PNVDFNIEYVHVNEKDADYL-IHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILI 1011
Cdd:PRK12467 2712 PLQvvykqarlPFSRLDWRDRADLEQALDALaAADRQQGFDLLSAPLLRLTLVRTGEDRHHLIYTNHHILMDGWSGSQLL 2791
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1012 KEFVELYKGNELPKLRVQYKDYVMW---QNGpyyknliSEQKNYWLTTLKG-ELPVLNFPTDFQRPTiQSFKGNVCSF-N 1086
Cdd:PRK12467 2792 GEVLQRYFGQPPPAREGRYRDYIAWlqaQDA-------EASEAFWKEQLAAlEEPTRLARALYPAPA-EAVAGHGAHYlH 2863
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1087 LGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHS--DTNHMIGMFINTLVMRNYLENDDEF 1164
Cdd:PRK12467 2864 LDATQTRQLIEFARRHRVTLNTLVQGAWLLLLQRFTGQDTVCFGATVAGRPAQlrGAEQQLGLFINTLPVIASPRAEQTV 2943
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1165 IEFLSRLKLNTLEAYENQDYPFeellegLDLHRDTSR--NPLFDTMFVFQNMdmnPISIGELEFTPYPFK------QSVS 1236
Cdd:PRK12467 2944 SDWLQQVQAQNLALREFEHTPL------ADIQRWAGQggEALFDSILVFENY---PISEALKQGAPSGLRfgavssREQT 3014
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1237 KFDLSLvATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFNKKENSNSN 1316
Cdd:PRK12467 3015 NYPLTL-AVGLGDTLELEFSYDRQHFDAAAIERLAESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPS 3093
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1317 YLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYL 1396
Cdd:PRK12467 3094 ERLVHQLIEAQVARTPEAPALVFGDQQLSYAELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYV 3173
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1397 PIDTDLPKQRVEYMLTDSGCSHVLVHQNSIIK-GIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPK 1475
Cdd:PRK12467 3174 PLDPEYPRERLAYMIEDSGVKLLLTQAHLLEQlPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPK 3253
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1476 GVMIEHRSLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLS 1555
Cdd:PRK12467 3254 GVGVRHGALANHLCWIAEAYELDAN--DRVLLFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIA 3331
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1556 YIPPTLLNEIY-DYFVRDNQKivLNKLLVGVEPIKTELLAKYDHLFRgNLQILNGYGPTEATVCCTSYRYESNKEITTQN 1634
Cdd:PRK12467 3332 CFPPAYLQQFAeDAGGADCAS--LDIYVFGGEAVPPAAFEQVKRKLK-PRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPY 3408
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1635 VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFE-RGEKLYKTGDIARWLPDGNIE 1713
Cdd:PRK12467 3409 APIGRPVAGRSIYVLDGQLNPVPVGVAGELYIGGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIE 3488
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1714 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQeDEAGEKYLCAYVVTE---KDIPIpEVRAYLATKLPHYMIP 1790
Cdd:PRK12467 3489 YLGRIDHQVKIRGFRIELGEIEARLLQHPSVREAVVLAR-DGAGGKQLVAYVVPAdpqGDWRE-TLRDHLAASLPDYMVP 3566
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1791 QQLIPIHNIPLTQNGKIDRSKLPKLNTLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENI 1870
Cdd:PRK12467 3567 AQLLVLAAMPLGPNGKVDRKALPDPDAKGSREYVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRI 3646
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1871 KRMFNVQLPLSLLFQKATIEQLSDViSRNKGIDSECLIPIQNRTNKDSQWFIIHGQGGGILNYYDLARELGEDKTVYGLQ 1950
Cdd:PRK12467 3647 RQSLGLKLSLRDLMSAPTIAELAGY-SPLGDVPVNLLLDLNRLETGFPALFCRHEGLGTVFDYEPLAVILEGDRHVLGLT 3725
|
1130 1140 1150 1160 1170 1180 1190 1200
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1951 SIGYDDSRFPNLSVEEMAVRYIEEIKQVKKEGPYTLLGWSFGGIVAFEMARKLEELGDKVSFLGLLDVHPIEQGREIlsl 2030
Cdd:PRK12467 3726 CRHLLDDGWQDTSLQAMAVQYADYILWQQAKGPYGLLGWSLGGTLARLVAELLEREGESEAFLGLFDNTLPLPDEFV--- 3802
|
1210
....*....|....*.
gi 446807313 2031 nIKNAFEELEKFNDQL 2046
Cdd:PRK12467 3803 -PQAEFLELLRQLGEL 3817
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
848-1905 |
0e+00 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 661.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 848 DFSKYILEMEKSNYISIEPVKQQEYYLASTSQKRMFIVDQFEDGTNTTYNMpTILKVEG-DIckDKFENIFQSLIERHEI 926
Cdd:PRK12316 4078 DFPLAGLDQARLDALPLPLGEIEDIYPLSPMQQGMLFHSLYEQEAGDYINQ-MRVDVQGlDV--ERFRAAWQAALDRHDV 4154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 927 LRTSF--QILDGELVQKIEPNVD--FNIEYVHVNEKDADYLI----HEFISPFDLSKPPLLRVLLLRIAEERHILVVDMH 998
Cdd:PRK12316 4155 LRSGFvwQGELGRPLQVVHKQVSlpFAELDWRGRADLQAALDalaaAERERGFDLQRAPLLRLVLVRTAEGRHHLIYTNH 4234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 999 HIISDGLSMGILIKEFVELYKGNELPKLRVQYKDYVMW---QNGpyyknliSEQKNYWLTtlkgELPVLNFPTDF----Q 1071
Cdd:PRK12316 4235 HILMDGWSNSQLLGEVLERYSGRPPAQPGGRYRDYIAWlqrQDA-------AASEAFWRE----QLAALDEPTRLaqaiA 4303
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1072 RPTIQSFKGNV-CSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHS--DTNHMIGMF 1148
Cdd:PRK12316 4304 RADLRSANGYGeHVRELDATATARLREFARTQRVTLNTLVQAAWLLLLQRYTGQDTVAFGATVAGRPAElpGIEGQIGLF 4383
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1149 INTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEgldlHRDTSRNPLFDTMFVFQNMdmnPIS-------- 1220
Cdd:PRK12316 4384 INTLPVIATPRAQQSVVEWLQQVQRQNLALREHEHTPLYEIQR----WAGQGGEALFDSLLVFENY---PVSealqqgap 4456
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1221 -------IGELEFTPYPFKQSVSkfdlslvateIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNIN 1293
Cdd:PRK12316 4457 gglrfgeVTNHEQTNYPLTLAVG----------LGETLSLQFSYDRGHFDAATIERLARHLTNLLEAMAEDPQRRLGELQ 4526
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1294 MLSIEEEHCIMNEFNKKENSNSNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGV 1373
Cdd:PRK12316 4527 LLEKAEQQRIVALWNRTDAGYPATRCVHQLVAERARMTPDAVAVVFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGI 4606
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1374 MMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVH-----QNSIIKGIefQGNVIDlMDMSFEEEP 1448
Cdd:PRK12316 4607 AMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAALLLTQshllqRLPIPDGL--ASLALD-RDEDWEGFP 4683
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1449 GEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGA 1528
Cdd:PRK12316 4684 AHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGERY--ELTPDDRVLQFMSFSFDGSHEGLYHPLINGA 4761
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1529 RMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELlakYDHLFRG--NLQI 1606
Cdd:PRK12316 4762 SVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGEPPSLRVYCFGGEAVAQAS---YDLAWRAlkPVYL 4838
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1607 LNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKF 1686
Cdd:PRK12316 4839 FNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQLNPLPVGVAGELYLGGEGVARGYLERPALTAERF 4918
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1687 IDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGeKYLCAYV 1765
Cdd:PRK12316 4919 VPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIELGEIEARLREHPAVREAVVIAQEGAVG-KQLVGYV 4997
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1766 V--TEKDIPIPEV--------RAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLN-TLGNSNYVPPRNEIDSSL 1834
Cdd:PRK12316 4998 VpqDPALADADEAqaelrdelKAALRERLPEYMVPAHLVFLARMPLTPNGKLDRKALPQPDaSLLQQAYVAPRSELEQQV 5077
|
1050 1060 1070 1080 1090 1100 1110
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1835 IDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSDVISRNKGIDSE 1905
Cdd:PRK12316 5078 AAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPLRELFQTPTLAAFVELAAAAGSGDDE 5148
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
279-772 |
0e+00 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 649.77 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd17655 1 ELFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 359 LPKQRVEYMLTDSGCSHVLTyQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd17655 81 YPEERIQYILEDSGADILLT-QSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEH 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 439 RSLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYIPPT 517
Cdd:cd17655 160 RGVVNLVEWANKVIYQGEH--LRVALFASISFDASVTEIFASLLSGNTLYIVRKEtVLDGQALTQYIRQNRITIIDLTPA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 518 LLNEIYDyfVRANQKISLNKLFVGVEPIKTELLAKYDHLFRGNLQILNLYGPTEATVCCTSYQYERDKEITTqNVPIGSP 597
Cdd:cd17655 238 HLKLLDA--ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQV-SVPIGKP 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 598 LLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDH 677
Cdd:cd17655 315 LGNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDH 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 678 QVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIP 757
Cdd:cd17655 395 QVKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIP 474
|
490
....*....|....*
gi 446807313 758 LTQNGKIDRKKLPQP 772
Cdd:cd17655 475 LTPNGKVDRKALPEP 489
|
|
| A_NRPS_Bac |
cd17655 |
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of ... |
1323-1814 |
0e+00 |
|
bacitracin synthetase and related proteins; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetases 1, 2, and 3 (BA1, also known as ATP-dependent cysteine adenylase or cysteine activase, BA2, also known as ATP-dependent lysine adenylase or lysine activase, and BA3, also known as ATP-dependent isoleucine adenylase or isoleucine activase) in Bacilli. Bacitracin is a mixture of related cyclic peptides used as a polypeptide antibiotic. This family also includes gramicidin synthetase 1 involved in synthesis of the cyclic peptide antibiotic gramicidin S via activation of phenylalanine. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341310 [Multi-domain] Cd Length: 490 Bit Score: 635.14 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL 1402
Cdd:cd17655 2 LFEEQAEKTPDHTAVVFEDQTLTYRELNERANQLARTLREKGVGPDTIVGIMAERSLEMIVGILGILKAGGAYLPIDPDY 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQRVEYMLTDSGCShVLVHQNSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHR 1482
Cdd:cd17655 82 PEERIQYILEDSGAD-ILLTQSHLQPPIAFIGLIDLLDEDTIYHEESENLEPVSKSDDLAYVIYTSGSTGKPKGVMIEHR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1483 SLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEEQVTLSYIPPTL 1561
Cdd:cd17655 161 GVVNLVEWANKVIYQGEH--LRVALFASISFDASVTEIFASLLSGNTLYIVRKEtVLDGQALTQYIRQNRITIIDLTPAH 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1562 LNEIYDyfVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFRGNLQILNGYGPTEATVCCTSYRYESNKEITTqNVPIGSPL 1641
Cdd:cd17655 239 LKLLDA--ADDSEGLSLKHLIVGGEALSTELAKKIIELFGTNPTITNAYGPTETTVDASIYQYEPETDQQV-SVPIGKPL 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1642 LNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQ 1721
Cdd:cd17655 316 GNTRIYILDQYGRPQPVGVAGELYIGGEGVARGYLNRPELTAEKFVDDPFVPGERMYRTGDLARWLPDGNIEFLGRIDHQ 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1722 VKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPL 1801
Cdd:cd17655 396 VKIRGYRIELGEIEARLLQHPDIKEAVVIARKDEQGQNYLCAYIVSEKELPVAQLREFLARELPDYMIPSYFIKLDEIPL 475
|
490
....*....|...
gi 446807313 1802 TQNGKIDRSKLPK 1814
Cdd:cd17655 476 TPNGKVDRKALPE 488
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
289-769 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 608.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 448
Cdd:cd05930 81 EDSGAKLVLT-----------------------------------DPDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 449 YEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIY-QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFV 527
Cdd:cd05930 126 QEAY--PLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLpEEVRKDPEALADLLAEEGITVLHLTPSLLRLLLQELE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 528 RANQKiSLNKLFVGVEPIKTELLAKYDHLFRGnLQILNLYGPTEATVCCTSYQYERDkEITTQNVPIGSPLLNTKIYILD 607
Cdd:cd05930 204 LAALP-SLRLVLVGGEALPPDLVRRWRELLPG-ARLVNLYGPTEATVDATYYRVPPD-DEEDGRVPIGRPIPNTRVYVLD 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 608 SFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIE 687
Cdd:cd05930 281 ENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGYRIE 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 688 LGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP--EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:cd05930 361 LGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDeeELRAHLAERLPDYMVPSAFVVLDALPLTPNGKVD 440
|
....
gi 446807313 766 RKKL 769
Cdd:cd05930 441 RKAL 444
|
|
| A_NRPS |
cd05930 |
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain ... |
1332-1812 |
0e+00 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341253 [Multi-domain] Cd Length: 444 Bit Score: 594.12 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd05930 1 PDAVAVVDGDQSLTYAELDARANRLARYLRERGVGPGDLVAVLLERSLEMVVAILAVLKAGAAYVPLDPSYPAERLAYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHqnsiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd05930 81 EDSGAKLVLTD-----------------------------------PDDLAYVIYTSGSTGKPKGVMVEHRGLVNLLLWM 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIY-QGEKFDVTKLVQVILEEQVTLSYIPPTLLNEiydyFV 1570
Cdd:cd05930 126 QEAY--PLTPGDRVLQFTSFSFDVSVWEIFGALLAGATLVVLpEEVRKDPEALADLLAEEGITVLHLTPSLLRL----LL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1571 RDNQKIVLNKL---LVGVEPIKTELLAKYDHLFRGnLQILNGYGPTEATVCCTSYRyESNKEITTQNVPIGSPLLNTKIY 1647
Cdd:cd05930 200 QELELAALPSLrlvLVGGEALPPDLVRRWRELLPG-ARLVNLYGPTEATVDATYYR-VPPDDEEDGRVPIGRPIPNTRVY 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1648 ILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGY 1727
Cdd:cd05930 278 VLDENLRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPNPFGPGERMYRTGDLVRWLPDGNLEFLGRIDDQVKIRGY 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1728 RIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--EVRAYLATKLPHYMIPQQLIPIHNIPLTQNG 1805
Cdd:cd05930 358 RIELGEIEAALLAHPGVREAAVVAREDGDGEKRLVAYVVPDEGGELDeeELRAHLAERLPDYMVPSAFVVLDALPLTPNG 437
|
....*..
gi 446807313 1806 KIDRSKL 1812
Cdd:cd05930 438 KVDRKAL 444
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
279-769 |
3.55e-174 |
|
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: 541.02 E-value: 3.55e-174
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd12117 1 ELFEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 359 LPKQRVEYMLTDSGCSHVLTYQNSiiKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd12117 81 LPAERLAFMLADAGAKVLLTDRSL--AGRAGGLEVAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 439 RSLTNFLC-AMYEDFSQDigitDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKF-DVPKLVQVILEEQVTLAYIPP 516
Cdd:cd12117 159 RGVVRLVKnTNYVTLGPD----DRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVTVLWLTA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 517 TLLNEIYDYFVRANQkiSLNKLFVGVEPIKTE----LLAKYDHLfrgnlQILNLYGPTEATVCCTSYQYERDKEITTQnV 592
Cdd:cd12117 235 ALFNQLADEDPECFA--GLRELLTGGEVVSPPhvrrVLAACPGL-----RLVNGYGPTENTTFTTSHVVTELDEVAGS-I 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 593 PIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 672
Cdd:cd12117 307 PIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 673 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIIS 752
Cdd:cd12117 387 GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVV 466
|
490
....*....|....*..
gi 446807313 753 IQNIPLTQNGKIDRKKL 769
Cdd:cd12117 467 LDELPLTANGKVDRRAL 483
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
22-1062 |
3.18e-172 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 590.59 E-value: 3.18e-172
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 22 YWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKDDVVIGM 101
Cdd:PRK12467 1307 YWKAQLGGEQPVLELPTDRPRPAVQSHRGARLAFELPPALAEGLRALARREGVTLFMLLLASFQTLLHRYSGQDDIRVGV 1386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 102 PVFKQGQEETV----FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNLPLLNtiVML 177
Cdd:PRK12467 1387 PIANRNRAETEgligFFVNTQVLRAEVDGQASFQQLLQQVKQAALEAQAHQDLPFEQLVEALQPERSLSHSPLFQ--VMF 1464
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 178 D-------------------------------DIHCYESTDKINSDMVirfmkneeqlkvqvdYNSTLYSEGLVSRIVNH 226
Cdd:PRK12467 1465 NhqrddhqaqaqlpglsveslswesqtaqfdlTLDTYESSEGLQASLT---------------YATDLFEASTIERLAGH 1529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 227 LYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTTRVHKTLLCetvtAPQLFEEQVKQNPNQIAIVCNGKEITYKQL 306
Cdd:PRK12467 1530 WLNLLQGLVADPERRLGELDLLDEAERRQILEGWNATHTGYPLARL----VHQLIEDQAAATPEAVALVFGEQELTYGEL 1605
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 307 NIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTY-----QN 381
Cdd:PRK12467 1606 NRRANRLAHRLIALGVGPEVLVGIAVERSLEMVVGLLAILKAGGAYVPLDPEYPRERLAYMIEDSGIELLLTQshlqaRL 1685
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 382 SIIKGVafQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDN 461
Cdd:PRK12467 1686 PLPDGL--RSLVLDQEDDWLEGYSDSNPAVNLAPQNLAYVIYTSGSTGRPKGAGNRHGALVNRLCATQEAY--QLSAADV 1761
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 462 VLFSSSISFDVTIFEIFVPLVCGARMTIYQ-GEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFV 540
Cdd:PRK12467 1762 VLQFTSFAFDVSVWELFWPLINGARLVIAPpGAHRDPEQLIQLIERQQVTTLHFVPSMLQQLLQMDEQVEHPLSLRRVVC 1841
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 541 GVEPIKTELLAKYDHLFrGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGE 620
Cdd:PRK12467 1842 GGEALEVEALRPWLERL-PDTGLFNLYGPTETAVDVTHWTCRRKDLEGRDSVPIGQPIANLSTYILDASLNPVPIGVAGE 1920
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 621 ICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYE 699
Cdd:PRK12467 1921 LYLGGVGLARGYLNRPALTAERFVADPFGTvGSRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLREQG 2000
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 700 TIKTAVVIQREDESGeKYLCAYVVTeKDIPIPE-----------VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKK 768
Cdd:PRK12467 2001 GVREAVVIAQDGANG-KQLVAYVVP-TDPGLVDddeaqvalraiLKNHLKASLPEYMVPAHLVFLARMPLTPNGKLDRKA 2078
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 769 LPQP-INNLKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVnKEFNVQLSIKSLFKFPVLV 847
Cdd:PRK12467 2079 LPAPdASELQQAYVAPQSELEQRLAAIWQDVLGLEQVGLHDNFFELGGDSIISIQVVSRA-RQAGIRFTPKDLFQHQTVQ 2157
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 848 DFSKYILEMEKSNYISIEPVKQQeyyLASTSQKRMFIVDQFEDGTNttYNMPTILKVEGDICKDKFENIFQSLIERHEIL 927
Cdd:PRK12467 2158 SLAAVAQEGDGTVSIDQGPVTGD---LPLLPIQQMFFADDIPERHH--WNQSVLLEPREALDAELLEAALQALLVHHDAL 2232
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 928 RTSFQILDGELVQKIEPNVDFNIEY---VHVNEKDA-DYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISD 1003
Cdd:PRK12467 2233 RLGFVQEDGGWSAMHRAPEQERRPLlwqVVVADKEElEALCEQAQRSLDLEEGPLLRAVLATLPDGSQRLLLVIHHLVVD 2312
|
1050 1060 1070 1080 1090 1100
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1004 GLSMGILIKE----FVELYKGN--ELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKG---ELP 1062
Cdd:PRK12467 2313 GVSWRILLEDlqtaYRQLQGGQpvKLPAKTSAFKAWAERLQTYAASAALADELGYWQAQLQGastELP 2380
|
|
| A_NRPS_Srf_like |
cd12117 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Bacillus subtilis ... |
1324-1812 |
2.49e-171 |
|
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: 533.32 E-value: 2.49e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLP 1403
Cdd:cd12117 3 FEEQAARTPDAVAVVYGDRSLTYAELNERANRLARRLRAAGVGPGDVVGVLAERSPELVVALLAVLKAGAAYVPLDPELP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1404 KQRVEYMLTDSGCShVLVHQNSIIKGIEFQGnVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRS 1483
Cdd:cd12117 83 AERLAFMLADAGAK-VLLTDRSLAGRAGGLE-VAVVIDEALDAGPAGNPAVPVSPDDLAYVMYTSGSTGRPKGVAVTHRG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1484 LTNFLC-AMYEDFSQDigitDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKF-DVTKLVQVILEEQVTLSYIPPTL 1561
Cdd:cd12117 161 VVRLVKnTNYVTLGPD----DRVLQTSPLAFDASTFEIWGALLNGARLVLAPKGTLlDPDALGALIAEEGVTVLWLTAAL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1562 LNEIydyfVRDNQKIV--LNKLLVGVEPIKTE----LLAKYDHLfrgnlQILNGYGPTEATVCCTSYRYESNKEITTQnV 1635
Cdd:cd12117 237 FNQL----ADEDPECFagLRELLTGGEVVSPPhvrrVLAACPGL-----RLVNGYGPTENTTFTTSHVVTELDEVAGS-I 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 PIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 1715
Cdd:cd12117 307 PIGRPIANTRVYVLDEDGRPVPPGVPGELYVGGDGLALGYLNRPALTAERFVADPFGPGERLYRTGDLARWLPDGRLEFL 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1716 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIP 1795
Cdd:cd12117 387 GRIDDQVKIRGFRIELGEIEAALRAHPGVREAVVVVREDAGGDKRLVAYVVAEGALDAAELRAFLRERLPAYMVPAAFVV 466
|
490
....*....|....*..
gi 446807313 1796 IHNIPLTQNGKIDRSKL 1812
Cdd:cd12117 467 LDELPLTANGKVDRRAL 483
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
902-1896 |
9.33e-171 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 586.15 E-value: 9.33e-171
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 902 LKVEGdICKDKFENIFQSLIERHEILRTSFQILDG--ELVQKIEPNVDFNIEYVHVNEKD------ADYLIHEFISPFDL 973
Cdd:PRK12316 1585 VDVQG-LDPDRFRAAWQATVDRHEILRSGFLWQDGleQPLQVIHKQVELPFAELDWRGREdlgqalDALAQAERQKGFDL 1663
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 974 SKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGNELPKLRVQYKDYVMWQNGPyyKNLISEqkNYW 1053
Cdd:PRK12316 1664 TRAPLLRLVLVRTGEGRHHLIYTNHHILMDGWSNAQLLGEVLQRYAGQPVAAPGGRYRDYIAWLQRQ--DAAASE--AFW 1739
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1054 lttlKGELPVLNFPTDFQRP--TIQSFKGNVCSFN-LGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVG 1130
Cdd:PRK12316 1740 ----KEQLAALEEPTRLAQAarTEDGQVGYGDHQQlLDPAQTRALAEFARAQKVTLNTLVQAAWLLLLQRYTGQETVAFG 1815
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1131 SPIAGRSH--SDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELlEGLDLHRDTSrnpLFDTM 1208
Cdd:PRK12316 1816 ATVAGRPAelPGIEQQIGLFINTLPVIAAPRPDQSVADWLQEVQALNLALREHEHTPLYDI-QRWAGQGGEA---LFDSL 1891
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1209 FVFQNMdmnPIS-------IGELEFTPyPFKQSVSKFDLSLvATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEV 1281
Cdd:PRK12316 1892 LVFENY---PVAealkqgaPAGLVFGR-VSNHEQTNYPLTL-AVTLGETLSLQYSYDRGHFDAAAIERLDRHLLHLLEQM 1966
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1282 TNNPRVRLRNINMLSIEEEHCIMNEFNKKENSNSNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLL 1361
Cdd:PRK12316 1967 AEDAQAALGELALLDAGERQRILADWDRTPEAYPRGPGVHQRIAEQAARAPEAIAVVFGDQHLSYAELDSRANRLAHRLR 2046
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1362 DQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcSHVLVHQNSIIKGIEFQGNVIDLM- 1440
Cdd:PRK12316 2047 ARGVGPEVRVAIAAERSFELVVALLAVLKAGGAYVPLDPNYPAERLAYMLEDSG-AALLLTQRHLLERLPLPAGVARLPl 2125
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1441 --DMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIF 1518
Cdd:PRK12316 2126 drDAEWADYPDTAPAVQLAGENLAYVIYTSGSTGLPKGVAVSHGALVAHCQAAGERY--ELSPADCELQFMSFSFDGAHE 2203
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1519 EIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDH 1598
Cdd:PRK12316 2204 QWFHPLLNGARVLIRDDELWDPEQLYDEMERHGVTILDFPPVYLQQLAEHAERDGRPPAVRVYCFGGEAVPAASLRLAWE 2283
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1599 LFRGNlQILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINR 1678
Cdd:PRK12316 2284 ALRPV-YLFNGYGPTEAVVTPLLWKCRPQDPCGAAYVPIGRALGNRRAYILDADLNLLAPGMAGELYLGGEGLARGYLNR 2362
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1679 KELTADKFIDHPFE-RGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQeDEAG 1757
Cdd:PRK12316 2363 PGLTAERFVPDPFSaSGERLYRTGDLARYRADGVVEYLGRIDHQVKIRGFRIELGEIEARLQAHPAVREAVVVAQ-DGAS 2441
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1758 EKYLCAYVV--TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLN-TLGNSNYVPPRNEIDSSL 1834
Cdd:PRK12316 2442 GKQLVAYVVpdDAAEDLLAELRAWLAARLPAYMVPAHWVVLERLPLNPNGKLDRKALPKPDvSQLRQAYVAPQEGLEQRL 2521
|
970 980 990 1000 1010 1020
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1835 IDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSDVI 1896
Cdd:PRK12316 2522 AAIWQAVLKVEQVGLDDHFFELGGHSLLATQVVSRVRQDLGLEVPLRILFERPTLAAFAASL 2583
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
890-2023 |
4.55e-170 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 558.12 E-value: 4.55e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 890 DGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNI-EYVHVNEKD-----ADYL 963
Cdd:PRK10252 24 SPLPSAWSVAHYVELTGELDAPLLARAVVAGLAEADTLRMRFTEDNGEVWQWVDPALTFPLpEIIDLRTQPdphaaAQAL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 964 IH-EFISPFDL-SKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKG---------NELPKLRVQYKD 1032
Cdd:PRK10252 104 MQaDLQQDLRVdSGKPLVFHQLIQLGDNRWYWYQRYHHLLVDGFSFPAITRRIAAIYCAwlrgeptpaSPFTPFADVVEE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1033 YVMWQNGPYYKnlisEQKNYWL---------TTLKGELPVLNFPT-DFQRPTIQSfkgnvcsfnlgTDLTFkVNKLATET 1102
Cdd:PRK10252 184 YQRYRASEAWQ----RDAAFWAeqrrqlpppASLSPAPLPGRSASaDILRLKLEF-----------TDGAF-RQLAAQAS 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1103 GTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQ 1182
Cdd:PRK10252 248 GVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRLGSAALTATGPVLNVLPLRVHIAAQETLPELATRLAAQLKKMRRHQ 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1183 DYPFEELLEglDLHRDTSRNPLFDTMFVFQNMDmNPISIGELEFTPY-----PFKqsvskfDLSL-VATEIDNNIHLKVE 1256
Cdd:PRK10252 328 RYDAEQIVR--DSGRAAGDEPLFGPVLNIKVFD-YQLDFPGVQAQTHtlatgPVN------DLELaLFPDEHGGLSIEIL 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1257 YSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSiEEEHCIMNEFNKKENSNSNYLLVhKMFEEQVKRNPNQIA 1336
Cdd:PRK10252 399 ANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILL-PGEYAQLAQVNATAVEIPETTLS-ALVAQQAAKTPDAPA 476
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1337 VVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGC 1416
Cdd:PRK10252 477 LADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYPDDRLKMMLEDARP 556
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1417 SHVLVHQnsiikgiEFQGNVIDLMDMSFEE------EPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCA 1490
Cdd:PRK10252 557 SLLITTA-------DQLPRFADVPDLTSLCynaplaPQGAAPLQLSQPHHTAYIIFTSGSTGRPKGVMVGQTAIVNRLLW 629
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1491 MYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKF-DVTKLVQVILEEQVTLSYIPPTLLneiyDYF 1569
Cdd:PRK10252 630 MQNHYP--LTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHrDPLAMQQFFAEYGVTTTHFVPSML----AAF 703
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1570 VR--DNQKIV-----LNKLLVGVEPIKTELLAKYDHLFRGNLQilNGYGPTEATVCCTSYRY--ESNKEITTQNVPIGSP 1640
Cdd:PRK10252 704 VAslTPEGARqscasLRQVFCSGEALPADLCREWQQLTGAPLH--NLYGPTEAAVDVSWYPAfgEELAAVRGSSVPIGYP 781
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1641 LLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDH 1720
Cdd:PRK10252 782 VWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVEYLGRSDD 861
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1721 QVKIRGYRIELGEIEASLLKYETIKTAV----VIDQEDEAG--EKYLCAYVVTEKDIPI--PEVRAYLATKLPHYMIPQQ 1792
Cdd:PRK10252 862 QLKIRGQRIELGEIDRAMQALPDVEQAVthacVINQAAATGgdARQLVGYLVSQSGLPLdtSALQAQLRERLPPHMVPVV 941
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1793 LIPIHNIPLTQNGKIDRSKLPKLNTLGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKR 1872
Cdd:PRK10252 942 LLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMKLAAQLSR 1021
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1873 MFNVQLPLSLLFQKATIEQLSDVI------SRNKGIDSecLIPIqnRTNKDSQWFIIHGQGGGILNYYDLARELGEDKTV 1946
Cdd:PRK10252 1022 QFARQVTPGQVMVASTVAKLATLLdaeedeSRRLGFGT--ILPL--REGDGPTLFCFHPASGFAWQFSVLSRYLDPQWSI 1097
|
1130 1140 1150 1160 1170 1180 1190
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 1947 YGLQSIGYDDSRFPNLSVEEMAVRYIEEIKQVKKEGPYTLLGWSFGGIVAFEMARKLEELGDKVSFLGLLDVHPIEQ 2023
Cdd:PRK10252 1098 YGIQSPRPDGPMQTATSLDEVCEAHLATLLEQQPHGPYHLLGYSLGGTLAQGIAARLRARGEEVAFLGLLDTWPPET 1174
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
21-1062 |
7.07e-170 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 583.46 E-value: 7.07e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 21 EYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKDDVVIG 100
Cdd:PRK12316 241 EYWRAQLGEEHPVLELPTDHPRPAVPSYRGSRYEFSIDPALAEALRGTARRQGLTLFMLLLGAFNVLLHRYSGQTDIRVG 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 101 MPVFKQGQEETV----FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNLPLLNtiVM 176
Cdd:PRK12316 321 VPIANRNRAEVEgligFFVNTQVLRSVFDGRTRVATLLAGVKDTVLGAQAHQDLPFERLVEALKVERSLSHSPLFQ--VM 398
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 177 LDDIHCYESTDKINS------------------DMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLYNILDILMKDP 238
Cdd:PRK12316 399 YNHQPLVADIEALDTvaglefgqlewksrttqfDLTLDTYEKGGRLHAALTYATDLFEARTVERMARHWQNLLRGMVENP 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 239 NKSAMDLDVMPKTEKNQILFDFNHTTRVHKTLLCetvtAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLL 318
Cdd:PRK12316 479 QARVDELPMLDAEERGQLVEGWNATAAEYPLQRG----VHRLFEEQVERTPEAPALAFGEETLDYAELNRRANRLAHALI 554
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 319 DQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSIIKGVAFQGSVINLMD 398
Cdd:PRK12316 555 ERGVGPDVLVGVAMERSIEMVVALLAILKAGGAYVPLDPEYPAERLAYMLEDSGVQLLLSQSHLGRKLPLAAGVQVLDLD 634
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 399 IP---FEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIF 475
Cdd:PRK12316 635 RPaawLEGYSEENPGTELNPENLAYVIYTSGSTGKPKGAGNRHRALSNRLCWMQQAYGLGVG--DTVLQKTPFSFDVSVW 712
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 476 EIFVPLVCGARMTI-YQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYdYFVRANQKISLNKLFVGVEPIKTELLAKYD 554
Cdd:PRK12316 713 EFFWPLMSGARLVVaAPGDHRDPAKLVELINREGVDTLHFVPSMLQAFL-QDEDVASCTSLRRIVCSGEALPADAQEQVF 791
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 555 HLfRGNLQILNLYGPTEATVCCTsyqYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYIN 634
Cdd:PRK12316 792 AK-LPQAGLYNLYGPTEAAIDVT---HWTCVEEGGDSVPIGRPIANLACYILDANLEPVPVGVLGELYLAGRGLARGYHG 867
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 635 RKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDesg 714
Cdd:PRK12316 868 RPGLTAERFVPSPFVAGERMYRTGDLARYRADGVIEYAGRIDHQVKLRGLRIELGEIEARLLEHPWVREAAVLAVDG--- 944
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 715 eKYLCAYVVTEKDI-PIPEV-RAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQP-INNLKSSHLEPTNSTERKL 791
Cdd:PRK12316 945 -KQLVGYVVLESEGgDWREAlKAHLAASLPEYMVPAQWLALERLPLTPNGKLDRKALPAPeASVAQQGYVAPRNALERTL 1023
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 792 VEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVnKEFNVQLSIKSLFKFPVLVDFSKyILEMEKSNYISIEPVKQQe 871
Cdd:PRK12316 1024 AAIWQDVLGVERVGLDDNFFELGGDSIVSIQVVSRA-RQAGIQLSPRDLFQHQTIRSLAL-VAKAGQATAADQGPASGE- 1100
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 872 yyLASTSQKRMFivdqFEDG--TNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFN 949
Cdd:PRK12316 1101 --VALAPVQRWF----FEQAipQRQHWNQSLLLQARQPLDPDRLGRALERLVAHHDALRLRFREEDGGWQQAYAAPQAGE 1174
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 950 IEYVH--VNEKDADYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKgNELPKLR 1027
Cdd:PRK12316 1175 VLWQRqaASEEELLALCEEAQRSLDLEQGPLLRALLVDMADGSQRLLLVIHHLVVDGVSWRILLEDLQRAYA-DLDADLP 1253
|
1050 1060 1070
....*....|....*....|....*....|....*....
gi 446807313 1028 VQYKDYVMW-QNGPYYKNLISEQKNYWLTTLKG---ELP 1062
Cdd:PRK12316 1254 ARTSSYQAWaRRLHEHAGARAEELDYWQAQLEDaphELP 1292
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
7-1136 |
2.98e-169 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 581.53 E-value: 2.98e-169
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:PRK12316 2776 QRAWMDSGEGARQLDYWRERLGGEQPVLELPLDRPRPALQSHRGARLDVALDVALSRELLALARREGVTLFMLLLASFQV 2855
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 87 LLSRYTDKDDVVIGMPVFKQGQEETV----FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLD 162
Cdd:PRK12316 2856 LLHRYSGQSDIRVGVPIANRNRAETErligFFVNTQVLRAQVDAQLAFRDLLGQVKEQALGAQAHQDLPFEQLVEALQPE 2935
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 163 GESNNLPLLNTIVMLDDIHCYEST-------------DKINSDMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLYN 229
Cdd:PRK12316 2936 RSLSHSPLFQVMYNHQSGERAAAQlpglhiesfawdgAATQFDLALDTWESAEGLGASLTYATDLFDARTVERLARHWQN 3015
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 230 ILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTTRVHKTLLCetvtAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIK 309
Cdd:PRK12316 3016 LLRGMVENPQRSVDELAMLDAEERGQLLEAWNATAAEYPLERG----VHRLFEEQVERTPDAVALAFGEQRLSYAELNRR 3091
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 310 ANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyqNSIIKGVAF 389
Cdd:PRK12316 3092 ANRLAHRLIERGVGPDVLVGVAVERSLEMVVGLLAILKAGGAYVPLDPEYPEERLAYMLEDSGAQLLLS--QSHLRLPLA 3169
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 390 QGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITDNVLFSSSIS 469
Cdd:PRK12316 3170 QGVQVLDLDRGDENYAEANPAIRTMPENLAYVIYTSGSTGKPKGVGIRHSALSNHLCWMQQAY--GLGVGDRVLQFTTFS 3247
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 470 FDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVtlAYIPPTLLNEIYDYF--VRANQKISLNKLFVGVEPIKT 547
Cdd:PRK12316 3248 FDVFVEELFWPLMSGARVVLAGPEDWRDPALLVELINSEG--VDVLHAYPSMLQAFLeeEDAHRCTSLKRIVCGGEALPA 3325
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 548 ELLAKYDhlfrGNLQILNLYGPTEATVCCTSYQYErdkEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIG 627
Cdd:PRK12316 3326 DLQQQVF----AGLPLYNLYGPTEATITVTHWQCV---EEGKDAVPIGRPIANRACYILDGSLEPVPVGALGELYLGGEG 3398
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 628 LARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI 707
Cdd:PRK12316 3399 LARGYHNRPGLTAERFVPDPFVPGERLYRTGDLARYRADGVIEYIGRVDHQVKIRGFRIELGEIEARLLEHPWVREAVVL 3478
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 708 QREDESgekyLCAYVVTEKDIP-IPEV-RAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQP-INNLKSSHLEPT 784
Cdd:PRK12316 3479 AVDGRQ----LVAYVVPEDEAGdLREAlKAHLKASLPEYMVPAHLLFLERMPLTPNGKLDRKALPRPdAALLQQDYVAPV 3554
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 785 NSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVnKEFNVQLSIKSLFKFPVLVDFSKyILEMEKSNYISI 864
Cdd:PRK12316 3555 NELERRLAAIWADVLKLEQVGLTDNFFELGGDSIISLQVVSRA-RQAGIRFTPKDLFQHQTIQGLAR-VARVGGGVAVDQ 3632
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 865 EPVK--------QQEYYLASTSQKRMfivdqfedgtnttYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDG 936
Cdd:PRK12316 3633 GPVSgetlllpiQQQFFEEPVPERHH-------------WNQSLLLKPREALDAAALEAALQALVEHHDALRLRFVEDAG 3699
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 937 ----ELVQKIEPN-VDFNIEYVHVNEKDAdyLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILI 1011
Cdd:PRK12316 3700 gwtaEHLPVELGGaLLWRAELDDAEELER--LGEEAQRSLDLADGPLLRALLATLADGSQRLLLVIHHLVVDGVSWRILL 3777
|
1050 1060 1070 1080 1090 1100 1110 1120
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1012 KEFVELYKGN------ELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKG---ELPVLNFPTDFQRPTIQSFKGnv 1082
Cdd:PRK12316 3778 EDLQQAYQQLlqgeapRLPAKTSSFKAWAERLQEHARGEALKAELAYWQEQLQGvssELPCDHPQGALQNRHAASVQT-- 3855
|
1130 1140 1150 1160 1170
....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1083 csfNLGTDLTFKVNKLATETGTTPYM-ILLAIYNILLSRYTGQEDIIVGSPIAGR 1136
Cdd:PRK12316 3856 ---RLDRELTRRLLQQAPAAYRTQVNdLLLTALARVVCRWTGEASALVQLEGHGR 3907
|
|
| PRK12467 |
PRK12467 |
peptide synthase; Provisional |
87-1042 |
8.57e-165 |
|
peptide synthase; Provisional
Pssm-ID: 237108 [Multi-domain] Cd Length: 3956 Bit Score: 567.48 E-value: 8.57e-165
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 87 LLSRYTDKDDV-----VIGMPVFKQGQEETV--FQNNFLLLRTqINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLL 159
Cdd:PRK12467 2894 LLQRFTGQDTVcfgatVAGRPAQLRGAEQQLglFINTLPVIAS-PRAEQTVSDWLQQVQAQNLALREFEHTPLADIQRWA 2972
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 160 SLDGESnnlpLLNTIVMLDDIHCYES-TDKINSDMVIRFMKNEEQ--------------LKVQVDYNSTLYSEGLVSRIV 224
Cdd:PRK12467 2973 GQGGEA----LFDSILVFENYPISEAlKQGAPSGLRFGAVSSREQtnypltlavglgdtLELEFSYDRQHFDAAAIERLA 3048
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 225 NHLYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTTRVHKTLLCetvtAPQLFEEQVKQNPNQIAIVCNGKEITYK 304
Cdd:PRK12467 3049 ESFDRLLQAMLNNPAARLGELPTLAAHERRQVLHAWNATAAAYPSERL----VHQLIEAQVARTPEAPALVFGDQQLSYA 3124
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 305 QLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSII 384
Cdd:PRK12467 3125 ELNRRANRLAHRLIAIGVGPDVLVGVAVERSVEMIVALLAVLKAGGAYVPLDPEYPRERLAYMIEDSGVKLLLTQAHLLE 3204
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 385 K-GVAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGitDNVL 463
Cdd:PRK12467 3205 QlPAPAGDTALTLDRLDLNGYSENNPSTRVMGENLAYVIYTSGSTGKPKGVGVRHGALANHLCWIAEAYELDAN--DRVL 3282
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 464 FSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKiSLNKLFVGVE 543
Cdd:PRK12467 3283 LFMSFSFDGAQERFLWTLICGGCLVVRDNDLWDPEELWQAIHAHRISIACFPPAYLQQFAEDAGGADCA-SLDIYVFGGE 3361
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 544 PIKTELLAKYDHLFRgNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICI 623
Cdd:PRK12467 3362 AVPPAAFEQVKRKLK-PRGLTNGYGPTEAVVTVTLWKCGGDAVCEAPYAPIGRPVAGRSIYVLDGQLNPVPVGVAGELYI 3440
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 624 SGIGLARGYINRKELTADKFIDHPFE-RGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIK 702
Cdd:PRK12467 3441 GGVGLARGYHQRPSLTAERFVADPFSgSGGRLYRTGDLARYRADGVIEYLGRIDHQVKIRGFRIELGEIEARLLQHPSVR 3520
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 703 TAVVIQREDESGeKYLCAYVVTE---KDIPIpEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSS 779
Cdd:PRK12467 3521 EAVVLARDGAGG-KQLVAYVVPAdpqGDWRE-TLRDHLAASLPDYMVPAQLLVLAAMPLGPNGKVDRKALPDPDAKGSRE 3598
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 780 HLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYIlemeks 859
Cdd:PRK12467 3599 YVAPRSEVEQQLAAIWADVLGVEQVGVTDNFFELGGDSLLALQVLSRIRQSLGLKLSLRDLMSAPTIAELAGYS------ 3672
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 860 nyisiePVKQQEYYLASTSQKRmfivdqfedgtnttynmptilkvegdickdkfENIFQSLIERHEILRTSFqilDGELV 939
Cdd:PRK12467 3673 ------PLGDVPVNLLLDLNRL--------------------------------ETGFPALFCRHEGLGTVF---DYEPL 3711
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 940 QKIepnvdfnieyvhvnekdadylihefispfdlskppllrvlllrIAEERHILVVDMHHIISDGlsmgilikefvelYK 1019
Cdd:PRK12467 3712 AVI-------------------------------------------LEGDRHVLGLTCRHLLDDG-------------WQ 3735
|
970 980
....*....|....*....|....*
gi 446807313 1020 GNELPKLRVQYKDYVMWQN--GPYY 1042
Cdd:PRK12467 3736 DTSLQAMAVQYADYILWQQakGPYG 3760
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
279-770 |
1.15e-164 |
|
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: 514.29 E-value: 1.15e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd17644 4 QLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLDPN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 359 LPKQRVEYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd17644 84 YPQERLTYILEDAQISVLLT-----------------------------------QPENLAYVIYTSGSTGKPKGVMIEH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 439 RSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKF-DVPKLVQVILEEQVTLAYIPPT 517
Cdd:cd17644 129 QSLVNLSHGLIKEY--GITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRsSLEDFVQYIQQWQLTVLSLPPA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 518 LLNEIYDYFVRANQKI--SLNKLFVGVEPIKTELLAKYDHLFRGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIG 595
Cdd:cd17644 207 YWHLLVLELLLSTIDLpsSLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSVPIG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 596 SPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER--GEKLYKTGDIARWLPDGNIEYLG 673
Cdd:cd17644 287 RPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIEYLG 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 674 RVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKD--IPIPEVRAYLATKLPYYMIPQQII 751
Cdd:cd17644 367 RIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEesPSTVELRQFLKAKLPDYMIPSAFV 446
|
490
....*....|....*....
gi 446807313 752 SIQNIPLTQNGKIDRKKLP 770
Cdd:cd17644 447 VLEELPLTPNGKIDRRALP 465
|
|
| A_NRPS_ApnA-like |
cd17644 |
similar to adenylation domain of anabaenopeptin synthetase (ApnA); This family of the ... |
1320-1813 |
1.76e-164 |
|
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: 513.52 E-value: 1.76e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:cd17644 2 IHQLFEEQVERTPDAVAVVFEDQQLTYEELNTKANQLAHYLQSLGVKSESLVGICVERSLEMIIGLLAILKAGGAYVPLD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSGCShVLVHQnsiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMI 1479
Cdd:cd17644 82 PNYPQERLTYILEDAQIS-VLLTQ----------------------------------PENLAYVIYTSGSTGKPKGVMI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1480 EHRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKF-DVTKLVQVILEEQVTLSYIP 1558
Cdd:cd17644 127 EHQSLVNLSHGLIKEY--GITSSDRVLQFASIAFDVAAEEIYVTLLSGATLVLRPEEMRsSLEDFVQYIQQWQLTVLSLP 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1559 PTLLNEIYDYFVRDNQKIV--LNKLLVGVEPIKTELLAKYDHLFRGNLQILNGYGPTEATVCCTSYRYESNKEITTQNVP 1636
Cdd:cd17644 205 PAYWHLLVLELLLSTIDLPssLRLVIVGGEAVQPELVRQWQKNVGNFIQLINVYGPTEATIAATVCRLTQLTERNITSVP 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1637 IGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER--GEKLYKTGDIARWLPDGNIEY 1714
Cdd:cd17644 285 IGRPIANTQVYILDENLQPVPVGVPGELHIGGVGLARGYLNRPELTAEKFISHPFNSseSERLYKTGDLARYLPDGNIEY 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1715 LGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKD--IPIPEVRAYLATKLPHYMIPQQ 1792
Cdd:cd17644 365 LGRIDNQVKIRGFRIELGEIEAVLSQHNDVKTAVVIVREDQPGNKRLVAYIVPHYEesPSTVELRQFLKAKLPDYMIPSA 444
|
490 500
....*....|....*....|.
gi 446807313 1793 LIPIHNIPLTQNGKIDRSKLP 1813
Cdd:cd17644 445 FVVLEELPLTPNGKIDRRALP 465
|
|
| PRK12316 |
PRK12316 |
peptide synthase; Provisional |
76-851 |
1.02e-162 |
|
peptide synthase; Provisional
Pssm-ID: 237054 [Multi-domain] Cd Length: 5163 Bit Score: 561.50 E-value: 1.02e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 76 LYTILLSGVKYLLSRYTDKDDVVIGMPVF-----KQGQEETV-FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCH 149
Cdd:PRK12316 4339 LNTLVQAAWLLLLQRYTGQDTVAFGATVAgrpaeLPGIEGQIgLFINTLPVIATPRAQQSVVEWLQQVQRQNLALREHEH 4418
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 150 FPFNKLTQLLSLDGES--------NNLPLLNTI-------VMLDDIHCYESTdkiNSDMVIRfMKNEEQLKVQVDYNSTL 214
Cdd:PRK12316 4419 TPLYEIQRWAGQGGEAlfdsllvfENYPVSEALqqgapggLRFGEVTNHEQT---NYPLTLA-VGLGETLSLQFSYDRGH 4494
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 215 YSEGLVSRIVNHLYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTTRVHKTLLCetvtAPQLFEEQVKQNPNQIAI 294
Cdd:PRK12316 4495 FDAATIERLARHLTNLLEAMAEDPQRRLGELQLLEKAEQQRIVALWNRTDAGYPATRC----VHQLVAERARMTPDAVAV 4570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 295 VCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCS 374
Cdd:PRK12316 4571 VFDEEKLTYAELNRRANRLAHALIARGVGPEVLVGIAMERSAEMMVGLLAVLKAGGAYVPLDPEYPRERLAYMMEDSGAA 4650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 375 HVLTyQNSIIKGVAFQGSVINLMDIPFEEEQ---VEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYED 451
Cdd:PRK12316 4651 LLLT-QSHLLQRLPIPDGLASLALDRDEDWEgfpAHDPAVRLHPDNLAYVIYTSGSTGRPKGVAVSHGSLVNHLHATGER 4729
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 452 FsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQ 531
Cdd:PRK12316 4730 Y--ELTPDDRVLQFMSFSFDGSHEGLYHPLINGASVVIRDDSLWDPERLYAEIHEHRVTVLVFPPVYLQQLAEHAERDGE 4807
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 532 KISLNKLFVGVEPIKTELlakYDHLFRG--NLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYILDSF 609
Cdd:PRK12316 4808 PPSLRVYCFGGEAVAQAS---YDLAWRAlkPVYLFNGYGPTETTVTVLLWKARDGDACGAAYMPIGTPLGNRSGYVLDGQ 4884
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 610 HRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIEL 688
Cdd:PRK12316 4885 LNPLPVGVAGELYLGGEGVARGYLERPALTAERFVPDPFgAPGGRLYRTGDLARYRADGVIDYLGRVDHQVKIRGFRIEL 4964
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 689 GEIEASLLKYETIKTAVVIQREDESGeKYLCAYVV--TEKDIPIPEV--------RAYLATKLPYYMIPQQIISIQNIPL 758
Cdd:PRK12316 4965 GEIEARLREHPAVREAVVIAQEGAVG-KQLVGYVVpqDPALADADEAqaelrdelKAALRERLPEYMVPAHLVFLARMPL 5043
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 759 TQNGKIDRKKLPQP-INNLKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSI 837
Cdd:PRK12316 5044 TPNGKLDRKALPQPdASLLQQAYVAPRSELEQQVAAIWAEVLQLERVGLDDNFFELGGHSLLAIQVTSRIQLELGLELPL 5123
|
810
....*....|....
gi 446807313 838 KSLFKFPVLVDFSK 851
Cdd:PRK12316 5124 RELFQTPTLAAFVE 5137
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
278-769 |
4.29e-159 |
|
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: 499.88 E-value: 4.29e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 278 PQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDT 357
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 358 ELPKQRVEYMLTDSGCSHVLTYQNSIIKGVAfQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIE 437
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPA-GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 438 HRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQ--GEKfDVPKLVQVILEEQVTLAYIP 515
Cdd:cd17646 160 HAGIVNRLLWMQDEY--PLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARpgGHR-DPAYLAALIREHGVTTCHFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 516 PTLLneiyDYFV---RANQKISLNKLFVGVEPIKTELLAKYDHLFRGNLQilNLYGPTEATVCCTSYQYERDKEITTqnV 592
Cdd:cd17646 237 PSML----RVFLaepAAGSCASLRRVFCSGEALPPELAARFLALPGAELH--NLYGPTEAAIDVTHWPVRGPAETPS--V 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 593 PIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 672
Cdd:cd17646 309 PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 673 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV---TEKDIPIPEVRAYLATKLPYYMIPQQ 749
Cdd:cd17646 389 GRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVpaaGAAGPDTAALRAHLAERLPEYMVPAA 468
|
490 500
....*....|....*....|
gi 446807313 750 IISIQNIPLTQNGKIDRKKL 769
Cdd:cd17646 469 FVVLDALPLTANGKLDRAAL 488
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
875-1285 |
2.63e-158 |
|
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: 494.95 E-value: 2.63e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 875 ASTSQKRMFIVDQFEDGtNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVH 954
Cdd:cd19531 4 LSFAQQRLWFLDQLEPG-SAAYNIPGALRLRGPLDVAALERALNELVARHEALRTTFVEVDGEPVQVILPPLPLPLPVVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 955 V-------NEKDADYLIHEFIS-PFDLS----------KppllrvlllrIAEERHILVVDMHHIISDGLSMGILIKEFVE 1016
Cdd:cd19531 83 LsglpeaeREAEAQRLAREEARrPFDLArgpllratllR----------LGEDEHVLLLTMHHIVSDGWSMGVLLRELAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1017 LYKG------NELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTD 1090
Cdd:cd19531 153 LYAAflagrpSPLPPLPIQYADYAVWQREWLQGEVLERQLAYWREQLAGAPPVLELPTDRPRPAVQSFRGARVRFTLPAE 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1091 LTFKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSR 1170
Cdd:cd19531 233 LTAALRALARREGATLFMTLLAAFQVLLHRYSGQDDIVVGTPVAGRNRAELEGLIGFFVNTLVLRTDLSGDPTFRELLAR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1171 LKLNTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIGELEFTPYPFKQSVSKFDLSLVATEIDNN 1250
Cdd:cd19531 313 VRETALEAYAHQDLPFEKLVEALQPERDLSRSPLFQVMFVLQNAPAAALELPGLTVEPLEVDSGTAKFDLTLSLTETDGG 392
|
410 420 430
....*....|....*....|....*....|....*
gi 446807313 1251 IHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19531 393 LRGSLEYNTDLFDAATIERMAGHFQTLLEAIVADP 427
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
289-770 |
2.27e-156 |
|
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: 491.99 E-value: 2.27e-156
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGCSHVLTyQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 448
Cdd:cd17656 82 LDSGVRVVLT-QRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 449 YEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYIPPTLLNEIydyfv 527
Cdd:cd17656 161 REKTNINFS--DKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREEtKRDVEQLFDLVKRHNIEVVFLPVAFLKFI----- 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 528 rANQKISLNKLFVGVEPIKT---ELLAK---YDHLFRGNLQILNLYGPTEATVCCTsyqYERDKEITTQNVP-IGSPLLN 600
Cdd:cd17656 234 -FSEREFINRFPTCVKHIITageQLVITnefKEMLHEHNVHLHNHYGPSETHVVTT---YTINPEAEIPELPpIGKPISN 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 601 TKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVK 680
Cdd:cd17656 310 TWIYILDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVK 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 681 IRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQ 760
Cdd:cd17656 390 IRGYRIELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTP 469
|
490
....*....|
gi 446807313 761 NGKIDRKKLP 770
Cdd:cd17656 470 NGKVDRKALP 479
|
|
| A_NRPS_ProA |
cd17656 |
gramicidin S synthase 2, also known as ATP-dependent proline adenylase; This family of the ... |
1332-1813 |
1.12e-153 |
|
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: 484.29 E-value: 1.12e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd17656 2 PDAVAVVFENQKLTYRELNERSNQLARFLREKGVKKDSIVAIMMERSAEMIVGILGILKAGGAFVPIDPEYPEERRIYIM 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVhQNSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd17656 82 LDSGVRVVLT-QRHLKSKLSFNKSTILLEDPSISQEDTSNIDYINNSDDLLYIIYTSGTTGKPKGVQLEHKNMVNLLHFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEEQVTLSYIPPTLLNEIYDY-- 1568
Cdd:cd17656 161 REKTNINFS--DKVLQFATCSFDVCYQEIFSTLLSGGTLYIIREEtKRDVEQLFDLVKRHNIEVVFLPVAFLKFIFSEre 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1569 FVRDNQKIVLNKLLVGVEPIKTELLAKYdhLFRGNLQILNGYGPTEATVCcTSYRYESNKEITtQNVPIGSPLLNTKIYI 1648
Cdd:cd17656 239 FINRFPTCVKHIITAGEQLVITNEFKEM--LHEHNVHLHNHYGPSETHVV-TTYTINPEAEIP-ELPPIGKPISNTWIYI 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1649 LDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYR 1728
Cdd:cd17656 315 LDQEQQLQPQGIVGELYISGASVARGYLNRQELTAEKFFPDPFDPNERMYRTGDLARYLPDGNIEFLGRADHQVKIRGYR 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1729 IELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:cd17656 395 IELGEIEAQLLNHPGVSEAVVLDKADDKGEKYLCAYFVMEQELNISQLREYLAKQLPEYMIPSFFVPLDQLPLTPNGKVD 474
|
....*
gi 446807313 1809 RSKLP 1813
Cdd:cd17656 475 RKALP 479
|
|
| A_NRPS_AB3403-like |
cd17646 |
Peptide Synthetase; The adenylation (A) domain of NRPS recognizes a specific amino acid or ... |
1321-1812 |
1.58e-153 |
|
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: 484.09 E-value: 1.58e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1321 HKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDT 1400
Cdd:cd17646 1 HALVAEQAARTPDAPAVVDEGRTLTYRELDERANRLAHLLRARGVGPEDRVAVLLPRSADLVVALLAVLKAGAAYLPLDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1401 DLPKQRVEYMLTDSGCSHVLVHQNSIIKGIEfQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIE 1480
Cdd:cd17646 81 GYPADRLAYMLADAGPAVVLTTADLAARLPA-GGDVALLGDEALAAPPATPPLVPPRPDNLAYVIYTSGSTGRPKGVMVT 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1481 HRSLTNFLCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQ--GEKfDVTKLVQVILEEQVTLSYIP 1558
Cdd:cd17646 160 HAGIVNRLLWMQDEY--PLGPGDRVLQKTPLSFDVSVWELFWPLVAGARLVVARpgGHR-DPAYLAALIREHGVTTCHFV 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1559 PTLLneiyDYFV---RDNQKIVLNKLLVGVEPIKTELLAKYDHLFRGNLQilNGYGPTEATVCCTSYRYESNKEITTqnV 1635
Cdd:cd17646 237 PSML----RVFLaepAAGSCASLRRVFCSGEALPPELAARFLALPGAELH--NLYGPTEAAIDVTHWPVRGPAETPS--V 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 PIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 1715
Cdd:cd17646 309 PIGRPVPNTRLYVLDDALRPVPVGVPGELYLGGVQLARGYLGRPALTAERFVPDPFGPGSRMYRTGDLARWRPDGALEFL 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1716 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV---TEKDIPIPEVRAYLATKLPHYMIPQQ 1792
Cdd:cd17646 389 GRSDDQVKIRGFRVEPGEIEAALAAHPAVTHAVVVARAAPAGAARLVGYVVpaaGAAGPDTAALRAHLAERLPEYMVPAA 468
|
490 500
....*....|....*....|
gi 446807313 1793 LIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd17646 469 FVVLDALPLTANGKLDRAAL 488
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
279-770 |
1.19e-151 |
|
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: 477.05 E-value: 1.19e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd17645 2 QLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDPD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 359 LPKQRVEYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd17645 82 YPGERIAYMLADSSAKILLT-----------------------------------NPDDLAYVIYTSGSTGLPKGVMIEH 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 439 RSLTNFlCAMYEDFSQdIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYIPPT 517
Cdd:cd17645 127 HNLVNL-CEWHRPYFG-VTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSErRLDLDALNDYFNQEGITISFLPTG 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 518 LLNEiydYFVRANQkiSLNKLFVGVEPIKTELLAKYdhlfrgnlQILNLYGPTEATVCCTSYqyERDKEitTQNVPIGSP 597
Cdd:cd17645 205 AAEQ---FMQLDNQ--SLRVLLTGGDKLKKIERKGY--------KLVNNYGPTENTVVATSF--EIDKP--YANIPIGKP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 598 LLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDH 677
Cdd:cd17645 268 IDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLDQ 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 678 QVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIP 757
Cdd:cd17645 348 QVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKALP 427
|
490
....*....|...
gi 446807313 758 LTQNGKIDRKKLP 770
Cdd:cd17645 428 LTANGKVDRKALP 440
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
1332-1812 |
1.25e-151 |
|
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: 477.34 E-value: 1.25e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLvhqnsiikgiefqgnvidlmdmsfeeepgedmhmmIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd17650 81 EDSGAKLLL-----------------------------------TQPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFSQDiGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIY-QGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFV 1570
Cdd:cd17650 126 RREYELD-SFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICpDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVY 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1571 RDNQKIVLNKLL-VGVEPIKTELLAKYDHLFRGNLQILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYIL 1649
Cdd:cd17650 205 RNGLDLSAMRLLiVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1650 DSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 1729
Cdd:cd17650 285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1730 ELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:cd17650 365 ELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444
|
...
gi 446807313 1810 SKL 1812
Cdd:cd17650 445 RAL 447
|
|
| A_NRPS_LgrA-like |
cd17645 |
adenylation (A) domain of linear gramicidin synthetase (LgrA) and similar proteins; This ... |
1321-1813 |
1.73e-150 |
|
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: 473.97 E-value: 1.73e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1321 HKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDT 1400
Cdd:cd17645 1 HQLFEEQVERTPDHVAVVDRGQSLTYKQLNEKANQLARHLRGKGVKPDDQVGIMLDKSLDMIAAILGVLKAGGAYVPIDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1401 DLPKQRVEYMLTDSGCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIE 1480
Cdd:cd17645 81 DYPGERIAYMLADSSAKILLT-----------------------------------NPDDLAYVIYTSGSTGLPKGVMIE 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1481 HRSLTNFlCAMYEDFSQdIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEEQVTLSYIPP 1559
Cdd:cd17645 126 HHNLVNL-CEWHRPYFG-VTPADKSLVYASFSFDASAWEIFPHLTAGAALHVVPSErRLDLDALNDYFNQEGITISFLPT 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TLLNEiydYFVRDNQKivLNKLLVGVEPIKTELLAKYdhlfrgnlQILNGYGPTEATVCCTSyrYESNKEitTQNVPIGS 1639
Cdd:cd17645 204 GAAEQ---FMQLDNQS--LRVLLTGGDKLKKIERKGY--------KLVNNYGPTENTVVATS--FEIDKP--YANIPIGK 266
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1640 PLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVD 1719
Cdd:cd17645 267 PIDNTRVYILDEALQLQPIGVAGELCIAGEGLARGYLNRPELTAEKFIVHPFVPGERMYRTGDLAKFLPDGNIEFLGRLD 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1720 HQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNI 1799
Cdd:cd17645 347 QQVKIRGYRIEPGEIEPFLMNHPLIELAAVLAKEDADGRKYLVAYVTAPEEIPHEELREWLKNDLPDYMIPTYFVHLKAL 426
|
490
....*....|....
gi 446807313 1800 PLTQNGKIDRSKLP 1813
Cdd:cd17645 427 PLTANGKVDRKALP 440
|
|
| A_NRPS_PpsD_like |
cd17650 |
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation ... |
289-769 |
3.92e-150 |
|
similar to adenylation domain of plipastatin synthase (PpsD); This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) includes bacitracin synthetase 1 (BacA) in Bacillus licheniformis, tyrocidine synthetase in Brevibacillus brevis, plipastatin synthase (PpsD, an important antifungal protein) in Bacillus subtilis and mannopeptimycin peptide synthetase (MppB) in Streptomyces hygroscopicus. Plipastatin has strong fungitoxic activity and is involved in inhibition of phospholipase A2 and biofilm formation. Bacitracin, a mixture of related cyclic peptides, is used as a polypeptide antibiotic while function of tyrocidine is thought to be regulation of sporulation. MppB is involved in biosynthetic pathway of mannopeptimycin, a novel class of mannosylated lipoglycopeptides. The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester bond to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341305 [Multi-domain] Cd Length: 447 Bit Score: 473.11 E-value: 3.92e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd17650 1 PDAIAVSDATRQLTYRELNERANQLARTLRGLGVAPGSVVGVCADRSLDAIVGLLAVLKAGGAYVPIDPDYPAERLQYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 448
Cdd:cd17650 81 EDSGAKLLLT-----------------------------------QPEDLAYVIYTSGTTGKPKGVMVEHRNVAHAAHAW 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 449 YEDFSQDiGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIY-QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFV 527
Cdd:cd17650 126 RREYELD-SFPVRLLQMASFSFDVFAGDFARSLLNGGTLVICpDEVKLDPAALYDLILKSRITLMESTPALIRPVMAYVY 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 528 RANQKIS-LNKLFVGVEPIKTELLAKYDHLFRGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYIL 606
Cdd:cd17650 205 RNGLDLSaMRLLIVGSDGCKAQDFKTLAARFGQGMRIINSYGVTEATIDSTYYEEGRDPLGDSANVPIGRPLPNTAMYVL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 607 DSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 686
Cdd:cd17650 285 DERLQPQPVGVAGELYIGGAGVARGYLNRPELTAERFVENPFAPGERMYRTGDLARWRADGNVELLGRVDHQVKIRGFRI 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 687 ELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:cd17650 365 ELGEIESQLARHPAIDEAVVAVREDKGGEARLCAYVVAAATLNTAELRAFLAKELPSYMIPSYYVQLDALPLTPNGKVDR 444
|
...
gi 446807313 767 KKL 769
Cdd:cd17650 445 RAL 447
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
279-769 |
5.74e-150 |
|
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: 472.57 E-value: 5.74e-150
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd12115 3 DLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLDPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 359 LPKQRVEYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd12115 83 YPPERLRFILEDAQARLVLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVAIEH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 439 RSLTNFLCAMYEDFSQDIgiTDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQgekfDVPKLVQVILEEQVTLAYIPPTL 518
Cdd:cd12115 128 RNAAAFLQWAAAAFSAEE--LAGVLASTSICFDLSVFELFGPLATGGKVVLAD----NVLALPDLPAAAEVTLINTVPSA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 519 LNEI--YDYFVRANQKISLnklfVGvEPIKTELLAKydhlFRGNLQ---ILNLYGPTEATVCCTSYQYERDKEittQNVP 593
Cdd:cd12115 202 AAELlrHDALPASVRVVNL----AG-EPLPRDLVQR----LYARLQverVVNLYGPSEDTTYSTVAPVPPGAS---GEVS 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 594 IGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLG 673
Cdd:cd12115 270 IGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGLLEFLG 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 674 RVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP--EVRAYLATKLPYYMIPQQII 751
Cdd:cd12115 350 RADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLveDLRRHLGTRLPAYMVPSRFV 429
|
490
....*....|....*...
gi 446807313 752 SIQNIPLTQNGKIDRKKL 769
Cdd:cd12115 430 RLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
289-770 |
1.27e-149 |
|
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: 470.97 E-value: 1.27e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 448
Cdd:cd17652 81 ADARPALLLT-----------------------------------TPDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 449 YEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDV-PKLVQVILEEQVTLAYIPPTLLNEiydyfV 527
Cdd:cd17652 126 IAAF--DVGPGSRVLQFASPSFDASVWELLMALLAGATLVLAPAEELLPgEPLADLLREHRITHVTLPPAALAA-----L 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 528 RANQKISLNKLFVGVEPIKTELLAKYDhlfRGNlQILNLYGPTEATVCCTSYQYERDkeitTQNVPIGSPLLNTKIYILD 607
Cdd:cd17652 199 PPDDLPDLRTLVVAGEACPAELVDRWA---PGR-RMINAYGPTETTVCATMAGPLPG----GGVPPIGRPVPGTRVYVLD 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 608 SFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 686
Cdd:cd17652 271 ARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKIRGFRI 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 687 ELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTE-KDIPIP-EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKI 764
Cdd:cd17652 351 ELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPApGAAPTAaELRAHLAERLPGYMVPAAFVVLDALPLTPNGKL 430
|
....*.
gi 446807313 765 DRKKLP 770
Cdd:cd17652 431 DRRALP 436
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
302-706 |
1.76e-148 |
|
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: 466.74 E-value: 1.76e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 302 TYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyQ 380
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLT-D 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 381 NSIIKGVAFQGSVINLMDIPFEEE-----QVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM--YEDFS 453
Cdd:TIGR01733 80 SALASRLAGLVLPVILLDPLELAAlddapAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLarRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 454 QDigitDNVLFSSSISFDVTIFEIFVPLVCGARMTIY--QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDyfVRANQ 531
Cdd:TIGR01733 160 PD----DRVLQFASLSFDASVEEIFGALLAGATLVVPpeDEERDDAALLAALIAEHPVTVLNLTPSLLALLAA--ALPPA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 532 KISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYILDSFHR 611
Cdd:TIGR01733 234 LASLRLVILGGEALTPALVDRWRARG-PGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 612 LQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF--ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 689
Cdd:TIGR01733 313 PVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELG 392
|
410
....*....|....*..
gi 446807313 690 EIEASLLKYETIKTAVV 706
Cdd:TIGR01733 393 EIEAALLRHPGVREAVV 409
|
|
| A_NRPS_Sfm_like |
cd12115 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including Saframycin A gene ... |
1320-1812 |
1.06e-147 |
|
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: 466.41 E-value: 1.06e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:cd12115 1 LHDLVEAQAARTPDAIALVCGDESLTYAELNRRANRLAARLRAAGVGPESRVGVCLERTPDLVVALLAVLKAGAAYVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSGCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMI 1479
Cdd:cd12115 81 PAYPPERLRFILEDAQARLVLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVAI 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1480 EHRSLTNFLCAMYEDFSQDIgiTDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQgekfDVTKLVQVILEEQVTLSYIPP 1559
Cdd:cd12115 126 EHRNAAAFLQWAAAAFSAEE--LAGVLASTSICFDLSVFELFGPLATGGKVVLAD----NVLALPDLPAAAEVTLINTVP 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TLLNEI--YDYFVRDNQkiVLNklLVGvEPIKTELLAKydhlFRGNLQ---ILNGYGPTEATVcctsyrYESNKEITT-- 1632
Cdd:cd12115 200 SAAAELlrHDALPASVR--VVN--LAG-EPLPRDLVQR----LYARLQverVVNLYGPSEDTT------YSTVAPVPPga 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1633 -QNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGN 1711
Cdd:cd12115 265 sGEVSIGRPLANTQAYVLDRALQPVPLGVPGELYIGGAGVARGYLGRPGLTAERFLPDPFGPGARLYRTGDLVRWRPDGL 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1712 IEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--EVRAYLATKLPHYMI 1789
Cdd:cd12115 345 LEFLGRADNQVKVRGFRIELGEIEAALRSIPGVREAVVVAIGDAAGERRLVAYIVAEPGAAGLveDLRRHLGTRLPAYMV 424
|
490 500
....*....|....*....|...
gi 446807313 1790 PQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd12115 425 PSRFVRLDALPLTPNGKIDRSAL 447
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
281-770 |
1.12e-147 |
|
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: 467.98 E-value: 1.12e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 281 FEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 361 KQRVEYMLTDSGCSHVLTYQnsiikGVAFQGSVINLMDIPFEEEQVE-----DLQITMEPQNLAYVIYTSGSTGQPKGVM 435
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHP-----ALAGELAVELVAVTLLDQPGAAagadaEPDPALDADDLAYVIYTSGSTGRPKGVV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 436 IEHRSLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYI 514
Cdd:cd17651 156 MPHRSLANLVAWQARASSLGPG--ARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEvRTDPPALAAWLDEQRISRVFL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 515 PPTLLNEIYDYFVRAN-QKISLNKLFVGVEP-IKTELLAkydHLFRG--NLQILNLYGPTEATVCcTSYQYERDKEITTQ 590
Cdd:cd17651 234 PTVALRALAEHGRPLGvRLAALRYLLTGGEQlVLTEDLR---EFCAGlpGLRLHNHYGPTETHVV-TALSLPGDPAAWPA 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 591 NVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIE 670
Cdd:cd17651 310 PPPIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELE 389
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 671 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP--EVRAYLATKLPYYMIPQ 748
Cdd:cd17651 390 FLGRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDaaELRAALATHLPEYMVPS 469
|
490 500
....*....|....*....|..
gi 446807313 749 QIISIQNIPLTQNGKIDRKKLP 770
Cdd:cd17651 470 AFVLLDALPLTPNGKLDRRALP 491
|
|
| A_NRPS_CmdD_like |
cd17652 |
similar to adenylation domain of chondramide synthase cmdD; This family of the adenylation (A) ... |
1332-1813 |
5.56e-145 |
|
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: 458.26 E-value: 5.56e-145
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd17652 1 PDAPAVVFGDETLTYAELNARANRLARLLAARGVGPERLVALALPRSAELVVAILAVLKAGAAYLPLDPAYPAERIAYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHqnsiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd17652 81 ADARPALLLTT-----------------------------------PDNLAYVIYTSGSTGRPKGVVVTHRGLANLAAAQ 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARM------TIYQGEKfdvtkLVQVILEEQVTLSYIPPTLLNEI 1565
Cdd:cd17652 126 IAAF--DVGPGSRVLQFASPSFDASVWELLMALLAGATLvlapaeELLPGEP-----LADLLREHRITHVTLPPAALAAL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1566 YDYFVRDnqkivLNKLLVGVEPIKTELLAKYDhlfRGNlQILNGYGPTEATVCCTSYRYESnkeiTTQNVPIGSPLLNTK 1645
Cdd:cd17652 199 PPDDLPD-----LRTLVVAGEACPAELVDRWA---PGR-RMINAYGPTETTVCATMAGPLP----GGGVPPIGRPVPGTR 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1646 IYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKI 1724
Cdd:cd17652 266 VYVLDARLRPVPPGVPGELYIAGAGLARGYLNRPGLTAERFVADPFgAPGSRMYRTGDLARWRADGQLEFLGRADDQVKI 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1725 RGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTE-KDIPIP-EVRAYLATKLPHYMIPQQLIPIHNIPLT 1802
Cdd:cd17652 346 RGFRIELGEVEAALTEHPGVAEAVVVVRDDRPGDKRLVAYVVPApGAAPTAaELRAHLAERLPGYMVPAAFVVLDALPLT 425
|
490
....*....|.
gi 446807313 1803 QNGKIDRSKLP 1813
Cdd:cd17652 426 PNGKLDRRALP 436
|
|
| entF |
PRK10252 |
enterobactin non-ribosomal peptide synthetase EntF; |
56-855 |
1.91e-142 |
|
enterobactin non-ribosomal peptide synthetase EntF;
Pssm-ID: 236668 [Multi-domain] Cd Length: 1296 Bit Score: 479.93 E-value: 1.91e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 56 QFPSDIAKRAVAisNNSDMLLYTILLSGVKYLLSRYTDKDDVVIGMPVFKQ----GQEETVFQNNFLLLRTQINQEDNFK 131
Cdd:PRK10252 233 EFTDGAFRQLAA--QASGVQRPDLALALVALWLGRLCGRMDYAAGFIFMRRlgsaALTATGPVLNVLPLRVHIAAQETLP 310
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 132 EIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNL--PLLNtIVMLD---DIHCYESTDKINS-----DMVIRFMKNE 201
Cdd:PRK10252 311 ELATRLAAQLKKMRRHQRYDAEQIVRDSGRAAGDEPLfgPVLN-IKVFDyqlDFPGVQAQTHTLAtgpvnDLELALFPDE 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 202 E-QLKVQVDYNSTLYSEGLVSRIVNHLYNILDILMKDPNKSAMDLDVMPKTEKNQiLFDFNHTTRVhktlLCETvTAPQL 280
Cdd:PRK10252 390 HgGLSIEILANPQRYDEATLIAHAERLKALIAQFAADPALLCGDVDILLPGEYAQ-LAQVNATAVE----IPET-TLSAL 463
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 281 FEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:PRK10252 464 VAQQAAKTPDAPALADARYQFSYREMREQVVALANLLRERGVKPGDSVAVALPRSVFLTLALHAIVEAGAAWLPLDTGYP 543
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 361 KQRVEYMLTDSGCSHVLTYQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITmEPQNLAYVIYTSGSTGQPKGVMIEHRS 440
Cdd:PRK10252 544 DDRLKMMLEDARPSLLITTADQLPRFADVPDLTSLCYNAPLAPQGAAPLQLS-QPHHTAYIIFTSGSTGRPKGVMVGQTA 622
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 441 LTNFLCAMYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVP-KLVQVILEEQVTLAYIPPTLL 519
Cdd:PRK10252 623 IVNRLLWMQNHYP--LTADDVVLQKTPCSFDVSVWEFFWPFIAGAKLVMAEPEAHRDPlAMQQFFAEYGVTTTHFVPSML 700
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 520 neiyDYFVRA-------NQKISLNKLFVGVEPIKTELLAKYDHLFRGNLQilNLYGPTEATVCCTSYQYERD--KEITTQ 590
Cdd:PRK10252 701 ----AAFVASltpegarQSCASLRQVFCSGEALPADLCREWQQLTGAPLH--NLYGPTEAAVDVSWYPAFGEelAAVRGS 774
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 591 NVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIE 670
Cdd:PRK10252 775 SVPIGYPVWNTGLRILDARMRPVPPGVAGDLYLTGIQLAQGYLGRPDLTASRFIADPFAPGERMYRTGDVARWLDDGAVE 854
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 671 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV-----IQREDESG-EKYLCAYVVTEKDIPI--PEVRAYLATKLP 742
Cdd:PRK10252 855 YLGRSDDQLKIRGQRIELGEIDRAMQALPDVEQAVThacviNQAAATGGdARQLVGYLVSQSGLPLdtSALQAQLRERLP 934
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 743 YYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAAR 822
Cdd:PRK10252 935 PHMVPVVLLQLDQLPLSANGKLDRKALPLPELKAQVPGRAPKTGTETIIAAAFSSLLGCDVVDADADFFALGGHSLLAMK 1014
|
810 820 830
....*....|....*....|....*....|...
gi 446807313 823 LISIVNKEFNVQLSIKSLFKFPVLVDFSKYILE 855
Cdd:PRK10252 1015 LAAQLSRQFARQVTPGQVMVASTVAKLATLLDA 1047
|
|
| A_NRPS_VisG_like |
cd17651 |
similar to adenylation domain of virginiamycin S synthetase; This family of the adenylation (A) ... |
1324-1813 |
3.51e-142 |
|
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: 452.57 E-value: 3.51e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLP 1403
Cdd:cd17651 1 FERQAARTPDAPALVAEGRRLTYAELDRRANRLAHRLRARGVGPGDLVALCARRSAELVVALLAILKAGAAYVPLDPAYP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1404 KQRVEYMLTDSGCSHVLVHQNSiikGIEFQGNVIDLM--DMSFEEEPGEDMHMM-IEPHNLAYVIYTSGSTGQPKGVMIE 1480
Cdd:cd17651 81 AERLAFMLADAGPVLVLTHPAL---AGELAVELVAVTllDQPGAAAGADAEPDPaLDADDLAYVIYTSGSTGRPKGVVMP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1481 HRSLTNFLCAMYEDFSQDIGitDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEEQVTLSYIPP 1559
Cdd:cd17651 158 HRSLANLVAWQARASSLGPG--ARTLQFAGLGFDVSVQEIFSTLCAGATLVLPPEEvRTDPPALAAWLDEQRISRVFLPT 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TLLNEIYDYFVRDN-QKIVLNKLLVGVEP-IKTELLAkydHLFRG--NLQILNGYGPTEATVCcTSYRYESNKEITTQNV 1635
Cdd:cd17651 236 VALRALAEHGRPLGvRLAALRYLLTGGEQlVLTEDLR---EFCAGlpGLRLHNHYGPTETHVV-TALSLPGDPAAWPAPP 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 PIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 1715
Cdd:cd17651 312 PIGRPIDNTRVYVLDAALRPVPPGVPGELYIGGAGLARGYLNRPELTAERFVPDPFVPGARMYRTGDLARWLPDGELEFL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1716 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--EVRAYLATKLPHYMIPQQL 1793
Cdd:cd17651 392 GRADDQVKIRGFRIELGEIEAALARHPGVREAVVLAREDRPGEKRLVAYVVGDPEAPVDaaELRAALATHLPEYMVPSAF 471
|
490 500
....*....|....*....|
gi 446807313 1794 IPIHNIPLTQNGKIDRSKLP 1813
Cdd:cd17651 472 VLLDALPLTPNGKLDRRALP 491
|
|
| AA-adenyl-dom |
TIGR01733 |
amino acid adenylation domain; This model represents a domain responsible for the specific ... |
1345-1749 |
1.63e-141 |
|
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: 447.10 E-value: 1.63e-141
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:TIGR01733 1 TYRELDERANRLARHLRAAgGVGPGDRVAVLLERSAELVVAILAVLKAGAAYVPLDPAYPAERLAFILEDAGARLLLTDS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nSIIKGIEFQGNVIDLMDMSFEEE-----PGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM--YEDFS 1496
Cdd:TIGR01733 81 -ALASRLAGLVLPVILLDPLELAAlddapAPPPPDAPSGPDDLAYVIYTSGSTGRPKGVVVTHRSLVNLLAWLarRYGLD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1497 QDigitDNVLFSSSISFDVTIFEIFVPLIYGARMTIY--QGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDyfVRDNQ 1574
Cdd:TIGR01733 160 PD----DRVLQFASLSFDASVEEIFGALLAGATLVVPpeDEERDDAALLAALIAEHPVTVLNLTPSLLALLAA--ALPPA 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1575 KIVLNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYILDSFHR 1654
Cdd:TIGR01733 234 LASLRLVILGGEALTPALVDRWRARG-PGARLINLYGPTETTVWSTATLVDPDDAPRESPVPIGRPLANTRLYVLDDDLR 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1655 IQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF--ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 1732
Cdd:TIGR01733 313 PVPVGVVGELYIGGPGVARGYLNRPELTAERFVPDPFagGDGARLYRTGDLVRYLPDGNLEFLGRIDDQVKIRGYRIELG 392
|
410
....*....|....*..
gi 446807313 1733 EIEASLLKYETIKTAVV 1749
Cdd:TIGR01733 393 EIEAALLRHPGVREAVV 409
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
289-770 |
3.87e-140 |
|
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: 445.27 E-value: 3.87e-140
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGCSHVLTYqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 448
Cdd:cd17649 81 EDSGAGLLLTH----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 449 YEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPK-LVQVILEEQVTLAYIPPTLLNEIYDYFV 527
Cdd:cd17649 127 AERY--GLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWASADeLAEMVRELGVTVLDLPPAYLQQLAEEAD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 528 RANQK--ISLNKLFVGVEPIKTELLAKYdhlFRGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYI 605
Cdd:cd17649 205 RTGDGrpPSLRLYIFGGEALSPELLRRW---LKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 606 LDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGY 684
Cdd:cd17649 282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 685 RIELGEIEASLLKYETIKTAVVIQReDESGEKYLCAYVVTEKDIPIPEVRAYLAT----KLPYYMIPQQIISIQNIPLTQ 760
Cdd:cd17649 362 RIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPELRAQLRTalraSLPDYMVPAHLVFLARLPLTP 440
|
490
....*....|
gi 446807313 761 NGKIDRKKLP 770
Cdd:cd17649 441 NGKLDRKALP 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
289-769 |
1.90e-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: 1.90e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGCSHVLTyQNSIIKGVAFQGSVInLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 448
Cdd:cd12116 81 EDAEPALVLT-DDALPDRLPAGLPVL-LLALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 449 YEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFV 527
Cdd:cd12116 159 RERLG--LGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPREtQRDPEALARLIEAHSITVMQATPATWRMLLDAGW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 528 RANQKIslnKLFVGVEPIKTELLAkydHLFRGNLQILNLYGPTEATV--CCTSYQYERDKeittqnVPIGSPLLNTKIYI 605
Cdd:cd12116 237 QGRAGL---TALCGGEALPPDLAA---RLLSRVGSLWNLYGPTETTIwsTAARVTAAAGP------IPIGRPLANTQVYV 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 606 LDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGY 684
Cdd:cd12116 305 LDAALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGH 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 685 RIELGEIEASLLKYETIKTAVVIQREDEsGEKYLCAYVVTEKDIPIP--EVRAYLATKLPYYMIPQQIISIQNIPLTQNG 762
Cdd:cd12116 385 RIELGEIEAALAAHPGVAQAAVVVREDG-GDRRLVAYVVLKAGAAPDaaALRAHLRATLPAYMVPSAFVRLDALPLTANG 463
|
....*..
gi 446807313 763 KIDRKKL 769
Cdd:cd12116 464 KLDRKAL 470
|
|
| A_NRPS_PvdJ-like |
cd17649 |
non-ribosomal peptide synthetase; This family of the adenylation (A) domain of nonribosomal ... |
1332-1813 |
2.47e-137 |
|
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: 437.18 E-value: 2.47e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd17649 1 PDAVALVFGDQSLSYAELDARANRLAHRLRALGVGPEVRVGIALERSLEMVVALLAILKAGGAYVPLDPEYPAERLRYML 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHqnsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd17649 81 EDSGAGLLLTH----------------------------------HPRQLAYVIYTSGSTGTPKGVAVSHGPLAAHCQAT 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKF-DVTKLVQVILEEQVTLSYIPPTLLNEIYDYFV 1570
Cdd:cd17649 127 AERY--GLTPGDRELQFASFNFDGAHEQLLPPLICGACVVLRPDELWaSADELAEMVRELGVTVLDLPPAYLQQLAEEAD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1571 RDNQK--IVLNKLLVGVEPIKTELLAKYdhlFRGNLQILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYI 1648
Cdd:cd17649 205 RTGDGrpPSLRLYIFGGEALSPELLRRW---LKAPVRLFNAYGPTEATVTPLVWKCEAGAARAGASMPIGRPLGGRSAYI 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1649 LDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGY 1727
Cdd:cd17649 282 LDADLNPVPVGVTGELYIGGEGLARGYLGRPELTAERFVPDPFgAPGSRLYRTGDLARWRDDGVIEYLGRVDHQVKIRGF 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1728 RIELGEIEASLLKYETIKTAVVIDQeDEAGEKYLCAYVVTEKDIPIPEVRAYLAT----KLPHYMIPQQLIPIHNIPLTQ 1803
Cdd:cd17649 362 RIELGEIEAALLEHPGVREAAVVAL-DGAGGKQLVAYVVLRAAAAQPELRAQLRTalraSLPDYMVPAHLVFLARLPLTP 440
|
490
....*....|
gi 446807313 1804 NGKIDRSKLP 1813
Cdd:cd17649 441 NGKLDRKALP 450
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
289-769 |
3.74e-137 |
|
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: 436.74 E-value: 3.74e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCA- 447
Cdd:cd17643 81 ADSGPSLLLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAt 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 448 --MYEDFSQDIGitdnVLFSSSiSFDVTIFEIFVPLVCGARMTIyqgekfdVPKLV--------QVILEEQVTLAYIPPT 517
Cdd:cd17643 126 qrWFGFNEDDVW----TLFHSY-AFDFSVWEIWGALLHGGRLVV-------VPYEVarspedfaRLLRDEGVTVLNQTPS 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 518 LLNEIYDYFVRAN-QKISLNKLFVGVEPIKTELLAK-YDHLFRGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIG 595
Cdd:cd17643 194 AFYQLVEAADRDGrDPLALRYVIFGGEALEAAMLRPwAGRFGLDRPQLVNMYGITETTVHVTFRPLDAADLPAAAASPIG 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 596 SPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKTGDIARWLPDGNIEYLGR 674
Cdd:cd17643 274 RPLPGLRVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGR 353
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 675 VDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV--TEKDIPIPEVRAYLATKLPYYMIPQQIIS 752
Cdd:cd17643 354 ADEQVKIRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVadDGAAADIAELRALLKELLPDYMVPARYVP 433
|
490
....*....|....*..
gi 446807313 753 IQNIPLTQNGKIDRKKL 769
Cdd:cd17643 434 LDALPLTVNGKLDRAAL 450
|
|
| A_NRPS_Cytc1-like |
cd17643 |
similar to adenylation domain of cytotrienin synthetase CytC1; This family of the adenylation ... |
1332-1812 |
2.42e-136 |
|
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: 434.43 E-value: 2.42e-136
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd17643 1 PEAVAVVDEDRRLTYGELDARANRLARTLRAEGVGPGDRVALALPRSAELIVALLAILKAGGAYVPIDPAYPVERIAFIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCA- 1490
Cdd:cd17643 81 ADSGPSLLLT-----------------------------------DPDDLAYVIYTSGSTGRPKGVVVSHANVLALFAAt 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1491 --MYEDFSQDIGitdnVLFSSSiSFDVTIFEIFVPLIYGARMTIY-QGEKFDVTKLVQVILEEQVT-LSYIPPTLLNEIY 1566
Cdd:cd17643 126 qrWFGFNEDDVW----TLFHSY-AFDFSVWEIWGALLHGGRLVVVpYEVARSPEDFARLLRDEGVTvLNQTPSAFYQLVE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1567 DYFVRDNQKIVLNKLLVGVEPIKTELLAK-YDHLFRGNLQILNGYGPTEATVCcTSYRYESNKEITTQNV-PIGSPLLNT 1644
Cdd:cd17643 201 AADRDGRDPLALRYVIFGGEALEAAMLRPwAGRFGLDRPQLVNMYGITETTVH-VTFRPLDAADLPAAAAsPIGRPLPGL 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1645 KIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFER-GEKLYKTGDIARWLPDGNIEYLGRVDHQVK 1723
Cdd:cd17643 280 RVYVLDADGRPVPPGVVGELYVSGAGVARGYLGRPELTAERFVANPFGGpGSRMYRTGDLARRLPDGELEYLGRADEQVK 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1724 IRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV--TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPL 1801
Cdd:cd17643 360 IRGFRIELGEIEAALATHPSVRDAAVIVREDEPGDTRLVAYVVadDGAAADIAELRALLKELLPDYMVPARYVPLDALPL 439
|
490
....*....|.
gi 446807313 1802 TQNGKIDRSKL 1812
Cdd:cd17643 440 TVNGKLDRAAL 450
|
|
| A_NRPS_Ta1_like |
cd12116 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including salinosporamide A ... |
1332-1812 |
1.92e-135 |
|
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: 432.49 E-value: 1.92e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd12116 1 PDATAVRDDDRSLSYAELDERANRLAARLRARGVGPGDRVAVYLPRSARLVAAMLAVLKAGAAYVPLDPDYPADRLRYIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCShVLVHQNSIIKGIEFQGNVIDLmDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd12116 81 EDAEPA-LVLTDDALPDRLPAGLPVLLL-ALAAAAAAPAAPRTPVSPDDLAYVIYTSGSTGRPKGVVVSHRNLVNFLHSM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFV 1570
Cdd:cd12116 159 RERLG--LGPGDRLLAVTTYAFDISLLELLLPLLAGARVVIAPREtQRDPEALARLIEAHSITVMQATPATWRMLLDAGW 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1571 RDNQKIvlnKLLVGVEPIKTELLAkydHLFRGNLQILNGYGPTEATVCCTSYRYESNKEittqNVPIGSPLLNTKIYILD 1650
Cdd:cd12116 237 QGRAGL---TALCGGEALPPDLAA---RLLSRVGSLWNLYGPTETTIWSTAARVTAAAG----PIPIGRPLANTQVYVLD 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1651 SFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 1729
Cdd:cd12116 307 AALRPVPPGVPGELYIGGDGVAQGYLGRPALTAERFVPDPFaGPGSRLYRTGDLVRRRADGRLEYLGRADGQVKIRGHRI 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1730 ELGEIEASLLKYETIKTAVVIDQEDEaGEKYLCAYVVTEKDIPIP--EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:cd12116 387 ELGEIEAALAAHPGVAQAAVVVREDG-GDRRLVAYVVLKAGAAPDaaALRAHLRATLPAYMVPSAFVRLDALPLTANGKL 465
|
....*
gi 446807313 1808 DRSKL 1812
Cdd:cd12116 466 DRKAL 470
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
879-1896 |
8.17e-132 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 464.26 E-value: 8.17e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 879 QKRMFIVDQFEDGTNTTYnMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGE-LVQKIEPNVDFNIEYVHVNE 957
Cdd:PRK05691 3264 QEGLLLHTLLEPGTGLYY-MQDRYRINSALDPERFAQAWQAVVARHEALRASFSWNAGEtMLQVIHKPGRTPIDYLDWRG 3342
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 958 KDAD--------YLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY----KGNElPK 1025
Cdd:PRK05691 3343 LPEDgqeqrlqaLHKQEREAGFDLLNQPPFHLRLIRVDEARYWFMMSNHHILIDAWCRSLLMNDFFEIYtalgEGRE-AQ 3421
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1026 LRV--QYKDYVMWQNgpyyKNLISEQKNYWLTTLKG-ELPVLnFPTDfqRPTIQSFKGNVCSFNLGTDLT-------FKV 1095
Cdd:PRK05691 3422 LPVppRYRDYIGWLQ----RQDLAQARQWWQDNLRGfERPTP-IPSD--RPFLREHAGDSGGMVVGDCYTrldaadgARL 3494
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1096 NKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGR--SHSDTNHMIGMFINTLVMRNYLENDDE---FIEFLSR 1170
Cdd:PRK05691 3495 RELAQAHQLTVNTFAQAAWALVLRRYSGDRDVLFGVTVAGRpvSMPQMQRTVGLFINSIALRVQLPAAGQrcsVRQWLQG 3574
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1171 LKLNTLEAYENQDYPFEELLEGLDLHRDtsrNPLFDTMFVFQNMdmnPISIGELEFTPYPFKQSVS-----KFDLSLVAT 1245
Cdd:PRK05691 3575 LLDSNMELREYEYLPLVAIQECSELPKG---QPLFDSLFVFENA---PVEVSVLDRAQSLNASSDSgrthtNFPLTAVCY 3648
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1246 EIDNnIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEEEHCIMNEFNKKENsnsNYLLVH---K 1322
Cdd:PRK05691 3649 PGDD-LGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSER---DYPLEQsyvR 3724
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL 1402
Cdd:PRK05691 3725 LFEAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGL 3804
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQRVEYMLTDSG-----CSHVLVHQNSIIKGiEFQGNVIDLM----DMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQ 1473
Cdd:PRK05691 3805 PAQRLQRIIELSRtpvlvCSAACREQARALLD-ELGCANRPRLlvweEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGL 3883
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1474 PKGVMIEHRS-LTNFLCAM-YEDFSQdigiTDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEE 1550
Cdd:PRK05691 3884 PKGVMVEQRGmLNNQLSKVpYLALSE----ADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAiAHDPQGLLAHVQAQ 3959
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1551 QVTLSYIPPTLlneIYDYFVRDNQKI-VLNKLLVGVEPIKTELLAKYdhLFR-GNLQILNGYGPTEATVCCTSYRYEsnk 1628
Cdd:PRK05691 3960 GITVLESVPSL---IQGMLAEDRQALdGLRWMLPTGEAMPPELARQW--LQRyPQIGLVNAYGPAECSDDVAFFRVD--- 4031
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1629 EITTQN--VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIAR 1705
Cdd:PRK05691 4032 LASTRGsyLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLAR 4111
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1706 WLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGeKYLCAYVV-----TEKDIPIPEVRAYL 1780
Cdd:PRK05691 4112 RRSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNG-KHLVGYLVphqtvLAQGALLERIKQRL 4190
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1781 ATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLNT--LGNSNYVPPRNEIDSSLIDIWSSILGVNNIGINDNFFELGG 1858
Cdd:PRK05691 4191 RAELPDYMVPLHWLWLDRLPLNANGKLDRKALPALDIgqLQSQAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGG 4270
|
1050 1060 1070
....*....|....*....|....*....|....*...
gi 446807313 1859 HSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSDVI 1896
Cdd:PRK05691 4271 HSLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYI 4308
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
279-769 |
5.46e-131 |
|
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as an (amino) acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms a thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family of siderophore-synthesizing NRPS includes the third adenylation domain of SidN from the endophytic fungus Neotyphodium lolii, ferrichrome siderophore synthetase, HC-toxin synthetase, and enniatin synthase. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341242 [Multi-domain] Cd Length: 481 Bit Score: 420.41 E-value: 5.46e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd05918 3 DLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLDPS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 359 LPKQRVEYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitMEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd05918 83 HPLQRLQEILQDTGAKVVLT----------------------------------SSPSDAAYVIFTSGSTGKPKGVVIEH 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 439 RSLtnflCAMYEDFSQDIGITDN--VLFSSSISFDVTIFEIFVPLVCGA---------RMTiyqgekfdvpKLVQVILEE 507
Cdd:cd05918 129 RAL----STSALAHGRALGLTSEsrVLQFASYTFDVSILEIFTTLAAGGclcipseedRLN----------DLAGFINRL 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 508 QVTLAYIPPTLLNeiydyFVRANQKISLNKLFVGVEPIKTELLAKYDHlfrgNLQILNLYGPTEATVCCTSYQyeRDKEI 587
Cdd:cd05918 195 RVTWAFLTPSVAR-----LLDPEDVPSLRTLVLGGEALTQSDVDTWAD----RVRLINAYGPAECTIAATVSP--VVPST 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 588 TTQNvpIGSPLlNTKIYILD--SFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHP-------FERGEKLYKTG 658
Cdd:cd05918 264 DPRN--IGRPL-GATCWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTG 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 659 DIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLK-YETIKTAVV--IQREDESGEKYLCAYVVTEKDIP------ 729
Cdd:cd05918 341 DLVRYNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVevVKPKDGSSSPQLVAFVVLDGSSSgsgdgd 420
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446807313 730 -------------IPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05918 421 slflepsdefralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| A_NRPS_SidN3_like |
cd05918 |
The adenylation (A) domain of siderophore-synthesizing nonribosomal peptide synthetases (NRPS); ... |
1320-1812 |
9.07e-130 |
|
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: 416.94 E-value: 9.07e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:cd05918 1 VHDLIEERARSQPDAPAVCAWDGSLTYAELDRLSSRLAHHLRSLGVGPGVFVPLCFEKSKWAVVAMLAVLKAGGAFVPLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSGCSHVLVHQnsiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMI 1479
Cdd:cd05918 81 PSHPLQRLQEILQDTGAKVVLTSS----------------------------------PSDAAYVIFTSGSTGKPKGVVI 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1480 EHRSLtnflCAMYEDFSQDIGITDN--VLFSSSISFDVTIFEIFVPLIYGArmTIYQGEKFD-VTKLVQVILEEQVTLSY 1556
Cdd:cd05918 127 EHRAL----STSALAHGRALGLTSEsrVLQFASYTFDVSILEIFTTLAAGG--CLCIPSEEDrLNDLAGFINRLRVTWAF 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1557 IPPTLLNEIydyfvrDNQKIV-LNKLLVGVEPIKTELLAKYDHlfrgNLQILNGYGPTEATVCCTSyryesNKEITTQNV 1635
Cdd:cd05918 201 LTPSVARLL------DPEDVPsLRTLVLGGEALTQSDVDTWAD----RVRLINAYGPAECTIAATV-----SPVVPSTDP 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 P-IGSPLlNTKIYILD--SFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHP-------FERGEKLYKTGDIAR 1705
Cdd:cd05918 266 RnIGRPL-GATCWVVDpdNHDRLVPIGAVGELLIEGPILARGYLNDPEKTAAAFIEDPawlkqegSGRGRRLYRTGDLVR 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1706 WLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLK-YETIKTAVV--IDQEDEAGEKYLCAYVVTEKDIP---------- 1772
Cdd:cd05918 345 YNPDGSLEYVGRKDTQVKIRGQRVELGEIEHHLRQsLPGAKEVVVevVKPKDGSSSPQLVAFVVLDGSSSgsgdgdslfl 424
|
490 500 510 520
....*....|....*....|....*....|....*....|....*....
gi 446807313 1773 ---------IPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05918 425 epsdefralVAELRSKLRQRLPSYMVPSVFLPLSHLPLTASGKIDRRAL 473
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
7-1019 |
5.44e-127 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 448.85 E-value: 5.44e-127
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDcLSLNNIQASK-ESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVK 85
Cdd:PRK05691 1906 QRQWLESGERQRQLDYWKAQLGNEHPLLELPAD-RPRPPVQSHRgELYRFDLSPELAARVRAFNAQRGLTLFMTMTATLA 1984
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 86 YLLSRYTDKDDVVIGMPVFKQGQEET-----VFQNNfLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLS 160
Cdd:PRK05691 1985 ALLYRYSGQRDLRIGAPVANRIRPESegligAFLNT-QVLRCQLDGQMSVSELLEQVRQTVIEGQSHQDLPFDHLVEALQ 2063
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 161 LDGESNNLPLLNtiVMlddihC------YESTDKInSDMVIRFMKNEEQ-----LKVQVD-----------YNSTLYSEG 218
Cdd:PRK05691 2064 PPRSAAYNPLFQ--VM-----CnvqrweFQQSRQL-AGMTVEYLVNDARatkfdLNLEVTdldgrlgccltYSRDLFDEP 2135
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 219 LVSRIVNHLYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTT---RVHKTLlcetvtaPQLFEEQVKQNPNQIAIV 295
Cdd:PRK05691 2136 RIARMAEHWQNLLEALLGDPQQRLAELPLLAAAEQQQLLDSLAGEAgeaRLDQTL-------HGLFAAQAARTPQAPALT 2208
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 296 CNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSH 375
Cdd:PRK05691 2209 FAGQTLSYAELDARANRLARALRERGVGPQVRVGLALERSLEMVVGLLAILKAGGAYVPLDPEYPLERLHYMIEDSGIGL 2288
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 376 VLTYQ------NSIIKGVA---FQGSVINLMDIPFEEeqvedLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLC 446
Cdd:PRK05691 2289 LLSDRalfealGELPAGVArwcLEDDAAALAAYSDAP-----LPFLSLPQHQAYLIYTSGSTGKPKGVVVSHGEIAMHCQ 2363
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 447 AMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYF 526
Cdd:PRK05691 2364 AVIERF--GMRADDCELHFYSINFDAASERLLVPLLCGARVVLRAQGQWGAEEICQLIREQQVSILGFTPSYGSQLAQWL 2441
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 527 VRANQKISLNKLFVGVEPIKTELLAKYDHLFRGNlQILNLYGPTEATV----CCTSYQYERDkeitTQNVPIGSPLLNTK 602
Cdd:PRK05691 2442 AGQGEQLPVRMCITGGEALTGEHLQRIRQAFAPQ-LFFNAYGPTETVVmplaCLAPEQLEEG----AASVPIGRVVGARV 2516
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 603 IYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFE-RGEKLYKTGDIARWLPDGNIEYLGRVDHQVKI 681
Cdd:PRK05691 2517 AYILDADLALVPQGATGELYVGGAGLAQGYHDRPGLTAERFVADPFAaDGGRLYRTGDLVRLRADGLVEYVGRIDHQVKI 2596
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 682 RGYRIELGEIEASLLKYETIKTAVVIQREDESGeKYLCAYVVTEKDIPIPE--------VRAYLATKLPYYMIPQQIISI 753
Cdd:PRK05691 2597 RGFRIELGEIESRLLEHPAVREAVVLALDTPSG-KQLAGYLVSAVAGQDDEaqaalreaLKAHLKQQLPDYMVPAHLILL 2675
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 754 QNIPLTQNGKIDRKKLPQP-INNLKSSHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVnKEFN 832
Cdd:PRK05691 2676 DSLPLTANGKLDRRALPAPdPELNRQAYQAPRSELEQQLAQIWREVLNVERVGLGDNFFELGGDSILSIQVVSRA-RQLG 2754
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 833 VQLSIKSLFKFPVLVDFSKYILEMEKSNY--------ISIEPVkqQEYYLASTSQKRMFivdqfedgtnttYNMPTILKV 904
Cdd:PRK05691 2755 IHFSPRDLFQHQTVQTLAAVATHSEAAQAeqgplqgaSGLTPI--QHWFFDSPVPQPQH------------WNQALLLEP 2820
|
970 980 990 1000 1010 1020 1030 1040
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 905 EGDICKDKFENIFQSLIERHEILRTSFQILDGE-LVQKIEPNVDFNIEYVHVNE-KDADYLIHEFISPFDLSKPPLLRVL 982
Cdd:PRK05691 2821 RQALDPALLEQALQALVEHHDALRLRFSQADGRwQAEYRAVTAQELLWQVTVADfAECAALFADAQRSLDLQQGPLLRAL 2900
|
1050 1060 1070
....*....|....*....|....*....|....*..
gi 446807313 983 LLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYK 1019
Cdd:PRK05691 2901 LVDGPQGQQRLLLAIHHLVVDGVSWRVLLEDLQALYR 2937
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
289-769 |
2.15e-126 |
|
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: 407.04 E-value: 2.15e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGCSHVLTYqnsiiKGVAFQGSVINLMDIPFEEEQVEDLQ---ITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFL 445
Cdd:cd12114 81 ADAGARLVLTD-----GPDAQLDVAVFDVLILDLDALAAPAPpppVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 446 CAMYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTI-YQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYD 524
Cdd:cd12114 156 LDINRRFA--VGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLpDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLD 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 525 YFVRANQKI-SLNKLFVGVEPIKTELLAKYdHLFRGNLQILNLYGPTEATVCCTSYqyerdkEITTQN-----VPIGSPL 598
Cdd:cd12114 234 VLEAAQALLpSLRLVLLSGDWIPLDLPARL-RALAPDARLISLGGATEASIWSIYH------PIDEVPpdwrsIPYGRPL 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 599 LNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQ 678
Cdd:cd12114 307 ANQRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQ 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 679 VKIRGYRIELGEIEASLLKYETIKTAVVIQReDESGEKYLCAYVVTEKDIPIP---EVRAYLATKLPYYMIPQQIISIQN 755
Cdd:cd12114 385 VKVRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPIapdALRAFLAQTLPAYMIPSRVIALEA 463
|
490
....*....|....
gi 446807313 756 IPLTQNGKIDRKKL 769
Cdd:cd12114 464 LPLTANGKVDRAAL 477
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
279-769 |
4.55e-126 |
|
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: 404.38 E-value: 4.55e-126
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 279 QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:cd17653 1 DAFERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 359 LPKQRVEYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqiTMEPQNLAYVIYTSGSTGQPKGVMIEH 438
Cdd:cd17653 81 LPSARIQAILRTSGATLLLT---------------------------------TDSPDDLAYIIFTSGSTGIPKGVMVPH 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 439 RSLTNFLcaMYEDFSQDIGITDNVLFSSSISFDVTIFEIFVPLVCGArmTIYQGEKFDvpKLVQVIleEQVTLAYIPPTL 518
Cdd:cd17653 128 RGVLNYV--SQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGG--TLVLADPSD--PFAHVA--RTVDALMSTPSI 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 519 LNEIydyfvRANQKISLNKLFVGVEPIKTELLAKYdhlfRGNLQILNLYGPTEATVCCTSYQYERDkeittQNVPIGSPL 598
Cdd:cd17653 200 LSTL-----SPQDFPNLKTIFLGGEAVPPSLLDRW----SPGRRLYNAYGPTECTISSTMTELLPG-----QPVTIGKPI 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 599 LNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQ 678
Cdd:cd17653 266 PNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGREDNQ 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 679 VKIRGYRIELGEIEASLLKYE-TIKTAVVIQREDEsgekyLCAYVVTEkDIPIPEVRAYLATKLPYYMIPQQIISIQNIP 757
Cdd:cd17653 346 VKVRGFRINLEEIEEVVLQSQpEVTQAAAIVVNGR-----LVAFVTPE-TVDVDGLRSELAKHLPSYAVPDRIIALDSFP 419
|
490
....*....|..
gi 446807313 758 LTQNGKIDRKKL 769
Cdd:cd17653 420 LTANGKVDRKAL 431
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
868-1299 |
3.46e-124 |
|
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: 399.79 E-value: 3.46e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 868 KQQEYYLaSTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQI-LDGELVQKIEPNV 946
Cdd:pfam00668 1 VQDEYPL-SPAQKRMWFLEKLEPHS-SAYNMPAVLKLTGELDPERLEKALQELINRHDALRTVFIRqENGEPVQVILEER 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 947 DFNIEY---VHVNEKDADYLIHEFI-----SPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY 1018
Cdd:pfam00668 79 PFELEIidiSDLSESEEEEAIEAFIqrdlqSPFDLEKGPLFRAGLFRIAENRHHLLLSMHHIIVDGVSLGILLRDLADLY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1019 ----KGNELPKLRVQ-YKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTF 1093
Cdd:pfam00668 159 qqllKGEPLPLPPKTpYKDYAEWLQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEE 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1094 KVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKL 1173
Cdd:pfam00668 239 LLRKLAKAHGTTLNDVLLAAYGLLLSRYTGQDDIVVGTPGSGRPSPDIERMVGMFVNTLPLRIDPKGGKTFSELIKRVQE 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1174 NTLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMD-----MNPISIGELEFTPYPFKQSVSKFDLSLVATEID 1248
Cdd:pfam00668 319 DLLSAEPHQGYPFGDLVNDLRLPRDLSRHPLFDPMFSFQNYLgqdsqEEEFQLSELDLSVSSVIEEEAKYDLSLTASERG 398
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1249 NNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRVRLRNINMLSIEE 1299
Cdd:pfam00668 399 GGLTIKIDYNTSLFDEETIERFAEHFKELLEQAIAHPSQPLSELDLLSDAE 449
|
|
| A_NRPS_TlmIV_like |
cd12114 |
The adenylation domain of nonribosomal peptide synthetases (NRPS), including ... |
1332-1812 |
9.96e-123 |
|
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: 396.64 E-value: 9.96e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd12114 1 PDATAVICGDGTLTYGELAERARRVAGALKAAGVRPGDLVAVTLPKGPEQVVAVLGILAAGAAYVPVDIDQPAARREAIL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHQNSIIKGIEFQGNVIDLMDmsFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM 1491
Cdd:cd12114 81 ADAGARLVLTDGPDAQLDVAVFDVLILDLD--ALAAPAPPPPVDVAPDDLAYVIFTSGSTGTPKGVMISHRAALNTILDI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 YEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTI-YQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYfV 1570
Cdd:cd12114 159 NRRFA--VGPDDRVLALSSLSFDLSVYDIFGALSAGATLVLpDEARRRDPAHWAELIERHGVTLWNSVPALLEMLLDV-L 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1571 RDNQKIV--LNKLLVGVEPIKTELLAKYdHLFRGNLQILNGYGPTEATVCCTSYryesnkEITTQN-----VPIGSPLLN 1643
Cdd:cd12114 236 EAAQALLpsLRLVLLSGDWIPLDLPARL-RALAPDARLISLGGATEASIWSIYH------PIDEVPpdwrsIPYGRPLAN 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1644 TKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVK 1723
Cdd:cd12114 309 QRYRVLDPRGRDCPDWVPGELWIGGRGVALGYLGDPELTAARFVTHP--DGERLYRTGDLGRYRPDGTLEFLGRRDGQVK 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1724 IRGYRIELGEIEASLLKYETIKTAVVIDQeDEAGEKYLCAYVVTEKDIPIP---EVRAYLATKLPHYMIPQQLIPIHNIP 1800
Cdd:cd12114 387 VRGYRIELGEIEAALQAHPGVARAVVVVL-GDPGGKRLAAFVVPDNDGTPIapdALRAFLAQTLPAYMIPSRVIALEALP 465
|
490
....*....|..
gi 446807313 1801 LTQNGKIDRSKL 1812
Cdd:cd12114 466 LTANGKVDRAAL 477
|
|
| A_NRPS_GliP_like |
cd17653 |
nonribosomal peptide synthase GliP-like; This family includes the adenylation (A) domain of ... |
1324-1812 |
4.47e-121 |
|
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: 390.13 E-value: 4.47e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLP 1403
Cdd:cd17653 3 FERIAAAHPDAVAVESLGGSLTYGELDAASNALANRLLQLGVVPGDVVPLLSDRSLEMLVAILAILKAGAAYVPLDAKLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1404 KQRVEYMLTDSGCShVLVHQNSiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMIEHRS 1483
Cdd:cd17653 83 SARIQAILRTSGAT-LLLTTDS--------------------------------PDDLAYIIFTSGSTGIPKGVMVPHRG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1484 LTNFLcaMYEDFSQDIGITDNVLFSSSISFDVTIFEIFVPLIYGArmTIYQGEK----FDVTKLVQVILEEQVTLSYIPP 1559
Cdd:cd17653 130 VLNYV--SQPPARLDVGPGSRVAQVLSIAFDACIGEIFSTLCNGG--TLVLADPsdpfAHVARTVDALMSTPSILSTLSP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TllneiyDYfvrDNQKIVLnkllVGVEPIKTELLAKYdhlfRGNLQILNGYGPTEATVCCTSYRYESNkeittQNVPIGS 1639
Cdd:cd17653 206 Q------DF---PNLKTIF----LGGEAVPPSLLDRW----SPGRRLYNAYGPTECTISSTMTELLPG-----QPVTIGK 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1640 PLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVD 1719
Cdd:cd17653 264 PIPNSTCYILDADLQPVPEGVVGEICISGVQVARGYLGNPALTASKFVPDPFWPGSRMYRTGDYGRWTEDGGLEFLGRED 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1720 HQVKIRGYRIELGEIEASLLKYE-TIKTAVVIDQEDEagekyLCAYVVTEkDIPIPEVRAYLATKLPHYMIPQQLIPIHN 1798
Cdd:cd17653 344 NQVKVRGFRINLEEIEEVVLQSQpEVTQAAAIVVNGR-----LVAFVTPE-TVDVDGLRSELAKHLPSYAVPDRIIALDS 417
|
490
....*....|....
gi 446807313 1799 IPLTQNGKIDRSKL 1812
Cdd:cd17653 418 FPLTANGKVDRKAL 431
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
1332-1813 |
6.70e-115 |
|
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: 373.27 E-value: 6.70e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKR-ESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYM 1410
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1411 LTDSGCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCA 1490
Cdd:cd17648 81 LEDTGARVVIT-----------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1491 MYEDFSQDIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGE-KFDVTKLVQVILEEQVTLSYIPPTLLNEiYDYF 1569
Cdd:cd17648 126 LSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEmRFDPDRFYAYINREKVTYLSGTPSVLQQ-YDLA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1570 VRDNQKIVLnklLVGvEPIKTELLAKYDHLFRGnlQILNGYGPTEATVCCTSYRYESNKEITTQnvpIGSPLLNTKIYIL 1649
Cdd:cd17648 205 RLPHLKRVD---AAG-EEFTAPVFEKLRSRFAG--LIINAYGPTETTVTNHKRFFPGDQRFDKS---LGRPVRNTKCYVL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1650 DSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFE--------RGEKLYKTGDIARWLPDGNIEYLGRVDHQ 1721
Cdd:cd17648 276 NDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1722 VKIRGYRIELGEIEASLLKYETIKTAVVI-----DQEDEAGEKYLCAYVVTEKD-IPIPEVRAYLATKLPHYMIPQQLIP 1795
Cdd:cd17648 356 VKIRGQRIEPGEVEAALASYPGVRECAVVakedaSQAQSRIQKYLVGYYLPEPGhVPESDLLSFLRAKLPRYMVPARLVR 435
|
490
....*....|....*...
gi 446807313 1796 IHNIPLTQNGKIDRSKLP 1813
Cdd:cd17648 436 LEGIPVTINGKLDVRALP 453
|
|
| A_NRPS_ACVS-like |
cd17648 |
N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase; This family contains ACV ... |
289-770 |
2.51e-114 |
|
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: 371.73 E-value: 2.51e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKR-EFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYM 367
Cdd:cd17648 1 PDRVAVVYGDKRLTYRELNERANRLAHYLLSVAEIRpDDLVGLVLDKSELMIIAILAVWKAGAAYVPIDPSYPDERIQFI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 368 LTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCA 447
Cdd:cd17648 81 LEDTGARVVIT-----------------------------------NSTDLAYAIYTSGTTGKPKGVLVEHGSVVNLRTS 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 448 MYEDFSQDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGE-KFDVPKLVQVILEEQVTLAYIPPTLLNEiYDyF 526
Cdd:cd17648 126 LSERYFGRDNGDEAVLFFSNYVFDFFVEQMTLALLNGQKLVVPPDEmRFDPDRFYAYINREKVTYLSGTPSVLQQ-YD-L 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 527 VRANqkiSLNKLFVGVEPIKTELLAKYDHLFRGnlQILNLYGPTEATVCCTSYQYERDKEITTQnvpIGSPLLNTKIYIL 606
Cdd:cd17648 204 ARLP---HLKRVDAAGEEFTAPVFEKLRSRFAG--LIINAYGPTETTVTNHKRFFPGDQRFDKS---LGRPVRNTKCYVL 275
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 607 DSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFE--------RGEKLYKTGDIARWLPDGNIEYLGRVDHQ 678
Cdd:cd17648 276 NDAMKRVPVGAVGELYLGGDGVARGYLNRPELTAERFLPNPFQteqerargRNARLYKTGDLVRWLPSGELEYLGRNDFQ 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 679 VKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-----GEKYLCAYVVTEKD-IPIPEVRAYLATKLPYYMIPQQIIS 752
Cdd:cd17648 356 VKIRGQRIEPGEVEAALASYPGVRECAVVAKEDASqaqsrIQKYLVGYYLPEPGhVPESDLLSFLRAKLPRYMVPARLVR 435
|
490
....*....|....*...
gi 446807313 753 IQNIPLTQNGKIDRKKLP 770
Cdd:cd17648 436 LEGIPVTINGKLDVRALP 453
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
285-769 |
1.86e-105 |
|
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: 345.77 E-value: 1.86e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 285 VKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRV 364
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 365 EYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNF 444
Cdd:cd05945 81 REILDAAKPALLIA-----------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 445 LCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPK-LVQVILEEQVT----------LAY 513
Cdd:cd05945 126 TNWMLSDF--PLGPGDVFLNQAPFSFDLSVMDLYPALASGATLVPVPRDATADPKqLFRFLAEHGITvwvstpsfaaMCL 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 514 IPPTLLNEIY---DYFvranqkislnkLFVGvEPIKTELLAKYDHLFRGNlQILNLYGPTEATVCCTsyQYERDKEITTQ 590
Cdd:cd05945 204 LSPTFTPESLpslRHF-----------LFCG-EVLPHKTARALQQRFPDA-RIYNTYGPTEATVAVT--YIEVTPEVLDG 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 591 N--VPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGeklYKTGDIARWLPDGN 668
Cdd:cd05945 269 YdrLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRA---YRTGDLVRLEADGL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 669 IEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP---EVRAYLATKLPYYM 745
Cdd:cd05945 346 LFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGltkAIKAELAERLPPYM 425
|
490 500
....*....|....*....|....
gi 446807313 746 IPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05945 426 IPRRFVYLDELPLNANGKIDRKAL 449
|
|
| PRK05691 |
PRK05691 |
peptide synthase; Validated |
202-859 |
2.19e-105 |
|
peptide synthase; Validated
Pssm-ID: 235564 [Multi-domain] Cd Length: 4334 Bit Score: 379.13 E-value: 2.19e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 202 EQLKVQVDYNSTLYSEGLVSRIVNHLYNILDILMKDPNKSAMDLDVMPKTEKNQILFDFNHTTRVHKtLLCETVtapQLF 281
Cdd:PRK05691 3651 DDLGLHLSYDQRYFDAPTVERLLGEFKRLLLALVQGFHGDLSELPLLGEQERDFLLDGCNRSERDYP-LEQSYV---RLF 3726
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 282 EEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPK 361
Cdd:PRK05691 3727 EAQVAAHPQRIAASCLDQQWSYAELNRAANRLGHALRAAGVGVDQPVALLAERGLDLLGMIVGSFKAGAGYLPLDPGLPA 3806
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 362 QRVEYMLTDSG-----CSHVLTYQ-NSIIKGVAFQGSVINLM--DIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKG 433
Cdd:PRK05691 3807 QRLQRIIELSRtpvlvCSAACREQaRALLDELGCANRPRLLVweEVQAGEVASHNPGIYSGPDNLAYVIYTSGSTGLPKG 3886
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 434 VMIEHRS-LTNFLCAM-YEDFSQdigiTDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPK-LVQVILEEQVT 510
Cdd:PRK05691 3887 VMVEQRGmLNNQLSKVpYLALSE----ADVIAQTASQSFDISVWQFLAAPLFGARVEIVPNAIAHDPQgLLAHVQAQGIT 3962
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 511 LAYIPPTLLNEIYdyfvrANQKISLNKL---FVGVEPIKTELLAKYdhLFR-GNLQILNLYGPTEatvCCTSYQYERDKE 586
Cdd:PRK05691 3963 VLESVPSLIQGML-----AEDRQALDGLrwmLPTGEAMPPELARQW--LQRyPQIGLVNAYGPAE---CSDDVAFFRVDL 4032
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 587 ITTQN--VPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF-ERGEKLYKTGDIARW 663
Cdd:PRK05691 4033 ASTRGsyLPIGSPTDNNRLYLLDEALELVPLGAVGELCVAGTGVGRGYVGDPLRTALAFVPHPFgAPGERLYRTGDLARR 4112
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 664 LPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGeKYLCAYVV-----TEKDIPIPEVRAYLA 738
Cdd:PRK05691 4113 RSDGVLEYVGRIDHQVKIRGYRIELGEIEARLHEQAEVREAAVAVQEGVNG-KHLVGYLVphqtvLAQGALLERIKQRLR 4191
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 739 TKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQP-INNLKS-SHLEPTNSTERKLVEIWKDVLGIQRIGIRDNFFEIGGH 816
Cdd:PRK05691 4192 AELPDYMVPLHWLWLDRLPLNANGKLDRKALPALdIGQLQSqAYLAPRNELEQTLATIWADVLKVERVGVHDNFFELGGH 4271
|
650 660 670 680
....*....|....*....|....*....|....*....|...
gi 446807313 817 SLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYILEMEKS 859
Cdd:PRK05691 4272 SLLATQIASRVQKALQRNVPLRAMFECSTVEELAEYIEGLAGS 4314
|
|
| DltA |
cd05945 |
D-alanine:D-alanyl carrier protein ligase (DltA) and similar proteins; This family includes ... |
1328-1812 |
2.13e-101 |
|
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: 334.22 E-value: 2.13e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1328 VKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRV 1407
Cdd:cd05945 1 AAANPDRPAVVEGGRTLTYRELKERADALAAALASLGLDAGDPVVVYGHKSPDAIAAFLAALKAGHAYVPLDASSPAERI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1408 EYMLTDSGCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNF 1487
Cdd:cd05945 81 REILDAAKPALLIA-----------------------------------DGDDNAYIIFTSGSTGRPKGVQISHDNLVSF 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1488 LCAMYEDFsqDIGITDNVLFSSSISFDVTIFEIFVPLIYGArmTIYQ---GEKFDVTKLVQVILEEQVTLSYIPPTLLne 1564
Cdd:cd05945 126 TNWMLSDF--PLGPGDVFLNQAPFSFDLSVMDLYPALASGA--TLVPvprDATADPKQLFRFLAEHGITVWVSTPSFA-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1565 iydyfvrdnqkivlnKLLVGVEPIKTELLAKYDH-LFRGN---------LQ-------ILNGYGPTEATVCCTSYRYesN 1627
Cdd:cd05945 200 ---------------AMCLLSPTFTPESLPSLRHfLFCGEvlphktaraLQqrfpdarIYNTYGPTEATVAVTYIEV--T 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1628 KEITTQN--VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERGeklYKTGDIAR 1705
Cdd:cd05945 263 PEVLDGYdrLPIGYAKPGAKLVILDEDGRPVPPGEKGELVISGPSVSKGYLNNPEKTAAAFFPDEGQRA---YRTGDLVR 339
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1706 WLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP---EVRAYLAT 1782
Cdd:cd05945 340 LEADGLLFYRGRLDFQVKLNGYRIELEEIEAALRQVPGVKEAVVVPKYKGEKVTELIAFVVPKPGAEAGltkAIKAELAE 419
|
490 500 510
....*....|....*....|....*....|
gi 446807313 1783 KLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05945 420 RLPPYMIPRRFVYLDELPLNANGKIDRKAL 449
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
281-682 |
3.29e-101 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 332.35 E-value: 3.29e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 281 FEEQVKQNPNQIAIVCN-GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTEL 359
Cdd:pfam00501 1 LERQAARTPDKTALEVGeGRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 360 PKQRVEYMLTDSGCSHVLTYQNSIIKGVA---------------FQGSVINLMDIPFEEEQVEDLQITME---PQNLAYV 421
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELLealgklevvklvlvlDRDPVLKEEPLPEEAKPADVPPPPPPppdPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 422 IYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGIT--DNVLFSSSISFDV-TIFEIFVPLVCGARMTIYQGE-KFDV 497
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpdDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFpALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 498 PKLVQVILEEQVTLAYIPPTLLNEIYDY-FVRANQKISLNKLFVGVEPIKTELLAKYDHLFRGnlQILNLYGPTEATVCC 576
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG--ALVNGYGLTETTGVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 577 TSYQYERDKEITTqnVPIGSPLLNTKIYILDSFH-RLQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLY 655
Cdd:pfam00501 319 TTPLPLDEDLRSL--GSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWY 390
|
410 420
....*....|....*....|....*..
gi 446807313 656 KTGDIARWLPDGNIEYLGRVDHQVKIR 682
Cdd:pfam00501 391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| AMP-binding |
pfam00501 |
AMP-binding enzyme; |
1324-1725 |
3.62e-101 |
|
AMP-binding enzyme;
Pssm-ID: 459834 [Multi-domain] Cd Length: 417 Bit Score: 332.35 E-value: 3.62e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNE-KGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL 1402
Cdd:pfam00501 1 LERQAARTPDKTALEVGEgRRLTYRELDERANRLAAGLRALGVGKGDRVAILLPNSPEWVVAFLACLKAGAVYVPLNPRL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQRVEYMLTDSGCSHVLVHQNSIIKGI-EFQGN--------VIDLMDMSFEEE---------PGEDMHMMIEPHNLAYV 1464
Cdd:pfam00501 81 PAEELAYILEDSGAKVLITDDALKLEELlEALGKlevvklvlVLDRDPVLKEEPlpeeakpadVPPPPPPPPDPDDLAYI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1465 IYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGIT--DNVLFSSSISFDV-TIFEIFVPLIYGARMTIYQGE-KFDV 1540
Cdd:pfam00501 161 IYTSGTTGKPKGVMLTHRNLVANVLSIKRVRPRGFGLGpdDRVLSTLPLFHDFgLSLGLLGPLLAGATVVLPPGFpALDP 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1541 TKLVQVILEEQVTLSYIPPTLLNEIYDY-FVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFRGnlQILNGYGPTEATVCC 1619
Cdd:pfam00501 241 AALLELIERYKVTVLYGVPTLLNMLLEAgAPKRALLSSLRLVLSGGAPLPPELARRFRELFGG--ALVNGYGLTETTGVV 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1620 TSYRYESNKEITTqnVPIGSPLLNTKIYILDSFH-RIQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLY 1698
Cdd:pfam00501 319 TTPLPLDEDLRSL--GSVGRPLPGTEVKIVDDETgEPVPPGEPGELCVRGPGVMKGYLNDPELTAEAFDE------DGWY 390
|
410 420
....*....|....*....|....*..
gi 446807313 1699 KTGDIARWLPDGNIEYLGRVDHQVKIR 1725
Cdd:pfam00501 391 RTGDLGRRDEDGYLEIVGRKKDQIKLG 417
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
876-1285 |
5.69e-99 |
|
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: 326.53 E-value: 5.69e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 876 STSQKRMFIVDQFEdGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVH- 954
Cdd:cd19538 5 SFAQRRLWFLHQLE-GPSATYNIPLVIKLKGKLDVQALQQALYDVVERHESLRTVFPEEDGVPYQLILEEDEATPKLEIk 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 955 -VNEKDADYLIHEFIS-PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKG------NELPKL 1026
Cdd:cd19538 84 eVDEEELESEINEAVRyPFDLSEEPPFRATLFELGENEHVLLLLLHHIAADGWSLAPLTRDLSKAYRArckgeaPELAPL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1027 RVQYKDYVMWQ-----NGPYYKNLISEQKNYWLTTLKGeLPV-LNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLAT 1100
Cdd:cd19538 164 PVQYADYALWQqellgDESDPDSLIARQLAYWKKQLAG-LPDeIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLAK 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1101 ETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYE 1180
Cdd:cd19538 243 DNNVTLFMVLQAGFAALLTRLGAGTDIPIGSPVAGRNDDSLEDLVGFFVNTLVLRTDTSGNPSFRELLERVKETNLEAYE 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1181 NQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIGELEFTPYPFKQSVSKFDLSL-----VATEIDNNIHLKV 1255
Cdd:cd19538 323 HQDIPFERLVEALNPTRSRSRHPLFQIMLALQNTPQPSLDLPGLEAKLELRTVGSAKFDLTFelreqYNDGTPNGIEGFI 402
|
410 420 430
....*....|....*....|....*....|
gi 446807313 1256 EYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19538 403 EYRTDLFDHETIEALAQRYLLLLESAVENP 432
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
278-771 |
3.01e-98 |
|
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: 325.23 E-value: 3.01e-98
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 278 PQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDT 357
Cdd:COG0318 2 ADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 358 ELPKQRVEYMLTDSGCSHVLTyqnsiikgvafqgsvinlmdipfeeeqvedlqitmepqnlAYVIYTSGSTGQPKGVMIE 437
Cdd:COG0318 82 RLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVMLT 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 438 HRSLtnflCAMYEDFSQDIGIT--DNVLFSSSISFDV-TIFEIFVPLVCGARMTIYqgEKFDVPKLVQVILEEQVTLAYI 514
Cdd:COG0318 122 HRNL----LANAAAIAAALGLTpgDVVLVALPLFHVFgLTVGLLAPLLAGATLVLL--PRFDPERVLELIERERVTVLFG 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 515 PPTLLNEIYDYFVRANQKIS-LNKLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTsyqYERDKEITTQNVP 593
Cdd:COG0318 196 VPTMLARLLRHPEFARYDLSsLRLVVSGGAPLPPELLERFEERF--GVRIVEGYGLTETSPVVT---VNPEDPGERRPGS 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 594 IGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHpfergekLYKTGDIARWLPDGNIEYLG 673
Cdd:COG0318 271 VGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG-------WLRTGDLGRLDEDGYLYIVG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 674 RVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEKyLCAYVVTEKDIPI--PEVRAYLATKLPYYMIPQQI 750
Cdd:COG0318 344 RKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEkWGER-VVAFVVLRPGAELdaEELRAFLRERLARYKVPRRV 422
|
490 500
....*....|....*....|.
gi 446807313 751 ISIQNIPLTQNGKIDRKKLPQ 771
Cdd:COG0318 423 EFVDELPRTASGKIDRRALRE 443
|
|
| MenE/FadK |
COG0318 |
O-succinylbenzoic acid-CoA ligase MenE or related acyl-CoA synthetase (AMP-forming) [Lipid ... |
1320-1815 |
1.34e-95 |
|
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: 317.52 E-value: 1.34e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:COG0318 1 LADLLRRAAARHPDRPALVFGGRRLTYAELDARARRLAAALRALGVGPGDRVALLLPNSPEFVVAFLAALRAGAVVVPLN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSGCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiephnlAYVIYTSGSTGQPKGVMI 1479
Cdd:COG0318 81 PRLTAEELAYILEDSGARALVT----------------------------------------ALILYTSGTTGRPKGVML 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1480 EHRSLtnflCAMYEDFSQDIGIT--DNVLFSSSISFDV-TIFEIFVPLIYGARMTIYqgEKFDVTKLVQVILEEQVTLSY 1556
Cdd:COG0318 121 THRNL----LANAAAIAAALGLTpgDVVLVALPLFHVFgLTVGLLAPLLAGATLVLL--PRFDPERVLELIERERVTVLF 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1557 IPPTLLNEIYDYFVRDNQKI-VLNKLLVGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATVCCTSYRYESNKEITtqnV 1635
Cdd:COG0318 195 GVPTMLARLLRHPEFARYDLsSLRLVVSGGAPLPPELLERFEERF--GVRIVEGYGLTETSPVVTVNPEDPGERRP---G 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 PIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHpfergekLYKTGDIARWLPDGNIEYL 1715
Cdd:COG0318 270 SVGRPLPGVEVRIVDEDGRELPPGEVGEIVVRGPNVMKGYWNDPEATAEAFRDG-------WLRTGDLGRLDEDGYLYIV 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1716 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVTEKDIPI--PEVRAYLATKLPHYMIPQQ 1792
Cdd:COG0318 343 GRKKDMIISGGENVYPAEVEEVLAAHPGVAEAAVVGVPDEKwGER-VVAFVVLRPGAELdaEELRAFLRERLARYKVPRR 421
|
490 500
....*....|....*....|...
gi 446807313 1793 LIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:COG0318 422 VEFVDELPRTASGKIDRRALRER 444
|
|
| LCL_NRPS-like |
cd19540 |
LCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs) and similar domains; ... |
879-1285 |
1.50e-90 |
|
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: 302.03 E-value: 1.50e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 879 QKRMFIVDQFeDGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEP--NVDFNIEYVHVN 956
Cdd:cd19540 8 QQRLWFLNRL-DGPSAAYNIPLALRLTGALDVDALRAALADVVARHESLRTVFPEDDGGPYQVVLPaaEARPDLTVVDVT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 957 EKDADYLIHEFIS-PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY----KGNE--LPKLRVQ 1029
Cdd:cd19540 87 EDELAARLAEAARrGFDLTAELPLRARLFRLGPDEHVLVLVVHHIAADGWSMAPLARDLATAYaarrAGRApdWAPLPVQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1030 YKDYVMWQ-------NGPyyKNLISEQKNYWLTTLKGeLP-VLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATE 1101
Cdd:cd19540 167 YADYALWQrellgdeDDP--DSLAARQLAYWRETLAG-LPeELELPTDRPRPAVASYRGGTVEFTIDAELHARLAALARE 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1102 TGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYEN 1181
Cdd:cd19540 244 HGATLFMVLHAALAVLLSRLGAGDDIPIGTPVAGRGDEALDDLVGMFVNTLVLRTDVSGDPTFAELLARVRETDLAAFAH 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1182 QDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIGELEFTPYPFKQSVSKFDLSLVATE------IDNNIHLKV 1255
Cdd:cd19540 324 QDVPFERLVEALNPPRSTARHPLFQVMLAFQNTAAATLELPGLTVEPVPVDTGVAKFDLSFTLTErrdadgAPAGLTGEL 403
|
410 420 430
....*....|....*....|....*....|
gi 446807313 1256 EYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19540 404 EYATDLFDRSTAERLADRFVRVLEAVVADP 433
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
23-859 |
1.99e-89 |
|
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: 322.40 E-value: 1.99e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 23 WLDKLSgDVELSRFPCDCLSLNNIQASKESYYCQFPSdiAKRAVAISNNSdmllYTILLSGVKYLLSRYTDKDDVVIGMP 102
Cdd:TIGR03443 2 WSERLD-NPTLSVLPHDYLRPANNRLVEATYSLQLPS--AEVTAGGGSTP----FIILLAAFAALVYRLTGDEDIVLGTS 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 103 VFKQGQEetvfqnnfLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNLPLLNTIvmlddiHC 182
Cdd:TIGR03443 75 SNKSGRP--------FVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPPLFRL------AF 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 183 YESTDKINS--------DMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLYNILDILMKDPNKSAMDLDVMPKTEKN 254
Cdd:TIGR03443 141 QDAPDNQQTtystgsttDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDEPIGKVSLITPSQKS 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 255 qILFDfnHTTRVHktlLCETVTA-PQLFEEQVKQNPNQIAIV------CNG---KEITYKQLNIKANQLARRLLDQGVKR 324
Cdd:TIGR03443 221 -LLPD--PTKDLD---WSGFRGAiHDIFADNAEKHPDRTCVVetpsflDPSsktRSFTYKQINEASNILAHYLLKTGIKR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 325 EFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQR-VEYM----------LTDSGC--SHVLTYQN------SIIK 385
Cdd:TIGR03443 295 GDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqTIYLsvakpralivIEKAGTldQLVRDYIDkelelrTEIP 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 386 GVAFQ--GSVI------NLMDI--PFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqd 455
Cdd:TIGR03443 375 ALALQddGSLVggslegGETDVlaPYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRF--- 451
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 456 iGITDNVLFS--SSISFDVTIFEIFVPLVCGARMTIYQGEKFDVP-KLVQVILEEQVTLAYIPPT---LLNeiydyfVRA 529
Cdd:TIGR03443 452 -GLSENDKFTmlSGIAHDPIQRDMFTPLFLGAQLLVPTADDIGTPgRLAEWMAKYGATVTHLTPAmgqLLS------AQA 524
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 530 NQKI-SL-NKLFVGvepiktELLAKYDHL----FRGNLQILNLYGPTEaTVCCTSYQyerdkEITTQN------------ 591
Cdd:TIGR03443 525 TTPIpSLhHAFFVG------DILTKRDCLrlqtLAENVCIVNMYGTTE-TQRAVSYF-----EIPSRSsdstflknlkdv 592
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 592 VPIGSPLLNTKIYILDSFHRLQPIGVP--GEICISGIGLARGYINRKELTADKFIDHPF-------------ERGEK--- 653
Cdd:TIGR03443 593 MPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNNWFvdpshwidldkenNKPERefw 672
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 654 ------LYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKD 727
Cdd:TIGR03443 673 lgprdrLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVRENVTLVRRDKDEEPTLVSYIVPQDK 752
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 728 IP----------------------------IPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQP------- 772
Cdd:TIGR03443 753 SDeleefksevddeessdpvvkglikyrklIKDIREYLKKKLPSYAIPTVIVPLKKLPLNPNGKVDKPALPFPdtaqlaa 832
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 773 --INNLKSSHLEPTNSTERKLVEIWKDVLGIQ--RIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVD 848
Cdd:TIGR03443 833 vaKNRSASAADEEFTETEREIRDLWLELLPNRpaTISPDDSFFDLGGHSILATRMIFELRKKLNVELPLGLIFKSPTIKG 912
|
970
....*....|.
gi 446807313 849 FSKYILEMEKS 859
Cdd:TIGR03443 913 FAKEVDRLKKG 923
|
|
| alpha_am_amid |
TIGR03443 |
L-aminoadipate-semialdehyde dehydrogenase; Members of this protein family are ... |
1053-1904 |
9.47e-89 |
|
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: 320.09 E-value: 9.47e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1053 WLTTLKGeLPVLNFPTDFQRPTIQSFKGNVCSFNLGTDltfkvnKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSp 1132
Cdd:TIGR03443 2 WSERLDN-PTLSVLPHDYLRPANNRLVEATYSLQLPSA------EVTAGGGSTPFIILLAAFAALVYRLTGDEDIVLGT- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1133 iagRSHSDTNhmigmfinTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRDTSRNP-LFDTMFVF 1211
Cdd:TIGR03443 74 ---SSNKSGR--------PFVLRLNITPELSFLQLYAKVSEEEKEGASDIGVPFDELSEHIQAAKKLERTPpLFRLAFQD 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1212 QNmdmnpisigeleftpyPFKQS-VSKF---DLSLVATEIDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNPRV 1287
Cdd:TIGR03443 143 AP----------------DNQQTtYSTGsttDLTVFLTPSSPELELSIYYNSLLFSSDRITIVADQLAQLLSAASSNPDE 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1288 RLRNINMLSIEEEHCIMNEfnKKENSNSNYL-LVHKMFEEQVKRNPNQIAVV------CNEKG---ITYNELNIKANQLA 1357
Cdd:TIGR03443 207 PIGKVSLITPSQKSLLPDP--TKDLDWSGFRgAIHDIFADNAEKHPDRTCVVetpsflDPSSKtrsFTYKQINEASNILA 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1358 RRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQR--------------------------VEYM- 1410
Cdd:TIGR03443 285 HYLLKTGIKRGDVVMIYAYRGVDLVVAVMGVLKAGATFSVIDPAYPPARqtiylsvakpraliviekagtldqlvRDYId 364
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1411 -------------LTDSGCshvlvhqnsiIKGIEFQGNVIDLMdMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGV 1477
Cdd:TIGR03443 365 kelelrteipalaLQDDGS----------LVGGSLEGGETDVL-APYQALKDTPTGVVVGPDSNPTLSFTSGSEGIPKGV 433
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1478 MIEHRSLTNFLCAMYEDFsqdiGITDNVLFS--SSISFDVTIFEIFVPLIYGARMTIYQGEkfDV---TKLVQVILEEQV 1552
Cdd:TIGR03443 434 LGRHFSLAYYFPWMAKRF----GLSENDKFTmlSGIAHDPIQRDMFTPLFLGAQLLVPTAD--DIgtpGRLAEWMAKYGA 507
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1553 TLSYIPPTLlneiydyfvrdnqkivlNKLLVG--VEPIKT--------ELLAKYDHL----FRGNLQILNGYGPTEaTVC 1618
Cdd:TIGR03443 508 TVTHLTPAM-----------------GQLLSAqaTTPIPSlhhaffvgDILTKRDCLrlqtLAENVCIVNMYGTTE-TQR 569
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1619 CTSY-----RYESNKEITTQN--VPIGSPLLNTKIYILDSFHRIQPIGVP--GEICISGIGLARGYINRKELTADKFIDH 1689
Cdd:TIGR03443 570 AVSYfeipsRSSDSTFLKNLKdvMPAGKGMKNVQLLVVNRNDRTQTCGVGevGEIYVRAGGLAEGYLGLPELNAEKFVNN 649
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1690 PF-------------ERGEK---------LYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTA 1747
Cdd:TIGR03443 650 WFvdpshwidldkenNKPERefwlgprdrLYRTGDLGRYLPDGNVECCGRADDQVKIRGFRIELGEIDTHLSQHPLVREN 729
|
810 820 830 840 850 860 870 880
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1748 VVIDQEDEAGEKYLCAYVVTEKDIP----------------------------IPEVRAYLATKLPHYMIPQQLIPIHNI 1799
Cdd:TIGR03443 730 VTLVRRDKDEEPTLVSYIVPQDKSDeleefksevddeessdpvvkglikyrklIKDIREYLKKKLPSYAIPTVIVPLKKL 809
|
890 900 910 920 930 940 950 960
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1800 PLTQNGKIDRSKLPKLNT--------LGNSNYVPPR-NEIDSSLIDIWSSIL--GVNNIGINDNFFELGGHSLKGLKLFE 1868
Cdd:TIGR03443 810 PLNPNGKVDKPALPFPDTaqlaavakNRSASAADEEfTETEREIRDLWLELLpnRPATISPDDSFFDLGGHSILATRMIF 889
|
970 980 990
....*....|....*....|....*....|....*.
gi 446807313 1869 NIKRMFNVQLPLSLLFQKATIEQLSDVISRNKGIDS 1904
Cdd:TIGR03443 890 ELRKKLNVELPLGLIFKSPTIKGFAKEVDRLKKGEE 925
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
281-775 |
6.90e-79 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 271.00 E-value: 6.90e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 281 FEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGV--KREFIV-GVMmerSIEMIVGILGILKAGGAYLPIDT 357
Cdd:PRK04813 8 IEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLpdKSPIIVfGHM---SPEMLATFLGAVKAGHAYIPVDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 358 ELPKQRVEYMLTDSGCSHVLTYQNSIIKGVafQGSVINLMDIPFEEEQVEDLQIT--MEPQNLAYVIYTSGSTGQPKGVM 435
Cdd:PRK04813 85 SSPAERIEMIIEVAKPSLIIATEELPLEIL--GIPVITLDELKDIFATGNPYDFDhaVKGDDNYYIIFTSGTTGKPKGVQ 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 436 IEHRSLTNFLCAMYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQV------ 509
Cdd:PRK04813 163 ISHDNLVSFTNWMLEDFA--LPEGPQFLNQAPYSFDLSVMDLYPTLASGGTLVALPKDMTANFKQLFETLPQLPinvwvs 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 510 TLAYIPPTLLNEIYDyfvrANQKISLNK-LFVGVE-PIKT--ELLAKYDhlfrgNLQILNLYGPTEATVCCTsyQYERDK 585
Cdd:PRK04813 241 TPSFADMCLLDPSFN----EEHLPNLTHfLFCGEElPHKTakKLLERFP-----SATIYNTYGPTEATVAVT--SIEITD 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 586 EITTQN--VPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfERGEKLYKTGDIARw 663
Cdd:PRK04813 310 EMLDQYkrLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQPAYHTGDAGY- 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 664 LPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVT-----EKDIPI-PEVRAYL 737
Cdd:PRK04813 386 LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPkeedfEREFELtKAIKKEL 465
|
490 500 510
....*....|....*....|....*....|....*...
gi 446807313 738 ATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINN 775
Cdd:PRK04813 466 KERLMEYMIPRKFIYRDSLPLTPNGKIDRKALIEEVNK 503
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
876-1285 |
1.22e-76 |
|
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: 261.93 E-value: 1.22e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 876 STSQKRMFIVDQFEDGTNTtYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILD-GELVQKIEPNVDFNIEyvH 954
Cdd:cd19539 5 SFAQERLWFIDQGEDGGPA-YNIPGAWRLTGPLDVEALREALRDVVARHEALRTLLVRDDgGVPRQEILPPGPAPLE--V 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 955 VNEKDADY----LIHEFIS-----PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGNE--- 1022
Cdd:cd19539 82 RDLSDPDSdrerRLEELLReresrGFDLDEEPPIRAVLGRFDPDDHVLVLVAHHTAFDAWSLDVFARDLAALYAARRkgp 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1023 ---LPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGeLPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLA 1099
Cdd:cd19539 162 aapLPELRQQYKEYAAWQREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1100 TETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAY 1179
Cdd:cd19539 241 KRARSSLFMVLLAAYCVLLRRYTGQTDIVVGTPVAGRNHPRFESTVGFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQ 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1180 ENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQN-MDMNPISIGELEFTPYPFKQSVSKFDLSLVATEIDNNIHLKVEYS 1258
Cdd:cd19539 321 RHQELPFQQLVAELPVDRDAGRHPLVQIVFQVTNaPAGELELAGGLSYTEGSDIPDGAKFDLNLTVTEEGTGLRGSLGYA 400
|
410 420
....*....|....*....|....*..
gi 446807313 1259 IKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19539 401 TSLFDEETIQGFLADYLQVLRQLLANP 427
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
282-774 |
6.07e-75 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 259.69 E-value: 6.07e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 282 EEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGV-KREFIVgVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:TIGR01734 7 QAFAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILpKKSPII-VYGHMEPHMLVAFLGSIKSGHAYIPVDTSIP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 361 KQRVEymltdsgcshvltyqnsIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNLA-----------------YVIY 423
Cdd:TIGR01734 86 SERIE-----------------MIIEAAGPELVIHTAELSIDAVGTQIITLSALEQAETsggpvsfdhavkgddnyYIIY 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 424 TSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGITdnVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQV 503
Cdd:TIGR01734 149 TSGSTGNPKGVQISHDNLVSFTNWMLADFPLSEGKQ--FLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 504 ILEEQV------TLAYIPPTLLNEiydYFvraNQKI--SLNK-LFVGVE-PIKT--ELLAKYDhlfrgNLQILNLYGPTE 571
Cdd:TIGR01734 227 ELPKTGlnvwvsTPSFVDMCLLDP---NF---NQENypHLTHfLFCGEElPVKTakALLERFP-----KATIYNTYGPTE 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 572 ATVCCTSYQYERdkEITTQN--VPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHpfe 649
Cdd:TIGR01734 296 ATVAVTSVKITQ--EILDQYprLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH--- 370
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 650 RGEKLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGE-KYLCAYVVT---- 724
Cdd:TIGR01734 371 EGQPAYRTGDAGT-ITDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAIVPeted 449
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446807313 725 -EKDIPI-PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPIN 774
Cdd:TIGR01734 450 fEKEFQLtKAIKKELKKSLPAYMIPRKFIYRDQLPLTANGKIDRKALAEEVN 501
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
1353-2164 |
1.52e-74 |
|
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: 268.11 E-value: 1.52e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1353 ANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSII--KGI 1430
Cdd:COG3319 36 AAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALALALAAAAAALLLAALALLLALLAALalALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1431 EFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGITDNVLFSSS 1510
Cdd:COG3319 116 ALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVLVLAALLALLLAALLALALALAALLLLALA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1511 ISFDVTIFEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLnkLLVGVEPIKT 1590
Cdd:COG3319 196 AALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAALLLLLALALLLLLALLL--LLGLLALLLA 273
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1591 ELLAKYDHLFRGNLQILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIG 1670
Cdd:COG3319 274 LLLLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGG 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1671 LARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKyETIKTAVVI 1750
Cdd:COG3319 354 AGGLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAE-AAAVAAAVA 432
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1751 DQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATK--LPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLNTLGNSNYVPPRN 1828
Cdd:COG3319 433 AAAAAAAAAAALAAAVVAAAALAAAALLLLLLLllLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAA 512
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1829 EIDSSLIDIWSSILGVNNIGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSDVISRNKGIDSECLI 1908
Cdd:COG3319 513 ALELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAPTLAALAAALAAAAAAAALSPL 592
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1909 PIQNRTNKDSQWFIIHGQGGGILNYYDLARELGEDKTVYGLQSIGYDDSRFPNLSVEEMAVRYIEEIKQVKKEGPYTLLG 1988
Cdd:COG3319 593 VPLRAGGSGPPLFCVHPAGGNVLCYRPLARALGPDRPVYGLQAPGLDGGEPPPASVEEMAARYVEAIRAVQPEGPYHLLG 672
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1989 WSFGGIVAFEMARKLEELGDKVSFLGLLDVHPIEQGREILSLNIKNAFEELEKFNDQLGIEKISFEQMSEEQLIESLLKK 2068
Cdd:COG3319 673 WSFGGLVAYEMARQLEAQGEEVALLVLLDSYAPGALARLDEAELLAALLRDLARGVDLPLDAEELRALDPEERLARLLER 752
|
730 740 750 760 770 780 790 800
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 2069 ftLNENSCQQNFEDPMMNKL-KVMIANRYAYLKYnCKQKIKADIFLFNASINDIHPLVD-YNRWNEYTSGEVYALQVPGS 2146
Cdd:COG3319 753 --LREAGLPAGLDAERLRRLlRVFRANLRALRRY-RPRPYDGPVLLFRAEEDPPGRADDpALGWRPLVAGGLEVHDVPGD 829
|
810
....*....|....*...
gi 446807313 2147 HLSMLEKPHIHELVKSIK 2164
Cdd:COG3319 830 HFSMLREPHVAELAAALR 847
|
|
| PRK04813 |
PRK04813 |
D-alanine--poly(phosphoribitol) ligase subunit DltA; |
1322-1812 |
8.57e-74 |
|
D-alanine--poly(phosphoribitol) ligase subunit DltA;
Pssm-ID: 235313 [Multi-domain] Cd Length: 503 Bit Score: 256.36 E-value: 8.57e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1322 KMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTD 1401
Cdd:PRK04813 6 ETIEEFAQTQPDFPAYDYLGEKLTYGQLKEDSDALAAFIDSLKLPDKSPIIVFGHMSPEMLATFLGAVKAGHAYIPVDVS 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1402 LPKQRVEYMLTDSGCSHVL--VHQNSIIKGIEfqgnVIDLMD--MSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGV 1477
Cdd:PRK04813 86 SPAERIEMIIEVAKPSLIIatEELPLEILGIP----VITLDElkDIFATGNPYDFDHAVKGDDNYYIIFTSGTTGKPKGV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1478 MIEHRSLTNFLCAMYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLIYGArmTIYQGEKfDVTK----LVQVILEEQV- 1552
Cdd:PRK04813 162 QISHDNLVSFTNWMLEDFA--LPEGPQFLNQAPYSFDLSVMDLYPTLASGG--TLVALPK-DMTAnfkqLFETLPQLPIn 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1553 ----TLSYIPPTLLNEIYD--------YFvrdnqkivlnkLLVGVE-PIKT--ELLAKYDhlfrgNLQILNGYGPTEATV 1617
Cdd:PRK04813 237 vwvsTPSFADMCLLDPSFNeehlpnltHF-----------LFCGEElPHKTakKLLERFP-----SATIYNTYGPTEATV 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1618 CCTSYryESNKEITTQN--VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfERGE 1695
Cdd:PRK04813 301 AVTSI--EITDEMLDQYkrLPIGYAKPDSPLLIIDEEGTKLPDGEQGEIVISGPSVSKGYLNNPEKTAEAFFT---FDGQ 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1696 KLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVT-----EKD 1770
Cdd:PRK04813 376 PAYHTGDAGY-LEDGLLFYQGRIDFQIKLNGYRIELEEIEQNLRQSSYVESAVVVPYNKDHKVQYLIAYVVPkeedfERE 454
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446807313 1771 IPI-PEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK04813 455 FELtKAIKKELKERLMEYMIPRKFIYRDSLPLTPNGKIDRKAL 497
|
|
| D-ala-DACP-lig |
TIGR01734 |
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also ... |
1319-1812 |
1.02e-69 |
|
D-alanine--poly(phosphoribitol) ligase, subunit 1; This model represents the enzyme (also called D-alanine-D-alanyl carrier protein ligase) which activates D-alanine as an adenylate via the reaction D-ala + ATP -> D-ala-AMP + PPi, and further catalyzes the condensation of the amino acid adenylate with the D-alanyl carrier protein (D-ala-ACP). The D-alanine is then further transferred to teichoic acid in the biosynthesis of lipoteichoic acid (LTA) and wall teichoic acid (WTA) in gram positive bacteria, both polysacchatides. [Cell envelope, Biosynthesis and degradation of murein sacculus and peptidoglycan]
Pssm-ID: 273780 [Multi-domain] Cd Length: 502 Bit Score: 244.28 E-value: 1.02e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1319 LVHKMFEeQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPI 1398
Cdd:TIGR01734 2 LIEAIQA-FAETYPQTIAYRYQGQELTYQQLKEQSDRLAAFIQKRILPKKSPIIVYGHMEPHMLVAFLGSIKSGHAYIPV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1399 DTDLPKQRVEYMLTDSGCSHVLVHQNSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVM 1478
Cdd:TIGR01734 81 DTSIPSERIEMIIEAAGPELVIHTAELSIDAVGTQIITLSALEQAETSGGPVSFDHAVKGDDNYYIIYTSGSTGNPKGVQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1479 IEHRSLTNFLCAMYEDFSQDIGITdnVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQV------ 1552
Cdd:TIGR01734 161 ISHDNLVSFTNWMLADFPLSEGKQ--FLNQAPFSFDLSVMDLYPCLASGGTLHCLDKDITNNFKLLFEELPKTGlnvwvs 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1553 TLSYIPPTLLNEiydYFVRDNQKIVLNKLLVGVE-PIKT--ELLAKYDhlfrgNLQILNGYGPTEATVCCTSYryESNKE 1629
Cdd:TIGR01734 239 TPSFVDMCLLDP---NFNQENYPHLTHFLFCGEElPVKTakALLERFP-----KATIYNTYGPTEATVAVTSV--KITQE 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1630 ITTQN--VPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHpfeRGEKLYKTGDIARwL 1707
Cdd:TIGR01734 309 ILDQYprLPIGFAKPDMNLFIMDEEGEPLPEGEKGEIVIVGPSVSKGYLNNPEKTAEAFFSH---EGQPAYRTGDAGT-I 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1708 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGE-KYLCAYVVT-----EKDIPI-PEVRAYL 1780
Cdd:TIGR01734 385 TDGQLFYQGRLDFQIKLHGYRIELEDIEFNLRQSSYIESAVVVPKYNKDHKvEYLIAAIVPetedfEKEFQLtKAIKKEL 464
|
490 500 510
....*....|....*....|....*....|..
gi 446807313 1781 ATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:TIGR01734 465 KKSLPAYMIPRKFIYRDQLPLTANGKIDRKAL 496
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
871-1285 |
4.94e-67 |
|
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: 233.84 E-value: 4.94e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 871 EYYLaSTSQKRMFIVdQFEDGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKI-EPNVDFN 949
Cdd:cd19066 1 KIPL-SPMQRGMWFL-KKLATDPSAFNVAIEMFLTGSLDLARLKQALDAVMERHDVLRTRFCEEAGRYEQVVlDKTVRFR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 950 IEYV---HVNEKDA---DYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKG--- 1020
Cdd:cd19066 79 IEIIdlrNLADPEArllELIDQIQQTIYDLERGPLVRVALFRLADERDVLVVAIHHIIVDGGSFQILFEDISSVYDAaer 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1021 --NELPKLRVQYKDYVMWQNgpyyKNLISEQKN----YWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFK 1094
Cdd:cd19066 159 qkPTLPPPVGSYADYAAWLE----KQLESEAAQadlaYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKR 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1095 VNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLN 1174
Cdd:cd19066 235 LREVARESGTTPTQLLLAAFALALKRLTASIDVVIGLTFLNRPDEAVEDTIGLFLNLLPLRIDTSPDATFPELLKRTKEQ 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1175 TLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIGELEF-TPYPFKQSVSKFDLSLVATE-IDNNIH 1252
Cdd:cd19066 315 SREAIEHQRVPFIELVRHLGVVPEAPKHPLFEPVFTFKNNQQQLGKTGGFIFtTPVYTSSEGTVFDLDLEASEdPDGDLL 394
|
410 420 430
....*....|....*....|....*....|...
gi 446807313 1253 LKVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19066 395 LRLEYSRGVYDERTIDRFAERYMTALRQLIENP 427
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
418-765 |
1.25e-64 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 223.70 E-value: 1.25e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 418 LAYVIYTSGSTGQPKGVMIEHRSLtnflCAMYEDFSQDIGIT--DNVLFSSSISFDVTIFEIFVPLVCGARMTIYqgEKF 495
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNL----LAAAAALAASGGLTegDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL--PKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 496 DVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKIS-LNKLFVGVEPIKTELLAKYdhLFRGNLQILNLYGPTEATV 574
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSsLRALVSGGAPLPPELLERF--EEAPGIKLVNGYGLTETGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 575 CCTSYqyeRDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergeKL 654
Cdd:cd04433 154 TVATG---PPDDDARKPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 655 YKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP--E 732
Cdd:cd04433 224 YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDaeE 303
|
330 340 350
....*....|....*....|....*....|...
gi 446807313 733 VRAYLATKLPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:cd04433 304 LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| AFD_class_I |
cd04433 |
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as ... |
1461-1808 |
1.84e-64 |
|
Adenylate forming domain, Class I, also known as the ANL superfamily; This family is known as the ANL (acyl-CoA synthetases, the NRPS adenylation domains, and the Luciferase enzymes) superfamily. It includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases.The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341228 [Multi-domain] Cd Length: 336 Bit Score: 223.32 E-value: 1.84e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPKGVMIEHRSLtnflCAMYEDFSQDIGIT--DNVLFSSSISFDVTIFEIFVPLIYGARMTIYqgEKF 1538
Cdd:cd04433 2 PALILYTSGTTGKPKGVVLSHRNL----LAAAAALAASGGLTegDVFLSTLPLFHIGGLFGLLGALLAGGTVVLL--PKF 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1539 DVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIV-LNKLLVGVEPIKTELLAKYdhLFRGNLQILNGYGPTEATV 1617
Cdd:cd04433 76 DPEAALELIEREKVTILLGVPTLLARLLKAPESAGYDLSsLRALVSGGAPLPPELLERF--EEAPGIKLVNGYGLTETGG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1618 CCTSYRYESNKEittQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergeKL 1697
Cdd:cd04433 154 TVATGPPDDDAR---KPGSVGRPVPGVEVRIVDPDGGELPPGEIGELVVRGPSVMKGYWNNPEATAAVDED-------GW 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1698 YKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--E 1775
Cdd:cd04433 224 YRTGDLGRLDEDGYLYIVGRLKDMIKSGGENVYPAEVEAVLLGHPGVAEAAVVGVPDPEWGERVVAVVVLRPGADLDaeE 303
|
330 340 350
....*....|....*....|....*....|...
gi 446807313 1776 VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:cd04433 304 LRAHVRERLAPYKVPRRVVFVDALPRTASGKID 336
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
894-1285 |
4.67e-64 |
|
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: 225.27 E-value: 4.67e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 894 TTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHVNEKDADYLIhEFI----- 968
Cdd:cd20484 22 SAYNVPLCFRFSSKLDVEKFKQACQFVLEQHPILKSVIEEEDGVPFQKIEPSKPLSFQEEDISSLKESEII-AYLrekak 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 969 SPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKG---NELPKLRV---QYKDYVMWQNgpyy 1042
Cdd:cd20484 101 EPFVLENGPLMRVHLFSRSEQEHFVLITIHHIIFDGSSSLTLIHSLLDAYQAllqGKQPTLASspaSYYDFVAWEQ---- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1043 KNLIS----EQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILL 1118
Cdd:cd20484 177 DMLAGaegeEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKLLL 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1119 SRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYPFEELLEGLDLHRD 1198
Cdd:cd20484 257 HRYTGQEDIIVGMPTMGRPEERFDSLIGYFINMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLNIPRS 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1199 TSRNPLFDTMFVFQNMdmnpISIGELEFTPYPFKQSVS-----------KFDLSLVATEIDNNIHLKVEYSIKLFKAETI 1267
Cdd:cd20484 337 QANSPVFQVAFFYQNF----LQSTSLQQFLAEYQDVLSiefvegihqegEYELVLEVYEQEDRFTLNIKYNPDLFDASTI 412
|
410
....*....|....*...
gi 446807313 1268 ERLMVHFTNIVEEVTNNP 1285
Cdd:cd20484 413 ERMMEHYVKLAEELIANP 430
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
299-772 |
1.29e-60 |
|
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as alpha-aminoadipate reductase (EC 1.2.1.95) or alpha-AR or L-aminoadipate-semialdehyde dehydrogenase (EC 1.2.1.31), which catalyzes the activation of alpha-aminoadipate by ATP-dependent adenylation and the reduction of activated alpha-aminoadipate by NADPH. The activated alpha-aminoadipate is bound to the phosphopantheinyl group of the enzyme itself before it is reduced to (S)-2-amino-6-oxohexanoate.
Pssm-ID: 341302 [Multi-domain] Cd Length: 520 Bit Score: 218.16 E-value: 1.29e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 299 KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRveymltdsgcshvlt 378
Cdd:cd17647 19 RSFTYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR--------------- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 379 yQNsIIKGVAFQGSVINLmdipfeeeqvEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqdiGI 458
Cdd:cd17647 84 -QN-IYLGVAKPRGLIVI----------RAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRF----NL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 459 TDNVLFS--SSISFDVTIFEIFVPLVCGARMTIYQGEKFDVP-KLVQVILEEQVTLAYIPPTLlNEIYDYFVRANQKISL 535
Cdd:cd17647 148 SENDKFTmlSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPgRLAEWMAKYGATVTHLTPAM-GQLLTAQATTPFPKLH 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 536 NKLFVGvepiktELLAKYDHL----FRGNLQILNLYGPTEaTVCCTSYqYERDKEITTQN--------VPIGSPLLNTKI 603
Cdd:cd17647 227 HAFFVG------DILTKRDCLrlqtLAENVRIVNMYGTTE-TQRAVSY-FEVPSRSSDPTflknlkdvMPAGRGMLNVQL 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 604 YILDSFHRLQ--PIGVPGEICISGIGLARGYINRKELTADKFIDHPF-----------ERGE-----------KLYKTGD 659
Cdd:cd17647 299 LVVNRNDRTQicGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkDNNEpwrqfwlgprdRLYRTGD 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 660 IARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIP---------- 729
Cdd:cd17647 379 LGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPddesfaqedv 458
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 730 -------------------IPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQP 772
Cdd:cd17647 459 pkevstdpivkgligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQFP 520
|
|
| COG4908 |
COG4908 |
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General ... |
875-1107 |
1.02e-59 |
|
Uncharacterized conserved protein, contains a NRPS condensation (elongation) domain [General function prediction only];
Pssm-ID: 443936 [Multi-domain] Cd Length: 243 Bit Score: 206.04 E-value: 1.02e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 875 ASTSQKRMFivdqFEDGTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVH 954
Cdd:COG4908 1 LSPAQKRFL----FLEPGSNAYNIPAVLRLEGPLDVEALERALRELVRRHPALRTRFVEEDGEPVQRIDPDADLPLEVVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 955 VNEKDA--------DYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY------KG 1020
Cdd:COG4908 77 LSALPEpereaeleELVAEEASRPFDLARGPLLRAALIRLGEDEHVLLLTIHHIISDGWSLGILLRELAALYaallegEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1021 NELPKLRVQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLAT 1100
Cdd:COG4908 157 PPLPELPIQYADYAAWQRAWLQSEALEKQLEYWRQQLAGAPPVLELPTDRPRPAVQTFRGATLSFTLPAELTEALKALAK 236
|
....*..
gi 446807313 1101 ETGTTPY 1107
Cdd:COG4908 237 AHGATVN 243
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
301-769 |
1.41e-59 |
|
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: 213.10 E-value: 1.41e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 301 ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQ 380
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQNK 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 381 NSIIKGVAFQGSVINlMDIPFEEeqvedlqitmepqNLAYVIYTSGSTGQPKGVMIEHRSLTNFLcamyEDFSQDIGIT- 459
Cdd:cd17654 97 ELDNAPLSFTPEHRH-FNIRTDE-------------CLAYVIHTSGTTGTPKIVAVPHKCILPNI----QHFRSLFNITs 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 460 DNVLFSSSI-SFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEE--QVTLAYIPPTLLN----EIYDYFVRANQK 532
Cdd:cd17654 159 EDILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKrhRITVLQATPTLFRrfgsQSIKSTVLSATS 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 533 iSLNKLFVGVEPIKTELLAK-YDHLFRGnLQILNLYGPTEatVCCTSYQYERDKEITTqnVPIGSPLLNTKIYILDsfhr 611
Cdd:cd17654 239 -SLRVLALGGEPFPSLVILSsWRGKGNR-TRIFNIYGITE--VSCWALAYKVPEEDSP--VQLGSPLLGTVIEVRD---- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 612 LQPIGVPGEicISGIGLARGYINRKELTADKfidhpfergEKLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIELGEI 691
Cdd:cd17654 309 QNGSEGTGQ--VFLGGLNRVCILDDEVTVPK---------GTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINLDLI 376
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 692 EASLLKYETIKTAVVIQREDesgEKYLCAYVVTEKDIPIPEvRAYLaTKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd17654 377 QQVIESCLGVESCAVTLSDQ---QRLIAFIVGESSSSRIHK-ELQL-TLLSSHAIPDTFVQIDKLPLTSHGKVDKSEL 449
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
1323-1812 |
3.09e-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: 212.81 E-value: 3.09e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL 1402
Cdd:cd05936 4 LLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNPLY 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQRVEYMLTDSGCShvlvhqnSIIKGIEFQGNVIDLMDMSFEEEPgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHR 1482
Cdd:cd05936 84 TPRELEHILNDSGAK-------ALIVAVSFTDLLAAGAPLGERVAL--------TPEDVAVLQYTSGTTGVPKGAMLTHR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1483 SLTNFLCAMYEDFSQDIGITDNVLfsssisfdVTI--FEIF-------VPLIYGARMTIYqgEKFDVTKLVQVILEEQVT 1553
Cdd:cd05936 149 NLVANALQIKAWLEDLLEGDDVVL--------AALplFHVFgltvallLPLALGATIVLI--PRFRPIGVLKEIRKHRVT 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1554 LsyIP--PTLLNEIYDYFvrDNQKIVLNKLLV---GVEPIKTELLAKYDHLFRGNlqILNGYGPTEA--TVCCTSYRYEs 1626
Cdd:cd05936 219 I--FPgvPTMYIALLNAP--EFKKRDFSSLRLcisGGAPLPVEVAERFEELTGVP--IVEGYGLTETspVVAVNPLDGP- 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1627 NKEITtqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARW 1706
Cdd:cd05936 292 RKPGS-----IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIGYM 359
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1707 LPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKyLCAYVVTEKDIPI--PEVRAYLATK 1783
Cdd:cd05936 360 DEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPySGEA-VKAFVVLKEGASLteEEIIAFCREQ 438
|
490 500
....*....|....*....|....*....
gi 446807313 1784 LPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05936 439 LAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| A_NRPS_acs4 |
cd17654 |
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal ... |
1344-1812 |
2.41e-58 |
|
acyl-CoA synthetase family member 4; This family of the adenylation (A) domain of nonribosomal peptide synthases (NRPS) contains acyl-CoA synthethase family member 4, also known as 2-aminoadipic 6-semialdehyde dehydrogenase or aminoadipate-semialdehyde dehydrogenase, most of which are uncharacterized. Acyl-CoA synthetase catalyzes the initial reaction in fatty acid metabolism, by forming a thioester with CoA. NRPSs are large multifunctional enzymes which synthesize many therapeutically useful peptides in bacteria and fungi via a template-directed, nucleic acid independent nonribosomal mechanism. These natural products include antibiotics, immunosuppressants, plant and animal toxins, and enzyme inhibitors. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341309 [Multi-domain] Cd Length: 449 Bit Score: 209.64 E-value: 2.41e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHq 1423
Cdd:cd17654 17 VSYADLAEKISNLSNFLRKKFQTEERAIGLRCDRGTESPVAILAILFLGAAYAPIDPASPEQRSLTVMKKCHVSYLLQN- 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nsiikgiefqgnviDLMDMSFEEEPGEDMHMMIE-PHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLcamyEDFSQDIGIT 1502
Cdd:cd17654 96 --------------KELDNAPLSFTPEHRHFNIRtDECLAYVIHTSGTTGTPKIVAVPHKCILPNI----QHFRSLFNIT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1503 -DNVLFSSSI-SFDVTIFEIFVPLIYGARMTIYQGEKFDVTKLVQVILEE--QVTLSYIPPTLLNEiydYFVRDNQKIVL 1578
Cdd:cd17654 158 sEDILFLTSPlTFDPSVVEIFLSLSSGATLLIVPTSVKVLPSKLADILFKrhRITVLQATPTLFRR---FGSQSIKSTVL 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1579 NK------LLVGVEPIKTELLAK-YDHLFRGnLQILNGYGPTEatVCCTSYRYESNKEITTqnVPIGSPLLNTKIYILDs 1651
Cdd:cd17654 235 SAtsslrvLALGGEPFPSLVILSsWRGKGNR-TRIFNIYGITE--VSCWALAYKVPEEDSP--VQLGSPLLGTVIEVRD- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1652 fhrIQPIGVPGEicISGIGLARGYINRKELTADKfidhpfergEKLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIEL 1731
Cdd:cd17654 309 ---QNGSEGTGQ--VFLGGLNRVCILDDEVTVPK---------GTMRATGDFVT-VKDGELFFLGRKDSQIKRRGKRINL 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1732 GEIEASLLKYETIKTAVVIDQEDeagEKYLCAYVVTEKDIPIPEvRAYLaTKLPHYMIPQQLIPIHNIPLTQNGKIDRSK 1811
Cdd:cd17654 374 DLIQQVIESCLGVESCAVTLSDQ---QRLIAFIVGESSSSRIHK-ELQL-TLLSSHAIPDTFVQIDKLPLTSHGKVDKSE 448
|
.
gi 446807313 1812 L 1812
Cdd:cd17654 449 L 449
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
876-1281 |
1.84e-57 |
|
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: 206.34 E-value: 1.84e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 876 STSQKRMFIVDQF-EDgtNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVH 954
Cdd:cd20483 5 STFQRRLWFLHNFlED--KTFLNLLLVCHIKGKPDVNLLQKALSELVRRHEVLRTAYFEGDDFGEQQVLDDPSFHLIVID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 955 VN-EKDADYLIHEFIS-----PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKG-------N 1021
Cdd:cd20483 83 LSeAADPEAALDQLVRnlrrqELDIEEGEVIRGWLVKLPDEEFALVLASHHIAWDRGSSKSIFEQFTALYDAlragrdlA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1022 ELPKLRVQYKDYVMWQN----GPYYKNLISeqknYWLTTLKG---ELPVLNFPTDfQRPTIQSFKGNVCSFNLGTDLTFK 1094
Cdd:cd20483 163 TVPPPPVQYIDFTLWHNallqSPLVQPLLD----FWKEKLEGipdASKLLPFAKA-ERPPVKDYERSTVEATLDKELLAR 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1095 VNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLN 1174
Cdd:cd20483 238 MKRICAQHAVTPFMFLLAAFRAFLYRYTEDEDLTIGMVDGDRPHPDFDDLVGFFVNMLPIRCRMDCDMSFDDLLESTKTT 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1175 TLEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQnMD--MNPISIGELEFTPYPFKQSVSKFDLSLVATEI-DNNI 1251
Cdd:cd20483 318 CLEAYEHSAVPFDYIVDALDVPRSTSHFPIGQIAVNYQ-VHgkFPEYDTGDFKFTDYDHYDIPTACDIALEAEEDpDGGL 396
|
410 420 430
....*....|....*....|....*....|
gi 446807313 1252 HLKVEYSIKLFKAETIERLMVHFTNIVEEV 1281
Cdd:cd20483 397 DLRLEFSTTLYDSADMERFLDNFVTFLTSV 426
|
|
| FC-FACS_FadD_like |
cd05936 |
Prokaryotic long-chain fatty acid CoA synthetases similar to Escherichia coli FadD; This ... |
278-769 |
6.73e-56 |
|
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: 202.79 E-value: 6.73e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 278 PQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDT 357
Cdd:cd05936 2 ADLLEEAARRFPDKTALIFMGRKLTYRELDALAEAFAAGLQNLGVQPGDRVALMLPNCPQFPIAYFGALKAGAVVVPLNP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 358 ELPKQRVEYMLTDSGCShvltyqnSIIKGVAFQGSVINLMDIPFEEEqvedlqitMEPQNLAYVIYTSGSTGQPKGVMIE 437
Cdd:cd05936 82 LYTPRELEHILNDSGAK-------ALIVAVSFTDLLAAGAPLGERVA--------LTPEDVAVLQYTSGTTGVPKGAMLT 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 438 HRSLTNFLCAMYEDFSQDIGITDNVLfsssisfdVTI--FEIF-------VPLVCGARMTIYqgEKFDVPKLVQVILEEQ 508
Cdd:cd05936 147 HRNLVANALQIKAWLEDLLEGDDVVL--------AALplFHVFgltvallLPLALGATIVLI--PRFRPIGVLKEIRKHR 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 509 VTLayIP--PTLLNEIYDYFvrANQKISLNKL---FVGVEPIKTELLAKYDHLFRGNlqILNLYGPTEA--TVCCTSYQY 581
Cdd:cd05936 217 VTI--FPgvPTMYIALLNAP--EFKKRDFSSLrlcISGGAPLPVEVAERFEELTGVP--IVEGYGLTETspVVAVNPLDG 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 582 ERdKEITtqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIA 661
Cdd:cd05936 291 PR-KPGS-----IGIPLPGTEVKIVDDDGEELPPGEVGELWVRGPQVMKGYWNRPEETAEAFVDGWL-------RTGDIG 357
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 662 RWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEKyLCAYVVTEKDIPI--PEVRAYLA 738
Cdd:cd05936 358 YMDEDGYFFIVDRKKDMIIVGGFNVYPREVEEVLYEHPAVAEAAVVGVPDPySGEA-VKAFVVLKEGASLteEEIIAFCR 436
|
490 500 510
....*....|....*....|....*....|.
gi 446807313 739 TKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05936 437 EQLAGYKVPRQVEFRDELPKSAVGKILRREL 467
|
|
| A_NRPS_alphaAR |
cd17647 |
Alpha-aminoadipate reductase; This family contains L-2-aminoadipate reductase, also known as ... |
1345-1813 |
8.18e-55 |
|
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: 201.21 E-value: 8.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRveymltdsgcshvlvhQN 1424
Cdd:cd17647 22 TYRDINEASNIVAHYLIKTGIKRGDVVMIYSYRGVDLMVAVMGVLKAGATFSVIDPAYPPAR----------------QN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 sIIKGIEFQGNVIDLmdmsfeeepgEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqdiGITDN 1504
Cdd:cd17647 86 -IYLGVAKPRGLIVI----------RAAGVVVGPDSNPTLSFTSGSEGIPKGVLGRHFSLAYYFPWMAKRF----NLSEN 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 VLFS--SSISFDVTIFEIFVPLIYGARMTIYQGEKFDVT-KLVQVILEEQVTLSYIPPT----LLNEIYDYFVRDNQKIV 1577
Cdd:cd17647 151 DKFTmlSGIAHDPIQRDMFTPLFLGAQLLVPTQDDIGTPgRLAEWMAKYGATVTHLTPAmgqlLTAQATTPFPKLHHAFF 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1578 LNKLLVGVEPIKTELLAKydhlfrgNLQILNGYGPTEatvcctSYRYESNKEITTQN------------VPIGSPLLNTK 1645
Cdd:cd17647 231 VGDILTKRDCLRLQTLAE-------NVRIVNMYGTTE------TQRAVSYFEVPSRSsdptflknlkdvMPAGRGMLNVQ 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1646 IYILDSFHRIQ--PIGVPGEICISGIGLARGYINRKELTADKFIDHPF-----------ERGE-----------KLYKTG 1701
Cdd:cd17647 298 LLVVNRNDRTQicGIGEVGEIYVRAGGLAEGYRGLPELNKEKFVNNWFvepdhwnyldkDNNEpwrqfwlgprdRLYRTG 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1702 DIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIP--------- 1772
Cdd:cd17647 378 DLGRYLPNGDCECCGRADDQVKIRGFRIELGEIDTHISQHPLVRENITLVRRDKDEEPTLVSYIVPRFDKPddesfaqed 457
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1773 --------------------IPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLP 1813
Cdd:cd17647 458 vpkevstdpivkgligyrklIKDIREFLKKRLASYAIPSLIVVLDKLPLNPNGKVDKPKLQ 518
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
1317-1812 |
4.11e-54 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 199.26 E-value: 4.11e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1317 YLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYL 1396
Cdd:PRK06187 5 PLTIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLH 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1397 PIDTDLPKQRVEYMLTDSGCSHVLVHQNSI-----IKG-IEFQGNVI-----DLMDM-----SFEE----EPGEDMHMMI 1456
Cdd:PRK06187 85 PINIRLKPEEIAYILNDAEDRVVLVDSEFVpllaaILPqLPTVRTVIvegdgPAAPLapevgEYEEllaaASDTFDFPDI 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1457 EPHNLAYVIYTSGSTGQPKGVMIEHRSLT--NFLCAMYEDFSQDigitdnvlfSSSISFdVTIFEIF------VPLIYGA 1528
Cdd:PRK06187 165 DENDAAAMLYTSGTTGHPKGVVLSHRNLFlhSLAVCAWLKLSRD---------DVYLVI-VPMFHVHawglpyLALMAGA 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1529 RMtIYQGEkFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIV-LNKLLVGVEPIKTELLAKYDHLFRGnlQIL 1607
Cdd:PRK06187 235 KQ-VIPRR-FDPENLLDLIETERVTFFFAVPTIWQMLLKAPRAYFVDFSsLRLVIYGGAALPPALLREFKEKFGI--DLV 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1608 NGYGPTEATVCCTSYRYEsnKEITTQNVPIGS---PLLNTKIYILDSFHRIQP--IGVPGEICISGIGLARGYINRKELT 1682
Cdd:PRK06187 311 QGYGMTETSPVVSVLPPE--DQLPGQWTKRRSagrPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPEAT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1683 ADKFIDhpferGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYL 1761
Cdd:PRK06187 389 AETIDG-----G--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEKwGERPV 461
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446807313 1762 cAYVVTEKDIPI--PEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK06187 462 -AVVVLKPGATLdaKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVL 513
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
1328-1812 |
4.88e-54 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 199.95 E-value: 4.88e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1328 VKRNPNQIAVV-CNEKG----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL 1402
Cdd:COG0365 19 AEGRGDKVALIwEGEDGeertLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSPVFPGF 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQRVEYMLTDSGCSHVLVHQNSIIKGIEFQG---------------NVI------------------DLMDMSFEEEPG 1449
Cdd:COG0365 99 GAEALADRIEDAEAKVLITADGGLRGGKVIDLkekvdealeelpsleHVIvvgrtgadvpmegdldwdELLAAASAEFEP 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1450 EDM---HMMiephnlaYVIYTSGSTGQPKGVMIEHRSLTNFLcAMYEDFSQDIGITDNVLFSSSISFdVT--IFEIFVPL 1524
Cdd:COG0365 179 EPTdadDPL-------FILYTSGTTGKPKGVVHTHGGYLVHA-ATTAKYVLDLKPGDVFWCTADIGW-ATghSYIVYGPL 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1525 IYGARMTIYQGEKF--DVTKLVQVILEEQVTLSYIPPTLlneiYDYFVRDNQKIVLN------KLLVGV-EPIKTELLAK 1595
Cdd:COG0365 250 LNGATVVLYEGRPDfpDPGRLWELIEKYGVTVFFTAPTA----IRALMKAGDEPLKKydlsslRLLGSAgEPLNPEVWEW 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1596 -YDHLfrgNLQILNGYGPTEATVCCTSYRyesnkeITTQNVP--IGSPLLNTKIYILDSFHRIQPIGVPGEICISG--IG 1670
Cdd:COG0365 326 wYEAV---GVPIVDGWGQTETGGIFISNL------PGLPVKPgsMGKPVPGYDVAVVDEDGNPVPPGEEGELVIKGpwPG 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1671 LARGYINRKELTADKFidhpFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI 1750
Cdd:COG0365 397 MFRGYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVSHPAVAEAAVV 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 1751 DQEDEAGEKYLCAYVVTEKDIP-----IPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:COG0365 473 GVPDEIRGQVVKAFVVLKPGVEpsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
873-1285 |
3.67e-53 |
|
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: 193.57 E-value: 3.67e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 873 YLASTSQKRMFIVDQFEDGTNTtYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQIL-DGELVQKIEPNVDFNIE 951
Cdd:cd19543 2 YPLSPMQEGMLFHSLLDPGSGA-YVEQMVITLEGPLDPDRFRAAWQAVVDRHPILRTSFVWEgLGEPLQVVLKDRKLPWR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 952 YV---HVNEKDADYLIHEFIS-----PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY----- 1018
Cdd:cd19543 81 ELdlsHLSEAEQEAELEALAEedrerGFDLARAPLMRLTLIRLGDDRYRLVWSFHHILLDGWSLPILLKELFAIYaalge 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1019 -KGNELPKLRvQYKDYVMW---QNGpyyknliSEQKNYWLTTLKG--ELPVLnfPTDFQRPTIQSFKGNVCSFNLGTDLT 1092
Cdd:cd19543 161 gQPPSLPPVR-PYRDYIAWlqrQDK-------EAAEAYWREYLAGfeEPTPL--PKELPADADGSYEPGEVSFELSAELT 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1093 FKVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRsHSDTN---HMIGMFINTLVMRNYLENDDEFIEFLS 1169
Cdd:cd19543 231 ARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVFGTTVSGR-PAELPgieTMVGLFINTLPVRVRLDPDQTVLELLK 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1170 RLKLNTLEAYENQDYPFEELLEGLDLHRdtsrnPLFDTMFVFQNMdmnPI--------SIGELEFTP-YPFKQsvSKFDL 1240
Cdd:cd19543 310 DLQAQQLELREHEYVPLYEIQAWSEGKQ-----ALFDHLLVFENY---PVdesleeeqDEDGLRITDvSAEEQ--TNYPL 379
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446807313 1241 SLVATEiDNNIHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19543 380 TVVAIP-GEELTIKLSYDAEVFDEATIERLLGHLRRVLEQVAANP 423
|
|
| Acs |
COG0365 |
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism]; |
280-769 |
7.79e-53 |
|
Acyl-coenzyme A synthetase/AMP-(fatty) acid ligase [Lipid transport and metabolism];
Pssm-ID: 440134 [Multi-domain] Cd Length: 565 Bit Score: 196.49 E-value: 7.79e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 280 LFEEQVKQNPNQIAIVCNG-----KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLP 354
Cdd:COG0365 14 CLDRHAEGRGDKVALIWEGedgeeRTLTYAELRREVNRFANALRALGVKKGDRVAIYLPNIPEAVIAMLACARIGAVHSP 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 355 IDTELPKQRVEYMLTDSGCSHVLTYQnsiikGVAFQGSVINLM------------------------------DIPFEE- 403
Cdd:COG0365 94 VFPGFGAEALADRIEDAEAKVLITAD-----GGLRGGKVIDLKekvdealeelpslehvivvgrtgadvpmegDLDWDEl 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 404 --EQVEDLQIT-MEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLcAMYEDFSQDIGITDNVLFSSSISFdVT--IFEIF 478
Cdd:COG0365 169 laAASAEFEPEpTDADDPLFILYTSGTTGKPKGVVHTHGGYLVHA-ATTAKYVLDLKPGDVFWCTADIGW-ATghSYIVY 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 479 VPLVCGARMTIYQGEKF--DVPKLVQVILEEQVTLAYIPPTLlneiYDYFVRANQKI-------SLNKLF-VGvEPIKTE 548
Cdd:COG0365 247 GPLLNGATVVLYEGRPDfpDPGRLWELIEKYGVTVFFTAPTA----IRALMKAGDEPlkkydlsSLRLLGsAG-EPLNPE 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 549 LLAK-YDHLfrgNLQILNLYGPTEATVCCTSyqyerdkeittqNVP--------IGSPLLNTKIYILDSFHRLQPIGVPG 619
Cdd:COG0365 322 VWEWwYEAV---GVPIVDGWGQTETGGIFIS------------NLPglpvkpgsMGKPVPGYDVAVVDEDGNPVPPGEEG 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 620 EICISG--IGLARGYINRKELTADKFidhpFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLK 697
Cdd:COG0365 387 ELVIKGpwPGMFRGYWNDPERYRETY----FGRFPGWYRTGDGARRDEDGYFWILGRSDDVINVSGHRIGTAEIESALVS 462
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 698 YETIKTAVVIQREDESGEKYLCAYVVTEKDIP-----IPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:COG0365 463 HPAVAEAAVVGVPDEIRGQVVKAFVVLKPGVEpsdelAKELQAHVREELGPYAYPREIEFVDELPKTRSGKIMRRLL 539
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
297-764 |
1.92e-52 |
|
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341237 [Multi-domain] Cd Length: 486 Bit Score: 193.20 E-value: 1.92e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 297 NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHV 376
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 377 LTYQNS---IIKGVAFQGSV--INLMDI-------------PFEEEQVEDLQITME--PQNLAYVIYTSGSTGQPKGVMI 436
Cdd:cd05911 87 FTDPDGlekVKEAAKELGPKdkIIVLDDkpdgvlsiedllsPTLGEEDEDLPPPLKdgKDDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 437 EHRSLTnFLCAMYEDFSQDIGITDNVLFSSSISFDVT-IFEIFVPLVCGARMTIYQgeKFDVPKLVQVILEEQVTLAYIP 515
Cdd:cd05911 167 SHRNLI-ANLSQVQTFLYGNDGSNDVILGFLPLYHIYgLFTTLASLLNGATVIIMP--KFDSELFLDLIEKYKITFLYLV 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 516 PTLLNEIYDY-FVRANQKISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEATVCCTSYQYERDKEITTqnvpi 594
Cdd:cd05911 244 PPIAAALAKSpLLDKYDLSSLRVILSGGAPLSKELQELLAKRF-PNATIKQGYGMTETGGILTVNPDGDDKPGSV----- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 595 GSPLLNTKIYILDSFHR-LQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLG 673
Cdd:cd05911 318 GRLLPNVEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYFDEDGYLYIVD 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 674 RVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-------TEKdipipEVRAYLATKLP-YYM 745
Cdd:cd05911 392 RKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEVSGELPRAYVVrkpgeklTEK-----EVKDYVAKKVAsYKQ 466
|
490
....*....|....*....
gi 446807313 746 IPQQIISIQNIPLTQNGKI 764
Cdd:cd05911 467 LRGGVVFVDEIPKSASGKI 485
|
|
| C_PKS-NRPS |
cd19532 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
876-1285 |
2.00e-51 |
|
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: 188.43 E-value: 2.00e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 876 STSQKRMFIVDQF-EDgtNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSF--QILDGELVQKIEPNVDFNIEY 952
Cdd:cd19532 5 SFGQSRFWFLQQYlED--PTTFNVTFSYRLTGPLDVARLERAVRAVGQRHEALRTCFftDPEDGEPMQGVLASSPLRLEH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 953 VHV-NEKDADYLIHEFIS-PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGNELPKLRVQY 1030
Cdd:cd19532 83 VQIsDEAEVEEEFERLKNhVYDLESGETMRIVLLSLSPTEHYLIFGYHHIAMDGVSFQIFLRDLERAYNGQPLLPPPLQY 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1031 KDYVMWQNGPYYKNLISEQKNYW---LTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPY 1107
Cdd:cd19532 163 LDFAARQRQDYESGALDEDLAYWkseFSTLPEPLPLLPFAKVKSRPPLTRYDTHTAERRLDAALAARIKEASRKLRVTPF 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1108 MILLAIYNILLSRYTGQEDIIVGspI--AGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQDYP 1185
Cdd:cd19532 243 HFYLAALQVLLARLLDVDDICIG--IadANRTDEDFMETIGFFLNLLPLRFRRDPSQTFADVLKETRDKAYAALAHSRVP 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1186 FEELLEGLDLHRDTSRNPLFDTMF-----VFQNMDMNPISIGELEF----TPYpfkqsvskfDLSLvatEIDNN------ 1250
Cdd:cd19532 321 FDVLLDELGVPRSATHSPLFQVFInyrqgVAESRPFGDCELEGEEFedarTPY---------DLSL---DIIDNpdgdcl 388
|
410 420 430
....*....|....*....|....*....|....*.
gi 446807313 1251 IHLKV-EYsikLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19532 389 LTLKVqSS---LYSEEDAELLLDSYVNLLEAFARDP 421
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
299-769 |
9.66e-51 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341275 [Multi-domain] Cd Length: 439 Bit Score: 186.87 E-value: 9.66e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 299 KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVlt 378
Cdd:cd05971 5 EKVTFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL-- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 379 yqnsiikgvafqgsvinlmdipfeeeqvedlqITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMY---EDFSQD 455
Cdd:cd05971 83 --------------------------------VTDGSDDPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQfpfNLFPRD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 456 igitDNVLFSSS----ISfdvTIFEIFVP-LVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEI-YDYFVRA 529
Cdd:cd05971 131 ----GDLYWTPAdwawIG---GLLDVLLPsLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMrQQGEQLK 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 530 NQKISLNKLFVGVEPIKTELLA-KYDHLfrgNLQILNLYGPTEATVCCTSYQYERDkeitTQNVPIGSPLLNTKIYILDS 608
Cdd:cd05971 204 HAQVKLRAIATGGESLGEELLGwAREQF---GVEVNEFYGQTECNLVIGNCSALFP----IKPGSMGKPIPGHRVAIVDD 276
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 609 FHRLQPIGVPGEICI---SGIGLArGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYR 685
Cdd:cd05971 277 NGTPLPPGEVGEIAVelpDPVAFL-GYWNNPSATEKKMAG-------DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYR 348
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 686 IELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-----TEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQ 760
Cdd:cd05971 349 IGPAEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpgeTPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTA 428
|
....*....
gi 446807313 761 NGKIDRKKL 769
Cdd:cd05971 429 TGKIRRREL 437
|
|
| PRK06187 |
PRK06187 |
long-chain-fatty-acid--CoA ligase; Validated |
276-773 |
1.90e-50 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235730 [Multi-domain] Cd Length: 521 Bit Score: 188.47 E-value: 1.90e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 276 TAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI 355
Cdd:PRK06187 7 TIGRILRHGARKHPDKEAVYFDGRRTTYAELDERVNRLANALRALGVKKGDRVAVFDWNSHEYLEAYFAVPKIGAVLHPI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 356 DTELPKQRVEYMLTDSGCSHVLTYQN--SIIKGVA----FQGSVINLMDIPFEEEQV--------------EDLQITMEP 415
Cdd:PRK06187 87 NIRLKPEEIAYILNDAEDRVVLVDSEfvPLLAAILpqlpTVRTVIVEGDGPAAPLAPevgeyeellaaasdTFDFPDIDE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 416 QNLAYVIYTSGSTGQPKGVMIEHRSLT--NFLCAMYEDFSQDigitdnvlfSSSISFdVTIFEIF------VPLVCGARM 487
Cdd:PRK06187 167 NDAAAMLYTSGTTGHPKGVVLSHRNLFlhSLAVCAWLKLSRD---------DVYLVI-VPMFHVHawglpyLALMAGAKQ 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 488 tIYQGEkFDVPKLVQVILEEQVTLAYIPPT----LLNEIYDYFVRANqkiSLNKLFVGVEPIKTELLAKYDHLFRGnlQI 563
Cdd:PRK06187 237 -VIPRR-FDPENLLDLIETERVTFFFAVPTiwqmLLKAPRAYFVDFS---SLRLVIYGGAALPPALLREFKEKFGI--DL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 564 LNLYGPTEATVCCTSYQYERDkeiTTQNVPI----GSPLLNTKIYILDSFHRLQP--IGVPGEICISGIGLARGYINRKE 637
Cdd:PRK06187 310 VQGYGMTETSPVVSVLPPEDQ---LPGQWTKrrsaGRPLPGVEARIVDDDGDELPpdGGEVGEIIVRGPWLMQGYWNRPE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 638 LTADKFIDhpferGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEK 716
Cdd:PRK06187 387 ATAETIDG-----G--WLHTGDVGYIDEDGYLYITDRIKDVIISGGENIYPRELEDALYGHPAVAEVAVIGVPDEkWGER 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 717 YLcAYVVTEKDIPI--PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPI 773
Cdd:PRK06187 460 PV-AVVVLKPGATLdaKELRAFLRGRLAKFKLPKRIAFVDELPRTSVGKILKRVLREQY 517
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
287-766 |
3.68e-50 |
|
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, including Mycobacterium tuberculosis acid-induced operon MymA encoding the fatty acyl-CoA synthetase FadD13 which is essential for virulence and intracellular growth of the pathogen. The fatty acyl-CoA synthetase activates lipids before entering into the metabolic pathways and is also involved in transmembrane lipid transport. However, unlike soluble fatty acyl-CoA synthetases, but like the mammalian integral-membrane very-long-chain acyl-CoA synthetases, FadD13 accepts lipid substrates up to the maximum length of C26, and this is facilitated by an extensive hydrophobic tunnel from the active site to a positively charged patch. Also included is feruloyl-CoA synthetase (Fcs) in Rhodococcus strains where it is involved in biotechnological vanillin production from eugenol and ferulic acid via a non-beta-oxidative pathway.
Pssm-ID: 341286 [Multi-domain] Cd Length: 435 Bit Score: 185.12 E-value: 3.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 287 QNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEY 366
Cdd:cd17631 7 RHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 367 MLTDSGcSHVLtyqnsiikgvafqgsvinlmdipfeeeqVEDLQITMepqnlayviYTSGSTGQPKGVMIEHRSLTnflc 446
Cdd:cd17631 87 ILADSG-AKVL----------------------------FDDLALLM---------YTSGTTGRPKGAMLTHRNLL---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 447 AMYEDFSQDIGIT-DNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDY 525
Cdd:cd17631 125 WNAVNALAALDLGpDDVLLVVAPLFHIGGLGVFTLPTLLRGGTVVILRKFDPETVLDLIERHRVTSFFLVPTMIQALLQH 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 526 FVRANQKIS-LNKLFVGVEPIKTELLAKYDhlfRGNLQILNLYGPTEAT--VCCTSYQYERDKeittqnvpIGS---PLL 599
Cdd:cd17631 205 PRFATTDLSsLRAVIYGGAPMPERLLRALQ---ARGVKFVQGYGMTETSpgVTFLSPEDHRRK--------LGSagrPVF 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 600 NTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQV 679
Cdd:cd17631 274 FVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLYIVDRKKDMI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 680 KIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTEKDIP--IPEVRAYLATKLPYYMIPQQIISIQNI 756
Cdd:cd17631 347 ISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwGEA-VVAVVVPRPGAEldEDELIAHCRERLARYKIPKSVEFVDAL 425
|
490
....*....|
gi 446807313 757 PLTQNGKIDR 766
Cdd:cd17631 426 PRNATGKILK 435
|
|
| FACL_FadD13-like |
cd17631 |
fatty acyl-CoA synthetase, including FadD13; This family contains fatty acyl-CoA synthetases, ... |
1330-1809 |
5.80e-49 |
|
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: 181.65 E-value: 5.80e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1330 RNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEY 1409
Cdd:cd17631 7 RHPDRTALVFGGRSLTYAELDERVNRLAHALRALGVAKGDRVAVLSKNSPEFLELLFAAARLGAVFVPLNFRLTPPEVAY 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1410 MLTDSGcSHVLVHQnsiikgiefqgnvidlmdmsfeeepgedmhmmiephnLAYVIYTSGSTGQPKGVMIEHRSLTnflc 1489
Cdd:cd17631 87 ILADSG-AKVLFDD-------------------------------------LALLMYTSGTTGRPKGAMLTHRNLL---- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1490 AMYedfsqdigitdnvlFSSSISFDVTIFEIFV---PLIYGARM------TIYQG------EKFDVTKLVQVILEEQVTL 1554
Cdd:cd17631 125 WNA--------------VNALAALDLGPDDVLLvvaPLFHIGGLgvftlpTLLRGgtvvilRKFDPETVLDLIERHRVTS 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1555 SYIPPTLLNEIYDYFVRDNQKIV-LNKLLVGVEPIKTELLAKYDhlfRGNLQILNGYGPTEATVCCTSYRYEsnkEITTQ 1633
Cdd:cd17631 191 FFLVPTMIQALLQHPRFATTDLSsLRAVIYGGAPMPERLLRALQ---ARGVKFVQGYGMTETSPGVTFLSPE---DHRRK 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1634 NVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIE 1713
Cdd:cd17631 265 LGSAGRPVFFVEVRIVDPDGREVPPGEVGEIVVRGPHVMAGYWNRPEATAAAFRDGWF-------HTGDLGRLDEDGYLY 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1714 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVTEKDIP--IPEVRAYLATKLPHYMIP 1790
Cdd:cd17631 338 IVDRKKDMIISGGENVYPAEVEDVLYEHPAVAEVAVIGVPDEKwGEA-VVAVVVPRPGAEldEDELIAHCRERLARYKIP 416
|
490
....*....|....*....
gi 446807313 1791 QQLIPIHNIPLTQNGKIDR 1809
Cdd:cd17631 417 KSVEFVDALPRNATGKILK 435
|
|
| MACS_like_3 |
cd05971 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1345-1812 |
7.75e-49 |
|
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: 181.48 E-value: 7.75e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVlvhqn 1424
Cdd:cd05971 8 TFKELKTASNRFANVLKEIGLEKGDRVGVFLSQGPECAIAHIAILRSGAIAVPLFALFGPEALEYRLSNSGASAL----- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 siikgiefqgnVIDLMDmsfeeepgedmhmmiephNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMY---EDFSQDigi 1501
Cdd:cd05971 83 -----------VTDGSD------------------DPALIIYTSGTTGPPKGALHAHRVLLGHLPGVQfpfNLFPRD--- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1502 tDNVLFSSS----ISfdvTIFEIFVP-LIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEI-YDYFVRDNQK 1575
Cdd:cd05971 131 -GDLYWTPAdwawIG---GLLDVLLPsLYFGVPVLAHRMTKFDPKAALDLMSRYGVTTAFLPPTALKMMrQQGEQLKHAQ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1576 IVLNKLLVGVEPIKTELLA-KYDHLfrgNLQILNGYGPTEATVCCTSyryeSNKEITTQNVPIGSPLLNTKIYILDSFHR 1654
Cdd:cd05971 207 VKLRAIATGGESLGEELLGwAREQF---GVEVNEFYGQTECNLVIGN----CSALFPIKPGSMGKPIPGHRVAIVDDNGT 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1655 IQPIGVPGEICI---SGIGLArGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIEL 1731
Cdd:cd05971 280 PLPPGEVGEIAVelpDPVAFL-GYWNNPSATEKKMAG-------DWLLTGDLGRKDSDGYFWYVGRDDDVITSSGYRIGP 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1732 GEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-----TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGK 1806
Cdd:cd05971 352 AEIEECLLKHPAVLMAAVVGIPDPIRGEIVKAFVVlnpgeTPSDALAREIQELVKTRLAAHEYPREIEFVNELPRTATGK 431
|
....*.
gi 446807313 1807 IDRSKL 1812
Cdd:cd05971 432 IRRREL 437
|
|
| Firefly_Luc_like |
cd05911 |
Firefly luciferase of light emitting insects and 4-Coumarate-CoA Ligase (4CL); This family ... |
1340-1807 |
5.05e-47 |
|
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: 177.40 E-value: 5.05e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1340 NEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHV 1419
Cdd:cd05911 7 TGKELTYAQLRTLSRRLAAGLRKLGLKKGDVVGIISPNSTYYPPVFLGCLFAGGIFSAANPIYTADELAHQLKISKPKVI 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1420 LVHQNSI------IKGIEFQGNVI----------DLMDMSFEEEPGEDMHMMIEPH----NLAYVIYTSGSTGQPKGVMI 1479
Cdd:cd05911 87 FTDPDGLekvkeaAKELGPKDKIIvlddkpdgvlSIEDLLSPTLGEEDEDLPPPLKdgkdDTAAILYSSGTTGLPKGVCL 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1480 EHRSLTnflcamyedfsQDIGITDNVLFSSSISFDVTIfeIFVPL--IYGARMTI---YQGE------KFDVTKLVQVIL 1548
Cdd:cd05911 167 SHRNLI-----------ANLSQVQTFLYGNDGSNDVIL--GFLPLyhIYGLFTTLaslLNGAtviimpKFDSELFLDLIE 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1549 EEQVTLSYIPPTLLNEIYDYFVRDNQKI-VLNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEATVCCTSYRYESN 1627
Cdd:cd05911 234 KYKITFLYLVPPIAAALAKSPLLDKYDLsSLRVILSGGAPLSKELQELLAKRF-PNATIKQGYGMTETGGILTVNPDGDD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1628 KEITTqnvpiGSPLLNTKIYILDSFHR-IQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARW 1706
Cdd:cd05911 313 KPGSV-----GRLLPNVEAKIVDDDGKdSLGPNEPGEICVRGPQVMKGYYNNPEATKETFDEDGW------LHTGDIGYF 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1707 LPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKYLcAYVV-------TEKdipipEVRA 1778
Cdd:cd05911 382 DEDGYLYIVDRKKELIKYKGFQVAPAELEAVLLEHPGVADAAVIGIPDEvSGELPR-AYVVrkpgeklTEK-----EVKD 455
|
490 500 510
....*....|....*....|....*....|...
gi 446807313 1779 YLATKLPHYmipQQL----IPIHNIPLTQNGKI 1807
Cdd:cd05911 456 YVAKKVASY---KQLrggvVFVDEIPKSASGKI 485
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
1332-1815 |
9.40e-47 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 176.31 E-value: 9.40e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHQNSIIK-GIEFQGNVIDLMDMSFEE-EPGEDMHMmiepHNLAYVIYTSGSTGQPKGVMiehRSLTN-FL 1488
Cdd:PRK03640 96 DDAEVKCLITDDDFEAKlIPGISVKFAELMNGPKEEaEIQEEFDL----DEVATIMYTSGTTGKPKGVI---QTYGNhWW 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1489 CAMYEdfSQDIGITDNvlfsssisfD-----VTIFEI------FVPLIYGarMTIYQGEKFDVTKLVQVILEEQVTLSYI 1557
Cdd:PRK03640 169 SAVGS--ALNLGLTED---------DcwlaaVPIFHIsglsilMRSVIYG--MRVVLVEKFDAEKINKLLQTGGVTIISV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1558 PPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHlfrGNLQILNGYGPTE--ATVCCTSYRYESNKeittqnv 1635
Cdd:PRK03640 236 VSTMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKE---KGIPVYQSYGMTEtaSQIVTLSPEDALTK------- 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 pIGS---PLLNTKIYILDSFHRIQPiGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNI 1712
Cdd:PRK03640 306 -LGSagkPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFL 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1713 EYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQ 1792
Cdd:PRK03640 377 YVLDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKR 456
|
490 500
....*....|....*....|...
gi 446807313 1793 LIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK03640 457 FYFVEELPRNASGKLLRHELKQL 479
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
292-769 |
3.37e-45 |
|
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: 170.93 E-value: 3.37e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 292 IAIVCNGKEITYKQLNIKANQLARRLLDQG-VKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTD 370
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 371 SGCSHVLtyqnsiikgvafqgsvinlmdipfeeeqvedlqitmepqNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYE 450
Cdd:cd05941 83 SEPSLVL---------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 451 --DFSQDigitDNVLFSSSIsFDV--TIFEIFVPLVCGARMtIYQGeKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDY- 525
Cdd:cd05941 124 awRWTED----DVLLHVLPL-HHVhgLVNALLCPLFAGASV-EFLP-KFDPKEVAISRLMPSITVFMGVPTIYTRLLQYy 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 526 --------FVRANQKISLnKLFV-GVEPIKTELLAKYDHLFrGNlQILNLYGPTEaTVCCTSYQYERDKEITTqnvpIGS 596
Cdd:cd05941 197 eahftdpqFARAAAAERL-RLMVsGSAALPVPTLEEWEAIT-GH-TLLERYGMTE-IGMALSNPLDGERRPGT----VGM 268
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 597 PLLNTKIYILD-SFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGR- 674
Cdd:cd05941 269 PLPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF------TDDGWFKTGDLGVVDEDGYYWILGRs 342
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 675 -VDhQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTEKDIP---IPEVRAYLATKLPYYMIPQQ 749
Cdd:cd05941 343 sVD-IIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDwGER-VVAVVVLRAGAAalsLEELKEWAKQRLAPYKRPRR 420
|
490 500
....*....|....*....|
gi 446807313 750 IISIQNIPLTQNGKIDRKKL 769
Cdd:cd05941 421 LILVDELPRNAMGKVNKKEL 440
|
|
| PRK03640 |
PRK03640 |
o-succinylbenzoate--CoA ligase; |
289-776 |
4.46e-45 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 235146 [Multi-domain] Cd Length: 483 Bit Score: 171.68 E-value: 4.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:PRK03640 16 PDRTAIEFEEKKVTFMELHEAVVSVAGKLAALGVKKGDRVALLMKNGMEMILVIHALQQLGAVAVLLNTRLSREELLWQL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGCSHVLTYQNSIIKgvAFQGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMiehRSLTN-FLCA 447
Cdd:PRK03640 96 DDAEVKCLITDDDFEAK--LIPGISVKFAELMNGPKEEAEIQEEFDLDEVATIMYTSGTTGKPKGVI---QTYGNhWWSA 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 448 MYEdfSQDIGITDNvlfsssisfD-----VTIFEI------FVPLVCGarMTIYQGEKFDVPKLVQVILEEQVTLAYIPP 516
Cdd:PRK03640 171 VGS--ALNLGLTED---------DcwlaaVPIFHIsglsilMRSVIYG--MRVVLVEKFDAEKINKLLQTGGVTIISVVS 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 517 TLLNEIYDYFVRANQKISLNKLFVGVEPIKTELLAKYDHlfrGNLQILNLYGPTE--ATVCCTSYQYERDKeittqnvpI 594
Cdd:PRK03640 238 TMLQRLLERLGEGTYPSSFRCMLLGGGPAPKPLLEQCKE---KGIPVYQSYGMTEtaSQIVTLSPEDALTK--------L 306
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 595 GS---PLLNTKIYILDSFHRLQPiGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEY 671
Cdd:PRK03640 307 GSagkPLFPCELKIEKDGVVVPP-FEEGEIVVKGPNVTKGYLNREDATRETFQDGWF-------KTGDIGYLDEEGFLYV 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 672 LGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQII 751
Cdd:PRK03640 379 LDRRSDLIISGGENIYPAEIEEVLLSHPGVAEAGVVGVPDDKWGQVPVAFVVKSGEVTEEELRHFCEEKLAKYKVPKRFY 458
|
490 500
....*....|....*....|....*
gi 446807313 752 SIQNIPLTQNGKIDRKKLPQPINNL 776
Cdd:PRK03640 459 FVEELPRNASGKLLRHELKQLVEEM 483
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
276-769 |
1.00e-44 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 171.24 E-value: 1.00e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 276 TAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI 355
Cdd:PRK07656 6 TLPELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPL 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 356 DTELPKQRVEYMLTDSGCSHVLTYQnsiikgvAFQGSVINLMD--------IPFEEEQVEDLQITM-------------- 413
Cdd:PRK07656 86 NTRYTADEAAYILARGDAKALFVLG-------LFLGVDYSATTrlpalehvVICETEEDDPHTEKMktftdflaagdpae 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 414 -----EPQNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGIT--DNVL----FsssisfdvtiFEIF---- 478
Cdd:PRK07656 159 rapevDPDDVADILFTSGTTGRPKGAMLTHRQLL----SNAADWAEYLGLTegDRYLaanpF----------FHVFgyka 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 479 ---VPLVCGArmTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFV-GVEPIKTELLakyd 554
Cdd:PRK07656 225 gvnAPLMRGA--TILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAEDLSSLRLAVtGAASMPVALL---- 298
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 555 HLFRGNLQ---ILNLYGPTEA--TVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLA 629
Cdd:PRK07656 299 ERFESELGvdiVLTGYGLSEAsgVTTFNRLDDDRKTVAGT----IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVM 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 630 RGYINRKELTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQR 709
Cdd:PRK07656 375 KGYYDDPEATAAAI------DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGV 448
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446807313 710 EDES-GEkYLCAYVVTEKDIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK07656 449 PDERlGE-VGKAYVVLKPGAELTEeeLIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
1345-1812 |
5.12e-44 |
|
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: 167.24 E-value: 5.12e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQN 1424
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 SIIKGIEfqgnVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqdIGITDN 1504
Cdd:TIGR01923 81 LEEKDFQ----ADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLG--FTEDDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 VLFSSSIsFDVTIFEI-FVPLIYGarMTIYQGEKFdvTKLVQVILEEQVTLSYIPPTLLNEIYDyfvRDNQKIVLNKLLV 1583
Cdd:TIGR01923 155 WLLSLPL-YHISGLSIlFRWLIEG--ATLRIVDKF--NQLLEMIANERVTHISLVPTQLNRLLD---EGGHNENLRKILL 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1584 GVEPIKTELLAKYDHLfrgNLQILNGYGPTE-ATVCCTSyryesNKEITTQNVPIGSPLLNTKIYIldsfhRIQPIGVPG 1662
Cdd:TIGR01923 227 GGSAIPAPLIEEAQQY---GLPIYLSYGMTEtCSQVTTA-----TPEMLHARPDVGRPLAGREIKI-----KVDNKEGHG 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1663 EICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYE 1742
Cdd:TIGR01923 294 EIMVKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHP 366
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1743 TIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:TIGR01923 367 GIQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| MCS |
cd05941 |
Malonyl-CoA synthetase (MCS); MCS catalyzes the formation of malonyl-CoA in a two-step ... |
1335-1812 |
2.19e-43 |
|
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: 165.54 E-value: 2.19e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1335 IAVVCNEKGITYNELNIKANQLARRLLDQG-VKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTD 1413
Cdd:cd05941 3 IAIVDDGDSITYADLVARAARLANRLLALGkDLRGDRVAFLAPPSAEYVVAQLAIWRAGGVAVPLNPSYPLAELEYVITD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1414 SGCSHVLvhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiephNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYE 1493
Cdd:cd05941 83 SEPSLVL---------------------------------------DPALILYTSGTTGRPKGVVLTHANLAANVRALVD 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1494 --DFSQDigitDNVLFSSSIsFDV--TIFEIFVPLIYGARMtIYQGeKFDVTKLVQVILEEQVTLSYIPPTL---LNEIY 1566
Cdd:cd05941 124 awRWTED----DVLLHVLPL-HHVhgLVNALLCPLFAGASV-EFLP-KFDPKEVAISRLMPSITVFMGVPTIytrLLQYY 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1567 DYFVRDNQKIVLN-----KLLV-GVEPIKTELLAKYDHLFrGNlQILNGYGPTEaTVCCTSYRYESNKEITTqnvpIGSP 1640
Cdd:cd05941 197 EAHFTDPQFARAAaaerlRLMVsGSAALPVPTLEEWEAIT-GH-TLLERYGMTE-IGMALSNPLDGERRPGT----VGMP 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1641 LLNTKIYILD-SFHRIQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGR-- 1717
Cdd:cd05941 270 LPGVQARIVDeETGEPLPRGEVGEIQVRGPSVFKEYWNKPEATKEEF------TDDGWFKTGDLGVVDEDGYYWILGRss 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1718 VDhQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVTEKDIP---IPEVRAYLATKLPHYMIPQQL 1793
Cdd:cd05941 344 VD-IIKSGGYKVSALEIERVLLAHPGVSECAVIGVPDPDwGER-VVAVVVLRAGAAalsLEELKEWAKQRLAPYKRPRRL 421
|
490
....*....|....*....
gi 446807313 1794 IPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05941 422 ILVDELPRNAMGKVNKKEL 440
|
|
| PRK07656 |
PRK07656 |
long-chain-fatty-acid--CoA ligase; Validated |
1322-1812 |
1.44e-42 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236072 [Multi-domain] Cd Length: 513 Bit Score: 164.69 E-value: 1.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1322 KMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTD 1401
Cdd:PRK07656 9 ELLARAARRFGDKEAYVFGDQRLTYAELNARVRRAAAALAALGIGKGDRVAIWAPNSPHWVIAALGALKAGAVVVPLNTR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1402 LPKQRVEYMLTDSGCSHVLVHQN------SIIKGIEFQGNVIDLMDMSfEEEPGEDMHMM---------------IEPHN 1460
Cdd:PRK07656 89 YTADEAAYILARGDAKALFVLGLflgvdySATTRLPALEHVVICETEE-DDPHTEKMKTFtdflaagdpaerapeVDPDD 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGIT--DNVL----FsssisfdvtiFEIF-------VPLIYG 1527
Cdd:PRK07656 168 VADILFTSGTTGRPKGAMLTHRQLL----SNAADWAEYLGLTegDRYLaanpF----------FHVFgykagvnAPLMRG 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1528 ArmTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKivLNKLLVGVE---PIKTELLakydHLFRGNL 1604
Cdd:PRK07656 234 A--TILPLPVFDPDEVFRLIETERITVLPGPPTMYNSLLQHPDRSAED--LSSLRLAVTgaaSMPVALL----ERFESEL 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1605 Q---ILNGYGPTEAT-VCCTSYRYESNKEITTQnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKE 1680
Cdd:PRK07656 306 GvdiVLTGYGLSEASgVTTFNRLDDDRKTVAGT---IGTAIAGVENKIVNELGEEVPVGEVGELLVRGPNVMKGYYDDPE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1681 LTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQED----EA 1756
Cdd:PRK07656 383 ATAAAI------DADGWLHTGDLGRLDEEGYLYIVDRKKDMFIVGGFNVYPAEVEEVLYEHPAVAEAAVIGVPDerlgEV 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1757 GekylCAYVVTEKDIPIPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK07656 457 G----KAYVVLKPGAELTEeeLIAYCREHLAKYKVPRSIEFLDELPKNATGKVLKRAL 510
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
1345-1812 |
2.08e-42 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 162.12 E-value: 2.08e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcshvlvhqn 1424
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAG--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 siIKGIefqgnVIDLMDMSFeeepgedmhmmiephnlayVIYTSGSTGQPKGVMIEHRSLTNFLcaMYEDFSQDIGITDN 1504
Cdd:cd05972 73 --AKAI-----VTDAEDPAL-------------------IYFTSGTTGLPKGVLHTHSYPLGHI--PTAAYWLGLRPDDI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 VLFSSSISFDVTI-FEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPT----LLNEIYDYFVRDNqkivLN 1579
Cdd:cd05972 125 HWNIADPGWAKGAwSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPTayrmLIKQDLSSYKFSH----LR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1580 KLLVGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATVCCTSYRYESNKeittqnvP--IGSPLLNTKIYILDSFHRIQP 1657
Cdd:cd05972 201 LVVSAGEPLNPEVIEWWRAAT--GLPIRDGYGQTETGLTVGNFPDMPVK-------PgsMGRPTPGYDVAIIDDDGRELP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1658 IGVPGEICI--SGIGLARGYINRKELTADKFidhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE 1735
Cdd:cd05972 272 PGEEGDIAIklPPPGLFLGYVGDPEKTEASI-------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1736 ASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP-----EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRS 1810
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSeelaeELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRV 424
|
..
gi 446807313 1811 KL 1812
Cdd:cd05972 425 EL 426
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
1344-1812 |
2.44e-42 |
|
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: 161.36 E-value: 2.44e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcshvlvhq 1423
Cdd:cd05912 2 YTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTPNELAFQLKDSD-------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nsiikgiefqgnvIDLMDMsfeeepgedmhmmiephnlAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDfsqdIGITD 1503
Cdd:cd05912 74 -------------VKLDDI-------------------ATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALN----LGLTE 117
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1504 NVLFSSSisfdVTIFEI------FVPLIYGarMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKiV 1577
Cdd:cd05912 118 DDNWLCA----LPLFHIsglsilMRSVIYG--MTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPN-N 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1578 LNKLLVGVEPIKTELLAKYDHLfrgNLQILNGYGPTEAT--VCCTSYRYESNKeittqnvpIGS---PLLNTKIYILdsf 1652
Cdd:cd05912 191 LRCILLGGGPAPKPLLEQCKEK---GIPVYQSYGMTETCsqIVTLSPEDALNK--------IGSagkPLFPVELKIE--- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1653 HRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 1732
Cdd:cd05912 257 DDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYPA 329
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1733 EIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05912 330 EIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHEL 409
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
896-1285 |
3.07e-42 |
|
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: 161.46 E-value: 3.07e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 896 YNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFqILDG--ELVQKIEPNVDFNIEYV---HVNEKDA---DYLIHEF 967
Cdd:cd19536 24 YLHNYTYTVGRRLNLDLLLEALQVLIDRHDILRTSF-IEDGlgQPVQVVHRQAQVPVTELdltPLEEQLDplrAYKEETK 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 968 ISPFDLSKPPLLRVLLLRIAEERH-ILVVDMHHIISDGLSMGILIKEFVELYKG------NELPKlRVQYKDYVMWqngp 1040
Cdd:cd19536 103 IRRFDLGRAPLVRAALVRKDERERfLLVISDHHSILDGWSLYLLVKEILAVYNQlleykpLSLPP-AQPYRDFVAH---- 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1041 yykNLISEQK----NYWLTTLKG-ELPVLNFPTDfqrpTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYN 1115
Cdd:cd19536 178 ---ERASIQQaaseRYWREYLAGaTLATLPALSE----AVGGGPEQDSELLVSVPLPVRSRSLAKRSGIPLSTLLLAAWA 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1116 ILLSRYTGQEDIIVGSPIAGRSH--SDTNHMIGMFINTLVMRNYLeNDDEFIEFLSRLKLNTLEAYENQDYPFEellegl 1193
Cdd:cd19536 251 LVLSRHSGSDDVVFGTVVHGRSEetTGAERLLGLFLNTLPLRVTL-SEETVEDLLKRAQEQELESLSHEQVPLA------ 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1194 DLHRDTSRNPLFDTMFVFQNMDM---NPISIGELEFTPYP-FKQSVSKFDLSLVATEIDNNIHLKVEYSIKLFKAETIER 1269
Cdd:cd19536 324 DIQRCSEGEPLFDSIVNFRHFDLdfgLPEWGSDEGMRRGLlFSEFKSNYDVNLSVLPKQDRLELKLAYNSQVLDEEQAQR 403
|
410
....*....|....*.
gi 446807313 1270 LMVHFTNIVEEVTNNP 1285
Cdd:cd19536 404 LAAYYKSAIAELATAP 419
|
|
| menE |
TIGR01923 |
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, ... |
302-769 |
5.86e-42 |
|
O-succinylbenzoate-CoA ligase; This model represents an enzyme, O-succinylbenzoate-CoA ligase, which is involved in the fourth step of the menaquinone biosynthesis pathway. O-succinylbenzoate-CoA ligase, together with menB - naphtoate synthase, take 2-succinylbenzoate and convert it into 1,4-di-hydroxy-2- naphtoate. [Biosynthesis of cofactors, prosthetic groups, and carriers, Menaquinone and ubiquinone]
Pssm-ID: 162605 [Multi-domain] Cd Length: 436 Bit Score: 161.08 E-value: 5.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 302 TYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQN 381
Cdd:TIGR01923 1 TWQDLDCEAAHLAKALKAQGIRSGSRVALVGQNSIEMVLLLHACLLLGAEIAMLNTRLTENERTNQLEDLDVQLLLTDSL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 382 SIIKGVafqgSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqdIGITDN 461
Cdd:TIGR01923 81 LEEKDF----QADSLDRIEAAGRYETSLSASFNMDQIATLMFTSGTTGKPKAVPHTFRNHYASAVGSKENLG--FTEDDN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 462 VLFSSSIsFDVTIFEIFVPLVCGArMTIYQGEKFDvpKLVQVILEEQVTLAYIPPTLLNEIYDyfvRANQKISLNKLFVG 541
Cdd:TIGR01923 155 WLLSLPL-YHISGLSILFRWLIEG-ATLRIVDKFN--QLLEMIANERVTHISLVPTQLNRLLD---EGGHNENLRKILLG 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 542 VEPIKTELLAKYDHLfrgNLQILNLYGPTE-ATVCCTSyqyerDKEITTQNVPIGSPLLNTKIYIldsfhRLQPIGVPGE 620
Cdd:TIGR01923 228 GSAIPAPLIEEAQQY---GLPIYLSYGMTEtCSQVTTA-----TPEMLHARPDVGRPLAGREIKI-----KVDNKEGHGE 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 621 ICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYET 700
Cdd:TIGR01923 295 IMVKGANLMKGYLYQGELTPAFEQQGWF-------NTGDIGELDGEGFLYVLGRRDDLIISGGENIYPEEIETVLYQHPG 367
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 701 IKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:TIGR01923 368 IQEAVVVPKPDAEWGQVPVAYIVSESDISQAKLIAYLTEKLAKYKVPIAFEKLDELPYNASGKILRNQL 436
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
1332-1812 |
1.74e-41 |
|
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: 161.38 E-value: 1.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHQ------NSIIKGIEFQGNVIDLMD--------MSFEEEPGEDMHMM----IEPHNLAYVIYTSGSTGQ 1473
Cdd:cd05959 98 EDSRARVVVVSGelapvlAAALTKSEHTLVVLIVSGgagpeagaLLLAELVAAEAEQLkpaaTHADDPAFWLYSSGSTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1474 PKGVMIEHRSLTnflcAMYEDFSQDI-GIT-DNVLFSSSISFdvtiF------EIFVPLIYGArMTIYQGEKFDVTKLVQ 1545
Cdd:cd05959 178 PKGVVHLHADIY----WTAELYARNVlGIReDDVCFSAAKLF----FayglgnSLTFPLSVGA-TTVLMPERPTPAAVFK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1546 VILEEQVTLSYIPPTLLNEIYDyfVRDNQKIVLNKLLVGV---EPIKTELLAKYDHLFrgNLQILNGYGPTEATVCCTSY 1622
Cdd:cd05959 249 RIRRYRPTVFFGVPTLYAAMLA--APNLPSRDLSSLRLCVsagEALPAEVGERWKARF--GLDILDGIGSTEMLHIFLSN 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1623 RYESNKEITTqnvpiGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEkLYKTGD 1702
Cdd:cd05959 325 RPGRVRYGTT-----GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF------QGE-WTRTGD 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1703 IARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-----TEKDIPIPEVR 1777
Cdd:cd05959 393 KYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpgyEDSEALEEELK 472
|
490 500 510
....*....|....*....|....*....|....*
gi 446807313 1778 AYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05959 473 EFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
280-769 |
7.35e-41 |
|
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: 159.95 E-value: 7.35e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 280 LFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTEL 359
Cdd:TIGR03098 5 LLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPINPLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 360 PKQRVEYMLTDSGC-------------SHVLTYQNSIIKGVAFQGSVINLMDIPFEEEQV-EDLQITMEPQ--------N 417
Cdd:TIGR03098 85 KAEQVAHILADCNVrllvtsserldllHPALPGCHDLRTLIIVGDPAHASEGHPGEEPASwPKLLALGDADpphpvidsD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 418 LAYVIYTSGSTGQPKGVMIEHRSLTN--FLCAMYEDFSQDigitDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQgekF 495
Cdd:TIGR03098 165 MAAILYTSGSTGRPKGVVLSHRNLVAgaQSVATYLENRPD----DRLLAVLPLSFDYGFNQLTTAFYVGATVVLHD---Y 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 496 DVPK-LVQVILEEQVT-LAYIPPtLLNEIYDYFVRANQKISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEAT 573
Cdd:TIGR03098 238 LLPRdVLKALEKHGITgLAAVPP-LWAQLAQLDWPESAAPSLRYLTNSGGAMPRATLSRLRSFL-PNARLFLMYGLTEAF 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 574 VCCTSYQYERDKEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHP-FERGE 652
Cdd:TIGR03098 316 RSTYLPPEEVDRRPDS----IGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTAERFRPLPpFPGEL 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 653 KLYKT----GDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-QREDESGEKYLCAYVVTEKD 727
Cdd:TIGR03098 392 HLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFgVPDPTLGQAIVLVVTPPGGE 471
|
490 500 510 520
....*....|....*....|....*....|....*....|...
gi 446807313 728 IPIPEV-RAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:TIGR03098 472 ELDRAAlLAECRARLPNYMVPALIHVRQALPRNANGKIDRKAL 514
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
298-770 |
1.16e-40 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 157.07 E-value: 1.16e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 298 GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVL 377
Cdd:cd05934 1 GRRWTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 378 TyqnsiikgvafqgsvinlmdipfeeeqvedlqitmepqNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDF---SQ 454
Cdd:cd05934 81 V--------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFglgED 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 455 DIGITDNVLFSSsisfDVTIFEIFVPLVCGARMTIyqGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKIs 534
Cdd:cd05934 123 DVYLTVLPLFHI----NAQAVSVLAALSVGATLVL--LPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRA- 195
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 535 lNKL-FVGVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTsyqyeRDKEITTQNVPIGSPLLNTKIYILDSFHRLQ 613
Cdd:cd05934 196 -HRLrAAYGAPNPPELHEEFEERF--GVRLLEGYGMTETIVGVI-----GPRDEPRRPGSIGRPAPGYEVRIVDDDGQEL 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 614 PIGVPGEICI---SGIGLARGYINRKELTADKfidhpFERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGE 690
Cdd:cd05934 268 PAGEPGELVIrglRGWGFFKGYYNMPEATAEA-----MRNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAE 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 691 IEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPI--PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKK 768
Cdd:cd05934 341 VERAILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLdpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQ 420
|
..
gi 446807313 769 LP 770
Cdd:cd05934 421 LR 422
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
1345-1812 |
2.70e-40 |
|
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: 156.39 E-value: 2.70e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcSHVLVHQN 1424
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAK-AKVFVVPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 siikgiEFQGnvidlmdMSFEEEPGEdmhmmiephnLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqdIGITDN 1504
Cdd:cd05903 82 ------RFRQ-------FDPAAMPDA----------VALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG--LGPGDV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 VLFSSSIS-FDVTIFEIFVPLIYGARmTIYQgEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIV-LNKLL 1582
Cdd:cd05903 137 FLVASPMAhQTGFVYGFTLPLLLGAP-VVLQ-DIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSrLRTFV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1583 VGVEPIKTELLAKYDHLfrGNLQILNGYGPTE---ATVCCTSyrYESNKEITTQnvpiGSPLLNTKIYILDSFHRIQPIG 1659
Cdd:cd05903 215 CGGATVPRSLARRAAEL--LGAKVCSAYGSTEcpgAVTSITP--APEDRRLYTD----GRPLPGVEIKVVDDTGATLAPG 286
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1660 VPGEICISGIGLARGYINRKELTADKFidhpferGEKLYKTGDIARWLPDGNIEYLGRVDhQVKIR-GYRIELGEIEASL 1738
Cdd:cd05903 287 VEGELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSK-DIIIRgGENIPVLEVEDLL 358
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1739 LKYETIKTAVVIDQEDE-AGEKyLCAYVVTEK--DIPIPEVRAYL-ATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05903 359 LGHPGVIEAAVVALPDErLGER-ACAVVVTKSgaLLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFRL 435
|
|
| OSB_CoA_lg |
cd05912 |
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA ... |
300-771 |
4.92e-40 |
|
O-succinylbenzoate-CoA ligase (also known as O-succinylbenzoate-CoA synthase, OSB-CoA synthetase, or MenE); O-succinylbenzoic acid-CoA synthase catalyzes the coenzyme A (CoA)- and ATP-dependent conversion of o-succinylbenzoic acid to o-succinylbenzoyl-CoA. The reaction is the fourth step of the biosynthesis pathway of menaquinone (vitamin K2). In certain bacteria, menaquinone is used during fumarate reduction in anaerobic respiration. In cyanobacteria, the product of the menaquinone pathway is phylloquinone (2-methyl-3-phytyl-1,4-naphthoquinone), a molecule used exclusively as an electron transfer cofactor in Photosystem 1. In green sulfur bacteria and heliobacteria, menaquinones are used as loosely bound secondary electron acceptors in the photosynthetic reaction center.
Pssm-ID: 341238 [Multi-domain] Cd Length: 411 Bit Score: 154.81 E-value: 4.92e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 300 EITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKqrveymltdsgcsHVLTY 379
Cdd:cd05912 1 SYTFAELFEEVSRLAEHLAALGVRKGDRVALLSKNSIEMILLIHALWLLGAEAVLLNTRLTP-------------NELAF 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 380 QnsiikgvafqgsvinlmdipfeeeqVEDLQITMEpqNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDfsqdIGIT 459
Cdd:cd05912 68 Q-------------------------LKDSDVKLD--DIATIMYTSGTTGKPKGVQQTFGNHWWSAIGSALN----LGLT 116
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 460 DNVLFSSSisfdVTIFEI------FVPLVCGarMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKi 533
Cdd:cd05912 117 EDDNWLCA----LPLFHIsglsilMRSVIYG--MTVYLVDKFDAEQVLHLINSGKVTIISVVPTMLQRLLEILGEGYPN- 189
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 534 SLNKLFVGVEPIKTELLAKYDHLfrgNLQILNLYGPTEAT--VCCTSYQYERDKeittqnvpIGS---PLLNTKIYILds 608
Cdd:cd05912 190 NLRCILLGGGPAPKPLLEQCKEK---GIPVYQSYGMTETCsqIVTLSPEDALNK--------IGSagkPLFPVELKIE-- 256
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 609 fHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIEL 688
Cdd:cd05912 257 -DDGQPPYEVGEILLKGPNVTKGYLNRPDATEESFENGWF-------KTGDIGYLDEEGFLYVLDRRSDLIISGGENIYP 328
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 689 GEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKK 768
Cdd:cd05912 329 AEIEEVLLSHPAIKEAGVVGIPDDKWGQVPVAFVVSERPISEEELIAYCSEKLAKYKVPKKIYFVDELPRTASGKLLRHE 408
|
...
gi 446807313 769 LPQ 771
Cdd:cd05912 409 LKQ 411
|
|
| MACS_like |
cd05972 |
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of ... |
302-769 |
6.75e-40 |
|
Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes.
Pssm-ID: 341276 [Multi-domain] Cd Length: 428 Bit Score: 154.80 E-value: 6.75e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 302 TYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyqn 381
Cdd:cd05972 2 SFRELKRESAKAANVLAKLGLRKGDRVAVLLPRVPELWAVILAVIKLGAVYVPLTTLLGPKDIEYRLEAAGAKAIVT--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 382 siikgvafqgsvinlmdipfeeeqvedlqitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLcaMYEDFSQDIGITDN 461
Cdd:cd05972 79 --------------------------------DAEDPALIYFTSGTTGLPKGVLHTHSYPLGHI--PTAAYWLGLRPDDI 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 462 VLFSSSISFDVTI-FEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTllneIYDYFVRAN---QKISLNK 537
Cdd:cd05972 125 HWNIADPGWAKGAwSSFFGPWLLGATVFVYEGPRFDAERILELLERYGVTSFCGPPT----AYRMLIKQDlssYKFSHLR 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 538 LFVGV-EPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTSYqyeRDKEITtqnvP--IGSPLLNTKIYILDSFHRLQP 614
Cdd:cd05972 201 LVVSAgEPLNPEVIEWWRAAT--GLPIRDGYGQTETGLTVGNF---PDMPVK----PgsMGRPTPGYDVAIIDDDGRELP 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 615 IGVPGEICI--SGIGLARGYINRKELTADKFidhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE 692
Cdd:cd05972 272 PGEEGDIAIklPPPGLFLGYVGDPEKTEASI-------RGDYYLTGDRAYRDEDGYFWFVGRADDIIKSSGYRIGPFEVE 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 693 ASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP-----EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRK 767
Cdd:cd05972 345 SALLEHPAVAEAAVVGSPDPVRGEVVKAFVVLTSGYEPSeelaeELQGHVKKVLAPYKYPREIEFVEELPKTISGKIRRV 424
|
..
gi 446807313 768 KL 769
Cdd:cd05972 425 EL 426
|
|
| FACL_DitJ_like |
cd05934 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1344-1813 |
3.68e-39 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Members of this family include DitJ from Pseudomonas and similar proteins.
Pssm-ID: 341257 [Multi-domain] Cd Length: 422 Bit Score: 152.45 E-value: 3.68e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVhq 1423
Cdd:cd05934 4 WTYAELLRESARIAAALAALGIRPGDRVALMLDNCPEFLFAWFALAKLGAVLVPINTALRGDELAYIIDHSGAQLVVV-- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nsiikgiefqgnvidlmdmsfeeepgedmhmmiephNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDF---SQDIG 1500
Cdd:cd05934 82 ------------------------------------DPASILYTSGTTGPPKGVVITHANLTFAGYYSARRFglgEDDVY 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1501 ITDNVLFSSsisfDVTIFEIFVPLIYGARMTIyqGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIvlNK 1580
Cdd:cd05934 126 LTVLPLFHI----NAQAVSVLAALSVGATLVL--LPRFSASRFWSDVRRYGATVTNYLGAMLSYLLAQPPSPDDRA--HR 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1581 L-LVGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATVCCTSYRYESNKEITtqnvpIGSPLLNTKIYILDSFHRIQPIG 1659
Cdd:cd05934 198 LrAAYGAPNPPELHEEFEERF--GVRLLEGYGMTETIVGVIGPRDEPRRPGS-----IGRPAPGYEVRIVDDDGQELPAG 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1660 VPGEICI---SGIGLARGYINRKELTADKfidhpFERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEA 1736
Cdd:cd05934 271 EPGELVIrglRGWGFFKGYYNMPEATAEA-----MRNG--WFHTGDLGYRDADGFFYFVDRKKDMIRRRGENISSAEVER 343
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1737 SLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPI--PEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLP 1813
Cdd:cd05934 344 AILRHPAVREAAVVAVPDEVGEDEVKAVVVLRPGETLdpEELFAFCEGQLAYFKVPRYIRFVDDLPKTPTEKVAKAQLR 422
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
310-769 |
1.03e-38 |
|
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: 152.21 E-value: 1.03e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 310 ANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGA----YLPIDTELPKQRVEYMLTDSGcSHVLTYQNSIIK 385
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAG-GRIVLADAGAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 386 GVAFQGSVINLMDIPFEEEQVEDLQ-----ITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITD 460
Cdd:cd05922 82 RLRDALPASPDPGTVLDADGIRAARasapaHEVSHEDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYL--GITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 461 NVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVpKLVQVILEEQVT-LAYIPPTLlnEIYDYFVRANQKI-SLNKL 538
Cdd:cd05922 160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDD-AFWEDLREHGATgLAGVPSTY--AMLTRLGFDPAKLpSLRYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 539 FVGVEPIKTELLAKYDHLFRGNlQILNLYGPTEATVCCTSYQYERDKEITTQnvpIGSPLLNTKIYILDSFHRLQPIGVP 618
Cdd:cd05922 237 TQAGGRLPQETIARLRELLPGA-QVYVMYGQTEATRRMTYLPPERILEKPGS---IGLAIPGGEFEILDDDGTPTPPGEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 619 GEICISGIGLARGYINRKELTADKfidhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 698
Cdd:cd05922 313 GEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSI 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 699 ETIKTAVVIQREDESGEKylCAYVVTEKDIPIP-EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05922 387 GLIIEAAAVGLPDPLGEK--LALFVTAPDKIDPkDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
873-1285 |
1.23e-38 |
|
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: 150.53 E-value: 1.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 873 YLASTSQKrMFIVDQFEDGTntTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQ--ILDGELVQKIEPNVDFNI 950
Cdd:cd19542 2 YPCTPMQE-GMLLSQLRSPG--LYFNHFVFDLDSSVDVERLRNAWRQLVQRHDILRTVFVesSAEGTFLQVVLKSLDPPI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 951 EYVHVNEKDADYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGNELPKlRVQY 1030
Cdd:cd19542 79 EEVETDEDSLDALTRDLLDDPTLFGQPPHRLTLLETSSGEVYLVLRISHALYDGVSLPIILRDLAAAYNGQLLPP-APPF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1031 KDYVmwqngPY-YKNLISEQKNYWLTTLKGELPVLnFPT----DFQRPTIQSFKGNvcsfnlgtdlTFKVNKLATETGTT 1105
Cdd:cd19542 158 SDYI-----SYlQSQSQEESLQYWRKYLQGASPCA-FPSlspkRPAERSLSSTRRS----------LAKLEAFCASLGVT 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1106 PYMILLAIYNILLSRYTGQEDIIVGSPIAGR--SHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAYENQD 1183
Cdd:cd19542 222 LASLFQAAWALVLARYTGSRDVVFGYVVSGRdlPVPGIDDIVGPCINTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQH 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1184 YPFEELLEGLdlhRDTSRNPLFDTMFVFQNMDMNPISIGELEFTpypFKQSVSK----FDLSLVATEIDNNIHLKVEYSI 1259
Cdd:cd19542 302 LSLREIQRAL---GLWPSGTLFNTLVSYQNFEASPESELSGSSV---FELSAAEdpteYPVAVEVEPSGDSLKVSLAYST 375
|
410 420
....*....|....*....|....*.
gi 446807313 1260 KLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19542 376 SVLSEEQAEELLEQFDDILEALLANP 401
|
|
| BCL_4HBCL |
cd05959 |
Benzoate CoA ligase (BCL) and 4-Hydroxybenzoate-Coenzyme A Ligase (4-HBA-CoA ligase); Benzoate ... |
289-769 |
1.48e-38 |
|
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: 152.91 E-value: 1.48e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd05959 18 GDKTAFIDDAGSLTYAELEAEARRVAGALRALGVKREERVLLIMLDTVDFPTAFLGAIRAGIVPVPVNTLLTPDDYAYYL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGC-------------------SHVLTYQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITmEPQNLAYVIYTSGSTG 429
Cdd:cd05959 98 EDSRArvvvvsgelapvlaaaltkSEHTLVVLIVSGGAGPEAGALLLAELVAAEAEQLKPAAT-HADDPAFWLYSSGSTG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 430 QPKGVMIEHRSLTnflcAMYEDFSQDI-GIT-DNVLFSSSISFdvtiF------EIFVPLVCGARMTIYQGekFDVPKLV 501
Cdd:cd05959 177 RPKGVVHLHADIY----WTAELYARNVlGIReDDVCFSAAKLF----FayglgnSLTFPLSVGATTVLMPE--RPTPAAV 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 502 -QVILEEQVTLAYIPPTLlneiYDYFVRAN--QKISLNKLFVGV---EPIKTELLAKYDHLFrgNLQILNLYGPTEATVC 575
Cdd:cd05959 247 fKRIRRYRPTVFFGVPTL----YAAMLAAPnlPSRDLSSLRLCVsagEALPAEVGERWKARF--GLDILDGIGSTEMLHI 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 576 CTSYQYERDKEITTqnvpiGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEkLY 655
Cdd:cd05959 321 FLSNRPGRVRYGTT-----GKPVPGYEVELRDEDGGDVADGEPGELYVRGPSSATMYWNNRDKTRDTF------QGE-WT 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 656 KTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-----TEKDIPI 730
Cdd:cd05959 389 RTGDKYVRDDDGFYTYAGRADDMLKVSGIWVSPFEVESALVQHPAVLEAAVVGVEDEDGLTKPKAFVVlrpgyEDSEALE 468
|
490 500 510
....*....|....*....|....*....|....*....
gi 446807313 731 PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05959 469 EELKEFVKDRLAPYKYPRWIVFVDELPKTATGKIQRFKL 507
|
|
| C_NRPS-like |
cd19537 |
Condensation family domain with an atypical active site motif; Condensation (C) domains of ... |
894-1270 |
2.26e-38 |
|
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: 149.26 E-value: 2.26e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 894 TTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPnvdfniEYVHVNE-KDADylIHEFIS-PF 971
Cdd:cd19537 22 SSFNVSFACRLSGDVDRDRLASAWNTVLARHRILRSRYVPRDGGLRRSYSS------SPPRVQRvDTLD--VWKEINrPF 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 972 DLSKppllrvlllriaEE--------RHILVVdMHHIISDGLSMGILIKEFVELYKGNELPKLRVQYKDYVMWQngpyyK 1043
Cdd:cd19537 94 DLER------------EDpirvfispDTLLVV-MSHIICDLTTLQLLLREVSAAYNGKLLPPVRREYLDSTAWS-----R 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1044 NLISEQKNYWLTTLKGeLPVLNFPTdfqRPTIQSFKGNVCSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRYTG 1123
Cdd:cd19537 156 PASPEDLDFWSEYLSG-LPLLNLPR---RTSSKSYRGTSRVFQLPGSLYRSLLQFSTSSGITLHQLALAAVALALQDLSD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1124 QEDIIVGSPIAGRSHSDTNHMIGMFINTLVMR-NY-LENDDEFIEFL------SRLKL-NTLeayenqdyPFEELLEGLD 1194
Cdd:cd19537 232 RTDIVLGAPYLNRTSEEDMETVGLFLEPLPIRiRFpSSSDASAADFLravrrsSQAALaHAI--------PWHQLLEHLG 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1195 LHRDTSRNPLFDTMFVFQNMDMnpisiGELEFtPYPFKQSV------SKFDLSLVATEIDNN-IHLKVEYSIKLFKAETI 1267
Cdd:cd19537 304 LPPDSPNHPLFDVMVTFHDDRG-----VSLAL-PIPGVEPLytwaegAKFPLMFEFTALSDDsLLLRLEYDTDCFSEEEI 377
|
...
gi 446807313 1268 ERL 1270
Cdd:cd19537 378 DRI 380
|
|
| ligase_PEP_1 |
TIGR03098 |
acyl-CoA ligase (AMP-forming), exosortase A-associated; This group of proteins contains an ... |
1319-1814 |
5.53e-38 |
|
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: 151.09 E-value: 5.53e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1319 LVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPI 1398
Cdd:TIGR03098 1 LLHHLLEDAAARLPDATALVHHDRTLTYAALSERVLALASGLRGLGLARGERVAIYLDKRLETVTAMFGAALAGGVFVPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1399 DTDLPKQRVEYMLTDSGC-------------SHVLVHQNSIIKGIEFqgnviDLMDMSFEEEPGEDMHMM---------I 1456
Cdd:TIGR03098 81 NPLLKAEQVAHILADCNVrllvtsserldllHPALPGCHDLRTLIIV-----GDPAHASEGHPGEEPASWpkllalgdaD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1457 EPH-----NLAYVIYTSGSTGQPKGVMIEHRSLTN--FLCAMYEDFSQDigitDNVLFSSSISFDVTIFEIFVPLIYGAR 1529
Cdd:TIGR03098 156 PPHpvidsDMAAILYTSGSTGRPKGVVLSHRNLVAgaQSVATYLENRPD----DRLLAVLPLSFDYGFNQLTTAFYVGAT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1530 MTIYQgeKFDVTKLVQVILEEQVT-LSYIPP---TLLNEIYDYFVRDNQKIVLNKllVGVEPikTELLAKYDHLFrGNLQ 1605
Cdd:TIGR03098 232 VVLHD--YLLPRDVLKALEKHGITgLAAVPPlwaQLAQLDWPESAAPSLRYLTNS--GGAMP--RATLSRLRSFL-PNAR 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1606 ILNGYGPTEAtvcctsYR--YESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTA 1683
Cdd:TIGR03098 305 LFLMYGLTEA------FRstYLPPEEVDRRPDSIGKAIPNAEVLVLREDGSECAPGEEGELVHRGALVAMGYWNDPEKTA 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1684 DKFIDHP-FERGEKLYKT----GDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVID-QEDEAG 1757
Cdd:TIGR03098 379 ERFRPLPpFPGELHLPELavwsGDTVRRDEEGFLYFVGRRDEMIKTSGYRVSPTEVEEVAYATGLVAEAVAFGvPDPTLG 458
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1758 EKYLCAYVVTEKDIPIPEV-RAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPK 1814
Cdd:TIGR03098 459 QAIVLVVTPPGGEELDRAAlLAECRARLPNYMVPALIHVRQALPRNANGKIDRKALAK 516
|
|
| CHC_CoA_lg |
cd05903 |
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); ... |
302-769 |
1.41e-37 |
|
Cyclohexanecarboxylate-CoA ligase (also called cyclohex-1-ene-1-carboxylate:CoA ligase); Cyclohexanecarboxylate-CoA ligase activates the aliphatic ring compound, cyclohexanecarboxylate, for degradation. It catalyzes the synthesis of cyclohexanecarboxylate-CoA thioesters in a two-step reaction involving the formation of cyclohexanecarboxylate-AMP anhydride, followed by the nucleophilic substitution of AMP by CoA.
Pssm-ID: 341229 [Multi-domain] Cd Length: 437 Bit Score: 148.30 E-value: 1.41e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 302 TYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGcSHVLTyqn 381
Cdd:cd05903 3 TYSELDTRADRLAAGLAALGVGPGDVVAFQLPNWWEFAVLYLACLRIGAVTNPILPFFREHELAFILRRAK-AKVFV--- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 382 siikgvafqgsvinlmdIPFEEEQVEDLQitmEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqdIGITDN 461
Cdd:cd05903 79 -----------------VPERFRQFDPAA---MPDAVALLLFTSGTTGEPKGVMHSHNTLSASIRQYAERLG--LGPGDV 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 462 VLFSSSIS-FDVTIFEIFVPLVCGARmTIYQgEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFV 540
Cdd:cd05903 137 FLVASPMAhQTGFVYGFTLPLLLGAP-VVLQ-DIWDPDKALALMREHGVTFMMGATPFLTDLLNAVEEAGEPLSRLRTFV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 541 ----GVEPIKTELLAKydhlfRGNLQILNLYGPTE---ATVCCTSyqYERDKEITTQnvpiGSPLLNTKIYILDSFHRLQ 613
Cdd:cd05903 215 cggaTVPRSLARRAAE-----LLGAKVCSAYGSTEcpgAVTSITP--APEDRRLYTD----GRPLPGVEIKVVDDTGATL 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 614 PIGVPGEICISGIGLARGYINRKELTADKFidhpferGEKLYKTGDIARWLPDGNIEYLGRVDhQVKIR-GYRIELGEIE 692
Cdd:cd05903 284 APGVEGELLSRGPSVFLGYLDRPDLTADAA-------PEGWFRTGDLARLDEDGYLRITGRSK-DIIIRgGENIPVLEVE 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 693 ASLLKYETIKTAVVIQREDES-GEKyLCAYVVTEK--DIPIPEVRAYL-ATKLPYYMIPQQIISIQNIPLTQNGKIDRKK 768
Cdd:cd05903 356 DLLLGHPGVIEAAVVALPDERlGER-ACAVVVTKSgaLLTFDELVAYLdRQGVAKQYWPERLVHVDDLPRTPSGKVQKFR 434
|
.
gi 446807313 769 L 769
Cdd:cd05903 435 L 435
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
875-1285 |
2.63e-37 |
|
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: 147.63 E-value: 2.63e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 875 ASTSQKRMFIVDQFEDGTnTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKI------EPNvdf 948
Cdd:cd19546 7 ATAGQLRTWLLARLDEET-RGRHLSVALRLRGRLDRDALEAALGDVAARHEILRTTFPGDGGDVHQRIldadaaRPE--- 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 949 nIEYVHVNEKDADYLIHEFIS-PFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY------KGN 1021
Cdd:cd19546 83 -LPVVPATEEELPALLADRAAhLFDLTRETPWRCTLFALSDTEHVLLLVVHRIAADDESLDVLVRDLAAAYgarregRAP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1022 ELPKLRVQYKDYVMWQ----NGPYYKN-LISEQKNYWLTTLKGELPVLNFPTDFQRPTIQSFKGNVCSFNLGTDLTFKVN 1096
Cdd:cd19546 162 ERAPLPLQFADYALWErellAGEDDRDsLIGDQIAYWRDALAGAPDELELPTDRPRPVLPSRRAGAVPLRLDAEVHARLM 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1097 KLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRS-HSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNT 1175
Cdd:cd19546 242 EAAESAGATMFTVVQAALAMLLTRLGAGTDVTVGTVLPRDDeEGDLEGMVGPFARPLALRTDLSGDPTFRELLGRVREAV 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1176 LEAYENQDYPFEELLEGLDLHRDTSRNPLFDTMFVFQNMDMNPISIGE---LEFTPYPFKQSVSKFDLSLVATEIDNN-- 1250
Cdd:cd19546 322 REARRHQDVPFERLAELLALPPSADRHPVFQVALDVRDDDNDPWDAPElpgLRTSPVPLGTEAMELDLSLALTERRNDdg 401
|
410 420 430
....*....|....*....|....*....|....*....
gi 446807313 1251 ----IHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19546 402 dpdgLDGSLRYAADLFDRATAAALARRLVRVLEQVAADP 440
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
876-1285 |
4.51e-37 |
|
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: 146.36 E-value: 4.51e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 876 STSQKRMFIVDQFEDGTNTtYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVDFNIEYVHV 955
Cdd:cd19533 5 TSAQRGVWFAEQLDPEGSI-YNLAEYLEITGPVDLAVLERALRQVIAEAETLRLRFTEEEGEPYQWIDPYTPVPIRHIDL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 956 NEKDA------DYLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY----KGNELP- 1024
Cdd:cd19533 84 SGDPDpegaaqQWMQEDLRKPLPLDNDPLFRHALFTLGDNRHFWYQRVHHIVMDGFSFALFGQRVAEIYtallKGRPAPp 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1025 ----------KLRVQYKDYVMWQngpyyknlisEQKNYWLTTLKGELPvlnfPTDFQRPTIQSFKGNVC-SFNLGTDLTF 1093
Cdd:cd19533 164 apfgsfldlvEEEQAYRQSERFE----------RDRAFWTEQFEDLPE----PVSLARRAPGRSLAFLRrTAELPPELTR 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1094 KVNKLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKL 1173
Cdd:cd19533 230 TLLEAAEAHGASWPSFFIALVAAYLHRLTGANDVVLGVPVMGRLGAAARQTPGMVANTLPLRLTVDPQQTFAELVAQVSR 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1174 NTLEAYENQDYPFEELLEglDLHRDTSRNPLFDTMFVFQNMDMnPISIGELEFTPYPFkQSVSKFDLSLVATE-IDNN-I 1251
Cdd:cd19533 310 ELRSLLRHQRYRYEDLRR--DLGLTGELHPLFGPTVNYMPFDY-GLDFGGVVGLTHNL-SSGPTNDLSIFVYDrDDESgL 385
|
410 420 430
....*....|....*....|....*....|....
gi 446807313 1252 HLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19533 386 RIDFDANPALYSGEDLARHQERLLRLLEEAAADP 419
|
|
| FACL_like_6 |
cd05922 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1353-1812 |
9.07e-37 |
|
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: 146.43 E-value: 9.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1353 ANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGA----YLPIDTDLPKQRVEYMLTDSGcSHVLVHQNSIIK 1428
Cdd:cd05922 3 VSAAASALLEAGGVRGERVVLILPNRFTYIELSFAVAYAGGRlglvFVPLNPTLKESVLRYLVADAG-GRIVLADAGAAD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1429 GIEFQGNVIDLMDMSFEEEPGEDMHMMIEPH-----NLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqDIGITD 1503
Cdd:cd05922 82 RLRDALPASPDPGTVLDADGIRAARASAPAHevsheDLALLLYTSGSTGSPKLVRLSHQNLLANARSIAEYL--GITADD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1504 NVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKFDVTkLVQVILEEQVT-LSYIPPTLlnEIYDYFVRDNQKI-VLNKL 1581
Cdd:cd05922 160 RALTVLPLSYDYGLSVLNTHLLRGATLVLTNDGVLDDA-FWEDLREHGATgLAGVPSTY--AMLTRLGFDPAKLpSLRYL 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1582 LVGVEPIKTELLAKYDHLFRGNlQILNGYGPTEATVCCTsyrYESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVP 1661
Cdd:cd05922 237 TQAGGRLPQETIARLRELLPGA-QVYVMYGQTEATRRMT---YLPPERILEKPGSIGLAIPGGEFEILDDDGTPTPPGEP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1662 GEICISGIGLARGYINRKELTADKfidhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 1741
Cdd:cd05922 313 GEIVHRGPNVMKGYWNDPPYRRKE------GRGGGVLHTGDLARRDEDGFLFIVGRRDRMIKLFGNRISPTEIEAAARSI 386
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1742 ETIKTAVVIDQEDEAGEKylCAYVVTEKDIPIP-EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05922 387 GLIIEAAAVGLPDPLGEK--LALFVTAPDKIDPkDVLRSLAERLPPYKVPATVRVVDELPLTASGKVDYAAL 456
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
1322-1766 |
1.28e-36 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 148.71 E-value: 1.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1322 KMFEEQVKRNPNQIAVVCNEKG----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLP 1397
Cdd:COG1022 15 DLLRRRAARFPDRVALREKEDGiwqsLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAVTVP 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1398 IDTDLPKQRVEYMLTDSGCSHVLV-------------HQNSIIKGI---EFQGNVIDLMDMSFEE--EPGEDMHMM---- 1455
Cdd:COG1022 95 IYPTSSAEEVAYILNDSGAKVLFVedqeqldkllevrDELPSLRHIvvlDPRGLRDDPRLLSLDEllALGREVADPaele 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1456 -----IEPHNLAYVIYTSGSTGQPKGVMIEHRsltNFLCAMyEDFSQDIGITDNvlfSSSISFdv--tIFE--IFVPLIY 1526
Cdd:COG1022 175 arraaVKPDDLATIIYTSGTTGRPKGVMLTHR---NLLSNA-RALLERLPLGPG---DRTLSFlplahVFErtVSYYALA 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1527 gARMTIYQGEkfDVTKLVQVILEEQVTLSYIPPTLLNEIYD--------------------------YFVRDNQ------ 1574
Cdd:COG1022 248 -AGATVAFAE--SPDTLAEDLREVKPTFMLAVPRVWEKVYAgiqakaeeagglkrklfrwalavgrrYARARLAgkspsl 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1575 ----------KIVLNKL-----------LVGVEPIKTELlakyDHLFRG-NLQILNGYGPTEATVCCTSYRYESNKeITT 1632
Cdd:COG1022 325 llrlkhaladKLVFSKLrealggrlrfaVSGGAALGPEL----ARFFRAlGIPVLEGYGLTETSPVITVNRPGDNR-IGT 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1633 qnvpIGSPLLNTKIyildsfhRiqpIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPDGNI 1712
Cdd:COG1022 400 ----VGPPLPGVEV-------K---IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGELDEDGFL 459
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1713 EYLGRVDHQVKIR-GYRIELGEIEASLLKYETIKTAVVIDQedeaGEKYLCAYVV 1766
Cdd:COG1022 460 RITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVVGD----GRPFLAALIV 510
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
302-769 |
6.11e-35 |
|
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: 140.33 E-value: 6.11e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 302 TYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYqn 381
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITT-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 382 siikgvafqgsvinlmdipfeeeqvEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGITDN 461
Cdd:cd05969 80 -------------------------EELYERTDPEDPTLLHYTSGTTGTPKGVLHVHDAMI----FYYFTGKYVLDLHPD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 462 VLFSSSIS---FDVTIFEIFVPLVCGARMTIYQGeKFDVPKLVQVILEEQVTLAYIPPT---LLNEIYDYFVRANQKISL 535
Cdd:cd05969 131 DIYWCTADpgwVTGTVYGIWAPWLNGVTNVVYEG-RFDAESWYGIIERVKVTVWYTAPTairMLMKEGDELARKYDLSSL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 536 NKLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTE-ATVCCTSYqyerdkeiTTQNVPIGS---PLLNTKIYILDSFHR 611
Cdd:cd05969 210 RFIHSVGEPLNPEAIRWGMEVF--GVPIHDTWWQTEtGSIMIANY--------PCMPIKPGSmgkPLPGVKAAVVDENGN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 612 LQPIGVPGEICISG--IGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 689
Cdd:cd05969 280 ELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFID-------GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 690 EIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPiP------EVRAYLATKLPYYMIPQQIISIQNIPLTQNGK 763
Cdd:cd05969 353 EVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE-PsdelkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGK 431
|
....*.
gi 446807313 764 IDRKKL 769
Cdd:cd05969 432 IMRRVL 437
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
276-764 |
2.11e-34 |
|
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the adenylation domain of nonribosomal peptide synthetases and firefly luciferases. The adenylate-forming enzymes catalyze an ATP-dependent two-step reaction to first activate a carboxylate substrate as an adenylate and then transfer the carboxylate to the pantetheine group of either coenzyme A or an acyl-carrier protein. The active site of the domain is located at the interface of a large N-terminal subdomain and a smaller C-terminal subdomain.
Pssm-ID: 341289 [Multi-domain] Cd Length: 587 Bit Score: 141.56 E-value: 2.11e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 276 TAPQLFEEQVKQNPNQIAIVCNGKE------ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAG 349
Cdd:cd17634 54 LAANALDRHLRENGDRTAIIYEGDDtsqsrtISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 350 GAYLPIDTELPKQRVEYMLTDSGCSHVLT------------YQNSIIKGVAFQG-SVINLM-------DIPFEE------ 403
Cdd:cd17634 134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITadggvragrsvpLKKNVDDALNPNVtSVEHVIvlkrtgsDIDWQEgrdlww 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 404 -EQVEDLQ-----ITMEPQNLAYVIYTSGSTGQPKGVMIEHrslTNFLCAMYEDFSQ--DIGITDNVLFSSSISFDVT-I 474
Cdd:cd17634 214 rDLIAKASpehqpEAMNAEDPLFILYTSGTTGKPKGVLHTT---GGYLVYAATTMKYvfDYGPGDIYWCTADVGWVTGhS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 475 FEIFVPLVCGARMTIYQGeKFDVP---KLVQVILEEQVTLAYIPPTLLNEIY---DYFVRANQKISLNKLFVGVEPIKTE 548
Cdd:cd17634 291 YLLYGPLACGATTLLYEG-VPNWPtpaRMWQVVDKHGVNILYTAPTAIRALMaagDDAIEGTDRSSLRILGSVGEPINPE 369
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 549 LLAKY-DHLFRGNLQILNLYGPTEAT-VCCTSYqyeRDKEITTQNVPIgSPLLNTKIYILDSFHRLQPIGVPGEICISGI 626
Cdd:cd17634 370 AYEWYwKKIGKEKCPVVDTWWQTETGgFMITPL---PGAIELKAGSAT-RPVFGVQPAVVDNEGHPQPGGTEGNLVITDP 445
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 627 --GLARGYINRKeltaDKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTA 704
Cdd:cd17634 446 wpGQTRTLFGDH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEA 521
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 705 VVIQREDE-SGEKYLCAYVVTEKDIPIP----EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKI 764
Cdd:cd17634 522 AVVGIPHAiKGQAPYAYVVLNHGVEPSPelyaELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
299-728 |
3.81e-34 |
|
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: 138.50 E-value: 3.81e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 299 KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI-DTELPKQrVEYMLTDSGCSHVL 377
Cdd:cd05907 4 QPITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIyPTSSAEQ-IAYILNDSEAKALF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 378 tyqnsiikgvafqgsvinlmdipfeeeqVEDlqitmePQNLAYVIYTSGSTGQPKGVMIEHRSLtnflcamyedFSQDIG 457
Cdd:cd05907 83 ----------------------------VED------PDDLATIIYTSGTTGRPKGVMLSHRNI----------LSNALA 118
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 458 ITDNVLF---SSSISF--DVTIFE----IFVPLVCGARMTIYQGEKFDVPKLVQVileeQVTLAYIPPTLLNEIYDYFVR 528
Cdd:cd05907 119 LAERLPAtegDRHLSFlpLAHVFErragLYVPLLAGARIYFASSAETLLDDLSEV----RPTVFLAVPRVWEKVYAAIKV 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 529 ANQKISLNKLF------------VGVEPIKTELLakydHLFRG-NLQILNLYGPTE--ATVCCTSyqyERDKEITTqnvp 593
Cdd:cd05907 195 KAVPGLKRKLFdlavggrlrfaaSGGAPLPAELL----HFFRAlGIPVYEGYGLTEtsAVVTLNP---PGDNRIGT---- 263
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 594 IGSPLLNTKIYILDSfhrlqpigvpGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLG 673
Cdd:cd05907 264 VGKPLPGVEVRIADD----------GEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITG 327
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 674 RV-DHQVKIRGYRIELGEIEASLLKYETIKTAVVIQRedesGEKYLCAYVVTEKDI 728
Cdd:cd05907 328 RKkDLIITSGGKNISPEPIENALKASPLISQAVVIGD----GRPFLVALIVPDPEA 379
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1458-1812 |
4.98e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 135.48 E-value: 4.98e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1458 PHNLAYVIYTSGSTGQPKGVMIEHRSLTN--FLCAMYEDF-SQDIGITDNVLFSSsisFDVTIfEIFVPLIYGARMtIYQ 1534
Cdd:cd05917 1 PDDVINIQFTSGTTGSPKGATLTHHNIVNngYFIGERLGLtEQDRLCIPVPLFHC---FGSVL-GVLACLTHGATM-VFP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1535 GEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIV-LNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPT 1613
Cdd:cd05917 76 SPSFDPLAVLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSsLRTGIMAGAPCPPELMKRVIEVM-NMKDVTIAYGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1614 EATVCCTSYRyeSNKEITTQNVPIGSPLLNTKIYILDSFHRIQP-IGVPGEICISGIGLARGYINRKELTAdKFIDhpfe 1692
Cdd:cd05917 155 ETSPVSTQTR--TDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTA-EAID---- 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1693 rGEKLYKTGDIARWLPDGNIEYLGRVDHQVkIRG-YRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVV--TE 1768
Cdd:cd05917 228 -GDGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERyGEE-VCAWIRlkEG 304
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446807313 1769 KDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05917 305 AELTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| VL_LC_FACS_like |
cd05907 |
Long-chain fatty acid CoA synthetases and Bubblegum-like very long-chain fatty acid CoA ... |
1344-1788 |
5.08e-34 |
|
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: 138.11 E-value: 5.08e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPI-DTDLPKQrVEYMLTDSGCSHVLVh 1422
Cdd:cd05907 6 ITWAEFAEEVRALAKGLIALGVEPGDRVAILSRNRPEWTIADLAILAIGAVPVPIyPTSSAEQ-IAYILNDSEAKALFV- 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1423 qnsiikgiefqgnvidlmdmsfeeEPGEDmhmmiephnLAYVIYTSGSTGQPKGVMIEHRSLtnflcamyedFSQDIGIT 1502
Cdd:cd05907 84 ------------------------EDPDD---------LATIIYTSGTTGRPKGVMLSHRNI----------LSNALALA 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1503 DNVLF---SSSISF--DVTIFE----IFVPLIYGARMTIYQGEKFDVTKLVQVileeQVTLSYIPPTLLNEIYDYFVRDN 1573
Cdd:cd05907 121 ERLPAtegDRHLSFlpLAHVFErragLYVPLLAGARIYFASSAETLLDDLSEV----RPTVFLAVPRVWEKVYAAIKVKA 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1574 QKIVLNKLL------------VGVEPIKTELLakydHLFRG-NLQILNGYGPTE--ATVCCTsyRYESNKEITtqnvpIG 1638
Cdd:cd05907 197 VPGLKRKLFdlavggrlrfaaSGGAPLPAELL----HFFRAlGIPVYEGYGLTEtsAVVTLN--PPGDNRIGT-----VG 265
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1639 SPLLNTKIyildsfhRIQPigvPGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLGRV 1718
Cdd:cd05907 266 KPLPGVEV-------RIAD---DGEILVRGPNVMLGYYKNPEATAEALDADGW------LHTGDLGEIDEDGFLHITGRK 329
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1719 -DHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQedeaGEKYLCAYVVTEKDIpipeVRAYLATKLPHYM 1788
Cdd:cd05907 330 kDLIITSGGKNISPEPIENALKASPLISQAVVIGD----GRPFLVALIVPDPEA----LEAWAEEHGIAYT 392
|
|
| FACL_like_2 |
cd05917 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
423-769 |
6.86e-34 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341241 [Multi-domain] Cd Length: 349 Bit Score: 135.10 E-value: 6.86e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 423 YTSGSTGQPKGVMIEHRSLTN--FLCAMYEDF-SQDIGITDNVLFSSsisFDVTIfEIFVPLVCGARMtIYQGEKFDVPK 499
Cdd:cd05917 9 FTSGTTGSPKGATLTHHNIVNngYFIGERLGLtEQDRLCIPVPLFHC---FGSVL-GVLACLTHGATM-VFPSPSFDPLA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 500 LVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKIS-LNKLFVGVEPIKTELLakydhlfRGNLQILNL------YGPTEA 572
Cdd:cd05917 84 VLEAIEKEKCTALHGVPTMFIAELEHPDFDKFDLSsLRTGIMAGAPCPPELM-------KRVIEVMNMkdvtiaYGMTET 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 573 TVCCTsyQYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQP-IGVPGEICISGIGLARGYINRKELTAdKFIDhpferG 651
Cdd:cd05917 157 SPVST--QTRTDDSIEKRVNTVGRIMPHTEAKIVDPEGGIVPpVGVPGELCIRGYSVMKGYWNDPEKTA-EAID-----G 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 652 EKLYKTGDIARWLPDGNIEYLGRVDHQVkIRG-YRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVV--TEKD 727
Cdd:cd05917 229 DGWLHTGDLAVMDEDGYCRIVGRIKDMI-IRGgENIYPREIEEFLHTHPKVSDVQVVGVPDERyGEE-VCAWIRlkEGAE 306
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 446807313 728 IPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05917 307 LTEEDIKAYCKGKIAHYKVPRYVFFVDEFPLTVSGKIQKFKL 348
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
297-769 |
9.03e-34 |
|
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: 138.21 E-value: 9.03e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 297 NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHV 376
Cdd:cd05926 11 STPALTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 377 LTYQNSI-------------IKGVAFQGSVINLM----DIPFEEE--QVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIE 437
Cdd:cd05926 91 LTPKGELgpasraasklglaILELALDVGVLIRApsaeSLSNLLAdkKNAKSEGVPLPDDLALILHTSGTTGRPKGVPLT 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 438 HR----SLTNfLCAMYEdfsqdigitdnvLFSSSISFDVT-IFEI-------FVPLVCGARMTIyqGEKFD--------- 496
Cdd:cd05926 171 HRnlaaSATN-ITNTYK------------LTPDDRTLVVMpLFHVhglvaslLSTLAAGGSVVL--PPRFSastfwpdvr 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 497 ---------VPKLVQVILEEQVTLAYIPPTLLNeiydyFVRAnqkislnklfvGVEPIKTELLAKYDHLFRgnLQILNLY 567
Cdd:cd05926 236 dynatwytaVPTIHQILLNRPEPNPESPPPKLR-----FIRS-----------CSASLPPAVLEALEATFG--APVLEAY 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 568 GPTEATVCCTSYQYERDKEITTQnVPIGSpllNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHP 647
Cdd:cd05926 298 GMTEAAHQMTSNPLPPGPRKPGS-VGKPV---GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDG 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 648 FergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTEK 726
Cdd:cd05926 374 W------FRTGDLGYLDADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKyGEE-VAAAVVLRE 446
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446807313 727 DIPI--PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05926 447 GASVteEELRAFCRKHLAAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
1344-1812 |
1.19e-33 |
|
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain fatty acyl-CoA synthetases, which catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Fatty acyl-CoA synthetases are responsible for fatty acid degradation as well as physiological regulation of cellular functions via the production of fatty acyl-CoA esters.
Pssm-ID: 341258 [Multi-domain] Cd Length: 430 Bit Score: 136.45 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:cd05935 2 LTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAVVGS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSL--TNFLCAMYEDFSQDigi 1501
Cdd:cd05935 82 ---------------------------------ELDDLALIPYTSGTTGLPKGCMHTHFSAaaNALQSAVWTGLTPS--- 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1502 tdNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDyfVRDNQKIVLNKL 1581
Cdd:cd05935 126 --DVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLA--TPEFKTRDLSSL 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1582 LV---GVEPIKTELLAKYDHLFrgNLQILNGYGPTEaTVCCTSYRYESNKEITTQnvpiGSPLLNTKIYILD-SFHRIQP 1657
Cdd:cd05935 202 KVltgGGAPMPPAVAEKLLKLT--GLRFVEGYGLTE-TMSQTHTNPPLRPKLQCL----GIP*FGVDARVIDiETGRELP 274
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1658 IGVPGEICISGIGLARGYINRKELTADKFIDhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEAS 1737
Cdd:cd05935 275 PNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEAK 351
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1738 LLKYETIKTAVVIDQEDE-AGEKyLCAYVV---------TEKDIpIPEVRAYLATklphYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:cd05935 352 LYKHPAI*EVCVISVPDErVGEE-VKAFIVlrpeyrgkvTEEDI-IEWAREQMAA----YKYPREVEFVDELPRSASGKI 425
|
....*
gi 446807313 1808 DRSKL 1812
Cdd:cd05935 426 LWRLL 430
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
291-769 |
2.22e-33 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 135.67 E-value: 2.22e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 291 QIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTD 370
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 371 SGCSHVLTYQNSIikgvafqgsvinlmdipfeeeqvedlqitmepqnlAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYE 450
Cdd:cd05919 81 CEARLVVTSADDI-----------------------------------AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 451 DFsqdIGITDN-VLFSSSISFdvtiF------EIFVPLVCGARMTIYQGEKfDVPKLVQVILEEQVTLAYIPPTLLNEIY 523
Cdd:cd05919 126 EA---LGLTPGdRVFSSAKMF----FgyglgnSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYANLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 524 DYFVRANQKISLNKLFVGV-EPIKTELLAKYDHLFRGnlQILNLYGPTEAT---VCCTSYQYERDkeiTTqnvpiGSPLL 599
Cdd:cd05919 198 DSCAGSPDALRSLRLCVSAgEALPRGLGERWMEHFGG--PILDGIGATEVGhifLSNRPGAWRLG---ST-----GRPVP 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 600 NTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEkLYKTGDIARWLPDGNIEYLGRVDHQV 679
Cdd:cd05919 268 GYEIRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG-WYRTGDKFCRDADGWYTHAGRADDML 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 680 KIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTE-----KDIPIPEVRAYLATKLPYYMIPQQIISIQ 754
Cdd:cd05919 341 KVGGQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKspaapQESLARDIHRHLLERLSAHKVPRRIAFVD 420
|
490
....*....|....*
gi 446807313 755 NIPLTQNGKIDRKKL 769
Cdd:cd05919 421 ELPRTATGKLQRFKL 435
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
248-773 |
3.01e-33 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 137.42 E-value: 3.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 248 MPKTEKNQILFdfnhTTRVHKTLLCETVTAPQLFEEQVKQNPNQIAIV--CNGKEITYKQLNIKANQLARRLLDQGVKRE 325
Cdd:PLN02330 5 IQKQEDNEHIF----RSRYPSVPVPDKLTLPDFVLQDAELYADKVAFVeaVTGKAVTYGEVVRDTRRFAKALRSLGLRKG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 326 FIVGVMMERSIEMIVGILGILKAGGAY-----LPIDTELPKQrVEYMLTDSGCSHVLTYQNS-------IIKGVAFQGSV 393
Cdd:PLN02330 81 QVVVVVLPNVAEYGIVALGIMAAGGVFsganpTALESEIKKQ-AEAAGAKLIVTNDTNYGKVkglglpvIVLGEEKIEGA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 394 INLMDIPFEEEQVEDLQITME--PQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYedFSQDIGITDNVLFSSSISFd 471
Cdd:PLN02330 160 VNWKELLEAADRAGDTSDNEEilQTDLCALPFSSGTTGISKGVMLTHRNLVANLCSSL--FSVGPEMIGQVVTLGLIPF- 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 472 vtiFEIF-VPLVCGARM----TIYQGEKFDVPKLVQVILEEQVTLAYI-PPTLLNEIYDYFVRAN--QKISLNKLFVGVE 543
Cdd:PLN02330 237 ---FHIYgITGICCATLrnkgKVVVMSRFELRTFLNALITQEVSFAPIvPPIILNLVKNPIVEEFdlSKLKLQAIMTAAA 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 544 PIKTELLAKYDHLFRGnLQILNLYGPTEATvCCTSYQYERDKE--ITTQNvPIGSPLLNTKIYILDSFHRLQ-PIGVPGE 620
Cdd:PLN02330 314 PLAPELLTAFEAKFPG-VQVQEAYGLTEHS-CITLTHGDPEKGhgIAKKN-SVGFILPNLEVKFIDPDTGRSlPKNTPGE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 621 ICISGIGLARGYINRKELTaDKFIDHpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYET 700
Cdd:PLN02330 391 LCVRSQCVMQGYYNNKEET-DRTIDE-----DGWLHTGDIGYIDDDGDIFIVDRIKELIKYKGFQVAPAELEAILLTHPS 464
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 701 IKTAVVIQREDESGEKYLCAYVVTEKDIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPI 773
Cdd:PLN02330 465 VEDAAVVPLPDEEAGEIPAACVVINPKAKESEedILNFVAANVAHYKKVRVVQFVDSIPKSLSGKIMRRLLKEKM 539
|
|
| MACS_like_4 |
cd05969 |
Uncharacterized subfamily of Acetyl-CoA synthetase like family (ACS); This family is most ... |
1345-1812 |
4.11e-33 |
|
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: 134.94 E-value: 4.11e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQN 1424
Cdd:cd05969 2 TFAQLKVLSARFANVLKSLGVGKGDRVFVLSPRSPELYFSMLGIGKIGAVICPLFSAFGPEAIRDRLENSEAKVLITTEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 siikgiefqgnVIDLMDMsfeeepgEDMhmmiephnlAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGITDN 1504
Cdd:cd05969 82 -----------LYERTDP-------EDP---------TLLHYTSGTTGTPKGVLHVHDAMI----FYYFTGKYVLDLHPD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 VLFSSSIS---FDVTIFEIFVPLIYGARMTIYQGeKFDVTKLVQVILEEQVTLSYIPPT---LLNEIYDYFVRDNQKIVL 1578
Cdd:cd05969 131 DIYWCTADpgwVTGTVYGIWAPWLNGVTNVVYEG-RFDAESWYGIIERVKVTVWYTAPTairMLMKEGDELARKYDLSSL 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1579 NKLLVGVEPIKTELLAKYDHLFrgNLQILNGYGPTE-ATVCCTSYryesnkeiTTQNVPIGS---PLLNTKIYILDSFHR 1654
Cdd:cd05969 210 RFIHSVGEPLNPEAIRWGMEVF--GVPIHDTWWQTEtGSIMIANY--------PCMPIKPGSmgkPLPGVKAAVVDENGN 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1655 IQPIGVPGEICISG--IGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 1732
Cdd:cd05969 280 ELPPGTKGILALKPgwPSMFRGIWNDEERYKNSFID-------GWYLTGDLAYRDEDGYFWFVGRADDIIKTSGHRVGPF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1733 EIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPiP------EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGK 1806
Cdd:cd05969 353 EVESALMEHPAVAEAGVIGKPDPLRGEIIKAFISLKEGFE-PsdelkeEIINFVRQKLGAHVAPREIEFVDNLPKTRSGK 431
|
....*.
gi 446807313 1807 IDRSKL 1812
Cdd:cd05969 432 IMRRVL 437
|
|
| BCL_like |
cd05919 |
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate ... |
1334-1812 |
6.79e-33 |
|
Benzoate CoA ligase (BCL) and similar adenylate forming enzymes; This family contains benzoate CoA ligase (BCL) and related ligases that catalyze the acylation of benzoate derivatives, 2-aminobenzoate and 4-hydroxybenzoate. Aromatic compounds represent the second most abundant class of organic carbon compounds after carbohydrates. Xenobiotic aromatic compounds are also a major class of man-made pollutants. Some bacteria use benzoate as the sole source of carbon and energy through benzoate degradation. Benzoate degradation starts with its activation to benzoyl-CoA by benzoate CoA ligase. The reaction catalyzed by benzoate CoA ligase proceeds via a two-step process; the first ATP-dependent step forms an acyl-AMP intermediate, and the second step forms the acyl-CoA ester with release of the AMP.
Pssm-ID: 341243 [Multi-domain] Cd Length: 436 Bit Score: 134.13 E-value: 6.79e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1334 QIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTD 1413
Cdd:cd05919 1 KTAFYAADRSVTYGQLHDGANRLGSALRNLGVSSGDRVLLLMLDSPELVQLFLGCLARGAIAVVINPLLHPDDYAYIARD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1414 SGCSHVLVHQNSIikgiefqgnvidlmdmsfeeepgedmhmmiephnlAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYE 1493
Cdd:cd05919 81 CEARLVVTSADDI-----------------------------------AYLLYSSGTTGPPKGVMHAHRDPLLFADAMAR 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1494 DFsqdIGITDN-VLFSSSISFdvtiF------EIFVPLIYGARMTIYQGEKfDVTKLVQVILEEQVTLSYIPPTLLNEIY 1566
Cdd:cd05919 126 EA---LGLTPGdRVFSSAKMF----FgyglgnSLWFPLAVGASAVLNPGWP-TAERVLATLARFRPTVLYGVPTFYANLL 197
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1567 DYFVRDNQKIVLNKLLVGV-EPIKTELLAKYDHLFRGnlQILNGYGPTEatvccTSYRYESNKEITTQNVPIGSPLLNTK 1645
Cdd:cd05919 198 DSCAGSPDALRSLRLCVSAgEALPRGLGERWMEHFGG--PILDGIGATE-----VGHIFLSNRPGAWRLGSTGRPVPGYE 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1646 IYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEkLYKTGDIARWLPDGNIEYLGRVDHQVKIR 1725
Cdd:cd05919 271 IRLVDEEGHTIPPGEEGDLLVRGPSAAVGYWNNPEKSRATF------NGG-WYRTGDKFCRDADGWYTHAGRADDMLKVG 343
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1726 GYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTE-----KDIPIPEVRAYLATKLPHYMIPQQLIPIHNIP 1800
Cdd:cd05919 344 GQWVSPVEVESLIIQHPAVAEAAVVAVPESTGLSRLTAFVVLKspaapQESLARDIHRHLLERLSAHKVPRRIAFVDELP 423
|
490
....*....|..
gi 446807313 1801 LTQNGKIDRSKL 1812
Cdd:cd05919 424 RTATGKLQRFKL 435
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
282-769 |
1.48e-32 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 134.60 E-value: 1.48e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 282 EEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 361 KQRVEYMLTDSGCSHVL---TYQNSI--IKGVAFQGSVINLMDiPFEEEQVEDLQITMEPQNLAYVI-YTSGSTGQPKGV 434
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFvekTFQNMAlsMQKVSYVQRVISITS-LKEIEDRKIDNFVEKNESASFIIcYTSGTTGKPKGA 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 435 MIEHRSLtnFLCAMYEDFSQDIGITDnvlfsSSISFdVTIFEI-------FVPLVCGARMTIyqGEKFDVPKLVQVILEE 507
Cdd:PRK06839 168 VLTQENM--FWNALNNTFAIDLTMHD-----RSIVL-LPLFHIggiglfaFPTLFAGGVIIV--PRKFEPTKALSMIEKH 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 508 QVTLAYIPPTLLNEIYDYFVRANQKISLNKLFV-GVEPIKTELLAKYDHlfRGnLQILNLYGPTEA--TVCCTSYQYERD 584
Cdd:PRK06839 238 KVTVVMGVPTIHQALINCSKFETTNLQSVRWFYnGGAPCPEELMREFID--RG-FLFGQGFGMTETspTVFMLSEEDARR 314
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 585 KEITtqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIARWL 664
Cdd:PRK06839 315 KVGS-----IGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLC-------TGDLARVD 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 665 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPE--VRAYLATKLP 742
Cdd:PRK06839 383 EDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEkdVIEHCRLFLA 462
|
490 500
....*....|....*....|....*..
gi 446807313 743 YYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK06839 463 KYKIPKEIVFLKELPKNATGKIQKAQL 489
|
|
| FAA1 |
COG1022 |
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism]; |
276-723 |
1.77e-32 |
|
Long-chain acyl-CoA synthetase (AMP-forming) [Lipid transport and metabolism];
Pssm-ID: 440645 [Multi-domain] Cd Length: 603 Bit Score: 136.00 E-value: 1.77e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 276 TAPQLFEEQVKQNPNQIAIVC--NG--KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGA 351
Cdd:COG1022 12 TLPDLLRRRAARFPDRVALREkeDGiwQSLTWAEFAERVRALAAGLLALGVKPGDRVAILSDNRPEWVIADLAILAAGAV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 352 YLPIDTELPKQRVEYMLTDSGCSHV-----------LTYQNS------II----KGVAFQGSVINLMDI------PFEEE 404
Cdd:COG1022 92 TVPIYPTSSAEEVAYILNDSGAKVLfvedqeqldklLEVRDElpslrhIVvldpRGLRDDPRLLSLDELlalgreVADPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 405 QVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRsltNFLCAMyEDFSQDIGITDNvlfSSSISFdv--tIFE---IFV 479
Cdd:COG1022 172 ELEARRAAVKPDDLATIIYTSGTTGRPKGVMLTHR---NLLSNA-RALLERLPLGPG---DRTLSFlplahVFErtvSYY 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 480 PLVCGArmTIYQGEkfDVPKLVQVILEEQVTLAYIPPTLLNEIYDyfvRANQKIS-----LNKLF-----VGVE------ 543
Cdd:COG1022 245 ALAAGA--TVAFAE--SPDTLAEDLREVKPTFMLAVPRVWEKVYA---GIQAKAEeagglKRKLFrwalaVGRRyararl 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 544 ---PIKTELLAKY---------------------------------DHLFRG-NLQILNLYGPTEATVCCTSYQYERDKe 586
Cdd:COG1022 318 agkSPSLLLRLKHaladklvfsklrealggrlrfavsggaalgpelARFFRAlGIPVLEGYGLTETSPVITVNRPGDNR- 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 587 ITTqnvpIGSPLLNTKIyildsfhRlqpIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPD 666
Cdd:COG1022 397 IGT----VGPPLPGVEV-------K---IAEDGEILVRGPNVMKGYYKNPEATAEAFDADGW------LHTGDIGELDED 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 667 GNIEYLGRVDHQVKIR-GYRIELGEIEASLLKYETIKTAVVIqredESGEKYLCAYVV 723
Cdd:COG1022 457 GFLRITGRKKDLIVTSgGKNVAPQPIENALKASPLIEQAVVV----GDGRPFLAALIV 510
|
|
| FACL_fum10p_like |
cd05926 |
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL ... |
1344-1812 |
4.59e-32 |
|
Subfamily of fatty acid CoA ligase (FACL) similar to Fum10p of Gibberella moniliformis; FACL catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, followed by the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Fum10p is a fatty acid CoA ligase involved in the synthesis of fumonisin, a polyketide mycotoxin, in Gibberella moniliformis.
Pssm-ID: 341249 [Multi-domain] Cd Length: 493 Bit Score: 132.82 E-value: 4.59e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLV-- 1421
Cdd:cd05926 15 LTYADLAELVDDLARQLAALGIKKGDRVAIALPNGLEFVVAFLAAARAGAVVAPLNPAYKKAEFEFYLADLGSKLVLTpk 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1422 -----------HQNSIIKGIEFQGNVIDLM----DMSFEEEPGEDMHMMIEPHN--LAYVIYTSGSTGQPKGVMIEHR-- 1482
Cdd:cd05926 95 gelgpasraasKLGLAILELALDVGVLIRApsaeSLSNLLADKKNAKSEGVPLPddLALILHTSGTTGRPKGVPLTHRnl 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1483 --SLTNfLCAMYEdfsqdigitdnvLFSSSISFDVT-IFEI-------FVPLIYGARMTIyqGEKFDVTKLVQVILEEQV 1552
Cdd:cd05926 175 aaSATN-ITNTYK------------LTPDDRTLVVMpLFHVhglvaslLSTLAAGGSVVL--PPRFSASTFWPDVRDYNA 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1553 TLSYIPPTLLNEIYDYFVRDNQKiVLNKLLV---GVEPIKTELLAKYDHLFRgnLQILNGYGPTEATVCCTSyryesNKE 1629
Cdd:cd05926 240 TWYTAVPTIHQILLNRPEPNPES-PPPKLRFirsCSASLPPAVLEALEATFG--APVLEAYGMTEAAHQMTS-----NPL 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1630 ITTQNVP--IGSPLlNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWL 1707
Cdd:cd05926 312 PPGPRKPgsVGKPV-GVEVRILDEDGEILPPGVVGEICLRGPNVTRGYLNNPEANAEAAFKDGW------FRTGDLGYLD 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1708 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVTEKDIPI--PEVRAYLATKL 1784
Cdd:cd05926 385 ADGYLFLTGRIKELINRGGEKISPLEVDGVLLSHPAVLEAVAFGVPDEKyGEE-VAAAVVLREGASVteEELRAFCRKHL 463
|
490 500
....*....|....*....|....*...
gi 446807313 1785 PHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05926 464 AAFKVPKKVYFVDELPKTATGKIQRRKV 491
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
297-769 |
7.74e-32 |
|
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: 132.36 E-value: 7.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 297 NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYL---PIDT--ELPKQrveymLTDS 371
Cdd:cd05904 29 TGRALTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTtanPLSTpaEIAKQ-----VKDS 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 372 GCSHVLTyQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQN-----------LAYVIYTSGSTGQPKGVMIEHRS 440
Cdd:cd05904 104 GAKLAFT-TAELAEKLASLALPVVLLDSAEFDSLSFSDLLFEADEAeppvvvikqddVAALLYSSGTTGRSKGVMLTHRN 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 441 LTNfLCAMYEDFSQDIGITDNVLFSSSISFDVTIFEIFV--PLVCGArmTIYQGEKFDVPKLVQVILEEQVTLAYI-PPT 517
Cdd:cd05904 183 LIA-MVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFAlgLLRLGA--TVVVMPRFDLEELLAAIERYKVTHLPVvPPI 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 518 LLNEIYDYFVRANQKISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEATvCCTSYQYERDKEittqNVPIGS- 596
Cdd:cd05904 260 VLALVKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKF-PNVDLGQGYGMTEST-GVVAMCFAPEKD----RAKYGSv 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 597 ----PLLNTKIYILDSfHRLQPIGVPGEICISGIGLARGYINRKELTAdKFIDhpferGEKLYKTGDIARWLPDGNIEYL 672
Cdd:cd05904 334 grlvPNVEAKIVDPET-GESLPPNQTGELWIRGPSIMKGYLNNPEATA-ATID-----KEGWLHTGDLCYIDEDGYLFIV 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 673 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-------TEKdipipEVRAYLATKLPYYM 745
Cdd:cd05904 407 DRLKELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVrkpgsslTED-----EIMDFVAKQVAPYK 481
|
490 500
....*....|....*....|....
gi 446807313 746 IPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05904 482 KVRKVAFVDAIPKSPSGKILRKEL 505
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
1329-1807 |
1.53e-31 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 131.55 E-value: 1.53e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1329 KRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVE 1408
Cdd:PRK06145 13 RRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1409 YMLTDSGCSHVLVHQN-SIIKGIEFQGNVIDLM---DMSFEEEPGEDMHMM--IEPHNLAYVIYTSGSTGQPKGVMIehr 1482
Cdd:PRK06145 93 YILGDAGAKLLLVDEEfDAIVALETPKIVIDAAaqaDSRRLAQGGLEIPPQaaVAPTDLVRLMYTSGTTDRPKGVMH--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1483 SLTNFlcaMYEDFSQDI--GIT-DNVLFSSSISFDVTIFEI--FVPLIYGARMTIYQgeKFDVTKLVQVILEEQVTLSYI 1557
Cdd:PRK06145 170 SYGNL---HWKSIDHVIalGLTaSERLLVVGPLYHVGAFDLpgIAVLWVGGTLRIHR--EFDPEAVLAAIERHRLTCAWM 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1558 PPTLLNEIYDYFVRDNQKI-VLNKLLVGVEPIKTELLAKYDHLFRGNlQILNGYGPTEAtvCCTSYRYESNKEITTqnvp 1636
Cdd:PRK06145 245 APVMLSRVLTVPDRDRFDLdSLAWCIGGGEKTPESRIRDFTRVFTRA-RYIDAYGLTET--CSGDTLMEAGREIEK---- 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1637 IGS---PLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIE 1713
Cdd:PRK06145 318 IGStgrALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEEGFLY 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1714 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLCAYVVTE-KDIPIPEVRAYLATKLPHYMIPQ 1791
Cdd:PRK06145 391 LTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIGVHDDRwGERITAVVVLNPgATLTLEALDRHCRQRLASFKVPR 470
|
490
....*....|....*.
gi 446807313 1792 QLIPIHNIPLTQNGKI 1807
Cdd:PRK06145 471 QLKVRDELPRNPSGKV 486
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
297-769 |
2.15e-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: 130.91 E-value: 2.15e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 297 NGKEITYKQLNIKANQLARRLLDQGVKREFiVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHV 376
Cdd:cd05909 4 LGTSLTYRKLLTGAIALARKLAKMTKEGEN-VGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 377 LTYQNSIIKG-------VAFQGSVINLMD------------------IPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQP 431
Cdd:cd05909 83 LTSKQFIEKLklhhlfdVEYDARIVYLEDlrakiskadkckaflagkFPPKWLLRIFGVAPVQPDDPAVILFTSGSEGLP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 432 KGVMIEHRSL-TN-FLCAMYEDFSQDigitDNVL----FSSSISFDVTifeIFVPLVCGARMTIYQgEKFDVPKLVQVIL 505
Cdd:cd05909 163 KGVVLSHKNLlANvEQITAIFDPNPE----DVVFgalpFFHSFGLTGC---LWLPLLSGIKVVFHP-NPLDYKKIPELIY 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 506 EEQVTLAYIPPTLLNeiydYFVRANQK---ISLNKLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTSYQYE 582
Cdd:cd05909 235 DKKATILLGTPTFLR----GYARAAHPedfSSLRLVVAGAEKLKDTLRQEFQEKF--GIRILEGYGTTECSPVISVNTPQ 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 583 RDKEITTQNVPIgsPLLNTKIYILDSfHRLQPIGVPGEICISGIGLARGYINRKELTAdkfidhpFERGEKLYKTGDIAR 662
Cdd:cd05909 309 SPNKEGTVGRPL--PGMEVKIVSVET-HEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGK 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 663 WLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAV-VIQREDES-GEKYLCayVVTEKDIPIPEVRAYL-AT 739
Cdd:cd05909 379 IDGEGFLTITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNEVaVVSVPDGRkGEKIVL--LTTTTDTDPSSLNDILkNA 456
|
490 500 510
....*....|....*....|....*....|
gi 446807313 740 KLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05909 457 GISNLAKPSYIHQVEEIPLLGTGKPDYVTL 486
|
|
| LC_FACS_like |
cd05935 |
Putative long-chain fatty acid CoA ligase; The members of this family are putative long-chain ... |
300-769 |
2.62e-31 |
|
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: 129.52 E-value: 2.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 300 EITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLty 379
Cdd:cd05935 1 SLTYLELLEVVKKLASFLSNKGVRKGDRVGICLQNSPQYVIAYFAIWRANAVVVPINPMLKERELEYILNDSGAKVAV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 380 qnsiikgvafqgsvinlmdipfeeeqvedlqITMEPQNLAYVIYTSGSTGQPKGVMIEHRSL--TNFLCAMYEDFSQdig 457
Cdd:cd05935 79 -------------------------------VGSELDDLALIPYTSGTTGLPKGCMHTHFSAaaNALQSAVWTGLTP--- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 458 itDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDyfVRANQKISLNK 537
Cdd:cd05935 125 --SDVILACLPLFHVTGFVGSLNTAVYVGGTYVLMARWDRETALELIEKYKVTFWTNIPTMLVDLLA--TPEFKTRDLSS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 538 LFV---GVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTSYQYERDKEITtqnvpIGSPLLNTKIYILD-SFHRLQ 613
Cdd:cd05935 201 LKVltgGGAPMPPAVAEKLLKLT--GLRFVEGYGLTETMSQTHTNPPLRPKLQC-----LGIP*FGVDARVIDiETGREL 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 614 PIGVPGEICISGIGLARGYINRKELTADKFIDhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEA 693
Cdd:cd05935 274 PPNEVGEIVVRGPQIFKGYWNRPEETEESFIE---IKGRRFFRTGDLGYMDEEGYFFFVDRVKRMINVSGFKVWPAEVEA 350
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 694 SLLKYETIKTAVVIQREDESGEKYLCAYVV---------TEKDIpIPEVRAYLATklpyYMIPQQIISIQNIPLTQNGKI 764
Cdd:cd05935 351 KLYKHPAI*EVCVISVPDERVGEEVKAFIVlrpeyrgkvTEEDI-IEWAREQMAA----YKYPREVEFVDELPRSASGKI 425
|
....*
gi 446807313 765 DRKKL 769
Cdd:cd05935 426 LWRLL 430
|
|
| ACS-like |
cd17634 |
acetate-CoA ligase; This family includes acyl- and aryl-CoA ligases, as well as the ... |
1319-1807 |
6.62e-31 |
|
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: 130.77 E-value: 6.62e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1319 LVHKMFEEQVKRNPNQIAVV------CNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAG 1392
Cdd:cd17634 54 LAANALDRHLRENGDRTAIIyegddtSQSRTISYRELHREVCRFAGTLLDLGVKKGDRVAIYMPMIPEAAVAMLACARIG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1393 GAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSIIKG--IEFQGNVIDLMDMS----------------FEEEPGEDM-- 1452
Cdd:cd17634 134 AVHSVIFGGFAPEAVAGRIIDSSSRLLITADGGVRAGrsVPLKKNVDDALNPNvtsvehvivlkrtgsdIDWQEGRDLww 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1453 HMMIE------------PHNLAYVIYTSGSTGQPKGVMIEHrslTNFLCAMYEDFSQ--DIGITDNVLFSSSISFDVT-I 1517
Cdd:cd17634 214 RDLIAkaspehqpeamnAEDPLFILYTSGTTGKPKGVLHTT---GGYLVYAATTMKYvfDYGPGDIYWCTADVGWVTGhS 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 FEIFVPLIYGARMTIYQGEKF--DVTKLVQVILEEQVTLSYIPPTLLNEIY---DYFVRDNQKIVLNKLLVGVEPIKTEL 1592
Cdd:cd17634 291 YLLYGPLACGATTLLYEGVPNwpTPARMWQVVDKHGVNILYTAPTAIRALMaagDDAIEGTDRSSLRILGSVGEPINPEA 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1593 LAKY-DHLFRGNLQILNGYGPTEAT-VCCTSYRYESNKEITTQNVPIgsplLNTKIYILDSFHRIQPIGVPGEICISGI- 1669
Cdd:cd17634 371 YEWYwKKIGKEKCPVVDTWWQTETGgFMITPLPGAIELKAGSATRPV----FGVQPAVVDNEGHPQPGGTEGNLVITDPw 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1670 -GLARGYINRKeltaDKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAV 1748
Cdd:cd17634 447 pGQTRTLFGDH----ERFEQTYFSTFKGMYFSGDGARRDEDGYYWITGRSDDVINVAGHRLGTAEIESVLVAHPKVAEAA 522
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313 1749 VIDQEDE-AGEKYLCAYVVTEKDIPIP----EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:cd17634 523 VVGIPHAiKGQAPYAYVVLNHGVEPSPelyaELRNWVRKEIGPLATPDVVHWVDSLPKTRSGKI 586
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
1308-1812 |
1.14e-30 |
|
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: 129.54 E-value: 1.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1308 NKKENSNSNYLLVHKMFEEQvkrnPNQIAVV-CNEKG----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMV 1382
Cdd:cd05970 11 NVPENFNFAYDVVDAMAKEY----PDKLALVwCDDAGeeriFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFW 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1383 IGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSII-----KGIEFQGNVIDLMDMSFEEEPG-EDMHMMI 1456
Cdd:cd05970 87 YSLLALHKLGAIAIPATHQLTAKDIVYRIESADIKMIVAIAEDNIpeeieKAAPECPSKPKLVWVGDPVPEGwIDFRKLI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1457 E--------PHNLAY--------VIYTSGSTGQPKgvMIEHR---SLTNFLCAMYedfSQDIGITDNVLFSSSISFDVTI 1517
Cdd:cd05970 167 KnaspdferPTANSYpcgedillVYFSSGTTGMPK--MVEHDftyPLGHIVTAKY---WQNVREGGLHLTVADTGWGKAV 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 F-EIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTllneIYDYFVR-DNQKIVLNKL---LVGVEPIKTEL 1592
Cdd:cd05970 242 WgKIYGQWIAGAAVFVYDYDKFDPKALLEKLSKYGVTTFCAPPT----IYRFLIReDLSRYDLSSLrycTTAGEALNPEV 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1593 LAKYDHLfrGNLQILNGYGPTEATVCCTSYRYESNKEITtqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICIS----- 1667
Cdd:cd05970 318 FNTFKEK--TGIKLMEGFGQTETTLTIATFPWMEPKPGS-----MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgk 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1668 GIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTA 1747
Cdd:cd05970 391 PVGLFGGYYKDAEKTAEVWHD-------GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLEC 463
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1748 VVIDQEDEAGEKYLCAYVVTEKDIP-----IPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05970 464 AVTGVPDPIRGQVVKATIVLAKGYEpseelKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRRVEI 533
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
283-783 |
2.25e-30 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 128.71 E-value: 2.25e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 283 EQVKQNPNQIAIVCN-GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPK 361
Cdd:PRK06087 31 QTARAMPDKIAVVDNhGASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 362 QRVEYMLTDSGcSHVL---TYQNSI---------------IKGVAF------QGSVINLMDIPFEEEQVEDlQITMEPQN 417
Cdd:PRK06087 111 AELVWVLNKCQ-AKMFfapTLFKQTrpvdlilplqnqlpqLQQIVGvdklapATSSLSLSQIIADYEPLTT-AITTHGDE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 418 LAYVIYTSGSTGQPKGVMIEHrsltNFLCAMYEDFSQDIGIT-DNVLFSSSISFDVTIF--EIFVPLVCGARMTIYQgeK 494
Cdd:PRK06087 189 LAAVLFTSGTEGLPKGVMLTH----NNILASERAYCARLNLTwQDVFMMPAPLGHATGFlhGVTAPFLIGARSVLLD--I 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 495 FDVPKLVQVILEEQVT--LAYIPptllnEIYDYFVRANQK---ISLNKLFV-GVEPIKTELLakyDHLFRGNLQILNLYG 568
Cdd:PRK06087 263 FTPDACLALLEQQRCTcmLGATP-----FIYDLLNLLEKQpadLSALRFFLcGGTTIPKKVA---RECQQRGIKLLSVYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 569 PTEAtvccTSYQYERDKEITTQNVPI-GSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTAdKFIDHp 647
Cdd:PRK06087 335 STES----SPHAVVNLDDPLSRFMHTdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA-RALDE- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 648 fergEKLYKTGDIARWLPDGNIEYLGRvDHQVKIR-GYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTE 725
Cdd:PRK06087 409 ----EGWYYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDERlGER-SCAYVVLK 482
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446807313 726 KDIPIP---EVRAYLATK-LPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPI-NNLKSSHLEP 783
Cdd:PRK06087 483 APHHSLtleEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRKDImRRLTQDVCEE 545
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
288-769 |
7.71e-30 |
|
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: 126.08 E-value: 7.71e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 288 NPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYM 367
Cdd:cd05923 16 DACAIADPARGLRLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPALINPRLKAAELAEL 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 368 LT-DSGCSHVLTyqnsIIKGVAfQGSVINLMDIPFEEEQVEDLQIT----------MEPQNLAYVIYTSGSTGQPKGVMI 436
Cdd:cd05923 96 IErGEMTAAVIA----VDAQVM-DAIFQSGVRVLALSDLVGLGEPEsagpliedppREPEQPAFVFYTSGTTGLPKGAVI 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 437 EHRSLTNFLCAMYEDFSQDIGITDNVLFSSSISFDVTIFEIFVPLVCGARmTIYQGEKFDVPKLVQVILEEQVTLAYIPP 516
Cdd:cd05923 171 PQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVAALALDG-TYVVVEEFDPADALKLIEQERVTSLFATP 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 517 TLLNEIYDYFVRANQKI-SLNKL-FVGVEpIKTELLAKYDHLFRGnlQILNLYGPTEATvcctSYQYERDKEITTQnvpi 594
Cdd:cd05923 250 THLDALAAAAEFAGLKLsSLRHVtFAGAT-MPDAVLERVNQHLPG--EKVNIYGTTEAM----NSLYMRDARTGTE---- 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 595 GSPLLNTKIY---ILDSFHRLQPIGVPGEICISGIGLA--RGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNI 669
Cdd:cd05923 319 MRPGFFSEVRivrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GWYRTGDVGYVDPSGDV 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 670 EYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLCAYVVTEKDIPIPEVRAY-LATKLPYYMIP 747
Cdd:cd05923 392 RILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwGQSVTACVVPREGTLSADELDQFcRASELADFKRP 471
|
490 500
....*....|....*....|..
gi 446807313 748 QQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05923 472 RRYFFLDELPKNAMNKVLRRQL 493
|
|
| PRK06087 |
PRK06087 |
medium-chain fatty-acid--CoA ligase; |
1326-1814 |
7.90e-30 |
|
medium-chain fatty-acid--CoA ligase;
Pssm-ID: 180393 [Multi-domain] Cd Length: 547 Bit Score: 127.17 E-value: 7.90e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1326 EQVKRNPNQIAVVCNE-KGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPK 1404
Cdd:PRK06087 31 QTARAMPDKIAVVDNHgASYTYSALDHAASRLANWLLAKGIEPGDRVAFQLPGWCEFTIIYLACLKVGAVSVPLLPSWRE 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1405 QRVEYMLTDSGCS-----------------HVLVHQNSIIKGIEF------QGNVIDLMDMSFEEEPGEDmHMMIEPHNL 1461
Cdd:PRK06087 111 AELVWVLNKCQAKmffaptlfkqtrpvdliLPLQNQLPQLQQIVGvdklapATSSLSLSQIIADYEPLTT-AITTHGDEL 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1462 AYVIYTSGSTGQPKGVMIEHrsltNFLCAMYEDFSQDIGIT-DNVLFSSSISFDVTIF--EIFVPLIYGARMTIYQgeKF 1538
Cdd:PRK06087 190 AAVLFTSGTEGLPKGVMLTH----NNILASERAYCARLNLTwQDVFMMPAPLGHATGFlhGVTAPFLIGARSVLLD--IF 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1539 DVTKLVQVILEEQVTLSY-IPP---TLLNEIydyfvrDNQKIVLNKL---LVGVEPIKTELLakyDHLFRGNLQILNGYG 1611
Cdd:PRK06087 264 TPDACLALLEQQRCTCMLgATPfiyDLLNLL------EKQPADLSALrffLCGGTTIPKKVA---RECQQRGIKLLSVYG 334
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1612 PTEAtvccTSYRYESNKEITTQNVPI-GSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTAdKFIDHp 1690
Cdd:PRK06087 335 STES----SPHAVVNLDDPLSRFMHTdGYAAAGVEIKVVDEARKTLPPGCEGEEASRGPNVFMGYLDEPELTA-RALDE- 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1691 fergEKLYKTGDIARWLPDGNIEYLGRvDHQVKIR-GYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKyLCAYVVTE 1768
Cdd:PRK06087 409 ----EGWYYSGDLCRMDEAGYIKITGR-KKDIIVRgGENISSREVEDILLQHPKIHDACVVAMPDErLGER-SCAYVVLK 482
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 446807313 1769 KDIPIP---EVRAYLATK-LPHYMIPQQLIPIHNIPLTQNGKIDRSKLPK 1814
Cdd:PRK06087 483 APHHSLtleEVVAFFSRKrVAKYKYPEHIVVIDKLPRTASGKIQKFLLRK 532
|
|
| PLN02330 |
PLN02330 |
4-coumarate--CoA ligase-like 1 |
1342-1812 |
8.97e-30 |
|
4-coumarate--CoA ligase-like 1
Pssm-ID: 215189 [Multi-domain] Cd Length: 546 Bit Score: 127.02 E-value: 8.97e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1342 KGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAY-----LPIDTDLPKQ----RVEYMLT 1412
Cdd:PLN02330 54 KAVTYGEVVRDTRRFAKALRSLGLRKGQVVVVVLPNVAEYGIVALGIMAAGGVFsganpTALESEIKKQaeaaGAKLIVT 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1413 DS---------GCSHVLVHQNSIIKGIEFQgNVIDLMDMSFEEEPGEDMHMMiephNLAYVIYTSGSTGQPKGVMIEHRS 1483
Cdd:PLN02330 134 NDtnygkvkglGLPVIVLGEEKIEGAVNWK-ELLEAADRAGDTSDNEEILQT----DLCALPFSSGTTGISKGVMLTHRN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1484 LTNFLCAMYedFSQDIGITDNVLFSSSISFdvtiFEIF-VPLIYGARM----TIYQGEKFDVTKLVQVILEEQVTLSYI- 1557
Cdd:PLN02330 209 LVANLCSSL--FSVGPEMIGQVVTLGLIPF----FHIYgITGICCATLrnkgKVVVMSRFELRTFLNALITQEVSFAPIv 282
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1558 PPTLLNEIYDYFVR--DNQKIVLNKLLVGVEPIKTELLAKYDHLFRGnLQILNGYGPTEATvCCTSYRYESNKE--ITTQ 1633
Cdd:PLN02330 283 PPIILNLVKNPIVEefDLSKLKLQAIMTAAAPLAPELLTAFEAKFPG-VQVQEAYGLTEHS-CITLTHGDPEKGhgIAKK 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1634 NvPIGSPLLNTKIYILD-SFHRIQPIGVPGEICISGIGLARGYINRKELTaDKFIDHpfergEKLYKTGDIARWLPDGNI 1712
Cdd:PLN02330 361 N-SVGFILPNLEVKFIDpDTGRSLPKNTPGELCVRSQCVMQGYYNNKEET-DRTIDE-----DGWLHTGDIGYIDDDGDI 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1713 EYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPE--VRAYLATKLPHYMIP 1790
Cdd:PLN02330 434 FIVDRIKELIKYKGFQVAPAELEAILLTHPSVEDAAVVPLPDEEAGEIPAACVVINPKAKESEedILNFVAANVAHYKKV 513
|
490 500
....*....|....*....|..
gi 446807313 1791 QQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PLN02330 514 RVVQFVDSIPKSLSGKIMRRLL 535
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
286-769 |
1.16e-29 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 126.69 E-value: 1.16e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 286 KQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVE 365
Cdd:PRK06178 44 RERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 366 YMLTDSGCSHVLTYQN--SIIKGVAFQGSV----------------------------------INLMDIPfEEEQVEDL 409
Cdd:PRK06178 124 YELNDAGAEVLLALDQlaPVVEQVRAETSLrhvivtsladvlpaeptlplpdslraprlaaagaIDLLPAL-RACTAPVP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 410 QITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTnFLCAMYEDFSQDIGiTDNVLfsssISFdVTIFEI-------FVPLV 482
Cdd:PRK06178 203 LPPPALDALAALNYTGGTTGMPKGCEHTQRDMV-YTAAAAYAVAVVGG-EDSVF----LSF-LPEFWIagenfglLFPLF 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 483 CGARMTIYQgeKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDY-FVRANQKISLNKlfVGVEPIKTELLAKYDHLFR--- 558
Cdd:PRK06178 276 SGATLVLLA--RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHpRFAEYDLSSLRQ--VRVVSFVKKLNPDYRQRWRalt 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 559 GNLQILNLYGPTEATVC--CTSYQYERDKEITTQNVPIGSPLLNTKIYILD-SFHRLQPIGVPGEICISGIGLARGYINR 635
Cdd:PRK06178 352 GSVLAEAAWGMTETHTCdtFTAGFQDDDFDLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGYWNK 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 636 KELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGE 715
Cdd:PRK06178 432 PEATAEALRD-------GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDPDKG 504
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 716 KYLCAYVV--TEKDIPIPEVRAYLATKLPYYMIPqQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK06178 505 QVPVAFVQlkPGADLTAAALQAWCRENMAVYKVP-EIRIVDALPMTATGKVRKQDL 559
|
|
| 4CL |
cd05904 |
4-Coumarate-CoA Ligase (4CL); 4-Coumarate:coenzyme A ligase is a key enzyme in the ... |
1344-1812 |
2.62e-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: 124.65 E-value: 2.62e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYL---PIDT--DLPKQrveymLTDSGCSH 1418
Cdd:cd05904 33 LTYAELERRVRRLAAGLAKRGGRKGDVVLLLSPNSIEFPVAFLAVLSLGAVVTtanPLSTpaEIAKQ-----VKDSGAKL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1419 VLVhQNSIIKGIEFQGNVIDLMD-----------MSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNf 1487
Cdd:cd05904 108 AFT-TAELAEKLASLALPVVLLDsaefdslsfsdLLFEADEAEPPVVVIKQDDVAALLYSSGTTGRSKGVMLTHRNLIA- 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1488 LCAMYEDFSQDIGITDNVLFSSSISFDVTIFEIFV--PLIYGArmTIYQGEKFDVTKLVQVILEEQVT-LSYIPPTLLNE 1564
Cdd:cd05904 186 MVAQFVAGEGSNSDSEDVFLCVLPMFHIYGLSSFAlgLLRLGA--TVVVMPRFDLEELLAAIERYKVThLPVVPPIVLAL 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1565 IYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEATVCCTSyryESNKEitTQNVPIGS----- 1639
Cdd:cd05904 264 VKSPIVDKYDLSSLRQIMSGAAPLGKELIEAFRAKF-PNVDLGQGYGMTESTGVVAM---CFAPE--KDRAKYGSvgrlv 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1640 PLLNTKIYILDSfHRIQPIGVPGEICISGIGLARGYINRKELTAdKFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVD 1719
Cdd:cd05904 338 PNVEAKIVDPET-GESLPPNQTGELWIRGPSIMKGYLNNPEATA-ATID-----KEGWLHTGDLCYIDEDGYLFIVDRLK 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1720 HQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-------TEKdipipEVRAYLATKLPHYMIPQQ 1792
Cdd:cd05904 411 ELIKYKGFQVAPAELEALLLSHPEILDAAVIPYPDEEAGEVPMAFVVrkpgsslTED-----EIMDFVAKQVAPYKKVRK 485
|
490 500
....*....|....*....|
gi 446807313 1793 LIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05904 486 VAFVDAIPKSPSGKILRKEL 505
|
|
| CBAL |
cd05923 |
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) ... |
1320-1812 |
3.45e-29 |
|
4-Chlorobenzoate-CoA ligase (CBAL); CBAL catalyzes the conversion of 4-chlorobenzoate (4-CB) to 4-chlorobenzoyl-coenzyme A (4-CB-CoA) by the two-step adenylation and thioester-forming reactions. 4-Chlorobenzoate (4-CBA) is an environmental pollutant derived from microbial breakdown of aromatic pollutants, such as polychlorinated biphenyls (PCBs), DDT, and certain herbicides. The 4-CBA degrading pathway converts 4-CBA to the metabolite 4-hydroxybezoate (4-HBA), allowing some soil-dwelling microbes to utilize 4-CBA as an alternate carbon source. This pathway consists of three chemical steps catalyzed by 4-CBA-CoA ligase, 4-CBA-CoA dehalogenase, and 4HBA-CoA thioesterase in sequential reactions.
Pssm-ID: 341247 [Multi-domain] Cd Length: 493 Bit Score: 124.16 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKG--ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLP 1397
Cdd:cd05923 3 VFEMLRRAASRAPDACAIADPARGlrLTYSELRARIEAVAARLHARGLRPGQRVAVVLPNSVEAVIALLALHRLGAVPAL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1398 IDTDLPKQRVEYmLTDSGCSHVLVHQN------SIIKG---IEFQGNVIDLMDMSFEEEPGEDMHMmiEPHNLAYVIYTS 1468
Cdd:cd05923 83 INPRLKAAELAE-LIERGEMTAAVIAVdaqvmdAIFQSgvrVLALSDLVGLGEPESAGPLIEDPPR--EPEQPAFVFYTS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1469 GSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGITDNVLFSSSISFDVTIFEIFV-PLIYGArmTIYQGEKFDVTKLVQVI 1547
Cdd:cd05923 160 GTTGLPKGAVIPQRAAESRVLFMSTQAGLRHGRHNVVLGLMPLYHVIGFFAVLVaALALDG--TYVVVEEFDPADALKLI 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1548 LEEQVTLSYIPPTLLNEIYDYFVRDNQKI-VLNKLLVGVEPIKTELLAKYDHLFRGnlQILNGYGPTEAtvcctsYRYES 1626
Cdd:cd05923 238 EQERVTSLFATPTHLDALAAAAEFAGLKLsSLRHVTFAGATMPDAVLERVNQHLPG--EKVNIYGTTEA------MNSLY 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1627 NKEITTQNVpiGSPLLNTKIY---ILDSFHRIQPIGVPGEICISGIGLA--RGYINRKELTADKFIDhpfergeKLYKTG 1701
Cdd:cd05923 310 MRDARTGTE--MRPGFFSEVRivrIGGSPDEALANGEEGELIVAAAADAafTGYLNQPEATAKKLQD-------GWYRTG 380
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1702 DIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLCAYVVTEKDIPIPEVRAY- 1779
Cdd:cd05923 381 DVGYVDPSGDVRILGRVDDMIISGGENIHPSEIERVLSRHPGVTEVVVIGVADERwGQSVTACVVPREGTLSADELDQFc 460
|
490 500 510
....*....|....*....|....*....|...
gi 446807313 1780 LATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05923 461 RASELADFKRPRRYFFLDELPKNAMNKVLRRQL 493
|
|
| AAS_C |
cd05909 |
C-terminal domain of the acyl-acyl carrier protein synthetase (also called ... |
1344-1815 |
1.30e-28 |
|
C-terminal domain of the acyl-acyl carrier protein synthetase (also called 2-acylglycerophosphoethanolamine acyltransferase, Aas); Acyl-acyl carrier protein synthase (Aas) is a membrane protein responsible for a minor pathway of incorporating exogenous fatty acids into membrane phospholipids. Its in vitro activity is characterized by the ligation of free fatty acids between 8 and 18 carbons in length to the acyl carrier protein sulfydryl group (ACP-SH) in the presence of ATP and Mg2+. However, its in vivo function is as a 2-acylglycerophosphoethanolamine (2-acyl-GPE) acyltransferase. The reaction occurs in two steps: the acyl chain is first esterified to acyl carrier protein (ACP) via a thioester bond, followed by a second step where the acyl chain is transferred to a 2-acyllysophospholipid, thus completing the transacylation reaction. This model represents the C-terminal domain of the enzyme, which belongs to the class I adenylate-forming enzyme family, including acyl-CoA synthetases.
Pssm-ID: 341235 [Multi-domain] Cd Length: 490 Bit Score: 122.44 E-value: 1.30e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDqGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:cd05909 8 LTYRKLLTGAIALARKLAK-MTKEGENVGVMLPPSAGGALANFALALSGKVPVMLNYTAGLRELRACIKLAGIKTVLTSK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 NSIIKG-------IEFQGNVIDLMDM----SFEEEPGEDMHMMI--------------EPHNLAYVIYTSGSTGQPKGVM 1478
Cdd:cd05909 87 QFIEKLklhhlfdVEYDARIVYLEDLrakiSKADKCKAFLAGKFppkwllrifgvapvQPDDPAVILFTSGSEGLPKGVV 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1479 IEHRSL-TN-FLCAMYEDFSQDigitDNVL----FSSSISFDVTifeIFVPLIYGARMTIYQgEKFDVTKLVQVILEEQV 1552
Cdd:cd05909 167 LSHKNLlANvEQITAIFDPNPE----DVVFgalpFFHSFGLTGC---LWLPLLSGIKVVFHP-NPLDYKKIPELIYDKKA 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1553 TLSYIPPTLLNeIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATVCCTSYRYESNKEITT 1632
Cdd:cd05909 239 TILLGTPTFLR-GYARAAHPEDFSSLRLVVAGAEKLKDTLRQEFQEKF--GIRILEGYGTTECSPVISVNTPQSPNKEGT 315
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1633 QNVPIgsPLLNTKIYILDSfHRIQPIGVPGEICISGIGLARGYINRKELTAdkfidhpFERGEKLYKTGDIARWLPDGNI 1712
Cdd:cd05909 316 VGRPL--PGMEVKIVSVET-HEEVPIGEGGLLLVRGPNVMLGYLNEPELTS-------FAFGDGWYDTGDIGKIDGEGFL 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1713 EYLGRVDHQVKIRGYRIELGEIEASLLKYETIKT--AVVIDQEDEAGEKYLCayVVTEKDIPIPEVRAYL-ATKLPHYMI 1789
Cdd:cd05909 386 TITGRLSRFAKIAGEMVSLEAIEDILSEILPEDNevAVVSVPDGRKGEKIVL--LTTTTDTDPSSLNDILkNAGISNLAK 463
|
490 500
....*....|....*....|....*.
gi 446807313 1790 PQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:cd05909 464 PSYIHQVEEIPLLGTGKPDYVTLKAL 489
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
288-769 |
1.99e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 122.35 E-value: 1.99e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 288 NPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYM 367
Cdd:PRK08316 24 YPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEELAYI 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 368 LTDSGCSHVLT----YQNS----------------IIKGVAFQGSVINLMDIpFEEEQVEDLQITMEPQNLAYVIYTSGS 427
Cdd:PRK08316 104 LDHSGARAFLVdpalAPTAeaalallpvdtlilslVLGGREAPGGWLDFADW-AEAGSVAEPDVELADDDLAQILYTSGT 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 428 TGQPKGVMIEHRSLtnflcaMYEDFSQ----DIGITDNVLFS----SSISFDVtifeIFVPLV-CGARMTIYQGEkfDVP 498
Cdd:PRK08316 183 ESLPKGAMLTHRAL------IAEYVSCivagDMSADDIPLHAlplyHCAQLDV----FLGPYLyVGATNVILDAP--DPE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 499 KLVQVILEEQVTLAYIPPT----LLNeiYDYFVRANQKiSLNKLFVG-----VEPIKtELLAKYDhlfrgNLQILNLYGP 569
Cdd:PRK08316 251 LILRTIEAERITSFFAPPTvwisLLR--HPDFDTRDLS-SLRKGYYGasimpVEVLK-ELRERLP-----GLRFYNCYGQ 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 570 TE----ATVCctsyqyeRDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFID 645
Cdd:PRK08316 322 TEiaplATVL-------GPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAEAFRG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 646 HPFErgeklykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVT- 724
Cdd:PRK08316 395 GWFH-------SGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAVVVPk 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*.
gi 446807313 725 -EKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK08316 468 aGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKILKREL 513
|
|
| PRK06839 |
PRK06839 |
o-succinylbenzoate--CoA ligase; |
1325-1817 |
2.48e-28 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 168698 [Multi-domain] Cd Length: 496 Bit Score: 121.89 E-value: 2.48e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1325 EEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLP 1403
Cdd:PRK06839 9 EKRAYLHPDRIAIITEEEEMTYKQLHEYVSKVAAYLIYElNVKKGERIAILSQNSLEYIVLLFAIAKVECIAVPLNIRLT 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1404 KQRVEYMLTDSGCSHVLV---HQNSI--IKGIEFQGNVIDLMDMSFE--------EEPGEDMHMMIephnlayvIYTSGS 1470
Cdd:PRK06839 89 ENELIFQLKDSGTTVLFVektFQNMAlsMQKVSYVQRVISITSLKEIedrkidnfVEKNESASFII--------CYTSGT 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1471 TGQPKGVMIEHRSLtnFLCAMYEDFSQDIGITDnvlfsSSISFdVTIFEI-------FVPLIYGARMTIyqGEKFDVTKL 1543
Cdd:PRK06839 161 TGKPKGAVLTQENM--FWNALNNTFAIDLTMHD-----RSIVL-LPLFHIggiglfaFPTLFAGGVIIV--PRKFEPTKA 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1544 VQVILEEQVTLSYIPPTL---LNEIYDYFVRDNQKIVLnkLLVGVEPIKTELLAKYDHlfRGnLQILNGYGPTEA--TVC 1618
Cdd:PRK06839 231 LSMIEKHKVTVVMGVPTIhqaLINCSKFETTNLQSVRW--FYNGGAPCPEELMREFID--RG-FLFGQGFGMTETspTVF 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1619 CTSyryesnKEITTQNV-PIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFErgekl 1697
Cdd:PRK06839 306 MLS------EEDARRKVgSIGKPVLFCDYELIDENKNKVEVGEVGELLIRGPNVMKEYWNRPDATEETIQDGWLC----- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1698 ykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPE-- 1775
Cdd:PRK06839 375 --TGDLARVDEDGFVYIVGRKKEMIISGGENIYPLEVEQVINKLSDVYEVAVVGRQHVKWGEIPIAFIVKKSSSVLIEkd 452
|
490 500 510 520
....*....|....*....|....*....|....*....|..
gi 446807313 1776 VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLNT 1817
Cdd:PRK06839 453 VIEHCRLFLAKYKIPKEIVFLKELPKNATGKIQKAQLVNQLK 494
|
|
| Thioesterase |
pfam00975 |
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of ... |
1921-2157 |
3.85e-28 |
|
Thioesterase domain; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 395776 [Multi-domain] Cd Length: 223 Bit Score: 114.41 E-value: 3.85e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1921 FIIHGQGGGILNYYDLARELGEDKTVYGLQSIGYDDSRFPNLSVEEMAVRYIEEIKQVKKEGPYTLLGWSFGGIVAFEMA 2000
Cdd:pfam00975 4 FCFPPAGGSASSFRSLARRLPPPAEVLAVQYPGRGRGEPPLNSIEALADEYAEALRQIQPEGPYALFGHSMGGMLAFEVA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 2001 RKLEELGDKVSFLGLLDVHPIEQGREILSLNIKNAfEELEKFNDQLGIEKISFEqmseeqlIESLLKKFtlnenscqqnf 2080
Cdd:pfam00975 84 RRLERQGEAVRSLFLSDASAPHTVRYEASRAPDDD-EVVAEFTDEGGTPEELLE-------DEELLSML----------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 2081 edpmmnkLKVMIANRYAYLKYNCKQKIKADIFLFNASINDIHPLVDYNRWNE-YTSGEVYALQVPGSHLSMLEKP----- 2154
Cdd:pfam00975 145 -------LPALRADYRALESYSCPPLDAQSATLFYGSDDPLHDADDLAEWVRdHTPGEFDVHVFDGDHFYLIEHLeavle 217
|
...
gi 446807313 2155 HIH 2157
Cdd:pfam00975 218 IIE 220
|
|
| PRK08316 |
PRK08316 |
acyl-CoA synthetase; Validated |
1328-1807 |
7.32e-28 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181381 [Multi-domain] Cd Length: 523 Bit Score: 120.81 E-value: 7.32e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1328 VKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRV 1407
Cdd:PRK08316 21 ARRYPDKTALVFGDRSWTYAELDAAVNRVAAALLDLGLKKGDRVAALGHNSDAYALLWLACARAGAVHVPVNFMLTGEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1408 EYMLTDSGCSHVLV----------------HQNSI----IKGIEFQGNVIDLMDMSFEEEPGE-DMHMMIEphNLAYVIY 1466
Cdd:PRK08316 101 AYILDHSGARAFLVdpalaptaeaalallpVDTLIlslvLGGREAPGGWLDFADWAEAGSVAEpDVELADD--DLAQILY 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1467 TSGSTGQPKGVMIEHRSLtnflcaMYEDFSQ----DIGITDNVLFS----SSISFDVtifeIFVPLIY-GARMTIYQGEk 1537
Cdd:PRK08316 179 TSGTESLPKGAMLTHRAL------IAEYVSCivagDMSADDIPLHAlplyHCAQLDV----FLGPYLYvGATNVILDAP- 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1538 fDVTKLVQVILEEQVTLSYIPPT----LLNEIyDYFVRDNQKivLNKLLVG-----VEPIKtELLAKYDhlfrgNLQILN 1608
Cdd:PRK08316 248 -DPELILRTIEAERITSFFAPPTvwisLLRHP-DFDTRDLSS--LRKGYYGasimpVEVLK-ELRERLP-----GLRFYN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1609 GYGPTE----ATVCctsyryeSNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTAD 1684
Cdd:PRK08316 318 CYGQTEiaplATVL-------GPEEHLRRPGSAGRPVLNVETRVVDDDGNDVAPGEVGEIVHRSPQLMLGYWDDPEKTAE 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1685 KFIDHPFErgeklykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAY 1764
Cdd:PRK08316 391 AFRGGWFH-------SGDLGVMDEEGYITVVDRKKDMIKTGGENVASREVEEALYTHPAVAEVAVIGLPDPKWIEAVTAV 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446807313 1765 VVT--EKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:PRK08316 464 VVPkaGATVTEDELIAHCRARLAGFKVPKRVIFVDELPRNPSGKI 508
|
|
| MACS_AAE_MA_like |
cd05970 |
Medium-chain acyl-CoA synthetase (MACS) of AAE_MA like; MACS catalyzes the two-step activation ... |
286-766 |
9.96e-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: 120.29 E-value: 9.96e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 286 KQNPNQIAIV-CNG----KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:cd05970 28 KEYPDKLALVwCDDageeRIFTFAELADYSDKTANFFKAMGIGKGDTVMLTLKRRYEFWYSLLALHKLGAIAIPATHQLT 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 361 KQRVEYMLTDSGCSHVLTYQNSII-----KGVAFQGSVINL-------MD--IPFEEEqVEDLQITMEP---------QN 417
Cdd:cd05970 108 AKDIVYRIESADIKMIVAIAEDNIpeeieKAAPECPSKPKLvwvgdpvPEgwIDFRKL-IKNASPDFERptansypcgED 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 418 LAYVIYTSGSTGQPKgvMIEHR---SLTNFLCAMYedfSQDIGITDNVLFSSSISFDVTIF-EIFVPLVCGARMTIYQGE 493
Cdd:cd05970 187 ILLVYFSSGTTGMPK--MVEHDftyPLGHIVTAKY---WQNVREGGLHLTVADTGWGKAVWgKIYGQWIAGAAVFVYDYD 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 494 KFDVPKLVQVILEEQVTLAYIPPTllneIYDYFVRAN-QKISLNKL---FVGVEPIKTELLAKYDHLfrGNLQILNLYGP 569
Cdd:cd05970 262 KFDPKALLEKLSKYGVTTFCAPPT----IYRFLIREDlSRYDLSSLrycTTAGEALNPEVFNTFKEK--TGIKLMEGFGQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 570 TEATVCCTSYQYERDKEITtqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICIS-----GIGLARGYINRKELTADKFI 644
Cdd:cd05970 336 TETTLTIATFPWMEPKPGS-----MGKPAPGYEIDLIDREGRSCEAGEEGEIVIRtskgkPVGLFGGYYKDAEKTAEVWH 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 645 DhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVT 724
Cdd:cd05970 411 D-------GYYHTGDAAWMDEDGYLWFVGRTDDLIKSSGYRIGPFEVESALIQHPAVLECAVTGVPDPIRGQVVKATIVL 483
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446807313 725 EKDIP-----IPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:cd05970 484 AKGYEpseelKKELQDHVKKVTAPYKYPRIVEFVDELPKTISGKIRR 530
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
415-769 |
1.24e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 120.09 E-value: 1.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 415 PQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFS--QDIgitdNVLFSSSISFDVTIFeiFVP-LVCGArmTIYQ 491
Cdd:PRK06188 167 PPDIAGLAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEwpADP----RFLMCTPLSHAGGAF--FLPtLLRGG--TVIV 238
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 492 GEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDY-FVRANQKISLNKLFVGVEPIKTELLAKYDHLFrGNLqILNLYGPT 570
Cdd:PRK06188 239 LAKFDPAEVLRAIEEQRITATFLVPTMIYALLDHpDLRTRDLSSLETVYYGASPMSPVRLAEAIERF-GPI-FAQYYGQT 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 571 EATVcCTSYQYERDKEITTQNV--PIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidhpf 648
Cdd:PRK06188 317 EAPM-VITYLRKRDHDPDDPKRltSCGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF----- 390
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 649 eRGEKLYkTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTEKD 727
Cdd:PRK06188 391 -RDGWLH-TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwGEA-VTAVVVLRPG 467
|
330 340 350 360
....*....|....*....|....*....|....*....|....
gi 446807313 728 IPI--PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK06188 468 AAVdaAELQAHVKERKGSVHAPKQVDFVDSLPLTALGKPDKKAL 511
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
1332-1812 |
5.85e-27 |
|
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: 117.40 E-value: 5.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVHQnsiikgiEFQGN-VIDLMDMSFEEEPGEDMHMMIEphnlayVIYTSGSTGQPKGVMIEHRSLtnFLCA 1490
Cdd:cd12118 98 RHSEAKVLFVDR-------EFEYEdLLAEGDPDFEWIPPADEWDPIA------LNYTSGTTGRPKGVVYHHRGA--YLNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1491 MyedfsqdigitDNVLFSSSISFDVTIFEI---------FVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTL 1561
Cdd:cd12118 163 L-----------ANILEWEMKQHPVYLWTLpmfhcngwcFPWTVAAVGGTNVCLRKVDAKAIYDLIEKHKVTHFCGAPTV 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1562 LNEIYDYFVRDNQKI--VLNKLLVGVEPIKTeLLAKYDHLfrgNLQILNGYGPTE----ATVCctSYRYESNKEITT--- 1632
Cdd:cd12118 232 LNMLANAPPSDARPLphRVHVMTAGAPPPAA-VLAKMEEL---GFDVTHVYGLTEtygpATVC--AWKPEWDELPTEera 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1633 -----QNVPIgspLLNTKIYILDSfHRIQPigVP------GEICISGIGLARGYINRKELTADKFidhpfeRGeKLYKTG 1701
Cdd:cd12118 306 rlkarQGVRY---VGLEEVDVLDP-ETMKP--VPrdgktiGEIVFRGNIVMKGYLKNPEATAEAF------RG-GWFHSG 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1702 DIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYV-------VTEKDIpi 1773
Cdd:cd12118 373 DLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKwGEV-PCAFVelkegakVTEEEI-- 449
|
490 500 510
....*....|....*....|....*....|....*....
gi 446807313 1774 pevRAYLATKLPHYMIPQQLIPIHnIPLTQNGKIDRSKL 1812
Cdd:cd12118 450 ---IAFCREHLAGFMVPKTVVFGE-LPKTSTGKIQKFVL 484
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
283-769 |
8.24e-27 |
|
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: 116.66 E-value: 8.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 283 EQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGayLPIdTELPKQ 362
Cdd:cd05920 23 RSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPV-LALPSH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 363 RveymltdsgcSHVLTYQNSIIKGVAFQGS-VINLMDipFEEEQVEDLQITMEPqnlAYVIYTSGSTGQPKGVMIEHRSL 441
Cdd:cd05920 100 R----------RSELSAFCAHAEAVAYIVPdRHAGFD--HRALARELAESIPEV---ALFLLSGGTTGTPKLIPRTHNDY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 442 ----------------TNFLCAMyedfsqdiGITDNVLFSSSISFDVtifeifvpLVCGARMTIYQ----GEKFDVpklv 501
Cdd:cd05920 165 aynvrasaevcgldqdTVYLAVL--------PAAHNFPLACPGVLGT--------LLAGGRVVLAPdpspDAAFPL---- 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 502 qvILEEQVTLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVEPIKTELLAKYDHLFRGNLQilNLYGPTEATVCCTSYQ 580
Cdd:cd05920 225 --IEREGVTVTALVPALVSLWLDAAASRRADLsSLRLLQVGGARLSPALARRVPPVLGCTLQ--QVFGMAEGLLNYTRLD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 581 YERDKEITTQNVPIgSPllNTKIYILDSFHRLQPIGVPGEICISGIGLARGYI-----NRKELTADKFidhpfergeklY 655
Cdd:cd05920 301 DPDEVIIHTQGRPM-SP--DDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYrapehNARAFTPDGF-----------Y 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 656 KTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVV-TEKDIPIPEV 733
Cdd:cd05920 367 RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGER-SCAFVVlRDPPPSAAQL 445
|
490 500 510
....*....|....*....|....*....|....*..
gi 446807313 734 RAYL-ATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05920 446 RRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| PRK06145 |
PRK06145 |
acyl-CoA synthetase; Validated |
286-769 |
9.76e-27 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 102207 [Multi-domain] Cd Length: 497 Bit Score: 116.91 E-value: 9.76e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 286 KQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVE 365
Cdd:PRK06145 13 RRTPDRAALVYRDQEISYAEFHQRILQAAGMLHARGIGQGDVVALLMKNSAAFLELAFAASYLGAVFLPINYRLAADEVA 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 366 YMLTDSGCSHVLTYQN----------SIIKGVAFQGSVINLMDIPFEEEQvedlQITMEPQNLAYVIYTSGSTGQPKGVM 435
Cdd:PRK06145 93 YILGDAGAKLLLVDEEfdaivaletpKIVIDAAAQADSRRLAQGGLEIPP----QAAVAPTDLVRLMYTSGTTDRPKGVM 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 436 IehrSLTNFlcaMYEDFSQDI--GIT-DNVLFSSSISFDVTIFEI--FVPLVCGARMTIYQgeKFDVPKLVQVILEEQVT 510
Cdd:PRK06145 169 H---SYGNL---HWKSIDHVIalGLTaSERLLVVGPLYHVGAFDLpgIAVLWVGGTLRIHR--EFDPEAVLAAIERHRLT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 511 LAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVEPIKTELLAKYDHLFRGNlQILNLYGPTEAtvCCTSYQYERDKEITT 589
Cdd:PRK06145 241 CAWMAPVMLSRVLTVPDRDRFDLdSLAWCIGGGEKTPESRIRDFTRVFTRA-RYIDAYGLTET--CSGDTLMEAGREIEK 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 590 qnvpIGS---PLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPD 666
Cdd:PRK06145 318 ----IGStgrALAHVEIRIADGAGRWLPPNMKGEICMRGPKVTKGYWKDPEKTAEAFYGDWF-------RSGDVGYLDEE 386
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 667 GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-QREDESGEKYLCAYVVTE-KDIPIPEVRAYLATKLPYY 744
Cdd:PRK06145 387 GFLYLTDRKKDMIISGGENIASSEVERVIYELPEVAEAAVIgVHDDRWGERITAVVVLNPgATLTLEALDRHCRQRLASF 466
|
490 500
....*....|....*....|....*
gi 446807313 745 MIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK06145 467 KVPRQLKVRDELPRNPSGKVLKRVL 491
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
1320-1812 |
1.08e-26 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 117.44 E-value: 1.08e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:PRK06710 26 LHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVIGYYGTLLAGGIVVQTN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSGC----------------------SHVLV--------------------HQNSIIKGIEfQGNVI 1437
Cdd:PRK06710 106 PLYTERELEYQLHDSGAkvilcldlvfprvtnvqsatkiEHVIVtriadflpfpknllypfvqkKQSNLVVKVS-ESETI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1438 DLMDmSFEEEPGEDMHMMIEPHN-LAYVIYTSGSTGQPKGVMIEHRSL-TNFLCAMYEDFsqdigitdNVLFSSSISFDV 1515
Cdd:PRK06710 185 HLWN-SVEKEVNTGVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLY--------NCKEGEEVVLGV 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1516 TIFEIFVPLIYGARMTIYQG------EKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDY-FVRDNQKIVLNKLLVGVEPI 1588
Cdd:PRK06710 256 LPFFHVYGMTAVMNLSIMQGykmvliPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSpLLKEYDISSIRACISGSAPL 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1589 KTELLAKYDHLFRGNLqiLNGYGPTEAT-VCCTSYRYEsnkeittQNVP--IGSPLLNTKIYI--LDSFHRIQPiGVPGE 1663
Cdd:PRK06710 336 PVEVQEKFETVTGGKL--VEGYGLTESSpVTHSNFLWE-------KRVPgsIGVPWPDTEAMImsLETGEALPP-GEIGE 405
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1664 ICISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYET 1743
Cdd:PRK06710 406 IVVKGPQIMKGYWNKPEETAAVLQD-------GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNVYPREVEEVLYEHEK 478
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1744 IKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPE------VRAYLATklphYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK06710 479 VQEVVTIGVPDPYRGETVKAFVVLKEGTECSEeelnqfARKYLAA----YKVPKVYEFRDELPKTTVGKILRRVL 549
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
268-766 |
1.11e-26 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 117.57 E-value: 1.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 268 KTLLCETVtaPQLFEEQVKQNPNQIAIVC--NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGI 345
Cdd:PRK12583 13 KPLLTQTI--GDAFDATVARFPDREALVVrhQALRYTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFAT 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 346 LKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLT--------YQN---SIIKGVAFQGS-------------VINL----- 396
Cdd:PRK12583 91 ARIGAILVNINPAYRASELEYALGQSGVRWVICadafktsdYHAmlqELLPGLAEGQPgalacerlpelrgVVSLapapp 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 397 ------MDIPFEEEQV--EDL---QITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTN--FLCAmyedfsQDIGITDnvl 463
Cdd:PRK12583 171 pgflawHELQARGETVsrEALaerQASLDRDDPINIQYTSGTTGFPKGATLSHHNILNngYFVA------ESLGLTE--- 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 464 fSSSISFDVTIFEIF----VPLVC---GARMtIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANqkISLN 536
Cdd:PRK12583 242 -HDRLCVPVPLYHCFgmvlANLGCmtvGACL-VYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGN--FDLS 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 537 KLFVGV---EPIKTELLAK-YDHLFRGNLQILnlYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIyiLDSFHRL 612
Cdd:PRK12583 318 SLRTGImagAPCPIEVMRRvMDEMHMAEVQIA--YGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKV--VDPDGAT 393
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 613 QPIGVPGEICISGIGLARGYINRKELTAdKFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVkIRG-YRIELGEI 691
Cdd:PRK12583 394 VPRGEIGELCTRGYSVMKGYWNNPEATA-ESID-----EDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGgENIYPREI 466
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 692 EASLLKYETIKTAVVIQREDES-GEKyLCAYVVTE--KDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:PRK12583 467 EEFLFTHPAVADVQVFGVPDEKyGEE-IVAWVRLHpgHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQK 543
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
1324-1812 |
1.17e-26 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 117.08 E-value: 1.17e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNEKG------ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLP 1397
Cdd:PRK13295 30 LDACVASCPDKTAVTAVRLGtgaprrFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNP 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1398 IDTDLPKQRVEYMLTDSGCSHVLVHQnsIIKGIEFQGNVIDLM----------------DMSFEE-------EPGEDMHM 1454
Cdd:PRK13295 110 LMPIFRERELSFMLKHAESKVLVVPK--TFRGFDHAAMARRLRpelpalrhvvvvggdgADSFEAllitpawEQEPDAPA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1455 MIE-----PHNLAYVIYTSGSTGQPKGVMieHRSltNFLCAMYEDFSQDIGIT-DNVLFSSSISFDVT--IFEIFVPLIY 1526
Cdd:PRK13295 188 ILArlrpgPDDVTQLIYTSGTTGEPKGVM--HTA--NTLMANIVPYAERLGLGaDDVILMASPMAHQTgfMYGLMMPVML 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1527 GARMtIYQgEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYfVRDNQKIV--LNKLLVGVEPIKTELLAKYDHLFrgNL 1604
Cdd:PRK13295 264 GATA-VLQ-DIWDPARAAELIRTEGVTFTMASTPFLTDLTRA-VKESGRPVssLRTFLCAGAPIPGALVERARAAL--GA 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1605 QILNGYGPTE-ATVCCTSYRYESNKEITTQnvpiGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTA 1683
Cdd:PRK13295 339 KIVSAWGMTEnGAVTLTKLDDPDERASTTD----GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1684 DKFidhpfergEKLYKTGDIARWLPDGNIEYLGRvDHQVKIRG-YRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyL 1761
Cdd:PRK13295 415 TDA--------DGWFDTGDLARIDADGYIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPDERlGER-A 484
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446807313 1762 CAYVVTE--KDIPIPEVRAYL-ATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK13295 485 CAFVVPRpgQSLDFEEMVEFLkAQKVAKQYIPERLVVRDALPRTPSGKIQKFRL 538
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
301-766 |
2.01e-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: 114.92 E-value: 2.01e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 301 ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyq 380
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSGARLVVT-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 381 nsiikgvafqgsvinlmDIPFEEEQVEDLQITMepqnlayviYTSGSTGQPKGVMIEHRSLTNFlcAMYEDFSQDIGITD 460
Cdd:cd05973 79 -----------------DAANRHKLDSDPFVMM---------FTSGTTGLPKGVPVPLRALAAF--GAYLRDAVDLRPED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 461 NVLFSSSISFDVTIF-EIFVPLVCGARMTIYQGeKFDVPKLVQVILEEQVTLAYIPPTllneIYDYF------VRANQKI 533
Cdd:cd05973 131 SFWNAADPGWAYGLYyAITGPLALGHPTILLEG-GFSVESTWRVIERLGVTNLAGSPT----AYRLLmaagaeVPARPKG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 534 SLNKLFVGVEPIKTELLakydHLFRGNL--QILNLYGPTE-ATVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILDSFH 610
Cdd:cd05973 206 RLRRVSSAGEPLTPEVI----RWFDAALgvPIHDHYGQTElGMVLANHHALEHPVHAGS----AGRAMPGWRVAVLDDDG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 611 RLQPIGVPGEICI----SGIGLARGYINRKELTADKfidhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 686
Cdd:cd05973 278 DELGPGEPGRLAIdianSPLMWFRGYQLPDTPAIDG----------GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 687 ELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-TEKDIPIPEVRAYLA----TKLPYYMIPQQIISIQNIPLTQN 761
Cdd:cd05973 348 GPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlRGGHEGTPALADELQlhvkKRLSAHAYPRTIHFVDELPKTPS 427
|
....*
gi 446807313 762 GKIDR 766
Cdd:cd05973 428 GKIQR 432
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
302-769 |
2.70e-26 |
|
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: 115.81 E-value: 2.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 302 TYKQLNIKANQLARRLLDQGVKREFIVGVMM---ERSIEMIVGILGIlkagGAYL-PIDTELPKQRVEYMLTDSGcSHVL 377
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAwntHRHLELYYAVPGM----GAVLhTINPRLFPEQIAYIINHAE-DRVV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 378 TYQNSI------IKG--------VAFQGSVINLMDIPFEEEQVEDLQITMEP--------QNLAYVI-YTSGSTGQPKGV 434
Cdd:cd12119 102 FVDRDFlplleaIAPrlptvehvVVMTDDAAMPEPAGVGVLAYEELLAAESPeydwpdfdENTAAAIcYTSGTTGNPKGV 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 435 MIEHRSLtnFLCAMyedfsqDIGITDNVLFSSSISF--DVTIFEI------FVPLVCGARMtIYQGEKFDVPKLVQVILE 506
Cdd:cd12119 182 VYSHRSL--VLHAM------AALLTDGLGLSESDVVlpVVPMFHVnawglpYAAAMVGAKL-VLPGPYLDPASLAELIER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 507 EQVTLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVEPIKTELLAKYDHLFrgnLQILNLYGPTEATVCCTSYQY---- 581
Cdd:cd12119 253 EGVTFAAGVPTVWQGLLDHLEANGRDLsSLRRVVIGGSAVPRSLIEAFEERG---VRVIHAWGMTETSPLGTVARPpseh 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 582 ------ERDKEITTQNVPIgsPLLNTKIYILDSfhrlqpIGVP------GEICISGIGLARGYINRKELTADKFIDHPFe 649
Cdd:cd12119 330 snlsedEQLALRAKQGRPV--PGVELRIVDDDG------RELPwdgkavGELQVRGPWVTKSYYKNDEESEALTEDGWL- 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 650 rgeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLcAYVV----- 723
Cdd:cd12119 401 ------RTGDVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKwGERPL-AVVVlkega 473
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446807313 724 --TEKdipipEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd12119 474 tvTAE-----ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
1323-1812 |
2.92e-26 |
|
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: 116.01 E-value: 2.92e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGayLPIDTdL 1402
Cdd:COG1021 30 LLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPVFA-L 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQR-------------VEYMLTD------------------SGCSHVLVHQNSiikgiefqGNVIDLMDMsfEEEPGED 1451
Cdd:COG1021 107 PAHRraeishfaeqseaVAYIIPDrhrgfdyralarelqaevPSLRHVLVVGDA--------GEFTSLDAL--LAAPADL 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1452 MHMMIEPHNLAYVIYTSGSTGQPKGVMIEHR----SL------------TNFLCAMyedfsqdiGITDN----------- 1504
Cdd:COG1021 177 SEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDdylySVrasaeicgldadTVYLAAL--------PAAHNfplsspgvlgv 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 ------VLFSSSISFDvTIFeifvPLIygARmtiyqgEKFDVTKLVqvileeqvtlsyiPPTLLN-----EIYDYFVRDn 1573
Cdd:COG1021 249 lyaggtVVLAPDPSPD-TAF----PLI--ER------ERVTVTALV-------------PPLALLwldaaERSRYDLSS- 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1574 qkivLNKLLVG--------VEPIKTELLAKYDHLFrgnlqilngyGPTEATVCCTsyRYESNKEI--TTQNVPIgSPLln 1643
Cdd:COG1021 302 ----LRVLQVGgaklspelARRVRPALGCTLQQVF----------GMAEGLVNYT--RLDDPEEVilTTQGRPI-SPD-- 362
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1644 TKIYILDSFHRIQPIGVPGEICISGIGLARGY-----INRKELTADKFidhpfergeklYKTGDIARWLPDGNIEYLGRV 1718
Cdd:COG1021 363 DEVRIVDEDGNPVPPGEVGELLTRGPYTIRGYyrapeHNARAFTPDGF-----------YRTGDLVRRTPDGYLVVEGRA 431
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1719 DHQVkIR-GYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVT-EKDIPIPEVRAYLATK-LPHYMIPQQLI 1794
Cdd:COG1021 432 KDQI-NRgGEKIAAEEVENLLLAHPAVHDAAVVAMPDEYlGER-SCAFVVPrGEPLTLAELRRFLRERgLAAFKLPDRLE 509
|
570
....*....|....*...
gi 446807313 1795 PIHNIPLTQNGKIDRSKL 1812
Cdd:COG1021 510 FVDALPLTAVGKIDKKAL 527
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
1340-1771 |
3.61e-26 |
|
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA synthetases, including an Arabidopsis gene At4g14070 that plays a role in activation and elongation of exogenous fatty acids. FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Eukaryotes generally have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341295 [Multi-domain] Cd Length: 468 Bit Score: 114.76 E-value: 3.61e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1340 NEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCShV 1419
Cdd:cd17640 2 PPKRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV-A 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1420 LVHQNSiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDI 1499
Cdd:cd17640 81 LVVEND--------------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQP 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1500 GitDNVL------FSSSISFDVTIFEIFVPLIYGARMTIyqgeKFDVTKLVQVILeeqVTLSYIPPTLLNEIYDYFVRDN 1573
Cdd:cd17640 129 G--DRFLsilpiwHSYERSAEYFIFACGCSQAYTSIRTL----KDDLKRVKPHYI---VSVPRLWESLYSGIQKQVSKSS 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1574 --QKIVLNKLLVGVEpIKTEL-----LAKY-DHLFRG-NLQILNGYGPTEATVCCTSYRYESNKEITtqnvpIGSPLLNT 1644
Cdd:cd17640 200 piKQFLFLFFLSGGI-FKFGIsgggaLPPHvDTFFEAiGIEVLNGYGLTETSPVVSARRLKCNVRGS-----VGRPLPGT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1645 KIYILDSFHR-IQPIGVPGEICISGIGLARGYINRKELTAdKFIDHpfergEKLYKTGDIARWLPDGNIEYLGRV-DHQV 1722
Cdd:cd17640 274 EIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATS-KVLDS-----DGWFNTGDLGWLTCGGELVLTGRAkDTIV 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 446807313 1723 KIRGYRIELGEIEASLLKYETIKTAVVIDQEdeagEKYLCAYVVTEKDI 1771
Cdd:cd17640 348 LSNGENVEPQPIEEALMRSPFIEQIMVVGQD----QKRLGALIVPNFEE 392
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
297-769 |
4.70e-26 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 115.08 E-value: 4.70e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 297 NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGA-------YLPidTELPKQrveymLT 369
Cdd:PLN02246 47 TGRVYTYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttanpfYTP--AEIAKQ-----AK 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 370 DSGCSHVLTYQNSI--IKGVAFQGSV-INLMDIPFE------------EEQVEDLQItmEPQNLAYVIYTSGSTGQPKGV 434
Cdd:PLN02246 120 ASGAKLIITQSCYVdkLKGLAEDDGVtVVTIDDPPEgclhfseltqadENELPEVEI--SPDDVVALPYSSGTTGLPKGV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 435 MIEHRSLTNflcamyeDFSQDI-GITDNVLFSSSisfDVTI-----FEIFV---PLVCGARM--TIYQGEKFDVPKLVQV 503
Cdd:PLN02246 198 MLTHKGLVT-------SVAQQVdGENPNLYFHSD---DVILcvlpmFHIYSlnsVLLCGLRVgaAILIMPKFEIGALLEL 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 504 ILEEQVTLA-YIPPTLLNEIYDYFVRANQKISLNKLFVGVEPIKTELlakyDHLFRGNLQILNL---YGPTEA-TVCCTS 578
Cdd:PLN02246 268 IQRHKVTIApFVPPIVLAIAKSPVVEKYDLSSIRMVLSGAAPLGKEL----EDAFRAKLPNAVLgqgYGMTEAgPVLAMC 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 579 YQYErdKE-ITTQNVPIGSPLLNTKIYILD-----SFHRLQPigvpGEICISGIGLARGYINRKELTAdKFIDHpfergE 652
Cdd:PLN02246 344 LAFA--KEpFPVKSGSCGTVVRNAELKIVDpetgaSLPRNQP----GEICIRGPQIMKGYLNDPEATA-NTIDK-----D 411
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 653 KLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPE 732
Cdd:PLN02246 412 GWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNGSEITE 491
|
490 500 510
....*....|....*....|....*....|....*....
gi 446807313 733 --VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PLN02246 492 deIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| 23DHB-AMP_lg |
cd05920 |
2,3-dihydroxybenzoate-AMP ligase; 2,3-dihydroxybenzoate-AMP ligase activates 2, ... |
1326-1812 |
5.03e-26 |
|
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: 114.35 E-value: 5.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1326 EQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGayLPIDTdLPKQ 1405
Cdd:cd05920 23 RSAARHPDRIAVVDGDRRLTYRELDRRADRLAAGLRGLGIRPGDRVVVQLPNVAEFVVLFFALLRLGA--VPVLA-LPSH 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1406 R---VEYMLTDSGCSHVLVHqnsiikgiefqgnvidlmDMSFEEEPGEDMHMMIEPHN-LAYVIYTSGSTGQPKGVMIEH 1481
Cdd:cd05920 100 RrseLSAFCAHAEAVAYIVP------------------DRHAGFDHRALARELAESIPeVALFLLSGGTTGTPKLIPRTH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1482 RSL----------------TNFLCAMyedfsqdiGITDNVLFSSSISFDVtifeifvpLIYGARMTIYQ-GEKFDVTKLV 1544
Cdd:cd05920 162 NDYaynvrasaevcgldqdTVYLAVL--------PAAHNFPLACPGVLGT--------LLAGGRVVLAPdPSPDAAFPLI 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1545 QvilEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLL-VGVEPIKTELLAKYDHLFRGNLQILngYGPTEATVCCTSYR 1623
Cdd:cd05920 226 E---REGVTVTALVPALVSLWLDAAASRRADLSSLRLLqVGGARLSPALARRVPPVLGCTLQQV--FGMAEGLLNYTRLD 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1624 YESNKEITTQNVPIgSPllNTKIYILDSFHRIQPIGVPGEICISGIGLARGYI-----NRKELTADKFidhpfergeklY 1698
Cdd:cd05920 301 DPDEVIIHTQGRPM-SP--DDEIRVVDEEGNPVPPGEEGELLTRGPYTIRGYYrapehNARAFTPDGF-----------Y 366
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1699 KTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVV-TEKDIPIPEV 1776
Cdd:cd05920 367 RTGDLVRRTPDGYLVVEGRIKDQINRGGEKIAAEEVENLLLRHPAVHDAAVVAMPDELlGER-SCAFVVlRDPPPSAAQL 445
|
490 500 510
....*....|....*....|....*....|....*..
gi 446807313 1777 RAYL-ATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05920 446 RRFLrERGLAAYKLPDRIEFVDSLPLTAVGKIDKKAL 482
|
|
| ttLC_FACS_AEE21_like |
cd12118 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles and Arabidopsis; This ... |
289-769 |
5.41e-26 |
|
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: 114.32 E-value: 5.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:cd12118 18 PDRTSIVYGDRRYTWRQTYDRCRRLASALAALGISRGDTVAVLAPNTPAMYELHFGVPMAGAVLNALNTRLDAEEIAFIL 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGCSHVLTYQnsiikgvAFQG-SVINLMDIPFEEEQVEDlqitmEPQNLAyVIYTSGSTGQPKGVMIEHRSLtnFLCA 447
Cdd:cd12118 98 RHSEAKVLFVDR-------EFEYeDLLAEGDPDFEWIPPAD-----EWDPIA-LNYTSGTTGRPKGVVYHHRGA--YLNA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 448 MyedfsqdigitDNVLFSSSISFDV--TIFEIF----------VPLVCGarmTIYQGEKFDVPKLVQVILEEQVTLAYIP 515
Cdd:cd12118 163 L-----------ANILEWEMKQHPVylWTLPMFhcngwcfpwtVAAVGG---TNVCLRKVDAKAIYDLIEKHKVTHFCGA 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 516 PTLLNEIYDYFVRANQKIS--LNKLFVGVEPIKTeLLAKYDHLfrgNLQILNLYGPTE----ATVCCTSYQY------ER 583
Cdd:cd12118 229 PTVLNMLANAPPSDARPLPhrVHVMTAGAPPPAA-VLAKMEEL---GFDVTHVYGLTEtygpATVCAWKPEWdelpteER 304
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 584 DKEITTQNVPIgspLLNTKIYILDSfHRLQPigVP------GEICISGIGLARGYINRKELTADKFidhpfeRGeKLYKT 657
Cdd:cd12118 305 ARLKARQGVRY---VGLEEVDVLDP-ETMKP--VPrdgktiGEIVFRGNIVMKGYLKNPEATAEAF------RG-GWFHS 371
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 658 GDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYV-------VTEKDIp 729
Cdd:cd12118 372 GDLAVIHPDGYIEIKDRSKDIIISGGENISSVEVEGVLYKHPAVLEAAVVARPDEKwGEV-PCAFVelkegakVTEEEI- 449
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446807313 730 ipevRAYLATKLPYYMIPQQIIsIQNIPLTQNGKIDRKKL 769
Cdd:cd12118 450 ----IAFCREHLAGFMVPKTVV-FGELPKTSTGKIQKFVL 484
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
415-769 |
6.80e-26 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 117.33 E-value: 6.80e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 415 PQNLAYVIYTSGSTGQPKGVMIEHRS-LTNFlcamyEDFSQDIGIT--DNVL----FSSSISFDVTifeIFVPLVCGARM 487
Cdd:PRK08633 781 PDDTATIIFSSGSEGEPKGVMLSHHNiLSNI-----EQISDVFNLRndDVILsslpFFHSFGLTVT---LWLPLLEGIKV 852
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 488 tIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNeIYDYFVRANQKI--SLNKLFVGVEPIKTELLAKYDHLFrgNLQILN 565
Cdd:PRK08633 853 -VYHPDPTDALGIAKLVAKHRATILLGTPTFLR-LYLRNKKLHPLMfaSLRLVVAGAEKLKPEVADAFEEKF--GIRILE 928
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 566 LYGPTEAT-VCCTSYQYERDKEITTQ----NVPIGSPLLNTKIYILD--SFHRLqPIGVPGEICISGIGLARGYINRKEL 638
Cdd:PRK08633 929 GYGATETSpVASVNLPDVLAADFKRQtgskEGSVGMPLPGVAVRIVDpeTFEEL-PPGEDGLILIGGPQVMKGYLGDPEK 1007
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 639 TAD--KFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY---ETIKTAVVIQREDES 713
Cdd:PRK08633 1008 TAEviKDID-----GIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKAlggEEVVFAVTAVPDEKK 1082
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 714 GEKylCAYVVTEKDIPIPEVRAYLA-TKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK08633 1083 GEK--LVVLHTCGAEDVEELKRAIKeSGLPNLWKPSRYFKVEALPLLGSGKLDLKGL 1137
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
1332-1808 |
1.09e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 114.21 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:PRK07798 17 PDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNVNYRYVEDELRYLL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGcSHVLVHQNS-----------------IIK-----GIEFQGNVIDLMDM--------SFEEEPGEDMhmmiephnl 1461
Cdd:PRK07798 97 DDSD-AVALVYEREfaprvaevlprlpklrtLVVvedgsGNDLLPGAVDYEDAlaagsperDFGERSPDDL--------- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1462 aYVIYTSGSTGQPKGVMIEH----RSLTNFLCAMYEDFSQDI-GITDNVLFSSSisfdvTIFEIFVPLIYGARMT----- 1531
Cdd:PRK07798 167 -YLLYTGGTTGMPKGVMWRQedifRVLLGGRDFATGEPIEDEeELAKRAAAGPG-----MRRFPAPPLMHGAGQWaafaa 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1532 --------IYQGEKFDVTKLVQVILEEQVTLSYI-------PptLLNEI-----YDyfvrdnqkivLNKLLV----GV-- 1585
Cdd:PRK07798 241 lfsgqtvvLLPDVRFDADEVWRTIEREKVNVITIvgdamarP--LLDALeargpYD----------LSSLFAiasgGAlf 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1586 -EPIKTELLakyDHLfrGNLQILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSpllNTKIyILDSFHRIQP-IGVPGE 1663
Cdd:PRK07798 309 sPSVKEALL---ELL--PNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGP---RTVV-LDEDGNPVEPgSGEIGW 379
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1664 ICISG-IGLarGYINRKELTADKFidhPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYE 1742
Cdd:PRK07798 380 IARRGhIPL--GYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVEEALKAHP 454
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1743 TIKTAVVIDQEDEAGEKYLCAyVVTEKDIPIP---EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:PRK07798 455 DVADALVVGVPDERWGQEVVA-VVQLREGARPdlaELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| EntE |
COG1021 |
EntE, 2,3-dihydroxybenzoate-AMP synthase component of non-ribosomal peptide synthetase ... |
276-769 |
1.43e-25 |
|
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: 113.70 E-value: 1.43e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 276 TAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGayLPI 355
Cdd:COG1021 26 TLGDLLRRRAERHPDRIAVVDGERRLSYAELDRRADRLAAGLLALGLRPGDRVVVQLPNVAEFVIVFFALFRAGA--IPV 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 356 DTeLPKQR-------------VEYMLTD---------------SGCSHVltyQNSIIKGVAfqGSVINLMDIPfeEEQVE 407
Cdd:COG1021 104 FA-LPAHRraeishfaeqseaVAYIIPDrhrgfdyralarelqAEVPSL---RHVLVVGDA--GEFTSLDALL--AAPAD 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 408 DLQITMEPQNLAYVIYTSGSTGQPKGVMIEHR----SL------------TNFLCAMyedfsqdiGITDNVLFSSsisfd 471
Cdd:COG1021 176 LSEPRPDPDDVAFFQLSGGTTGLPKLIPRTHDdylySVrasaeicgldadTVYLAAL--------PAAHNFPLSS----- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 472 vtiFEIFVPLVCGARMTIYQGEKFDVpkLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVG--------V 542
Cdd:COG1021 243 ---PGVLGVLYAGGTVVLAPDPSPDT--AFPLIERERVTVTALVPPLALLWLDAAERSRYDLsSLRVLQVGgaklspelA 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 543 EPIKTELLAKydhlfrgnLQilNLYGPTEATVCCTSYQYERDKEITTQNVPIgSPLlnTKIYILDSFHRLQPIGVPGEIC 622
Cdd:COG1021 318 RRVRPALGCT--------LQ--QVFGMAEGLVNYTRLDDPEEVILTTQGRPI-SPD--DEVRIVDEDGNPVPPGEVGELL 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 623 ISGIGLARGY-----INRKELTADKFidhpfergeklYKTGDIARWLPDGNIEYLGRVDHQVkIR-GYRIELGEIEASLL 696
Cdd:COG1021 385 TRGPYTIRGYyrapeHNARAFTPDGF-----------YRTGDLVRRTPDGYLVVEGRAKDQI-NRgGEKIAAEEVENLLL 452
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 697 KYETIKTAVVIQREDES-GEKyLCAYVVT-EKDIPIPEVRAYLATK-LPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:COG1021 453 AHPAVHDAAVVAMPDEYlGER-SCAFVVPrGEPLTLAELRRFLRERgLAAFKLPDRLEFVDALPLTAVGKIDKKAL 527
|
|
| FUM14_C_NRPS-like |
cd19545 |
Condensation domains of nonribosomal peptide synthetases (NRPSs) similar to the ester-bond ... |
870-1285 |
1.48e-25 |
|
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: 111.62 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 870 QEYYLASTSQkrmfivdqfedgTNTTYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSF-QILDGELVQKIEPNVDF 948
Cdd:cd19545 8 QEGLMALTAR------------QPGAYVGQRVFELPPDIDLARLQAAWEQVVQANPILRTRIvQSDSGGLLQVVVKESPI 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 949 NIEYVHVNEkdaDYLIHEFISPFDLSKPPLLRVLLLRIAEERHiLVVDMHHIISDGLSMGILIKEFVELYKGNELPKlRV 1028
Cdd:cd19545 76 SWTESTSLD---EYLEEDRAAPMGLGGPLVRLALVEDPDTERY-FVWTIHHALYDGWSLPLILRQVLAAYQGEPVPQ-PP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1029 QYKDYVmwqngPYYKNLISEQ-KNYWLTTLKGELPVlNFPTdFQRPTIQSFKGNVCSFNLgtdltfkVNKLATETGTTPY 1107
Cdd:cd19545 151 PFSRFV-----KYLRQLDDEAaAEFWRSYLAGLDPA-VFPP-LPSSRYQPRPDATLEHSI-------SLPSSASSGVTLA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1108 MILLAIYNILLSRYTGQEDIIVGSPIAGRSH--SDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLNTLEAyenqdYP 1185
Cdd:cd19545 217 TVLRAAWALVLSRYTGSDDVVFGVTLSGRNApvPGIEQIVGPTIATVPLRVRIDPEQSVEDFLQTVQKDLLDM-----IP 291
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1186 FEELleGL----DLHRDTSRNPLFDTMFVFQ-----------NMDMNPISIGELEFTPYPfkqsvskfdLSLVATEIDNN 1250
Cdd:cd19545 292 FEHT--GLqnirRLGPDARAACNFQTLLVVQpalpsstseslELGIEEESEDLEDFSSYG---------LTLECQLSGSG 360
|
410 420 430
....*....|....*....|....*....|....*
gi 446807313 1251 IHLKVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19545 361 LRVRARYDSSVISEEQVERLLDQFEHVLQQLASAP 395
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
1327-1812 |
1.79e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 112.98 E-value: 1.79e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1327 QVKRNPNQIAVVCNEKGI--TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPK 1404
Cdd:PRK09088 4 HARLQPQRLAAVDLALGRrwTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1405 QRVEYMLTDSGcSHVLVHQNSIIKGIEFQGNVIDLMDMSFEEEPgeDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSL 1484
Cdd:PRK09088 84 SELDALLQDAE-PRLLLGDDAVAAGRTDVEDLAAFIASADALEP--ADTPSIPPERVSLILFTSGTSGQPKGVMLSERNL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1485 ----TNFlcamyedfsqdiGITDNVLFSSSISFDVTIFEIfVPLIYGARMTIYQGEkfdvTKLVQVILEEQVTLSYIP-P 1559
Cdd:PRK09088 161 qqtaHNF------------GVLGRVDAHSSFLCDAPMFHI-IGLITSVRPVLAVGG----SILVSNGFEPKRTLGRLGdP 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TLlnEIYDYF--------VRDNQKIV------LNKLLVGVEP-IKTELLAKYDHlfrgNLQILNGYGPTEA------TVC 1618
Cdd:PRK09088 224 AL--GITHYFcvpqmaqaFRAQPGFDaaalrhLTALFTGGAPhAAEDILGWLDD----GIPMVDGFGMSEAgtvfgmSVD 297
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1619 CTSYRYESNkeittqNVPIGSPLLNTKIyiLDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEKLY 1698
Cdd:PRK09088 298 CDVIRAKAG------AAGIPTPTVQTRV--VDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1699 KTGDIARWLPDGnieYLGRVDHQVKI---RGYRIELGEIEASLLKYETIKTAVVIDQED-EAGEKYLCAYVVTEKDIPIP 1774
Cdd:PRK09088 364 RTGDIARRDADG---FFWVVDRKKDMfisGGENVYPAEIEAVLADHPGIRECAVVGMADaQWGEVGYLAIVPADGAPLDL 440
|
490 500 510
....*....|....*....|....*....|....*....
gi 446807313 1775 E-VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK09088 441 ErIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| Ac_CoA_lig_AcsA |
TIGR02188 |
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called ... |
284-769 |
1.99e-25 |
|
acetate--CoA ligase; This model describes acetate-CoA ligase (EC 6.2.1.1), also called acetyl-CoA synthetase and acetyl-activating enzyme. It catalyzes the reaction ATP + acetate + CoA = AMP + diphosphate + acetyl-CoA and belongs to the family of AMP-binding enzymes described by pfam00501.
Pssm-ID: 274022 [Multi-domain] Cd Length: 626 Bit Score: 114.27 E-value: 1.99e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 284 QVKQNPNQIAIVCNG------KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILG------------- 344
Cdd:TIGR02188 66 HLEARPDKVAIIWEGdepgevRKITYRELHREVCRFANVLKSLGVKKGDRVAIYMPMIPEAAIAMLAcarigaihsvvfg 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 345 ----------ILKA-------------GGAYLPIdtelpKQRVEYMLTDSGCS--HVLTYQNSIIKGVAFQGSvinlMDI 399
Cdd:TIGR02188 146 gfsaealadrINDAgaklvitadeglrGGKVIPL-----KAIVDEALEKCPVSveHVLVVRRTGNPVVPWVEG----RDV 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 400 PFEEEqVEDLQITMEPQNLA-----YVIYTSGSTGQPKGVMieHRSLTNFLCAMY----------EDF---SQDIG-ITD 460
Cdd:TIGR02188 217 WWHDL-MAKASAYCEPEPMDsedplFILYTSGSTGKPKGVL--HTTGGYLLYAAMtmkyvfdikdGDIfwcTADVGwITG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 461 NvlfsSSIsfdvtifeIFVPLVCGARMTIYQGekfdVP------KLVQVILEEQVTLAYIPPT---LLNEIYDYFVRANQ 531
Cdd:TIGR02188 294 H----SYI--------VYGPLANGATTVMFEG----VPtypdpgRFWEIIEKHKVTIFYTAPTairALMRLGDEWVKKHD 357
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 532 KISLNKL-FVGvEPIKTELLAKYDHLFrgnlqilnlyGPTEATVCCTSYQYERDKEITTqnvPI--------GS---PLL 599
Cdd:TIGR02188 358 LSSLRLLgSVG-EPINPEAWMWYYKVV----------GKERCPIVDTWWQTETGGIMIT---PLpgatptkpGSatlPFF 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 600 NTKIYILD-SFHRLQPIGVPGEICISGI--GLARGYINRKEltadKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVD 676
Cdd:TIGR02188 424 GIEPAVVDeEGNPVEGPGEGGYLVIKQPwpGMLRTIYGDHE----RFVDTYFSPFPGYYFTGDGARRDKDGYIWITGRVD 499
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 677 HQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPI-----PEVRAYLATKLPYYMIPQQII 751
Cdd:TIGR02188 500 DVINVSGHRLGTAEIESALVSHPAVAEAAVVGIPDDIKGQAIYAFVTLKDGYEPddelrKELRKHVRKEIGPIAKPDKIR 579
|
570
....*....|....*...
gi 446807313 752 SIQNIPLTQNGKIDRKKL 769
Cdd:TIGR02188 580 FVPGLPKTRSGKIMRRLL 597
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
277-767 |
2.20e-25 |
|
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This uncharacterized acyl-CoA synthetase family (EC 6.2.1.16, or acetoacetate#CoA ligase or acetoacetate:CoA ligase (AMP-forming)) is highly homologous to acetoacetyl-CoA synthetase. However, the proteins in this family exist in only bacteria and archaea. AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms.
Pssm-ID: 341272 [Multi-domain] Cd Length: 610 Bit Score: 113.74 E-value: 2.20e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 277 APQLFEEQVKQNPNQIAIVCNG-----KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGA 351
Cdd:cd05968 63 VEQLLDKWLADTRTRPALRWEGedgtsRTLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGGI 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 352 YLPIDTELPKQRVEYMLTDSG--------------------------CSHVLTYQNSIIK---GVAFQGSVINLMDIPFE 402
Cdd:cd05968 143 VVPIFSGFGKEAAATRLQDAEakalitadgftrrgrevnlkeeadkaCAQCPTVEKVVVVrhlGNDFTPAKGRDLSYDEE 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 403 EEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHrslTNFLCAMYED--FSQDIGITDNVLFSSSISFDVTIFEIFVP 480
Cdd:cd05968 223 KETAGDGAERTESEDPLMIIYTSGTTGKPKGTVHVH---AGFPLKAAQDmyFQFDLKPGDLLTWFTDLGWMMGPWLIFGG 299
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 481 LVCGARMTIYQG-EKFDVP-KLVQVILEEQVTLAYIPPTLLNEIY---DYFVRANQKISLNKLFVGVEPIKTE-LLAKYD 554
Cdd:cd05968 300 LILGATMVLYDGaPDHPKAdRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGEPWNPEpWNWLFE 379
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 555 HLFRGNLQILNLYGPTEAT---VCCtsYQYERDKEITtqnvpIGSPLLNTKIYILDSfhRLQPI-GVPGEICISG--IGL 628
Cdd:cd05968 380 TVGKGRNPIINYSGGTEISggiLGN--VLIKPIKPSS-----FNGPVPGMKADVLDE--SGKPArPEVGELVLLApwPGM 450
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 629 ARGYInRKEltaDKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQ 708
Cdd:cd05968 451 TRGFW-RDE---DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLESAAIG 526
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 709 REDE-SGEKYLCaYVVTEKDI-PIP----EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRK 767
Cdd:cd05968 527 VPHPvKGEAIVC-FVVLKPGVtPTEalaeELMERVADELGKPLSPERILFVKDLPKTRNAKVMRR 590
|
|
| PRK07798 |
PRK07798 |
acyl-CoA synthetase; Validated |
276-765 |
4.31e-25 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236100 [Multi-domain] Cd Length: 533 Bit Score: 112.29 E-value: 4.31e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 276 TAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI 355
Cdd:PRK07798 4 NIADLFEAVADAVPDRVALVCGDRRLTYAELEERANRLAHYLIAQGLGPGDHVGIYARNRIEYVEAMLGAFKARAVPVNV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 356 DTELPKQRVEYMLTDSGcSHVLTYQNSIIKGVA----------------------FQGSVINLMDI--------PFEEEQ 405
Cdd:PRK07798 84 NYRYVEDELRYLLDDSD-AVALVYEREFAPRVAevlprlpklrtlvvvedgsgndLLPGAVDYEDAlaagsperDFGERS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 406 VEDLqitmepqnlaYVIYTSGSTGQPKGVMIEH----RSLTNFLCAMYEDFSQDI-GITDNVLFS-SSISFDV------- 472
Cdd:PRK07798 163 PDDL----------YLLYTGGTTGMPKGVMWRQedifRVLLGGRDFATGEPIEDEeELAKRAAAGpGMRRFPApplmhga 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 473 TIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTL------AYIPPtLLNEI-----YDyfvranqkisLNKLFV- 540
Cdd:PRK07798 233 GQWAAFAALFSGQTVVLLPDVRFDADEVWRTIEREKVNVitivgdAMARP-LLDALeargpYD----------LSSLFAi 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 541 ---GV---EPIKTELLakyDHLfrGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSpllNTKIyILDSFHRLQP 614
Cdd:PRK07798 302 asgGAlfsPSVKEALL---ELL--PNVVLTDSIGSSETGFGGSGTVAKGAVHTGGPRFTIGP---RTVV-LDEDGNPVEP 372
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 615 -IGVPGEICISG-IGLarGYINRKELTADKFidhPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE 692
Cdd:PRK07798 373 gSGEIGWIARRGhIPL--GYYKDPEKTAETF---PTIDGVRYAIPGDRARVEADGTITLLGRGSVCINTGGEKVFPEEVE 447
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 693 ASLLKYETIKTAVVIQREDESGEKYLCAyVVTEKDIPIP---EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:PRK07798 448 EALKAHPDVADALVVGVPDERWGQEVVA-VVQLREGARPdlaELRAHCRSSLAGYKVPRAIWFVDEVQRSPAGKAD 522
|
|
| Condensation |
pfam00668 |
Condensation domain; This domain is found in many multi-domain enzymes which synthesize ... |
7-257 |
5.14e-25 |
|
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: 110.89 E-value: 5.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:pfam00668 182 LQQYLQSEDYQKDAAYWLEQLEGELPVLQLPKDYARPADRSFKGDRLSFTLDEDTEELLRKLAKAHGTTLNDVLLAAYGL 261
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 87 LLSRYTDKDDVVIGMPVfkQGQEETVFQN------NFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLS 160
Cdd:pfam00668 262 LLSRYTGQDDIVVGTPG--SGRPSPDIERmvgmfvNTLPLRIDPKGGKTFSELIKRVQEDLLSAEPHQGYPFGDLVNDLR 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 161 LDGESNNLPLLNTIVMLD---------DIHcYESTDKINSDMVIRFMKN----------EEQLKVQVDYNSTLYSEGLVS 221
Cdd:pfam00668 340 LPRDLSRHPLFDPMFSFQnylgqdsqeEEF-QLSELDLSVSSVIEEEAKydlsltaserGGGLTIKIDYNTSLFDEETIE 418
|
250 260 270
....*....|....*....|....*....|....*.
gi 446807313 222 RIVNHLYNILDILMKDPNKSAMDLDVMPKTEKNQIL 257
Cdd:pfam00668 419 RFAEHFKELLEQAIAHPSQPLSELDLLSDAEKQKLL 454
|
|
| PRK06710 |
PRK06710 |
long-chain-fatty-acid--CoA ligase; Validated |
261-769 |
7.08e-25 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 180666 [Multi-domain] Cd Length: 563 Bit Score: 112.05 E-value: 7.08e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 261 NHTTRVHKTLLCETVTAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIV 340
Cdd:PRK06710 10 SYPEEIPSTISYDIQPLHKYVEQMASRYPEKKALHFLGKDITFSVFHDKVKRFANYLQKLGVEKGDRVAIMLPNCPQAVI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 341 GILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSIIKGVAFQGS-------VINLMD-IPF----------- 401
Cdd:PRK06710 90 GYYGTLLAGGIVVQTNPLYTERELEYQLHDSGAKVILCLDLVFPRVTNVQSAtkiehviVTRIADfLPFpknllypfvqk 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 402 ---------------------EEEQVEDLQITMEPQN-LAYVIYTSGSTGQPKGVMIEHRSL-TNFLCAMYEDFsqdigi 458
Cdd:PRK06710 170 kqsnlvvkvsesetihlwnsvEKEVNTGVEVPCDPENdLALLQYTGGTTGFPKGVMLTHKNLvSNTLMGVQWLY------ 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 459 tdNVLFSSSISFDVTIFEIFVPLVCGARMTIYQG------EKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQK 532
Cdd:PRK06710 244 --NCKEGEEVVLGVLPFFHVYGMTAVMNLSIMQGykmvliPKFDMKMVFEAIKKHKVTLFPGAPTIYIALLNSPLLKEYD 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 533 I-SLNKLFVGVEPIKTELLAKYDHLFRGNLqiLNLYGPTEAT-VCCTSYQYERdkeittqNVP--IGSPLLNTKIYI--L 606
Cdd:PRK06710 322 IsSIRACISGSAPLPVEVQEKFETVTGGKL--VEGYGLTESSpVTHSNFLWEK-------RVPgsIGVPWPDTEAMImsL 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 607 DSFHRLQPiGVPGEICISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 686
Cdd:PRK06710 393 ETGEALPP-GEIGEIVVKGPQIMKGYWNKPEETAAVLQD-------GWLHTGDVGYMDEDGFFYVKDRKKDMIVASGFNV 464
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 687 ELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPE------VRAYLATklpyYMIPQQIISIQNIPLTQ 760
Cdd:PRK06710 465 YPREVEEVLYEHEKVQEVVTIGVPDPYRGETVKAFVVLKEGTECSEeelnqfARKYLAA----YKVPKVYEFRDELPKTT 540
|
....*....
gi 446807313 761 NGKIDRKKL 769
Cdd:PRK06710 541 VGKILRRVL 549
|
|
| PRK12583 |
PRK12583 |
acyl-CoA synthetase; Provisional |
1324-1812 |
7.90e-25 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 237145 [Multi-domain] Cd Length: 558 Bit Score: 111.79 E-value: 7.90e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNEKGI--TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTD 1401
Cdd:PRK12583 24 FDATVARFPDREALVVRHQALryTWRQLADAVDRLARGLLALGVQPGDRVGIWAPNCAEWLLTQFATARIGAILVNINPA 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1402 LPKQRVEYMLTDSGCSHVLVHQNsiIKGIEFQGNVIDLMDMSFEEEPGEDMH-----------MMIE--PHNLAY----- 1463
Cdd:PRK12583 104 YRASELEYALGQSGVRWVICADA--FKTSDYHAMLQELLPGLAEGQPGALACerlpelrgvvsLAPAppPGFLAWhelqa 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 ------------------------VIYTSGSTGQPKGVMIEHRSLTN--FLCAmyedfsQDIGITDnvlfSSSISFDVTI 1517
Cdd:PRK12583 182 rgetvsrealaerqasldrddpinIQYTSGTTGFPKGATLSHHNILNngYFVA------ESLGLTE----HDRLCVPVPL 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 FEIF-------VPLIYGARMtIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKivLNKLLVGV---EP 1587
Cdd:PRK12583 252 YHCFgmvlanlGCMTVGACL-VYPNEAFDPLATLQAVEEERCTALYGVPTMFIAELDHPQRGNFD--LSSLRTGImagAP 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1588 IKTELLAK-YDHLFRGNLQIlnGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNTKIyiLDSFHRIQPIGVPGEICI 1666
Cdd:PRK12583 329 CPIEVMRRvMDEMHMAEVQI--AYGMTETSPVSLQTTAADDLERRVETVGRTQPHLEVKV--VDPDGATVPRGEIGELCT 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1667 SGIGLARGYINRKELTAdKFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVkIRG-YRIELGEIEASLLKYETIK 1745
Cdd:PRK12583 405 RGYSVMKGYWNNPEATA-ESID-----EDGWMHTGDLATMDEQGYVRIVGRSKDMI-IRGgENIYPREIEEFLFTHPAVA 477
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1746 TAVVIDQEDEA-GEKyLCAYVVTE--KDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK12583 478 DVQVFGVPDEKyGEE-IVAWVRLHpgHAASEEELREFCKARIAHFKVPRYFRFVDEFPMTVTGKVQKFRM 546
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
298-781 |
8.96e-25 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 111.47 E-value: 8.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 298 GKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYL---PIDTELP-KQRVeymltdSG 372
Cdd:PLN02574 64 GFSISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTtmnPSSSLGEiKKRV------VD 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 373 CSHVLTYQ--NSIIKGVAFQGSVINLMD-----------IPFEEEQVEDLQITMEP----QNLAYVIYTSGSTGQPKGVM 435
Cdd:PLN02574 138 CSVGLAFTspENVEKLSPLGVPVIGVPEnydfdskriefPKFYELIKEDFDFVPKPvikqDDVAAIMYSSGTTGASKGVV 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 436 IEHRsltNFLcAMYEDF-----SQ-DIGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQV 509
Cdd:PLN02574 218 LTHR---NLI-AMVELFvrfeaSQyEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKV 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 510 T-LAYIPPTLLNEIYDY-FVRANQKISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEATVCCT-SYQYERDKE 586
Cdd:PLN02574 294 ThFPVVPPILMALTKKAkGVCGEVLKSLKQVSCGAAPLSGKFIQDFVQTL-PHVDFIQGYGMTESTAVGTrGFNTEKLSK 372
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 587 ITTqnVPIGSPLLNTKIYILDSFHRLQPiGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLPD 666
Cdd:PLN02574 373 YSS--VGLLAPNMQAKVVDWSTGCLLPP-GNCGELWIQGPGVMKGYLNNPKATQSTIDK------DGWLRTGDIAYFDED 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 667 GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPE--VRAYLATKLPYY 744
Cdd:PLN02574 444 GYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQeaVINYVAKQVAPY 523
|
490 500 510
....*....|....*....|....*....|....*..
gi 446807313 745 MIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSSHL 781
Cdd:PLN02574 524 KKVRKVVFVQSIPKSPAGKILRRELKRSLTNSVSSRL 560
|
|
| PRK06188 |
PRK06188 |
acyl-CoA synthetase; Validated |
1328-1812 |
1.16e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235731 [Multi-domain] Cd Length: 524 Bit Score: 110.85 E-value: 1.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1328 VKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPI------DTD 1401
Cdd:PRK06188 22 LKRYPDRPALVLGDTRLTYGQLADRISRYIQAFEALGLGTGDAVALLSLNRPEVLMAIGAAQLAGLRRTALhplgslDDH 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1402 LpkqrveYMLTDSGCSHVLVHQN-------------SIIKGIEFQGNVIDLMDM-----SFEEEPGEDMHmmiEPHNLAY 1463
Cdd:PRK06188 102 A------YVLEDAGISTLIVDPApfveralallarvPSLKHVLTLGPVPDGVDLlaaaaKFGPAPLVAAA---LPPDIAG 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 VIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFS--QDIgitdNVLFSSSISFDVTIFeiFVP-LIYGArmTIYQGEKFDV 1540
Cdd:PRK06188 173 LAYTGGTTGKPKGVMGTHRSIATMAQIQLAEWEwpADP----RFLMCTPLSHAGGAF--FLPtLLRGG--TVIVLAKFDP 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1541 TKLVQVILEEQVTLSYIPPTLLNEIYDY-FVRDNQKIVLNKLLVGVEPIK----TELLAKYDHLFrgnLQIlngYGPTEA 1615
Cdd:PRK06188 245 AEVLRAIEEQRITATFLVPTMIYALLDHpDLRTRDLSSLETVYYGASPMSpvrlAEAIERFGPIF---AQY---YGQTEA 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1616 TVCCTsyrYESNKEITTQNVPI----GSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFidhpf 1691
Cdd:PRK06188 319 PMVIT---YLRKRDHDPDDPKRltscGRPTPGLRVALLDEDGREVAQGEVGEICVRGPLVMDGYWNRPEETAEAF----- 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1692 eRGEKLYkTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVTEKD 1770
Cdd:PRK06188 391 -RDGWLH-TGDVAREDEDGFYYIVDRKKDMIVTGGFNVFPREVEDVLAEHPAVAQVAVIGVPDEKwGEA-VTAVVVLRPG 467
|
490 500 510 520
....*....|....*....|....*....|....*....|....*
gi 446807313 1771 IPI--PEVRAYL-ATKLPHYMiPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK06188 468 AAVdaAELQAHVkERKGSVHA-PKQVDFVDSLPLTALGKPDKKAL 511
|
|
| PRK08633 |
PRK08633 |
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated |
1461-1815 |
1.22e-24 |
|
2-acyl-glycerophospho-ethanolamine acyltransferase; Validated
Pssm-ID: 236315 [Multi-domain] Cd Length: 1146 Bit Score: 113.10 E-value: 1.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPKGVMIEHRS-LTNFlcamyEDFSQDIGIT--DNVL----FSSSISFDVTifeIFVPLIYGARMtIY 1533
Cdd:PRK08633 784 TATIIFSSGSEGEPKGVMLSHHNiLSNI-----EQISDVFNLRndDVILsslpFFHSFGLTVT---LWLPLLEGIKV-VY 854
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1534 QGEKFDVTKLVQVILEEQVTLSYIPPTLLNeIYdyfVRdNQKI------VLNKLLVGVEPIKTELLAKYDHLFrgNLQIL 1607
Cdd:PRK08633 855 HPDPTDALGIAKLVAKHRATILLGTPTFLR-LY---LR-NKKLhplmfaSLRLVVAGAEKLKPEVADAFEEKF--GIRIL 927
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1608 NGYGPTE----ATVCCTSYRYESNKEIT-TQNVPIGSPLLNTKIYILD--SFHRIqPIGVPGEICISGIGLARGYINRKE 1680
Cdd:PRK08633 928 EGYGATEtspvASVNLPDVLAADFKRQTgSKEGSVGMPLPGVAVRIVDpeTFEEL-PPGEDGLILIGGPQVMKGYLGDPE 1006
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1681 LTAD--KFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLK--YETIKTAVVIDQEDEA 1756
Cdd:PRK08633 1007 KTAEviKDID-----GIGWYVTGDKGHLDEDGFLTITDRYSRFAKIGGEMVPLGAVEEELAKalGGEEVVFAVTAVPDEK 1081
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1757 -GEKylCAYVVTEKDIPIPEVRAYLA-TKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK08633 1082 kGEK--LVVLHTCGAEDVEELKRAIKeSGLPNLWKPSRYFKVEALPLLGSGKLDLKGLKEL 1140
|
|
| PRK06178 |
PRK06178 |
acyl-CoA synthetase; Validated |
1329-1815 |
1.26e-24 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235724 [Multi-domain] Cd Length: 567 Bit Score: 111.29 E-value: 1.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1329 KRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVE 1408
Cdd:PRK06178 44 RERPQRPAIIFYGHVITYAELDELSDRFAALLRQRGVGAGDRVAVFLPNCPQFHIVFFGILKLGAVHVPVSPLFREHELS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1409 YMLTDSGCShVLVHQNSIIKGIE-------------------------------------FQGNVIDLMDmSFEEEPGED 1451
Cdd:PRK06178 124 YELNDAGAE-VLLALDQLAPVVEqvraetslrhvivtsladvlpaeptlplpdslraprlAAAGAIDLLP-ALRACTAPV 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1452 MHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTnFLCAMYEDFSQDIGiTDNVLfsssISFdVTIFEI-------FVPL 1524
Cdd:PRK06178 202 PLPPPALDALAALNYTGGTTGMPKGCEHTQRDMV-YTAAAAYAVAVVGG-EDSVF----LSF-LPEFWIagenfglLFPL 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1525 IYGARMTIYQgeKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDY--FVRDNqkivLNKL-LVGVEPIKTELLAKYDHLFR 1601
Cdd:PRK06178 275 FSGATLVLLA--RWDAVAFMAAVERYRVTRTVMLVDNAVELMDHprFAEYD----LSSLrQVRVVSFVKKLNPDYRQRWR 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1602 ---GNLQILNGYGPTEATVC--CTSYRYESNKEITTQNVPIGSPLLNTKIYILD-SFHRIQPIGVPGEICISGIGLARGY 1675
Cdd:PRK06178 349 altGSVLAEAAWGMTETHTCdtFTAGFQDDDFDLLSQPVFVGLPVPGTEFKICDfETGELLPLGAEGEIVVRTPSLLKGY 428
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1676 INRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE 1755
Cdd:PRK06178 429 WNKPEATAEALRD-------GWLHTGDIGKIDEQGFLHYLGRRKEMLKVNGMSVFPSEVEALLGQHPAVLGSAVVGRPDP 501
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1756 AGEKYLCAYVV--TEKDIPIPEVRAYLATKLPHYMIPQQLIpIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK06178 502 DKGQVPVAFVQlkPGADLTAAALQAWCRENMAVYKVPEIRI-VDALPMTATGKVRKQDLQAL 562
|
|
| ttLC_FACS_AlkK_like |
cd12119 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1345-1812 |
1.37e-24 |
|
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: 110.41 E-value: 1.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQN 1424
Cdd:cd12119 27 TYAEVAERARRLANALRRLGVKPGDRVATLAWNTHRHLELYYAVPGMGAVLHTINPRLFPEQIAYIINHAEDRVVFVDRD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 --SIIKGIE-----FQGNVIDLMDMSFEEEPGEDMHM---MIEPH-----------NLAYVI-YTSGSTGQPKGVMIEHR 1482
Cdd:cd12119 107 flPLLEAIAprlptVEHVVVMTDDAAMPEPAGVGVLAyeeLLAAEspeydwpdfdeNTAAAIcYTSGTTGNPKGVVYSHR 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1483 SLtnFLCAMyedfsqDIGITDNVLFSSSisfDVtiFEIFVP--------LIYGARMT----IYQGEKFDVTKLVQVILEE 1550
Cdd:cd12119 187 SL--VLHAM------AALLTDGLGLSES---DV--VLPVVPmfhvnawgLPYAAAMVgaklVLPGPYLDPASLAELIERE 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1551 QVTLSYIPPTLLNEIYDYFVRDNQKIV-LNKLLVGVEPIKTELLAKYDHLFrgnLQILNGYGPTEATVCCTSYRY----- 1624
Cdd:cd12119 254 GVTFAAGVPTVWQGLLDHLEANGRDLSsLRRVVIGGSAVPRSLIEAFEERG---VRVIHAWGMTETSPLGTVARPpsehs 330
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1625 -ESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPI-GVP-GEICISGIGLARGYINRKELTADKFIDHPFergeklyKTG 1701
Cdd:cd12119 331 nLSEDEQLALRAKQGRPVPGVELRIVDDDGRELPWdGKAvGELQVRGPWVTKSYYKNDEESEALTEDGWL-------RTG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1702 DIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLcAYVV-------TEKdipi 1773
Cdd:cd12119 404 DVATIDEDGYLTITDRSKDVIKSGGEWISSVELENAIMAHPAVAEAAVIGVPHPKwGERPL-AVVVlkegatvTAE---- 478
|
490 500 510
....*....|....*....|....*....|....*....
gi 446807313 1774 pEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd12119 479 -ELLEFLADKVAKWWLPDDVVFVDEIPKTSTGKIDKKAL 516
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
1322-1812 |
2.35e-24 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 110.23 E-value: 2.35e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1322 KMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTD 1401
Cdd:PRK06155 25 AMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPINTA 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1402 LPKQRVEYMLTDSGcSHVLVHQNSIIKGIEfqgnVIDLMDMSFEE------------EPGEDMHMM-----------IEP 1458
Cdd:PRK06155 105 LRGPQLEHILRNSG-ARLLVVEAALLAALE----AADPGDLPLPAvwlldapasvsvPAGWSTAPLppldapapaaaVQP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1459 HNLAYVIYTSGSTGQPKGVMIEHRSLtnFLCAMYEdfSQDIGIT-DNVLFSSSISFDVTIFEIFVP-LIYGARMTIyqGE 1536
Cdd:PRK06155 180 GDTAAILYTSGTTGPSKGVCCPHAQF--YWWGRNS--AEDLEIGaDDVLYTTLPLFHTNALNAFFQaLLAGATYVL--EP 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1537 KFDVTKLVQVILEEQVTLSYipptLLNEIYDYFV------RDNQKIVLNKLLVGVEPiktELLAKYDHLFrgNLQILNGY 1610
Cdd:PRK06155 254 RFSASGFWPAVRRHGATVTY----LLGAMVSILLsqpareSDRAHRVRVALGPGVPA---ALHAAFRERF--GVDLLDGY 324
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1611 GPTEATVCCTsyryesnkeittqnVPIGSPLLNTKIYILDSFH-RIQ-------PIGVPGEICISG---IGLARGYINRK 1679
Cdd:PRK06155 325 GSTETNFVIA--------------VTHGSQRPGSMGRLAPGFEaRVVdehdqelPDGEPGELLLRAdepFAFATGYFGMP 390
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1680 ELTADKFIDHPFErgeklykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEK 1759
Cdd:PRK06155 391 EKTVEAWRNLWFH-------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGED 463
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1760 YLCAYVVTEKDIPIP--EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK06155 464 EVMAAVVLRDGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
1461-1815 |
3.79e-24 |
|
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: 105.88 E-value: 3.79e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGItdnVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKFDv 1540
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD---SWLLSLPLYHVGGLAILVRSLLAGAELVLLERNQA- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1541 tkLVQVILEEQVT-LSYIPPTLLNEIYDYFVRDNQKiVLNKLLVGVEPIKTELLAKYdhLFRGnLQILNGYGPTEATVCC 1619
Cdd:cd17630 78 --LAEDLAPPGVThVSLVPTQLQRLLDSGQGPAALK-SLRAVLLGGAPIPPELLERA--ADRG-IPLYTTYGMTETASQV 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1620 TSYRYESNKEITtqnvpIGSPLLNTKIYILDsfhriqpigvPGEICISGIGLARGYINRKEltadkfIDHPFERGekLYK 1699
Cdd:cd17630 152 ATKRPDGFGRGG-----VGVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQL------VPEFNEDG--WFT 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1700 TGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKyLCAYVVTEKDIPIPEVRA 1778
Cdd:cd17630 209 TKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVGVPDEElGQR-PVAVIVGRGPADPAELRA 287
|
330 340 350
....*....|....*....|....*....|....*..
gi 446807313 1779 YLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:cd17630 288 WLKDKLARFKLPKRIYPVPELPRTGGGKVDRRALRAW 324
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
283-771 |
6.99e-24 |
|
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: 108.38 E-value: 6.99e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 283 EQVKQNPNQIAIV--CNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:cd17642 25 KRYASVPGTIAFTdaHTGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 361 KQRVEYMLTDS----------GCSHVLTYQ--NSIIKGVAFQGSVINLM-------------DIPFEEEQVEDLQITMEP 415
Cdd:cd17642 105 ERELDHSLNISkptivfcskkGLQKVLNVQkkLKIIKTIIILDSKEDYKgyqclytfitqnlPPGFNEYDFKPPSFDRDE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 416 QnLAYVIYTSGSTGQPKGVMIEHRSLtnflCAMYEDFSQDIgitdnvlFSSSISFDVTIFEIfVP-------------LV 482
Cdd:cd17642 185 Q-VALIMNSSGSTGLPKGVQLTHKNI----VARFSHARDPI-------FGNQIIPDTAILTV-IPfhhgfgmfttlgyLI 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 483 CGARMTIYQgeKFDVPKLVQVILEEQVTLAYIPPTLL-----NEIYDYFVRANqkisLNKLFVGVEPIKTELLAKYDHLF 557
Cdd:cd17642 252 CGFRVVLMY--KFEEELFLRSLQDYKVQSALLVPTLFaffakSTLVDKYDLSN----LHEIASGGAPLSKEVGEAVAKRF 325
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 558 RGNLqILNLYGPTEATVCCTSYQYERDKEITTQNVpigSPLLNTKIYILDSFHRLQPiGVPGEICISGIGLARGYINRKE 637
Cdd:cd17642 326 KLPG-IRQGYGLTETTSAILITPEGDDKPGAVGKV---VPFFYAKVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPE 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 638 LTADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKY 717
Cdd:cd17642 401 ATKALIDK------DGWLHSGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGEL 474
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 718 LCAYVVTE--KDIPIPEVRAYLATKL-PYYMIPQQIISIQNIPLTQNGKIDRKKLPQ 771
Cdd:cd17642 475 PAAVVVLEagKTMTEKEVMDYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKIRE 531
|
|
| PLN02246 |
PLN02246 |
4-coumarate--CoA ligase |
1345-1812 |
7.11e-24 |
|
4-coumarate--CoA ligase
Pssm-ID: 215137 [Multi-domain] Cd Length: 537 Bit Score: 108.53 E-value: 7.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGA-------YLPidTDLPKQrveymLTDSGCS 1417
Cdd:PLN02246 52 TYADVELLSRRVAAGLHKLGIRQGDVVMLLLPNCPEFVLAFLGASRRGAVtttanpfYTP--AEIAKQ-----AKASGAK 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1418 HVLVHQNSI--IKGIEFQGNV----ID-----------LMDMSFEEEPGEDMHmmiePHNLAYVIYTSGSTGQPKGVMIE 1480
Cdd:PLN02246 125 LIITQSCYVdkLKGLAEDDGVtvvtIDdppegclhfseLTQADENELPEVEIS----PDDVVALPYSSGTTGLPKGVMLT 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1481 HRSLTNflcamyeDFSQDI-GITDNVLFSSSisfDVTIfeIFVPL--IY------------GARMTIYQgeKFDVTKLVQ 1545
Cdd:PLN02246 201 HKGLVT-------SVAQQVdGENPNLYFHSD---DVIL--CVLPMfhIYslnsvllcglrvGAAILIMP--KFEIGALLE 266
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1546 VILEEQVTLS-YIPPTLL----NEIYDYFVRDNQKIVLNkllvGVEPIKTELlakyDHLFRGNL--QIL-NGYGPTEA-T 1616
Cdd:PLN02246 267 LIQRHKVTIApFVPPIVLaiakSPVVEKYDLSSIRMVLS----GAAPLGKEL----EDAFRAKLpnAVLgQGYGMTEAgP 338
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1617 VCCTSYRYEsnKE-ITTQNVPIGSPLLNTKIYILD-----SFHRIQPigvpGEICISGIGLARGYINRKELTAdKFIDHp 1690
Cdd:PLN02246 339 VLAMCLAFA--KEpFPVKSGSCGTVVRNAELKIVDpetgaSLPRNQP----GEICIRGPQIMKGYLNDPEATA-NTIDK- 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1691 fergEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKD 1770
Cdd:PLN02246 411 ----DGWLHTGDIGYIDDDDELFIVDRLKELIKYKGFQVAPAELEALLISHPSIADAAVVPMKDEVAGEVPVAFVVRSNG 486
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446807313 1771 IPIPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PLN02246 487 SEITEdeIKQFVAKQVVFYKRIHKVFFVDSIPKAPSGKILRKDL 530
|
|
| OSB_MenE-like |
cd17630 |
O-succinylbenzoic acid-CoA ligase; This family contains O-succinylbenzoyl-CoA (OSB-CoA) ... |
418-767 |
8.10e-24 |
|
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: 104.72 E-value: 8.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 418 LAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGItdnVLFSSSISFDVTIFEIFVP-LVCGARMTIYQGEkfd 496
Cdd:cd17630 2 LATVILTSGSTGTPKAVVHTAANLLASAAGLHSRLGFGGGD---SWLLSLPLYHVGGLAILVRsLLAGAELVLLERN--- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 497 vPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFVGVEPIKTELLAkydhlfRGNLQILNL---YGPTE-- 571
Cdd:cd17630 76 -QALAEDLAPPGVTHVSLVPTQLQRLLDSGQGPAALKSLRAVLLGGAPIPPELLE------RAADRGIPLyttYGMTEta 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 572 ATVCCTSYQYERDKEIttqnvpiGSPLLNTKIYILDsfhrlqpigvPGEICISGIGLARGYINRKEltadkfIDHPFERG 651
Cdd:cd17630 149 SQVATKRPDGFGRGGV-------GVLLPGRELRIVE----------DGEIWVGGASLAMGYLRGQL------VPEFNEDG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 652 ekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-QREDESGEKyLCAYVVTEKDIPI 730
Cdd:cd17630 206 --WFTTKDLGELHADGRLTVLGRADNMIISGGENIQPEEIEAALAAHPAVRDAFVVgVPDEELGQR-PVAVIVGRGPADP 282
|
330 340 350
....*....|....*....|....*....|....*..
gi 446807313 731 PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRK 767
Cdd:cd17630 283 AELRAWLKDKLARFKLPKRIYPVPELPRTGGGKVDRR 319
|
|
| PRK13295 |
PRK13295 |
cyclohexanecarboxylate-CoA ligase; Reviewed |
300-769 |
9.34e-24 |
|
cyclohexanecarboxylate-CoA ligase; Reviewed
Pssm-ID: 171961 [Multi-domain] Cd Length: 547 Bit Score: 108.22 E-value: 9.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 300 EITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGcSHVL-- 377
Cdd:PRK13295 55 RFTYRELAALVDRVAVGLARLGVGRGDVVSCQLPNWWEFTVLYLACSRIGAVLNPLMPIFRERELSFMLKHAE-SKVLvv 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 378 ---------------------TYQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITME----PQNLAYVIYTSGSTGQPK 432
Cdd:PRK13295 134 pktfrgfdhaamarrlrpelpALRHVVVVGGDGADSFEALLITPAWEQEPDAPAILARlrpgPDDVTQLIYTSGTTGEPK 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 433 GVMieHRSltNFLCAMYEDFSQDIGIT-DNVLFSSSISFDVT--IFEIFVPLVCGARMtIYQgEKFDVPKLVQVILEEQV 509
Cdd:PRK13295 214 GVM--HTA--NTLMANIVPYAERLGLGaDDVILMASPMAHQTgfMYGLMMPVMLGATA-VLQ-DIWDPARAAELIRTEGV 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 510 TLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTE-ATVCCTSYQYERDKEI 587
Cdd:PRK13295 288 TFTMASTPFLTDLTRAVKESGRPVsSLRTFLCAGAPIPGALVERARAAL--GAKIVSAWGMTEnGAVTLTKLDDPDERAS 365
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 588 TTQnvpiGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidhpfergEKLYKTGDIARWLPDG 667
Cdd:PRK13295 366 TTD----GCPLPGVEVRVVDADGAPLPAGQIGRLQVRGCSNFGGYLKRPQLNGTDA--------DGWFDTGDLARIDADG 433
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 668 NIEYLGRvDHQVKIRG-YRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTE--KDIPIPEVRAYLATK--- 740
Cdd:PRK13295 434 YIRISGR-SKDVIIRGgENIPVVEIEALLYRHPAIAQVAIVAYPDERlGER-ACAFVVPRpgQSLDFEEMVEFLKAQkva 511
|
490 500
....*....|....*....|....*....
gi 446807313 741 LPYymIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK13295 512 KQY--IPERLVVRDALPRTPSGKIQKFRL 538
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
278-769 |
1.26e-23 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 107.80 E-value: 1.26e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 278 PQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDT 357
Cdd:PRK07059 26 ADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYVVVNVNP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 358 ELPKQRVEYMLTDSGCSHVLTYQN-----------SIIKGV---------AFQGSVINLM-----------DIP----FE 402
Cdd:PRK07059 106 LYTPRELEHQLKDSGAEAIVVLENfattvqqvlakTAVKHVvvasmgdllGFKGHIVNFVvrrvkkmvpawSLPghvrFN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 403 EEQVEDLQITMEPQNL-----AYVIYTSGSTGQPKGVMIEHRS-LTNFL--CAMYEDFSQDIGITDNVLFSSSISfdvtI 474
Cdd:PRK07059 186 DALAEGARQTFKPVKLgpddvAFLQYTGGTTGVSKGATLLHRNiVANVLqmEAWLQPAFEKKPRPDQLNFVCALP----L 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 475 FEIFVPLVCGArMTIYQG-------EKFDVPKLVQVILEEQVTLayIPPtlLNEIYDYFVRAN--QKISLNKLFVGV--- 542
Cdd:PRK07059 262 YHIFALTVCGL-LGMRTGgrnilipNPRDIPGFIKELKKYQVHI--FPA--VNTLYNALLNNPdfDKLDFSKLIVANggg 336
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 543 ----EPIKTELLAKYdhlfrgNLQILNLYGPTEATVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVP 618
Cdd:PRK07059 337 mavqRPVAERWLEMT------GCPITEGYGLSETSPVATCNPVDATEFSGT----IGLPLPSTEVSIRDDDGNDLPLGEP 406
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 619 GEICISGIGLARGYINRKE-----LTADKFidhpfergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEA 693
Cdd:PRK07059 407 GEICIRGPQVMAGYWNRPDetakvMTADGF-----------FRTGDVGVMDERGYTKIVDRKKDMILVSGFNVYPNEIEE 475
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 694 SLLKYETIKTAVVIQREDE-SGEKyLCAYVVtEKDIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK07059 476 VVASHPGVLEVAAVGVPDEhSGEA-VKLFVV-KKDPALTEedVKAFCKERLTNYKRPKFVEFRTELPKTNVGKILRREL 552
|
|
| PRK09088 |
PRK09088 |
acyl-CoA synthetase; Validated |
284-769 |
1.85e-23 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 181644 [Multi-domain] Cd Length: 488 Bit Score: 106.81 E-value: 1.85e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 284 QVKQNPNQIAIV--CNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPK 361
Cdd:PRK09088 4 HARLQPQRLAAVdlALGRRWTYAELDALVGRLAAVLRRRGCVDGERLAVLARNSVWLVALHFACARVGAIYVPLNWRLSA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 362 QRVEYMLTDSgcshvltyQNSIIKG----VAFQGSVINLMDIPFEEEQVE-DLQITMEPQNLAYVIYTSGSTGQPKGVMI 436
Cdd:PRK09088 84 SELDALLQDA--------EPRLLLGddavAAGRTDVEDLAAFIASADALEpADTPSIPPERVSLILFTSGTSGQPKGVML 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 437 EHRSL----TNFlcamyedfsqdiGITDNVLFSSSISFDVTIFEIfVPLVCGARMTIYQGEKFdvpkLVQVILEEQVTLA 512
Cdd:PRK09088 156 SERNLqqtaHNF------------GVLGRVDAHSSFLCDAPMFHI-IGLITSVRPVLAVGGSI----LVSNGFEPKRTLG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 513 YIP-PTLlnEIYDYF--------VRANQKI------SLNKLFVGVEP-IKTELLAKYDHlfrgNLQILNLYGPTEA-TVC 575
Cdd:PRK09088 219 RLGdPAL--GITHYFcvpqmaqaFRAQPGFdaaalrHLTALFTGGAPhAAEDILGWLDD----GIPMVDGFGMSEAgTVF 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 576 CTSYQYERdkeITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEKLY 655
Cdd:PRK09088 293 GMSVDCDV---IRAKAGAAGIPTPTVQTRVVDDQGNDCPAGVPGELLLRGPNLSPGYWRRPQATARAF------TGDGWF 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 656 KTGDIARWLPDGnieYLGRVDHQVKI---RGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLCAYVVTEKDIPIP 731
Cdd:PRK09088 364 RTGDIARRDADG---FFWVVDRKKDMfisGGENVYPAEIEAVLADHPGIRECAVVGMADAQwGEVGYLAIVPADGAPLDL 440
|
490 500 510
....*....|....*....|....*....|....*....
gi 446807313 732 E-VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK09088 441 ErIRSHLSTRLAKYKVPKHLRLVDALPRTASGKLQKARL 479
|
|
| AACS_like |
cd05968 |
Uncharacterized acyl-CoA synthetase subfamily similar to Acetoacetyl-CoA synthetase; This ... |
1319-1809 |
3.03e-23 |
|
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: 107.19 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1319 LVHKMFEEQVKRNPNQIAVVC-NEKG----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGG 1393
Cdd:cd05968 62 IVEQLLDKWLADTRTRPALRWeGEDGtsrtLTYGELLYEVKRLANGLRALGVGKGDRVGIYLPMIPEIVPAFLAVARIGG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1394 AYLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSIIKGIEFqgNVIDLMDMSFEEEPGEDmHMMIE--------PHNLAY-- 1463
Cdd:cd05968 142 IVVPIFSGFGKEAAATRLQDAEAKALITADGFTRRGREV--NLKEEADKACAQCPTVE-KVVVVrhlgndftPAKGRDls 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 ----------------------VIYTSGSTGQPKGVMIEHrslTNFLCAMYED--FSQDIGITDNVLFSSSISFDVTIFE 1519
Cdd:cd05968 219 ydeeketagdgaertesedplmIIYTSGTTGKPKGTVHVH---AGFPLKAAQDmyFQFDLKPGDLLTWFTDLGWMMGPWL 295
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1520 IFVPLIYGARMTIYQG--EKFDVTKLVQVILEEQVTLSYIPPTLLNEIY---DYFVRDNQKIVLNKLLVGVEPIKTE-LL 1593
Cdd:cd05968 296 IFGGLILGATMVLYDGapDHPKADRLWRMVEDHEITHLGLSPTLIRALKprgDAPVNAHDLSSLRVLGSTGEPWNPEpWN 375
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1594 AKYDHLFRGNLQILNGYGPTEAT---VCCtsYRYESNKEITtqnvpIGSPLLNTKIYILDSfhRIQPI-GVPGEICISG- 1668
Cdd:cd05968 376 WLFETVGKGRNPIINYSGGTEISggiLGN--VLIKPIKPSS-----FNGPVPGMKADVLDE--SGKPArPEVGELVLLAp 446
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1669 -IGLARGYInRKEltaDKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTA 1747
Cdd:cd05968 447 wPGMTRGFW-RDE---DRYLETYWSRFDNVWVHGDFAYYDEEGYFYILGRSDDTINVAGKRVGPAEIESVLNAHPAVLES 522
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1748 VVIDQEDEA-GEKYLCaYVVTEKDI-PIP----EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:cd05968 523 AAIGVPHPVkGEAIVC-FVVLKPGVtPTEalaeELMERVADELGKPLSPERILFVKDLPKTRNAKVMR 589
|
|
| MACS_like_2 |
cd05973 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1344-1814 |
3.04e-23 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341277 [Multi-domain] Cd Length: 437 Bit Score: 105.29 E-value: 3.04e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcSHVLVhq 1423
Cdd:cd05973 1 LTFGELRALSARFANALQELGVGPGDVVAGLLPRTPELVVTILGIWRLGAVYQPLFTAFGPKAIEHRLRTSG-ARLVV-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nsiikgiefqgnvidlMDMSFEEEPGEDMHMMIephnlayviYTSGSTGQPKGVMIEHRSLTNFlcAMYEDFSQDIGITD 1503
Cdd:cd05973 78 ----------------TDAANRHKLDSDPFVMM---------FTSGTTGLPKGVPVPLRALAAF--GAYLRDAVDLRPED 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1504 NVLFSSSISFDVTIF-EIFVPLIYGARMTIYQGeKFDVTKLVQVILEEQVTLSYIPPTllneIYDYFVRDNQ------KI 1576
Cdd:cd05973 131 SFWNAADPGWAYGLYyAITGPLALGHPTILLEG-GFSVESTWRVIERLGVTNLAGSPT----AYRLLMAAGAevparpKG 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1577 VLNKLLVGVEPIKTELLakydHLFRGNL--QILNGYGPTE-ATVCCTSYRYESNKEITTqnvpIGSPLLNTKIYILDSFH 1653
Cdd:cd05973 206 RLRRVSSAGEPLTPEVI----RWFDAALgvPIHDHYGQTElGMVLANHHALEHPVHAGS----AGRAMPGWRVAVLDDDG 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1654 RIQPIGVPGEICI----SGIGLARGYINRKELTADKfidhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 1729
Cdd:cd05973 278 DELGPGEPGRLAIdianSPLMWFRGYQLPDTPAIDG----------GYYLTGDTVEFDPDGSFSFIGRADDVITMSGYRI 347
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1730 ELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-TEKDIPIPEVRAYLA----TKLPHYMIPQQLIPIHNIPLTQN 1804
Cdd:cd05973 348 GPFDVESALIEHPAVAEAAVIGVPDPERTEVVKAFVVlRGGHEGTPALADELQlhvkKRLSAHAYPRTIHFVDELPKTPS 427
|
490
....*....|
gi 446807313 1805 GKIDRSKLPK 1814
Cdd:cd05973 428 GKIQRFLLRR 437
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
287-780 |
3.39e-23 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 105.34 E-value: 3.39e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 287 QNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEY 366
Cdd:PRK09029 15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 367 MLTDSGCSHVLTYQNsiikgvafQGSVINLMDIPfEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRS-LTN-- 443
Cdd:PRK09029 95 LLPSLTLDFALVLEG--------ENTFSALTSLH-LQLVEGAHAVAWQPQRLATMTLTSGSTGLPKAAVHTAQAhLASae 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 444 -FLCAMyeDFSQDigitDNVLFSssisfdvtifeifVP-------------LVCGARMTIYQGEKFDvpklvQVIleEQV 509
Cdd:PRK09029 166 gVLSLM--PFTAQ----DSWLLS-------------LPlfhvsgqgivwrwLYAGATLVVRDKQPLE-----QAL--AGC 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 510 TLAYIPPTLLNEIYDYfvrANQKISLNKLFVGVEPIKTEL---LAKYD-HLFRGnlqilnlYGPTEA--TVCCtsyqyer 583
Cdd:PRK09029 220 THASLVPTQLWRLLDN---RSEPLSLKAVLLGGAAIPVELteqAEQQGiRCWCG-------YGLTEMasTVCA------- 282
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 584 dKEI-TTQNVpiGSPLLNTKIYILDsfhrlqpigvpGEICISGIGLARGYINRKELTadkfidhPFERGEKLYKTGDIAR 662
Cdd:PRK09029 283 -KRAdGLAGV--GSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGE 341
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 663 WLpDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQRED-ESGEKYLcAYVVTEKDIPIPEVRAYLATKL 741
Cdd:PRK09029 342 WQ-NGELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADaEFGQRPV-AVVESDSEAAVVNLAEWLQDKL 419
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446807313 742 -----P--YYMIPQQiisiqnipLTQNG-KIDRKKLPQPINNLKSSH 780
Cdd:PRK09029 420 arfqqPvaYYLLPPE--------LKNGGiKISRQALKEWVAQQLGNN 458
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
289-764 |
8.47e-23 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 105.24 E-value: 8.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:PRK07786 31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGCSHVLT-----------------YQNSIIKGVAFQGSVINLMDIPFEEEqvEDLQITMEPQNL-AYVIYTSGSTGQ 430
Cdd:PRK07786 111 SDCGAHVVVTeaalapvatavrdivplLSTVVVAGGSSDDSVLGYEDLLAEAG--PAHAPVDIPNDSpALIMYTSGTTGR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 431 PKGVMIEHRSLT----NFLCAMYEDFSQDIGitdnvlFSSSISFDVTIFEIFVP-LVCGARMTIYQGEKFDVPKLVQVIL 505
Cdd:PRK07786 189 PKGAVLTHANLTgqamTCLRTNGADINSDVG------FVGVPLFHIAGIGSMLPgLLLGAPTVIYPLGAFDPGQLLDVLE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 506 EEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFVGVEPIKTELLAKYDHLFRGNlQILNLYGPTEAT-VCCTSYQYERD 584
Cdd:PRK07786 263 AEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEA-QILAAFGQTEMSpVTCMLLGEDAI 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 585 KEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIARWL 664
Cdd:PRK07786 342 RKLGS----VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH-------SGDLVRQD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 665 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLCAYVVT--EKDIPIPEVRAYLATKL 741
Cdd:PRK07786 411 EEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwGEVPVAVAAVRndDAALTLEDLAEFLTDRL 490
|
490 500
....*....|....*....|...
gi 446807313 742 PYYMIPQQIISIQNIPLTQNGKI 764
Cdd:PRK07786 491 ARYKHPKALEIVDALPRNPAGKV 513
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
298-769 |
1.29e-22 |
|
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: 103.33 E-value: 1.29e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 298 GKEITYKQLNIKANQLARRLLDQGVKRE-FIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHV 376
Cdd:cd05958 8 EREWTYRDLLALANRIANVLVGELGIVPgNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKARITVA 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 377 LtyqnsiikgvafqgsvinlmdIPFEEEQVEDLQItmepqnlayVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDI 456
Cdd:cd05958 88 L---------------------CAHALTASDDICI---------LAFTSGTTGAPKATMHFHRDPL----ASADRYAVNV 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 457 -GITDNVLFSSS----ISFDVTIFEIFvPLVCGARMTIYqgEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQ 531
Cdd:cd05958 134 lRLREDDRFVGSpplaFTFGLGGVLLF-PFGVGASGVLL--EEATPDLLLSAIARYKPTVLFTAPTAYRAMLAHPDAAGP 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 532 KIS-LNKLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTSYQYERDKEITTqnvpiGSPLLNTKIYILDSFH 610
Cdd:cd05958 211 DLSsLRKCVSAGEALPAALHRAWKEAT--GIPIIDGIGSTEMFHIFISARPGDARPGAT-----GKPVPGYEAKVVDDEG 283
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 611 RLQPIGVPGEICISGIGLARGyiNRKELTADKFidhpfeRGEKLYkTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGE 690
Cdd:cd05958 284 NPVPDGTIGRLAVRGPTGCRY--LADKRQRTYV------QGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYNIAPPE 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 691 IEASLLKYETIKTAVVIQREDESGEKYLCAYVV-----TEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:cd05958 355 VEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVlrpgvIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTATGKLQ 434
|
....
gi 446807313 766 RKKL 769
Cdd:cd05958 435 RFAL 438
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
421-766 |
1.33e-22 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 101.57 E-value: 1.33e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 421 VIYTSGSTGQPKGVMIEHRSLtnFLCAMYEDFSQDIGITDNVLFS-SSISFDVTIFEIFVPLVCGARMTIYqGEKFDVPK 499
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTF--FAVPDILQKEGLNWVVGDVTYLpLPATHIGGLWWILTCLIHGGLCVTG-GENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 500 LVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVE-PIKTEllaKYDHLFRGNLQILNLYGPTE-ATVCC 576
Cdd:cd17635 83 LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVpSLRLIGYGGSrAIAAD---VRFIEATGLTNTAQVYGLSEtGTALC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 577 TsyQYERD-KEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergekly 655
Cdd:cd17635 160 L--PTDDDsIEINA----VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV------- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 656 KTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLCAYVVTEKDIP--IPE 732
Cdd:cd17635 227 NTGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEfGELVGLAVVASAELDEnaIRA 306
|
330 340 350
....*....|....*....|....*....|....
gi 446807313 733 VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:cd17635 307 LKHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
288-779 |
1.69e-22 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 104.30 E-value: 1.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 288 NPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAylPIDTELPKQRVE-- 365
Cdd:PRK10946 36 ASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSEln 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 366 -Y--------MLTDSgcSHVLTYQNSIIKgvAFQGSVINLMDIPFEEEQVE-DLQITMEPQNLAYVIYTS---------- 425
Cdd:PRK10946 114 aYasqiepalLIADR--QHALFSDDDFLN--TLVAEHSSLRVVLLLNDDGEhSLDDAINHPAEDFTATPSpadevaffql 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 426 --GSTGQPKGVMIEH--------RSL--------TNFLCAmyedfsqdIGITDNVLFSSSISFDVTIFEIFV-------P 480
Cdd:PRK10946 190 sgGSTGTPKLIPRTHndyyysvrRSVeicgftpqTRYLCA--------LPAAHNYPMSSPGALGVFLAGGTVvlapdpsA 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 481 LVCgarmtiyqgekfdvpklVQVILEEQVTL-AYIPPTL---LNEIYDYFVRAnQKISLNKLFVGVEPIKTELLAKYDHL 556
Cdd:PRK10946 262 TLC-----------------FPLIEKHQVNVtALVPPAVslwLQAIAEGGSRA-QLASLKLLQVGGARLSETLARRIPAE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 557 FRGNLQilNLYGPTEATVCCTSYQYERDKEITTQNVPIgSPllNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRK 636
Cdd:PRK10946 324 LGCQLQ--QVFGMAEGLVNYTRLDDSDERIFTTQGRPM-SP--DDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSP 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 637 ELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GE 715
Cdd:PRK10946 399 QHNASAFDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELmGE 472
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 716 KYlCAYVVTEKDIPIPEVRAYL-ATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSS 779
Cdd:PRK10946 473 KS-CAFLVVKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQWLASRASA 536
|
|
| ABCL |
cd05958 |
2-aminobenzoate-CoA ligase (ABCL); ABCL catalyzes the initial step in the 2-aminobenzoate ... |
1336-1812 |
2.69e-22 |
|
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: 102.56 E-value: 2.69e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1336 AVVCNEKGITYNELNIKANQLARRLLDQGVKRE-SIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDS 1414
Cdd:cd05958 3 CLRSPEREWTYRDLLALANRIANVLVGELGIVPgNRVLLRGSNSPELVACWFGIQKAGAIAVATMPLLRPKELAYILDKA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1415 GCSHVLVhqnsiikgiefqgnvidlmdmsfeeepgedMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYED 1494
Cdd:cd05958 83 RITVALC------------------------------AHALTASDDICILAFTSGTTGAPKATMHFHRDPL----ASADR 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1495 FSQDI-GITDNVLFSSS----ISFDVTIFEIFvPLIYGARMTIYQGEKFDvtKLVQVILEEQVTLSYIPPTLLNEIYDYF 1569
Cdd:cd05958 129 YAVNVlRLREDDRFVGSpplaFTFGLGGVLLF-PFGVGASGVLLEEATPD--LLLSAIARYKPTVLFTAPTAYRAMLAHP 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1570 VRDNQKIV-LNKLLVGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATvcctsYRYESNKEITTQNVPIGSPLLNTKIYI 1648
Cdd:cd05958 206 DAAGPDLSsLRKCVSAGEALPAALHRAWKEAT--GIPIIDGIGSTEMF-----HIFISARPGDARPGATGKPVPGYEAKV 278
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1649 LDSFHRIQPIGVPGEICISGIGLARGyiNRKELTADKFidhpfeRGEKLYkTGDIARWLPDGNIEYLGRVDHQVKIRGYR 1728
Cdd:cd05958 279 VDDEGNPVPDGTIGRLAVRGPTGCRY--LADKRQRTYV------QGGWNI-TGDTYSRDPDGYFRHQGRSDDMIVSGGYN 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1729 IELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-----TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQ 1803
Cdd:cd05958 350 IAPPEVEDVLLQHPAVAECAVVGHPDESRGVVVKAFVVlrpgvIPGPVLARELQDHAKAHIAPYKYPRAIEFVTELPRTA 429
|
....*....
gi 446807313 1804 NGKIDRSKL 1812
Cdd:cd05958 430 TGKLQRFAL 438
|
|
| LC_FACS_like |
cd17640 |
Long-chain fatty acid CoA synthetase; This family includes long-chain fatty acid (C12-C20) CoA ... |
299-728 |
2.75e-22 |
|
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: 102.82 E-value: 2.75e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 299 KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCShVLT 378
Cdd:cd17640 4 KRITYKDLYQEILDFAAGLRSLGVKAGEKVALFADNSPRWLIADQGIMALGAVDVVRGSDSSVEELLYILNHSESV-ALV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 379 YQNSiikgvafqgsvinlmdipfeeeqvedlqitmePQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGi 458
Cdd:cd17640 83 VEND--------------------------------SDDLATIIYTSGTTGNPKGVMLTHANLLHQIRSLSDIVPPQPG- 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 459 tDNVLfssSI-----SFDvTIFEIFVpLVCGARMtIYQGEKF--DVPKLVQVILEEQVTLAYIppTLLNEIYDYFV---R 528
Cdd:cd17640 130 -DRFL---SIlpiwhSYE-RSAEYFI-FACGCSQ-AYTSIRTlkDDLKRVKPHYIVSVPRLWE--SLYSGIQKQVSkssP 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 529 ANQKISLNKLFVGVepIKTEL-----LAKY-DHLFRG-NLQILNLYGPTEATVCCTSYQYERDKEITtqnvpIGSPLLNT 601
Cdd:cd17640 201 IKQFLFLFFLSGGI--FKFGIsgggaLPPHvDTFFEAiGIEVLNGYGLTETSPVVSARRLKCNVRGS-----VGRPLPGT 273
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 602 KIYILDSFHR-LQPIGVPGEICISGIGLARGYINRKELTAdKFIDHpfergEKLYKTGDIARWLPDGNIEYLGRV-DHQV 679
Cdd:cd17640 274 EIKIVDPEGNvVLPPGEKGIVWVRGPQVMKGYYKNPEATS-KVLDS-----DGWFNTGDLGWLTCGGELVLTGRAkDTIV 347
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 446807313 680 KIRGYRIELGEIEASLLKYETIKTAVVIQREdesgEKYLCAYVVTEKDI 728
Cdd:cd17640 348 LSNGENVEPQPIEEALMRSPFIEQIMVVGQD----QKRLGALIVPNFEE 392
|
|
| PLN02574 |
PLN02574 |
4-coumarate--CoA ligase-like |
1344-1812 |
3.16e-22 |
|
4-coumarate--CoA ligase-like
Pssm-ID: 215312 [Multi-domain] Cd Length: 560 Bit Score: 103.38 E-value: 3.16e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID-----TDLPKQRVE------YML 1411
Cdd:PLN02574 67 ISYSELQPLVKSMAAGLYHVmGVRQGDVVLLLLPNSVYFPVIFLAVLSLGGIVTTMNpssslGEIKKRVVDcsvglaFTS 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDS-------GCSHVLVHQNSII--KGIEFQGNvidLMDMSFEEEPGedMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHR 1482
Cdd:PLN02574 147 PENveklsplGVPVIGVPENYDFdsKRIEFPKF---YELIKEDFDFV--PKPVIKQDDVAAIMYSSGTTGASKGVVLTHR 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1483 sltNFLcAMYEDF-----SQ-DIGITDNVLFSSSISFDVTIFEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVT-LS 1555
Cdd:PLN02574 222 ---NLI-AMVELFvrfeaSQyEYPGSDNVYLAALPMFHIYGLSLFVVGLLSLGSTIVVMRRFDASDMVKVIDRFKVThFP 297
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1556 YIPPTLLNeiydyFVRDNQKIV------LNKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEATVCCTSyRYESNKE 1629
Cdd:PLN02574 298 VVPPILMA-----LTKKAKGVCgevlksLKQVSCGAAPLSGKFIQDFVQTL-PHVDFIQGYGMTESTAVGTR-GFNTEKL 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1630 ITTQNVPIGSPLLNTKIYILDSFHRIQPiGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLPD 1709
Cdd:PLN02574 371 SKYSSVGLLAPNMQAKVVDWSTGCLLPP-GNCGELWIQGPGVMKGYLNNPKATQSTIDK------DGWLRTGDIAYFDED 443
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1710 GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPE--VRAYLATKLPHY 1787
Cdd:PLN02574 444 GYLYIVDRLKEIIKYKGFQIAPADLEAVLISHPEIIDAAVTAVPDKECGEIPVAFVVRRQGSTLSQeaVINYVAKQVAPY 523
|
490 500
....*....|....*....|....*
gi 446807313 1788 MIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PLN02574 524 KKVRKVVFVQSIPKSPAGKILRREL 548
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
1344-1812 |
4.25e-22 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 101.88 E-value: 4.25e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDLRDRVDRGGAVYAAVDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 NSiikgiefqgnvidlmdmsfeeepGEDMHMMIephnlayvIYTSGSTGQPKGVMIEHRSL-TNFLCAMYEdfsqdIGIT 1502
Cdd:cd05974 81 NT-----------------------HADDPMLL--------YFTSGTTSKPKLVEHTHRSYpVGHLSTMYW-----IGLK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1503 --DNVLFSSSISFDVTIFE-IFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTllneIYDYFVRDNQ---KI 1576
Cdd:cd05974 125 pgDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPT----VWRMLIQQDLasfDV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1577 VLNKLLVGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATVCCtsyryeSNKeiTTQNVPIGS---PLLNTKIYILDsfh 1653
Cdd:cd05974 201 KLREVVGAGEPLNPEVIEQVRRAW--GLTIRDGYGQTETTALV------GNS--PGQPVKAGSmgrPLPGYRVALLD--- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1654 riqPIGVP---GEICIS-----GIGLARGYINRKELTADKFidhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIR 1725
Cdd:cd05974 268 ---PDGAPateGEVALDlgdtrPVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSS 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1726 GYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-TEKDIPIPE----VRAYLATKLPHYMIPQQLiPIHNIP 1800
Cdd:cd05974 338 DYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlRAGYEPSPEtaleIFRFSRERLAPYKRIRRL-EFAELP 416
|
490
....*....|..
gi 446807313 1801 LTQNGKIDRSKL 1812
Cdd:cd05974 417 KTISGKIRRVEL 428
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
421-766 |
4.48e-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: 4.48e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 421 VIYTSGSTGQPKGVMIEHRsltNFLCAMYEdFSQDIGITDNvlfsssisfDV--TIFEIF-VPLVCGARMTIYQG----- 492
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHG---NLIAANLQ-LIHAMGLTEA---------DVylNMLPLFhIAGLNLALATFHAGganvv 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 493 -EKFDVPKLVQVILEEQVTL-AYIPPTLLNeIYDYFVRANQKISLNKLFVGVE-PiktELLAKYDHLFRGNLQILnlYGP 569
Cdd:cd17637 72 mEKFDPAEALELIEEEKVTLmGSFPPILSN-LLDAAEKSGVDLSSLRHVLGLDaP---ETIQRFEETTGATFWSL--YGQ 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 570 TEaTVCCTSYQYERDKEITTqnvpiGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTAdkfidHPFE 649
Cdd:cd17637 146 TE-TSGLVTLSPYRERPGSA-----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTA-----YTFR 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 650 RGekLYKTGDIARWLPDGNIEYLGRVDHQ--VKIRGYRIELGEIEASLLKYETIKTAVVIQRED-ESGE--KYLCA---- 720
Cdd:cd17637 215 NG--WHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDpKWGEgiKAVCVlkpg 292
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446807313 721 YVVTEKdipipEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:cd17637 293 ATLTAD-----ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| entE |
PRK10946 |
(2,3-dihydroxybenzoyl)adenylate synthase; |
1330-1815 |
6.85e-22 |
|
(2,3-dihydroxybenzoyl)adenylate synthase;
Pssm-ID: 236803 [Multi-domain] Cd Length: 536 Bit Score: 102.38 E-value: 6.85e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1330 RNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAylPIDTDLPKQRVE- 1408
Cdd:PRK10946 35 AASDAIAVICGERQFSYRELNQASDNLACSLRRQGIKPGDTALVQLGNVAEFYITFFALLKLGVA--PVNALFSHQRSEl 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1409 --Y--------MLTDSgcSHVLVHQNSIIKgiEFQGNVIDLMDMSFEEEPGE-DMHMMIEPHNLAYVIYTS--------- 1468
Cdd:PRK10946 113 naYasqiepalLIADR--QHALFSDDDFLN--TLVAEHSSLRVVLLLNDDGEhSLDDAINHPAEDFTATPSpadevaffq 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1469 ---GSTGQPKGVMIEH--------RSL--------TNFLCAmyedfsqdIGITDNVLFSSSISFDVtiFEifvpliygAR 1529
Cdd:PRK10946 189 lsgGSTGTPKLIPRTHndyyysvrRSVeicgftpqTRYLCA--------LPAAHNYPMSSPGALGV--FL--------AG 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1530 MTIYQGEKFDVTKLVQVILEEQVTL-SYIPPTL---LNEIYDYFVRDnQKIVLNKLLVGVEPIKTELLAKYDHLFRGNLQ 1605
Cdd:PRK10946 251 GTVVLAPDPSATLCFPLIEKHQVNVtALVPPAVslwLQAIAEGGSRA-QLASLKLLQVGGARLSETLARRIPAELGCQLQ 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1606 ILngYGPTEATVCCTSYRYESNKEITTQNVPIgSPllNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADK 1685
Cdd:PRK10946 330 QV--FGMAEGLVNYTRLDDSDERIFTTQGRPM-SP--DDEVWVADADGNPLPQGEVGRLMTRGPYTFRGYYKSPQHNASA 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1686 FIDHPFergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYlCAY 1764
Cdd:PRK10946 405 FDANGF------YCSGDLVSIDPDGYITVVGREKDQINRGGEKIAAEEIENLLLRHPAVIHAALVSMEDELmGEKS-CAF 477
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1765 VVTEKDIPIPEVRAYL-ATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK10946 478 LVVKEPLKAVQLRRFLrEQGIAEFKLPDRVECVDSLPLTAVGKVDKKQLRQW 529
|
|
| Firefly_Luc |
cd17642 |
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect ... |
1340-1812 |
8.11e-22 |
|
insect luciferase, similar to plant 4-coumarate: CoA ligases; This family contains insect firefly luciferases that share significant sequence similarity to plant 4-coumarate:coenzyme A ligases, despite their functional diversity. Luciferase catalyzes the production of light in the presence of MgATP, molecular oxygen, and luciferin. In the first step, luciferin is activated by acylation of its carboxylate group with ATP, resulting in an enzyme-bound luciferyl adenylate. In the second step, luciferyl adenylate reacts with molecular oxygen, producing an enzyme-bound excited state product (Luc=O*) and releasing AMP. This excited-state product then decays to the ground state (Luc=O), emitting a quantum of visible light.
Pssm-ID: 341297 [Multi-domain] Cd Length: 532 Bit Score: 102.22 E-value: 8.11e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1340 NEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDS----- 1414
Cdd:cd17642 41 TGVNYSYAEYLEMSVRLAEALKKYGLKQNDRIAVCSENSLQFFLPVIAGLFIGVGVAPTNDIYNERELDHSLNISkptiv 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1415 -----GCSHVLVHQ--NSIIKGIEFQGNVIDLM----DMSFEEE---PGEDMHMMIEP-----HNLAYVIYTSGSTGQPK 1475
Cdd:cd17642 121 fcskkGLQKVLNVQkkLKIIKTIIILDSKEDYKgyqcLYTFITQnlpPGFNEYDFKPPsfdrdEQVALIMNSSGSTGLPK 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1476 GVMIEHRSLtnflCAMYEDFSQDIgitdnvlFSSSISFDVTIFEIfVPLIYGARMTIYQG-----------EKFDVTKLV 1544
Cdd:cd17642 201 GVQLTHKNI----VARFSHARDPI-------FGNQIIPDTAILTV-IPFHHGFGMFTTLGylicgfrvvlmYKFEEELFL 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1545 QVILEEQVTLSYIPPTLL-----NEIYDYFVRDNqkivLNKLLVGVEPIKTELLAKYDHLFRGNLqILNGYGPTEATVCC 1619
Cdd:cd17642 269 RSLQDYKVQSALLVPTLFaffakSTLVDKYDLSN----LHEIASGGAPLSKEVGEAVAKRFKLPG-IRQGYGLTETTSAI 343
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1620 TSYRYESNKEITTQNVpigSPLLNTKIYILDSFHRIQPiGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYK 1699
Cdd:cd17642 344 LITPEGDDKPGAVGKV---VPFFYAKVVDLDTGKTLGP-NERGELCVKGPMIMKGYVNNPEATKALIDK------DGWLH 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1700 TGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTE--KDIPIPEVR 1777
Cdd:cd17642 414 SGDIAYYDEDGHFFIVDRLKSLIKYKGYQVPPAELESILLQHPKIFDAGVAGIPDEDAGELPAAVVVLEagKTMTEKEVM 493
|
490 500 510
....*....|....*....|....*....|....*.
gi 446807313 1778 AYLATKL-PHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd17642 494 DYVASQVsTAKRLRGGVKFVDEVPKGLTGKIDRRKI 529
|
|
| PRK09029 |
PRK09029 |
O-succinylbenzoic acid--CoA ligase; Provisional |
1330-1812 |
8.87e-22 |
|
O-succinylbenzoic acid--CoA ligase; Provisional
Pssm-ID: 236363 [Multi-domain] Cd Length: 458 Bit Score: 101.10 E-value: 8.87e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1330 RNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEY 1409
Cdd:PRK09029 15 VRPQAIALRLNDEVLTWQQLCARIDQLAAGFAQQGVVEGSGVALRGKNSPETLLAYLALLQCGARVLPLNPQLPQPLLEE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1410 MLTDSGCSHVLVhqnsiikgIEFQGNVIDLMDMSFEEEPGEDMHMMiEPHNLAYVIYTSGSTGQPKGVMIEHRS-LTN-- 1486
Cdd:PRK09029 95 LLPSLTLDFALV--------LEGENTFSALTSLHLQLVEGAHAVAW-QPQRLATMTLTSGSTGLPKAAVHTAQAhLASae 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1487 -FLCAMyeDFSQDigitDNVLFSssisfdvtifeifVPLIY-------------GARMTIYQGEKFDvtklvQVIleEQV 1552
Cdd:PRK09029 166 gVLSLM--PFTAQ----DSWLLS-------------LPLFHvsgqgivwrwlyaGATLVVRDKQPLE-----QAL--AGC 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1553 TLSYIPPTLLNEIYDYfvrDNQKIVLNKLLVGVEPIKTELLAKYDHlfRGnLQILNGYGPTEA--TVCCtsyryesnKEI 1630
Cdd:PRK09029 220 THASLVPTQLWRLLDN---RSEPLSLKAVLLGGAAIPVELTEQAEQ--QG-IRCWCGYGLTEMasTVCA--------KRA 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1631 -TTQNVpiGSPLLNTKIYILDsfhriqpigvpGEICISGIGLARGYINRKELTadkfidhPFERGEKLYKTGDIARWLpD 1709
Cdd:PRK09029 286 dGLAGV--GSPLPGREVKLVD-----------GEIWLRGASLALGYWRQGQLV-------PLVNDEGWFATRDRGEWQ-N 344
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1710 GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQED-EAGEKYLcAYVVTEKDIPIPEVRAYLATKL---- 1784
Cdd:PRK09029 345 GELTILGRLDNLFFSGGEGIQPEEIERVINQHPLVQQVFVVPVADaEFGQRPV-AVVESDSEAAVVNLAEWLQDKLarfq 423
|
490 500 510
....*....|....*....|....*....|...
gi 446807313 1785 -P--HYMIPQQLipihnipltQNG--KIDRSKL 1812
Cdd:PRK09029 424 qPvaYYLLPPEL---------KNGgiKISRQAL 447
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
287-775 |
1.09e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 101.01 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 287 QNPNQIAIVCNGKEITYKQLNIKANQLARrLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEY 366
Cdd:PRK07638 13 LQPNKIAIKENDRVLTYKDWFESVCKVAN-WLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKE 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 367 MLTDSGCSHVLTYQNSIIKGVAFQGSVINLMDI-PFEEEQVEDLQITMEPQNLA-YVIYTSGSTGQPKGVMIEHRS-LTN 443
Cdd:PRK07638 92 RLAISNADMIVTERYKLNDLPDEEGRVIEIDEWkRMIEKYLPTYAPIENVQNAPfYMGFTSGSTGKPKAFLRAQQSwLHS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 444 FLCAMyEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLVCGArmTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLneiy 523
Cdd:PRK07638 172 FDCNV-HDFH--MKREDSVLIAGTLVHSLFLYGAISTLYVGQ--TVHLMRKFIPNQVLDKLETENISVMYTVPTML---- 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 524 DYFVRANQKISlNKLFVGVEPIKTELLAK------YDHLfrgnlQILNLYGPTEATVccTSYQYERDKEITTQNVpiGSP 597
Cdd:PRK07638 243 ESLYKENRVIE-NKMKIISSGAKWEAEAKekikniFPYA-----KLYEFYGASELSF--VTALVDEESERRPNSV--GRP 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 598 LLNTKIYILDSfhrlqpigvPGEICISG-IG--------LARGYINRKELtadkfidhPFERGEKLYKT-GDIARWLPDG 667
Cdd:PRK07638 313 FHNVQVRICNE---------AGEEVQKGeIGtvyvkspqFFMGYIIGGVL--------ARELNADGWMTvRDVGYEDEEG 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 668 NIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKylcAYVVTEKDIPIPEVRAYLATKLPYYMI 746
Cdd:PRK07638 376 FIYIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYwGEK---PVAIIKGSATKQQLKSFCLQRLSSFKI 452
|
490 500
....*....|....*....|....*....
gi 446807313 747 PQQIISIQNIPLTQNGKIDRKKLPQPINN 775
Cdd:PRK07638 453 PKEWHFVDEIPYTNSGKIARMEAKSWIEN 481
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
280-771 |
1.39e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 101.36 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 280 LFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTEL 359
Cdd:PRK06164 15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 360 PKQRVEYMLTDSGCShVLTYQNSIiKGVAFQGsVINLMD-----------------------IPFEEEQVEDLQITMEPQ 416
Cdd:PRK06164 95 RSHEVAHILGRGRAR-WLVVWPGF-KGIDFAA-ILAAVPpdalpplraiavvddaadatpapAPGARVQLFALPDPAPPA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 417 ---------NLAYVIYT-SGSTGQPKGVMieHRSLTnfLCAMYEDFSQDIGITDN--VLFSSSISFDVTIFEIFVPLVCG 484
Cdd:PRK06164 172 aageraadpDAGALLFTtSGTTSGPKLVL--HRQAT--LLRHARAIARAYGYDPGavLLAALPFCGVFGFSTLLGALAGG 247
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 485 ArmTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKL-FVGVEPIKTELLAKYdhLFRGnLQI 563
Cdd:PRK06164 248 A--PLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILDTAGERADFPSARLFgFASFAPALGELAALA--RARG-VPL 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 564 LNLYGPTE--ATVCCtsyqYERDKEITTQNVPIGSPLL-NTKIYILDSFH-RLQPIGVPGEICISGIGLARGYINRKELT 639
Cdd:PRK06164 323 TGLYGSSEvqALVAL----QPATDPVSVRIEGGGRPASpEARVRARDPQDgALLPDGESGEIEIRAPSLMRGYLDNPDAT 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 640 ADKFIDHPFergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDEsGEKYLC 719
Cdd:PRK06164 399 ARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD-GKTVPV 471
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 720 AYVVTEKDIPI--PEVRAYLATKLPYYMIPQQIISIQNIPLTQNG---KIDRKKLPQ 771
Cdd:PRK06164 472 AFVIPTDGASPdeAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRLRE 528
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
1344-1720 |
1.89e-21 |
|
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: 101.14 E-value: 1.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKR--ESIVGVMMKRSIEMVIGILGVLKAGGAYLPI-DTdLPKQRVEYMLTDSGCSHVL 1420
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLyDT-LGPEAIEYILNHAEISIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1421 VHqnsiiKGIEFqgnvidlmdMSFEEEpgEDM-------HMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYE 1493
Cdd:cd05927 85 CD-----AGVKV---------YSLEEF--EKLgkknkvpPPPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1494 DFSQDIGITDN-VLFSssisfdvtifeiFVPL--IY-----------GARMTIYQGekfDVTKLVQVILEEQVTLSYIPP 1559
Cdd:cd05927 149 ILEILNKINPTdVYIS------------YLPLahIFervvealflyhGAKIGFYSG---DIRLLLDDIKALKPTVFPGVP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TLLNEIYDYFVRDNQ---------------------------------KIVLNK-----------LLVGVEPIKTELLAK 1595
Cdd:cd05927 214 RVLNRIYDKIFNKVQakgplkrklfnfalnyklaelrsgvvraspfwdKLVFNKikqalggnvrlMLTGSAPLSPEVLEF 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1596 ydhlFRGNL--QILNGYGPTEAT-VCCTSYRYESNkeITTqnvpIGSPLLNTKIYILDsfhriqpigVP----------- 1661
Cdd:cd05927 294 ----LRVALgcPVLEGYGQTECTaGATLTLPGDTS--VGH----VGGPLPCAEVKLVD---------VPemnydakdpnp 354
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1662 -GEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDH 1720
Cdd:cd05927 355 rGEVCIRGPNVFSGYYKDPEKTAEALDE------DGWLHTGDIGEWLPNGTLKIIDRKKN 408
|
|
| FADD10 |
cd17635 |
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain ... |
1464-1809 |
1.93e-21 |
|
adenylate forming domain, fatty acid CoA ligase (FadD10); This family contains long chain fatty acid CoA ligases, including FadD10 which is involved in the synthesis of a virulence-related lipopeptide. FadD10 is a fatty acyl-AMP ligase (FAAL) that transfers fatty acids to an acyl carrier protein. Structures of FadD10 in apo- and complexed form with dodecanoyl-AMP, show a novel open conformation, facilitated by its unique inter-domain and intermolecular interactions, which is critical for the enzyme to carry out the acyl transfer onto the acyl carrier protein (Rv0100) rather than coenzyme A.
Pssm-ID: 341290 [Multi-domain] Cd Length: 340 Bit Score: 98.10 E-value: 1.93e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 VIYTSGSTGQPKGVMIEHRSLtnFLCAMYEDFSQDIGITDNVLFS-SSISFDVTIFEIFVPLIYGARMTIYqGEKFDVTK 1542
Cdd:cd17635 6 VIFTSGTTGEPKAVLLANKTF--FAVPDILQKEGLNWVVGDVTYLpLPATHIGGLWWILTCLIHGGLCVTG-GENTTYKS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1543 LVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKI-VLNKLLVGVE-PIKTEllaKYDHLFRGNLQILNGYGPTE-ATVCC 1619
Cdd:cd17635 83 LFKILTTNAVTTTCLVPTLLSKLVSELKSANATVpSLRLIGYGGSrAIAAD---VRFIEATGLTNTAQVYGLSEtGTALC 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1620 TSYRYESnKEITTqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFergeklyK 1699
Cdd:cd17635 160 LPTDDDS-IEINA----VGRPYPGVDVYLAATDGIAGPSASFGTIWIKSPANMLGYWNNPERTAEVLIDGWV-------N 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1700 TGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLCAYVVTEKDIP--IPEV 1776
Cdd:cd17635 228 TGDLGERREDGFLFITGRSSESINCGGVKIAPDEVERIAEGVSGVQECACYEISDEEfGELVGLAVVASAELDEnaIRAL 307
|
330 340 350
....*....|....*....|....*....|...
gi 446807313 1777 RAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:cd17635 308 KHTIRRELEPYARPSTIVIVTDIPRTQSGKVKR 340
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
414-768 |
2.65e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 100.84 E-value: 2.65e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 414 EPQNLAYVIYTSGSTGQPKGVMIEHRSL-TNflCAMYEDFSQDIGITDNVLFSSSISFD---VTIFEIFVPLvCGARMTI 489
Cdd:PRK05605 217 TPDDVALILYTSGTTGKPKGAQLTHRNLfAN--AAQGKAWVPGLGDGPERVLAALPMFHaygLTLCLTLAVS-IGGELVL 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 490 YqgEKFDVPKLVQVILEEQVT-LAYIPPtllneIYDYFVRANQK--ISLNKL---FVGVEPIKTELLAKYDHLFRGNLqi 563
Cdd:PRK05605 294 L--PAPDIDLILDAMKKHPPTwLPGVPP-----LYEKIAEAAEErgVDLSGVrnaFSGAMALPVSTVELWEKLTGGLL-- 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 564 LNLYGPTEAT--VCCTSyqyerdkeITTQNVP--IGSPLLNTKIYILD--SFHRLQPIGVPGEICISGIGLARGYINRKE 637
Cdd:PRK05605 365 VEGYGLTETSpiIVGNP--------MSDDRRPgyVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 638 LTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKY 717
Cdd:PRK05605 437 ETAKSFLD-------GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEE 509
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446807313 718 LCAYVVTEKDIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKK 768
Cdd:PRK05605 510 VVAAVVLEPGAALDPegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRRRE 562
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
287-770 |
4.78e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 99.62 E-value: 4.78e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 287 QNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPK----- 361
Cdd:PRK07788 61 RAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGpqlae 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 362 ----QRVEYMLTDSGCSHVLTY-QNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNL-------AYVIYTSGSTG 429
Cdd:PRK07788 141 vaarEGVKALVYDDEFTDLLSAlPPDLGRLRAWGGNPDDDEPSGSTDETLDDLIAGSSTAPLpkppkpgGIVILTSGTTG 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 430 QPKGVMIEH----RSLTNFLCAMyeDFSQDigitDNVLFSSSIsFDVTIFEIFVpLVCGARMTIYQGEKFDVPKLVQVIL 505
Cdd:PRK07788 221 TPKGAPRPEpsplAPLAGLLSRV--PFRAG----ETTLLPAPM-FHATGWAHLT-LAMALGSTVVLRRRFDPEATLEDIA 292
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 506 EEQVTLAYIPPTLLNEIYDYFVRANQKI---SLNKLFVGVEPIKTELLAKYDHLFrGNLqILNLYGPTEATVCCTSYQYE 582
Cdd:PRK07788 293 KHKATALVVVPVMLSRILDLGPEVLAKYdtsSLKIIFVSGSALSPELATRALEAF-GPV-LYNLYGSTEVAFATIATPED 370
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 583 RDKEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINrkelTADKfidhpfERGEKLYKTGDIAR 662
Cdd:PRK07788 371 LAEAPGT----VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD----GRDK------QIIDGLLSSGDVGY 436
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 663 WLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPE--VRAYLATK 740
Cdd:PRK07788 437 FDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQRLRAFVVKAPGAALDEdaIKDYVRDN 516
|
490 500 510
....*....|....*....|....*....|
gi 446807313 741 LPYYMIPQQIISIQNIPLTQNGKIDRKKLP 770
Cdd:PRK07788 517 LARYKVPRDVVFLDELPRNPTGKVLKRELR 546
|
|
| PRK07786 |
PRK07786 |
long-chain-fatty-acid--CoA ligase; Validated |
1332-1812 |
5.03e-21 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 169098 [Multi-domain] Cd Length: 542 Bit Score: 99.47 E-value: 5.03e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:PRK07786 31 PDAPALRFLGNTTTWRELDDRVAALAGALSRRGVGFGDRVLILMLNRTEFVESVLAANMLGAIAVPVNFRLTPPEIAFLV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 TDSGCSHVLVH-----------------QNSIIKGIEFQGNVIDLMDMSfeEEPGEDMHMMIEPHNL-AYVIYTSGSTGQ 1473
Cdd:PRK07786 111 SDCGAHVVVTEaalapvatavrdivpllSTVVVAGGSSDDSVLGYEDLL--AEAGPAHAPVDIPNDSpALIMYTSGTTGR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1474 PKGVMIEHRSLT----NFLCAMYEDFSQDIGitdnvlFSSSISFDVTIFEIFVP-LIYGARMTIYQGEKFDVTKLVQVIL 1548
Cdd:PRK07786 189 PKGAVLTHANLTgqamTCLRTNGADINSDVG------FVGVPLFHIAGIGSMLPgLLLGAPTVIYPLGAFDPGQLLDVLE 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1549 EEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYDHLFRGNlQILNGYGPTEAT-VCCTSYRYESN 1627
Cdd:PRK07786 263 AEKVTGIFLVPAQWQAVCAEQQARPRDLALRVLSWGAAPASDTLLRQMAATFPEA-QILAAFGQTEMSpVTCMLLGEDAI 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1628 KEITTqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIARWL 1707
Cdd:PRK07786 342 RKLGS----VGKVIPTVAARVVDENMNDVPVGEVGEIVYRAPTLMSGYWNNPEATAEAFAGGWFH-------SGDLVRQD 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1708 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLCAYVVT--EKDIPIPEVRAYLATKL 1784
Cdd:PRK07786 411 EEGYVWVVDRKKDMIISGGENIYCAEVENVLASHPDIVEVAVIGRADEKwGEVPVAVAAVRndDAALTLEDLAEFLTDRL 490
|
490 500
....*....|....*....|....*...
gi 446807313 1785 PHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK07786 491 ARYKHPKALEIVDALPRNPAGKVLKTEL 518
|
|
| PRK07638 |
PRK07638 |
acyl-CoA synthetase; Validated |
1331-1814 |
6.18e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236071 [Multi-domain] Cd Length: 487 Bit Score: 98.70 E-value: 6.18e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1331 NPNQIAVVCNEKGITYNELNIKANQLARrLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYM 1410
Cdd:PRK07638 14 QPNKIAIKENDRVLTYKDWFESVCKVAN-WLNEKESKNKTIAILLENRIEFLQLFAGAAMAGWTCVPLDIKWKQDELKER 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1411 LTDSGCSHVLVHQNSIIKGIEFQGNVIDL---MDMSFEEEP----GEDMHmmiepHNLAYVIYTSGSTGQPKGVMIEHRS 1483
Cdd:PRK07638 93 LAISNADMIVTERYKLNDLPDEEGRVIEIdewKRMIEKYLPtyapIENVQ-----NAPFYMGFTSGSTGKPKAFLRAQQS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1484 -LTNFLCAMyEDFSqdIGITDNVLFSSSIsfdvtIFEIFvplIYGARMTIYQG------EKFDVTKLVQVILEEQVTLSY 1556
Cdd:PRK07638 168 wLHSFDCNV-HDFH--MKREDSVLIAGTL-----VHSLF---LYGAISTLYVGqtvhlmRKFIPNQVLDKLETENISVMY 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1557 IPPTLLNEIY--DYFVRDNQKIVLNKLLVGVEPiKTELLAKYDHLfrgnlQILNGYGPTEATVCCTSYRYESNKEITTqn 1634
Cdd:PRK07638 237 TVPTMLESLYkeNRVIENKMKIISSGAKWEAEA-KEKIKNIFPYA-----KLYEFYGASELSFVTALVDEESERRPNS-- 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1635 vpIGSPLLNTKIYILDSF-HRIQPiGVPGEICISGIGLARGYINRKELtadkfidhPFERGEKLYKT-GDIARWLPDGNI 1712
Cdd:PRK07638 309 --VGRPFHNVQVRICNEAgEEVQK-GEIGTVYVKSPQFFMGYIIGGVL--------ARELNADGWMTvRDVGYEDEEGFI 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1713 EYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKylcAYVVTEKDIPIPEVRAYLATKLPHYMIPQ 1791
Cdd:PRK07638 378 YIVGREKNMILFGGINIFPEEIESVLHEHPAVDEIVVIGVPDSYwGEK---PVAIIKGSATKQQLKSFCLQRLSSFKIPK 454
|
490 500
....*....|....*....|...
gi 446807313 1792 QLIPIHNIPLTQNGKIDRSKLPK 1814
Cdd:PRK07638 455 EWHFVDEIPYTNSGKIARMEAKS 477
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
1336-1812 |
6.21e-21 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 98.52 E-value: 6.21e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1336 AVVCNEKGITYNELNIKANQLARRLLdqGVKResiVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSG 1415
Cdd:PRK07787 18 AVRIGGRVLSRSDLAGAATAVAERVA--GARR---VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1416 CSHVLVHQNSIIKGIEfqgNV-IDLMDMSFEEEPGEDmhmmiePHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYED 1494
Cdd:PRK07787 93 AQAWLGPAPDDPAGLP---HVpVRLHARSWHRYPEPD------PDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1495 FsqdiGIT-DNVLFSSSISFDV--TIFEIFVPLIYGARMtIYQGeKFDVTKLVQViLEEQVTLSYIPPTllneIYDYFVR 1571
Cdd:PRK07787 164 W----QWTaDDVLVHGLPLFHVhgLVLGVLGPLRIGNRF-VHTG-RPTPEAYAQA-LSEGGTLYFGVPT----VWSRIAA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1572 DN---QKIVLNKLLV-GVEPIKTELLAKYDHLfrGNLQILNGYGPTEaTVCCTSYRYESNKEITTqnvpIGSPLLNTKIY 1647
Cdd:PRK07787 233 DPeaaRALRGARLLVsGSAALPVPVFDRLAAL--TGHRPVERYGMTE-TLITLSTRADGERRPGW----VGLPLAGVETR 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1648 ILDSfhriqpIGVP--------GEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLGR-- 1717
Cdd:PRK07787 306 LVDE------DGGPvphdgetvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGRes 373
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1718 VDhQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKyLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPI 1796
Cdd:PRK07787 374 TD-LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDdLGQR-IVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFV 451
|
490
....*....|....*.
gi 446807313 1797 HNIPLTQNGKIDRSKL 1812
Cdd:PRK07787 452 DALPRNAMGKVLKKQL 467
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
1460-1807 |
7.31e-21 |
|
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: 96.03 E-value: 7.31e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1460 NLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGIT--DNVL----FSSSISFDVTifeIFVPLIYGArmTIY 1533
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL----RAAAAWADCADLTedDRYLiinpFFHTFGYKAG---IVACLLTGA--TVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1534 QGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLLV-GVEPIKTELLAKYdHLFRGNLQILNGYGP 1612
Cdd:cd17638 72 PVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtGAATVPVELVRRM-RSELGFETVLTAYGL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1613 TEAtVCCTSYRYESNKEITTQNVpiGSPLLNTKIYILDsfhriqpigvPGEICISGIGLARGYINRKELTAdKFIDhpfE 1692
Cdd:cd17638 151 TEA-GVATMCRPGDDAETVATTC--GRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATA-EAID---A 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1693 RGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIP 1772
Cdd:cd17638 214 DG--WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVVARPGVT 291
|
330 340 350
....*....|....*....|....*....|....*..
gi 446807313 1773 IPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:cd17638 292 LTEedVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| PRK06155 |
PRK06155 |
crotonobetaine/carnitine-CoA ligase; Provisional |
276-769 |
1.67e-20 |
|
crotonobetaine/carnitine-CoA ligase; Provisional
Pssm-ID: 235719 [Multi-domain] Cd Length: 542 Bit Score: 97.91 E-value: 1.67e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 276 TAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI 355
Cdd:PRK06155 22 TLPAMLARQAERYPDRPLLVFGGTRWTYAEAARAAAAAAHALAAAGVKRGDRVALMCGNRIEFLDVFLGCAWLGAIAVPI 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 356 DTELPKQRVEYMLTDSGC------SHVLTYQNSIIKGV-------AFQGSVINLMDIPFEEEQVEDLQ-----ITMEPQN 417
Cdd:PRK06155 102 NTALRGPQLEHILRNSGArllvveAALLAALEAADPGDlplpavwLLDAPASVSVPAGWSTAPLPPLDapapaAAVQPGD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 418 LAYVIYTSGSTGQPKGVMIEHRSLtnFLCAMYEdfSQDIGIT-DNVLFSSSISFDVTIFEIFVP-LVCGARMTIyqGEKF 495
Cdd:PRK06155 182 TAAILYTSGTTGPSKGVCCPHAQF--YWWGRNS--AEDLEIGaDDVLYTTLPLFHTNALNAFFQaLLAGATYVL--EPRF 255
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 496 DVPKLVQVILEEQVTLAYipptLLNEIYDYFVR--ANQKISLNKLFVGVEP-IKTELLAKYDHLFrgNLQILNLYGPTEA 572
Cdd:PRK06155 256 SASGFWPAVRRHGATVTY----LLGAMVSILLSqpARESDRAHRVRVALGPgVPAALHAAFRERF--GVDLLDGYGSTET 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 573 TVCCTsyqyerdkeittqnVPIGSPLLNTKIYILDSFH--------RLQPIGVPGEICISG---IGLARGYINRKELTAD 641
Cdd:PRK06155 330 NFVIA--------------VTHGSQRPGSMGRLAPGFEarvvdehdQELPDGEPGELLLRAdepFAFATGYFGMPEKTVE 395
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 642 KFIDHPFErgeklykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAY 721
Cdd:PRK06155 396 AWRNLWFH-------TGDRVVRDADGWFRFVDRIKDAIRRRGENISSFEVEQVLLSHPAVAAAAVFPVPSELGEDEVMAA 468
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|
gi 446807313 722 VVTEKDIPIP--EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK06155 469 VVLRDGTALEpvALVRHCEPRLAYFAVPRYVEFVAALPKTENGKVQKFVL 518
|
|
| FadD3 |
cd17638 |
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ... |
417-764 |
1.86e-20 |
|
acyl-CoA synthetase FadD3 and similar proteins; This family contains long chain fatty acid CoA ligases, including FadD3 which is an acyl-CoA synthetase that initiates catabolism of cholesterol rings C and D in actinobacteria. The cholesterol catabolic pathway occurs in most mycolic acid-containing actinobacteria, such as Rhodococcus jostii RHA1, and is critical for Mycobacterium tuberculosis (Mtb) during infection. FadD3 catalyzes the ATP-dependent CoA thioesterification of 3a-alpha-H-4alpha(3'-propanoate)-7a-beta-methylhexahydro-1,5-indanedione (HIP) to yield HIP-CoA. Hydroxylated analogs of HIP, 5alpha-OH HIP and 1beta-OH HIP, can also be used.
Pssm-ID: 341293 [Multi-domain] Cd Length: 330 Bit Score: 94.88 E-value: 1.86e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 417 NLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGIT--DNVL----FSSSISFDVTifeIFVPLVCGArmTIY 490
Cdd:cd17638 1 DVSDIMFTSGTTGRSKGVMCAHRQTL----RAAAAWADCADLTedDRYLiinpFFHTFGYKAG---IVACLLTGA--TVV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 491 QGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFV-GVEPIKTELLAKydhlFRGNLQILNL--- 566
Cdd:cd17638 72 PVAVFDVDAILEAIERERITVLPGPPTLFQSLLDHPGRKKFDLSSLRAAVtGAATVPVELVRR----MRSELGFETVlta 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 567 YGPTEA---TVCctsyqyERDKEITTQNVPIGSPLLNTKIYILDsfhrlqpigvPGEICISGIGLARGYINRKELTAdKF 643
Cdd:cd17638 148 YGLTEAgvaTMC------RPGDDAETVATTCGRACPGFEVRIAD----------DGEVLVRGYNVMQGYLDDPEATA-EA 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 644 IDhpfERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV 723
Cdd:cd17638 211 ID---ADG--WLHTGDVGELDERGYLRITDRLKDMYIVGGFNVYPAEVEGALAEHPGVAQVAVIGVPDERMGEVGKAFVV 285
|
330 340 350 360
....*....|....*....|....*....|....*....|...
gi 446807313 724 TEKDIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKI 764
Cdd:cd17638 286 ARPGVTLTEedVIAWCRERLANYKVPRFVRFLDELPRNASGKV 328
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
417-766 |
3.55e-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: 94.01 E-value: 3.55e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 417 NLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLVCGaRMTIYQGeKFD 496
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFN--ISGEDAILAPGPLSHSLFLYGAISALYLG-GTFIGQR-KFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 497 VPKLVQVILEEQVTLAYIPPTLLNEIYdyfvRANQKISLNK-LFVGVEPIKTELLAKYDHLFRgNLQILNLYGPTEAT-V 574
Cdd:cd17633 77 PKSWIRKINQYNATVIYLVPTMLQALA----RTLEPESKIKsIFSSGQKLFESTKKKLKNIFP-KANLIEFYGTSELSfI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 575 CCTSYQYERDKEittqnvPIGSPLLNTKIYILDSFHrlqpiGVPGEICISGIGLARGYINRKELTADKFidhpfergekl 654
Cdd:cd17633 152 TYNFNQESRPPN------SVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW----------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 655 YKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAyVVTEKDIPIPEVR 734
Cdd:cd17633 210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA-LYSGDKLTYKQLK 288
|
330 340 350
....*....|....*....|....*....|..
gi 446807313 735 AYLATKLPYYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:cd17633 289 RFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| PRK07059 |
PRK07059 |
Long-chain-fatty-acid--CoA ligase; Validated |
1315-1812 |
3.59e-20 |
|
Long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235923 [Multi-domain] Cd Length: 557 Bit Score: 97.01 E-value: 3.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1315 SNYLLVHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGA 1394
Cdd:PRK07059 20 SQYPSLADLLEESFRQYADRPAFICMGKAITYGELDELSRALAAWLQSRGLAKGARVAIMMPNVLQYPVAIAAVLRAGYV 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1395 YLPIDTDLPKQRVEYMLTDSGCSHVLVHQN------SIIKGIEFQGNVIDLM-DM------------------------- 1442
Cdd:PRK07059 100 VVNVNPLYTPRELEHQLKDSGAEAIVVLENfattvqQVLAKTAVKHVVVASMgDLlgfkghivnfvvrrvkkmvpawslp 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1443 ---SFEEEPGEDMHMMIEPHNL-----AYVIYTSGSTGQPKGVMIEHRSLT-----------------------NFLCAM 1491
Cdd:PRK07059 180 ghvRFNDALAEGARQTFKPVKLgpddvAFLQYTGGTTGVSKGATLLHRNIVanvlqmeawlqpafekkprpdqlNFVCAL 259
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1492 --YEDFSqdigITDNVLFSSSISfDVTIfeifvpLIYGARmtiyqgekfDVTKLVQVILEEQVTLsyIPP--TLLNEIYD 1567
Cdd:PRK07059 260 plYHIFA----LTVCGLLGMRTG-GRNI------LIPNPR---------DIPGFIKELKKYQVHI--FPAvnTLYNALLN 317
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1568 YfvRDNQKIVLNKLLVGV-------EPIKTELLAKYdhlfrgNLQILNGYGPTEATVCCTSYRYESNKEITTqnvpIGSP 1640
Cdd:PRK07059 318 N--PDFDKLDFSKLIVANgggmavqRPVAERWLEMT------GCPITEGYGLSETSPVATCNPVDATEFSGT----IGLP 385
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1641 LLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKE-----LTADKFidhpfergeklYKTGDIARWLPDGNIEYL 1715
Cdd:PRK07059 386 LPSTEVSIRDDDGNDLPLGEPGEICIRGPQVMAGYWNRPDetakvMTADGF-----------FRTGDVGVMDERGYTKIV 454
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1716 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVtEKDIPIPE--VRAYLATKLPHYMIPQQL 1793
Cdd:PRK07059 455 DRKKDMILVSGFNVYPNEIEEVVASHPGVLEVAAVGVPDEHSGEAVKLFVV-KKDPALTEedVKAFCKERLTNYKRPKFV 533
|
570
....*....|....*....
gi 446807313 1794 IPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK07059 534 EFRTELPKTNVGKILRREL 552
|
|
| AFD_YhfT-like |
cd17633 |
fatty acid-CoA ligase VraA; This family of acyl-CoA ligases includes Bacillus subtilis YhfT, ... |
1460-1809 |
3.71e-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: 94.01 E-value: 3.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1460 NLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqdIGITDNVLFSSSISFDVTIFEIFVPLiYGARMTIYQGeKFD 1539
Cdd:cd17633 1 NPFYIGFTSGTTGLPKAYYRSERSWIESFVCNEDLFN--ISGEDAILAPGPLSHSLFLYGAISAL-YLGGTFIGQR-KFN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1540 VTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQ-KIVLNkllvGVEPIKTELLAKYDHLFRgNLQILNGYGPTEAtvc 1618
Cdd:cd17633 77 PKSWIRKINQYNATVIYLVPTMLQALARTLEPESKiKSIFS----SGQKLFESTKKKLKNIFP-KANLIEFYGTSEL--- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1619 ctSY-RYESNKEITTQNvPIGSPLLNTKIYILDSFHriqpiGVPGEICISGIGLARGYINRKELTADKFidhpfergekl 1697
Cdd:cd17633 149 --SFiTYNFNQESRPPN-SVGRPFPNVEIEIRNADG-----GEIGKIFVKSEMVFSGYVRGGFSNPDGW----------- 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1698 YKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAyVVTEKDIPIPEVR 1777
Cdd:cd17633 210 MSVGDIGYVDEEGYLYLVGRESDMIIIGGINIFPTEIESVLKAIPGIEEAIVVGIPDARFGEIAVA-LYSGDKLTYKQLK 288
|
330 340 350
....*....|....*....|....*....|..
gi 446807313 1778 AYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:cd17633 289 RFLKQKLSRYEIPKKIIFVDSLPYTSSGKIAR 320
|
|
| MACS_like_1 |
cd05974 |
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the ... |
301-769 |
4.53e-20 |
|
Uncharacterized subfamily of medium-chain acyl-CoA synthetase (MACS); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. MACS enzymes are localized to mitochondria.
Pssm-ID: 341278 [Multi-domain] Cd Length: 432 Bit Score: 95.71 E-value: 4.53e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 301 ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVeymltdsgcshvltyQ 380
Cdd:cd05974 1 VSFAEMSARSSRVANFLRSIGVGRGDRILLMLGNVVELWEAMLAAMKLGAVVIPATTLLTPDDL---------------R 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 381 NSIIKGVAFQGSVinlmdipfeeeqvEDLQITMEPQnLAYviYTSGSTGQPKGVMIEHRSL-TNFLCAMYEdfsqdIGIT 459
Cdd:cd05974 66 DRVDRGGAVYAAV-------------DENTHADDPM-LLY--FTSGTTSKPKLVEHTHRSYpVGHLSTMYW-----IGLK 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 460 --DNVLFSSSISFDVTIFE-IFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTllneIYDYFVRANQ---KI 533
Cdd:cd05974 125 pgDVHWNISSPGWAKHAWScFFAPWNAGATVFLFNYARFDAKRVLAALVRYGVTTLCAPPT----VWRMLIQQDLasfDV 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 534 SLNKLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVCCTSYqyerdkeiTTQNVPIGS---PLLNTKIYILDsfh 610
Cdd:cd05974 201 KLREVVGAGEPLNPEVIEQVRRAW--GLTIRDGYGQTETTALVGNS--------PGQPVKAGSmgrPLPGYRVALLD--- 267
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 611 rlqPIGVP---GEICIS-----GIGLARGYINRKELTADKFidhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIR 682
Cdd:cd05974 268 ---PDGAPateGEVALDlgdtrPVGLMKGYAGDPDKTAHAM-------RGGYYRTGDIAMRDEDGYLTYVGRADDVFKSS 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 683 GYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-TEKDIPIPE----VRAYLATKL-PYYMIPQqiISIQNI 756
Cdd:cd05974 338 DYRISPFELESVLIEHPAVAEAAVVPSPDPVRLSVPKAFIVlRAGYEPSPEtaleIFRFSRERLaPYKRIRR--LEFAEL 415
|
490
....*....|...
gi 446807313 757 PLTQNGKIDRKKL 769
Cdd:cd05974 416 PKTISGKIRRVEL 428
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
276-769 |
2.08e-19 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 94.56 E-value: 2.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 276 TAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLP 354
Cdd:PRK08751 26 TVAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVN 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 355 IDTELPKQRVEYMLTDSGCSHVL-------TYQNSI----IKGVAF----------QGSVINLMdIPFEEEQVEDLQIT- 412
Cdd:PRK08751 106 VNPLYTPRELKHQLIDSGASVLVvidnfgtTVQQVIadtpVKQVITtglgdmlgfpKAALVNFV-VKYVKKLVPEYRINg 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 413 --------------------MEPQNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGITDNVLFSSSISFD- 471
Cdd:PRK08751 185 airfrealalgrkhsmptlqIEPDDIAFLQYTGGTTGVAKGAMLTHRNLV----ANMQQAHQWLAGTGKLEEGCEVVITa 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 472 VTIFEIFVPLVCGARMTIYQG------EKFDVPKLVQVILEEQVTLAYIPPTLLNEI-----YDYFVRANQKISLNKLFV 540
Cdd:PRK08751 261 LPLYHIFALTANGLVFMKIGGcnhlisNPRDMPGFVKELKKTRFTAFTGVNTLFNGLlntpgFDQIDFSSLKMTLGGGMA 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 541 gVEPIKTELLAKYDHLfrgnlQILNLYGPTEAT--VCCTSYqyerdkEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVP 618
Cdd:PRK08751 341 -VQRSVAERWKQVTGL-----TLVEAYGLTETSpaACINPL------TLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEI 408
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 619 GEICISGIGLARGYINRKELTAdKFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 698
Cdd:PRK08751 409 GELCIKGPQVMKGYWKRPEETA-KVMD-----ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMM 482
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313 699 E-TIKTAVVIQREDESGEkyLCAYVVTEKD--IPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK08751 483 PgVLEVAAVGVPDEKSGE--IVKVVIVKKDpaLTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| ACLS-CaiC |
cd17637 |
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ... |
1464-1809 |
2.27e-19 |
|
acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II; This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized, but may be similar to Carnitine-CoA ligase (CaiC) which catalyzes the transfer of CoA to carnitine. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341292 [Multi-domain] Cd Length: 333 Bit Score: 91.56 E-value: 2.27e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 VIYTSGSTGQPKGVMIEHRsltNFLCAMYEdFSQDIGITD-----NVLfsssisfdvtifeifvPL--IYGARM---TIY 1533
Cdd:cd17637 5 IIHTAAVAGRPRGAVLSHG---NLIAANLQ-LIHAMGLTEadvylNML----------------PLfhIAGLNLalaTFH 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1534 QG------EKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKIVLNKLLVGVE-PiktELLAKYDHLFRGNLQI 1606
Cdd:cd17637 65 AGganvvmEKFDPAEALELIEEEKVTLMGSFPPILSNLLDAAEKSGVDLSSLRHVLGLDaP---ETIQRFEETTGATFWS 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1607 lnGYGPTEaTVCCTSYRYESNKEITTqnvpiGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTAdkf 1686
Cdd:cd17637 142 --LYGQTE-TSGLVTLSPYRERPGSA-----GRPGPLVRVRIVDDNDRPVPAGETGEIVVRGPLVFQGYWNLPELTA--- 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1687 idHPFERGekLYKTGDIARWLPDGNIEYLGRVDHQ--VKIRGYRIELGEIEASLLKYETIKTAVVIDQED-EAGE--KYL 1761
Cdd:cd17637 211 --YTFRNG--WHHTGDLGRFDEDGYLWYAGRKPEKelIKPGGENVYPAEVEKVILEHPAIAEVCVIGVPDpKWGEgiKAV 286
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1762 CA----YVVTEKdipipEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:cd17637 287 CVlkpgATLTAD-----ELIEFVGSRIARYKKPRYVVFVEALPKTADGSIDR 333
|
|
| LC-FACS_euk |
cd05927 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS); The members of this family are ... |
301-677 |
3.00e-19 |
|
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: 94.20 E-value: 3.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 301 ITYKQLNIKANQLARRLLDQGVKR--EFIVGVMMERSIEMIVGILGILKAGGAYLPI-DTeLPKQRVEYMLTDSGCSHVL 377
Cdd:cd05927 6 ISYKEVAERADNIGSALRSLGGKPapASFVGIYSINRPEWIISELACYAYSLVTVPLyDT-LGPEAIEYILNHAEISIVF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 378 tyqnsIIKGVAFQgSVINLMDIpfEEEQVEDLqITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIG 457
Cdd:cd05927 85 -----CDAGVKVY-SLEEFEKL--GKKNKVPP-PPPKPEDLATICYTSGTTGNPKGVMLTHGNIVSNVAGVFKILEILNK 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 458 ITDNvlfSSSISF--DVTIFEIFVPLVC---GARMTIYQGekfDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQK 532
Cdd:cd05927 156 INPT---DVYISYlpLAHIFERVVEALFlyhGAKIGFYSG---DIRLLLDDIKALKPTVFPGVPRVLNRIYDKIFNKVQA 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 533 IS--LNKLFvgvepiKTELLAKYDHLFRGNL----------------------------------------------QIL 564
Cdd:cd05927 230 KGplKRKLF------NFALNYKLAELRSGVVraspfwdklvfnkikqalggnvrlmltgsaplspevleflrvalgcPVL 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 565 NLYGPTEaTVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILDsfhrlqpigVP------------GEICISGIGLARGY 632
Cdd:cd05927 304 EGYGQTE-CTAGATLTLPGDTSVGH----VGGPLPCAEVKLVD---------VPemnydakdpnprGEVCIRGPNVFSGY 369
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446807313 633 INRKELTADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDH 677
Cdd:cd05927 370 YKDPEKTAEALDE------DGWLHTGDIGEWLPNGTLKIIDRKKN 408
|
|
| C_PKS-NRPS_PksJ-like |
cd20484 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
7-238 |
3.58e-19 |
|
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: 92.76 E-value: 3.58e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:cd20484 175 EQDMLAGAEGEEHRAYWKQQLSGTLPILELPADRPRSSAPSFEGQTYTRRLPSELSNQIKSFARSQSINLSTVFLGIFKL 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 87 LLSRYTDKDDVVIGMPVFkqGQEETVFQN------NFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLS 160
Cdd:cd20484 255 LLHRYTGQEDIIVGMPTM--GRPEERFDSligyfiNMLPIRSRILGEETFSDFIRKLQLTVLDGLDHAAYPFPAMVRDLN 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 161 LDGESNNLPLLNTIVML-----------------DDIHCyESTDKINS----DMVIRFMKNEEQLKVQVDYNSTLYSEGL 219
Cdd:cd20484 333 IPRSQANSPVFQVAFFYqnflqstslqqflaeyqDVLSI-EFVEGIHQegeyELVLEVYEQEDRFTLNIKYNPDLFDAST 411
|
250
....*....|....*....
gi 446807313 220 VSRIVNHLYNILDILMKDP 238
Cdd:cd20484 412 IERMMEHYVKLAEELIANP 430
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
1322-1812 |
4.86e-19 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 93.34 E-value: 4.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1322 KMFEEQVKRNPNQIAVVCNEKGI--TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:PRK08315 20 QLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILVTIN 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSGCShVLVHQNSIiKGIEFQGNVIDLMDMSFEEEPGE-------DMHMMI----EPHNLAY----- 1463
Cdd:PRK08315 100 PAYRLSELEYALNQSGCK-ALIAADGF-KDSDYVAMLYELAPELATCEPGQlqsarlpELRRVIflgdEKHPGMLnfdel 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 -----------------------VI---YTSGSTGQPKGVMIEHRSLTN--FLCAMYEDFSQDigitDNVLfsssisfdv 1515
Cdd:PRK08315 178 lalgravddaelaarqatldpddPIniqYTSGTTGFPKGATLTHRNILNngYFIGEAMKLTEE----DRLC--------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1516 tifeIFVPLIY--------------GARMtIYQGEKFDVTKLVQVILEEQVTLSYIPPTL----LNEI----YDyfvrdn 1573
Cdd:PRK08315 245 ----IPVPLYHcfgmvlgnlacvthGATM-VYPGEGFDPLATLAAVEEERCTALYGVPTMfiaeLDHPdfarFD------ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1574 qkivLNKLLVGV---EPIKTELLAKYD---HLfrgnLQILNGYGPTEAT-VCCTSYRYES-NKEITTqnvpIGSPLLNTK 1645
Cdd:PRK08315 314 ----LSSLRTGImagSPCPIEVMKRVIdkmHM----SEVTIAYGMTETSpVSTQTRTDDPlEKRVTT----VGRALPHLE 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1646 IYILDSF-HRIQPIGVPGEICISGIGLARGYINRKELTADKfID-----HpfergeklykTGDIARWLPDGNIEYLGRVD 1719
Cdd:PRK08315 382 VKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDadgwmH----------TGDLAVMDEEGYVNIVGRIK 450
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1720 HQVkIRG----Y-RielgEIEASLLKYETIKTAVVIDQEDeagEKY---LCAYVVTEKDIPIP--EVRAYLATKLPHYMI 1789
Cdd:PRK08315 451 DMI-IRGgeniYpR----EIEEFLYTHPKIQDVQVVGVPD---EKYgeeVCAWIILRPGATLTeeDVRDFCRGKIAHYKI 522
|
570 580
....*....|....*....|...
gi 446807313 1790 PQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK08315 523 PRYIRFVDEFPMTVTGKIQKFKM 545
|
|
| PRK05605 |
PRK05605 |
long-chain-fatty-acid--CoA ligase; Validated |
1453-1809 |
6.09e-19 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 235531 [Multi-domain] Cd Length: 573 Bit Score: 93.14 E-value: 6.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1453 HMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSL-TNflCAMYEDFSQDIGITDNVLFSSSISFD---VTIFEIFVPLIyGA 1528
Cdd:PRK05605 213 HPRPTPDDVALILYTSGTTGKPKGAQLTHRNLfAN--AAQGKAWVPGLGDGPERVLAALPMFHaygLTLCLTLAVSI-GG 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1529 RMTIYqgEKFDVTKLVQVILEEQVTlsYIP--PTLLNEIYDYFVRDNQKI--VLNKLlVGVEPIKTELLAKYDHLFRGNL 1604
Cdd:PRK05605 290 ELVLL--PAPDIDLILDAMKKHPPT--WLPgvPPLYEKIAEAAEERGVDLsgVRNAF-SGAMALPVSTVELWEKLTGGLL 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1605 qiLNGYGPTEatvccTSYRYESNKeITTQNVP--IGSPLLNTKIYILD--SFHRIQPIGVPGEICISGIGLARGYINRKE 1680
Cdd:PRK05605 365 --VEGYGLTE-----TSPIIVGNP-MSDDRRPgyVGVPFPDTEVRIVDpeDPDETMPDGEEGELLVRGPQVFKGYWNRPE 436
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1681 LTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKY 1760
Cdd:PRK05605 437 ETAKSFLD-------GWFRTGDVVVMEEDGFIRIVDRIKELIITGGFNVYPAEVEEVLREHPGVEDAAVVGLPREDGSEE 509
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1761 LCAYVVTEKDIPIPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:PRK05605 510 VVAAVVLEPGAALDPegLRAYCREHLTRYKVPRRFYHVDELPRDQLGKVRR 560
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
1341-1790 |
1.12e-18 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 91.26 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1341 EKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVL 1420
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1421 VhqnsiikgiefqgnvidlmdmsfeeepgedmhmmiephNLAYVIYTSGSTGQPKGVMIEHR---SLTNFLCAMYEDFSQ 1497
Cdd:cd05940 81 V--------------------------------------DAALYIYTSGTTGLPKAAIISHRrawRGGAFFAGSGGALPS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1498 DIGITDNVLFSSSISfdvtIFEIFVPLIYGArmTIYQGEKFDVTKLVQVILEEQVTL-SYIPPT---LLN---EIYDyfv 1570
Cdd:cd05940 123 DVLYTCLPLYHSTAL----IVGWSACLASGA--TLVIRKKFSASNFWDDIRKYQATIfQYIGELcryLLNqppKPTE--- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1571 RDNQ--KIVLNkllvGVEP-IKTELLAKYdhlfrGNLQILNGYGPTEATVCCTSY--------------RYESNKEITTQ 1633
Cdd:cd05940 194 RKHKvrMIFGN----GLRPdIWEEFKERF-----GVPRIAEFYAATEGNSGFINFfgkpgaigrnpsllRKVAPLALVKY 264
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1634 NVPIGSPLLNTkiyilDSFHRIQPIGVPGEiCISGIG-LAR--GYINRKELTADKFIDhPFERGEKLYKTGDIARWLPDG 1710
Cdd:cd05940 265 DLESGEPIRDA-----EGRCIKVPRGEPGL-LISRINpLEPfdGYTDPAATEKKILRD-VFKKGDAWFNTGDLMRLDGEG 337
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1711 NIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-----DQEDEAGekylCAYVVT--EKDIPIPEVRAYLATK 1783
Cdd:cd05940 338 FWYFVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVYgvqvpGTDGRAG----MAAIVLqpNEEFDLSALAAHLEKN 413
|
....*..
gi 446807313 1784 LPHYMIP 1790
Cdd:cd05940 414 LPGYARP 420
|
|
| PRK08315 |
PRK08315 |
AMP-binding domain protein; Validated |
276-769 |
1.12e-18 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236236 [Multi-domain] Cd Length: 559 Bit Score: 92.18 E-value: 1.12e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 276 TAPQLFEEQVKQNPNQIAIVCNGKEI--TYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYL 353
Cdd:PRK08315 17 TIGQLLDRTAARYPDREALVYRDQGLrwTYREFNEEVDALAKGLLALGIEKGDRVGIWAPNVPEWVLTQFATAKIGAILV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 354 PIDTELPKQRVEYMLTDSGCSHVLT--------YQNSI----------------------IKGVAFQGSVINLMDIPFEE 403
Cdd:PRK08315 97 TINPAYRLSELEYALNQSGCKALIAadgfkdsdYVAMLyelapelatcepgqlqsarlpeLRRVIFLGDEKHPGMLNFDE 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 404 ----------EQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTN--FLCAMYEDFSQDigitDNVLfsssisfd 471
Cdd:PRK08315 177 llalgravddAELAARQATLDPDDPINIQYTSGTTGFPKGATLTHRNILNngYFIGEAMKLTEE----DRLC-------- 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 472 vtifeIFVP-----------LVC---GARMtIYQGEKFDvPKLV-QVILEEQVTLAYIPPTL----LNEI----YDyfvr 528
Cdd:PRK08315 245 -----IPVPlyhcfgmvlgnLACvthGATM-VYPGEGFD-PLATlAAVEEERCTALYGVPTMfiaeLDHPdfarFD---- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 529 anqkisLNKLFVGV---EPIKTELLAKYD---HLfrgnLQILNLYGPTEAT-VcctSYQYERD----KEITTqnvpIGSP 597
Cdd:PRK08315 314 ------LSSLRTGImagSPCPIEVMKRVIdkmHM----SEVTIAYGMTETSpV---STQTRTDdpleKRVTT----VGRA 376
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 598 LLNTKIYILDSF-HRLQPIGVPGEICISGIGLARGYINRKELTADKfID-----HpfergeklykTGDIARWLPDGNIEY 671
Cdd:PRK08315 377 LPHLEVKIVDPEtGETVPRGEQGELCTRGYSVMKGYWNDPEKTAEA-IDadgwmH----------TGDLAVMDEEGYVNI 445
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 672 LGRVDHQVkIRG----Y-RielgEIEASLLKYETIKTAVVIQREDEsgeKY---LCAYVVTEKDIPIP--EVRAYLATKL 741
Cdd:PRK08315 446 VGRIKDMI-IRGgeniYpR----EIEEFLYTHPKIQDVQVVGVPDE---KYgeeVCAWIILRPGATLTeeDVRDFCRGKI 517
|
570 580
....*....|....*....|....*...
gi 446807313 742 PYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK08315 518 AHYKIPRYIRFVDEFPMTVTGKIQKFKM 545
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
1344-1767 |
1.41e-18 |
|
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: 91.51 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGgayLPIDT---DLPKQRVEYMLTDSGCSHVL 1420
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTvyaTLGEDALIHSLNETECSAIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1421 VHQNsiikgiefqgnvidlmdmsfeeepgedmhmmiePHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIG 1500
Cdd:cd17639 83 TDGK---------------------------------PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1501 ITDNVLFSSSISFdvtIFEI---FVPLIYGARM----------TIYQGEKFDV-----TKLVQV----------ILEEQV 1552
Cdd:cd17639 130 PDDRYLAYLPLAH---IFELaaeNVCLYRGGTIgygsprtltdKSKRGCKGDLtefkpTLMVGVpaiwdtirkgVLAKLN 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1553 TLSYIPPTL-----------LNEIYDYFVRDnqKIVLNK-----------LLVGVEPIKTEllakyDHLFRGNL--QILN 1608
Cdd:cd17639 207 PMGGLKRTLfwtayqsklkaLKEGPGTPLLD--ELVFKKvraalggrlryMLSGGAPLSAD-----TQEFLNIVlcPVIQ 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1609 GYGPTEaTVCCTsyryesnkeiTTQNVP------IGSPLLNTKIYILD------SFHRIQPigvPGEICISGIGLARGYI 1676
Cdd:cd17639 280 GYGLTE-TCAGG----------TVQDPGdletgrVGPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYY 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1677 NRKELTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIR-GYRIELGEIEASLLKYETIKTAVVIDQEDE 1755
Cdd:cd17639 346 KNPEKTKEAF------DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDK 419
|
490
....*....|..
gi 446807313 1756 AgekYLCAYVVT 1767
Cdd:cd17639 420 S---YPVAIVVP 428
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
1324-1791 |
1.41e-18 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 92.24 E-value: 1.41e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLP 1403
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1404 KQRVEYMLTDSGCSHVLV------------------HQNSIIKGIEFQ--GNVIDLMDMSFE---EEPGEDMHMMIEphN 1460
Cdd:PRK08279 123 GAVLAHSLNLVDAKHLIVgeelveafeearadlarpPRLWVAGGDTLDdpEGYEDLAAAAAGaptTNPASRSGVTAK--D 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPK-GVMIEHRSLTnflcaMYEDFSQDIGITDNvlfsssisfDVtifeIFVPL-IY------------ 1526
Cdd:PRK08279 201 TAFYIYTSGTTGLPKaAVMSHMRWLK-----AMGGFGGLLRLTPD---------DV----LYCCLpLYhntggtvawssv 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1527 ---GARMTIyqGEKFDVTKLVQVILEEQVTL-SYIpptllNEIYDYFV--------RDNQ--KIVLNkllvGVEP-IKTE 1591
Cdd:PRK08279 263 laaGATLAL--RRKFSASRFWDDVRRYRATAfQYI-----GELCRYLLnqppkptdRDHRlrLMIGN----GLRPdIWDE 331
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1592 LLAKYdhlfrGNLQILNGYGPTEATVcctSYRYESNKEITTQNVPI---------------GSPLLNTKiyildsfHRIQ 1656
Cdd:PRK08279 332 FQQRF-----GIPRILEFYAASEGNV---GFINVFNFDGTVGRVPLwlahpyaivkydvdtGEPVRDAD-------GRCI 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1657 PIGvPGEI--CISGIGLAR---GYiNRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIEL 1731
Cdd:PRK08279 397 KVK-PGEVglLIGRITDRGpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVAT 474
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1732 GEIEASLLKYETIKTAVVI-----DQEDEAGekyLCAYVVTE-KDIPIPEVRAYLATKLPHYMIPQ 1791
Cdd:PRK08279 475 TEVENALSGFPGVEEAVVYgvevpGTDGRAG---MAAIVLADgAEFDLAALAAHLYERLPAYAVPL 537
|
|
| PRK07787 |
PRK07787 |
acyl-CoA synthetase; Validated |
293-772 |
2.06e-18 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236096 [Multi-domain] Cd Length: 471 Bit Score: 90.82 E-value: 2.06e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 293 AIVCNGKEITYKQLNIKANQLARRLLdqGVKRefiVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSG 372
Cdd:PRK07787 18 AVRIGGRVLSRSDLAGAATAVAERVA--GARR---VAVLATPTLATVLAVVGALIAGVPVVPVPPDSGVAERRHILADSG 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 373 CSHVLtyqnsiikgVAFQGSVINLMDIPFEEEQVEDLQI-TMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYED 451
Cdd:PRK07787 93 AQAWL---------GPAPDDPAGLPHVPVRLHARSWHRYpEPDPDAPALIVYTSGTTGPPKGVVLSRRAIAADLDALAEA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 452 FsqdiGIT-DNVLFSSSISFDV--TIFEIFVPLVCGARMtIYQGeKFDvPKLVQVILEEQVTLAYIPPTLLNEIYDYFVR 528
Cdd:PRK07787 164 W----QWTaDDVLVHGLPLFHVhgLVLGVLGPLRIGNRF-VHTG-RPT-PEAYAQALSEGGTLYFGVPTVWSRIAADPEA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 529 AnQKISLNKLFV-GVEPIKTELLAKYDHLfrGNLQILNLYGPTEaTVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILD 607
Cdd:PRK07787 237 A-RALRGARLLVsGSAALPVPVFDRLAAL--TGHRPVERYGMTE-TLITLSTRADGERRPGW----VGLPLAGVETRLVD 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 608 SfhrlqpIGVP--------GEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLGR--VDh 677
Cdd:PRK07787 309 E------DGGPvphdgetvGELQVRGPTLFDGYLNRPDATAAAFTADGW------FRTGDVAVVDPDGMHRIVGResTD- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 678 QVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKyLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNI 756
Cdd:PRK07787 376 LIKSGGYRIGAGEIETALLGHPGVREAAVVGVPDDDlGQR-IVAYVVGADDVAADELIDFVAQQLSVHKRPREVRFVDAL 454
|
490
....*....|....*.
gi 446807313 757 PLTQNGKIDRKKLPQP 772
Cdd:PRK07787 455 PRNAMGKVLKKQLLSE 470
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
1325-1814 |
3.42e-18 |
|
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step activation of medium chain fatty acids (containing 4-12 carbons). The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. The acyl-CoA is a key intermediate in many important biosynthetic and catabolic processes. MACS enzymes are localized to mitochondria. Two murine MACS family proteins are found in liver and kidney. In rodents, a MACS member is detected particularly in the olfactory epithelium and is called O-MACS. O-MACS demonstrates substrate preference for the fatty acid lengths of C6-C12.
Pssm-ID: 341251 [Multi-domain] Cd Length: 530 Bit Score: 90.60 E-value: 3.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1325 EEQVKRNPNQIAVVCNEKGI----TYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:cd05928 19 EKAGKRPPNPALWWVNGKGDevkwSFRELGSLSRKAANVLSGAcGLQRGDRVAVILPRVPEWWLVNVACIRTGLVFIPGT 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLtdsgcshvlvhQNSIIKGIEFQGNVIDLMD-----------------------MSFEE---EPGEDMH 1453
Cdd:cd05928 99 IQLTAKDILYRL-----------QASKAKCIVTSDELAPEVDsvasecpslktkllvseksrdgwLNFKEllnEASTEHH 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1454 MMIEPHNLAYVIY-TSGSTGQPKgvMIEHR----SLTNFLCAMY--EDFSQDI--GITDNVLFSSSISfdvtifEIFVPL 1524
Cdd:cd05928 168 CVETGSQEPMAIYfTSGTTGSPK--MAEHShsslGLGLKVNGRYwlDLTASDImwNTSDTGWIKSAWS------SLFEPW 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1525 IYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTllneIYDYFVRDN----QKIVLNKLLVGVEPIKTELLAKYDHlf 1600
Cdd:cd05928 240 IQGACVFVHHLPRFDPLVILKTLSSYPITTFCGAPT----VYRMLVQQDlssyKFPSLQHCVTGGEPLNPEVLEKWKA-- 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1601 RGNLQILNGYGPTEATVCCTSYRyesNKEITTQNVPIGSPLLNTKIyiLDSFHRIQPIGVPGEICIS-----GIGLARGY 1675
Cdd:cd05928 314 QTGLDIYEGYGQTETGLICANFK---GMKIKPGSMGKASPPYDVQI--IDDNGNVLPPGTEGDIGIRvkpirPFGLFSGY 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1676 INRKELTADKfidhpfERGEkLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE 1755
Cdd:cd05928 389 VDNPEKTAAT------IRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDP 461
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1756 AGEKYLCAYVV-------TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPK 1814
Cdd:cd05928 462 IRGEVVKAFVVlapqflsHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNELRD 527
|
|
| Cyc_NRPS |
cd19535 |
Cyc (heterocyclization) domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
907-1184 |
3.67e-18 |
|
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: 89.47 E-value: 3.67e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 907 DICKDKFENIFQSLIERHEILRTSFQIlDGElvQKIEPNV-DFNIEyVH----VNEKDAD--------YLIHEFISP--- 970
Cdd:cd19535 36 DLDPDRLERAWNKLIARHPMLRAVFLD-DGT--QQILPEVpWYGIT-VHdlrgLSEEEAEaaleelreRLSHRVLDVerg 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 971 --FDLSkppllrvlLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELYKGNE--LPKLRVQYKDYVMWQNgPYYKNLI 1046
Cdd:cd19535 112 plFDIR--------LSLLPEGRTRLHLSIDLLVADALSLQILLRELAALYEDPGepLPPLELSFRDYLLAEQ-ALRETAY 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1047 SEQKNYW---LTTLKG--ELPVLNFPTDFQRPTIQSFkgnvcSFNLGTDLTFKVNKLATETGTTPYMILLAIYNILLSRY 1121
Cdd:cd19535 183 ERARAYWqerLPTLPPapQLPLAKDPEEIKEPRFTRR-----EHRLSAEQWQRLKERARQHGVTPSMVLLTAYAEVLARW 257
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 1122 TGQEDIIVGSPIAGR--SHSDTNHMIGMFIN-TLV-MRNylENDDEFIEFLSRLKLNTLEAYENQDY 1184
Cdd:cd19535 258 SGQPRFLLNLTLFNRlpLHPDVNDVVGDFTSlLLLeVDG--SEGQSFLERARRLQQQLWEDLDHSSY 322
|
|
| FATP_FACS |
cd05940 |
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its ... |
298-747 |
5.50e-18 |
|
Fatty acid transport proteins (FATP) play dual roles as fatty acid transporters and its activation enzymes; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. At least five copies of FATPs are identified in mammalian cells. This family also includes prokaryotic FATPs. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis.
Pssm-ID: 341263 [Multi-domain] Cd Length: 449 Bit Score: 89.34 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 298 GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVL 377
Cdd:cd05940 1 DEALTYAELDAMANRYARWLKSLGLKPGDVVALFMENRPEYVLLWLGLVKIGAVAALINYNLRGESLAHCLNVSSAKHLV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 378 TyqnsiikgvafqgsvinlmdipfeeeqvedlqitmepqNLAYVIYTSGSTGQPKGVMIEHR---SLTNFLCAMYEDFSQ 454
Cdd:cd05940 81 V--------------------------------------DAALYIYTSGTTGLPKAAIISHRrawRGGAFFAGSGGALPS 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 455 DIGITDNVLFSSSISfdvtIFEIFVPLVCGArmTIYQGEKFDVPKLVQVILEEQVTL-AYIPPT---LLN---EIYDyfv 527
Cdd:cd05940 123 DVLYTCLPLYHSTAL----IVGWSACLASGA--TLVIRKKFSASNFWDDIRKYQATIfQYIGELcryLLNqppKPTE--- 193
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 528 RANQ--KISLNklfvGVEP-IKTELLAKYdhlfrGNLQILNLYGPTEATvcCTSYQYERDKEITTQNVPIGSPLLNTKI- 603
Cdd:cd05940 194 RKHKvrMIFGN----GLRPdIWEEFKERF-----GVPRIAEFYAATEGN--SGFINFFGKPGAIGRNPSLLRKVAPLALv 262
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 604 -YILDS---------FHRLQPIGVPGEiCISGIG-LAR--GYINRKELTADKFIDhPFERGEKLYKTGDIARWLPDGNIE 670
Cdd:cd05940 263 kYDLESgepirdaegRCIKVPRGEPGL-LISRINpLEPfdGYTDPAATEKKILRD-VFKKGDAWFNTGDLMRLDGEGFWY 340
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 671 YLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV--IQREDESGEKYLCAYVV-TEKDIPIPEVRAYLATKLPYYMIP 747
Cdd:cd05940 341 FVDRLGDTFRWKGENVSTTEVAAVLGAFPGVEEANVygVQVPGTDGRAGMAAIVLqPNEEFDLSALAAHLEKNLPGYARP 420
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
284-769 |
5.79e-18 |
|
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: 90.31 E-value: 5.79e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 284 QVKQNPNQIAIVCNGKE------ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAG-------G 350
Cdd:cd05966 62 HLKERGDKVAIIWEGDEpdqsrtITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLACARIGavhsvvfA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 351 AYLPidtELPKQRVEymltDSGCSHVLTyqnsiIKGVAFQGSVINL--------------------------------MD 398
Cdd:cd05966 142 GFSA---ESLADRIN----DAQCKLVIT-----ADGGYRGGKVIPLkeivdealekcpsvekvlvvkrtggevpmtegRD 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 399 IPFEEEqVEDLQITMEPQNLA-----YVIYTSGSTGQPKGVMieHRS--------LT-----------NFLCAmyedfsQ 454
Cdd:cd05966 210 LWWHDL-MAKQSPECEPEWMDsedplFILYTSGSTGKPKGVV--HTTggyllyaaTTfkyvfdyhpddIYWCT------A 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 455 DIG-ITDNvlfsSSIsfdvtifeIFVPLVCGARMTIYQGekfdVP------KLVQVILEEQVTLAYIPPT---LLNEIYD 524
Cdd:cd05966 281 DIGwITGH----SYI--------VYGPLANGATTVMFEG----TPtypdpgRYWDIVEKHKVTIFYTAPTairALMKFGD 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 525 YFVRANQKISLNKL-FVGvEPIKTEL-LAKYDHLFRGNLQILNLYGPTEATVCCtsyqyerdkeIT-----TQNVPiGS- 596
Cdd:cd05966 345 EWVKKHDLSSLRVLgSVG-EPINPEAwMWYYEVIGKERCPIVDTWWQTETGGIM----------ITplpgaTPLKP-GSa 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 597 --PLLNTKIYILDSFHRLQPIGVPGEICISGI--GLARGYINRKEltadKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 672
Cdd:cd05966 413 trPFFGIEPAILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWIT 488
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 673 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEKyLCAYVV-----TEKDIPIPEVRAYLATKLPYYMI 746
Cdd:cd05966 489 GRVDDVINVSGHRLGTAEVESALVAHPAVAEAAVVGRPHDiKGEA-IYAFVTlkdgeEPSDELRKELRKHVRKEIGPIAT 567
|
570 580
....*....|....*....|...
gi 446807313 747 PQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05966 568 PDKIQFVPGLPKTRSGKIMRRIL 590
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
286-680 |
7.25e-18 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 89.57 E-value: 7.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 286 KQNPNQIAIVCNG----------KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI 355
Cdd:PRK09274 17 QERPDQLAVAVPGgrgadgklayDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGAVPVLV 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 356 DTEL--------------------PKQRVEYMLTDSGCS---HVLTYQNSIIKGVAFQGSVinLMDIPFEEEQVEDLQit 412
Cdd:PRK09274 97 DPGMgiknlkqclaeaqpdafigiPKAHLARRLFGWGKPsvrRLVTVGGRLLWGGTTLATL--LRDGAAAPFPMADLA-- 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 413 mePQNLAYVIYTSGSTGQPKGVMIEHRSltnfLCAMYEDFSQDIGITDNvlfsssiSFDVTIFEIFV--PLVCGARMTIy 490
Cdd:PRK09274 173 --PDDMAAILFTSGSTGTPKGVVYTHGM----FEAQIEALREDYGIEPG-------EIDLPTFPLFAlfGPALGMTSVI- 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 491 qgekfdvP-------------KLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVEPIKTELLAKYDHL 556
Cdd:PRK09274 239 -------PdmdptrpatvdpaKLFAAIERYGVTNLFGSPALLERLGRYGEANGIKLpSLRRVISAGAPVPIAVIERFRAM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 557 FRGNLQILNLYGPTEATVCCT---SYQYERDKEITTQN--VPIGSPLLNTKIYI----------LDSFHRLqPIGVPGEI 621
Cdd:PRK09274 312 LPPDAEILTPYGATEALPISSiesREILFATRAATDNGagICVGRPVDGVEVRIiaisdapipeWDDALRL-ATGEIGEI 390
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 622 CISGIGLARGYINRKELTA-DKFIDhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVK 680
Cdd:PRK09274 391 VVAGPMVTRSYYNRPEATRlAKIPD---GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVE 447
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
271-769 |
8.58e-18 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 89.69 E-value: 8.58e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 271 LCETVTAP----QLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGIL 346
Cdd:PLN03102 6 LCEANNVPltpiTFLKRASECYPNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 347 KAGGAYLPIDTELPKQRVEYMLTDSG-------------CSHVL----TYQNSIIKGVAFqgsvINLMDIP----FEEEQ 405
Cdd:PLN03102 86 MAGAVLNPINTRLDATSIAAILRHAKpkilfvdrsfeplAREVLhllsSEDSNLNLPVIF----IHEIDFPkrpsSEELD 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 406 VEDLQITMEPQNLAY--------------VIYTSGSTGQPKGVMIEHRSLtnFLCAMYEDFSQDIGITDNVLFSSSI--- 468
Cdd:PLN03102 162 YECLIQRGEPTPSLVarmfriqdehdpisLNYTSGTTADPKGVVISHRGA--YLSTLSAIIGWEMGTCPVYLWTLPMfhc 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 469 ---SFDVTIFEIFVPLVCGARMTiyqgekfdVPKLVQVILEEQVTLAYIPPTLLNeiydYFVRANQ-----KISLNKLFV 540
Cdd:PLN03102 240 ngwTFTWGTAARGGTSVCMRHVT--------APEIYKNIEMHNVTHMCCVPTVFN----ILLKGNSldlspRSGPVHVLT 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 541 GVEPIKTELLAKYDHLfrgNLQILNLYGPTEAT--VCCTSYQYERDKEITTQNVPIGSP--LLNTKIYILDSFHRLQPIG 616
Cdd:PLN03102 308 GGSPPPAALVKKVQRL---GFQVMHAYGLTEATgpVLFCEWQDEWNRLPENQQMELKARqgVSILGLADVDVKNKETQES 384
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 617 VP------GEICISGIGLARGYINRKELTADKFiDHPFergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGE 690
Cdd:PLN03102 385 VPrdgktmGEIVIKGSSIMKGYLKNPKATSEAF-KHGW------LNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVE 457
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 691 IEASLLKY-ETIKTAVVIQREDESGEKyLCAYVVTEK-DIPIPEVRAYLATK-----------LPYYMIPQQIISIQNIP 757
Cdd:PLN03102 458 VENVLYKYpKVLETAVVAMPHPTWGET-PCAFVVLEKgETTKEDRVDKLVTRerdlieycrenLPHFMCPRKVVFLQELP 536
|
570
....*....|..
gi 446807313 758 LTQNGKIDRKKL 769
Cdd:PLN03102 537 KNGNGKILKPKL 548
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
289-764 |
1.16e-17 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 88.86 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYM 367
Cdd:PRK08314 24 PDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEELAHY 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 368 LTDSGCSHVLTYQNSIIKGVAFQGS-------VINLMD----------------------------IPFEE---EQVEDL 409
Cdd:PRK08314 104 VTDSGARVAIVGSELAPKVAPAVGNlrlrhviVAQYSDylpaepeiavpawlraepplqalapggvVAWKEalaAGLAPP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 410 QITMEPQNLAYVIYTSGSTGQPKGVMIEHRSL--TNFLCAMYEDfsqdiGITDNVLFSSSISFDVTIFE--IFVPLVCGA 485
Cdd:PRK08314 184 PHTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVmaNAVGSVLWSN-----STPESVVLAVLPLFHVTGMVhsMNAPIYAGA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 486 rmTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLneiYDYFvrANQKIS---LNKL-FVG------VEPIKTELLAKYdh 555
Cdd:PRK08314 259 --TVVLMPRWDREAAARLIERYRVTHWTNIPTMV---VDFL--ASPGLAerdLSSLrYIGgggaamPEAVAERLKELT-- 329
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 556 lfrgNLQILNLYGPTEatvccTSYQyerdkeiTTQNVP-------IGSPLLNTKIYILD--SFHRLqPIGVPGEICISGI 626
Cdd:PRK08314 330 ----GLDYVEGYGLTE-----TMAQ-------THSNPPdrpklqcLGIPTFGVDARVIDpeTLEEL-PPGEVGEIVVHGP 392
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 627 GLARGYINRKELTADKFIDhpFErGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV 706
Cdd:PRK08314 393 QVFKGYWNRPEATAEAFIE--ID-GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACV 469
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 707 IQREDE-SGE--KylcAYVV---------TEKDIpIPEVRAYLATklpyYMIPQQIISIQNIPLTQNGKI 764
Cdd:PRK08314 470 IATPDPrRGEtvK---AVVVlrpeargktTEEEI-IAWAREHMAA----YKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
286-767 |
1.23e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 88.94 E-value: 1.23e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 286 KQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVE 365
Cdd:PRK07470 18 RRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 366 YMLTDSGCS----------HV-------LTYQNSIIKGVAFQGS-----VINLMDIPFEEEQVE-DlqitmEPqnlAYVI 422
Cdd:PRK07470 98 YLAEASGARamichadfpeHAaavraasPDLTHVVAIGGARAGLdyealVARHLGARVANAAVDhD-----DP---CWFF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 423 YTSGSTGQPKGVMIEHRSL----TNFLCAMYEDFSQDigitDNVLFSSSISFDVTIFEIfVPLVCGARMTIYQGEKFDVP 498
Cdd:PRK07470 170 FTSGTTGRPKAAVLTHGQMafviTNHLADLMPGTTEQ----DASLVVAPLSHGAGIHQL-CQVARGAATVLLPSERFDPA 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 499 KLVQVILEEQVTLAYIPPTLLN--------EIYD-----YFV-------RANQKISLNKLfvgvepikTELLAKYdhlfr 558
Cdd:PRK07470 245 EVWALVERHRVTNLFTVPTILKmlvehpavDRYDhsslrYVIyagapmyRADQKRALAKL--------GKVLVQY----- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 559 gnlqilnlYGPTEATVCCT---SYQYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINR 635
Cdd:PRK07470 312 --------FGLGEVTGNITvlpPALHDAEDGPDARIGTCGFERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNN 383
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 636 KELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQRED---- 711
Cdd:PRK07470 384 PEANAKAFRDGWF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDpvwg 456
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 712 ESGekylCAYVVTEKDIPI--PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRK 767
Cdd:PRK07470 457 EVG----VAVCVARDGAPVdeAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKITKK 510
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
1344-1810 |
1.30e-17 |
|
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: 88.83 E-value: 1.30e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESiVGVMMKRSIEMVIGILGVLKAGG----AYLPidtDLPKQ--RVEYMLTDSGCS 1417
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVGKPGDR-VLLLAPPGLDFVAAFLGCLYAGAiavpLPPP---TPGRHaeRLAAILADAGPR 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1418 HVLV----------HQNSIIKGIEFQGNVIDLMDmsfEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSL-TN 1486
Cdd:cd05931 101 VVLTtaaalaavraFAASRPAAGTPRLLVVDLLP---DTSAADWPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLlAN 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1487 FLCAM--YEDFSQDIGIT------DNVLfsssisfdvtIFEIFVPLIYGARMTIYQGEKFdVTK---LVQVILEEQVTLS 1555
Cdd:cd05931 178 VRQIRraYGLDPGDVVVSwlplyhDMGL----------IGGLLTPLYSGGPSVLMSPAAF-LRRplrWLRLISRYRATIS 246
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1556 YIPptllNEIYDYFVR-----DNQKIVLNKL---LVGVEPIKTELLAKYDHLFRG-NLQ---ILNGYGPTEATV------ 1617
Cdd:cd05931 247 AAP----NFAYDLCVRrvrdeDLEGLDLSSWrvaLNGAEPVRPATLRRFAEAFAPfGFRpeaFRPSYGLAEATLfvsggp 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1618 -----CCTSYRYESNK----------EITTQNVPIGSPLLNTKIYILDSFHRIQ-PIGVPGEICISGIGLARGYINRKEL 1681
Cdd:cd05931 323 pgtgpVVLRVDRDALAgravavaaddPAARELVSCGRPLPDQEVRIVDPETGRElPDGEVGEIWVRGPSVASGYWGRPEA 402
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1682 TADKFIDHPFERGEKLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIELGEIEASlLKYETIKT------AVVIDQEDE 1755
Cdd:cd05931 403 TAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDIEAT-AEEAHPALrpgcvaAFSVPDDGE 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1756 AGEKYLCAYV--VTEKDIP--IPEVRAYLATKlpHYMIPQQ--LIPIHNIPLTQNGKIDRS 1810
Cdd:cd05931 481 ERLVVVAEVErgADPADLAaiAAAIRAAVARE--HGVAPADvvLVRPGSIPRTSSGKIQRR 539
|
|
| PLN03102 |
PLN03102 |
acyl-activating enzyme; Provisional |
1332-1812 |
1.31e-17 |
|
acyl-activating enzyme; Provisional
Pssm-ID: 215576 [Multi-domain] Cd Length: 579 Bit Score: 88.92 E-value: 1.31e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL--------- 1402
Cdd:PLN03102 28 PNRTSIIYGKTRFTWPQTYDRCCRLAASLISLNITKNDVVSVLAPNTPAMYEMHFAVPMAGAVLNPINTRLdatsiaail 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 ----PK------------QRVEYML-TDSGCSH---VLVHQNSIIKGIEFQGNVIDLMDMSFEEEPG--EDMHMMIEPHN 1460
Cdd:PLN03102 108 rhakPKilfvdrsfeplaREVLHLLsSEDSNLNlpvIFIHEIDFPKRPSSEELDYECLIQRGEPTPSlvARMFRIQDEHD 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPKGVMIEHRSLtnFLCAMYEDFSQDIGITDNVLFSSSI----------------SFDVTIFEIFVPL 1524
Cdd:PLN03102 188 PISLNYTSGTTADPKGVVISHRGA--YLSTLSAIIGWEMGTCPVYLWTLPMfhcngwtftwgtaargGTSVCMRHVTAPE 265
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1525 IYGarmtiyQGEKFDVTKLVQVileeqvtlsyipPTLLNeiydyFVRDNQKIVLN------KLLVGVEPIKTELLAKYDH 1598
Cdd:PLN03102 266 IYK------NIEMHNVTHMCCV------------PTVFN-----ILLKGNSLDLSprsgpvHVLTGGSPPPAALVKKVQR 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1599 LfrgNLQILNGYGPTEAT--VCCTSYRYESNKEITTQNVPIGSP--LLNTKIYILDSFHRIQPIGVP------GEICISG 1668
Cdd:PLN03102 323 L---GFQVMHAYGLTEATgpVLFCEWQDEWNRLPENQQMELKARqgVSILGLADVDVKNKETQESVPrdgktmGEIVIKG 399
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1669 IGLARGYINRKELTADKFiDHPFergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY-ETIKTA 1747
Cdd:PLN03102 400 SSIMKGYLKNPKATSEAF-KHGW------LNTGDVGVIHPDGHVEIKDRSKDIIISGGENISSVEVENVLYKYpKVLETA 472
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 1748 VVIDQEDEAGEKyLCAYVVTEK-DIPIPEVRAYLATK-----------LPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PLN03102 473 VVAMPHPTWGET-PCAFVVLEKgETTKEDRVDKLVTRerdlieycrenLPHFMCPRKVVFLQELPKNGNGKILKPKL 548
|
|
| LC_FACS_euk1 |
cd17639 |
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The ... |
301-724 |
1.33e-17 |
|
Eukaryotic long-chain fatty acid CoA synthetase (LC-FACS), including fungal proteins; The members of this family are eukaryotic fatty acid CoA synthetases (EC 6.2.1.3) that activate fatty acids with chain lengths of 12 to 20 and includes fungal proteins. They act on a wide range of long-chain saturated and unsaturated fatty acids, but the enzymes from different tissues show some variation in specificity. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions. Organisms tend to have multiple isoforms of LC-FACS genes with multiple splice variants. For example, nine genes are found in Arabidopsis and six genes are expressed in mammalian cells. In Schizosaccharomyces pombe, lcf1 gene encodes a new fatty acyl-CoA synthetase that preferentially recognizes myristic acid as a substrate.
Pssm-ID: 341294 [Multi-domain] Cd Length: 507 Bit Score: 88.43 E-value: 1.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 301 ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGgayLPIDT---ELPKQRVEYMLTDSGCSHVL 377
Cdd:cd17639 6 MSYAEVWERVLNFGRGLVELGLKPGDKVAIFAETRAEWLITALGCWSQN---IPIVTvyaTLGEDALIHSLNETECSAIF 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 378 TYQNsiikgvafqgsvinlmdipfeeeqvedlqitmePQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIG 457
Cdd:cd17639 83 TDGK---------------------------------PDDLACIMYTSGSTGNPKGVMLTHGNLVAGIAGLGDRVPELLG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 458 ITDNVLFSSSISFdvtIFEIFVPLVC---GARM----------TIYQGEKFD-----------VPKLVQVI---LEEQV- 509
Cdd:cd17639 130 PDDRYLAYLPLAH---IFELAAENVClyrGGTIgygsprtltdKSKRGCKGDltefkptlmvgVPAIWDTIrkgVLAKLn 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 510 TLAYIPPTLLNEIYDYFVRANQKIS----LNKLFVGvePIKTEL-------------LAKYDHLFRGNL--QILNLYGPT 570
Cdd:cd17639 207 PMGGLKRTLFWTAYQSKLKALKEGPgtplLDELVFK--KVRAALggrlrymlsggapLSADTQEFLNIVlcPVIQGYGLT 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 571 EaTVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILD------SFHRLQPigvPGEICISGIGLARGYINRKELTADKFi 644
Cdd:cd17639 285 E-TCAGGTVQDPGDLETGR----VGPPLPCCEIKLVDweeggySTDKPPP---RGEILIRGPNVFKGYYKNPEKTKEAF- 355
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 645 dhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIR-GYRIELGEIEASLLKYETIKTAVVIQREDESgekYLCAYVV 723
Cdd:cd17639 356 -----DGDGWFHTGDIGEFHPDGTLKIIDRKKDLVKLQnGEYIALEKLESIYRSNPLVNNICVYADPDKS---YPVAIVV 427
|
.
gi 446807313 724 T 724
Cdd:cd17639 428 P 428
|
|
| ACS |
cd05966 |
Acetyl-CoA synthetase (also known as acetate-CoA ligase and acetyl-activating enzyme); ... |
1327-1815 |
1.44e-17 |
|
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: 89.16 E-value: 1.44e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1327 QVKRNPNQIAV------VCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILG---------VLKA 1391
Cdd:cd05966 62 HLKERGDKVAIiwegdePDQSRTITYRELLREVCRFANVLKSLGVKKGDRVAIYMPMIPELVIAMLAcarigavhsVVFA 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1392 G-------------GAYLPIDTD--------LP-KQRVEYMLTDSGC-SHVLVHQNSiikgiefqGNVIDLM---DMSFE 1445
Cdd:cd05966 142 GfsaesladrindaQCKLVITADggyrggkvIPlKEIVDEALEKCPSvEKVLVVKRT--------GGEVPMTegrDLWWH 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1446 EE-PGEDMHMMIEP----HNLaYVIYTSGSTGQPKGVMieHRS--------LT-----------NFLCAmyedfsQDIG- 1500
Cdd:cd05966 214 DLmAKQSPECEPEWmdseDPL-FILYTSGSTGKPKGVV--HTTggyllyaaTTfkyvfdyhpddIYWCT------ADIGw 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1501 ITDNvlfsSSIsfdvtifeIFVPLIYGARMTIYQGEKF--DVTKLVQVILEEQVTLSYIPPTLLNEiydyFVRDNQKIVL 1578
Cdd:cd05966 285 ITGH----SYI--------VYGPLANGATTVMFEGTPTypDPGRYWDIVEKHKVTIFYTAPTAIRA----LMKFGDEWVK 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1579 N------KLL--VGvEPIKTEL-LAKYDHLFRGNLQILNGYGPTEatvccTSYRYESNKEITTQNVPiGS---PLLNTKI 1646
Cdd:cd05966 349 KhdlsslRVLgsVG-EPINPEAwMWYYEVIGKERCPIVDTWWQTE-----TGGIMITPLPGATPLKP-GSatrPFFGIEP 421
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1647 YILDSFHRIQPIGVPGEICISGI--GLARGYINRKEltadKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKI 1724
Cdd:cd05966 422 AILDEEGNEVEGEVEGYLVIKRPwpGMARTIYGDHE----RYEDTYFSKFPGYYFTGDGARRDEDGYYWITGRVDDVINV 497
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1725 RGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-----TEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNI 1799
Cdd:cd05966 498 SGHRLGTAEVESALVAHPAVAEAAVVGRPHDIKGEAIYAFVTlkdgeEPSDELRKELRKHVRKEIGPIATPDKIQFVPGL 577
|
570
....*....|....*.
gi 446807313 1800 PLTQNGKIDRSKLPKL 1815
Cdd:cd05966 578 PKTRSGKIMRRILRKI 593
|
|
| PRK08279 |
PRK08279 |
long-chain-acyl-CoA synthetase; Validated |
281-748 |
1.45e-17 |
|
long-chain-acyl-CoA synthetase; Validated
Pssm-ID: 236217 [Multi-domain] Cd Length: 600 Bit Score: 89.16 E-value: 1.45e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 281 FEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELP 360
Cdd:PRK08279 43 FEEAAARHPDRPALLFEDQSISYAELNARANRYAHWAAARGVGKGDVVALLMENRPEYLAAWLGLAKLGAVVALLNTQQR 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 361 KQRVEYMLTDSGCSHVL-------TYQnSIIKGVAFQGSVINLMDIPFEEEQ-VEDL----------------QITMEpq 416
Cdd:PRK08279 123 GAVLAHSLNLVDAKHLIvgeelveAFE-EARADLARPPRLWVAGGDTLDDPEgYEDLaaaaagapttnpasrsGVTAK-- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 417 NLAYVIYTSGSTGQPK-GVMIEHRSLTnflcaMYEDFSQDIGITDNvlfsssisfDVtiFEIFVPL-------VC----- 483
Cdd:PRK08279 200 DTAFYIYTSGTTGLPKaAVMSHMRWLK-----AMGGFGGLLRLTPD---------DV--LYCCLPLyhntggtVAwssvl 263
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 484 --GARMTIyqGEKFDVPKLVQVILEEQVTL-AYIpptllNEIYDYFV--------RANqkiSLNKLF-VGVEP-IKTELL 550
Cdd:PRK08279 264 aaGATLAL--RRKFSASRFWDDVRRYRATAfQYI-----GELCRYLLnqppkptdRDH---RLRLMIgNGLRPdIWDEFQ 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 551 AKYdhlfrGNLQILNLYGPTEATVCCTSYqYERDKeiTTQNVPI---------------GSPLLNTKiyildsfHRLQPI 615
Cdd:PRK08279 334 QRF-----GIPRILEFYAASEGNVGFINV-FNFDG--TVGRVPLwlahpyaivkydvdtGEPVRDAD-------GRCIKV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 616 GvPGEI--CISGIGLAR---GYiNRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGE 690
Cdd:PRK08279 399 K-PGEVglLIGRITDRGpfdGY-TDPEASEKKILRDVFKKGDAWFNTGDLMRDDGFGHAQFVDRLGDTFRWKGENVATTE 476
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 691 IEASLLKYETIKTAVV--IQREDESGEKYLCAYVVTE-KDIPIPEVRAYLATKLPYYMIPQ 748
Cdd:PRK08279 477 VENALSGFPGVEEAVVygVEVPGTDGRAGMAAIVLADgAEFDLAALAAHLYERLPAYAVPL 537
|
|
| PRK06164 |
PRK06164 |
acyl-CoA synthetase; Validated |
1323-1812 |
1.98e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235722 [Multi-domain] Cd Length: 540 Bit Score: 88.26 E-value: 1.98e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDL 1402
Cdd:PRK06164 15 LLDAHARARPDAVALIDEDRPLSRAELRALVDRLAAWLAAQGVRRGDRVAVWLPNCIEWVVLFLACARLGATVIAVNTRY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1403 PKQRVEYMLTDSGCShVLVHQNSIiKGIEFQGNV-------------IDLMDMSFEEEPGE---------DMHMMIE--- 1457
Cdd:PRK06164 95 RSHEVAHILGRGRAR-WLVVWPGF-KGIDFAAILaavppdalpplraIAVVDDAADATPAPapgarvqlfALPDPAPpaa 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1458 -------PHNLAYVIYTSGSTGQPKGVMieHRSLTnfLCAMYEDFSQDIGITDN--VLFSSSISFDVTIFEIFVPLIYGA 1528
Cdd:PRK06164 173 ageraadPDAGALLFTTSGTTSGPKLVL--HRQAT--LLRHARAIARAYGYDPGavLLAALPFCGVFGFSTLLGALAGGA 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1529 rmTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDyfVRDNQKIVLNKLLVGV---EPIKTELLAkydhLFRGNLQ 1605
Cdd:PRK06164 249 --PLVCEPVFDAARTARALRRHRVTHTFGNDEMLRRILD--TAGERADFPSARLFGFasfAPALGELAA----LARARGV 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1606 ILNG-YGPTE--ATVCC------TSYRYESNkeittqNVPIgSPllNTKIYILDSFH-RIQPIGVPGEICISGIGLARGY 1675
Cdd:PRK06164 321 PLTGlYGSSEvqALVALqpatdpVSVRIEGG------GRPA-SP--EARVRARDPQDgALLPDGESGEIEIRAPSLMRGY 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1676 INRKELTADKFIDHPFergeklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE 1755
Cdd:PRK06164 392 LDNPDATARALTDDGY------FRTGDLGYTRGDGQFVYQTRMGDSLRLGGFLVNPAEIEHALEALPGVAAAQVVGATRD 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1756 aGEKYLCAYVVTEKDIPI--PEVRAYLATKLPHYMIPQQLIPIHNIPLTQNG---KIDRSKL 1812
Cdd:PRK06164 466 -GKTVPVAFVIPTDGASPdeAGLMAACREALAGFKVPARVQVVEAFPVTESAngaKIQKHRL 526
|
|
| PRK07470 |
PRK07470 |
acyl-CoA synthetase; Validated |
1329-1807 |
3.37e-17 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 180988 [Multi-domain] Cd Length: 528 Bit Score: 87.40 E-value: 3.37e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1329 KRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVE 1408
Cdd:PRK07470 18 RRFPDRIALVWGDRSWTWREIDARVDALAAALAARGVRKGDRILVHSRNCNQMFESMFAAFRLGAVWVPTNFRQTPDEVA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1409 YMLTDSGCSHVLV------HQNSIIKGIEFQGNVIDLMDMSFEEEPG----EDMHMMIEPHNLAY-----VIYTSGSTGQ 1473
Cdd:PRK07470 98 YLAEASGARAMIChadfpeHAAAVRAASPDLTHVVAIGGARAGLDYEalvaRHLGARVANAAVDHddpcwFFFTSGTTGR 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1474 PKGVMIEHRSL----TNFLCAMYEDFSQDigitDNVLFSSSISFDVTIFEIfVPLIYGARMTIYQGEKFDVTKLVQVILE 1549
Cdd:PRK07470 178 PKAAVLTHGQMafviTNHLADLMPGTTEQ----DASLVVAPLSHGAGIHQL-CQVARGAATVLLPSERFDPAEVWALVER 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1550 EQVTLSYIPPTLLN--------EIYD-----YFV-------RDNQKIVLNKLlvgvepikTELLAKYdhlfrgnlqilng 1609
Cdd:PRK07470 253 HRVTNLFTVPTILKmlvehpavDRYDhsslrYVIyagapmyRADQKRALAKL--------GKVLVQY------------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1610 YGPTEATVCCTSYRYESNKEITTQNVPIGS---PLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKF 1686
Cdd:PRK07470 312 FGLGEVTGNITVLPPALHDAEDGPDARIGTcgfERTGMEVQIQDDEGRELPPGETGEICVIGPAVFAGYYNNPEANAKAF 391
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1687 IDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLcAYV 1765
Cdd:PRK07470 392 RDGWF-------RTGDLGHLDARGFLYITGRASDMYISGGSNVYPREIEEKLLTHPAVSEVAVLGVPDPVwGEVGV-AVC 463
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446807313 1766 VTEKDIPI--PEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:PRK07470 464 VARDGAPVdeAELLAWLDGKVARYKLPKRFFFWDALPKSGYGKI 507
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
567-769 |
5.22e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 87.18 E-value: 5.22e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 567 YGPTEATVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFidh 646
Cdd:PRK12492 365 YGLTETSPVASTNPYGELARLGT----VGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEAL--- 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 647 pfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEKYLCAYVVTE 725
Cdd:PRK12492 438 ---DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDErSGEAVKLFVVARD 514
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 446807313 726 KDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK12492 515 PGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
1634-1899 |
5.97e-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: 83.65 E-value: 5.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1634 NVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF--ERGEKLYKTGDIARWLPDGN 1711
Cdd:COG3433 17 PPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYpaQPGRQADDLRLLLRRGLGPG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1712 IEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEkDIPIPEVRAYLATKLPHYMIPQ 1791
Cdd:COG3433 97 GGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAAL-DGLAAAAALAALDKVPPDVVAA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1792 QLIPIHNIPLTQNGKIDRSKLPKL-NTLGNSNYVPPRNEIDSSLI-----DIWSSILGV--NNIGINDNFFELGGHSLKG 1863
Cdd:COG3433 176 SAVVALDALLLLALKVVARAAPALaAAEALLAAASPAPALETALTeeelrADVAELLGVdpEEIDPDDNLFDLGLDSIRL 255
|
250 260 270
....*....|....*....|....*....|....*.
gi 446807313 1864 LKLFENIKRMfNVQLPLSLLFQKATIEQLSDVISRN 1899
Cdd:COG3433 256 MQLVERWRKA-GLDVSFADLAEHPTLAAWWALLAAA 290
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1458-1815 |
6.33e-17 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 84.84 E-value: 6.33e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1458 PHNLAYVIYTSGSTGQPKgvMIEHRSLTNFLCAMYEDFSQDIGITDNVLFSSSIsFDV--TIFEIFVPLIYGARMTI--- 1532
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPK--LAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPL-FHVngSVVTLLTPLASGAHVVLagp 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1533 --YQG-----------EKFDVTKLVQVileeqvtlsyipPTLLNEIYDyfVRDNQKI-VLNKLLVGVEPIKTELLAKY-D 1597
Cdd:cd05944 78 agYRNpglfdnfwklvERYRITSLSTV------------PTVYAALLQ--VPVNADIsSLRFAMSGAAPLPVELRARFeD 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1598 HLfrgNLQILNGYGPTEATvcCTSYRYESNKEITTQNVPIGSPLLNTKIYILD-SFHRIQPIGVP--GEICISGIGLARG 1674
Cdd:cd05944 144 AT---GLPVVEGYGLTEAT--CLVAVNPPDGPKRPGSVGLRLPYARVRIKVLDgVGRLLRDCAPDevGEICVAGPGVFGG 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1675 YINrKELTADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVkIR-GYRIELGEIEASLLKYETIKTAVVIDQE 1753
Cdd:cd05944 219 YLY-TEGNKNAFVA------DGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQP 290
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1754 D-EAGEkYLCAYVVTEKDIPIP--EVRAYLATKLPHY-MIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:cd05944 291 DaHAGE-LPVAYVQLKPGAVVEeeELLAWARDHVPERaAVPKHIEVLEELPVTAVGKVFKPALRAD 355
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
290-769 |
6.60e-17 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 86.87 E-value: 6.60e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 290 NQIAIVCNGKE----ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGG-------AYLPidtE 358
Cdd:PRK04319 59 DKVALRYLDASrkekYTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAivgplfeAFME---E 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 359 LPKQRVEymltDSGCSHVLT----YQNSIIKGVAFQGSVInLMDIPFEE-EQVEDLQITME------------PQNLAYV 421
Cdd:PRK04319 136 AVRDRLE----DSEAKVLITtpalLERKPADDLPSLKHVL-LVGEDVEEgPGTLDFNALMEqasdefdiewtdREDGAIL 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 422 IYTSGSTGQPKGVMIEHRS-LTNFLCAMYE-DFSQDigitdnvlfsssisfDV------------TIFEIFVPLVCGARM 487
Cdd:PRK04319 211 HYTSGSTGKPKGVLHVHNAmLQHYQTGKYVlDLHED---------------DVywctadpgwvtgTSYGIFAPWLNGATN 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 488 TIYQGEkFDVPKLVQVILEEQVTLAYIPPTLLNeiydYFVRAN----QKISLNKL----FVGvEPIKTELLAKYDHLFrg 559
Cdd:PRK04319 276 VIDGGR-FSPERWYRILEDYKVTVWYTAPTAIR----MLMGAGddlvKKYDLSSLrhilSVG-EPLNPEVVRWGMKVF-- 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 560 NLQILNLYGPTE--ATVCCTSYqyerdkeitTQNVPIGS---PLLNTKIYILDSFHRLQPIGVPGEICI-----SgigLA 629
Cdd:PRK04319 348 GLPIHDNWWMTEtgGIMIANYP---------AMDIKPGSmgkPLPGIEAAIVDDQGNELPPNRMGNLAIkkgwpS---MM 415
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 630 RGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQR 709
Cdd:PRK04319 416 RGIWNNPEKYESYFAG-------DWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGK 488
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 710 EDE-SGE--KylcAYV-----VTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK04319 489 PDPvRGEiiK---AFValrpgYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMRRVL 553
|
|
| PRK12492 |
PRK12492 |
long-chain-fatty-acid--CoA ligase; Provisional |
1606-1812 |
8.63e-17 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 171539 [Multi-domain] Cd Length: 562 Bit Score: 86.41 E-value: 8.63e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1606 ILNGYGPTEATVCCTSYRYESNKEITTqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADK 1685
Cdd:PRK12492 361 IVEGYGLTETSPVASTNPYGELARLGT----VGIPVPGTALKVIDDDGNELPLGERGELCIKGPQVMKGYWQQPEATAEA 436
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1686 FidhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKYLCAY 1764
Cdd:PRK12492 437 L------DAEGWFKTGDIAVIDPDGFVRIVDRKKDLIIVSGFNVYPNEIEDVVMAHPKVANCAAIGVPDErSGEAVKLFV 510
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446807313 1765 VVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK12492 511 VARDPGLSVEELKAYCKENFTGYKVPKHIVLRDSLPMTPVGKILRREL 558
|
|
| FAAL |
cd05931 |
Fatty acyl-AMP ligase (FAAL); FAAL belongs to the class I adenylate forming enzyme family and ... |
301-695 |
1.07e-16 |
|
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: 86.14 E-value: 1.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 301 ITYKQLNIKANQLARRLLDQGVKREfIVGVMMERSIEMIVGILGILKAGG----AYLPIDTELpKQRVEYMLTDSGCSHV 376
Cdd:cd05931 25 LTYAELDRRARAIAARLQAVGKPGD-RVLLLAPPGLDFVAAFLGCLYAGAiavpLPPPTPGRH-AERLAAILADAGPRVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 377 LTyQNSIIKGVAFQGSVINLMDIP--FEEEQVED------LQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSL-TNFLCA 447
Cdd:cd05931 103 LT-TAAALAAVRAFAASRPAAGTPrlLVVDLLPDtsaadwPPPSPDPDDIAYLQYTSGSTGTPKGVVVTHRNLlANVRQI 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 448 M--YEDFSQDIGIT------DNVLfsssisfdvtIFEIFVPLVCGARMTIYQGEKFdV--PKL-VQVILEEQVTLAYIPp 516
Cdd:cd05931 182 RraYGLDPGDVVVSwlplyhDMGL----------IGGLLTPLYSGGPSVLMSPAAF-LrrPLRwLRLISRYRATISAAP- 249
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 517 tllNEIYDYFVRanqKI-----------SLNKLFVGVEPIKTELLAKYDHLFRGnlqiLNL--------YGPTEATV--- 574
Cdd:cd05931 250 ---NFAYDLCVR---RVrdedlegldlsSWRVALNGAEPVRPATLRRFAEAFAP----FGFrpeafrpsYGLAEATLfvs 319
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 575 --------CCTSYQYE----------RDKEITTQNVPIGSPLLNTKIYILDS-FHRLQPIGVPGEICISGIGLARGYINR 635
Cdd:cd05931 320 ggppgtgpVVLRVDRDalagravavaADDPAARELVSCGRPLPDQEVRIVDPeTGRELPDGEVGEIWVRGPSVASGYWGR 399
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 636 KELTADKFIDHPFERGEKLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIELGEIEASL 695
Cdd:cd05931 400 PEATAETFGALAATDEGGWLRTGDLGF-LHDGELYITGRLKDLIIVRGRNHYPQDIEATA 458
|
|
| MACS_euk |
cd05928 |
Eukaryotic Medium-chain acyl-CoA synthetase (MACS or ACSM); MACS catalyzes the two-step ... |
421-769 |
1.15e-16 |
|
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: 85.60 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 421 VIYTSGSTGQPKgvMIEHR----SLTNFLCAMY--EDFSQDI--GITDNVLFSSSISfdvtifEIFVPLVCGARMTIYQG 492
Cdd:cd05928 179 IYFTSGTTGSPK--MAEHShsslGLGLKVNGRYwlDLTASDImwNTSDTGWIKSAWS------SLFEPWIQGACVFVHHL 250
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 493 EKFDVPKLVQVILEEQVTLAYIPPTllneIYDYFVRAN----QKISLNKLFVGVEPIKTELLAKYDHlfRGNLQILNLYG 568
Cdd:cd05928 251 PRFDPLVILKTLSSYPITTFCGAPT----VYRMLVQQDlssyKFPSLQHCVTGGEPLNPEVLEKWKA--QTGLDIYEGYG 324
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 569 PTEATVCCTSYQYERDKEITtqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICIS-----GIGLARGYINRKELTADKf 643
Cdd:cd05928 325 QTETGLICANFKGMKIKPGS-----MGKASPPYDVQIIDDNGNVLPPGTEGDIGIRvkpirPFGLFSGYVDNPEKTAAT- 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 644 idhpfERGEkLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV 723
Cdd:cd05928 399 -----IRGD-FYLTGDRGIMDEDGYFWFMGRADDVINSSGYRIGPFEVESALIEHPAVVESAVVSSPDPIRGEVVKAFVV 472
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|...
gi 446807313 724 -------TEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05928 473 lapqflsHDPEQLTKELQQHVKSVTAPYKYPRKVEFVQELPKTVTGKIQRNEL 525
|
|
| PRK08751 |
PRK08751 |
long-chain fatty acid--CoA ligase; |
1320-1812 |
2.18e-16 |
|
long-chain fatty acid--CoA ligase;
Pssm-ID: 181546 [Multi-domain] Cd Length: 560 Bit Score: 84.93 E-value: 2.18e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1320 VHKMFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPI 1398
Cdd:PRK08751 27 VAEVFATSVAKFADRPAYHSFGKTITYREADQLVEQFAAYLLGElQLKKGDRVALMMPNCLQYPIATFGVLRAGLTVVNV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1399 DTDLPKQRVEYMLTDSGCSHVLVHQN------SIIKGIEFQgNVI-----DLMD-------------------------- 1441
Cdd:PRK08751 107 NPLYTPRELKHQLIDSGASVLVVIDNfgttvqQVIADTPVK-QVIttglgDMLGfpkaalvnfvvkyvkklvpeyringa 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1442 MSFEEEPGE-DMHMM----IEPHNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGITDNVLFSSSISFD-V 1515
Cdd:PRK08751 186 IRFREALALgRKHSMptlqIEPDDIAFLQYTGGTTGVAKGAMLTHRNLV----ANMQQAHQWLAGTGKLEEGCEVVITaL 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1516 TIFEIFVPLIYGARMTIYQG------EKFDVTKLVQVILEEQVTLSYIPPTLLNEI-----YDYFVRDNQKIVLNKLLVg 1584
Cdd:PRK08751 262 PLYHIFALTANGLVFMKIGGcnhlisNPRDMPGFVKELKKTRFTAFTGVNTLFNGLlntpgFDQIDFSSLKMTLGGGMA- 340
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1585 VEPIKTELLAKYDHLfrgnlQILNGYGPTEAT--VCCTSYryesnkEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPG 1662
Cdd:PRK08751 341 VQRSVAERWKQVTGL-----TLVEAYGLTETSpaACINPL------TLKEYNGSIGLPIPSTDACIKDDAGTVLAIGEIG 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1663 EICISGIGLARGYINRKELTAdKFIDhpferGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYE 1742
Cdd:PRK08751 410 ELCIKGPQVMKGYWKRPEETA-KVMD-----ADGWLHTGDIARMDEQGFVYIVDRKKDMILVSGFNVYPNEIEDVIAMMP 483
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446807313 1743 TIKTAVVIDQEDE-AGEkyLCAYVVTEKD--IPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK08751 484 GVLEVAAVGVPDEkSGE--IVKVVIVKKDpaLTAEDVKAHARANLTGYKQPRIIEFRKELPKTNVGKILRREL 554
|
|
| FACL_like_4 |
cd05944 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
415-769 |
2.36e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341266 [Multi-domain] Cd Length: 359 Bit Score: 83.30 E-value: 2.36e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 415 PQNLAYVIYTSGSTGQPKgvMIEHRSLTNFLCAMYEDFSQDIGITDNVLFSSSIsFDV--TIFEIFVPLVCGARMTIYQG 492
Cdd:cd05944 1 SDDVAAYFHTGGTTGTPK--LAQHTHSNEVYNAWMLALNSLFDPDDVLLCGLPL-FHVngSVVTLLTPLASGAHVVLAGP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 493 EKFDVPKLVQVI--LEEQVTLAYIP--PTLLNEIYDYFVRANQKiSLNKLFVGVEPIKTELLAKY-DHLfrgNLQILNLY 567
Cdd:cd05944 78 AGYRNPGLFDNFwkLVERYRITSLStvPTVYAALLQVPVNADIS-SLRFAMSGAAPLPVELRARFeDAT---GLPVVEGY 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 568 GPTEATvCCTSYQYeRDKEITTQNVPIGSPLLNTKIYILD-SFHRLQPIGVP--GEICISGIGLARGYINrKELTADKFI 644
Cdd:cd05944 154 GLTEAT-CLVAVNP-PDGPKRPGSVGLRLPYARVRIKVLDgVGRLLRDCAPDevGEICVAGPGVFGGYLY-TEGNKNAFV 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 645 DhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVkIR-GYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV 723
Cdd:cd05944 231 A------DGWLNTGDLGRLDADGYLFITGRAKDLI-IRgGHNIDPALIEEALLRHPAVAFAGAVGQPDAHAGELPVAYVQ 303
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 446807313 724 TEKDIPIP--EVRAYLATKLP-YYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05944 304 LKPGAVVEeeELLAWARDHVPeRAAVPKHIEVLEELPVTAVGKVFKPAL 352
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
337-770 |
2.43e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 83.93 E-value: 2.43e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 337 EMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCsHVLTYQNSiikgvafqgsvinlmDIPFEEEQVEDLqitmEPQ 416
Cdd:PRK08308 44 DIITLVFFLKEKGASVLPIHPDTPKEAAIRMAKRAGC-HGLLYGES---------------DFTKLEAVNYLA----EEP 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 417 NLayVIYTSGSTGQPKgvMIEhRSLTNF---LCAMYEDFSQDIGITDNVLFSSSISFDvtifeifvpLVCGARMTIYQGE 493
Cdd:PRK08308 104 SL--LQYSSGTTGEPK--LIR-RSWTEIdreIEAYNEALNCEQDETPIVACPVTHSYG---------LICGVLAALTRGS 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 494 KFDV-----PK-LVQVILEEQVTLAYIPPTLLNeIYDYFVRANQKIslNKLFVGVEPIKTELLAKydhlFRGN-LQILNL 566
Cdd:PRK08308 170 KPVIitnknPKfALNILRNTPQHILYAVPLMLH-ILGRLLPGTFQF--HAVMTSGTPLPEAWFYK----LRERtTYMMQQ 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 567 YGPTEATVCCTSYQYERDKEIttqnvpiGSPLLNTKIYILDSFHRlqpigvPGEICISgiglargyINRKELtadkfidh 646
Cdd:PRK08308 243 YGCSEAGCVSICPDMKSHLDL-------GNPLPHVSVSAGSDENA------PEEIVVK--------MGDKEI-------- 293
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 647 pfergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEKyLCAYVVTE 725
Cdd:PRK08308 294 ---------FTKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPvAGER-VKAKVISH 363
|
410 420 430 440
....*....|....*....|....*....|....*....|....*
gi 446807313 726 KDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLP 770
Cdd:PRK08308 364 EEIDPVQLREWCIQHLAPYQVPHEIESVTEIPKNANGKVSRKLLE 408
|
|
| beta-lac_NRPS |
cd19547 |
Condensation domain of nonribosomal peptide synthetases (NRPSs) similar to Nocardia uniformis ... |
873-1285 |
2.63e-16 |
|
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: 83.90 E-value: 2.63e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 873 YLASTSQKRMFIVDQFEDGTNTTYNMpTILKVEGDICKDKFENIFQSLIERHEILRTSFQILD-GELVQKIEPNVDFNIE 951
Cdd:cd19547 2 YPLAPMQEGMLFRGLFWPDSDAYFNQ-NVLELVGGTDEDVLREAWRRVADRYEILRTGFTWRDrAEPLQYVRDDLAPPWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 952 YVHVNEKDAD--------YLIHEFISPFDLSKPPLLRVLLLRIAEERHILVVDMHHIISDG--LSM--GILIKEFVELYK 1019
Cdd:cd19547 81 LLDWSGEDPDrraellerLLADDRAAGLSLADCPLYRLTLVRLGGGRHYLLWSHHHILLDGwcLSLiwGDVFRVYEELAH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1020 GNElPKLRV--QYKDYVMWQNGPYYKNliSEQKNYWLTTLKgELPvlnfPTDF-QRPTIQSFKGNVCSFNLGTDLTFKVN 1096
Cdd:cd19547 161 GRE-PQLSPcrPYRDYVRWIRARTAQS--EESERFWREYLR-DLT----PSPFsTAPADREGEFDTVVHEFPEQLTRLVN 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1097 KLATETGTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGR--SHSDTNHMIGMFINTLVMRNYLENDDEFIEFLSRLKLN 1174
Cdd:cd19547 233 EAARGYGVTTNAISQAAWSMLLALQTGARDVVHGLTIAGRppELEGSEHMVGIFINTIPLRIRLDPDQTVTGLLETIHRD 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1175 TLEAYENQDYPFEELLEGLDLHRdTSRNPLFDTMFVFQNMDMNPISIGELEFTPYPFK-QSVSKFDLSLVATEIDnNIHL 1253
Cdd:cd19547 313 LATTAAHGHVPLAQIKSWASGER-LSGGRVFDNLVAFENYPEDNLPGDDLSIQIIDLHaQEKTEYPIGLIVLPLQ-KLAF 390
|
410 420 430
....*....|....*....|....*....|..
gi 446807313 1254 KVEYSIKLFKAETIERLMVHFTNIVEEVTNNP 1285
Cdd:cd19547 391 HFNYDTTHFTRAQVDRFIEVFRLLTEQLCRRP 422
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1463-1808 |
3.12e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 82.82 E-value: 3.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1463 YVIYTSGSTGQPKGVMIEHR-----SLTNFLCAMYEDFSQDIGITDNVLFSSSISFDVTifeifvPLIYGARM------- 1530
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEdifrmLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAP------PLMHGTGSwtafggl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1531 -----TIYQGEKFDVTKLVQVILEEQVTLSYI-------PptLLNEIYDYFVRD--NQKIVLNKLLVGVEPIKTELLaky 1596
Cdd:cd05924 81 lggqtVVLPDDRFDPEEVWRTIEKHKVTSMTIvgdamarP--LIDALRDAGPYDlsSLFAISSGGALLSPEVKQGLL--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1597 DHLfrGNLQILNGYGPTEATVCCTSYRYES-NKEITTQNVPIGSPLLNtkiyilDSFHRIQP-IGVPGEICISGIgLARG 1674
Cdd:cd05924 156 ELV--PNITLVDAFGSSETGFTGSGHSAGSgPETGPFTRANPDTVVLD------DDGRVVPPgSGGVGWIARRGH-IPLG 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1675 YINRKELTADKFidhPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQED 1754
Cdd:cd05924 227 YYGDEAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVVGRPD 303
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1755 EAGEKYLCAYVVTEK--DIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:cd05924 304 ERWGQEVVAVVQLREgaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
1344-1814 |
3.80e-16 |
|
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: 84.26 E-value: 3.80e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVK-RESIVgVMMKRSIEMVIGILGVLKAGGAYLP----IDTDLPKQRVEYM-----LTD 1413
Cdd:cd05906 40 QSYQDLLEDARRLAAGLRQLGLRpGDSVI-LQFDDNEDFIPAFWACVLAGFVPAPltvpPTYDEPNARLRKLrhiwqLLG 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1414 SGcsHVLVHQNSI--IKGIE--FQGNVIDLMDMSFEEEPGEDMHMMI-EPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFL 1488
Cdd:cd05906 119 SP--VVLTDAELVaeFAGLEtlSGLPGIRVLSIEELLDTAADHDLPQsRPDDLALLMLTSGSTGFPKAVPLTHRNILARS 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1489 ---CAMYEDFSQDIGIT----DNVlfsSSISFdvtiFEIFvPLIYGARMTIYQGEKF--DVTKLVQVILEEQVTLSYIPP 1559
Cdd:cd05906 197 agkIQHNGLTPQDVFLNwvplDHV---GGLVE----LHLR-AVYLGCQQVHVPTEEIlaDPLRWLDLIDRYRVTITWAPN 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1560 TLLNEIYDYFVRDNQK----IVLNKLLVGVEPIKT-------ELLAKYdhlfrgNLQ---ILNGYGPTE----ATVCCTS 1621
Cdd:cd05906 269 FAFALLNDLLEEIEDGtwdlSSLRYLVNAGEAVVAktirrllRLLEPY------GLPpdaIRPAFGMTEtcsgVIYSRSF 342
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1622 YRYESNKEITTqnVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTG 1701
Cdd:cd05906 343 PTYDHSQALEF--VSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGPVVTKGYYNNPEANAEAFTE------DGWFRTG 414
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1702 DIArWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLlkyETIK------TAVVIDQEDEAGEKYLCAYVVTEKDIP--- 1772
Cdd:cd05906 415 DLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAV---EEVPgvepsfTAAFAVRDPGAETEELAIFFVPEYDLQdal 490
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446807313 1773 ---IPEVRAYLATKL---PHYMIPqqlIPIHNIPLTQNGKIDRSKLPK 1814
Cdd:cd05906 491 setLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKLKA 535
|
|
| AcpA |
COG3433 |
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites ... |
576-853 |
4.06e-16 |
|
Acyl carrier protein/domain [Lipid transport and metabolism, Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442659 [Multi-domain] Cd Length: 295 Bit Score: 81.33 E-value: 4.06e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 576 CTSYQYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDHPF--ERGEK 653
Cdd:COG3433 2 AIATPPPAPPTPDEPPPVIPPAIVQARALLLIVDLQGYFGGFGGEGGLLGAGLLLRIRLLAAAARAPFIPVPYpaQPGRQ 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 654 LYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEkDIPIPEV 733
Cdd:COG3433 82 ADDLRLLLRRGLGPGGGLERLVQQVVIRAERGEEEELLLVLRAAAVVRVAVLAALRGAGVGLLLIVGAVAAL-DGLAAAA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 734 RAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSSHLEP------TNSTERKLVEIWKDVLGI--QRIG 805
Cdd:COG3433 161 ALAALDKVPPDVVAASAVVALDALLLLALKVVARAAPALAAAEALLAAASpapaleTALTEEELRADVAELLGVdpEEID 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 446807313 806 IRDNFFEIGGHSLKAARLISIVNKEfNVQLSIKSLFKFPVLVDFSKYI 853
Cdd:COG3433 241 PDDNLFDLGLDSIRLMQLVERWRKA-GLDVSFADLAEHPTLAAWWALL 287
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
288-775 |
4.91e-16 |
|
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or propionate#CoA ligase (PrpE) catalyzes the first step of the 2-methylcitric acid cycle for propionate catabolism. It activates propionate to propionyl-CoA in a two-step reaction, which proceeds through a propionyl-AMP intermediate and requires ATP and Mg2+. In Salmonella enterica, the PrpE protein is required for growth of Salmonella enterica on propionate and can substitute for the acetyl-CoA synthetase (Acs) enzyme during growth on acetate. PrpE can also activate acetate, 3HP, and butyrate to their corresponding CoA-thioesters, although with less efficiency.
Pssm-ID: 341271 [Multi-domain] Cd Length: 617 Bit Score: 84.29 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 288 NPNQIAIVC------NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAG-------GAYLP 354
Cdd:cd05967 64 RGDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 355 ------IDTELPK------------QRVEYM------LTDSGCS--HVLTYQNSIIKGVAFQGsvinLMDIPFEEE--QV 406
Cdd:cd05967 144 kelasrIDDAKPKlivtascgiepgKVVPYKplldkaLELSGHKphHVLVLNRPQVPADLTKP----GRDLDWSELlaKA 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 407 EDLQ-ITMEPQNLAYVIYTSGSTGQPKGVMiehRSLTNFLCAMYEDFSQDIGI-TDNVLFSSSisfDVT-----IFEIFV 479
Cdd:cd05967 220 EPVDcVPVAATDPLYILYTSGTTGKPKGVV---RDNGGHAVALNWSMRNIYGIkPGDVWWAAS---DVGwvvghSYIVYG 293
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 480 PLVCGARMTIYQGEKFDVPKLVQ---VILEEQVTLAYIPPTLLNEIYDY-----FVRANQKISLNKLFVGVEPIKTELLA 551
Cdd:cd05967 294 PLLHGATTVLYEGKPVGTPDPGAfwrVIEKYQVNALFTAPTAIRAIRKEdpdgkYIKKYDLSSLRTLFLAGERLDPPTLE 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 552 KYDHLFrgNLQILNLYGPTEA--TVCCTSyqyerdKEITTQNVPIGS---PLLNTKIYILDSFHRLQPIGVPGEICISGi 626
Cdd:cd05967 374 WAENTL--GVPVIDHWWQTETgwPITANP------VGLEPLPIKAGSpgkPVPGYQVQVLDEDGEPVGPNELGNIVIKL- 444
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 627 GLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV 706
Cdd:cd05967 445 PLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAECAV 524
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 707 IQREDESGEKYLCAYVVTEKDIPI------PEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINN 775
Cdd:cd05967 525 VGVRDELKGQVPLGLVVLKEGVKItaeeleKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKIADG 599
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
1345-1750 |
6.05e-16 |
|
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: 83.29 E-value: 6.05e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLV--- 1421
Cdd:cd05932 8 TWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALFVgkl 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1422 -HQNSIIKGIEfqGNVIDLMDMSFEEEPGED-------MHMMIE------PHNLAYVIYTSGSTGQPKGVMIEHRSLTNF 1487
Cdd:cd05932 88 dDWKAMAPGVP--EGLISISLPPPSAANCQYqwddliaQHPPLEerptrfPEQLATLIYTSGTTGQPKGVMLTFGSFAWA 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1488 LCAMYEDFsqDIGITDNVL--------------FSSSISFDVTIF-----EIFVPLIYGARMTIYqgekFDVTKLvqVIL 1548
Cdd:cd05932 166 AQAGIEHI--GTEENDRMLsylplahvtervfvEGGSLYGGVLVAfaeslDTFVEDVQRARPTLF----FSVPRL--WTK 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1549 EEQVTLSYIPPTLLNEIYDYFVRDnqKIVLNKLLVGV------------EPIKTELLAKYDHLfrgNLQILNGYGPTEat 1616
Cdd:cd05932 238 FQQGVQDKIPQQKLNLLLKIPVVN--SLVKRKVLKGLgldqcrlagcgsAPVPPALLEWYRSL---GLNILEAYGMTE-- 310
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1617 vcctSYRYES-NKEITTQNVPIGSPLLNTKIYILDSfhriqpigvpGEICISGIGLARGYINRKELTADKFIDHPFERge 1695
Cdd:cd05932 311 ----NFAYSHlNYPGRDKIGTVGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFLR-- 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1696 klykTGDIARWLPDGNIEYLGRVDHQVKI-RGYRIELGEIEASLLKYETIKTAVVI 1750
Cdd:cd05932 375 ----TGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PRK07788 |
PRK07788 |
acyl-CoA synthetase; Validated |
1330-1815 |
8.34e-16 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236097 [Multi-domain] Cd Length: 549 Bit Score: 83.05 E-value: 8.34e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1330 RNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPK-QRVE 1408
Cdd:PRK07788 61 RAPDRAALIDERGTLTYAELDEQSNALARGLLALGVRAGDGVAVLARNHRGFVLALYAAGKVGARIILLNTGFSGpQLAE 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1409 YMLTDSgcSHVLVHQNsiikgiEFQGNVIDL-----------MDMSFEEEPG------EDMHMMIEPHNL-------AYV 1464
Cdd:PRK07788 141 VAAREG--VKALVYDD------EFTDLLSALppdlgrlrawgGNPDDDEPSGstdetlDDLIAGSSTAPLpkppkpgGIV 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1465 IYTSGSTGQPKGVMIEH----RSLTNFLCAMyeDFSQDigitDNVLFSSSIsFDVTIFEIFVpLIYGARMTIYQGEKFDV 1540
Cdd:PRK07788 213 ILTSGTTGTPKGAPRPEpsplAPLAGLLSRV--PFRAG----ETTLLPAPM-FHATGWAHLT-LAMALGSTVVLRRRFDP 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1541 TKLVQVILEEQVTLSYIPPTLLNEIYDyfvrdnqkivlnkllvgVEPiktELLAKYD----------------HLFRGNL 1604
Cdd:PRK07788 285 EATLEDIAKHKATALVVVPVMLSRILD-----------------LGP---EVLAKYDtsslkiifvsgsalspELATRAL 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1605 Q-----ILNGYGPTEATVCCTSYRYESNKEITTqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINrk 1679
Cdd:PRK07788 345 EafgpvLYNLYGSTEVAFATIATPEDLAEAPGT----VGRPPKGVTVKILDENGNEVPRGVVGRIFVGNGFPFEGYTD-- 418
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1680 elTADKfidhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEK 1759
Cdd:PRK07788 419 --GRDK------QIIDGLLSSGDVGYFDEDGLLFVDGRDDDMIVSGGENVFPAEVEDLLAGHPDVVEAAVIGVDDEEFGQ 490
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1760 YLCAYVVTEKDIPIPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK07788 491 RLRAFVVKAPGAALDEdaIKDYVRDNLARYKVPRDVVFLDELPRNPTGKVLKRELREM 548
|
|
| FACL_like_5 |
cd05924 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
420-765 |
9.12e-16 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341248 [Multi-domain] Cd Length: 364 Bit Score: 81.27 E-value: 9.12e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 420 YVIYTSGSTGQPKGVMIEHR-----SLTNFLCAMYEDFSQDIGITDNVLFSSSISFDVTifeifvPLVCGARM------- 487
Cdd:cd05924 7 YILYTGGTTGMPKGVMWRQEdifrmLMGGADFGTGEFTPSEDAHKAAAAAAGTVMFPAP------PLMHGTGSwtafggl 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 488 -----TIYQGEKFDVPKLVQVILEEQVTL------AYIPPtLLNEIydyfvRANQKISLNKLFV----GV---EPIKTEL 549
Cdd:cd05924 81 lggqtVVLPDDRFDPEEVWRTIEKHKVTSmtivgdAMARP-LIDAL-----RDAGPYDLSSLFAissgGAllsPEVKQGL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 550 LakyDHLfrGNLQILNLYGPTEATVCCTSYQYERDKEITT-QNVPIGSPLLNtkiyilDSFHRLQP-IGVPGEICISGIg 627
Cdd:cd05924 155 L---ELV--PNITLVDAFGSSETGFTGSGHSAGSGPETGPfTRANPDTVVLD------DDGRVVPPgSGGVGWIARRGH- 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 628 LARGYINRKELTADKFidhPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI 707
Cdd:cd05924 223 IPLGYYGDEAKTAETF---PEVDGVRYAVPGDRATVEADGTVTLLGRGSVCINTGGEKVFPEEVEEALKSHPAVYDVLVV 299
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 708 QREDESGEKYLCAYVVTEK--DIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:cd05924 300 GRPDERWGQEVVAVVQLREgaGVDLEELREHCRTRIARYKLPKQVVFVDEIERSPAGKAD 359
|
|
| LC_FACS_bac |
cd05932 |
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter ... |
300-707 |
1.02e-15 |
|
Bacterial long-chain fatty acid CoA synthetase (LC-FACS), including Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase; The members of this family are bacterial long-chain fatty acid CoA synthetase. Marinobacter hydrocarbonoclasticus isoprenoid Coenzyme A synthetase in this family is involved in the synthesis of isoprenoid wax ester storage compounds when grown on phytol as the sole carbon source. LC-FACS catalyzes the formation of fatty acyl-CoA in a two-step reaction: the formation of a fatty acyl-AMP molecule as an intermediate, and the formation of a fatty acyl-CoA. Free fatty acids must be "activated" to their CoA thioesters before participating in most catabolic and anabolic reactions.
Pssm-ID: 341255 [Multi-domain] Cd Length: 508 Bit Score: 82.52 E-value: 1.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 300 EITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHV--- 376
Cdd:cd05932 6 EFTWGEVADKARRLAAALRALGLEPGSKIALISKNCAEWFITDLAIWMAGHISVPLYPTLNPDTIRYVLEHSESKALfvg 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 377 -LTYQNSIIKGVAfqGSVINLMDIPFEE----EQVEDLQ---------ITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLT 442
Cdd:cd05932 86 kLDDWKAMAPGVP--EGLISISLPPPSAancqYQWDDLIaqhppleerPTRFPEQLATLIYTSGTTGQPKGVMLTFGSFA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 443 NFLCAMYEDFsqDIGITDNVL--------------FSSSISFDVTIF-----EIFVPLVCGARMTIYqgekFDVPKLvqV 503
Cdd:cd05932 164 WAAQAGIEHI--GTEENDRMLsylplahvtervfvEGGSLYGGVLVAfaeslDTFVEDVQRARPTLF----FSVPRL--W 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 504 ILEEQVTLAYIPPTLLN-----EIYDYFVRAN--QKISLNK---LFVGVEPIKTELLAKYDHLfrgNLQILNLYGPTEAT 573
Cdd:cd05932 236 TKFQQGVQDKIPQQKLNlllkiPVVNSLVKRKvlKGLGLDQcrlAGCGSAPVPPALLEWYRSL---GLNILEAYGMTENF 312
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 574 VCCTSYQYERDKEITtqnvpIGSPLLNTKIYILDSfhrlqpigvpGEICISGIGLARGYINRKELTADKFIDHPFERgek 653
Cdd:cd05932 313 AYSHLNYPGRDKIGT-----VGNAGPGVEVRISED----------GEILVRSPALMMGYYKDPEATAEAFTADGFLR--- 374
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 654 lykTGDIARWLPDGNIEYLGRVDHQVKI-RGYRIELGEIEASLLKYETIKTAVVI 707
Cdd:cd05932 375 ---TGDKGELDADGNLTITGRVKDIFKTsKGKYVAPAPIENKLAEHDRVEMVCVI 426
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
280-769 |
1.21e-15 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 82.79 E-value: 1.21e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 280 LFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTE 358
Cdd:PRK08974 28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVNVNPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 359 LPKQRVEYMLTDSGCSHVLTYQN--SIIKGVAFQ-------------------GSVINLM-----------DIPFEEEQV 406
Cdd:PRK08974 108 YTPRELEHQLNDSGAKAIVIVSNfaHTLEKVVFKtpvkhviltrmgdqlstakGTLVNFVvkyikrlvpkyHLPDAISFR 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 407 EDLQI---------TMEPQNLAYVIYTSGSTGQPKGVMIEHRS-LTNFLcamyedfsQDIGITDNVLFSSSiSFDVT--- 473
Cdd:PRK08974 188 SALHKgrrmqyvkpELVPEDLAFLQYTGGTTGVAKGAMLTHRNmLANLE--------QAKAAYGPLLHPGK-ELVVTalp 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 474 IFEIFVpLVCGARMTIYQGEK-------FDVPKLVQVILEEQVTLAyippTLLNEIYDYFVRANQKISLN----KLFVGV 542
Cdd:PRK08974 259 LYHIFA-LTVNCLLFIELGGQnllitnpRDIPGFVKELKKYPFTAI----TGVNTLFNALLNNEEFQELDfsslKLSVGG 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 543 -EPIKTELLAKYDHLFRGNLqiLNLYGPTEATVCCTSYQYERDKeittQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEI 621
Cdd:PRK08974 334 gMAVQQAVAERWVKLTGQYL--LEGYGLTECSPLVSVNPYDLDY----YSGSIGLPVPSTEIKLVDDDGNEVPPGEPGEL 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 622 CISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE-ASLLKYET 700
Cdd:PRK08974 408 WVKGPQVMLGYWQRPEATDEVIKD-------GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEIEdVVMLHPKV 480
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 701 IKTAVVIQREDESGEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK08974 481 LEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
393-773 |
1.26e-15 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 82.15 E-value: 1.26e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 393 VINLMDIPF---EEEQVEDLqitmePQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEdfSQDIGITDNVLFSSSIS 469
Cdd:cd05908 85 VWNTLKNPYlitEEEVLCEL-----ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILN--STEWKTKDRILSWMPLT 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 470 FDVTIFEI-FVPLVCGARMTIYQGEKFDV-PKL-VQVILEEQVTLAYIPptllNEIYDYFVRA--NQKI------SLNKL 538
Cdd:cd05908 158 HDMGLIAFhLAPLIAGMNQYLMPTRLFIRrPILwLKKASEHKATIVSSP----NFGYKYFLKTlkPEKAndwdlsSIRMI 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 539 FVGVEPIKTELLAKY-DHLFRGNLQ---ILNLYGPTEATVCCTS-----------------YQYERDKEITTQN------ 591
Cdd:cd05908 234 LNGAEPIDYELCHEFlDHMSKYGLKrnaILPVYGLAEASVGASLpkaqspfktitlgrrhvTHGEPEPEVDKKDsecltf 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 592 VPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIArWLPDGNIEY 671
Cdd:cd05908 314 VEVGKPIDETDIRICDEDNKILPDGYIGHIQIRGKNVTPGYYNNPEATAKVFTD------DGWLKTGDLG-FIRNGRLVI 386
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 672 LGRVDHQVKIRGYRIELGEIEASLLKYETI---KTAVVIQREDESGEKYLCAYVVTEKDIpipEVRAYLATKLPYYMIP- 747
Cdd:cd05908 387 TGREKDIIFVNGQNVYPHDIERIAEELEGVelgRVVACGVNNSNTRNEEIFCFIEHRKSE---DDFYPLGKKIKKHLNKr 463
|
410 420 430
....*....|....*....|....*....|.
gi 446807313 748 -----QQIISIQNIPLTQNGKIDRKKLPQPI 773
Cdd:cd05908 464 ggwqiNEVLPIRRIPKTTSGKVKRYELAQRY 494
|
|
| PRK08314 |
PRK08314 |
long-chain-fatty-acid--CoA ligase; Validated |
1329-1807 |
1.36e-15 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236235 [Multi-domain] Cd Length: 546 Bit Score: 82.32 E-value: 1.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1329 KRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRV 1407
Cdd:PRK08314 21 RRYPDKTAIVFYGRAISYRELLEEAERLAGYLQQEcGVRKGDRVLLYMQNSPQFVIAYYAILRANAVVVPVNPMNREEEL 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1408 EYMLTDSGCS----------------------HVLVHQ-------NSIIKGIEF-----------QGNVIDLMDMSFE-E 1446
Cdd:PRK08314 101 AHYVTDSGARvaivgselapkvapavgnlrlrHVIVAQysdylpaEPEIAVPAWlraepplqalaPGGVVAWKEALAAgL 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1447 EPGEdmhMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSL--TNFLCAMYEDfsqdiGITDNVLFSSSISFDVTIFE--IFV 1522
Cdd:PRK08314 181 APPP---HTAGPDDLAVLPYTSGTTGVPKGCMHTHRTVmaNAVGSVLWSN-----STPESVVLAVLPLFHVTGMVhsMNA 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1523 PLIYGArmTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLneiYDYFVRDN-QKIVLNKLLV----GV---EPIKTELLA 1594
Cdd:PRK08314 253 PIYAGA--TVVLMPRWDREAAARLIERYRVTHWTNIPTMV---VDFLASPGlAERDLSSLRYigggGAampEAVAERLKE 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1595 KYdhlfrgNLQILNGYGPTEaTVCCTsyryESNKEITTQNVPIGSPLLNTKIYILD-SFHRIQPIGVPGEICISGIGLAR 1673
Cdd:PRK08314 328 LT------GLDYVEGYGLTE-TMAQT----HSNPPDRPKLQCLGIPTFGVDARVIDpETLEELPPGEVGEIVVHGPQVFK 396
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1674 GYINRKELTADKFIDhpFErGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQE 1753
Cdd:PRK08314 397 GYWNRPEATAEAFIE--ID-GKRFFRTGDLGRMDEEGYFFITDRLKRMINASGFKVWPAEVENLLYKHPAIQEACVIATP 473
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1754 DE-AGE--KylcAYVV---------TEKDIpIPEVRAYLATklphYMIPQQLIPIHNIPLTQNGKI 1807
Cdd:PRK08314 474 DPrRGEtvK---AVVVlrpeargktTEEEI-IAWAREHMAA----YKYPRIVEFVDSLPKSGSGKI 531
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
1582-1812 |
1.54e-15 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 82.70 E-value: 1.54e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1582 LVGVEPIKTELLAKYDHlfRGNLQILNGYGPTEAT-VCCTSYRYESNKeittqnvpIGS-----PLLNTKIYILDSFHRI 1655
Cdd:PRK07529 339 LCGAAPLPVEVFRRFEA--ATGVRIVEGYGLTEATcVSSVNPPDGERR--------IGSvglrlPYQRVRVVILDDAGRY 408
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1656 Q---PIGVPGEICISGIGLARGYinrkeLTADKFIDHPFERGekLYKTGDIARWLPDGNIEYLGRVDHQVkIR-GYRIEL 1731
Cdd:PRK07529 409 LrdcAVDEVGVLCIAGPNVFSGY-----LEAAHNKGLWLEDG--WLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDP 480
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1732 GEIEASLLKYETIKTAVVIDQEDE-AGEkyL-CAYV--VTEKDIPIPEVRAYLATKLPH-YMIPQQLIPIHNIPLTQNGK 1806
Cdd:PRK07529 481 AAIEEALLRHPAVALAAAVGRPDAhAGE--LpVAYVqlKPGASATEAELLAFARDHIAErAAVPKHVRILDALPKTAVGK 558
|
....*.
gi 446807313 1807 IDRSKL 1812
Cdd:PRK07529 559 IFKPAL 564
|
|
| PrpE |
cd05967 |
Propionyl-CoA synthetase (PrpE); EC 6.2.1.17: propanoate:CoA ligase (AMP-forming) or ... |
1331-1837 |
3.61e-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: 81.21 E-value: 3.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1331 NPNQIAVVC------NEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAG-------GAYLP 1397
Cdd:cd05967 64 RGDQIALIYdspvtgTERTYTYAELLDEVSRLAGVLRKLGVVKGDRVIIYMPMIPEAAIAMLACARIGaihsvvfGGFAA 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1398 ------IDTDLPK------------QRVEYM------LTDSGCS--HVLVHQNSIIKGIEFQGnvidLMDMSFEEEpged 1451
Cdd:cd05967 144 kelasrIDDAKPKlivtascgiepgKVVPYKplldkaLELSGHKphHVLVLNRPQVPADLTKP----GRDLDWSEL---- 215
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1452 MHMmIEPHNLA--------YVIYTSGSTGQPKGVMiehRSLTNFLCAMYEDFSQDIGI-TDNVLFSSSisfDVT-----I 1517
Cdd:cd05967 216 LAK-AEPVDCVpvaatdplYILYTSGTTGKPKGVV---RDNGGHAVALNWSMRNIYGIkPGDVWWAAS---DVGwvvghS 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 FEIFVPLIYGARMTIYQGEKF---DVTKLVQVILEEQVTLSYIPPTLLNEIYDY-----FVRDNQKIVLNKLLVGVEPIK 1589
Cdd:cd05967 289 YIVYGPLLHGATTVLYEGKPVgtpDPGAFWRVIEKYQVNALFTAPTAIRAIRKEdpdgkYIKKYDLSSLRTLFLAGERLD 368
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1590 TELLAKYDHLFrgNLQILNGYGPTEATVCCTSyryeSNKEITTQNVPIGS---PLLNTKIYILDSFHRIQPIGVPGEICI 1666
Cdd:cd05967 369 PPTLEWAENTL--GVPVIDHWWQTETGWPITA----NPVGLEPLPIKAGSpgkPVPGYQVQVLDEDGEPVGPNELGNIVI 442
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1667 SGiGLARGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKT 1746
Cdd:cd05967 443 KL-PLPPGCLLTLWKNDERFKKLYLSKFPGYYDTGDAGYKDEDGYLFIMGRTDDVINVAGHRLSTGEMEESVLSHPAVAE 521
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1747 AVVIDQEDEAGEKYLCAYVVTEKDIPI------PEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLntLGN 1820
Cdd:cd05967 522 CAVVGVRDELKGQVPLGLVVLKEGVKItaeeleKELVALVREQIGPVAAFRLVIFVKRLPKTRSGKILRRTLRKI--ADG 599
|
570
....*....|....*...
gi 446807313 1821 SNY-VPPRNEIDSSLIDI 1837
Cdd:cd05967 600 EDYtIPSTIEDPSVLDEI 617
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
415-765 |
4.56e-15 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 81.55 E-value: 4.56e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 415 PQNLAYVIYTSGSTGQPKGVMIEHRsltNFLCAMYEdfsqdigITDNVLFSSS-ISFDV-TIFEIFvPLVCGARMTIYQG 492
Cdd:PRK06814 792 PDDPAVILFTSGSEGTPKGVVLSHR---NLLANRAQ-------VAARIDFSPEdKVFNAlPVFHSF-GLTGGLVLPLLSG 860
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 493 EKF----------DVPKLVQVIleeQVTLAYIPPTLLN------EIYDYFvranqkiSLNKLFVGVEPIKTELLAKYDHL 556
Cdd:PRK06814 861 VKVflypsplhyrIIPELIYDT---NATILFGTDTFLNgyaryaHPYDFR-------SLRYVFAGAEKVKEETRQTWMEK 930
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 557 FRgnLQILNLYGPTEAtvcctsyqyerdkeittqnvpigSPLL--NTKIY--------ILDSFH-RLQPI-GVP--GEIC 622
Cdd:PRK06814 931 FG--IRILEGYGVTET-----------------------APVIalNTPMHnkagtvgrLLPGIEyRLEPVpGIDegGRLF 985
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 623 ISGIGLARGYinrkeLTADK-FIDHPFERGEklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETI 701
Cdd:PRK06814 986 VRGPNVMLGY-----LRAENpGVLEPPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEELAAELWPD 1058
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 702 KTAVVIQREDES-GEKYLcaYVVTEKDIPIPEVRAYLATK-LPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:PRK06814 1059 ALHAAVSIPDARkGERII--LLTTASDATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK09274 |
PRK09274 |
peptide synthase; Provisional |
1329-1723 |
4.82e-15 |
|
peptide synthase; Provisional
Pssm-ID: 236443 [Multi-domain] Cd Length: 552 Bit Score: 80.71 E-value: 4.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1329 KRNPNQIAVVC----------NEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGayLPI 1398
Cdd:PRK09274 17 QERPDQLAVAVpggrgadgklAYDELSFAELDARSDAIAHGLNAAGIGRGMRAVLMVTPSLEFFALTFALFKAGA--VPV 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1399 DTD----------------------LPKQRVEYMLTDSGCSH----VLVHQNSIIKGIEFQGNVIDLMDMSFEeepgedM 1452
Cdd:PRK09274 95 LVDpgmgiknlkqclaeaqpdafigIPKAHLARRLFGWGKPSvrrlVTVGGRLLWGGTTLATLLRDGAAAPFP------M 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1453 HMMiEPHNLAYVIYTSGSTGQPKGVMIEHRSltnfLCAMYEDFSQDIGITDNvlfsssiSFDVTIFEIFV--PLIYGARM 1530
Cdd:PRK09274 169 ADL-APDDMAAILFTSGSTGTPKGVVYTHGM----FEAQIEALREDYGIEPG-------EIDLPTFPLFAlfGPALGMTS 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1531 TIyqgEKFDVTK--------LVQVILEEQVTLSYIPPTLLNEIYDYFVrdNQKIVLNKL---LVGVEPIKTELLAKYDHL 1599
Cdd:PRK09274 237 VI---PDMDPTRpatvdpakLFAAIERYGVTNLFGSPALLERLGRYGE--ANGIKLPSLrrvISAGAPVPIAVIERFRAM 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1600 FRGNLQILNGYGPTEAT-VCCTSYR--YESNKEITTQN--VPIGSPLLNTKIYI-------LDSFHRIQ--PIGVPGEIC 1665
Cdd:PRK09274 312 LPPDAEILTPYGATEALpISSIESReiLFATRAATDNGagICVGRPVDGVEVRIiaisdapIPEWDDALrlATGEIGEIV 391
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1666 ISGIGLARGYINRKELTA-DKFIDhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVK 1723
Cdd:PRK09274 392 VAGPMVTRSYYNRPEATRlAKIPD---GQGDVWHRMGDLGYLDAQGRLWFCGRKAHRVE 447
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
298-766 |
5.77e-15 |
|
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: 79.79 E-value: 5.77e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 298 GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVL 377
Cdd:cd05914 5 GEPLTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIF 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 378 tyqnsiikgvafqgsvinlmdipfeeeqvedlqiTMEPQNLAYVIYTSGSTGQPKGVMIEHRSL-TNflcAMYEDFSQDI 456
Cdd:cd05914 85 ----------------------------------VSDEDDVALINYTSGTTGNSKGVMLTYRNIvSN---VDGVKEVVLL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 457 GITDNVLfsSSISFDVT---IFEIFVPLVCGArmTIYQGEKFDVPKLVqVILEEQVTLAYIPPTLLnEIYDYFVRANQ-K 532
Cdd:cd05914 128 GKGDKIL--SILPLHHIyplTFTLLLPLLNGA--HVVFLDKIPSAKII-ALAFAQVTPTLGVPVPL-VIEKIFKMDIIpK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 533 ISLNKLF------VGVEPIKTELLAKYDHLFRGNLQI-------LNL----------------YGPTEATVCCTSYQYER 583
Cdd:cd05914 202 LTLKKFKfklakkINNRKIRKLAFKKVHEAFGGNIKEfviggakINPdveeflrtigfpytigYGMTETAPIISYSPPNR 281
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 584 DKEITTqnvpiGSPLLNTKIYILDSfhrlQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARW 663
Cdd:cd05914 282 IRLGSA-----GKVIDGVEVRIDSP----DPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK------DGWFHTGDLGKI 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 664 LPDGNIEYLGRVDHQ-VKIRGYRIELGEIEASLLKYETIKTAVVIQREDES---------GEKYLCAYVVTEKDIPIPEV 733
Cdd:cd05914 347 DAEGYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEKKLvalayidpdFLDVKALKQRNIIDAIKWEV 426
|
490 500 510
....*....|....*....|....*....|....
gi 446807313 734 RAYLATKLP-YYMIPQQIISIQNIPLTQNGKIDR 766
Cdd:cd05914 427 RDKVNQKVPnYKKISKVKIVKEEFEKTPKGKIKR 460
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
300-769 |
6.64e-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: 341236 [Multi-domain] Cd Length: 457 Bit Score: 79.81 E-value: 6.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 300 EITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDsgcshvlty 379
Cdd:cd05910 2 RLSFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQE--------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 380 qnsiIKGVAFQGsvinlmdIPFEEEQvedlqitmepqnlAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGIT 459
Cdd:cd05910 73 ----AEPDAFIG-------IPKADEP-------------AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEV 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 460 DNVLFSssisfdvtIFEIFVPLVCGAR----MTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKI-S 534
Cdd:cd05910 129 DLATFP--------LFALFGPALGLTSvipdMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLpS 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 535 LNKLFVGVEPIKTELLAKYDHLFRGNLQILNLYGPTEA-TVCCTSyqyERDKEITTQNVP-------IGSPLLNTKIYIL 606
Cdd:cd05910 201 LRRVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEAlPVSSIG---SRELLATTTAATsggagtcVGRPIPGVRVRII 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 607 ----------DSFHRLqPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERgeKLYKTGDIARWLPDGNIEYLGRVD 676
Cdd:cd05910 278 eiddepiaewDDTLEL-PRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEG--FWHRMGDLGYLDDEGRLWFCGRKA 354
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 677 HQVKIRGYRIELGEIEASLLKYETIK-TAVVIQREDESGEKYLCayVVTEKDIPIPEVRAY-----LATKLPYYMIPQQI 750
Cdd:cd05910 355 HRVITTGGTLYTEPVERVFNTHPGVRrSALVGVGKPGCQLPVLC--VEPLPGTITPRARLEqelraLAKDYPHTQRIGRF 432
|
490 500
....*....|....*....|.
gi 446807313 751 ISIQNIP--LTQNGKIDRKKL 769
Cdd:cd05910 433 LIHPSFPvdIRHNAKIFREKL 453
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
1458-1717 |
9.46e-15 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 80.14 E-value: 9.46e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1458 PHNLAYVIYTSGSTGQPKGVMIEHRSLtnflcamyedFSQDIGITDNVLFSSS---ISF--DVTIFE---IFVPLIYGAR 1529
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNL----------IANVAGSSLSTKFYPSdvhISYlpLAHIYErvnQIVMLHYGVA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1530 MTIYQGekfDVTKLVQVILEEQVTLSYIPPTLLNEIYDY---------FVRDN-----------------------QKIV 1577
Cdd:PLN02736 290 VGFYQG---DNLKLMDDLAALRPTIFCSVPRLYNRIYDGitnavkesgGLKERlfnaaynakkqalengknpspmwDRLV 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1578 LNKL-----------LVGVEPIKTELLAKYDHLFRGnlQILNGYGPTEaTVCCTSYRYESNKeiTTQNVpiGSPLLNTKI 1646
Cdd:PLN02736 367 FNKIkaklggrvrfmSSGASPLSPDVMEFLRICFGG--RVLEGYGMTE-TSCVISGMDEGDN--LSGHV--GSPNPACEV 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1647 YILDsfhriqpigVP-------------GEICISGIGLARGYInRKELTADKFIDhpferGEKLYKTGDIARWLPDGNIE 1713
Cdd:PLN02736 440 KLVD---------VPemnytsedqpyprGEICVRGPIIFKGYY-KDEVQTREVID-----EDGWLHTGDIGLWLPGGRLK 504
|
....
gi 446807313 1714 YLGR 1717
Cdd:PLN02736 505 IIDR 508
|
|
| LC_FACL_like |
cd05914 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); The members of this family are ... |
1344-1809 |
1.06e-14 |
|
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: 79.02 E-value: 1.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHq 1423
Cdd:cd05914 8 LTYKDLADNIAKFALLLKINGVGTGDRVALMGENRPEWGIAFFAIWTYGAIAVPILAEFTADEVHHILNHSEAKAIFVS- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 nsiikgiefqgnvidlmdmsfeeepgedmhmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSL-TNflcAMYEDFSQDIGIT 1502
Cdd:cd05914 87 ---------------------------------DEDDVALINYTSGTTGNSKGVMLTYRNIvSN---VDGVKEVVLLGKG 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1503 DNVLfsSSISFDVT---IFEIFVPLIYGArmTIYQGEKFDvTKLVQVILEEQVTLSYIPPTLLnEIYDYFVRDNQ-KIVL 1578
Cdd:cd05914 131 DKIL--SILPLHHIyplTFTLLLPLLNGA--HVVFLDKIP-SAKIIALAFAQVTPTLGVPVPL-VIEKIFKMDIIpKLTL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1579 NKLL------VGVEPIKTELLAKYDHLFRGNLQIL-----------------------NGYGPTEATVCCTSYRYESNKE 1629
Cdd:cd05914 205 KKFKfklakkINNRKIRKLAFKKVHEAFGGNIKEFviggakinpdveeflrtigfpytIGYGMTETAPIISYSPPNRIRL 284
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1630 ITTqnvpiGSPLLNTKIYILDSfhriQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLPD 1709
Cdd:cd05914 285 GSA-----GKVIDGVEVRIDSP----DPATGEGEIIVRGPNVMKGYYKNPEATAEAFDK------DGWFHTGDLGKIDAE 349
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1710 GNIEYLGRVDHQ-VKIRGYRIELGEIEASLLKYETIKTAVVIDQE---------DEAGEKYLCAYVVTEKDIPIPEVRAY 1779
Cdd:cd05914 350 GYLYIRGRKKEMiVLSSGKNIYPEEIEAKINNMPFVLESLVVVQEkklvalayiDPDFLDVKALKQRNIIDAIKWEVRDK 429
|
490 500 510
....*....|....*....|....*....|....
gi 446807313 1780 LATKLPHYmipQQL--IPIHNIPL--TQNGKIDR 1809
Cdd:cd05914 430 VNQKVPNY---KKIskVKIVKEEFekTPKGKIKR 460
|
|
| A_NRPS_TubE_like |
cd05906 |
The adenylation domain (A domain) of a family of nonribosomal peptide synthetases (NRPSs) ... |
414-769 |
1.37e-14 |
|
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: 79.25 E-value: 1.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 414 EPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFL---CAMYEDFSQDIGIT----DNVlfsSSISFdvtiFEIFvPLVCGAR 486
Cdd:cd05906 165 RPDDLALLMLTSGSTGFPKAVPLTHRNILARSagkIQHNGLTPQDVFLNwvplDHV---GGLVE----LHLR-AVYLGCQ 236
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 487 MTIYQGEKF--DVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQK----ISLNKLFVGVEPIKT-------ELLAKY 553
Cdd:cd05906 237 QVHVPTEEIlaDPLRWLDLIDRYRVTITWAPNFAFALLNDLLEEIEDGtwdlSSLRYLVNAGEAVVAktirrllRLLEPY 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 554 dhlfrgNLQ---ILNLYGPTE----ATVCCTSYQYERDKEITTqnVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGI 626
Cdd:cd05906 317 ------GLPpdaIRPAFGMTEtcsgVIYSRSFPTYDHSQALEF--VSLGRPIPGVSMRIVDDEGQLLPEGEVGRLQVRGP 388
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 627 GLARGYINRKELTADKFIDhpfergEKLYKTGDIArWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLlkyETIK---- 702
Cdd:cd05906 389 VVTKGYYNNPEANAEAFTE------DGWFRTGDLG-FLDNGNLTITGRTKDTIIVNGVNYYSHEIEAAV---EEVPgvep 458
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 703 --TAVVIQREDESGEKYLCAYVVTEKDIP------IPEVRAYLATKL---PYYMIPqqiISIQNIPLTQNGKIDRKKL 769
Cdd:cd05906 459 sfTAAFAVRDPGAETEELAIFFVPEYDLQdalsetLRAIRSVVSREVgvsPAYLIP---LPKEEIPKTSLGKIQRSKL 533
|
|
| caiC |
PRK08008 |
putative crotonobetaine/carnitine-CoA ligase; Validated |
1323-1812 |
1.57e-14 |
|
putative crotonobetaine/carnitine-CoA ligase; Validated
Pssm-ID: 181195 [Multi-domain] Cd Length: 517 Bit Score: 78.96 E-value: 1.57e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKG-----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLP 1397
Cdd:PRK08008 12 MWDDLADVYGHKTALIFESSGgvvrrYSYLELNEEINRTANLFYSLGIRKGDKVALHLDNCPEFIFCWFGLAKIGAIMVP 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1398 IDTDLPKQRVEYMLTDSGCSHVLVHQN-------------SIIKGIEFQGNVIDLMD--MSFE----EEPGE-DMHMMIE 1457
Cdd:PRK08008 92 INARLLREESAWILQNSQASLLVTSAQfypmyrqiqqedaTPLRHICLTRVALPADDgvSSFTqlkaQQPATlCYAPPLS 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1458 PHNLAYVIYTSGSTGQPKGVMIEHRSL------TNFLCAMYEDfsqDIGITdnVLFSSSISFDVTIfeIFVPLIYGARMT 1531
Cdd:PRK08008 172 TDDTAEILFTSGTTSRPKGVVITHYNLrfagyySAWQCALRDD---DVYLT--VMPAFHIDCQCTA--AMAAFSAGATFV 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1532 IYqgEKFDVTKLVQVILEEQVTLSYIPPTLLNEIY---------DYFVRDnqkiVLNKLLVGVEpiktellAKYDHLFRG 1602
Cdd:PRK08008 245 LL--EKYSARAFWGQVCKYRATITECIPMMIRTLMvqppsandrQHCLRE----VMFYLNLSDQ-------EKDAFEERF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1603 NLQILNGYGPTEATVCCT------SYRYESnkeittqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGI---GLAR 1673
Cdd:PRK08008 312 GVRLLTSYGMTETIVGIIgdrpgdKRRWPS----------IGRPGFCYEAEIRDDHNRPLPAGEIGEICIKGVpgkTIFK 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1674 GYINRKELTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQE 1753
Cdd:PRK08008 382 EYYLDPKATAKVL------EADGWLHTGDTGYVDEEGFFYFVDRRCNMIKRGGENVSCVELENIIATHPKIQDIVVVGIK 455
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1754 DEAGEKYLCAYVV-TE-KDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK08008 456 DSIRDEAIKAFVVlNEgETLSEEEFFAFCEQNMAKFKVPSYLEIRKDLPRNCSGKIIKKNL 516
|
|
| A_NRPS_MycA_like |
cd05908 |
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin ... |
1458-1812 |
1.62e-14 |
|
The adenylation domain of nonribosomal peptide synthetases (NRPS) similar to mycosubtilin synthase subunit A (MycA); The adenylation (A) domain of NRPS recognizes a specific amino acid or hydroxy acid and activates it as (amino)-acyl adenylate by hydrolysis of ATP. The activated acyl moiety then forms thioester to the enzyme-bound cofactor phosphopantetheine of a peptidyl carrier protein domain. This family includes NRPS similar to mycosubtilin synthase subunit A (MycA). Mycosubtilin, which is characterized by a beta-amino fatty acid moiety linked to the circular heptapeptide Asn-Tyr-Asn-Gln-Pro-Ser-Asn, belongs to the iturin family of lipopeptide antibiotics. The mycosubtilin synthase subunit A (MycA) combines functional domains derived from peptide synthetases, amino transferases, and fatty acid synthases. Nonribosomal peptide synthetases are large multifunction enzymes that synthesize many therapeutically useful peptides. NRPS has a distinct modular structure in which each module is responsible for the recognition, activation, and, in some cases, modification of a single amino acid residue of the final peptide product. The modules can be subdivided into domains that catalyze specific biochemical reactions.
Pssm-ID: 341234 [Multi-domain] Cd Length: 499 Bit Score: 78.68 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1458 PHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEdfSQDIGITDNVLFSSSISFDVTIFEI-FVPLIYGARMTIYQGE 1536
Cdd:cd05908 105 ADELAFIQFSSGSTGDPKGVMLTHENLVHNMFAILN--STEWKTKDRILSWMPLTHDMGLIAFhLAPLIAGMNQYLMPTR 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1537 KFDV--TKLVQVILEEQVTLSYIPptllNEIYDYFVR--DNQKI------VLNKLLVGVEPIKTELLAKY-DHLFRGNLQ 1605
Cdd:cd05908 183 LFIRrpILWLKKASEHKATIVSSP----NFGYKYFLKtlKPEKAndwdlsSIRMILNGAEPIDYELCHEFlDHMSKYGLK 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1606 ---ILNGYGPTEATVCCTSYRYESN-----------------KEITTQN------VPIGSPLLNTKIYILDSFHRIQPIG 1659
Cdd:cd05908 259 rnaILPVYGLAEASVGASLPKAQSPfktitlgrrhvthgepePEVDKKDsecltfVEVGKPIDETDIRICDEDNKILPDG 338
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1660 VPGEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIArWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLL 1739
Cdd:cd05908 339 YIGHIQIRGKNVTPGYYNNPEATAKVFTD------DGWLKTGDLG-FIRNGRLVITGREKDIIFVNGQNVYPHDIERIAE 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1740 KYETI---KTAVVIDQEDEAGEKYLCAYVVTEKDIpipEVRAYLATKLPHYMIP------QQLIPIHNIPLTQNGKIDRS 1810
Cdd:cd05908 412 ELEGVelgRVVACGVNNSNTRNEEIFCFIEHRKSE---DDFYPLGKKIKKHLNKrggwqiNEVLPIRRIPKTTSGKVKRY 488
|
..
gi 446807313 1811 KL 1812
Cdd:cd05908 489 EL 490
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
300-771 |
1.63e-14 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 79.06 E-value: 1.63e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 300 EITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSG-----C 373
Cdd:PRK05620 38 QTTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEdevivA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 374 SHVLTYQ-NSIIKGVAFQGSVINLMDIPFEEEQVEDL-QIT-------------------MEPQNLAYVIYTSGSTGQPK 432
Cdd:PRK05620 118 DPRLAEQlGEILKECPCVRAVVFIGPSDADSAAAHMPeGIKvysyealldgrstvydwpeLDETTAAAICYSTGTTGAPK 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 433 GVMIEHRSLtnFLCAMYEDFSQDIGITDNVLFSSSisfdVTIFEIF---VPLvcGARMT----IYQGEKFDVPKLVQVIL 505
Cdd:PRK05620 198 GVVYSHRSL--YLQSLSLRTTDSLAVTHGESFLCC----VPIYHVLswgVPL--AAFMSgtplVFPGPDLSAPTLAKIIA 269
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 506 EEQVTLAYIPPTLLNEIYDYFVRAN-QKISLNKLFVGVEPIKTELLAKYDHlfRGNLQILNLYGPTEATVCCT------- 577
Cdd:PRK05620 270 TAMPRVAHGVPTLWIQLMVHYLKNPpERMSLQEIYVGGSAVPPILIKAWEE--RYGVDVVHVWGMTETSPVGTvarppsg 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 578 -SYQYERDKEITTQNVPIGsplLNTKI----YILDSFHRLQpigvpGEICISGIGLARGYIN----RKELTADKFIDHPF 648
Cdd:PRK05620 348 vSGEARWAYRVSQGRFPAS---LEYRIvndgQVMESTDRNE-----GEIQVRGNWVTASYYHspteEGGGAASTFRGEDV 419
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 649 ERGEKLY------KTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLCAY 721
Cdd:PRK05620 420 EDANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwGERPLAVT 499
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....
gi 446807313 722 VVTEKDIPIPE----VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQ 771
Cdd:PRK05620 500 VLAPGIEPTREtaerLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDLRQ 553
|
|
| PRK08308 |
PRK08308 |
acyl-CoA synthetase; Validated |
1390-1815 |
1.70e-14 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236231 [Multi-domain] Cd Length: 414 Bit Score: 78.15 E-value: 1.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1390 KAGGAYLPIDTDLPKQRVEYMLTDSGCsHVLVHQNsiikgIEFqgnVIDLMDMSFEEEPGedmhmmiephnlaYVIYTSG 1469
Cdd:PRK08308 54 EKGASVLPIHPDTPKEAAIRMAKRAGC-HGLLYGE-----SDF---TKLEAVNYLAEEPS-------------LLQYSSG 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1470 STGQPKgvMIEhRSLTNF---LCAMYEDFSQDIGITDNVLFSSSISFDvtifeifvpLIYGARMTIYQGEKFDV--TK-- 1542
Cdd:PRK08308 112 TTGEPK--LIR-RSWTEIdreIEAYNEALNCEQDETPIVACPVTHSYG---------LICGVLAALTRGSKPVIitNKnp 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1543 --LVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQkivLNKLLVGVEPIKTELLAKydhlFRGN-LQILNGYGPTEATvcC 1619
Cdd:PRK08308 180 kfALNILRNTPQHILYAVPLMLHILGRLLPGTFQ---FHAVMTSGTPLPEAWFYK----LRERtTYMMQQYGCSEAG--C 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1620 TSYryesNKEITTQNvPIGSPLLNTKIYILDSFHRiqpigvPGEICISgiglargyINRKELtadkfidhpfergeklyK 1699
Cdd:PRK08308 251 VSI----CPDMKSHL-DLGNPLPHVSVSAGSDENA------PEEIVVK--------MGDKEI-----------------F 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1700 TGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKyLCAYVVTEKDIPIPEVRA 1778
Cdd:PRK08308 295 TKDLGYKSERGTLHFMGRMDDVINVSGLNVYPIEVEDVMLRLPGVQEAVVYRGKDPvAGER-VKAKVISHEEIDPVQLRE 373
|
410 420 430
....*....|....*....|....*....|....*..
gi 446807313 1779 YLATKLPHYMIPQQLIPIHNIPLTQNGKIDRsKLPKL 1815
Cdd:PRK08308 374 WCIQHLAPYQVPHEIESVTEIPKNANGKVSR-KLLEL 409
|
|
| PRK04319 |
PRK04319 |
acetyl-CoA synthetase; Provisional |
1344-1809 |
3.04e-14 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 235279 [Multi-domain] Cd Length: 570 Bit Score: 78.40 E-value: 3.04e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCS------ 1417
Cdd:PRK04319 74 YTYKELKELSNKFANVLKELGVEKGDRVFIFMPRIPELYFALLGALKNGAIVGPLFEAFMEEAVRDRLEDSEAKvlittp 153
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1418 ---------------HVLVhqnsIIKGIEFQGNVID---LMDMSFEEEPGEDMHmmiePHNLAYVIYTSGSTGQPKGVMI 1479
Cdd:PRK04319 154 allerkpaddlpslkHVLL----VGEDVEEGPGTLDfnaLMEQASDEFDIEWTD----REDGAILHYTSGSTGKPKGVLH 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1480 EHRS-LTNFLCAMYE-DFSQDigitdnvlfsssisfDV------------TIFEIFVPLIYGARMTIYQGEkFDVTKLVQ 1545
Cdd:PRK04319 226 VHNAmLQHYQTGKYVlDLHED---------------DVywctadpgwvtgTSYGIFAPWLNGATNVIDGGR-FSPERWYR 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1546 VILEEQVTLSYIPPTLLneiydyfvrdnqkivlnKLLVGVEPiktELLAKYD--HLfR-----G---------------N 1603
Cdd:PRK04319 290 ILEDYKVTVWYTAPTAI-----------------RMLMGAGD---DLVKKYDlsSL-RhilsvGeplnpevvrwgmkvfG 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1604 LQILNGYGPTE--ATVCCTSYryesnkeitTQNVPIGS---PLLNTKIYILDSFHRIQPIGVPGEICI-----SgigLAR 1673
Cdd:PRK04319 349 LPIHDNWWMTEtgGIMIANYP---------AMDIKPGSmgkPLPGIEAAIVDDQGNELPPNRMGNLAIkkgwpS---MMR 416
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1674 GYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQE 1753
Cdd:PRK04319 417 GIWNNPEKYESYFAG-------DWYVSGDSAYMDEDGYFWFQGRVDDVIKTSGERVGPFEVESKLMEHPAVAEAGVIGKP 489
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313 1754 DE-AGE--KylcAYV-----VTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:PRK04319 490 DPvRGEiiK---AFValrpgYEPSEELKEEIRGFVKKGLGAHAAPREIEFKDKLPKTRSGKIMR 550
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
1344-1812 |
3.61e-14 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 78.15 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLpkQRVEYMLTDSGCSHVLVHQ 1423
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPEL--HRDDHALAARNTEPALVVT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 NSIIKGIEFQGNVIDLMDMSFEE---EPGEdmHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYED----FS 1496
Cdd:PRK06060 109 SDALRDRFQPSRVAEAAELMSEAarvAPGG--YEPMGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKalrlTP 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1497 QDIGITdnvlfSSSISFDVTI-FEIFVPLIYGARMTIYQgekfdvtklVQVILEEQVTLS-YIPPTLLNEIYDYFVR--- 1571
Cdd:PRK06060 187 EDTGLC-----SARMYFAYGLgNSVWFPLATGGSAVINS---------APVTPEAAAILSaRFGPSVLYGVPNFFARvid 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1572 ----DNQKIVLNKLLVG--VEPIKTELLAKydhlFRGNLQILNGYGPTEatvccTSYRYESNKEITTQNVPIGSPLLNTK 1645
Cdd:PRK06060 253 scspDSFRSLRCVVSAGeaLELGLAERLME----FFGGIPILDGIGSTE-----VGQTFVSNRVDEWRLGTLGRVLPPYE 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1646 IYILDSFHRIQPIGVPGEICISGIGLARGYINRKEltadkfidhPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIR 1725
Cdd:PRK06060 324 IRVVAPDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIG 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1726 GYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPE-----VRAYLATKLPHYMIPQQLIPIHNIP 1800
Cdd:PRK06060 395 GVNVDPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGsvmrdLHRGLLNRLSAFKVPHRFAVVDRLP 474
|
490
....*....|..
gi 446807313 1801 LTQNGKIDRSKL 1812
Cdd:PRK06060 475 RTPNGKLVRGAL 486
|
|
| EntF2 |
COG3319 |
Thioesterase domain of type I polyketide synthase or non-ribosomal peptide synthetase ... |
310-849 |
3.81e-14 |
|
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: 78.59 E-value: 3.81e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 310 ANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSIIKGVAF 389
Cdd:COG3319 36 AAALLLLAAALLVALAALALAALALAALLAVALLAAALALAALAALAALALALAAAAAALLLAALALLLALLAALALALL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 390 QGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGITDNVLFSSSIS 469
Cdd:COG3319 116 ALLLAALLLALAALAAAAAAAALAAAAAAAAALAAAAGLGGGGGGAGVLVLVLAALLALLLAALLALALALAALLLLALA 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 470 FDVTIFEIFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFVGVEPIKTEL 549
Cdd:COG3319 196 AALALALLLLLALLLLLLLLLALLLLLLLALLAAAALLALLLALLLLLLAALLLLLALALLLLLALLLLLGLLALLLALL 275
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 550 LAKYDHLFRGNLQILNLYGPTEATVCCTSYQYERDKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLA 629
Cdd:COG3319 276 LLLALLLLAAAAALAAGGTATTAAVTTTAAAAAPGVAGALGPIGGGPGLLVLLVLLVLLLPLLLGVGGGGGGGGGGGGAG 355
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 630 RGYINRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKyETIKTAVVIQR 709
Cdd:COG3319 356 GLAGRGLRAAAALRDPAGAGARGRLRRGGDRGRRLGGGLLLGLGRLRLQRLRRGLREELEEAEAALAE-AAAVAAAVAAA 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 710 EDESGEKYLCAYVVTEKDIPIPEVRAYLATK--LPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNLKSSHLEPTNST 787
Cdd:COG3319 435 AAAAAAAAALAAAVVAAAALAAAALLLLLLLllLPPPLPPALLLLLLLLLLLLLAALLLAAAAPAAAAAAAAAPAPAAAL 514
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 788 ERKLVEIWKDVLGIQRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDF 849
Cdd:COG3319 515 ELALALLLLLLLGLGLVGDDDDFFGGGGGSLLALLLLLLLLALLLRLLLLLALLLAPTLAAL 576
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
289-770 |
4.22e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 77.73 E-value: 4.22e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:PRK13383 49 PGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAAAL 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 TDSGCSHVLTyQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQNlAYVIYTSGSTGQPKGVmiehrsltnflcAM 448
Cdd:PRK13383 129 RAHHISTVVA-DNEFAERIAGADDAVAVIDPATAGAEESGGRPAVAAPG-RIVLLTSGTTGKPKGV------------PR 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 449 YEDFSQDIGITDNVL------FSSSISFDVTIFE------IFVPLVCGArmTIYQGEKFDV-PKLVQVILEEQVTLAYIP 515
Cdd:PRK13383 195 APQLRSAVGVWVTILdrtrlrTGSRISVAMPMFHglglgmLMLTIALGG--TVLTHRHFDAeAALAQASLHRADAFTAVP 272
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 516 pTLLNEIYDYFVRANQKISLNKLFVGV---EPIKTELLAKYDHLFrGNLqILNLYGPTEATVCCTSYQYE-RDKEITtqn 591
Cdd:PRK13383 273 -VVLARILELPPRVRARNPLPQLRVVMssgDRLDPTLGQRFMDTY-GDI-LYNGYGSTEVGIGALATPADlRDAPET--- 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 592 vpIGSPLLNTKIYILDSFHRlqPIG--VPGEICISGiglargyinrkELTADKFIDHpferGEK-----LYKTGDIARWL 664
Cdd:PRK13383 347 --VGKPVAGCPVRILDRNNR--PVGprVTGRIFVGG-----------ELAGTRYTDG----GGKavvdgMTSTGDMGYLD 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 665 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEK--DIPIPEVRAYLATKLP 742
Cdd:PRK13383 408 NAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPgsGVDAAQLRDYLKDRVS 487
|
490 500
....*....|....*....|....*...
gi 446807313 743 YYMIPQQIISIQNIPLTQNGKIDRKKLP 770
Cdd:PRK13383 488 RFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
1345-1717 |
5.66e-14 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 77.75 E-value: 5.66e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGiLGVLKAGGAY-LPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:PLN02614 81 TYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIIS-MEACNAHGLYcVPLYDTLGAGAVEFIISHSEVSIVFVEE 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 NSIIK-------GIEFQGNVIDLMDMSFEE-EPGEDMHMMI--------------------EPHNLAYVIYTSGSTGQPK 1475
Cdd:PLN02614 160 KKISElfktcpnSTEYMKTVVSFGGVSREQkEEAETFGLVIyawdeflklgegkqydlpikKKSDICTIMYTSGTTGDPK 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1476 GVMIEHRSLTNFLCAMYEDF-SQDIGITDNVLFSSSIS----FDVTIFEIFVPliYGARMTIYQGekfDVTKLVQVILEE 1550
Cdd:PLN02614 240 GVMISNESIVTLIAGVIRLLkSANAALTVKDVYLSYLPlahiFDRVIEECFIQ--HGAAIGFWRG---DVKLLIEDLGEL 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1551 QVTLSYIPPTLLNEIYD-------------YFVRDN----------------------QKIVLNK-----------LLVG 1584
Cdd:PLN02614 315 KPTIFCAVPRVLDRVYSglqkklsdggflkKFVFDSafsykfgnmkkgqshveasplcDKLVFNKvkqglggnvriILSG 394
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1585 VEPIKTELlakyDHLFR--GNLQILNGYGPTEAtvcCTSYRYESNKEITTQNVpIGSPLLNTKIYiLDSFHRIQPIGVP- 1661
Cdd:PLN02614 395 AAPLASHV----ESFLRvvACCHVLQGYGLTES---CAGTFVSLPDELDMLGT-VGPPVPNVDIR-LESVPEMEYDALAs 465
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1662 ---GEICISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGR 1717
Cdd:PLN02614 466 tprGEICIRGKTLFSGYYKREDLTKEVLID-------GWLHTGDVGEWQPNGSMKIIDR 517
|
|
| PRK07529 |
PRK07529 |
AMP-binding domain protein; Validated |
414-769 |
5.71e-14 |
|
AMP-binding domain protein; Validated
Pssm-ID: 236043 [Multi-domain] Cd Length: 632 Bit Score: 77.69 E-value: 5.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 414 EPQNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGIT-DNVLFSSSISFDVT--IFEIFVPLVCGARMTI- 489
Cdd:PRK07529 211 GPDDVAAYFHTGGTTGMPKLAQHTHGNEV----ANAWLGALLLGLGpGDTVFCGLPLFHVNalLVTGLAPLARGAHVVLa 286
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 490 ----YQGEKFdVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFVGVEPIKTELLAKYDHlfRGNLQILN 565
Cdd:PRK07529 287 tpqgYRGPGV-IANFWKIVERYRINFLSGVPTVYAALLQVPVDGHDISSLRYALCGAAPLPVEVFRRFEA--ATGVRIVE 363
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 566 LYGPTEAT-VCCTSYqyeRDKEITTQNVPIGSPLLNTKIYILDSFHRLQ---PIGVPGEICISGIGLARGYinrkeLTAD 641
Cdd:PRK07529 364 GYGLTEATcVSSVNP---PDGERRIGSVGLRLPYQRVRVVILDDAGRYLrdcAVDEVGVLCIAGPNVFSGY-----LEAA 435
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 642 KFIDHPFERGekLYKTGDIARWLPDGNIEYLGRVDHQVkIR-GYRIELGEIEASLLKYETIKTAVVIQREDE-SGEkyL- 718
Cdd:PRK07529 436 HNKGLWLEDG--WLNTGDLGRIDADGYFWLTGRAKDLI-IRgGHNIDPAAIEEALLRHPAVALAAAVGRPDAhAGE--Lp 510
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446807313 719 CAYV--VTEKDIPIPEVRAYLATKLP-YYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK07529 511 VAYVqlKPGASATEAELLAFARDHIAeRAAVPKHVRILDALPKTAVGKIFKPAL 564
|
|
| PRK08974 |
PRK08974 |
long-chain-fatty-acid--CoA ligase FadD; |
1323-1812 |
7.35e-14 |
|
long-chain-fatty-acid--CoA ligase FadD;
Pssm-ID: 236359 [Multi-domain] Cd Length: 560 Bit Score: 77.02 E-value: 7.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVCNEKGITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYL---PI 1398
Cdd:PRK08974 28 MFEQAVARYADQPAFINMGEVMTFRKLEERSRAFAAYLQNGlGLKKGDRVALMMPNLLQYPIALFGILRAGMIVVnvnPL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1399 DTdlPKQrVEYMLTDSGCSHVLVHQN--SIIKGIEFQGNV---------------------------------IDLMD-M 1442
Cdd:PRK08974 108 YT--PRE-LEHQLNDSGAKAIVIVSNfaHTLEKVVFKTPVkhviltrmgdqlstakgtlvnfvvkyikrlvpkYHLPDaI 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1443 SFEEEPGEDMHMM-----IEPHNLAYVIYTSGSTGQPKGVMIEHRS-LTNFLCA--MYEDF---SQDIGITDNVLFSssi 1511
Cdd:PRK08974 185 SFRSALHKGRRMQyvkpeLVPEDLAFLQYTGGTTGVAKGAMLTHRNmLANLEQAkaAYGPLlhpGKELVVTALPLYH--- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1512 sfdvtIFEIFVP------------LIYGARmtiyqgekfDVTKLVQVILEEQVTLSyippTLLNEIYDYFVRDNQKIVLN 1579
Cdd:PRK08974 262 -----IFALTVNcllfielggqnlLITNPR---------DIPGFVKELKKYPFTAI----TGVNTLFNALLNNEEFQELD 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1580 ----KLLVGV-EPIKTELLAKYDHLFRGNLqiLNGYGPTEATVCCTSYRYESNKeittQNVPIGSPLLNTKIYILDSFHR 1654
Cdd:PRK08974 324 fsslKLSVGGgMAVQQAVAERWVKLTGQYL--LEGYGLTECSPLVSVNPYDLDY----YSGSIGLPVPSTEIKLVDDDGN 397
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1655 IQPIGVPGEICISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEI 1734
Cdd:PRK08974 398 EVPPGEPGELWVKGPQVMLGYWQRPEATDEVIKD-------GWLATGDIAVMDEEGFLRIVDRKKDMILVSGFNVYPNEI 470
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1735 E-ASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK08974 471 EdVVMLHPKVLEVAAVGVPSEVSGEAVKIFVVKKDPSLTEEELITHCRRHLTGYKVPKLVEFRDELPKSNVGKILRREL 549
|
|
| PRK13383 |
PRK13383 |
acyl-CoA synthetase; Provisional |
1330-1813 |
7.67e-14 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139531 [Multi-domain] Cd Length: 516 Bit Score: 76.57 E-value: 7.67e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1330 RNPNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEY 1409
Cdd:PRK13383 47 RWPGRTAIIDDDGALSYRELQRATESLARRLTRDGVAPGRAVGVMCRNGRGFVTAVFAVGLLGADVVPISTEFRSDALAA 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1410 MLTDSGCShVLVHQNSIIKGIEFQGN---VIDLMDMSFEEEPGEDMhmMIEPHNLayVIYTSGSTGQPKGVmiehrsltn 1486
Cdd:PRK13383 127 ALRAHHIS-TVVADNEFAERIAGADDavaVIDPATAGAEESGGRPA--VAAPGRI--VLLTSGTTGKPKGV--------- 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1487 flcAMYEDFSQDIGITDNVLFSSSISFDVTIfEIFVPLIYGARM-----------TIYQGEKFDV-TKLVQVILEEQVTL 1554
Cdd:PRK13383 193 ---PRAPQLRSAVGVWVTILDRTRLRTGSRI-SVAMPMFHGLGLgmlmltialggTVLTHRHFDAeAALAQASLHRADAF 268
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1555 SYIPpTLLNEIYDYFVRDNQKIVLNKLLVGV---EPIKTELLAKYDHLFrGNLqILNGYGPTEATVCCTSyryeSNKEIT 1631
Cdd:PRK13383 269 TAVP-VVLARILELPPRVRARNPLPQLRVVMssgDRLDPTLGQRFMDTY-GDI-LYNGYGSTEVGIGALA----TPADLR 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1632 TQNVPIGSPLLNTKIYILDSFHRiqPIG--VPGEICISGiglargyinrkELTADKFIDHpferGEK-----LYKTGDIA 1704
Cdd:PRK13383 342 DAPETVGKPVAGCPVRILDRNNR--PVGprVTGRIFVGG-----------ELAGTRYTDG----GGKavvdgMTSTGDMG 404
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1705 RWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEK--DIPIPEVRAYLAT 1782
Cdd:PRK13383 405 YLDNAGRLFIVGREDDMIISGGENVYPRAVENALAAHPAVADNAVIGVPDERFGHRLAAFVVLHPgsGVDAAQLRDYLKD 484
|
490 500 510
....*....|....*....|....*....|.
gi 446807313 1783 KLPHYMIPQQLIPIHNIPLTQNGKIDRSKLP 1813
Cdd:PRK13383 485 RVSRFEQPRDINIVSSIPRNPTGKVLRKELP 515
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
287-692 |
9.18e-14 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 76.45 E-value: 9.18e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 287 QNPNQIAI-VCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVE 365
Cdd:PRK07514 14 ADRDAPFIeTPDGLRYTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 366 YMLTDS----------------------GCSHVLTYqnsiikGVAFQGSVINL-MDIPFEEEQVEdlqitMEPQNLAYVI 422
Cdd:PRK07514 94 YFIGDAepalvvcdpanfawlskiaaaaGAPHVETL------DADGTGSLLEAaAAAPDDFETVP-----RGADDLAAIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 423 YTSGSTGQPKGVMIEHRSLTNFLCAM--YEDFSQDigitdnvlfsssisfDVTI--FEIF----------VPLVCGARMt 488
Cdd:PRK07514 163 YTSGTTGRSKGAMLSHGNLLSNALTLvdYWRFTPD---------------DVLIhaLPIFhthglfvatnVALLAGASM- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 489 IYQgEKFDVPKLVQviLEEQVTLAYIPPTllneiydYFVRANQKISLNK-------LFV-GVEPikteLLAKYDHLF--R 558
Cdd:PRK07514 227 IFL-PKFDPDAVLA--LMPRATVMMGVPT-------FYTRLLQEPRLTReaaahmrLFIsGSAP----LLAETHREFqeR 292
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 559 GNLQILNLYGPTEaTVCCTSYQYERDKEITTqnvpIGSPLLNTKIYILD--SFHRLqPIGVPGEICISGIGLARGYINRK 636
Cdd:PRK07514 293 TGHAILERYGMTE-TNMNTSNPYDGERRAGT----VGFPLPGVSLRVTDpeTGAEL-PPGEIGMIEVKGPNVFKGYWRMP 366
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 637 ELTADKFidhpfeRGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE 692
Cdd:PRK07514 367 EKTAEEF------RADGFFITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVE 416
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
421-765 |
1.48e-13 |
|
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, including acyl-CoA synthetase (AMP-forming)/AMP-acid ligase II, most of which are yet to be characterized. Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341291 [Multi-domain] Cd Length: 331 Bit Score: 74.26 E-value: 1.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 421 VIYTSGSTGQPKGVMIEHRSL-TNFLCAMYedfSQDIGiTDNVLFSSSISFDV-TIFEIFVPLVCGARMTIYQgeKFDVP 498
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALlAQALVLAV---LQAID-EGTVFLNSGPLFHIgTLMFTLATFHAGGTNVFVR--RVDAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 499 KLVQVILEEQVTLAYI-PPTL-----LNEIYDYFVRANQKISLNKLFVGVEPIKTELLAKYdhlFRGnlqilnlYGPTEA 572
Cdd:cd17636 79 EVLELIEAERCTHAFLlPPTIdqiveLNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRK---PGG-------YGQTEV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 573 TVCCTSYQYERdKEITTQNVPigSPLLntKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTADKFIDhpferge 652
Cdd:cd17636 149 MGLATFAALGG-GAIGGAGRP--SPLV--QVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 653 KLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVV-------TE 725
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVlkpgasvTE 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446807313 726 KDIpIPEVRAYLATklpyYMIPQQIISIQNIPLTQNGKID 765
Cdd:cd17636 297 AEL-IEHCRARIAS----YKKPKSVEFADALPRTAGGADD 331
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
273-772 |
2.23e-13 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 75.18 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 273 ETVTAPQLFEEQVKQNPNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAY 352
Cdd:PRK13382 41 EGMGPTSGFAIAAQRCPDRPGLIDELGTLTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADI 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 353 LPIDTELPKQRVEYMLTDSGcSHVLTYQNSIIKGV--AFQG--SVINLMDIPFEEEQVEDLQITMEPQNLA--------- 419
Cdd:PRK13382 121 LLLNTSFAGPALAEVVTREG-VDTVIYDEEFSATVdrALADcpQATRIVAWTDEDHDLTVEVLIAAHAGQRpeptgrkgr 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 420 YVIYTSGSTGQPKG--------------VM----IEHRSLTNFLCAMYE--DFSQdigitdnVLFSSSIsfdvtifeifv 479
Cdd:PRK13382 200 VILLTSGTTGTPKGarrsgpggigtlkaILdrtpWRAEEPTVIVAPMFHawGFSQ-------LVLAASL----------- 261
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 480 plvcgaRMTIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFVGV---EPIKTELLAKYDHL 556
Cdd:PRK13382 262 ------ACTIVTRRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPAEVRNRYSGRSLRFAAasgSRMRPDVVIAFMDQ 335
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 557 FrGNLqILNLYGPTEATVCCTSYQYERDKEITTQnvpiGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRK 636
Cdd:PRK13382 336 F-GDV-IYNNYNATEAGMIATATPADLRAAPDTA----GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGS 409
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 637 eltadkfiDHPFERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEK 716
Cdd:PRK13382 410 --------TKDFHDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQ 479
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 717 YLCAYVVTEKDIP-IPE-----VRAYLATklpyYMIPQQIISIQNIPLTQNGKIDRKKLPQP 772
Cdd:PRK13382 480 RLAAFVVLKPGASaTPEtlkqhVRDNLAN----YKVPRDIVVLDELPRGATGKILRRELQAR 537
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
1344-1812 |
2.58e-13 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 74.94 E-value: 2.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:PRK08276 12 VTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGAKVLIVSA 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 ------NSIIKGIEfQGNVIDLMD-------MSFEEE-------------PGEDMHmmiephnlayviYTSGSTGQPKGV 1477
Cdd:PRK08276 92 aladtaAELAAELP-AGVPLLLVVagpvpgfRSYEEAlaaqpdtpiadetAGADML------------YSSGTTGRPKGI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1478 MIE------HRSLTNFLCAMYEDFsqdIGITDNVLFSSSisfdvtifeifvPLIYGA----RMTIYQG-------EKFDV 1540
Cdd:PRK08276 159 KRPlpgldpDEAPGMMLALLGFGM---YGGPDSVYLSPA------------PLYHTAplrfGMSALALggtvvvmEKFDA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1541 TKLVQVILEEQVTLSYIPPTLlneiydyFVRdnqkivLNKLlvgvePikTELLAKYD----------------HLFRgnl 1604
Cdd:PRK08276 224 EEALALIERYRVTHSQLVPTM-------FVR------MLKL-----P--EEVRARYDvsslrvaihaaapcpvEVKR--- 280
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1605 QILNGYGPteatvccTSYRYESNKE------ITTQNV---P--IGSPLLnTKIYILDSFHRIQPIGVPGEICISGIGLAR 1673
Cdd:PRK08276 281 AMIDWWGP-------IIHEYYASSEgggvtvITSEDWlahPgsVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPF 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1674 GYINRKELTADKFIDHPFergeklYKTGDIArWL-PDGnieYL---GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV 1749
Cdd:PRK08276 353 EYHNDPEKTAAARNPHGW------VTVGDVG-YLdEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAV 422
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1750 I---DqeDEAGEKYLCayVVTEKDIPIP------EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK08276 423 FgvpD--EEMGERVKA--VVQPADGADAgdalaaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
297-771 |
3.68e-13 |
|
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA synthetase in fungi; Fatty acid transport protein (FATP) transports long-chain or very-long-chain fatty acids across the plasma membrane. FATPs also have fatty acid CoA synthetase activity, thus playing dual roles as fatty acid transporters and its activation enzymes. FATPs are the key players in the trafficking of exogenous fatty acids into the cell and in intracellular fatty acid homeostasis. Members of this family are fungal FATPs, including FAT1 from Cochliobolus heterostrophus.
Pssm-ID: 341260 [Multi-domain] Cd Length: 468 Bit Score: 74.39 E-value: 3.68e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 297 NGKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDtelpkqrveYMLTDSGCSH 375
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN---------YNLSGDPLIH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 376 VLTYQNSiikgvafqgsvinlmdipfeeeqvedLQITMEPQNLAYVIYTSGSTGQPKGVMIE-HRSLTNFLCamyedFSQ 454
Cdd:cd05937 73 CLKLSGS--------------------------RFVIVDPDDPAILIYTSGTTGLPKAAAISwRRTLVTSNL-----LSH 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 455 DIGITDNVLFSSSIS-FDVTIFEIFVPLVCGARMTIYQGEKFDVPKL-VQVILEEQVTLAYIPPT---LLN---EIYDyf 526
Cdd:cd05937 122 DLNLKNGDRTYTCMPlYHGTAAFLGACNCLMSGGTLALSRKFSASQFwKDVRDSGATIIQYVGELcryLLStppSPYD-- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 527 vrANQKISL---NklfvGVEPiktELLAKYDHLFrGNLQILNLYGPTEATVCCTSYQ-------------------YERD 584
Cdd:cd05937 200 --RDHKVRVawgN----GLRP---DIWERFRERF-NVPEIGEFYAATEGVFALTNHNvgdfgagaighhglirrwkFENQ 269
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 585 KEITTQNVPIGSPLLNTKiyilDSFHRLQPIGVPGEICI----SGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDI 660
Cdd:cd05937 270 VVLVKMDPETDDPIRDPK----TGFCVRAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDL 345
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 661 ARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV--IQREDESGEKYLCAYVVTEKDIPIPEVRAYLA 738
Cdd:cd05937 346 LRQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVygVKVPGHDGRAGCAAITLEESSAVPTEFTKSLL 425
|
490 500 510
....*....|....*....|....*....|....*...
gi 446807313 739 TK-----LPYYMIPQQIISIQNIPLTQNGKIDRKKLPQ 771
Cdd:cd05937 426 ASlarknLPSYAVPLFLRLTEEVATTDNHKQQKGVLRD 463
|
|
| FACL_like_1 |
cd05910 |
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ... |
1345-1812 |
3.69e-13 |
|
Uncharacterized subfamily of fatty acid CoA ligase (FACL); Fatty acyl-CoA ligases catalyze the ATP-dependent activation of fatty acids in a two-step reaction. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is a required step before free fatty acids can participate in most catabolic and anabolic reactions.
Pssm-ID: 341236 [Multi-domain] Cd Length: 457 Bit Score: 74.42 E-value: 3.69e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDsgcshvlvhqn 1424
Cdd:cd05910 4 SFRELDERSDRIAQGLTAYGIRRGMRAVLMVPPGPDFFALTFALFKAGAVPVLIDPGMGRKNLKQCLQE----------- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 siikgIEFQGnvidlmdmsFEEEPGEDmhmmiEPhnlAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIGITDN 1504
Cdd:cd05910 73 -----AEPDA---------FIGIPKAD-----EP---AAILFTSGSTGTPKGVVYRHGTFAAQIDALRQLYGIRPGEVDL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1505 VLFSssisfdvtIFEIFVPLIYGAR----MTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKI-VLN 1579
Cdd:cd05910 131 ATFP--------LFALFGPALGLTSvipdMDPTRPARADPQKLVGAIRQYGVSIVFGSPALLERVARYCAQHGITLpSLR 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1580 KLLVGVEPIKTELLAKYDHLFRGNLQILNGYGPTEA-TVCCTSYRyesNKEITTQNVP-------IGSPLLNTKIYIL-- 1649
Cdd:cd05910 203 RVLSAGAPVPIALAARLRKMLSDEAEILTPYGATEAlPVSSIGSR---ELLATTTAATsggagtcVGRPIPGVRVRIIei 279
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1650 --------DSFHRIqPIGVPGEICISGIGLARGYINRKELTADKFIDHPFERgeKLYKTGDIARWLPDGNIEYLGRVDHQ 1721
Cdd:cd05910 280 ddepiaewDDTLEL-PRGEIGEITVTGPTVTPTYVNRPVATALAKIDDNSEG--FWHRMGDLGYLDDEGRLWFCGRKAHR 356
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1722 VKIRGYRIELGEIEASLLKYETIK-TAVVIDQEDEAGEKYLCayVVTEKDIPIPEVRAY-----LATKLPH-YMIPQQLI 1794
Cdd:cd05910 357 VITTGGTLYTEPVERVFNTHPGVRrSALVGVGKPGCQLPVLC--VEPLPGTITPRARLEqelraLAKDYPHtQRIGRFLI 434
|
490
....*....|....*....
gi 446807313 1795 -PIHNIPLTQNGKIDRSKL 1812
Cdd:cd05910 435 hPSFPVDIRHNAKIFREKL 453
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
1344-1718 |
8.64e-13 |
|
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: 73.55 E-value: 8.64e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSgCSHVLVHQ 1423
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETS-EANILVVE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 N-------SIIKG--------IEFQG-------NVI---DLMDMSFEEePGEDMHMMIE---PHNLAYVIYTSGSTGQPK 1475
Cdd:cd05933 88 NqkqlqkiLQIQDklphlkaiIQYKEplkekepNLYswdEFMELGRSI-PDEQLDAIISsqkPNQCCTLIYTSGTTGMPK 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1476 GVMIEHRSLTNFLCAMyedfSQDIGITDN-VLFSSSISF------DVTIFEIFVPLIYGA-------------------- 1528
Cdd:cd05933 167 GVMLSHDNITWTAKAA----SQHMDLRPAtVGQESVVSYlplshiAAQILDIWLPIKVGGqvyfaqpdalkgtlvktlre 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1529 -RMTIYQG-----EKFDvTKLVQVI------------------LEEQVTL--SYIPPTLLNEIYDYFV--RDNQKIVLN- 1579
Cdd:cd05933 243 vRPTAFMGvprvwEKIQ-EKMKAVGaksgtlkrkiaswakgvgLETNLKLmgGESPSPLFYRLAKKLVfkKVRKALGLDr 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1580 --KLLVGVEPIKTELLakydHLFRG-NLQILNGYGPTEATVCCT-----SYR-YESNKEIttqnvpigsPLLNTKIyild 1650
Cdd:cd05933 322 cqKFFTGAAPISRETL----EFFLSlNIPIMELYGMSETSGPHTisnpqAYRlLSCGKAL---------PGCKTKI---- 384
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1651 sfHRIQPIGVpGEICISGIGLARGYINRKELTADKFIDHPFERgeklykTGDIARWLPDGNIEYLGRV 1718
Cdd:cd05933 385 --HNPDADGI-GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLH------SGDLGKLDEDGFLYITGRI 443
|
|
| PRK06060 |
PRK06060 |
p-hydroxybenzoic acid--AMP ligase FadD22; |
301-779 |
1.15e-12 |
|
p-hydroxybenzoic acid--AMP ligase FadD22;
Pssm-ID: 180374 [Multi-domain] Cd Length: 705 Bit Score: 73.53 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 301 ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTyq 380
Cdd:PRK06060 31 VTHGQIHDGAARLGEVLRNRGLSSGDRVLLCLPDSPDLVQLLLACLARGVMAFLANPELHRDDHALAARNTEPALVVT-- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 381 NSIIKGVAFQGSVINLMDIPFEEEQVE--DLQItMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYED----FSQ 454
Cdd:PRK06060 109 SDALRDRFQPSRVAEAAELMSEAARVApgGYEP-MGGDALAYATYTSGTTGPPKAAIHRHADPLTFVDAMCRKalrlTPE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 455 DIGITdnvlfSSSISFDVTI-FEIFVPLVCGARMTIYQgekfdvpklVQVILEEQVTL-AYIPPTLLNEIYDYFVR---- 528
Cdd:PRK06060 188 DTGLC-----SARMYFAYGLgNSVWFPLATGGSAVINS---------APVTPEAAAILsARFGPSVLYGVPNFFARvids 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 529 --ANQKISLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEATVCCTSYQYERDKEITtqnvpIGSPLLNTKIYIL 606
Cdd:PRK06060 254 csPDSFRSLRCVVSAGEALELGLAERLMEFF-GGIPILDGIGSTEVGQTFVSNRVDEWRLGT-----LGRVLPPYEIRVV 327
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 607 DSFHRLQPIGVPGEICISGIGLARGYINRKEltadkfidhPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRI 686
Cdd:PRK06060 328 APDGTTAGPGVEGDLWVRGPAIAKGYWNRPD---------SPVANEGWLDTRDRVCIDSDGWVTYRCRADDTEVIGGVNV 398
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 687 ELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIPE-----VRAYLATKLPYYMIPQQIISIQNIPLTQN 761
Cdd:PRK06060 399 DPREVERLIIEDEAVAEAAVVAVRESTGASTLQAFLVATSGATIDGsvmrdLHRGLLNRLSAFKVPHRFAVVDRLPRTPN 478
|
490 500
....*....|....*....|...
gi 446807313 762 GKIDRKKL-----PQPINNLKSS 779
Cdd:PRK06060 479 GKLVRGALrkqspTKPIWELSLT 501
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
269-771 |
1.24e-12 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 73.00 E-value: 1.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 269 TLLCETVTAPQLF---EEQVKQNPNQIAIVCNGKEI--TYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGIL 343
Cdd:PRK05852 7 AAPMASDFGPRIAdlvEVAATRLPEAPALVVTADRIaiSYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 344 GILKAGGAYLPIDTELPKQ-----------RVEYMLTDSGCSHVLTYQNSIIKGVAFQGSVINLMDI--PFEEEQVEDLQ 410
Cdd:PRK05852 87 AASRADLVVVPLDPALPIAeqrvrsqaagaRVVLIDADGPHDRAEPTTRWWPLTVNVGGDSGPSGGTlsVHLDAATEPTP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 411 ITMEPQNL----AYVIYTSGSTGQPKGVMIEHRSLT---NFLCAMYEDFSQDIGITDNVLFSSSisfdVTIFEIFVPLVC 483
Cdd:PRK05852 167 ATSTPEGLrpddAMIMFTGGTTGLPKMVPWTHANIAssvRAIITGYRLSPRDATVAVMPLYHGH----GLIAALLATLAS 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 484 GARMTIYQGEKFD------------------VPKLVQVILEEQVT--LAYIPPTLlneiydYFVRAnqkISLNKLFVGVE 543
Cdd:PRK05852 243 GGAVLLPARGRFSahtfwddikavgatwytaVPTIHQILLERAATepSGRKPAAL------RFIRS---CSAPLTAETAQ 313
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 544 PIKTELLAKydhlfrgnlqILNLYGPTEATVCCTSYQYE---RDKEITTQNVPIGSPLlNTKIYILDSFHRLQPIGVPGE 620
Cdd:PRK05852 314 ALQTEFAAP----------VVCAFGMTEATHQVTTTQIEgigQTENPVVSTGLVGRST-GAQIRIVGSDGLPLPAGAVGE 382
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 621 ICISGIGLARGYINRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYET 700
Cdd:PRK05852 383 VWLRGTTVVRGYLGDPTITAANFTDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPN 455
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446807313 701 IKTAVVIQREDES-GEKYLCAYVVTEKDIPIP-EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQ 771
Cdd:PRK05852 456 VMEAAVFGVPDQLyGEAVAAVIVPRESAPPTAeELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDRRAVAE 528
|
|
| PLN02614 |
PLN02614 |
long-chain acyl-CoA synthetase |
280-713 |
2.21e-12 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 166255 [Multi-domain] Cd Length: 666 Bit Score: 72.36 E-value: 2.21e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 280 LFEEQVKQNPNQIAI----VCNGKE-----ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGG 350
Cdd:PLN02614 50 VFRMSVEKYPNNPMLgrreIVDGKPgkyvwQTYQEVYDIVIKLGNSLRSVGVKDEAKCGIYGANSPEWIISMEACNAHGL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 351 AYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSIIK-------GVAFQGSVINLMDI-PFEEEQVEDLQITM--------- 413
Cdd:PLN02614 130 YCVPLYDTLGAGAVEFIISHSEVSIVFVEEKKISElfktcpnSTEYMKTVVSFGGVsREQKEEAETFGLVIyawdeflkl 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 414 -----------EPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDF-SQDIGITDNVLFSSSIS----FDVTIFEI 477
Cdd:PLN02614 210 gegkqydlpikKKSDICTIMYTSGTTGDPKGVMISNESIVTLIAGVIRLLkSANAALTVKDVYLSYLPlahiFDRVIEEC 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 478 FVPLvcGARMTIYQGekfDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFvraNQKISLNKLF------------------ 539
Cdd:PLN02614 290 FIQH--GAAIGFWRG---DVKLLIEDLGELKPTIFCAVPRVLDRVYSGL---QKKLSDGGFLkkfvfdsafsykfgnmkk 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 540 ----VGVEPIKTELL-AKYDHLFRGNLQ-ILNLYGPTEATV--------CC---TSYQYERDKEITTQNVP--------I 594
Cdd:PLN02614 362 gqshVEASPLCDKLVfNKVKQGLGGNVRiILSGAAPLASHVesflrvvaCChvlQGYGLTESCAGTFVSLPdeldmlgtV 441
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 595 GSPLLNTKIYiLDSFHRLQPIGVP----GEICISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPDGNIE 670
Cdd:PLN02614 442 GPPVPNVDIR-LESVPEMEYDALAstprGEICIRGKTLFSGYYKREDLTKEVLID-------GWLHTGDVGEWQPNGSMK 513
|
490 500 510 520
....*....|....*....|....*....|....*....|....
gi 446807313 671 YLGRVDHQVKI-RGYRIELGEIEASLLKYETIKTAVVIQREDES 713
Cdd:PLN02614 514 IIDRKKNIFKLsQGEYVAVENIENIYGEVQAVDSVWVYGNSFES 557
|
|
| PRK06814 |
PRK06814 |
acyl-[ACP]--phospholipid O-acyltransferase; |
1462-1808 |
2.33e-12 |
|
acyl-[ACP]--phospholipid O-acyltransferase;
Pssm-ID: 235865 [Multi-domain] Cd Length: 1140 Bit Score: 72.69 E-value: 2.33e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1462 AYVIYTSGSTGQPKGVMIEHRsltNFLCAMYE-----DFS-QDIGItdNVL--FSSsisFDVTIFEIfVPLIYGARMTIY 1533
Cdd:PRK06814 796 AVILFTSGSEGTPKGVVLSHR---NLLANRAQvaariDFSpEDKVF--NALpvFHS---FGLTGGLV-LPLLSGVKVFLY 866
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1534 QgEKFDVTKLVQVILEEQVTLSYIPPTLLN------EIYDYFVrdnqkivLNKLLVGVEPIKTELLAKYDHLFRgnLQIL 1607
Cdd:PRK06814 867 P-SPLHYRIIPELIYDTNATILFGTDTFLNgyaryaHPYDFRS-------LRYVFAGAEKVKEETRQTWMEKFG--IRIL 936
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1608 NGYGPTEAtvcctsyryesnkeittqnvpigSPLL--NTKIY--------ILDSFH-RIQPI-GVP--GEICISGIGLAR 1673
Cdd:PRK06814 937 EGYGVTET-----------------------APVIalNTPMHnkagtvgrLLPGIEyRLEPVpGIDegGRLFVRGPNVML 993
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1674 GYinrkeLTADK-FIDHPFERGEklYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE--ASLLkYETIKTAVVI 1750
Cdd:PRK06814 994 GY-----LRAENpGVLEPPADGW--YDTGDIVTIDEEGFITIKGRAKRFAKIAGEMISLAAVEelAAEL-WPDALHAAVS 1065
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1751 DQEDEAGEKYLcaYVVTEKDIPIPEVRAYLATK-LPHYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:PRK06814 1066 IPDARKGERII--LLTTASDATRAAFLAHAKAAgASELMVPAEIITIDEIPLLGTGKID 1122
|
|
| PRK08276 |
PRK08276 |
long-chain-fatty-acid--CoA ligase; Validated |
298-769 |
3.15e-12 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 236215 [Multi-domain] Cd Length: 502 Bit Score: 71.47 E-value: 3.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 298 GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSG----- 372
Cdd:PRK08276 9 GEVVTYGELEARSNRLAHGLRALGLREGDVVAILLENNPEFFEVYWAARRSGLYYTPINWHLTAAEIAYIVDDSGakvli 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 373 CSHVLTYQNSIIKGVAFQGSVINLMD-------IPFEEE--QVEDLQITMEPQNlAYVIYTSGSTGQPKGVMIE------ 437
Cdd:PRK08276 89 VSAALADTAAELAAELPAGVPLLLVVagpvpgfRSYEEAlaAQPDTPIADETAG-ADMLYSSGTTGRPKGIKRPlpgldp 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 438 HRSLTNFLCAMYEDFsqdIGITDNVLFSSSisfdvtifeifvPLVCGA----RMTIYQG-------EKFDVPKLVQVILE 506
Cdd:PRK08276 168 DEAPGMMLALLGFGM---YGGPDSVYLSPA------------PLYHTAplrfGMSALALggtvvvmEKFDAEEALALIER 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 507 EQVTLAYIPPTLlneiydyFVRanqkisLNKLfvgvePikTELLAKYD----------------HLFRgnlQILNLYGP- 569
Cdd:PRK08276 233 YRVTHSQLVPTM-------FVR------MLKL-----P--EEVRARYDvsslrvaihaaapcpvEVKR---AMIDWWGPi 289
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 570 -------TEA---TVcCTSYQYERDKEittqnvPIGSPLLnTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELT 639
Cdd:PRK08276 290 iheyyasSEGggvTV-ITSEDWLAHPG------SVGKAVL-GEVRILDEDGNELPPGEIGTVYFEMDGYPFEYHNDPEKT 361
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 640 ADKFIDHPFergeklYKTGDIArWL-PDGnieYL---GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQ-REDESG 714
Cdd:PRK08276 362 AAARNPHGW------VTVGDVG-YLdEDG---YLyltDRKSDMIISGGVNIYPQEIENLLVTHPKVADVAVFGvPDEEMG 431
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 715 EKYLCayVVTEKDIPIP------EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK08276 432 ERVKA--VVQPADGADAgdalaaELIAWLRGRLAHYKCPRSIDFEDELPRTPTGKLYKRRL 490
|
|
| FATP_chFAT1_like |
cd05937 |
Uncharacterized subfamily of bifunctional fatty acid transporter/very-long-chain acyl-CoA ... |
1340-1812 |
3.65e-12 |
|
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: 71.31 E-value: 3.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1340 NEKGITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDtdlpkqrveYMLTDSGCSH 1418
Cdd:cd05937 2 EGKTWTYSETYDLVLRYAHWLHDDlGVQAGDFVAIDLTNSPEFVFLWLGLWSIGAAPAFIN---------YNLSGDPLIH 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1419 VLVhqnsiIKGIEFqgnvidlmdmsfeeepgedmhMMIEPHNLAYVIYTSGSTGQPKGVMIE-HRSLTNFLCamyedFSQ 1497
Cdd:cd05937 73 CLK-----LSGSRF---------------------VIVDPDDPAILIYTSGTTGLPKAAAISwRRTLVTSNL-----LSH 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1498 DIGITDNVLFSSSIS-FDVTIFEI-FVPLIYGARmTIYQGEKFDVTKL-VQVILEEQVTLSYIPPT---LLN---EIYDy 1568
Cdd:cd05937 122 DLNLKNGDRTYTCMPlYHGTAAFLgACNCLMSGG-TLALSRKFSASQFwKDVRDSGATIIQYVGELcryLLStppSPYD- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1569 fvRDNQKIVL--NKL----------LVGVEPIK-----TELLAKYDHLFRGNLQI--LNGYGPTeatvcctSYRYESNKE 1629
Cdd:cd05937 200 --RDHKVRVAwgNGLrpdiwerfreRFNVPEIGefyaaTEGVFALTNHNVGDFGAgaIGHHGLI-------RRWKFENQV 270
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1630 ITTQNVP-IGSPLLNTKiyilDSFHRIQPIGVPGEICI----SGIGLARGYINRKELTADKFIDHPFERGEKLYKTGDIA 1704
Cdd:cd05937 271 VLVKMDPeTDDPIRDPK----TGFCVRAPVGEPGEMLGrvpfKNREAFQGYLHNEDATESKLVRDVFRKGDIYFRTGDLL 346
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1705 RWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-----DQEDEAGekylCAYV-VTEKDIPIPEVRA 1778
Cdd:cd05937 347 RQDADGRWYFLDRLGDTFRWKSENVSTTEVADVLGAHPDIAEANVYgvkvpGHDGRAG----CAAItLEESSAVPTEFTK 422
|
490 500 510
....*....|....*....|....*....|....*....
gi 446807313 1779 YLATK-----LPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05937 423 SLLASlarknLPSYAVPLFLRLTEEVATTDNHKQQKGVL 461
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
782-855 |
3.74e-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: 63.72 E-value: 3.74e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 782 EPTNSTERKLVEIWKDVLGI--QRIGIRDNFF-EIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVDFSKYILE 855
Cdd:COG0236 1 MPREELEERLAEIIAEVLGVdpEEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEE 77
|
|
| AcpP |
COG0236 |
Acyl carrier protein [Lipid transport and metabolism]; Acyl carrier protein is part of the ... |
1826-1901 |
1.19e-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: 1.19e-11
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 1826 PRNEIDSSLIDIWSSILGVN--NIGINDNFF-ELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSDVISRNKG 1901
Cdd:COG0236 2 PREELEERLAEIIAEVLGVDpeEITPDDSFFeDLGLDSLDAVELIAALEEEFGIELPDTELFEYPTVADLADYLEEKLA 80
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
1605-1812 |
1.20e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 69.79 E-value: 1.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1605 QILNGYGPTEATVCCTSYRYESNKEITtqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTAD 1684
Cdd:PRK05677 353 AICEGYGMTETSPVVSVNPSQAIQVGT-----IGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEATDE 427
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1685 KFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAY 1764
Cdd:PRK05677 428 ILDS------DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIKVF 501
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446807313 1765 VVTEKDIPIPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK05677 502 VVVKPGETLTKeqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
789-848 |
1.31e-11 |
|
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: 61.43 E-value: 1.31e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 789 RKLVEIWKDVLGI--QRIGIRDNFFEIGGHSLKAARLISIVNKEFNVQLSIKSLFKFPVLVD 848
Cdd:pfam00550 1 ERLRELLAEVLGVpaEEIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK07514 |
PRK07514 |
malonyl-CoA synthase; Validated |
1344-1735 |
1.34e-11 |
|
malonyl-CoA synthase; Validated
Pssm-ID: 181011 [Multi-domain] Cd Length: 504 Bit Score: 69.52 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLV-- 1421
Cdd:PRK07514 29 YTYGDLDAASARLANLLVALGVKPGDRVAVQVEKSPEALALYLATLRAGAVFLPLNTAYTLAELDYFIGDAEPALVVCdp 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1422 HQNSIIKGIEFQGNVIDL-----------------MDMSFEEEP-GEDmhmmiephNLAYVIYTSGSTGQPKGVMIEHRS 1483
Cdd:PRK07514 109 ANFAWLSKIAAAAGAPHVetldadgtgslleaaaaAPDDFETVPrGAD--------DLAAILYTSGTTGRSKGAMLSHGN 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1484 LTNFLCAM--YEDFSQDigitdnvlfsssisfDVTI--FEIF----------VPLIYGARMtIYQgEKFDvtkLVQVI-L 1548
Cdd:PRK07514 181 LLSNALTLvdYWRFTPD---------------DVLIhaLPIFhthglfvatnVALLAGASM-IFL-PKFD---PDAVLaL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1549 EEQVTLSYIPPTllneiydYFVRDNQKIVLNKLLV--------GVEPikteLLAKYDHLF--RGNLQILNGYGPTEaTVC 1618
Cdd:PRK07514 241 MPRATVMMGVPT-------FYTRLLQEPRLTREAAahmrlfisGSAP----LLAETHREFqeRTGHAILERYGMTE-TNM 308
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1619 CTSYRYESNKEITTqnvpIGSPLLNTKIYILDSFH-RIQPIGVPGEICISGIGLARGYINRKELTADKFidhpfeRGEKL 1697
Cdd:PRK07514 309 NTSNPYDGERRAGT----VGFPLPGVSLRVTDPETgAELPPGEIGMIEVKGPNVFKGYWRMPEKTAEEF------RADGF 378
|
410 420 430
....*....|....*....|....*....|....*...
gi 446807313 1698 YKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIE 1735
Cdd:PRK07514 379 FITGDLGKIDERGYVHIVGRGKDLIISGGYNVYPKEVE 416
|
|
| PLN02736 |
PLN02736 |
long-chain acyl-CoA synthetase |
415-674 |
1.46e-11 |
|
long-chain acyl-CoA synthetase
Pssm-ID: 178337 [Multi-domain] Cd Length: 651 Bit Score: 69.74 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 415 PQNLAYVIYTSGSTGQPKGVMIEHRSLtnflcamyedFSQDIGITDNVLFSSS---ISF--DVTIFE---IFVPLVCGAR 486
Cdd:PLN02736 220 PEDVATICYTSGTTGTPKGVVLTHGNL----------IANVAGSSLSTKFYPSdvhISYlpLAHIYErvnQIVMLHYGVA 289
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 487 MTIYQGekfDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQ--------------------------------KIS 534
Cdd:PLN02736 290 VGFYQG---DNLKLMDDLAALRPTIFCSVPRLYNRIYDGITNAVKesgglkerlfnaaynakkqalengknpspmwdRLV 366
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 535 LNKL-----------FVGVEPIKTELLAKYDHLFRGnlQILNLYGPTEaTVCCTSYQYERDKeiTTQNVpiGSPLLNTKI 603
Cdd:PLN02736 367 FNKIkaklggrvrfmSSGASPLSPDVMEFLRICFGG--RVLEGYGMTE-TSCVISGMDEGDN--LSGHV--GSPNPACEV 439
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 604 YILDsfhrlqpigVP-------------GEICISGIGLARGYInRKELTADKFIDhpferGEKLYKTGDIARWLPDGNIE 670
Cdd:PLN02736 440 KLVD---------VPemnytsedqpyprGEICVRGPIIFKGYY-KDEVQTREVID-----EDGWLHTGDIGLWLPGGRLK 504
|
....
gi 446807313 671 YLGR 674
Cdd:PLN02736 505 IIDR 508
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
302-769 |
1.47e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 69.40 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 302 TYKQLNIKANQLARRLLDQGVKREFIVGVM---MERSIEMIVGILGIlkagGA--------------------------- 351
Cdd:PRK06018 41 TYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI----GAichtvnprlfpeqiawiinhaedrvvi 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 352 ----YLP----IDTELPkqRVEYMLTDSGCSHVLtyQNSIIKGVAFQGSVinlmdipfeEEQVEDLQITMEPQNLAYVI- 422
Cdd:PRK06018 117 tdltFVPilekIADKLP--SVERYVVLTDAAHMP--QTTLKNAVAYEEWI---------AEADGDFAWKTFDENTAAGMc 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 423 YTSGSTGQPKGVMIEHRSltNFLCAMYEDFSQDIGITDnvlfSSSISFDVTIFEI------FVPLVCGARMtIYQGEKFD 496
Cdd:PRK06018 184 YTSGTTGDPKGVLYSHRS--NVLHALMANNGDALGTSA----ADTMLPVVPLFHAnswgiaFSAPSMGTKL-VMPGAKLD 256
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 497 VPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKI-SLNKLFVGVEPIKTELLAKYDHLfrgNLQILNLYGPTE---- 571
Cdd:PRK06018 257 GASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLpHLKMVVCGGSAMPRSMIKAFEDM---GVEVRHAWGMTEmspl 333
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 572 ATVCCTSYQYER---DKEItTQNVPIGSPLLNTKIYILDSFHRLQPIG--VPGEICISGIGLARGY--INRKELTADKFI 644
Cdd:PRK06018 334 GTLAALKPPFSKlpgDARL-DVLQKQGYPPFGVEMKITDDAGKELPWDgkTFGRLKVRGPAVAAAYyrVDGEILDDDGFF 412
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 645 DhpfergeklykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-QREDESGEKYLCAYVV 723
Cdd:PRK06018 413 D-----------TGDVATIDAYGYMRITDRSKDVIKSGGEWISSIDLENLAVGHPKVAEAAVIgVYHPKWDERPLLIVQL 481
|
490 500 510 520
....*....|....*....|....*....|....*....|....*..
gi 446807313 724 TEKDIPIP-EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK06018 482 KPGETATReEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTAL 528
|
|
| LCL_NRPS-like |
cd19531 |
LCL-type Condensation (C) domain of non-ribosomal peptide synthetases(NRPSs) and similar ... |
7-238 |
1.77e-11 |
|
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: 68.54 E-value: 1.77e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDclslnnIQASK-ESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVK 85
Cdd:cd19531 179 QREWLQGEVLERQLAYWREQLAGAPPVLELPTDrpr-paVQSFRgARVRFTLPAELTAALRALARREGATLFMTLLAAFQ 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 86 YLLSRYTDKDDVVIGMPVFKQGQEET-------VfqnNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQ- 157
Cdd:cd19531 258 VLLHRYSGQDDIVVGTPVAGRNRAELegligffV---NTLVLRTDLSGDPTFRELLARVRETALEAYAHQDLPFEKLVEa 334
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 158 ------------------LLSLDGESNNLPLLNTIVMLDDIHcyesTDKinSDMVIRFMKNEEQLKVQVDYNSTLYSEGL 219
Cdd:cd19531 335 lqperdlsrsplfqvmfvLQNAPAAALELPGLTVEPLEVDSG----TAK--FDLTLSLTETDGGLRGSLEYNTDLFDAAT 408
|
250
....*....|....*....
gi 446807313 220 VSRIVNHLYNILDILMKDP 238
Cdd:cd19531 409 IERMAGHFQTLLEAIVADP 427
|
|
| PtmA |
cd17636 |
long-chain fatty acid CoA ligase (FadD); This family contains fatty acid CoA ligases, ... |
1464-1808 |
4.02e-11 |
|
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: 66.94 E-value: 4.02e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1464 VIYTSGSTGQPKGVMIEHRSL-TNFLCAMYedfSQDIGiTDNVLFSSSISFDV-TIFEIFVPLIYGARMTIYQgeKFDVT 1541
Cdd:cd17636 5 AIYTAAFSGRPNGALLSHQALlAQALVLAV---LQAID-EGTVFLNSGPLFHIgTLMFTLATFHAGGTNVFVR--RVDAE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1542 KLVQVILEEQVTLSYI-PPTL-----LNEIYDYFVRDNQKIVLNKLLVGVEPIKTELLAKYdhlfrgnlqiLNGYGPTEa 1615
Cdd:cd17636 79 EVLELIEAERCTHAFLlPPTIdqiveLNADGLYDLSSLRSSPAAPEWNDMATVDTSPWGRK----------PGGYGQTE- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1616 TVCCTSYRYESNKEITTQNVPigSPLLntKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKELTADKFIDhpferge 1695
Cdd:cd17636 148 VMGLATFAALGGGAIGGAGRP--SPLV--QVRILDEDGREVPDGEVGEIVARGPTVMAGYWNRPEVNARRTRG------- 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1696 KLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVV-------TE 1768
Cdd:cd17636 217 GWHHTNDLGRREPDGSLSFVGPKTRMIKSGAENIYPAEVERCLRQHPAVADAAVIGVPDPRWAQSVKAIVVlkpgasvTE 296
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 446807313 1769 KDIpIPEVRAYLATklphYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:cd17636 297 AEL-IEHCRARIAS----YKKPKSVEFADALPRTAGGADD 331
|
|
| PRK05677 |
PRK05677 |
long-chain-fatty-acid--CoA ligase; Validated |
562-769 |
5.59e-11 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 168170 [Multi-domain] Cd Length: 562 Bit Score: 67.87 E-value: 5.59e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 562 QILNLYGPTEAT--VCCTSYQYerdkeitTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELT 639
Cdd:PRK05677 353 AICEGYGMTETSpvVSVNPSQA-------IQVGTIGIPVPSTLCKVIDDDGNELPLGEVGELCVKGPQVMKGYWQRPEAT 425
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 640 ADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLC 719
Cdd:PRK05677 426 DEILDS------DGWLKTGDIALIQEDGYMRIVDRKKDMILVSGFNVYPNELEDVLAALPGVLQCAAIGVPDEKSGEAIK 499
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 446807313 720 AYVVTEKDIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK05677 500 VFVVVKPGETLTKeqVMEHMRANLTGYKVPKAVEFRDELPTTNVGKILRREL 551
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
1345-1815 |
5.95e-11 |
|
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: 67.45 E-value: 5.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQN 1424
Cdd:cd05939 5 TFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALIFNLL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1425 SiikgiefqgnviDLMDMSFEEEPGEDmhmMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDF---SQDIGI 1501
Cdd:cd05939 85 D------------PLLTQSSTEPPSQD---DVNFRDKLFYIYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFgmrPEDVVY 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1502 TDNVLFSSSISfdvtIFEIFVPLIYGarMTIYQGEKFDVTKLVQVILEEQVTLS-YIpptllNEIYDYF----VRDNQKI 1576
Cdd:cd05939 150 DCLPLYHSAGG----IMGVGQALLHG--STVVIRKKFSASNFWDDCVKYNCTIVqYI-----GEICRYLlaqpPSEEEQK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1577 VLNKLLVGvEPIKTELLAKYDHLFRGNlQILNGYGPTEatvcCTSyryeSNKEITTQNVPIG-SPLLNTKIY-------- 1647
Cdd:cd05939 219 HNVRLAVG-NGLRPQIWEQFVRRFGIP-QIGEFYGATE----GNS----SLVNIDNHVGACGfNSRILPSVYpirlikvd 288
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1648 ------ILDSFHRIQPIGvPGEiciSGIGLAR-----------GYINRKElTADKFIDHPFERGEKLYKTGDIARWLPDG 1710
Cdd:cd05939 289 edtgelIRDSDGLCIPCQ-PGE---PGLLVGKiiqndplrrfdGYVNEGA-TNKKIARDVFKKGDSAFLSGDVLVMDELG 363
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1711 NIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-----DQEDEAGekyLCAYVVTEKDIPIPEVRAYLATKLP 1785
Cdd:cd05939 364 YLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYgvevpGVEGRAG---MAAIVDPERKVDLDRFSAVLAKSLP 440
|
490 500 510
....*....|....*....|....*....|
gi 446807313 1786 HYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:cd05939 441 PYARPQFIRLLPEVDKTGTFKLQKTDLQKE 470
|
|
| SgcC5_NRPS-like |
cd19539 |
SgcC5 is a non-ribosomal peptide synthetase (NRPS) condensation enzyme with ester- and amide- ... |
7-238 |
6.67e-11 |
|
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: 67.02 E-value: 6.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 7 QQVLLSSEKFKKEKEYWLDKLSGdVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:cd19539 179 QREALAAPRAAELLDFWRRRLRG-AEPTALPTDRPRPAGFPYPGADLRFELDAELVAALRELAKRARSSLFMVLLAAYCV 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 87 LLSRYTDKDDVVIGMPVFKQGQ---EETV-FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLD 162
Cdd:cd19539 258 LLRRYTGQTDIVVGTPVAGRNHprfESTVgFFVNLLPLRVDVSDCATFRDLIARVRKALVDAQRHQELPFQQLVAELPVD 337
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 163 GESNNLPLL-------NTIVMLDDIHCYES-------TDKINSDMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLY 228
Cdd:cd19539 338 RDAGRHPLVqivfqvtNAPAGELELAGGLSytegsdiPDGAKFDLNLTVTEEGTGLRGSLGYATSLFDEETIQGFLADYL 417
|
250
....*....|
gi 446807313 229 NILDILMKDP 238
Cdd:cd19539 418 QVLRQLLANP 427
|
|
| PRK13382 |
PRK13382 |
bile acid CoA ligase; |
1329-1813 |
6.92e-11 |
|
bile acid CoA ligase;
Pssm-ID: 172019 [Multi-domain] Cd Length: 537 Bit Score: 67.48 E-value: 6.92e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1329 KRNPNQIAVVcNEKGI-TYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRV 1407
Cdd:PRK13382 54 QRCPDRPGLI-DELGTlTWRELDERSDALAAALQALPIGEPRVVGIMCRNHRGFVEALLAANRIGADILLLNTSFAGPAL 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1408 EYMLTDSGCSHVLVHQnsiikgiEFqgnvIDLMDMSFEEEPG---------EDMHMMIE--------------PHNLAYV 1464
Cdd:PRK13382 133 AEVVTREGVDTVIYDE-------EF----SATVDRALADCPQatrivawtdEDHDLTVEvliaahagqrpeptGRKGRVI 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1465 IYTSGSTGQPKGVmieHRSLtnflcamyedfSQDIGITDNVLFSSSISFDVTIFEI--------FVPLIYGARM--TIYQ 1534
Cdd:PRK13382 202 LLTSGTTGTPKGA---RRSG-----------PGGIGTLKAILDRTPWRAEEPTVIVapmfhawgFSQLVLAASLacTIVT 267
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1535 GEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYF--VRDNQKIVLNKLLVGV-EPIKTELLAKYDHLFrGNLqILNGYG 1611
Cdd:PRK13382 268 RRRFDPEATLDLIDRHRATGLAVVPVMFDRIMDLPaeVRNRYSGRSLRFAAASgSRMRPDVVIAFMDQF-GDV-IYNNYN 345
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1612 PTEATVCCTSYRYESNKEITTQnvpiGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYINRKeltadkfiDHPF 1691
Cdd:PRK13382 346 ATEAGMIATATPADLRAAPDTA----GRPAEGTEIRILDQDFREVPTGEVGTIFVRNDTQFDGYTSGS--------TKDF 413
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1692 ERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDI 1771
Cdd:PRK13382 414 HDG--FMASGDVGYLDENGRLFVVGRDDEMIVSGGENVYPIEVEKTLATHPDVAEAAVIGVDDEQYGQRLAAFVVLKPGA 491
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446807313 1772 P-IPE-----VRAYLAtklpHYMIPQQLIPIHNIPLTQNGKIDRSKLP 1813
Cdd:PRK13382 492 SaTPEtlkqhVRDNLA----NYKVPRDIVVLDELPRGATGKILRRELQ 535
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
293-772 |
7.13e-11 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 67.03 E-value: 7.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 293 AIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSG 372
Cdd:PRK12406 4 TIISGDRRRSFDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 373 cSHVLTYQNSIIKGVAFQ-GSVINLMDIPFEEEQVEDLQI----------------------------TMEPQNLayvIY 423
Cdd:PRK12406 84 -ARVLIAHADLLHGLASAlPAGVTVLSVPTPPEIAAAYRIspalltppagaidwegwlaqqepydgppVPQPQSM---IY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 424 TSGSTGQPKGV-----MIEHRSLTNFLCAMYEDFSQDIG--ITDNVLFSSSISFDVTIFEIFVPLVCGARmtiyqgekFD 496
Cdd:PRK12406 160 TSGTTGHPKGVrraapTPEQAAAAEQMRALIYGLKPGIRalLTGPLYHSAPNAYGLRAGRLGGVLVLQPR--------FD 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 497 VPKLVQVILEEQVTLAYIPPTLLNEIYDY--FVRANQKIS-LNKLFVGVEP----IKTELLAKYDHLfrgnlqILNLYGP 569
Cdd:PRK12406 232 PEELLQLIERHRITHMHMVPTMFIRLLKLpeEVRAKYDVSsLRHVIHAAAPcpadVKRAMIEWWGPV------IYEYYGS 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 570 TE--ATVCCTSYQYERdKEITtqnvpIGSPLLNTKIYILDSFHRLQPIGVPGEICISGIGLAR-GYINRKELTADkfidh 646
Cdd:PRK12406 306 TEsgAVTFATSEDALS-HPGT-----VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKPEKRAE----- 374
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 647 pFERGEkLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEK 726
Cdd:PRK12406 375 -IDRGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDAEFGEALMAVVEPQP 452
|
490 500 510 520
....*....|....*....|....*....|....*....|....*...
gi 446807313 727 DIPIPE--VRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQP 772
Cdd:PRK12406 453 GATLDEadIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRLRDP 500
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
313-786 |
7.19e-11 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 67.52 E-value: 7.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 313 LARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPID----TELPKQRVEY----ML-TDSGCSH-VLTYQNS 382
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNyrwsFEEAKSAMLLvrpvMLvTDETCSSwYEELQND 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 383 IIKGVAFQgsviNLMDIPFEEEQVEDLQI-TME-----------------PQNLAYVIYTSGSTGQPKGVMIEHRSLTNF 444
Cdd:PLN02860 125 RLPSLMWQ----VFLESPSSSVFIFLNSFlTTEmlkqralgtteldyawaPDDAVLICFTSGTTGRPKGVTISHSALIVQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 445 LCAmyedfsqDIGI----TDNVLFSSS-------ISFDVTIF-----EIFVPlvcgarmtiyqgeKFDVPKLVQVILEEQ 508
Cdd:PLN02860 201 SLA-------KIAIvgygEDDVYLHTAplchiggLSSALAMLmvgacHVLLP-------------KFDAKAALQAIKQHN 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 509 VTLAYIPPTLLNEIydyfVRANQKI-------SLNKLFVGVEPIKTELLAKYDHLFrGNLQILNLYGPTEAtvcCTSYQY 581
Cdd:PLN02860 261 VTSMITVPAMMADL----ISLTRKSmtwkvfpSVRKILNGGGSLSSRLLPDAKKLF-PNAKLFSAYGMTEA---CSSLTF 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 582 ERDKEITTQNvPIGSPLLNTKIYiLDSFHRLQP--IGVPG---EICISGIGLAR-GYI-NRKELTADKFIDHPFERGEKL 654
Cdd:PLN02860 333 MTLHDPTLES-PKQTLQTVNQTK-SSSVHQPQGvcVGKPAphvELKIGLDESSRvGRIlTRGPHVMLGYWGQNSETASVL 410
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 655 YK-----TGDIArWLPD-GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI--------------------- 707
Cdd:PLN02860 411 SNdgwldTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVgvpdsrltemvvacvrlrdgw 489
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 708 QREDESGEKYLCAYVVTEKDIpipevRAYLATK-LPYYMIPQQIISIQN-IPLTQNGKIDRKKLPQPInnlkSSHLEPTN 785
Cdd:PLN02860 490 IWSDNEKENAKKNLTLSSETL-----RHHCREKnLSRFKIPKLFVQWRKpFPLTTTGKIRRDEVRREV----LSHLQSLP 560
|
.
gi 446807313 786 S 786
Cdd:PLN02860 561 S 561
|
|
| PRK06018 |
PRK06018 |
putative acyl-CoA synthetase; Provisional |
1318-1812 |
7.20e-11 |
|
putative acyl-CoA synthetase; Provisional
Pssm-ID: 235673 [Multi-domain] Cd Length: 542 Bit Score: 67.08 E-value: 7.20e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1318 LLVHKMFEEQVKRNPNQIAVVCNEKG----ITYNELNIKANQLARRLLDQGVKRESIVGVM---MKRSIEMVIGILGVlk 1390
Cdd:PRK06018 10 LLCHRIIDHAARIHGNREVVTRSVEGpivrTTYAQIHDRALKVSQALDRDGIKLGDRVATIawnTWRHLEAWYGIMGI-- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1391 agGA-------------------------------YLPIDTDLPKQ--RVEYMLTDSGCSHVlvHQNSIIKGIEFQGNVi 1437
Cdd:PRK06018 88 --GAichtvnprlfpeqiawiinhaedrvvitdltFVPILEKIADKlpSVERYVVLTDAAHM--PQTTLKNAVAYEEWI- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1438 dlmdmsfEEEPGEDMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSltNFLCAMYEDFSQDIGITdnvlfSSSISFDVti 1517
Cdd:PRK06018 163 -------AEADGDFAWKTFDENTAAGMCYTSGTTGDPKGVLYSHRS--NVLHALMANNGDALGTS-----AADTMLPV-- 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 feifVPLIY-------------GARMtIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYFVRDNQKI-VLNKLLV 1583
Cdd:PRK06018 227 ----VPLFHanswgiafsapsmGTKL-VMPGAKLDGASVYELLDTEKVTFTAGVPTVWLMLLQYMEKEGLKLpHLKMVVC 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1584 GVEPIKTELLAKYDHLfrgNLQILNGYGPTE----ATVCCTSYRYE--SNKEITTQNVPIGSPLLNTKIYILDSFHRIQP 1657
Cdd:PRK06018 302 GGSAMPRSMIKAFEDM---GVEVRHAWGMTEmsplGTLAALKPPFSklPGDARLDVLQKQGYPPFGVEMKITDDAGKELP 378
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1658 IG--VPGEICISGIGLARGY--INRKELTADKFIDhpfergeklykTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGE 1733
Cdd:PRK06018 379 WDgkTFGRLKVRGPAVAAAYyrVDGEILDDDGFFD-----------TGDVATIDAYGYMRITDRSKDVIKSGGEWISSID 447
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1734 IEASLLKYETIKTAVVIDQ-EDEAGEKYLCAYVVTEKDIPIP-EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSK 1811
Cdd:PRK06018 448 LENLAVGHPKVAEAAVIGVyHPKWDERPLLIVQLKPGETATReEILKYMDGKIAKWWMPDDVAFVDAIPHTATGKILKTA 527
|
.
gi 446807313 1812 L 1812
Cdd:PRK06018 528 L 528
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
285-769 |
7.78e-11 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 67.02 E-value: 7.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 285 VKQNPNQIAIVC--NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQ 362
Cdd:PRK13391 7 AQTTPDKPAVIMasTGEVVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVNSHLTPA 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 363 RVEYMLTDSGCSHVLTY--QNSIIKGVAFQGSVINL---MDIPFEEEQVEDLQ----------ITMEPQNLAyVIYTSGS 427
Cdd:PRK13391 87 EAAYIVDDSGARALITSaaKLDVARALLKQCPGVRHrlvLDGDGELEGFVGYAeavaglpatpIADESLGTD-MLYSSGT 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 428 TGQPKGVM--------IEHRSLTNFLCAMYedfsqdiGITDNVLFSSSISFDVTIFEIFVPLVCGARMTIYQGEKFDVPK 499
Cdd:PRK13391 166 TGRPKGIKrplpeqppDTPLPLTAFLQRLW-------GFRSDMVYLSPAPLYHSAPQRAVMLVIRLGGTVIVMEHFDAEQ 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 500 LVQVILEEQVTLAYIPPTLlneiydyFVR-------ANQKISLNKLFVGVEP-------IKTELLAKYDHLfrgnlqILN 565
Cdd:PRK13391 239 YLALIEEYGVTHTQLVPTM-------FSRmlklpeeVRDKYDLSSLEVAIHAaapcppqVKEQMIDWWGPI------IHE 305
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 566 LYGPTEA--TVCCTSYQYERDKEittqnvPIGSPLLNtKIYILDSFHRLQPIGVPGEICISGiGLARGYINRKELTADKF 643
Cdd:PRK13391 306 YYAATEGlgFTACDSEEWLAHPG------TVGRAMFG-DLHILDDDGAELPPGEPGTIWFEG-GRPFEYLNDPAKTAEAR 377
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 644 IDHPfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKylCAYV 722
Cdd:PRK13391 378 HPDG-----TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAVFGVPNEDlGEE--VKAV 450
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 446807313 723 VTEKDIPIP------EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK13391 451 VQPVDGVDPgpalaaELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK05852 |
PRK05852 |
fatty acid--CoA ligase family protein; |
1323-1809 |
8.14e-11 |
|
fatty acid--CoA ligase family protein;
Pssm-ID: 235625 [Multi-domain] Cd Length: 534 Bit Score: 67.22 E-value: 8.14e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQVKRNPNQIAVVC--NEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDT 1400
Cdd:PRK05852 21 LVEVAATRLPEAPALVVtaDRIAISYRDLARLVDDLAGQLTRSGLLPGDRVALRMGSNAEFVVALLAASRADLVVVPLDP 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1401 DLPKQRVEYMLTDSGCSHVLVHQNSI----------------IKGIEFQGNVIDLMDMSFEEEPgedMHMMIEPHNL--- 1461
Cdd:PRK05852 101 ALPIAEQRVRSQAAGARVVLIDADGPhdraepttrwwpltvnVGGDSGPSGGTLSVHLDAATEP---TPATSTPEGLrpd 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1462 -AYVIYTSGSTGQPKGVMIEHRSLT---NFLCAMYEDFSQDIGITD----------NVLFSSSISFDVTIF--------E 1519
Cdd:PRK05852 178 dAMIMFTGGTTGLPKMVPWTHANIAssvRAIITGYRLSPRDATVAVmplyhghgliAALLATLASGGAVLLpargrfsaH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1520 IFVPLIYGARMTIYQGekfdVTKLVQVILEEQVTLSY--IPPTLlneiydYFVRDNQKIVLNKllvGVEPIKTELLAKyd 1597
Cdd:PRK05852 258 TFWDDIKAVGATWYTA----VPTIHQILLERAATEPSgrKPAAL------RFIRSCSAPLTAE---TAQALQTEFAAP-- 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1598 hlfrgnlqILNGYGPTEATVCCTSYRYESNKEITTQNVPIGSPLLNT--KIYILDSFHRIQPIGVPGEICISGIGLARGY 1675
Cdd:PRK05852 323 --------VVCAFGMTEATHQVTTTQIEGIGQTENPVVSTGLVGRSTgaQIRIVGSDGLPLPAGAVGEVWLRGTTVVRGY 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1676 INRKELTADKFIDHPFergeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE 1755
Cdd:PRK05852 395 LGDPTITAANFTDGWL-------RTGDLGSLSAAGDLSIRGRIKELINRGGEKISPERVEGVLASHPNVMEAAVFGVPDQ 467
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1756 A-GEKYLCAYVVTEKDIPIP-EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:PRK05852 468 LyGEAVAAVIVPRESAPPTAeELVQFCRERLAAFEIPASFQEASGLPHTAKGSLDR 523
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
1346-1811 |
8.23e-11 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 67.34 E-value: 8.23e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1346 YNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGG--AYLPIDTDLpKQRVEY------MLTDSGCS 1417
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLvpVPLPLPMGF-GGRESYiaqlrgMLASAQPA 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1418 HVLVHQ------NSIIKGiefQGNVIDLMDMSFEEEPGEDMHM-MIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFL-- 1488
Cdd:PRK09192 131 AIITPDellpwvNEATHG---NPLLHVLSHAWFKALPEADVALpRPTPDDIAYLQYSSGSTRFPRGVIITHRALMANLra 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1489 -------------CAMYEDFSQDIGITDNVL--FSSSISFDVTIFEIFV--PLIYgarmtiyqgekfdvtklVQVILEEQ 1551
Cdd:PRK09192 208 ishdglkvrpgdrCVSWLPFYHDMGLVGFLLtpVATQLSVDYLPTRDFArrPLQW-----------------LDLISRNR 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1552 VTLSYIPPTLlneiYDYFVRDNQKIVLNKL-L-------VGVEPIKTELLAKYDHLFRGN----LQILNGYGPTEATVCC 1619
Cdd:PRK09192 271 GTISYSPPFG----YELCARRVNSKDLAELdLscwrvagIGADMIRPDVLHQFAEAFAPAgfddKAFMPSYGLAEATLAV 346
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1620 T-----------------------SYRYESNKEITTQNVPIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLARGYI 1676
Cdd:PRK09192 347 SfsplgsgivveevdrdrleyqgkAVAPGAETRRVRTFVNCGKALPGHEIEIRNEAGMPLPERVVGHICVRGPSLMSGYF 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1677 NRKE----LTADKFIDhpfergeklykTGDIArWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKT----AV 1748
Cdd:PRK09192 427 RDEEsqdvLAADGWLD-----------TGDLG-YLLDGYLYITGRAKDLIIINGRNIWPQDIEWIAEQEPELRSgdaaAF 494
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1749 VIDQEDeaGEKYLcayVVTEKDIPIPEVRAYLATKLPHYMIPQ-------QLIPIHNIPLTQNGKIDRSK 1811
Cdd:PRK09192 495 SIAQEN--GEKIV---LLVQCRISDEERRGQLIHALAALVRSEfgveaavELVPPHSLPRTSSGKLSRAK 559
|
|
| ACSBG_like |
cd05933 |
Bubblegum-like very long-chain fatty acid CoA synthetase (VL-FACS); This family of very ... |
301-675 |
1.07e-10 |
|
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: 67.00 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 301 ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSgCSHVLTYQ 380
Cdd:cd05933 9 LTYKEYYEACRQAAKAFLKLGLERFHGVGILGFNSPEWFIAAVGAIFAGGIAVGIYTTNSPEACQYVAETS-EANILVVE 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 381 N-------SIIKG--------VAFQGSV----INL------MDIPFE--EEQVEDLQITMEPQNLAYVIYTSGSTGQPKG 433
Cdd:cd05933 88 NqkqlqkiLQIQDklphlkaiIQYKEPLkekePNLyswdefMELGRSipDEQLDAIISSQKPNQCCTLIYTSGTTGMPKG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 434 VMIEHRSLTNFLCAMyedfSQDIGITDN-VLFSSSISF------DVTIFEIFVPLVCGA--------------------- 485
Cdd:cd05933 168 VMLSHDNITWTAKAA----SQHMDLRPAtVGQESVVSYlplshiAAQILDIWLPIKVGGqvyfaqpdalkgtlvktlrev 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 486 RMTIYQG-----EKFDvPKLVQVI------------------LEEQVTL--AYIPPTLLNEIYDYFV--RANQKISLN-- 536
Cdd:cd05933 244 RPTAFMGvprvwEKIQ-EKMKAVGaksgtlkrkiaswakgvgLETNLKLmgGESPSPLFYRLAKKLVfkKVRKALGLDrc 322
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 537 -KLFVGVEPIKTELLakydHLFRG-NLQILNLYGPTEATVCCTSYQyerdkeitTQNVPIGS-----PLLNTKIYILDSf 609
Cdd:cd05933 323 qKFFTGAAPISRETL----EFFLSlNIPIMELYGMSETSGPHTISN--------PQAYRLLScgkalPGCKTKIHNPDA- 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 610 hrlqpIGVpGEICISGIGLARGYINRKELTADKFIDHPFERgeklykTGDIARWLPDGNIEYLGRV 675
Cdd:cd05933 390 -----DGI-GEICFWGRHVFMGYLNMEDKTEEAIDEDGWLH------SGDLGKLDEDGFLYITGRI 443
|
|
| PLN02860 |
PLN02860 |
o-succinylbenzoate-CoA ligase |
1356-1809 |
2.10e-10 |
|
o-succinylbenzoate-CoA ligase
Pssm-ID: 215464 [Multi-domain] Cd Length: 563 Bit Score: 65.98 E-value: 2.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1356 LARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID----TDLPKQRVEY----ML-TDSGCS--------- 1417
Cdd:PLN02860 45 LAAGLLRLGLRNGDVVAIAALNSDLYLEWLLAVACAGGIVAPLNyrwsFEEAKSAMLLvrpvMLvTDETCSswyeelqnd 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1418 -------HVLVHQNSIIKGIEFqgNVIDLMDMSFEEEPGE-DMHMMIEPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLC 1489
Cdd:PLN02860 125 rlpslmwQVFLESPSSSVFIFL--NSFLTTEMLKQRALGTtELDYAWAPDDAVLICFTSGTTGRPKGVTISHSALIVQSL 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1490 AmyedfsqDIGI----TDNVLFSSS-------ISFDVTIF-----EIFVPliygarmtiyqgeKFDVTKLVQVILEEQVT 1553
Cdd:PLN02860 203 A-------KIAIvgygEDDVYLHTAplchiggLSSALAMLmvgacHVLLP-------------KFDAKAALQAIKQHNVT 262
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1554 LSYIPPTLLNEIYDY----FVRDNQKIVLnKLLVGVEPIKTELLAKYDHLFrGNLQILNGYGPTEAtvcCTSYRYesnke 1629
Cdd:PLN02860 263 SMITVPAMMADLISLtrksMTWKVFPSVR-KILNGGGSLSSRLLPDAKKLF-PNAKLFSAYGMTEA---CSSLTF----- 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1630 ittqnVPIGSPLLNTKIYILDSFHRI--QPIGVPGEICIS--------GIGLAR----GYI-NRKELTADKFIDHPFERG 1694
Cdd:PLN02860 333 -----MTLHDPTLESPKQTLQTVNQTksSSVHQPQGVCVGkpaphvelKIGLDEssrvGRIlTRGPHVMLGYWGQNSETA 407
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1695 EKLYK-----TGDIArWLPD-GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI------------------ 1750
Cdd:PLN02860 408 SVLSNdgwldTGDIG-WIDKaGNLWLIGRSNDRIKTGGENVYPEEVEAVLSQHPGVASVVVVgvpdsrltemvvacvrlr 486
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446807313 1751 --------DQEDEAGEKYLCAyvvtekdipiPEVRAYLATK-LPHYMIPQQLI----PihnIPLTQNGKIDR 1809
Cdd:PLN02860 487 dgwiwsdnEKENAKKNLTLSS----------ETLRHHCREKnLSRFKIPKLFVqwrkP---FPLTTTGKIRR 545
|
|
| PRK13390 |
PRK13390 |
acyl-CoA synthetase; Provisional |
289-769 |
2.26e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 139538 [Multi-domain] Cd Length: 501 Bit Score: 65.42 E-value: 2.26e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVC--NGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEY 366
Cdd:PRK13390 11 PDRPAVIVaeTGEQVSYRQLDDDSAALARVLYDAGLRTGDVVALLSDNSPEALVVLWAALRSGLYITAINHHLTAPEADY 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 367 MLTDSGCSHVLTyqNSIIKGVAFQGSVINLMDIPF--EEEQVEDLQITM--------EPQNLAYVIYTSGSTGQPKGVM- 435
Cdd:PRK13390 91 IVGDSGARVLVA--SAALDGLAAKVGADLPLRLSFggEIDGFGSFEAALagagprltEQPCGAVMLYSSGTTGFPKGIQp 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 436 -IEHRSLT---NFLCAMYEDFsqdIGITD-NVLFSSSISFDVTIFEiFVPLVCGARMTIYQGEKFDVPKLVQVILEEQVT 510
Cdd:PRK13390 169 dLPGRDVDapgDPIVAIARAF---YDISEsDIYYSSAPIYHAAPLR-WCSMVHALGGTVVLAKRFDAQATLGHVERYRIT 244
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 511 LAYIPPTLLNEI--YDYFVRANQKI-SLNKLFVGVEPIKTEL-LAKYDHLfrGNLqILNLYGPTEA---TVCCTSyqyer 583
Cdd:PRK13390 245 VTQMVPTMFVRLlkLDADVRTRYDVsSLRAVIHAAAPCPVDVkHAMIDWL--GPI-VYEYYSSTEAhgmTFIDSP----- 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 584 dkEITTQNVPIGSPLLNTkIYILDSFHRLQPIGVPGEICISGIGLARGYINRKELTAD-KFIDHPFergekLYKTGDIAR 662
Cdd:PRK13390 317 --DWLAHPGSVGRSVLGD-LHICDDDGNELPAGRIGTVYFERDRLPFRYLNDPEKTAAaQHPAHPF-----WTTVGDLGS 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 663 WLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQRED-ESGEKYLCAYVVTEKDIPIPEVRA----YL 737
Cdd:PRK13390 389 VDEDGYLYLADRKSFMIISGGVNIYPQETENALTMHPAVHDVAVIGVPDpEMGEQVKAVIQLVEGIRGSDELARelidYT 468
|
490 500 510
....*....|....*....|....*....|..
gi 446807313 738 ATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK13390 469 RSRIAHYKAPRSVEFVDELPRTPTGKLVKGLL 500
|
|
| hsFATP4_like |
cd05939 |
Fatty acid transport proteins (FATP), including FATP4 and FATP1, and similar proteins; Fatty ... |
298-769 |
2.62e-10 |
|
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: 65.14 E-value: 2.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 298 GKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVL 377
Cdd:cd05939 1 DRHWTFRELNEYSNKVANFFQAQGYRSGDVVALFMENRLEFVALWLGLAKIGVETALINSNLRLESLLHCITVSKAKALI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 378 TYQNSIIKgvafqgsvinlmdipfeeEQVEDLQITMEPQN----LAYvIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDF- 452
Cdd:cd05939 81 FNLLDPLL------------------TQSSTEPPSQDDVNfrdkLFY-IYTSGTTGLPKAAVIVHSRYYRIAAGAYYAFg 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 453 --SQDIGITDNVLFSSSISfdvtIFEIFVPLVCGarMTIYQGEKFDVPKLVQVILEEQVTLA-YIpptllNEIYDYFVRA 529
Cdd:cd05939 142 mrPEDVVYDCLPLYHSAGG----IMGVGQALLHG--STVVIRKKFSASNFWDDCVKYNCTIVqYI-----GEICRYLLAQ 210
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 530 NQKISLNKLFV------GVEP-IKTELLAKYdhlfrGNLQILNLYGPTEatvcCTSYQYERDKEITTqnvpIG-SPLLNT 601
Cdd:cd05939 211 PPSEEEQKHNVrlavgnGLRPqIWEQFVRRF-----GIPQIGEFYGATE----GNSSLVNIDNHVGA----CGfNSRILP 277
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 602 KIY--------------ILDSFHRLQPIGvPGEiciSGIGLAR-----------GYINRKElTADKFIDHPFERGEKLYK 656
Cdd:cd05939 278 SVYpirlikvdedtgelIRDSDGLCIPCQ-PGE---PGLLVGKiiqndplrrfdGYVNEGA-TNKKIARDVFKKGDSAFL 352
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 657 TGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVI-----QREDESGekyLCAYVVTEKDIPIP 731
Cdd:cd05939 353 SGDVLVMDELGYLYFKDRTGDTFRWKGENVSTTEVEGILSNVLGLEDVVVYgvevpGVEGRAG---MAAIVDPERKVDLD 429
|
490 500 510
....*....|....*....|....*....|....*...
gi 446807313 732 EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05939 430 RFSAVLAKSLPPYARPQFIRLLPEVDKTGTFKLQKTDL 467
|
|
| PP-binding |
pfam00550 |
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached ... |
1834-1891 |
2.80e-10 |
|
Phosphopantetheine attachment site; A 4'-phosphopantetheine prosthetic group is attached through a serine. This prosthetic group acts as a a 'swinging arm' for the attachment of activated fatty acid and amino-acid groups. This domain forms a four helix bundle. This family includes members not included in Prosite. The inclusion of these members is supported by sequence analysis and functional evidence. The related domain of Swiss:P19828 has the attachment serine replaced by an alanine.
Pssm-ID: 425746 [Multi-domain] Cd Length: 62 Bit Score: 57.96 E-value: 2.80e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1834 LIDIWSSILGVNN--IGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQ 1891
Cdd:pfam00550 3 LRELLAEVLGVPAeeIDPDTDLFDLGLDSLLAVELIARLEEEFGVEIPPSDLFEHPTLAE 62
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
1344-1785 |
4.70e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 64.45 E-value: 4.70e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQGVKResiVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGCSHVLVHQ 1423
Cdd:PRK06334 46 LSYNQVRKAVIALATKVSKYPDQH---IGIMMPASAGAYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSK 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1424 NSIIKGIEFQGNVI----DLMDM-------SFEEEPGEDMHMMI--------------EPHNLAYVIYTSGSTGQPKGVM 1478
Cdd:PRK06334 123 QLMQHLAQTHGEDAeypfSLIYMeevrkelSFWEKCRIGIYMSIpfewlmrwfgvsdkDPEDVAVILFTSGTEKLPKGVP 202
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1479 IEHRSLTNFLCAMYEDFSQdigITDNVLFSSSISFDVTIFE--IFVPLIYGARMtIYQGEKFDVTKLVQVILEEQVTLSY 1556
Cdd:PRK06334 203 LTHANLLANQRACLKFFSP---KEDDVMMSFLPPFHAYGFNscTLFPLLSGVPV-VFAYNPLYPKKIVEMIDEAKVTFLG 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1557 IPPTLLNEIYDYFVRDNQKI-VLNKLLVGVEPIKTELLAKYDHLFRgNLQILNGYGPTEATVCCTsyryesnkeITTQNV 1635
Cdd:PRK06334 279 STPVFFDYILKTAKKQESCLpSLRFVVIGGDAFKDSLYQEALKTFP-HIQLRQGYGTTECSPVIT---------INTVNS 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1636 P-----IGSPLLNTKIYIL-DSFHRIQPIGVPGEICISGIGLARGYINRKEltadkfiDHPFER--GEKLYKTGDIARWL 1707
Cdd:PRK06334 349 PkhescVGMPIRGMDVLIVsEETKVPVSSGETGLVLTRGTSLFSGYLGEDF-------GQGFVElgGETWYVTGDLGYVD 421
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1708 PDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETiktavvIDQEDEAGEKYLCAyvvtekdIPIPEVRAYLATKLP 1785
Cdd:PRK06334 422 RHGELFLKGRLSRFVKIGAEMVSLEALESILMEGFG------QNAADHAGPLVVCG-------LPGEKVRLCLFTTFP 486
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
420-769 |
6.43e-10 |
|
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: 63.94 E-value: 6.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 420 YVIYTSGSTGQPKGVM--IEHRSLTNFLCAMYEDFSQDIGitDNVLFSSsisfdvtifeifVPLVCGA-----RMTIYQG 492
Cdd:cd05929 129 KMLYSGGTTGRPKGIKrgLPGGPPDNDTLMAAALGFGPGA--DSVYLSP------------APLYHAApfrwsMTALFMG 194
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 493 ------EKFDVPKLVQVILEEQVTLAYIPPTLLNEI----------YDYfvranqkISLNKLFVGVEPIKTELLAKYDHL 556
Cdd:cd05929 195 gtlvlmEKFDPEEFLRLIERYRVTFAQFVPTMFVRLlklpeavrnaYDL-------SSLKRVIHAAAPCPPWVKEQWIDW 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 557 frGNLQILNLYGPTEAT--VCCTSYQYerdkeiTTQNVPIGSPLLNtKIYILDSFHRLQPIGVPGEICISGiGLARGYIN 634
Cdd:cd05929 268 --GGPIIWEYYGGTEGQglTIINGEEW------LTHPGSVGRAVLG-KVHILDEDGNEVPPGEIGEVYFAN-GPGFEYTN 337
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 635 RKELTADKFIDHPFErgeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESG 714
Cdd:cd05929 338 DPEKTAAARNEGGWS------TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAHPKVLDAAVVGVPDEEL 411
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 715 EKYLCAYVVTEKD-----IPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05929 412 GQRVHAVVQPAPGadagtALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| PRK12406 |
PRK12406 |
long-chain-fatty-acid--CoA ligase; Provisional |
1346-1812 |
7.84e-10 |
|
long-chain-fatty-acid--CoA ligase; Provisional
Pssm-ID: 183506 [Multi-domain] Cd Length: 509 Bit Score: 63.95 E-value: 7.84e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1346 YNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSGcSHVLVHQNS 1425
Cdd:PRK12406 14 FDELAQRAARAAGGLAALGVRPGDCVALLMRNDFAFFEAAYAAMRLGAYAVPVNWHFKPEEIAYILEDSG-ARVLIAHAD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1426 IIKGIEfqGNVIDLMDMSFEEEPGE--------DMHMMIEPHNLAY--------------------VIYTSGSTGQPKGV 1477
Cdd:PRK12406 93 LLHGLA--SALPAGVTVLSVPTPPEiaaayrisPALLTPPAGAIDWegwlaqqepydgppvpqpqsMIYTSGTTGHPKGV 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1478 miEHRSLTNFLCAMYEDFSQDI-GITDNV-------LFSSSisfdvtifeifvPLIYGaRMTIYQGE------KFDVTKL 1543
Cdd:PRK12406 171 --RRAAPTPEQAAAAEQMRALIyGLKPGIralltgpLYHSA------------PNAYG-LRAGRLGGvlvlqpRFDPEEL 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1544 VQVILEEQVTLSYIPPTLlneiydyFVRdnqkivLNKLlvgvepiKTELLAKYD-----HLFRGNLQ------------- 1605
Cdd:PRK12406 236 LQLIERHRITHMHMVPTM-------FIR------LLKL-------PEEVRAKYDvsslrHVIHAAAPcpadvkramieww 295
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1606 ---ILNGYGPTE--ATVCCTSYRYeSNKEITtqnvpIGSPLLNTKIYILDSFHRIQPIGVPGEICISGIGLAR-GYINRK 1679
Cdd:PRK12406 296 gpvIYEYYGSTEsgAVTFATSEDA-LSHPGT-----VGKAAPGAELRFVDEDGRPLPQGEIGEIYSRIAGNPDfTYHNKP 369
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1680 ELTADkfidhpFERGEkLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQED-EAGE 1758
Cdd:PRK12406 370 EKRAE------IDRGG-FITSGDVGYLDADGYLFLCDRKRDMVISGGVNIYPAEIEAVLHAVPGVHDCAVFGIPDaEFGE 442
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1759 KyLCAYVVTEKDIPIPE--VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK12406 443 A-LMAVVEPQPGATLDEadIRAQLKARLAGYKVPKHIEIMAELPREDSGKIFKRRL 497
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
1405-1738 |
7.88e-10 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 64.37 E-value: 7.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1405 QRVEYMLTDSGCSHVLVHQNSIIKGIEFqgnvidlmdmSFEEEPGEDMHM---MIEPHNLAYVIYTSGSTGQPKGVMIEH 1481
Cdd:PLN02387 203 KRVIYMDDEGVDSDSSLSGSSNWTVSSF----------SEVEKLGKENPVdpdLPSPNDIAVIMYTSGSTGLPKGVMMTH 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1482 RSLTNFLCAMYEDFSqDIGITD---------NVLfssSISFDVTIFEIFVPLIYGARMT-------IYQGEKFDVTKLvq 1545
Cdd:PLN02387 273 GNIVATVAGVMTVVP-KLGKNDvylaylplaHIL---ELAAESVMAAVGAAIGYGSPLTltdtsnkIKKGTKGDASAL-- 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1546 vileeQVTLSYIPPTLLNEIYDYfVRD--NQKIVLNKLLV-------------------GVEPIKTELLA--KYDHLFRG 1602
Cdd:PLN02387 347 -----KPTLMTAVPAILDRVRDG-VRKkvDAKGGLAKKLFdiaykrrlaaiegswfgawGLEKLLWDALVfkKIRAVLGG 420
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1603 NLQ------------------------ILNGYGPTEAtvcCTSYRYESNKEITTQNVpiGSPLLNTKIYILD---SFHRI 1655
Cdd:PLN02387 421 RIRfmlsggaplsgdtqrfiniclgapIGQGYGLTET---CAGATFSEWDDTSVGRV--GPPLPCCYVKLVSweeGGYLI 495
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1656 QPIGVP-GEICISGIGLARGYINRKELTADKF-IDhpfERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIR-GYRIELG 1732
Cdd:PLN02387 496 SDKPMPrGEIVIGGPSVTLGYFKNQEKTDEVYkVD---ERGMRWFYTGDIGQFHPDGCLEIIDRKKDIVKLQhGEYVSLG 572
|
....*.
gi 446807313 1733 EIEASL 1738
Cdd:PLN02387 573 KVEAAL 578
|
|
| PRK13391 |
PRK13391 |
acyl-CoA synthetase; Provisional |
1323-1812 |
8.77e-10 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 184022 [Multi-domain] Cd Length: 511 Bit Score: 63.56 E-value: 8.77e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1323 MFEEQ-VKRNPNQIAVVCNEKG--ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPID 1399
Cdd:PRK13391 1 MYPGIhAQTTPDKPAVIMASTGevVTYRELDERSNRLAHLFRSLGLKRGDHVAIFMENNLRYLEVCWAAERSGLYYTCVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1400 TDLPKQRVEYMLTDSG--------------------CSHV----LVHQNSIIKGIE-FQGNVIDLMDMSFEEEP-GEDMh 1453
Cdd:PRK13391 81 SHLTPAEAAYIVDDSGaralitsaakldvarallkqCPGVrhrlVLDGDGELEGFVgYAEAVAGLPATPIADESlGTDM- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1454 mmiephnlayvIYTSGSTGQPKGVM--------IEHRSLTNFLCAMYedfsqdiGITDNVLFSSSISFDVTIFEIFVPLI 1525
Cdd:PRK13391 160 -----------LYSSGTTGRPKGIKrplpeqppDTPLPLTAFLQRLW-------GFRSDMVYLSPAPLYHSAPQRAVMLV 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1526 YGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLlneiydyFVR-------DNQKIVLNKLLVGVEP-------IKTE 1591
Cdd:PRK13391 222 IRLGGTVIVMEHFDAEQYLALIEEYGVTHTQLVPTM-------FSRmlklpeeVRDKYDLSSLEVAIHAaapcppqVKEQ 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1592 LLAKYDHLfrgnlqILNGYGPTEA--TVCCTSYRYESNKEittqnvPIGSPLLNtKIYILDSFHRIQPIGVPGEICISGi 1669
Cdd:PRK13391 295 MIDWWGPI------IHEYYAATEGlgFTACDSEEWLAHPG------TVGRAMFG-DLHILDDDGAELPPGEPGTIWFEG- 360
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1670 GLARGYINRKELTADKFIDHPfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVV 1749
Cdd:PRK13391 361 GRPFEYLNDPAKTAEARHPDG-----TWSTVGDIGYVDEDGYLYLTDRAAFMIISGGVNIYPQEAENLLITHPKVADAAV 435
|
490 500 510 520 530 540 550
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1750 ID-QEDEAGEKylCAYVVTEKDIPIP------EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK13391 436 FGvPNEDLGEE--VKAVVQPVDGVDPgpalaaELIAFCRQRLSRQKCPRSIDFEDELPRLPTGKLYKRLL 503
|
|
| PRK06334 |
PRK06334 |
long chain fatty acid--[acyl-carrier-protein] ligase; Validated |
265-697 |
9.10e-10 |
|
long chain fatty acid--[acyl-carrier-protein] ligase; Validated
Pssm-ID: 180533 [Multi-domain] Cd Length: 539 Bit Score: 63.68 E-value: 9.10e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 265 RVHKTLLC-------ETVTAPQLFEEQVkqnpnqiaivcnGKeITYKQLNIKANQLARRLLDQGVKRefiVGVMMERSIE 337
Cdd:PRK06334 16 RSGKTVLEsflklcsEMTTATVCWDEQL------------GK-LSYNQVRKAVIALATKVSKYPDQH---IGIMMPASAG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 338 MIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSIIK-------GVAFQGSVINLMDIPFEEEQVEDLQ 410
Cdd:PRK06334 80 AYIAYFATLLSGKIPVMINWSQGLREVTACANLVGVTHVLTSKQLMQHlaqthgeDAEYPFSLIYMEEVRKELSFWEKCR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 411 ITM------------------EPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQdigITDNVLFSSSISFDV 472
Cdd:PRK06334 160 IGIymsipfewlmrwfgvsdkDPEDVAVILFTSGTEKLPKGVPLTHANLLANQRACLKFFSP---KEDDVMMSFLPPFHA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 473 TIFE--IFVPLVCGARMtIYQGEKFDVPKLVQVILEEQVTLAYIPPTLLneiyDYFVRANQKI-----SLNKLFVGVEPI 545
Cdd:PRK06334 237 YGFNscTLFPLLSGVPV-VFAYNPLYPKKIVEMIDEAKVTFLGSTPVFF----DYILKTAKKQesclpSLRFVVIGGDAF 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 546 KTELLAKYDHLFRgNLQILNLYGPTEATVCCTsyqyerdkeITTQNVP-----IGSPLLNTKIYIL-DSFHRLQPIGVPG 619
Cdd:PRK06334 312 KDSLYQEALKTFP-HIQLRQGYGTTECSPVIT---------INTVNSPkhescVGMPIRGMDVLIVsEETKVPVSSGETG 381
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 620 EICISGIGLARGYINRKEltadkfiDHPFER--GEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLK 697
Cdd:PRK06334 382 LVLTRGTSLFSGYLGEDF-------GQGFVElgGETWYVTGDLGYVDRHGELFLKGRLSRFVKIGAEMVSLEALESILME 454
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
690-763 |
9.64e-10 |
|
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: 56.78 E-value: 9.64e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 690 EIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP--EVRAYLATKLPYYMIPQQIISIQNIPLTQNGK 763
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLeeELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| DCL_NRPS |
cd19543 |
DCL-type Condensation domain of nonribosomal peptide synthetases (NRPSs), which catalyzes the ... |
20-238 |
1.01e-09 |
|
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: 62.99 E-value: 1.01e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 20 KEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKDDVVI 99
Cdd:cd19543 188 EAYWREYLAGFEEPTPLPKELPADADGSYEPGEVSFELSAELTARLQELARQHGVTLNTVVQGAWALLLSRYSGRDDVVF 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 100 GM-----PVFKQGQEETV--FQNNfLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGEsnnlpLLN 172
Cdd:cd19543 268 GTtvsgrPAELPGIETMVglFINT-LPVRVRLDPDQTVLELLKDLQAQQLELREHEYVPLYEIQAWSEGKQA-----LFD 341
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 173 TIVMLDD--IHCYESTDKINSDMVIRFMKNEEQ--------------LKVQVDYNSTLYSEGLVSRIVNHLYNILDILMK 236
Cdd:cd19543 342 HLLVFENypVDESLEEEQDEDGLRITDVSAEEQtnypltvvaipgeeLTIKLSYDAEVFDEATIERLLGHLRRVLEQVAA 421
|
..
gi 446807313 237 DP 238
Cdd:cd19543 422 NP 423
|
|
| PRK05620 |
PRK05620 |
long-chain fatty-acid--CoA ligase; |
1344-1812 |
2.07e-09 |
|
long-chain fatty-acid--CoA ligase;
Pssm-ID: 180167 [Multi-domain] Cd Length: 576 Bit Score: 62.49 E-value: 2.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1344 ITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYMLTDSG-----CS 1417
Cdd:PRK05620 39 TTFAAIGARAAALAHALHDElGITGDQRVGSMMYNCAEHLEVLFAVACMGAVFNPLNKQLMNDQIVHIINHAEdevivAD 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1418 HVLVHQ-NSIIKGIEFQGNVIDLMDMSFEEEPGEDMHMM--------------------IEPHNLAYVIYTSGSTGQPKG 1476
Cdd:PRK05620 119 PRLAEQlGEILKECPCVRAVVFIGPSDADSAAAHMPEGIkvysyealldgrstvydwpeLDETTAAAICYSTGTTGAPKG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1477 VMIEHRSLtnFLCAMYEDFSQDIGITDNVLFSSSisfdVTIFEIF---VPLiyGARMT----IYQGEKFDVTKLVQVILE 1549
Cdd:PRK05620 199 VVYSHRSL--YLQSLSLRTTDSLAVTHGESFLCC----VPIYHVLswgVPL--AAFMSgtplVFPGPDLSAPTLAKIIAT 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1550 EQVTLSYIPPTLLNEIYDYFVRDN-QKIVLNKLLVGVEPIKTELLAKYDHlfRGNLQILNGYGPTEATVCCTSYRYES-- 1626
Cdd:PRK05620 271 AMPRVAHGVPTLWIQLMVHYLKNPpERMSLQEIYVGGSAVPPILIKAWEE--RYGVDVVHVWGMTETSPVGTVARPPSgv 348
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1627 ------NKEITTQNVPIGsplLNTKI----YILDSFHRIQpigvpGEICISGIGLARGYIN----RKELTADKFIDHPFE 1692
Cdd:PRK05620 349 sgearwAYRVSQGRFPAS---LEYRIvndgQVMESTDRNE-----GEIQVRGNWVTASYYHspteEGGGAASTFRGEDVE 420
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1693 RGEKLY------KTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLCAYV 1765
Cdd:PRK05620 421 DANDRFtadgwlRTGDVGSVTRDGFLTIHDRARDVIRSGGEWIYSAQLENYIMAAPEVVECAVIGYPDDKwGERPLAVTV 500
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|.
gi 446807313 1766 VTEKDIPIPE----VRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:PRK05620 501 LAPGIEPTREtaerLRDQLRDRLPNWMLPEYWTFVDEIDKTSVGKFDKKDL 551
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
1444-1805 |
2.48e-09 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 62.47 E-value: 2.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1444 FEEEPGEDmhmmiephNLAYVIYTSGSTGQPKGVMIEHRSLTNF--LCAMYEDFSQDIGITDN-----------VLF--- 1507
Cdd:cd17632 216 FRPEPDDD--------PLALLIYTSGSTGTPKGAMYTERLVATFwlKVSSIQDIRPPASITLNfmpmshiagriSLYgtl 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1508 ----------SSSISfdvTIFE----------IFVPLIYGARMTIYQGE--KFDVTKLVQVILEEQVTLSyipptllnei 1565
Cdd:cd17632 288 arggtayfaaASDMS---TLFDdlalvrptelFLVPRVCDMLFQRYQAEldRRSVAGADAETLAERVKAE---------- 354
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1566 ydyfVRDNqkiVLNKLL----VGVEPIKTELLAKYDHLFrgNLQILNGYGPTEATVcctsyryesnkeITTQNVPIGSPL 1641
Cdd:cd17632 355 ----LRER---VLGGRLlaavCGSAPLSAEMKAFMESLL--DLDLHDGYGSTEAGA------------VILDGVIVRPPV 413
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1642 LNTKI-------YIL-DSFHriqpigvP-GEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDI-ARWLPDgN 1711
Cdd:cd17632 414 LDYKLvdvpelgYFRtDRPH-------PrGELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVmAELGPD-R 479
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1712 IEYLGRVDHQVKI-RGYRIELGEIEASLLKYETIKTAVVIDQEDEAgekYLCAYVVTEKD----IPIPEVRAYLATKLPH 1786
Cdd:cd17632 480 LVYVDRRNNVLKLsQGEFVTVARLEAVFAASPLVRQIFVYGNSERA---YLLAVVVPTQDalagEDTARLRAALAESLQR 556
|
410 420
....*....|....*....|....*....
gi 446807313 1787 ---------YMIPQQLIpIHNIPLTQ-NG 1805
Cdd:cd17632 557 iareaglqsYEIPRDFL-IETEPFTIaNG 584
|
|
| C_NRPS-like |
cd19066 |
Condensation domain of nonribosomal peptide synthetases (NRPSs); Condensation (C) domains of ... |
7-238 |
2.84e-09 |
|
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: 61.66 E-value: 2.84e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 7 QQVLLSSEKFKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKY 86
Cdd:cd19066 177 LEKQLESEAAQADLAYWTSYLHGLPPPLPLPKAKRPSQVASYEVLTLEFFLRSEETKRLREVARESGTTPTQLLLAAFAL 256
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 87 LLSRYTDKDDVVIGMPVFKQ---GQEETV-FQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLS-- 160
Cdd:cd19066 257 ALKRLTASIDVVIGLTFLNRpdeAVEDTIgLFLNLLPLRIDTSPDATFPELLKRTKEQSREAIEHQRVPFIELVRHLGvv 336
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 161 ------------LDGESNNLPLLNTIVMLDDIHCYESTDKINSDMVIRFMKNEE-QLKVQVDYNSTLYSEGLVSRIVNHL 227
Cdd:cd19066 337 peapkhplfepvFTFKNNQQQLGKTGGFIFTTPVYTSSEGTVFDLDLEASEDPDgDLLLRLEYSRGVYDERTIDRFAERY 416
|
250
....*....|.
gi 446807313 228 YNILDILMKDP 238
Cdd:cd19066 417 MTALRQLIENP 427
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
1462-1815 |
4.20e-09 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 60.83 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1462 AYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYedfsQDIGITDNVLFSSSiSFDVTIFEIFV-PLIYGARMTIYQ-GEKFD 1539
Cdd:PRK07824 38 ALVVATSGTTGTPKGAMLTAAALTASADATH----DRLGGPGQWLLALP-AHHIAGLQVLVrSVIAGSEPVELDvSAGFD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1540 VTKLVQVILE---EQVTLSYIPPTLLNEIYDyfvrdnqkivlnkllvgvePIKTELLAKYDhlfrgnlQILNGYGPTEAT 1616
Cdd:PRK07824 113 PTALPRAVAElggGRRYTSLVPMQLAKALDD-------------------PAATAALAELD-------AVLVGGGPAPAP 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1617 VcctsyrYESNKE-----ITTQN--------VPIGSPLLNTKIYILDsfhriqpigvpGEICISGIGLARGYINrkelta 1683
Cdd:PRK07824 167 V------LDAAAAaginvVRTYGmsetsggcVYDGVPLDGVRVRVED-----------GRIALGGPTLAKGYRN------ 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1684 dkFIDHPFERGEKLYKTGDIARwLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEA-GEKYLC 1762
Cdd:PRK07824 224 --PVDPDPFAEPGWFRTDDLGA-LDDGVLTVLGRADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRlGQRVVA 300
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....
gi 446807313 1763 AYVVTEKDIPIP-EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK07824 301 AVVGDGGPAPTLeALRAHVARTLDRTAAPRELHVVDELPRRGIGKVDRRALVRR 354
|
|
| starter-C_NRPS |
cd19533 |
Starter Condensation domains, found in the first module of nonribosomal peptide synthetases ... |
13-238 |
5.37e-09 |
|
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: 60.85 E-value: 5.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 13 SEKFKKEKEYWLDKLSGDVE---LSRfPCDCLSLNNIQASKEsyycqFPSDIAKRAVAISNNSDMLLYTILLSGVKYLLS 89
Cdd:cd19533 182 SERFERDRAFWTEQFEDLPEpvsLAR-RAPGRSLAFLRRTAE-----LPPELTRTLLEAAEAHGASWPSFFIALVAAYLH 255
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 90 RYTDKDDVVIGMPVFKQG----QEETVFQNNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGES 165
Cdd:cd19533 256 RLTGANDVVLGVPVMGRLgaaaRQTPGMVANTLPLRLTVDPQQTFAELVAQVSRELRSLLRHQRYRYEDLRRDLGLTGEL 335
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 166 NNL--PLLNTIVM---LDDIHCYESTDKINS----DMVIRFMK--NEEQLKVQVDYNSTLYSEGLVSRIVNHLYNILDIL 234
Cdd:cd19533 336 HPLfgPTVNYMPFdygLDFGGVVGLTHNLSSgptnDLSIFVYDrdDESGLRIDFDANPALYSGEDLARHQERLLRLLEEA 415
|
....
gi 446807313 235 MKDP 238
Cdd:cd19533 416 AADP 419
|
|
| AFD_CAR-like |
cd17632 |
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation ... |
415-762 |
6.05e-09 |
|
adenylation domain of carboxylic acid reductase (CAR); This family contains the adenylation domain of carboxylic acid reductase enzymes (CARs), and performs an equivalent function to that of the ANL superfamily of adenylating enzymes. It takes a carboxylic acid substrate and ATP, and produces an AMP-acyl phosphoester intermediate, releasing pyrophosphate. Kinetic analysis using various substrates shows that this enzyme has a broad but similar substrate specificity, preferring electron-rich acids. This suggests that attack by the carboxylate on the alpha-phosphate of adenosine triphosphate (ATP) is the step that determines the substrate specificity and reaction kinetics. CAR is an important enzyme for use as a biocatalyst providing regiospecific route to aldehydes from their respective carboxylic acids.
Pssm-ID: 341287 [Multi-domain] Cd Length: 588 Bit Score: 61.32 E-value: 6.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 415 PQNLAYVIYTSGSTGQPKGVMIEHRSLTNF--LCAMYEDFSQDIGITDN-----------VLF-------------SSSI 468
Cdd:cd17632 222 DDPLALLIYTSGSTGTPKGAMYTERLVATFwlKVSSIQDIRPPASITLNfmpmshiagriSLYgtlarggtayfaaASDM 301
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 469 SfdvTIFE----------IFVPLVCGARMTIYQGE--KFDVPKLVQVILEEQVTlAYIPPTLLNEiydyfvranqkiSLN 536
Cdd:cd17632 302 S---TLFDdlalvrptelFLVPRVCDMLFQRYQAEldRRSVAGADAETLAERVK-AELRERVLGG------------RLL 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 537 KLFVGVEPIKTELLAKYDHLFrgNLQILNLYGPTEATVcctsyqyerdkeITTQNVPIGSPLLNTKI-------YIL-DS 608
Cdd:cd17632 366 AAVCGSAPLSAEMKAFMESLL--DLDLHDGYGSTEAGA------------VILDGVIVRPPVLDYKLvdvpelgYFRtDR 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 609 FHrlqpigvP-GEICISGIGLARGYINRKELTADKFIDHPFergeklYKTGDI-ARWLPDgNIEYLGRVDHQVKI-RGYR 685
Cdd:cd17632 432 PH-------PrGELLVKTDTLFPGYYKRPEVTAEVFDEDGF------YRTGDVmAELGPD-RLVYVDRRNNVLKLsQGEF 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 686 IELGEIEASLLKYETIKTAVViqrEDESGEKYLCAYVVTEKD----IPIPEVRAYLATKLPY---------YMIPQQIIs 752
Cdd:cd17632 498 VTVARLEAVFAASPLVRQIFV---YGNSERAYLLAVVVPTQDalagEDTARLRAALAESLQRiareaglqsYEIPRDFL- 573
|
410
....*....|.
gi 446807313 753 IQNIPLTQ-NG 762
Cdd:cd17632 574 IETEPFTIaNG 584
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
1662-1815 |
1.00e-08 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 60.01 E-value: 1.00e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1662 GEICISGIGLARGYInrkeltaDKFIDHPfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 1741
Cdd:PRK07445 302 GNITIQAQSLALGYY-------PQILDSQ-----GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1742 ETIKTAVVIDQED-EAGEKYLCAYVVTEKDIPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKL 1815
Cdd:PRK07445 370 GLVQDVCVLGLPDpHWGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQI 444
|
|
| GrsT |
COG3208 |
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and ... |
1921-2007 |
1.35e-08 |
|
Surfactin synthase thioesterase subunit [Secondary metabolites biosynthesis, transport and catabolism];
Pssm-ID: 442441 [Multi-domain] Cd Length: 237 Bit Score: 57.55 E-value: 1.35e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1921 FIIHGQGGGILNYYDLARELGEDKTVYGLQsigYD--DSRF---PNLSVEEMAVRYIEEIKQvKKEGPYTLLGWSFGGIV 1995
Cdd:COG3208 10 FCFPYAGGSASAYRPWAAALPPDIEVLAVQ---LPgrGDRLgepPLTSLEELADDLAEELAP-LLDRPFALFGHSMGALL 85
|
90
....*....|..
gi 446807313 1996 AFEMARKLEELG 2007
Cdd:COG3208 86 AFELARRLERRG 97
|
|
| LCL_NRPS |
cd19538 |
LCL-type Condensation domain of non-ribosomal peptide synthetases (NRPSs) and similar domains; ... |
7-238 |
1.39e-08 |
|
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: 59.59 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 7 QQVLLSSEK-----FKKEKEYWLDKLSGDVELSRFPCDCLSLNNIQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILL 81
Cdd:cd19538 174 QQELLGDESdpdslIARQLAYWKKQLAGLPDEIELPTDYPRPAESSYEGGTLTFEIDSELHQQLLQLAKDNNVTLFMVLQ 253
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 82 SGVKYLLSRYTDKDDVVIGMPVFKQGQEETV-----FQNNfLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLT 156
Cdd:cd19538 254 AGFAALLTRLGAGTDIPIGSPVAGRNDDSLEdlvgfFVNT-LVLRTDTSGNPSFRELLERVKETNLEAYEHQDIPFERLV 332
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 157 QLLSLDGESNNLPLLNtiVMLD---------DIHCYESTDKINS------DMVI-----RFMKNEEQLKVQVDYNSTLYS 216
Cdd:cd19538 333 EALNPTRSRSRHPLFQ--IMLAlqntpqpslDLPGLEAKLELRTvgsakfDLTFelreqYNDGTPNGIEGFIEYRTDLFD 410
|
250 260
....*....|....*....|..
gi 446807313 217 EGLVSRIVNHLYNILDILMKDP 238
Cdd:cd19538 411 HETIEALAQRYLLLLESAVENP 432
|
|
| E-C_NRPS |
cd19544 |
Dual Epimerization/Condensation (E/C) domains of nonribosomal peptide synthetases (NRPSs); ... |
895-1155 |
1.90e-08 |
|
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: 58.99 E-value: 1.90e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 895 TYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSF---------QIldgelVQKiepNVDFNIEYVHVNEKD--ADYL 963
Cdd:cd19544 23 PYLLRSLLAFDSRARLDAFLAALQQVIDRHDILRTAIlweglsepvQV-----VWR---QAELPVEELTLDPGDdaLAQL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 964 IHEFIS---PFDLSKppllrvlllRIAEE----RHILVVDMHHIISDGLSMGILIKEfVELY---KGNELPKLrVQYKDY 1033
Cdd:cd19544 95 RARFDPrryRLDLRQapl---lraHVAEDpangRWLLLLLFHHLISDHTSLELLLEE-IQAIlagRAAALPPP-VPYRNF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1034 VM--WQNGPyyknlISEQKNYWLTTLKgelpvlnfptDFQRPT----IQSFKGNVCSFN-----LGTDLTFKVNKLATET 1102
Cdd:cd19544 170 VAqaRLGAS-----QAEHEAFFREMLG----------DVDEPTapfgLLDVQGDGSDITearlaLDAELAQRLRAQARRL 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1103 GTTPYMILLAIYNILLSRYTGQEDIIVGSPIAGRSH--SDTNHMIGMFINTLVMR 1155
Cdd:cd19544 235 GVSPASLFHLAWALVLARCSGRDDVVFGTVLSGRMQggAGADRALGMFINTLPLR 289
|
|
| BACL_like |
cd05929 |
Bacterial Bile acid CoA ligases and similar proteins; Bile acid-Coenzyme A ligase catalyzes ... |
1441-1812 |
2.11e-08 |
|
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: 59.31 E-value: 2.11e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1441 DMSFEEEPGEDMHMMIEPH-NLAYVIYTSGSTGQPKGVM--IEHRSLTNFLCAMYEDFSQDIGitDNVLFSSsisfdvti 1517
Cdd:cd05929 106 LEDYEAAEGGSPETPIEDEaAGWKMLYSGGTTGRPKGIKrgLPGGPPDNDTLMAAALGFGPGA--DSVYLSP-------- 175
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 feifVPLIYGA-----RMTIYQG------EKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDYF--VRDNQKIVLNKLLVG 1584
Cdd:cd05929 176 ----APLYHAApfrwsMTALFMGgtlvlmEKFDPEEFLRLIERYRVTFAQFVPTMFVRLLKLPeaVRNAYDLSSLKRVIH 251
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1585 V-EPIKTELLAKYDHLfrGNLQILNGYGPTEAT--VCCTSyryesnKEITTQNVPIGSPLLNtKIYILDSFHRIQPIGVP 1661
Cdd:cd05929 252 AaAPCPPWVKEQWIDW--GGPIIWEYYGGTEGQglTIING------EEWLTHPGSVGRAVLG-KVHILDEDGNEVPPGEI 322
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1662 GEICISGiGLARGYINRKELTADKFIDHPFErgeklyKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 1741
Cdd:cd05929 323 GEVYFAN-GPGFEYTNDPEKTAAARNEGGWS------TLGDVGYLDEDGYLYLTDRRSDMIISGGVNIYPQEIENALIAH 395
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446807313 1742 ETIKTAVVIDQED-EAGEKyLCAYVVTEKD-----IPIPEVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKL 1812
Cdd:cd05929 396 PKVLDAAVVGVPDeELGQR-VHAVVQPAPGadagtALAEELIAFLRDRLSRYKCPRSIEFVAELPRDDTGKLYRRLL 471
|
|
| AMP-binding_C |
pfam13193 |
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to ... |
1733-1806 |
2.14e-08 |
|
AMP-binding enzyme C-terminal domain; This is a small domain that is found C terminal to pfam00501. It has a central beta sheet core that is flanked by alpha helices.
Pssm-ID: 463804 [Multi-domain] Cd Length: 76 Bit Score: 52.93 E-value: 2.14e-08
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446807313 1733 EIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP--EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGK 1806
Cdd:pfam13193 1 EVESALVSHPAVAEAAVVGVPDELKGEAPVAFVVLKPGVELLeeELVAHVREELGPYAVPKEVVFVDELPKTRSGK 76
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
284-769 |
3.23e-08 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 59.00 E-value: 3.23e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 284 QVKQNPNQIAIVCNG------KEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILG------------- 344
Cdd:PRK00174 76 HLKTRGDKVAIIWEGddpgdsRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLAcarigavhsvvfg 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 345 ----------ILKA-------------GGAYLPIdtelpKQRVEYMLTDSGC-SHVLTYQNSIIKgVAFQGSvinlMDIP 400
Cdd:PRK00174 156 gfsaealadrIIDAgaklvitadegvrGGKPIPL-----KANVDEALANCPSvEKVIVVRRTGGD-VDWVEG----RDLW 225
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 401 FEEE-QVEDLQITMEPQN----LaYVIYTSGSTGQPKGVM------IEHRSLTN-----------FLCamyedfSQDIG- 457
Cdd:PRK00174 226 WHELvAGASDECEPEPMDaedpL-FILYTSGSTGKPKGVLhttggyLVYAAMTMkyvfdykdgdvYWC------TADVGw 298
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 458 ITDNvlfsSSIsfdvtifeIFVPLVCGARMTIYQGekfdVP------KLVQVILEEQVTLAYIPPTL---LNEIYDYFVR 528
Cdd:PRK00174 299 VTGH----SYI--------VYGPLANGATTLMFEG----VPnypdpgRFWEVIDKHKVTIFYTAPTAiraLMKEGDEHPK 362
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 529 ANQKISLNKL-FVGvEPIKTEllA---KYDHLFRGNLQILNLYGPTE--ATVcctsyqyerdkeIT-----TQNVPiGS- 596
Cdd:PRK00174 363 KYDLSSLRLLgSVG-EPINPE--AwewYYKVVGGERCPIVDTWWQTEtgGIM------------ITplpgaTPLKP-GSa 426
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 597 --PLLNTKIYILDSFHRLQPIGVPGEICI--SGIGLARGYINRKEltadKFIDHPFERGEKLYKTGDIARWLPDGNIEYL 672
Cdd:PRK00174 427 trPLPGIQPAVVDEEGNPLEGGEGGNLVIkdPWPGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGARRDEDGYYWIT 502
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 673 GRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDE-SGEKyLCAYVVTEKDIP-----IPEVRAYLATKLPYYMI 746
Cdd:PRK00174 503 GRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDiKGQG-IYAFVTLKGGEEpsdelRKELRNWVRKEIGPIAK 581
|
570 580
....*....|....*....|...
gi 446807313 747 PQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK00174 582 PDVIQFAPGLPKTRSGKIMRRIL 604
|
|
| PRK07824 |
PRK07824 |
o-succinylbenzoate--CoA ligase; |
595-769 |
3.73e-08 |
|
o-succinylbenzoate--CoA ligase;
Pssm-ID: 236108 [Multi-domain] Cd Length: 358 Bit Score: 57.75 E-value: 3.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 595 GSPLLNTKIYILDsfhrlqpigvpGEICISGIGLARGYINrkeltadkFIDHPFERGEKLYKTGDIARwLPDGNIEYLGR 674
Cdd:PRK07824 195 GVPLDGVRVRVED-----------GRIALGGPTLAKGYRN--------PVDPDPFAEPGWFRTDDLGA-LDDGVLTVLGR 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 675 VDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDES-GEKYLCAYVVTEKDIPIP-EVRAYLATKLPYYMIPQQIIS 752
Cdd:PRK07824 255 ADDAISTGGLTVLPQVVEAALATHPAVADCAVFGLPDDRlGQRVVAAVVGDGGPAPTLeALRAHVARTLDRTAAPRELHV 334
|
170
....*....|....*..
gi 446807313 753 IQNIPLTQNGKIDRKKL 769
Cdd:PRK07824 335 VDELPRRGIGKVDRRAL 351
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
278-484 |
4.15e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 58.42 E-value: 4.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 278 PQLFEEQVKQNPNQIAIVCNGKE---------ITYKQLNIKANQLARRLLDQGVKREFIVgVMMERSIEMIVGILGILKA 348
Cdd:PRK05850 4 PSLLRERASLQPDDAAFTFIDYEqdpagvaetLTWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 349 GGAYLPIDTELPKQ---RVEYMLTDSGCSHVLTyQNSIIKGV-----AFQGSV------INLMDIPFEEEQVEDLQitmE 414
Cdd:PRK05850 83 GLIAVPLSVPQGGAhdeRVSAVLRDTSPSVVLT-TSAVVDDVteyvaPQPGQSappvieVDLLDLDSPRGSDARPR---D 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 415 PQNLAYVIYTSGSTGQPKGVMIEHRSLT-NFLCAMYEDFsqdiGITDNV--LFSSSISF-----DV-TIFEIFVPLVCG 484
Cdd:PRK05850 159 LPSTAYLQYTSGSTRTPAGVMVSHRNVIaNFEQLMSDYF----GDTGGVppPDTTVVSWlpfyhDMgLVLGVCAPILGG 233
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
423-769 |
5.79e-08 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 57.93 E-value: 5.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 423 YTSGSTGQPKGVMIEHR-----SLTNFLCamyedFSQDIGI----TDNVLFSSSISFDVTIFEIFVPLVCGARMT---IY 490
Cdd:PLN02479 202 YTSGTTASPKGVVLHHRgaylmALSNALI-----WGMNEGAvylwTLPMFHCNGWCFTWTLAALCGTNICLRQVTakaIY 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 491 QGekfdvpklvqvILEEQVTLAYIPPTLLNEIYDyfVRANQKI-----SLNKLFVGVEPIKTELLAKYDHLFRgnlqILN 565
Cdd:PLN02479 277 SA-----------IANYGVTHFCAAPVVLNTIVN--APKSETIlplprVVHVMTAGAAPPPSVLFAMSEKGFR----VTH 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 566 LYGPTE----ATVCctSYQYERDKEittqnVPIGSPLLNTKI---YI----LDSFHRLQPIGVP------GEICISGIGL 628
Cdd:PLN02479 340 TYGLSEtygpSTVC--AWKPEWDSL-----PPEEQARLNARQgvrYIglegLDVVDTKTMKPVPadgktmGEIVMRGNMV 412
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 629 ARGYINRKELTADKFidhpfERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQ 708
Cdd:PLN02479 413 MKGYLKNPKANEEAF-----ANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTHPAVLEASVVA 485
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 709 REDESGEKYLCAYVV-------TEKDIPIPEVRAYLATKLPYYMIPQQIIsIQNIPLTQNGKIDRKKL 769
Cdd:PLN02479 486 RPDERWGESPCAFVTlkpgvdkSDEAALAEDIMKFCRERLPAYWVPKSVV-FGPLPKTATGKIQKHVL 552
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
288-769 |
7.38e-08 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 57.60 E-value: 7.38e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 288 NPNQIAIVCNGKE------ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPK 361
Cdd:PLN02654 102 NGDKIAIYWEGNEpgfdasLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 362 QRVEYMLTDSGCSHVLTyQNSIIKGVafqgSVINLMDI------PFEEEQVE-DLQITMEPQNLA--------------- 419
Cdd:PLN02654 182 ESLAQRIVDCKPKVVIT-CNAVKRGP----KTINLKDIvdaaldESAKNGVSvGICLTYENQLAMkredtkwqegrdvww 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 420 ----------------------YVIYTSGSTGQPKGVMieHR-------SLTNFLCAMYEDFSQDIGITDNVLFSSSISF 470
Cdd:PLN02654 257 qdvvpnyptkcevewvdaedplFLLYTSGSTGKPKGVL--HTtggymvyTATTFKYAFDYKPTDVYWCTADCGWITGHSY 334
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 471 dVTifeiFVPLVCGARMTIYQGEKF--DVPKLVQVILEEQVTLAYIPPTLLNEIY---DYFVRANQKISLNKLFVGVEPI 545
Cdd:PLN02654 335 -VT----YGPMLNGATVLVFEGAPNypDSGRCWDIVDKYKVTIFYTAPTLVRSLMrdgDEYVTRHSRKSLRVLGSVGEPI 409
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 546 KTELLAKYdhlfrgnlqiLNLYGPTEATVCCTSYQYERDKEITTqnvPI--------GS---PLLNTKIYILDSFHRLQP 614
Cdd:PLN02654 410 NPSAWRWF----------FNVVGDSRCPISDTWWQTETGGFMIT---PLpgawpqkpGSatfPFFGVQPVIVDEKGKEIE 476
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 615 IGVPGEICI--SGIGLAR---GYINRKELTADKfidhPFErgeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELG 689
Cdd:PLN02654 477 GECSGYLCVkkSWPGAFRtlyGDHERYETTYFK----PFA---GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTA 549
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 690 EIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKDIPIP-EVRAYLA----TKLPYYMIPQQIISIQNIPLTQNGKI 764
Cdd:PLN02654 550 EVESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSeELRKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKI 629
|
....*
gi 446807313 765 DRKKL 769
Cdd:PLN02654 630 MRRIL 634
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
289-764 |
9.47e-08 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 57.26 E-value: 9.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 289 PNQIAIVCNGKEITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYML 368
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 369 tDSGCSHVL----TYQNSIIKGVA-FQGSVINLMDI---------PFEEEQVEDLQITMEPqNLAYVI-----------Y 423
Cdd:PRK08162 112 -RHGEAKVLivdtEFAEVAREALAlLPGPKPLVIDVddpeypggrFIGALDYEAFLASGDP-DFAWTLpadewdaialnY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 424 TSGSTGQPKGVMIEHRSltNFLCAMyedfsqdigitdnvlfSSSISFDVTIFEIF---VPLV-CGA-----RMTIYQG-- 492
Cdd:PRK08162 190 TSGTTGNPKGVVYHHRG--AYLNAL----------------SNILAWGMPKHPVYlwtLPMFhCNGwcfpwTVAARAGtn 251
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 493 ---EKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDyfVRANQKISLN---KLFVGVEPIKTELLAKYDHLfrgNLQILNL 566
Cdd:PRK08162 252 vclRKVDPKLIFDLIREHGVTHYCGAPIVLSALIN--APAEWRAGIDhpvHAMVAGAAPPAAVIAKMEEI---GFDLTHV 326
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 567 YGPTE----ATVCCTSYQY------ERDKEITTQNVPIgsPLLNTkIYILDSfHRLQPigVP------GEICISGIGLAR 630
Cdd:PRK08162 327 YGLTEtygpATVCAWQPEWdalpldERAQLKARQGVRY--PLQEG-VTVLDP-DTMQP--VPadgetiGEIMFRGNIVMK 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 631 GYINRKELTADKFIDHPFErgeklykTGDIARWLPDGNIeylgrvdhQVKIR--------GYRIELGEIEASLLKYETIK 702
Cdd:PRK08162 401 GYLKNPKATEEAFAGGWFH-------TGDLAVLHPDGYI--------KIKDRskdiiisgGENISSIEVEDVLYRHPAVL 465
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446807313 703 TAVVIQREDESGEKYLCAYV-------VTEKDIpIPEVRAYLATklpyYMIPQQIIsIQNIPLTQNGKI 764
Cdd:PRK08162 466 VAAVVAKPDPKWGEVPCAFVelkdgasATEEEI-IAHCREHLAG----FKVPKAVV-FGELPKTSTGKI 528
|
|
| PRK07445 |
PRK07445 |
O-succinylbenzoic acid--CoA ligase; Reviewed |
619-771 |
1.29e-07 |
|
O-succinylbenzoic acid--CoA ligase; Reviewed
Pssm-ID: 236019 [Multi-domain] Cd Length: 452 Bit Score: 56.54 E-value: 1.29e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 619 GEICISGIGLARGYInrkeltaDKFIDHPfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 698
Cdd:PRK07445 302 GNITIQAQSLALGYY-------PQILDSQ-----GIFETDDLGYLDAQGYLHILGRNSQKIITGGENVYPAEVEAAILAT 369
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313 699 ETIKTAVVIQREDES-GEKYLCAYVVTEKDIPIPEVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQ 771
Cdd:PRK07445 370 GLVQDVCVLGLPDPHwGEVVTAIYVPKDPSISLEELKTAIKDQLSPFKQPKHWIPVPQLPRNPQGKINRQQLQQ 443
|
|
| C_PKS-NRPS |
cd20483 |
Condensation domain of hybrid polyketide synthetase/nonribosomal peptide synthetases (PKS ... |
5-237 |
1.51e-07 |
|
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: 56.11 E-value: 1.51e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 5 FT--QQVLLSSEKFKKEKEYWLDKLSGDVELS---------RFPCDCLSLNNIQASkesyycqFPSDIAKRAVAISNNSD 73
Cdd:cd20483 174 FTlwHNALLQSPLVQPLLDFWKEKLEGIPDASkllpfakaeRPPVKDYERSTVEAT-------LDKELLARMKRICAQHA 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 74 MLLYTILLSGVKYLLSRYTDKDDVVIGM-------PVFkqgqEETV-FQNNFLLLRTQINQEDNFKEIIYKIKETILESN 145
Cdd:cd20483 247 VTPFMFLLAAFRAFLYRYTEDEDLTIGMvdgdrphPDF----DDLVgFFVNMLPIRCRMDCDMSFDDLLESTKTTCLEAY 322
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 146 EHCHFPFNKLTQLLSLDGESNNLPLLNTIV-------MLD------DIHCYESTD-KINSDMVIRFMKNEE-QLKVQVDY 210
Cdd:cd20483 323 EHSAVPFDYIVDALDVPRSTSHFPIGQIAVnyqvhgkFPEydtgdfKFTDYDHYDiPTACDIALEAEEDPDgGLDLRLEF 402
|
250 260
....*....|....*....|....*..
gi 446807313 211 NSTLYSEGLVSRIVNHLYNILDILMKD 237
Cdd:cd20483 403 STTLYDSADMERFLDNFVTFLTSVIRD 429
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
1463-1834 |
1.60e-07 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 56.67 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1463 YVIYTSGSTGQPKGVMIEHRSltNFLCAMYEDFSQDIGITDNVLFSSS----ISFDVTIFEIfvpLIYGARMTIYQGekf 1538
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSNGP--HLVGLKYYWRSIIEKDIPTVVFSHSsigwVSFHGFLYGS---LSLGNTFVMFEG--- 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1539 DVTK-------LVQVILEEQVTLSYIPPTLLNeiydYFVRD--NQKIV--------LNKLLVGVEPIKtELLAKYdhlFR 1601
Cdd:PTZ00237 330 GIIKnkhieddLWNTIEKHKVTHTLTLPKTIR----YLIKTdpEATIIrskydlsnLKEIWCGGEVIE-ESIPEY---IE 401
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1602 GNLQI--LNGYGPTEaTVCCTSYRYES-NKEITTQNVPigSPLLNTKIYILDSfhRIQPIGVPGEICIS---GIGLARGY 1675
Cdd:PTZ00237 402 NKLKIksSRGYGQTE-IGITYLYCYGHiNIPYNATGVP--SIFIKPSILSEDG--KELNVNEIGEVAFKlpmPPSFATTF 476
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1676 INRKELTADKFIDHPfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE 1755
Cdd:PTZ00237 477 YKNDEKFKQLFSKFP-----GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDP 551
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1756 AGEKYLCAYVVTEKDIPIP---------EVRAYLATKLPHYMIPQQLIPIHNIPLTQNGKIDRSKLPKLntLGNSNYVPP 1826
Cdd:PTZ00237 552 DCYNVPIGLLVLKQDQSNQsidlnklknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKF--LNDSNYQLP 629
|
....*...
gi 446807313 1827 RNEIDSSL 1834
Cdd:PTZ00237 630 DNVNDSEI 637
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
414-681 |
1.66e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 56.75 E-value: 1.66e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 414 EPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM--YEDFSQDIGITDNVLFS----SSIsFDVTIFEIFvpLVCGARM 487
Cdd:PLN02430 218 KPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlFMEQFEDKMTHDDVYLSflplAHI-LDRMIEEYF--FRKGASV 294
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 488 TIYQGekfDVPKLVQVILEEQVTLAYIPPTLLNEIYDYFVRANQKISLNKLFVGVEPIKTELL---AKYDH--------- 555
Cdd:PLN02430 295 GYYHG---DLNALRDDLMELKPTLLAGVPRVFERIHEGIQKALQELNPRRRLIFNALYKYKLAwmnRGYSHkkaspmadf 371
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 556 -LFR-------GNLQILNLYG---PTE------ATVCC---TSYQYERDKEITTQNVP--------IGSPLLNTKIyild 607
Cdd:PLN02430 372 lAFRkvkaklgGRLRLLISGGaplSTEieeflrVTSCAfvvQGYGLTETLGPTTLGFPdemcmlgtVGAPAVYNEL---- 447
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 608 sfhRLQ--------PIGVP--GEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIARWLPDGNIEYLGRVDH 677
Cdd:PLN02430 448 ---RLEevpemgydPLGEPprGEICVRGKCLFSGYYKNPELTEEVMKDGWFH-------TGDIGEILPNGVLKIIDRKKN 517
|
....
gi 446807313 678 QVKI 681
Cdd:PLN02430 518 LIKL 521
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
410-765 |
1.99e-07 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 56.26 E-value: 1.99e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 410 QITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGITDNVLFSSSI----SFDVTIfEIFVPLVCGA 485
Cdd:PRK08043 359 QVKQQPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADFTPNDRFMSALplfhSFGLTV-GLFTPLLTGA 433
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 486 RMTIYQG--EKFDVPKLVqviLEEQVTLAYIPPTLLNEI------YD-----YFVRANQKISlnklfvgvEPIKTELLAK 552
Cdd:PRK08043 434 EVFLYPSplHYRIVPELV---YDRNCTVLFGTSTFLGNYarfanpYDfarlrYVVAGAEKLQ--------ESTKQLWQDK 502
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 553 YdhlfrgNLQILNLYGPTEatvcCTSyqyerdkeITTQNVPIGspllnTKIYildSFHRLQP------IGVPG-----EI 621
Cdd:PRK08043 503 F------GLRILEGYGVTE----CAP--------VVSINVPMA-----AKPG---TVGRILPgmdarlLSVPGieqggRL 556
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 622 CISGIGLARGYI---NRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 698
Cdd:PRK08043 557 QLKGPNIMNGYLrveKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGV 636
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446807313 699 ETIKTAVVIQREDES-GEkylcAYVV--TEKDIPIPEVRAYL-ATKLPYYMIPQQIISIQNIPLTQNGKID 765
Cdd:PRK08043 637 SPDKQHATAIKSDASkGE----ALVLftTDSELTREKLQQYArEHGVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| Abhydrolase_1 |
pfam00561 |
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes. |
1922-2154 |
2.59e-07 |
|
alpha/beta hydrolase fold; This catalytic domain is found in a very wide range of enzymes.
Pssm-ID: 395444 [Multi-domain] Cd Length: 245 Bit Score: 54.05 E-value: 2.59e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1922 IIHGQGGGILNYYDLARELGED-KTVYGLQSIGYDDSRFP----NLSVEEMAvRYIEEIKQVKKEGPYTLLGWSFGGIVA 1996
Cdd:pfam00561 5 LLHGLPGSSDLWRKLAPALARDgFRVIALDLRGFGKSSRPkaqdDYRTDDLA-EDLEYILEALGLEKVNLVGHSMGGLIA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1997 FEMARKLEELGDKVSFLG-LLDVHPIEQGREILSLNIKNAFEE--LEKFNDQLGIeKISFEQMSEEQLIESLLKKFTLNE 2073
Cdd:pfam00561 84 LAYAAKYPDRVKALVLLGaLDPPHELDEADRFILALFPGFFDGfvADFAPNPLGR-LVAKLLALLLLRLRLLKALPLLNK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 2074 NSCQQNFEDPMMNKL--KVMIANRYAYLKYNCKQKIKADIFLFNASINDIHPLVDYNRWNEYTSGEVYALQVPGSHLSML 2151
Cdd:pfam00561 163 RFPSGDYALAKSLVTgaLLFIETWSTELRAKFLGRLDEPTLIIWGDQDPLVPPQALEKLAQLFPNARLVVIPDAGHFAFL 242
|
...
gi 446807313 2152 EKP 2154
Cdd:pfam00561 243 EGP 245
|
|
| PLN02479 |
PLN02479 |
acetate-CoA ligase |
1662-1812 |
3.07e-07 |
|
acetate-CoA ligase
Pssm-ID: 178097 [Multi-domain] Cd Length: 567 Bit Score: 55.62 E-value: 3.07e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1662 GEICISGIGLARGYINRKELTADKFidhpfERGekLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKY 1741
Cdd:PLN02479 403 GEIVMRGNMVMKGYLKNPKANEEAF-----ANG--WFHSGDLGVKHPDGYIEIKDRSKDIIISGGENISSLEVENVVYTH 475
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1742 ETIKTAVVIDQEDEAGEKYLCAYVV-------TEKDIPIPEVRAYLATKLPHYMIPQQLIpIHNIPLTQNGKIDRSKL 1812
Cdd:PLN02479 476 PAVLEASVVARPDERWGESPCAFVTlkpgvdkSDEAALAEDIMKFCRERLPAYWVPKSVV-FGPLPKTATGKIQKHVL 552
|
|
| PRK12476 |
PRK12476 |
putative fatty-acid--CoA ligase; Provisional |
300-489 |
3.20e-07 |
|
putative fatty-acid--CoA ligase; Provisional
Pssm-ID: 171527 [Multi-domain] Cd Length: 612 Bit Score: 55.52 E-value: 3.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 300 EITYKQLNIKANQLARRLlDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI-DTELP--KQRVEYMLTDSGCSHV 376
Cdd:PRK12476 68 ELTWTQLGVRLRAVGARL-QQVAGPGDRVAILAPQGIDYVAGFFAAIKAGTIAVPLfAPELPghAERLDTALRDAEPTVV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 377 LTYQ------NSIIKGV--AFQGSVINLMDIPfeEEQVEDLQ-ITMEPQNLAYVIYTSGSTGQPKGVMIEHRSL-TNFLC 446
Cdd:PRK12476 147 LTTTaaaeavEGFLRNLprLRRPRVIAIDAIP--DSAGESFVpVELDTDDVSHLQYTSGSTRPPVGVEITHRAVgTNLVQ 224
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 446807313 447 AMYEdfsqdIGITDNVLFSSS---ISFDVTIFEIFVPLVCGARMTI 489
Cdd:PRK12476 225 MILS-----IDLLDRNTHGVSwlpLYHDMGLSMIGFPAVYGGHSTL 265
|
|
| PLN02430 |
PLN02430 |
long-chain-fatty-acid-CoA ligase |
1457-1724 |
3.60e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178049 [Multi-domain] Cd Length: 660 Bit Score: 55.59 E-value: 3.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1457 EPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAM--YEDFSQDIGITDNVLFSssisfdvtifeiFVPLIY-------- 1526
Cdd:PLN02430 218 KPLDICTIMYTSGTSGDPKGVVLTHEAVATFVRGVdlFMEQFEDKMTHDDVYLS------------FLPLAHildrmiee 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1527 -----GARMTIYQGekfDVTKLVQVILEeqvtlsyIPPTLLNEIYDYFVRDNQKIvlNKLLVGVEPIKTELlakYDHLFR 1601
Cdd:PLN02430 286 yffrkGASVGYYHG---DLNALRDDLME-------LKPTLLAGVPRVFERIHEGI--QKALQELNPRRRLI---FNALYK 350
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1602 GNLQILN-GYGPTEA----------------------------------------TVCC---TSYRYESNKEITTQNVP- 1636
Cdd:PLN02430 351 YKLAWMNrGYSHKKAspmadflafrkvkaklggrlrllisggaplsteieeflrvTSCAfvvQGYGLTETLGPTTLGFPd 430
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1637 -------IGSPLLNTKIYILD-SFHRIQPIGVP--GEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIARW 1706
Cdd:PLN02430 431 emcmlgtVGAPAVYNELRLEEvPEMGYDPLGEPprGEICVRGKCLFSGYYKNPELTEEVMKDGWFH-------TGDIGEI 503
|
330
....*....|....*...
gi 446807313 1707 LPDGNIEYLGRVDHQVKI 1724
Cdd:PLN02430 504 LPNGVLKIIDRKKNLIKL 521
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
1324-1717 |
5.89e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 54.85 E-value: 5.89e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1324 FEEQVKRNPNQIA----VVCNEKG-----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGA 1394
Cdd:PLN02861 49 FSDAVKKYPNNQMlgrrQVTDSKVgpyvwLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQGIT 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1395 YLPIDTDLPKQRVEYMLTDSGCSHVLVHQNSI-------------IKGIEFQGNVIDLMDM----------SFEEEP--G 1449
Cdd:PLN02861 129 YVPLYDTLGANAVEFIINHAEVSIAFVQESKIssilsclpkcssnLKTIVSFGDVSSEQKEeaeelgvscfSWEEFSlmG 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1450 EDMHMMIEPH--NLAYVIYTSGSTGQPKGVMIEHRSLtnflcaMYEDFSQD--IGITDNVLFSSSISFDvtifeiFVPLI 1525
Cdd:PLN02861 209 SLDCELPPKQktDICTIMYTSGTTGEPKGVILTNRAI------IAEVLSTDhlLKVTDRVATEEDSYFS------YLPLA 276
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1526 Y-------------GARMTIYQGekfDVTKLVQVILEEQVTLSYIPPTLLNEIY------------------DY------ 1568
Cdd:PLN02861 277 HvydqvietyciskGASIGFWQG---DIRYLMEDVQALKPTIFCGVPRVYDRIYtgimqkissggmlrkklfDFaynykl 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1569 ------FVRDNQKIVLNKLLVgvEPIKTELLAKYDHLFRGN----------LQILN------GYGPTEATVCCTSYRYES 1626
Cdd:PLN02861 354 gnlrkgLKQEEASPRLDRLVF--DKIKEGLGGRVRLLLSGAaplprhveefLRVTScsvlsqGYGLTESCGGCFTSIANV 431
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1627 NKEITTQNVP---IGSPLLNTKIYILDSFHriqpiGVP-GEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGD 1702
Cdd:PLN02861 432 FSMVGTVGVPmttIEARLESVPEMGYDALS-----DVPrGEICLRGNTLFSGYHKRQDLTEEVLIDGWFH-------TGD 499
|
490
....*....|....*
gi 446807313 1703 IARWLPDGNIEYLGR 1717
Cdd:PLN02861 500 IGEWQPNGAMKIIDR 514
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
300-769 |
5.95e-07 |
|
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: 54.74 E-value: 5.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 300 EITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQRVEYMLTDSGCShvLTY 379
Cdd:cd05915 24 RTTYAEVYQRARRLMGGLRALGVGVGDRVATLGFNHFRHLEAYFAVPGMGAVLHTANPRLSPKEIAYILNHAEDK--VLL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 380 QNSIIKGVAFQGSVI--NLMDIPFEE---EQVEDLQITMEPQ----------NLAYVIYTSGSTGQPKGVMIEHRSLtnF 444
Cdd:cd05915 102 FDPNLLPLVEAIRGElkTVQHFVVMDekaPEGYLAYEEALGEeadpvrvperAACGMAYTTGTTGLPKGVVYSHRAL--V 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 445 LCAMYedfsqdIGITDNVLFSSsisfdVTIFEIFVPLV-CGARMTIYQGEKF--------DVPK---LVQVILEEQVTLA 512
Cdd:cd05915 180 LHSLA------ASLVDGTALSE-----KDVVLPVVPMFhVNAWCLPYAATLVgakqvlpgPRLDpasLVELFDGEGVTFT 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 513 YIPPTLLNEIydyfvrANQKISLNKLFV--------GVEPikTELLAKYDHLfrGNLQILNLYGPTE----ATVCCTSYQ 580
Cdd:cd05915 249 AGVPTVWLAL------ADYLESTGHRLKtlrrlvvgGSAA--PRSLIARFER--MGVEVRQGYGLTEtspvVVQNFVKSH 318
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 581 YER--DKEITTQNVPIGSPLLNTKIYILDSfhrlQPIGVPGE------ICISGIGLARGYINRKELT-ADKFidhpfeRG 651
Cdd:cd05915 319 LESlsEEEKLTLKAKTGLPIPLVRLRVADE----EGRPVPKDgkalgeVQLKGPWITGGYYGNEEATrSALT------PD 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 652 eKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYV-VTEKDIPI 730
Cdd:cd05915 389 -GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHPKVKEAAVVAIPHPKWQERPLAVVvPRGEKPTP 467
|
490 500 510 520
....*....|....*....|....*....|....*....|
gi 446807313 731 PEVRAYLATKL-PYYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:cd05915 468 EELNEHLLKAGfAKWQLPDAYVFAEEIPRTSAGKFLKRAL 507
|
|
| PRK07769 |
PRK07769 |
long-chain-fatty-acid--CoA ligase; Validated |
300-489 |
6.01e-07 |
|
long-chain-fatty-acid--CoA ligase; Validated
Pssm-ID: 181109 [Multi-domain] Cd Length: 631 Bit Score: 54.74 E-value: 6.01e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 300 EITYKQLNIKANQLARRLlDQGVKREFIVGVMMERSIEMIVGILGILKAGGAYLPI-DTELPKQ--RVEYMLTDSGCSHV 376
Cdd:PRK07769 55 DLTWSQFGARNRAVGARL-QQVTKPGDRVAILAPQNLDYLIAFFGALYAGRIAVPLfDPAEPGHvgRLHAVLDDCTPSAI 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 377 LTyQNSIIKGVA--FQG-------SVINLMDIPfeeEQVEDLQITMEPQ--NLAYVIYTSGSTGQPKGVMIEHRSL-TNF 444
Cdd:PRK07769 134 LT-TTDSAEGVRkfFRArpakerpRVIAVDAVP---DEVGATWVPPEANedTIAYLQYTSGSTRIPAGVQITHLNLpTNV 209
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 446807313 445 LcAMYEDFSQDIGitdnvlfSSSISF-----DVTIFEIFVPLVCGARMTI 489
Cdd:PRK07769 210 L-QVIDALEGQEG-------DRGVSWlpffhDMGLITVLLPALLGHYITF 251
|
|
| PRK09192 |
PRK09192 |
fatty acyl-AMP ligase; |
303-441 |
8.04e-07 |
|
fatty acyl-AMP ligase;
Pssm-ID: 236403 [Multi-domain] Cd Length: 579 Bit Score: 54.24 E-value: 8.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 303 YKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAGG--AYLPIDTELpKQRVEY------MLTDSGCS 374
Cdd:PRK09192 52 YQTLRARAEAGARRLLALGLKPGDRVALIAETDGDFVEAFFACQYAGLvpVPLPLPMGF-GGRESYiaqlrgMLASAQPA 130
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 375 HVLT------YQNSIIKGVA--FQGSVINLMDIPfeeEQVEDLQiTMEPQNLAYVIYTSGSTGQPKGVMIEHRSL 441
Cdd:PRK09192 131 AIITpdellpWVNEATHGNPllHVLSHAWFKALP---EADVALP-RPTPDDIAYLQYSSGSTRFPRGVIITHRAL 201
|
|
| PLN02861 |
PLN02861 |
long-chain-fatty-acid-CoA ligase |
279-726 |
9.08e-07 |
|
long-chain-fatty-acid-CoA ligase
Pssm-ID: 178452 [Multi-domain] Cd Length: 660 Bit Score: 54.08 E-value: 9.08e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 279 QLFEEQVKQNPNQIAI----VCNGKE-----ITYKQLNIKANQLARRLLDQGVKREFIVGVMMERSIEMIVGILGILKAG 349
Cdd:PLN02861 47 QFFSDAVKKYPNNQMLgrrqVTDSKVgpyvwLTYKEVYDAAIRIGSAIRSRGVNPGDRCGIYGSNCPEWIIAMEACNSQG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 350 GAYLPIDTELPKQRVEYMLTDSGCSHVLTYQNSI-------------IKGVAFQGSVINLMDIPFEE-----------EQ 405
Cdd:PLN02861 127 ITYVPLYDTLGANAVEFIINHAEVSIAFVQESKIssilsclpkcssnLKTIVSFGDVSSEQKEEAEElgvscfsweefSL 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 406 VEDLQITMEPQ---NLAYVIYTSGSTGQPKGVMIEHRSLtnflcaMYEDFSQD--IGITDNVLFSSSISFD----VTIFE 476
Cdd:PLN02861 207 MGSLDCELPPKqktDICTIMYTSGTTGEPKGVILTNRAI------IAEVLSTDhlLKVTDRVATEEDSYFSylplAHVYD 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 477 IFVPLVC---GARMTIYQGekfDVPKLVQVILEEQVTLAYIPPTLLNEIYdyfVRANQKIS-----LNKLF--------- 539
Cdd:PLN02861 281 QVIETYCiskGASIGFWQG---DIRYLMEDVQALKPTIFCGVPRVYDRIY---TGIMQKISsggmlRKKLFdfaynyklg 354
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 540 -----------------VGVEPIKTELLAKYDHLFRGN----------LQILNL------YGPTEATVCCTSYQYERDKE 586
Cdd:PLN02861 355 nlrkglkqeeasprldrLVFDKIKEGLGGRVRLLLSGAaplprhveefLRVTSCsvlsqgYGLTESCGGCFTSIANVFSM 434
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 587 ITTQNVP---IGSPLLNTKIYILDSFHrlqpiGVP-GEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIAR 662
Cdd:PLN02861 435 VGTVGVPmttIEARLESVPEMGYDALS-----DVPrGEICLRGNTLFSGYHKRQDLTEEVLIDGWFH-------TGDIGE 502
|
490 500 510 520 530 540
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 663 WLPDGNIEYLGRVDHQVKI-RGYRIELGEIEASLLKYETIKTAVVIqreDESGEKYLCAYVVTEK 726
Cdd:PLN02861 503 WQPNGAMKIIDRKKNIFKLsQGEYVAVENLENTYSRCPLIASIWVY---GNSFESFLVAVVVPDR 564
|
|
| PRK08162 |
PRK08162 |
acyl-CoA synthetase; Validated |
1332-1807 |
1.17e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236169 [Multi-domain] Cd Length: 545 Bit Score: 53.80 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1332 PNQIAVVCNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQRVEYML 1411
Cdd:PRK08162 32 PDRPAVIHGDRRRTWAETYARCRRLASALARRGIGRGDTVAVLLPNIPAMVEAHFGVPMAGAVLNTLNTRLDAASIAFML 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1412 tDSGCSHVLvhqnsiIKGIEFQGN--------------VIDLMDMSFEE----------------EPGEDMHMmiePHNL 1461
Cdd:PRK08162 112 -RHGEAKVL------IVDTEFAEVarealallpgpkplVIDVDDPEYPGgrfigaldyeaflasgDPDFAWTL---PADE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1462 AYVI---YTSGSTGQPKGVMIEHRSltNFLCAMyedfsqdigitdnvlfSSSISFDVTIFEIF---VPLI------YGAR 1529
Cdd:PRK08162 182 WDAIalnYTSGTTGNPKGVVYHHRG--AYLNAL----------------SNILAWGMPKHPVYlwtLPMFhcngwcFPWT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1530 MTIYQG-----EKFDVTKLVQVILEEQVT-LSYIPptllneiydyfvrdnqkIVLNKLLVGVEpiktELLAKYDHLFRGN 1603
Cdd:PRK08162 244 VAARAGtnvclRKVDPKLIFDLIREHGVThYCGAP-----------------IVLSALINAPA----EWRAGIDHPVHAM 302
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1604 ------------------LQILNGYGPTE----ATVCC---------TSYRYESNKEittQNVPIgsPLLNTkIYILDSf 1652
Cdd:PRK08162 303 vagaappaaviakmeeigFDLTHVYGLTEtygpATVCAwqpewdalpLDERAQLKAR---QGVRY--PLQEG-VTVLDP- 375
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1653 HRIQPigVP------GEICISGIGLARGYINRKELTADKFIDHPFErgeklykTGDIARWLPDGNIeylgrvdhQVKIR- 1725
Cdd:PRK08162 376 DTMQP--VPadgetiGEIMFRGNIVMKGYLKNPKATEEAFAGGWFH-------TGDLAVLHPDGYI--------KIKDRs 438
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1726 -------GYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYV-------VTEKDIpIPEVRAYLAtklpHYMIPQ 1791
Cdd:PRK08162 439 kdiiisgGENISSIEVEDVLYRHPAVLVAAVVAKPDPKWGEVPCAFVelkdgasATEEEI-IAHCREHLA----GFKVPK 513
|
570
....*....|....*.
gi 446807313 1792 QLIpIHNIPLTQNGKI 1807
Cdd:PRK08162 514 AVV-FGELPKTSTGKI 528
|
|
| PTZ00237 |
PTZ00237 |
acetyl-CoA synthetase; Provisional |
420-791 |
1.33e-06 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 240325 [Multi-domain] Cd Length: 647 Bit Score: 53.59 E-value: 1.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 420 YVIYTSGSTGQPKGVMIEHRSltNFLCAMYEDFSQDIGITDNVLFSSS----ISFDVTIFEIfvpLVCGARMTIYQG--- 492
Cdd:PTZ00237 258 YILYTSGTTGNSKAVVRSNGP--HLVGLKYYWRSIIEKDIPTVVFSHSsigwVSFHGFLYGS---LSLGNTFVMFEGgii 332
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 493 -EKFDVPKLVQVILEEQVTLAYIPPTLLNEIYDY-----FVRANQKIS-LNKLFVGVEPIKtELLAKYdhlFRGNLQI-- 563
Cdd:PTZ00237 333 kNKHIEDDLWNTIEKHKVTHTLTLPKTIRYLIKTdpeatIIRSKYDLSnLKEIWCGGEVIE-ESIPEY---IENKLKIks 408
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 564 LNLYGPTEaTVCCTSYQYerdKEITTQNVPIGSPLLNTKIYILDSFHRLQPIGVPGEICIS---GIGLARGYINRKELTA 640
Cdd:PTZ00237 409 SRGYGQTE-IGITYLYCY---GHINIPYNATGVPSIFIKPSILSEDGKELNVNEIGEVAFKlpmPPSFATTFYKNDEKFK 484
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 641 DKFIDHPfergeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCA 720
Cdd:PTZ00237 485 QLFSKFP-----GYYNSGDLGFKDENGYYTIVSRSDDQIKISGNKVQLNTIETSILKHPLVLECCSIGIYDPDCYNVPIG 559
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 721 YVVTEKDIPIP---------EVRAYLATKLPYYMIPQQIISIQNIPLTQNGKIDRKKLPQPINNlkSSHLEPTNSTERKL 791
Cdd:PTZ00237 560 LLVLKQDQSNQsidlnklknEINNIITQDIESLAVLRKIIIVNQLPKTKTGKIPRQIISKFLND--SNYQLPDNVNDSEI 637
|
|
| PLN02387 |
PLN02387 |
long-chain-fatty-acid-CoA ligase family protein |
415-695 |
1.39e-06 |
|
long-chain-fatty-acid-CoA ligase family protein
Pssm-ID: 215217 [Multi-domain] Cd Length: 696 Bit Score: 53.58 E-value: 1.39e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 415 PQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSqDIGITD---------NVLfssSISFDVTIFEIFVPLVCGA 485
Cdd:PLN02387 249 PNDIAVIMYTSGSTGLPKGVMMTHGNIVATVAGVMTVVP-KLGKNDvylaylplaHIL---ELAAESVMAAVGAAIGYGS 324
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 486 RMT-------IYQGEKFDVPKLvqvileeQVTLAYIPPTLLNEIYD-YFVRANQKISLNK-LF----------------- 539
Cdd:PLN02387 325 PLTltdtsnkIKKGTKGDASAL-------KPTLMTAVPAILDRVRDgVRKKVDAKGGLAKkLFdiaykrrlaaiegswfg 397
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 540 -VGVEPIKTELLA--KYDHLFRGNLQIL---------------NL---------YGPTEATVCCTSYQYErdkEITTQNV 592
Cdd:PLN02387 398 aWGLEKLLWDALVfkKIRAVLGGRIRFMlsggaplsgdtqrfiNIclgapigqgYGLTETCAGATFSEWD---DTSVGRV 474
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 593 piGSPLLNTKIYILD---SFHRLQPIGVP-GEICISGIGLARGYINRKELTADKF-IDhpfERGEKLYKTGDIARWLPDG 667
Cdd:PLN02387 475 --GPPLPCCYVKLVSweeGGYLISDKPMPrGEIVIGGPSVTLGYFKNQEKTDEVYkVD---ERGMRWFYTGDIGQFHPDG 549
|
330 340
....*....|....*....|....*....
gi 446807313 668 NIEYLGRVDHQVKIR-GYRIELGEIEASL 695
Cdd:PLN02387 550 CLEIIDRKKDIVKLQhGEYVSLGKVEAAL 578
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
1691-1807 |
2.60e-06 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 52.66 E-value: 2.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1691 FERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKD 1770
Cdd:cd05943 479 FAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG 558
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446807313 1771 IPIPE-----VRAYLATKL-PHYmIPQQLIPIHNIPLTQNGKI 1807
Cdd:cd05943 559 VELDDelrkrIRSTIRSALsPRH-VPAKIIAVPDIPRTLSGKK 600
|
|
| PRK05850 |
PRK05850 |
acyl-CoA synthetase; Validated |
1345-1487 |
2.70e-06 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 235624 [Multi-domain] Cd Length: 578 Bit Score: 52.64 E-value: 2.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1345 TYNELNIKANQLARRLLDQGVKRESIVgVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPKQ---RVEYMLTDSGCSHVLV 1421
Cdd:PRK05850 37 TWSQLYRRTLNVAEELRRHGSTGDRAV-ILAPQGLEYIVAFLGALQAGLIAVPLSVPQGGAhdeRVSAVLRDTSPSVVLT 115
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446807313 1422 hQNSIIKGI-----EFQGNV------IDLMDMSFEEEPGEDMHmmiEPHNLAYVIYTSGSTGQPKGVMIEHRSLT-NF 1487
Cdd:PRK05850 116 -TSAVVDDVteyvaPQPGQSappvieVDLLDLDSPRGSDARPR---DLPSTAYLQYTSGSTRTPAGVMVSHRNVIaNF 189
|
|
| AACS |
cd05943 |
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that ... |
648-764 |
2.93e-06 |
|
Acetoacetyl-CoA synthetase (acetoacetate-CoA ligase, AACS); AACS is a cytosolic ligase that specifically activates acetoacetate to its coenzyme A ester by a two-step reaction. Acetoacetate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. This is the first step of the mevalonate pathway of isoprenoid biosynthesis via isopentenyl diphosphate. Isoprenoids are a large class of compounds found in all living organisms. AACS is widely distributed in bacteria, archaea and eukaryotes. In bacteria, AACS is known to exhibit an important role in the metabolism of poly-b-hydroxybutyrate, an intracellular reserve of organic carbon and chemical energy by some microorganisms. In mammals, AACS influences the rate of ketone body utilization for the formation of physiologically important fatty acids and cholesterol.
Pssm-ID: 341265 [Multi-domain] Cd Length: 629 Bit Score: 52.66 E-value: 2.93e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 648 FERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQREDESGEKYLCAYVVTEKD 727
Cdd:cd05943 479 FAKYPGVWAHGDWIEITPRGGVVILGRSDGTLNPGGVRIGTAEIYRVVEKIPEVEDSLVVGQEWKDGDERVILFVKLREG 558
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 446807313 728 IPIPE-----VRAYLATKLPYYMIPQQIISIQNIPLTQNGKI 764
Cdd:cd05943 559 VELDDelrkrIRSTIRSALSPRHVPAKIIAVPDIPRTLSGKK 600
|
|
| Dip2 |
cd05905 |
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of ... |
292-528 |
3.55e-06 |
|
Disco-interacting protein 2 (Dip2); Dip2 proteins show sequence similarity to other members of the adenylate forming enzyme family, including insect luciferase, acetyl CoA ligases and the adenylation domain of nonribosomal peptide synthetases (NRPS). However, its function may have diverged from other members of the superfamily. In mouse embryo, Dip2 homolog A plays an important role in the development of both vertebrate and invertebrate nervous systems. Dip2A appears to regulate cell growth and the arrangement of cells in organs. Biochemically, Dip2A functions as a receptor of FSTL1, an extracellular glycoprotein, and may play a role as a cardiovascular protective agent.
Pssm-ID: 341231 [Multi-domain] Cd Length: 571 Bit Score: 51.97 E-value: 3.55e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 292 IAIVCNGKE---ITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAGGAYLPIDTELPKQ----- 362
Cdd:cd05905 3 TLLDSKGKEattLTWGKLLSRAEKIAAVLQKKvGLKPGDRVALMYPDPLDFVAAFYGCLYAGVVPIPIEPPDISQqlgfl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 363 ----------RVEYMLTDSGCSHVLTYQNSIIKGVAFQGSVINLMDIPFEEEQVEDLQITMEPQN---LAYVIYTSGSTG 429
Cdd:cd05905 83 lgtckvrvalTVEACLKGLPKKLLKSKTAAEIAKKKGWPKILDFVKIPKSKRSKLKKWGPHPPTRdgdTAYIEYSFSSDG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 430 QPKGVMIEHRSLTNFL------CAMYE--------DFSQDIGitdnvlfsssisfdvtifeifvpLVCGARMTIYQGekf 495
Cdd:cd05905 163 SLSGVAVSHSSLLAHCralkeaCELYEsrplvtvlDFKSGLG-----------------------LWHGCLLSVYSG--- 216
|
250 260 270
....*....|....*....|....*....|...
gi 446807313 496 dvpklVQVILEEQVTLAYIPPTLLNEIYDYFVR 528
Cdd:cd05905 217 -----HHTILIPPELMKTNPLLWLQTLSQYKVR 244
|
|
| PLN02654 |
PLN02654 |
acetate-CoA ligase |
1331-1831 |
4.61e-06 |
|
acetate-CoA ligase
Pssm-ID: 215353 [Multi-domain] Cd Length: 666 Bit Score: 51.82 E-value: 4.61e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1331 NPNQIAVV--CNEKG----ITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAGGAYLPIDTDLPK 1404
Cdd:PLN02654 102 NGDKIAIYweGNEPGfdasLTYSELLDRVCQLANYLKDVGVKKGDAVVIYLPMLMELPIAMLACARIGAVHSVVFAGFSA 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1405 QRVEYMLTDsgCS-HVLVHQNSIIKGIEFQgNVIDLMDMSFEE---------------------------EPGEDMHMM- 1455
Cdd:PLN02654 182 ESLAQRIVD--CKpKVVITCNAVKRGPKTI-NLKDIVDAALDEsakngvsvgicltyenqlamkredtkwQEGRDVWWQd 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1456 -------------IEPHNLAYVIYTSGSTGQPKGVMieHR-------SLTNFLCAMYEDFSQDIGITDNVLFSSSISFdV 1515
Cdd:PLN02654 259 vvpnyptkcevewVDAEDPLFLLYTSGSTGKPKGVL--HTtggymvyTATTFKYAFDYKPTDVYWCTADCGWITGHSY-V 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1516 TifeiFVPLIYGARMTIYQGEKF--DVTKLVQVILEEQVTLSYIPPTLLNEIY---DYFVRDNQKIVLNKLLVGVEPIKT 1590
Cdd:PLN02654 336 T----YGPMLNGATVLVFEGAPNypDSGRCWDIVDKYKVTIFYTAPTLVRSLMrdgDEYVTRHSRKSLRVLGSVGEPINP 411
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1591 ELLAKYdhlfrgnlqiLNGYGPTEATVCCTSYRYESNKEITTQnVPIGSPLLNTKIYIldSFHRIQPIGV---------- 1660
Cdd:PLN02654 412 SAWRWF----------FNVVGDSRCPISDTWWQTETGGFMITP-LPGAWPQKPGSATF--PFFGVQPVIVdekgkeiege 478
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1661 -PGEICI--SGIGLAR---GYINRKELTADKfidhPFErgeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEI 1734
Cdd:PLN02654 479 cSGYLCVkkSWPGAFRtlyGDHERYETTYFK----PFA---GYYFSGDGCSRDKDGYYWLTGRVDDVINVSGHRIGTAEV 551
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1735 EASLLKYETIKTAVVIDQEDEAGEKYLCAYVVTEKDIPIP-EVRAYLA----TKLPHYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:PLN02654 552 ESALVSHPQCAEAAVVGIEHEVKGQGIYAFVTLVEGVPYSeELRKSLIltvrNQIGAFAAPDKIHWAPGLPKTRSGKIMR 631
|
570 580
....*....|....*....|....*..
gi 446807313 1810 SKLPK-----LNTLGNSNYVPPRNEID 1831
Cdd:PLN02654 632 RILRKiasrqLDELGDTSTLADPGVVD 658
|
|
| PRK08043 |
PRK08043 |
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase; |
1457-1808 |
5.47e-06 |
|
bifunctional acyl-ACP--phospholipid O-acyltransferase/long-chain-fatty-acid--ACP ligase;
Pssm-ID: 181207 [Multi-domain] Cd Length: 718 Bit Score: 51.63 E-value: 5.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1457 EPHNLAYVIYTSGSTGQPKGVMIEHRSLTnflcAMYEDFSQDIGITDNVLFSSSI----SFDVTIfEIFVPLIYGARMTI 1532
Cdd:PRK08043 363 QPEDAALILFTSGSEGHPKGVVHSHKSLL----ANVEQIKTIADFTPNDRFMSALplfhSFGLTV-GLFTPLLTGAEVFL 437
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1533 YQgekfdvTKLVQVILEEQV-----TLSYIPPTLLNEI------YDyFVRdnqkivLNKLLVGVEPIKTELLAKYDHLFr 1601
Cdd:PRK08043 438 YP------SPLHYRIVPELVydrncTVLFGTSTFLGNYarfanpYD-FAR------LRYVVAGAEKLQESTKQLWQDKF- 503
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1602 gNLQILNGYGPTEatvcCTSyryesnkeITTQNVPIGspllnTKIYildSFHRIQP------IGVPG-----EICISGIG 1670
Cdd:PRK08043 504 -GLRILEGYGVTE----CAP--------VVSINVPMA-----AKPG---TVGRILPgmdarlLSVPGieqggRLQLKGPN 562
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1671 LARGYI---NRKELTADKFIDHPFERGEKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKT- 1746
Cdd:PRK08043 563 IMNGYLrveKPGVLEVPTAENARGEMERGWYDTGDIVRFDEQGFVQIQGRAKRFAKIAGEMVSLEMVEQLALGVSPDKQh 642
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1747 AVVIDQEDEAGEkylcAYVV--TEKDIPIPEVRAYL-ATKLPHYMIPQQLIPIHNIPLTQNGKID 1808
Cdd:PRK08043 643 ATAIKSDASKGE----ALVLftTDSELTREKLQQYArEHGVPELAVPRDIRYLKQLPLLGSGKPD 703
|
|
| PKS_TE |
smart00824 |
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide ... |
1928-2026 |
6.45e-06 |
|
Thioesterase; Peptide synthetases are involved in the non-ribosomal synthesis of peptide antibiotics. Next to the operons encoding these enzymes, in almost all cases, are genes that encode proteins that have similarity to the type II fatty acid thioesterases of vertebrates. There are also modules within the peptide synthetases that also share this similarity. With respect to antibiotic production, thioesterases are required for the addition of the last amino acid to the peptide antibiotic, thereby forming a cyclic antibiotic. Thioesterases (non-integrated) have molecular masses of 25-29 kDa.
Pssm-ID: 214835 [Multi-domain] Cd Length: 212 Bit Score: 49.15 E-value: 6.45e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1928 GGILNYYDLARELGEDKTVYGLQSIGYDDS-RFPnlSVEEMAVRYI-EEIKQVKKEGPYTLLGWSFGGIVAFEMARKLEE 2005
Cdd:smart00824 10 SGPHEYARLAAALRGRRDVSALPLPGFGPGePLP--ASADALVEAQaEAVLRAAGGRPFVLVGHSSGGLLAHAVAARLEA 87
|
90 100
....*....|....*....|.
gi 446807313 2006 LGDKVSFLGLLDVHPIEQGRE 2026
Cdd:smart00824 88 RGIPPAAVVLLDTYPPGDPAP 108
|
|
| MenH |
COG0596 |
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, ... |
1923-2017 |
6.49e-06 |
|
2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold [Coenzyme transport and metabolism, General function prediction only]; 2-succinyl-6-hydroxy-2,4-cyclohexadiene-1-carboxylate synthase MenH and related esterases, alpha/beta hydrolase fold is part of the Pathway/BioSystem: Menaquinone biosynthesis
Pssm-ID: 440361 [Multi-domain] Cd Length: 221 Bit Score: 49.61 E-value: 6.49e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1923 IHGQGGGILNYYDLARELGEDKTVYGLQSIGYDDSRFP--NLSVEEMAVRYIEEIKQVKKEgPYTLLGWSFGGIVAFEMA 2000
Cdd:COG0596 29 LHGLPGSSYEWRPLIPALAAGYRVIAPDLRGHGRSDKPagGYTLDDLADDLAALLDALGLE-RVVLVGHSMGGMVALELA 107
|
90
....*....|....*..
gi 446807313 2001 RKleeLGDKVSFLGLLD 2017
Cdd:COG0596 108 AR---HPERVAGLVLVD 121
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
1461-1718 |
9.29e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 50.75 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1461 LAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIG--------------------ITDNVLFS--SSISF----- 1513
Cdd:PTZ00216 266 LALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLIGppeedetycsylplahimefGVTNIFLArgALIGFgsprt 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1514 ----------DVT----IFEIFVPLIygarmtiyqgekFD-VTKLVQvileeqvtlSYIPP--TLLNEIYD--YFVR--- 1571
Cdd:PTZ00216 346 ltdtfarphgDLTefrpVFLIGVPRI------------FDtIKKAVE---------AKLPPvgSLKRRVFDhaYQSRlra 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1572 -----D----NQKIV----------LNKLLVGVEPIKTELLAKYDHLFRGnlqILNGYGPTEaTVCCTSYRYESNkeITT 1632
Cdd:PTZ00216 405 lkegkDtpywNEKVFsapravlggrVRAMLSGGGPLSAATQEFVNVVFGM---VIQGWGLTE-TVCCGGIQRTGD--LEP 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1633 QNVpiGSPLLNTKIYILDS---FHRIQPigVP-GEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLP 1708
Cdd:PTZ00216 479 NAV--GQLLKGVEMKLLDTeeyKHTDTP--EPrGEILLRGPFLFKGYYKQEELTREVLDE------DGWFHTGDVGSIAA 548
|
330
....*....|
gi 446807313 1709 DGNIEYLGRV 1718
Cdd:PTZ00216 549 NGTLRIIGRV 558
|
|
| PTZ00216 |
PTZ00216 |
acyl-CoA synthetase; Provisional |
418-675 |
9.29e-06 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240316 [Multi-domain] Cd Length: 700 Bit Score: 50.75 E-value: 9.29e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 418 LAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFSQDIG--------------------ITDNVLFS--SSISF----- 470
Cdd:PTZ00216 266 LALIMYTSGTTGDPKGVMHTHGSLTAGILALEDRLNDLIGppeedetycsylplahimefGVTNIFLArgALIGFgsprt 345
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 471 ----------DVT----IFEIFVPLVcgarmtiyqgekFD-VPKLVQvileeqvtlAYIPP--TLLNEIYDYF----VRA 529
Cdd:PTZ00216 346 ltdtfarphgDLTefrpVFLIGVPRI------------FDtIKKAVE---------AKLPPvgSLKRRVFDHAyqsrLRA 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 530 ----------NQKI----------SLNKLFVGVEPIKTELLAKYDHLFRGnlqILNLYGPTEaTVCCTSYQyeRDKEITT 589
Cdd:PTZ00216 405 lkegkdtpywNEKVfsapravlggRVRAMLSGGGPLSAATQEFVNVVFGM---VIQGWGLTE-TVCCGGIQ--RTGDLEP 478
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 590 QNVpiGSPLLNTKIYILDS---FHRLQPigVP-GEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLP 665
Cdd:PTZ00216 479 NAV--GQLLKGVEMKLLDTeeyKHTDTP--EPrGEILLRGPFLFKGYYKQEELTREVLDE------DGWFHTGDVGSIAA 548
|
330
....*....|
gi 446807313 666 DGNIEYLGRV 675
Cdd:PTZ00216 549 NGTLRIIGRV 558
|
|
| PRK00174 |
PRK00174 |
acetyl-CoA synthetase; Provisional |
1327-1809 |
1.30e-05 |
|
acetyl-CoA synthetase; Provisional
Pssm-ID: 234677 [Multi-domain] Cd Length: 637 Bit Score: 50.52 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1327 QVKRNPNQIAVV------CNEKGITYNELNIKANQLARRLLDQGVKRESIVGVMMKRSIEMVIGILGVLKAG-------- 1392
Cdd:PRK00174 76 HLKTRGDKVAIIwegddpGDSRKITYRELHREVCRFANALKSLGVKKGDRVAIYMPMIPEAAVAMLACARIGavhsvvfg 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1393 --------------GAYLPIDTD--------LP-KQRVEYMLTDSGC-SHVLVHQNSiikgiefqGNVI----------- 1437
Cdd:PRK00174 156 gfsaealadriidaGAKLVITADegvrggkpIPlKANVDEALANCPSvEKVIVVRRT--------GGDVdwvegrdlwwh 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1438 DLMDMSFEEEPGEDM---HMMiephnlaYVIYTSGSTGQPKGVM------IEHRSLTN-----------FLCamyedfSQ 1497
Cdd:PRK00174 228 ELVAGASDECEPEPMdaeDPL-------FILYTSGSTGKPKGVLhttggyLVYAAMTMkyvfdykdgdvYWC------TA 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1498 DIG-ITDNvlfsSSIsfdvtifeIFVPLIYGARMTIYQG--EKFDVTKLVQVILEEQVTLSYIPPTLLNEiydyFVRDNQ 1574
Cdd:PRK00174 295 DVGwVTGH----SYI--------VYGPLANGATTLMFEGvpNYPDPGRFWEVIDKHKVTIFYTAPTAIRA----LMKEGD 358
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1575 KIVLN------KLL--VGvEPIKTEllA---KYDHLFRGNLQILNGYGPTE--ATVcctsyryesnkeIT-----TQNVP 1636
Cdd:PRK00174 359 EHPKKydlsslRLLgsVG-EPINPE--AwewYYKVVGGERCPIVDTWWQTEtgGIM------------ITplpgaTPLKP 423
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1637 iGS---PLLNTKIYILDSFHRIQPIGVPGEICI--SGIGLARGYINRKEltadKFIDHPFERGEKLYKTGDIARWLPDGN 1711
Cdd:PRK00174 424 -GSatrPLPGIQPAVVDEEGNPLEGGEGGNLVIkdPWPGMMRTIYGDHE----RFVKTYFSTFKGMYFTGDGARRDEDGY 498
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1712 IEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIDQEDE-AGEKyLCAYVVTEKDIP-----IPEVRAYLATKLP 1785
Cdd:PRK00174 499 YWITGRVDDVLNVSGHRLGTAEIESALVAHPKVAEAAVVGRPDDiKGQG-IYAFVTLKGGEEpsdelRKELRNWVRKEIG 577
|
570 580
....*....|....*....|....
gi 446807313 1786 HYMIPQQLIPIHNIPLTQNGKIDR 1809
Cdd:PRK00174 578 PIAKPDVIQFAPGLPKTRSGKIMR 601
|
|
| E_NRPS |
cd19534 |
Epimerization domain of nonribosomal peptide synthetases (NRPSs); belongs to the ... |
879-1129 |
1.62e-05 |
|
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: 49.56 E-value: 1.62e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 879 QKRMFivDQFEDGTNTtYNMPTILKVEGDICKDKFENIFQSLIERHEILRTSFQILDGELVQKIEPNVD--FNIEYVHVN 956
Cdd:cd19534 8 QRWFF--EQNLAGRHH-FNQSVLLRVPQGLDPDALRQALRALVEHHDALRMRFRREDGGWQQRIRGDVEelFRLEVVDLS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 957 EKDADYLIHEFISP----FDLSKPPLLRVLLLRIAEERHILVVDMHHIISDGLSMGILIKEFVELY----KGNELPK-LR 1027
Cdd:cd19534 85 SLAQAAAIEALAAEaqssLDLEEGPLLAAALFDGTDGGDRLLLVIHHLVVDGVSWRILLEDLEAAYeqalAGEPIPLpSK 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1028 VQYKDYVMWQNGPYYKNLISEQKNYWLTTLKGELPVLnfPTDFQRptiqsFKGNV--CSFNLGTDLTfkvNKLATET--- 1102
Cdd:cd19534 165 TSFQTWAELLAEYAQSPALLEELAYWRELPAADYWGL--PKDPEQ-----TYGDArtVSFTLDEEET---EALLQEAnaa 234
|
250 260
....*....|....*....|....*...
gi 446807313 1103 -GTTPYMILLAIYNILLSRYTGQEDIIV 1129
Cdd:cd19534 235 yRTEINDLLLAALALAFQDWTGRAPPAI 262
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
1341-1484 |
2.34e-05 |
|
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: 49.60 E-value: 2.34e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1341 EKGITYNELNIKANQLARRLLDQ-GVKRESIVGVMMKRSIEMVIGILGVLKAG--GAYLP-------------------- 1397
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNtnirsksllhcfrccgakvl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1398 -IDTDLPK--QRVEYMLTDSGCSHVLVHQNSIIKGIEfqgNVIDLMDMSFEEEPGEDMHMMIEPHNLAYVIYTSGSTGQP 1474
Cdd:cd05938 83 vVAPELQEavEEVLPALRADGVSVWYLSHTSNTEGVI---SLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLP 159
|
170
....*....|
gi 446807313 1475 KGVMIEHRSL 1484
Cdd:cd05938 160 KAARISHLRV 169
|
|
| X-Domain_NRPS |
cd19546 |
X-domain is a catalytically inactive Condensation-like domain shown to recruit oxygenases to ... |
21-179 |
2.64e-05 |
|
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: 49.02 E-value: 2.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 21 EYWLDKLSGDVELSRFPCDclSLNNIQASKE--SYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKDDVV 98
Cdd:cd19546 196 AYWRDALAGAPDELELPTD--RPRPVLPSRRagAVPLRLDAEVHARLMEAAESAGATMFTVVQAALAMLLTRLGAGTDVT 273
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 99 IGMpVFKQGQEETVFQ------NNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDGESNNLPLLN 172
Cdd:cd19546 274 VGT-VLPRDDEEGDLEgmvgpfARPLALRTDLSGDPTFRELLGRVREAVREARRHQDVPFERLAELLALPPSADRHPVFQ 352
|
....*..
gi 446807313 173 TIVMLDD 179
Cdd:cd19546 353 VALDVRD 359
|
|
| DCL_NRPS-like |
cd19536 |
DCL-type Condensation domains of nonribosomal peptide synthetases (NRPSs), such as terminal ... |
22-238 |
7.41e-05 |
|
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: 47.44 E-value: 7.41e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 22 YWLDKLsGDVELSRFPCDCLSLNniQASKESYYCQFPSDIAKRAVAISNNSDMLLYTILLSGVKYLLSRYTDKDDVVIGM 101
Cdd:cd19536 190 YWREYL-AGATLATLPALSEAVG--GGPEQDSELLVSVPLPVRSRSLAKRSGIPLSTLLLAAWALVLSRHSGSDDVVFGT 266
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 102 PVFKQGQEETVFQN------NFLLLRTQINQEDnFKEIIYKIKETILESNEHCHFPfnkltqLLSLDGESNNLPLLNTIV 175
Cdd:cd19536 267 VVHGRSEETTGAERllglflNTLPLRVTLSEET-VEDLLKRAQEQELESLSHEQVP------LADIQRCSEGEPLFDSIV 339
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 176 MLDDIHCYEST---------------DKINSDMVIRFMKN--EEQLKVQVDYNSTLYSEGLVSRIVNHLYNILDILMKDP 238
Cdd:cd19536 340 NFRHFDLDFGLpewgsdegmrrgllfSEFKSNYDVNLSVLpkQDRLELKLAYNSQVLDEEQAQRLAAYYKSAIAELATAP 419
|
|
| ttLC_FACS_like |
cd05915 |
Fatty acyl-CoA synthetases similar to LC-FACS from Thermus thermophiles; This family includes ... |
1664-1814 |
8.48e-05 |
|
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: 47.43 E-value: 8.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1664 ICISGIGLARGYINRKELT-ADKFidhpfeRGeKLYKTGDIARWLPDGNIEYLGRVDHQVKIRGYRIELGEIEASLLKYE 1742
Cdd:cd05915 363 VQLKGPWITGGYYGNEEATrSALT------PD-GFFRTGDIAVWDEEGYVEIKDRLKDLIKSGGEWISSVDLENALMGHP 435
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313 1743 TIKTAVVIDQEDEAGEKYLCAYV-VTEKDIPIPEVRAYLATKLPHY-MIPQQLIPIHNIPLTQNGKIDRSKLPK 1814
Cdd:cd05915 436 KVKEAAVVAIPHPKWQERPLAVVvPRGEKPTPEELNEHLLKAGFAKwQLPDAYVFAEEIPRTSAGKFLKRALRE 509
|
|
| CT_NRPS-like |
cd19542 |
Terminal Condensation (CT)-like domains of nonribosomal peptide synthetases (NRPSs); Unlike ... |
17-238 |
1.44e-04 |
|
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: 46.53 E-value: 1.44e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 17 KKEKEYWLDKLSGdVELSRFPCdcLSlnnIQASKESYYCQFPSDIAK-RAVAISNNSDMLlyTILLSGVKYLLSRYTDKD 95
Cdd:cd19542 170 EESLQYWRKYLQG-ASPCAFPS--LS---PKRPAERSLSSTRRSLAKlEAFCASLGVTLA--SLFQAAWALVLARYTGSR 241
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 96 DVVIG---------MPvfkqGQEETV---FqnNFLLLRTQINQEDNFKEIIYKIKETILESNEHCHFPFNKLTQLLSLDG 163
Cdd:cd19542 242 DVVFGyvvsgrdlpVP----GIDDIVgpcI--NTLPVRVKLDPDWTVLDLLRQLQQQYLRSLPHQHLSLREIQRALGLWP 315
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 164 ESnnlPLLNTIV----------MLDDIHCYESTDKINS----DMVIRFMKNEEQLKVQVDYNSTLYSEGLVSRIVNHLYN 229
Cdd:cd19542 316 SG---TLFNTLVsyqnfeaspeSELSGSSVFELSAAEDpteyPVAVEVEPSGDSLKVSLAYSTSVLSEEQAEELLEQFDD 392
|
....*....
gi 446807313 230 ILDILMKDP 238
Cdd:cd19542 393 ILEALLANP 401
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
1457-1730 |
2.89e-04 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 46.25 E-value: 2.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1457 EPHNLAYVIYTSGSTGQPKGVMIEHRSLTNFL-----CAMYEDFSQDIG--------ITDNVLFSSSISFDVTI------ 1517
Cdd:PTZ00342 302 DPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVvplckHSIFKKYNPKTHlsylpishIYERVIAYLSFMLGGTIniwskd 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1518 FEIFVPLIYGARMTIYQGEKFDVTKLVQVILEEQVTLSYIPPTLLNEIYDyFVRDNQKIVLNKLLVGVEPIKTELLAKYD 1597
Cdd:PTZ00342 382 INYFSKDIYNSKGNILAGVPKVFNRIYTNIMTEINNLPPLKRFLVKKILS-LRKSNNNGGFSKFLEGITHISSKIKDKVN 460
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1598 hlfrGNLQ-ILNGYGPTEATVC-----------CTSYRY-ESNKEITTQNV------PIGSPLLNTKIYILDSFHRIQPI 1658
Cdd:PTZ00342 461 ----PNLEvILNGGGKLSPKIAeelsvllnvnyYQGYGLtETTGPIFVQHAddnnteSIGGPISPNTKYKVRTWETYKAT 536
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446807313 1659 GVP--GEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVKI-RGYRIE 1730
Cdd:PTZ00342 537 DTLpkGELLIKSDSIFSGYFLEKEQTKNAFTE------DGYFKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
|
|
| Abhydrolase_6 |
pfam12697 |
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse ... |
1922-2001 |
6.88e-04 |
|
Alpha/beta hydrolase family; This family contains alpha/beta hydrolase enzymes of diverse specificity.
Pssm-ID: 463673 [Multi-domain] Cd Length: 211 Bit Score: 43.23 E-value: 6.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 1922 IIHGQGggiLNYYDLARELGEDKTVYGLQSIGYDDSRFPNLSVEEMAvRYIEEIKQVKKEGPYTLLGWSFGGIVAFEMAR 2001
Cdd:pfam12697 3 LVHGAG---LSAAPLAALLAAGVAVLAPDLPGHGSSSPPPLDLADLA-DLAALLDELGAARPVVLVGHSLGGAVALAAAA 78
|
|
| PTZ00342 |
PTZ00342 |
acyl-CoA synthetase; Provisional |
414-687 |
1.04e-03 |
|
acyl-CoA synthetase; Provisional
Pssm-ID: 240370 [Multi-domain] Cd Length: 746 Bit Score: 44.32 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 414 EPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFL-----CAMYEDFSQDIG--------ITDNVLFSSSISFDVTI------ 474
Cdd:PTZ00342 302 DPDFITSIVYTSGTSGKPKGVMLSNKNLYNTVvplckHSIFKKYNPKTHlsylpishIYERVIAYLSFMLGGTIniwskd 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 475 FEIFVPLVCGARMTIYQGekfdVPKLVQVILEEQVT-LAYIPPT---LLNEIYDyFVRANQKISLNKLFVGV----EPIK 546
Cdd:PTZ00342 382 INYFSKDIYNSKGNILAG----VPKVFNRIYTNIMTeINNLPPLkrfLVKKILS-LRKSNNNGGFSKFLEGIthisSKIK 456
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 547 TELLAKYDHLFRG----------------NLQILNLYGPTEATvCCTSYQYERDKEITTQNVPIgSPllNTKiYILDSFH 610
Cdd:PTZ00342 457 DKVNPNLEVILNGggklspkiaeelsvllNVNYYQGYGLTETT-GPIFVQHADDNNTESIGGPI-SP--NTK-YKVRTWE 531
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 611 RLQPIGVP--GEICISGIGLARGYINRKELTADKFIDhpfergEKLYKTGDIARWLPDGNIEYLGRVDHQVKI-RGYRIE 687
Cdd:PTZ00342 532 TYKATDTLpkGELLIKSDSIFSGYFLEKEQTKNAFTE------DGYFKTGDIVQINKNGSLTFLDRSKGLVKLsQGEYIE 605
|
|
| PRK07867 |
PRK07867 |
acyl-CoA synthetase; Validated |
315-769 |
1.40e-03 |
|
acyl-CoA synthetase; Validated
Pssm-ID: 236120 [Multi-domain] Cd Length: 529 Bit Score: 43.52 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 315 RRLLDQGvkREFIVGVMMERSIEMIV-----GILGILKAG------GAYLPIDTELPKQRVeyMLTDSGCSHVLtyqNSI 383
Cdd:PRK07867 46 RARLDPT--RPPHVGVLLDNTPEFSLllgaaALSGIVPVGlnptrrGAALARDIAHADCQL--VLTESAHAELL---DGL 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 384 IKGVafqgSVINLmDIPFEEEQVEDLQ------ITMEPQNLAYVIYTSGSTGQPKGVMIEHRSLTNFLCAMYEDFsqdiG 457
Cdd:PRK07867 119 DPGV----RVINV-DSPAWADELAAHRdaeppfRVADPDDLFMLIFTSGTSGDPKAVRCTHRKVASAGVMLAQRF----G 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 458 IT-DNVLFSSSISF--DVTIFEIFVPLVCGARMTIYQgeKFDVPKLVQVILEEQVT--------LAYI---PPtllneiy 523
Cdd:PRK07867 190 LGpDDVCYVSMPLFhsNAVMAGWAVALAAGASIALRR--KFSASGFLPDVRRYGATyanyvgkpLSYVlatPE------- 260
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 524 dyfvRANQKISLNKLFVGVE--PIKTELLAKydhlfRGNLQILNLYGPTEATVCCTSyqyerdkeitTQNVPIGS--PLL 599
Cdd:PRK07867 261 ----RPDDADNPLRIVYGNEgaPGDIARFAR-----RFGCVVVDGFGSTEGGVAITR----------TPDTPPGAlgPLP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 600 -NTKIY-----------ILDSFHRLQPIGVPGEIC-ISGIGLARGYINRKELTADKFIDhpfergeKLYKTGDIARWLPD 666
Cdd:PRK07867 322 pGVAIVdpdtgtecppaEDADGRLLNADEAIGELVnTAGPGGFEGYYNDPEADAERMRG-------GVYWSGDLAYRDAD 394
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 667 GNIEYLGRVDHQVKIRGYRIELGEIEASLLKYETIKTAVVIQRED-ESGEKYLCAYVVTEKDIPIPE-VRAYLATK--LP 742
Cdd:PRK07867 395 GYAYFAGRLGDWMRVDGENLGTAPIERILLRYPDATEVAVYAVPDpVVGDQVMAALVLAPGAKFDPDaFAEFLAAQpdLG 474
|
490 500
....*....|....*....|....*..
gi 446807313 743 YYMIPQQIISIQNIPLTQNGKIDRKKL 769
Cdd:PRK07867 475 PKQWPSYVRVCAELPRTATFKVLKRQL 501
|
|
| PKS_PP |
smart00823 |
Phosphopantetheine attachment site; Phosphopantetheine (or pantetheine 4' phosphate) is the ... |
1834-1894 |
3.79e-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: 38.39 E-value: 3.79e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446807313 1834 LIDIWSSILGVNN---IGINDNFFELGGHSLKGLKLFENIKRMFNVQLPLSLLFQKATIEQLSD 1894
Cdd:smart00823 17 VREQVAAVLGHAAaeaIDPDRPFRDLGLDSLMAVELRNRLEAATGLRLPATLVFDHPTPAALAE 80
|
|
| hsFATP2a_ACSVL_like |
cd05938 |
Fatty acid transport proteins (FATP) including hsFATP2, hsFATP5, and hsFATP6, and similar ... |
298-441 |
4.53e-03 |
|
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: 41.89 E-value: 4.53e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 298 GKEITYKQLNIKANQLARRLLDQ-GVKREFIVGVMMERSIEMIVGILGILKAG--GAYLP-------------------- 354
Cdd:cd05938 3 GETYTYRDVDRRSNQAARALLAHaGLRPGDTVALLLGNEPAFLWIWLGLAKLGcpVAFLNtnirsksllhcfrccgakvl 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446807313 355 -IDTELPK--QRVEYMLTDSGCSHVLTYQNSIIKGVafqGSVINLMDIPFEEEQVEDLQITMEPQNLAYVIYTSGSTGQP 431
Cdd:cd05938 83 vVAPELQEavEEVLPALRADGVSVWYLSHTSNTEGV---ISLLDKVDAASDEPVPASLRAHVTIKSPALYIYTSGTTGLP 159
|
170
....*....|
gi 446807313 432 KGVMIEHRSL 441
Cdd:cd05938 160 KAARISHLRV 169
|
|
|